http://togogenome.org/gene/10090:Or14c40 ^@ http://purl.uniprot.org/uniprot/Q7TS10 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp213 ^@ http://purl.uniprot.org/uniprot/E9QAW0|||http://purl.uniprot.org/uniprot/Q3UGD5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB|||Polar residues|||SCAN box ^@ http://togogenome.org/gene/10090:Cs ^@ http://purl.uniprot.org/uniprot/Q9CZU6 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Active Site|||Chain|||Modified Residue|||Transit Peptide ^@ Citrate synthase, mitochondrial|||Mitochondrion|||N6,N6,N6-trimethyllysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000005472 http://togogenome.org/gene/10090:Rabac1 ^@ http://purl.uniprot.org/uniprot/Q9Z0S9 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Homodimerization|||No effect.|||Partial retention in the endoplasmic reticulum.|||Partial retention in the endoplasmic reticulum; still forms homodimers.|||Prenylated Rab acceptor protein 1|||Required for interaction with GDI1|||Required for interaction with prenylated RAB3A and VAMP2|||Retention in the endoplasmic reticulum.|||Retention in the endoplasmic reticulum; does not form homodimers. ^@ http://purl.uniprot.org/annotation/PRO_0000220879 http://togogenome.org/gene/10090:Cyyr1 ^@ http://purl.uniprot.org/uniprot/Q8VIH7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cysteine and tyrosine-rich protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000021055 http://togogenome.org/gene/10090:Cyb5d2 ^@ http://purl.uniprot.org/uniprot/Q5SSH8 ^@ 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 ^@ Cytochrome b5 heme-binding|||Disordered|||In isoform 2.|||Neuferricin ^@ http://purl.uniprot.org/annotation/PRO_0000312322|||http://purl.uniprot.org/annotation/VSP_029827 http://togogenome.org/gene/10090:Alad ^@ http://purl.uniprot.org/uniprot/P10518|||http://purl.uniprot.org/uniprot/Q9DD05 ^@ Active Site|||Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Strand|||Turn ^@ Delta-aminolevulinic acid dehydratase|||N6-succinyllysine|||Phosphoserine|||Schiff-base intermediate with substrate ^@ http://purl.uniprot.org/annotation/PRO_0000140528 http://togogenome.org/gene/10090:Impdh2 ^@ http://purl.uniprot.org/uniprot/P24547|||http://purl.uniprot.org/uniprot/Q3UAT9 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant ^@ CBS|||CBS 1|||CBS 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In mycophenolic acid resistant cells.|||Inosine-5'-monophosphate dehydrogenase 2|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Thioimidate intermediate|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000093674 http://togogenome.org/gene/10090:Vmn1r88 ^@ http://purl.uniprot.org/uniprot/E9Q235 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnn2 ^@ http://purl.uniprot.org/uniprot/Q08093|||http://purl.uniprot.org/uniprot/Q543F3 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat ^@ Calponin-2|||Calponin-homology (CH)|||Calponin-like 1|||Calponin-like 2|||Calponin-like 3|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000204774 http://togogenome.org/gene/10090:Slc45a4 ^@ http://purl.uniprot.org/uniprot/Q0P5V9 ^@ 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 ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Solute carrier family 45 member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000333804|||http://purl.uniprot.org/annotation/VSP_033543|||http://purl.uniprot.org/annotation/VSP_033544 http://togogenome.org/gene/10090:Tmem233 ^@ http://purl.uniprot.org/uniprot/D3Z1U7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues|||Transmembrane protein 233 ^@ http://purl.uniprot.org/annotation/PRO_0000394963 http://togogenome.org/gene/10090:Defa31 ^@ http://purl.uniprot.org/uniprot/Q5G866 ^@ Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Alpha-defensin 23|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000300072|||http://purl.uniprot.org/annotation/PRO_0000300073 http://togogenome.org/gene/10090:Gucy1b2 ^@ http://purl.uniprot.org/uniprot/E9Q6H0|||http://purl.uniprot.org/uniprot/Q8BXH3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Guanylate cyclase|||Polar residues ^@ http://togogenome.org/gene/10090:Slc25a11 ^@ http://purl.uniprot.org/uniprot/Q5SX53|||http://purl.uniprot.org/uniprot/Q9CR62 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||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_0000090626 http://togogenome.org/gene/10090:Hspa1a ^@ http://purl.uniprot.org/uniprot/Q3TU85|||http://purl.uniprot.org/uniprot/Q61696 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Heat shock 70 kDa protein 1A|||N-acetylalanine|||N6,N6,N6-trimethyllysine; by METTL21A; alternate|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||Nucleotide-binding domain (NBD)|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Removed|||Substrate-binding domain (SBD) ^@ http://purl.uniprot.org/annotation/PRO_0000078250 http://togogenome.org/gene/10090:Bend6 ^@ http://purl.uniprot.org/uniprot/Q6PFX2 ^@ 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 6|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295661|||http://purl.uniprot.org/annotation/VSP_026967|||http://purl.uniprot.org/annotation/VSP_026968|||http://purl.uniprot.org/annotation/VSP_026969 http://togogenome.org/gene/10090:Gm11758 ^@ http://purl.uniprot.org/uniprot/A2BEI6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Taar4 ^@ http://purl.uniprot.org/uniprot/Q5QD15 ^@ 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|||Trace amine-associated receptor 4 ^@ http://purl.uniprot.org/annotation/PRO_0000070152 http://togogenome.org/gene/10090:Ptprz1 ^@ http://purl.uniprot.org/uniprot/B2RXS8|||http://purl.uniprot.org/uniprot/B9EKR1|||http://purl.uniprot.org/uniprot/Q8C4M8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Alpha-carbonic anhydrase|||Ancestral active site|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Receptor-type tyrosine-protein phosphatase zeta|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2|||protein-tyrosine-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000424882|||http://purl.uniprot.org/annotation/PRO_5004303894|||http://purl.uniprot.org/annotation/PRO_5015087163 http://togogenome.org/gene/10090:Ncs1 ^@ http://purl.uniprot.org/uniprot/Q8BNY6 ^@ 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 ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Interaction with IL1RAPL1|||N-myristoyl glycine|||Neuronal calcium sensor 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073789 http://togogenome.org/gene/10090:Vash1 ^@ http://purl.uniprot.org/uniprot/Q8C1W1 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Abolished tyrosine carboxypeptidase activity.|||Basic and acidic residues|||Cleavage|||Disordered|||Involved in heparin-binding and antiangiogenic activity|||Polar residues|||Tubulinyl-Tyr carboxypeptidase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000189981 http://togogenome.org/gene/10090:Oas1c ^@ http://purl.uniprot.org/uniprot/Q924S2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Inactive 2'-5' oligoadenylate synthetase 1C ^@ http://purl.uniprot.org/annotation/PRO_0000440068 http://togogenome.org/gene/10090:2810021J22Rik ^@ http://purl.uniprot.org/uniprot/Q8BIB6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Rpn1 ^@ http://purl.uniprot.org/uniprot/Q5RKP4|||http://purl.uniprot.org/uniprot/Q8BMR3|||http://purl.uniprot.org/uniprot/Q91YQ5 ^@ Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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_0000022242|||http://purl.uniprot.org/annotation/PRO_5005143758|||http://purl.uniprot.org/annotation/PRO_5005144430 http://togogenome.org/gene/10090:Fgd4 ^@ http://purl.uniprot.org/uniprot/Q91ZT5 ^@ Binding Site|||Chain|||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|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Actin filament-binding|||DH|||Disordered|||FYVE, RhoGEF and PH domain-containing protein 4|||FYVE-type|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||PH 1|||PH 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080948|||http://purl.uniprot.org/annotation/VSP_013083|||http://purl.uniprot.org/annotation/VSP_013084|||http://purl.uniprot.org/annotation/VSP_013085|||http://purl.uniprot.org/annotation/VSP_013086|||http://purl.uniprot.org/annotation/VSP_013087 http://togogenome.org/gene/10090:Rpl7 ^@ http://purl.uniprot.org/uniprot/P14148|||http://purl.uniprot.org/uniprot/Q5M9N8 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||4|||5|||6|||6 X 12 AA tandem repeats|||Large ribosomal subunit protein uL30|||Large ribosomal subunit protein uL30 N-terminal eukaryotes|||Large ribosomal subunit protein uL30-like ferredoxin-like fold|||N-acetylmethionine|||N6-acetyllysine|||N6-succinyllysine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000104634 http://togogenome.org/gene/10090:Cdc123 ^@ http://purl.uniprot.org/uniprot/Q8CII2 ^@ 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 ^@ Cell division cycle protein 123 homolog|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000228664|||http://purl.uniprot.org/annotation/VSP_017691|||http://purl.uniprot.org/annotation/VSP_017692 http://togogenome.org/gene/10090:Rundc3b ^@ http://purl.uniprot.org/uniprot/D3YUQ5|||http://purl.uniprot.org/uniprot/Q6PDC0 ^@ 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 ^@ Disordered|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RUN|||RUN domain-containing protein 3B ^@ http://purl.uniprot.org/annotation/PRO_0000336051 http://togogenome.org/gene/10090:Rmc1 ^@ http://purl.uniprot.org/uniprot/Q3TWH4|||http://purl.uniprot.org/uniprot/Q3U4H5|||http://purl.uniprot.org/uniprot/Q3UMX3|||http://purl.uniprot.org/uniprot/Q8VC42 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Mic1|||Regulator of MON1-CCZ1 complex ^@ http://purl.uniprot.org/annotation/PRO_0000096482 http://togogenome.org/gene/10090:Cilp2 ^@ http://purl.uniprot.org/uniprot/D3Z7H8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||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_0000437175|||http://purl.uniprot.org/annotation/PRO_0000437176|||http://purl.uniprot.org/annotation/PRO_5003052865 http://togogenome.org/gene/10090:Slc22a3 ^@ http://purl.uniprot.org/uniprot/Q547K2|||http://purl.uniprot.org/uniprot/Q9WTW5 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Transmembrane ^@ Helical|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Proline-rich sequence|||Solute carrier family 22 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000220504 http://togogenome.org/gene/10090:Npas1 ^@ http://purl.uniprot.org/uniprot/A2RSH6|||http://purl.uniprot.org/uniprot/P97459 ^@ 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 ^@ BHLH|||Basic and acidic residues|||Destabilizes heterodimerization with ARNT. Compromises the transcriptional repression activity of heterodimer ARNT:NPAS1.|||Disordered|||Neuronal PAS domain-containing protein 1|||PAC|||PAS|||PAS 1|||PAS 2|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127405 http://togogenome.org/gene/10090:Cmpk1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J093|||http://purl.uniprot.org/uniprot/Q9DBP5 ^@ Binding Site|||Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Region ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||LID|||N6-acetyllysine|||N6-succinyllysine|||NMP|||NMPbind|||Phosphoserine|||UMP-CMP kinase ^@ http://purl.uniprot.org/annotation/PRO_0000158950 http://togogenome.org/gene/10090:Ece2 ^@ http://purl.uniprot.org/uniprot/B2RQR8|||http://purl.uniprot.org/uniprot/Q80Z57|||http://purl.uniprot.org/uniprot/Q80Z58 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endothelin-converting enzyme 2|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform Ece2-2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Peptidase M13 C-terminal|||Peptidase M13 N-terminal|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000443294|||http://purl.uniprot.org/annotation/VSP_059326 http://togogenome.org/gene/10090:Tex30 ^@ http://purl.uniprot.org/uniprot/Q3TUU5 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Testis-expressed protein 30 ^@ http://purl.uniprot.org/annotation/PRO_0000274313 http://togogenome.org/gene/10090:Cstl1 ^@ http://purl.uniprot.org/uniprot/Q80Y72 ^@ 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 ^@ Cystatin|||Cystatin-like 1|||In isoform 1.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_5009369047|||http://purl.uniprot.org/annotation/VSP_058947 http://togogenome.org/gene/10090:Wdr31 ^@ http://purl.uniprot.org/uniprot/Q9JHB4 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Repeat|||Splice Variant ^@ In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat-containing protein 31 ^@ http://purl.uniprot.org/annotation/PRO_0000051381|||http://purl.uniprot.org/annotation/VSP_010419 http://togogenome.org/gene/10090:Eln ^@ http://purl.uniprot.org/uniprot/P54320 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ 4-hydroxyproline|||Allysine|||Elastin|||Hydroxyproline ^@ http://purl.uniprot.org/annotation/PRO_0000021164 http://togogenome.org/gene/10090:Arl15 ^@ http://purl.uniprot.org/uniprot/Q8BGR6 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ ADP-ribosylation factor-like protein 15 ^@ http://purl.uniprot.org/annotation/PRO_0000282388 http://togogenome.org/gene/10090:Agbl2 ^@ http://purl.uniprot.org/uniprot/Q8CDK2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes deglutamylase activity.|||Cytosolic carboxypeptidase 2|||Disordered|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 7.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Nucleophile|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000283750|||http://purl.uniprot.org/annotation/VSP_024362|||http://purl.uniprot.org/annotation/VSP_024363|||http://purl.uniprot.org/annotation/VSP_024364|||http://purl.uniprot.org/annotation/VSP_024365|||http://purl.uniprot.org/annotation/VSP_024366|||http://purl.uniprot.org/annotation/VSP_024367|||http://purl.uniprot.org/annotation/VSP_024368|||http://purl.uniprot.org/annotation/VSP_024369 http://togogenome.org/gene/10090:Mxd4 ^@ http://purl.uniprot.org/uniprot/Q91VN7 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gtsf1l ^@ http://purl.uniprot.org/uniprot/Q9CWD0 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Region|||Sequence Conflict|||Zinc Finger ^@ CHHC U11-48K-type 1|||CHHC U11-48K-type 2|||Disordered|||Gametocyte-specific factor 1-like ^@ http://purl.uniprot.org/annotation/PRO_0000221620 http://togogenome.org/gene/10090:Sugt1 ^@ http://purl.uniprot.org/uniprot/Q9CX34 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ 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|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Protein SGT1 homolog|||Removed|||SGS|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000106333 http://togogenome.org/gene/10090:Dusp15 ^@ http://purl.uniprot.org/uniprot/Q8R4V2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Splice Variant ^@ Disordered|||Dual specificity protein phosphatase 15|||In isoform 2.|||N-myristoyl glycine|||Phosphocysteine intermediate|||Polar residues|||Removed|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094825|||http://purl.uniprot.org/annotation/VSP_007294|||http://purl.uniprot.org/annotation/VSP_007295 http://togogenome.org/gene/10090:B3gat1 ^@ http://purl.uniprot.org/uniprot/Q9CW73 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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_0000195168|||http://purl.uniprot.org/annotation/VSP_058539 http://togogenome.org/gene/10090:Lcorl ^@ http://purl.uniprot.org/uniprot/A0A571BEC4|||http://purl.uniprot.org/uniprot/Q3U285 ^@ 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 ^@ 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.|||In isoform 4.|||In isoform 5.|||Ligand-dependent nuclear receptor corepressor-like protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000310464|||http://purl.uniprot.org/annotation/VSP_029291|||http://purl.uniprot.org/annotation/VSP_029292|||http://purl.uniprot.org/annotation/VSP_029293|||http://purl.uniprot.org/annotation/VSP_029294|||http://purl.uniprot.org/annotation/VSP_029295|||http://purl.uniprot.org/annotation/VSP_029296|||http://purl.uniprot.org/annotation/VSP_029297 http://togogenome.org/gene/10090:Or1o2 ^@ http://purl.uniprot.org/uniprot/Q8VFE1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ttll9 ^@ http://purl.uniprot.org/uniprot/A2APC3 ^@ 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|||Site|||Splice Variant ^@ Disordered|||Essential for specifying alpha-elongation versus initiation step of the polyglutamylase activity|||In isoform 2.|||Polar residues|||Probable tubulin polyglutamylase TTLL9|||TTL ^@ http://purl.uniprot.org/annotation/PRO_0000324518|||http://purl.uniprot.org/annotation/VSP_032261 http://togogenome.org/gene/10090:Senp7 ^@ http://purl.uniprot.org/uniprot/A0A0J9YUC9|||http://purl.uniprot.org/uniprot/E9Q1L5|||http://purl.uniprot.org/uniprot/Q3TPI1|||http://purl.uniprot.org/uniprot/Q8BUH8|||http://purl.uniprot.org/uniprot/Q9CQN9|||http://purl.uniprot.org/uniprot/Q9CX65 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolished protease activity and ability to desumoylate CGAS.|||Basic and acidic residues|||Disordered|||Nucleophile|||Phosphoserine|||Polar residues|||Protease|||Sentrin-specific protease 7|||Ubiquitin-like protease family profile ^@ http://purl.uniprot.org/annotation/PRO_0000267609 http://togogenome.org/gene/10090:Dnaaf1 ^@ http://purl.uniprot.org/uniprot/Q9D2H9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Dynein axonemal assembly factor 1|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000232890 http://togogenome.org/gene/10090:Tex13c1 ^@ http://purl.uniprot.org/uniprot/D3YU32 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Testis-expressed protein 13C-1 ^@ http://purl.uniprot.org/annotation/PRO_0000435875 http://togogenome.org/gene/10090:Tmprss7 ^@ http://purl.uniprot.org/uniprot/Q8BIK6 ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Basic residues|||CUB 1|||CUB 2|||Charge relay system|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||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 7 ^@ http://purl.uniprot.org/annotation/PRO_0000027860 http://togogenome.org/gene/10090:Dcakd ^@ http://purl.uniprot.org/uniprot/Q8BHC4 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ DPCK|||Dephospho-CoA kinase domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000316850 http://togogenome.org/gene/10090:Xab2 ^@ http://purl.uniprot.org/uniprot/Q9DCD2 ^@ 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 ^@ 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_0000106415 http://togogenome.org/gene/10090:Pycr1 ^@ http://purl.uniprot.org/uniprot/Q3UTR5|||http://purl.uniprot.org/uniprot/Q922W5 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ N-acetylserine|||Phosphoserine|||Pyrroline-5-carboxylate reductase 1, mitochondrial|||Pyrroline-5-carboxylate reductase catalytic N-terminal|||Pyrroline-5-carboxylate reductase dimerisation|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000187315 http://togogenome.org/gene/10090:Gad1 ^@ http://purl.uniprot.org/uniprot/D3Z1L8|||http://purl.uniprot.org/uniprot/P48318|||http://purl.uniprot.org/uniprot/Q548L6 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glutamate decarboxylase 1|||N6-(pyridoxal phosphate)lysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000146964 http://togogenome.org/gene/10090:Kel ^@ http://purl.uniprot.org/uniprot/Q9EQF2 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Interchain (with C-347 in XK)|||Kell blood group glycoprotein homolog|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000319886 http://togogenome.org/gene/10090:Mtrfr ^@ http://purl.uniprot.org/uniprot/Q80VP5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Basic and acidic residues|||Disordered|||GGQ|||GGQ domain|||In isoform 2.|||Mitochondrial translation release factor in rescue|||Mitochondrion|||N5-methylglutamine ^@ http://purl.uniprot.org/annotation/PRO_0000311836|||http://purl.uniprot.org/annotation/VSP_029604|||http://purl.uniprot.org/annotation/VSP_029605 http://togogenome.org/gene/10090:Slc22a7 ^@ http://purl.uniprot.org/uniprot/A0A0R4J122|||http://purl.uniprot.org/uniprot/Q91WU2 ^@ 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.|||Major facilitator superfamily (MFS) profile|||Solute carrier family 22 member 7 ^@ http://purl.uniprot.org/annotation/PRO_0000317482|||http://purl.uniprot.org/annotation/VSP_030995|||http://purl.uniprot.org/annotation/VSP_030996 http://togogenome.org/gene/10090:Slc16a8 ^@ http://purl.uniprot.org/uniprot/O35308|||http://purl.uniprot.org/uniprot/Q5UB50 ^@ 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|||Basolateral sorting signal|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Major facilitator superfamily (MFS) profile|||Monocarboxylate transporter 3 ^@ http://purl.uniprot.org/annotation/PRO_0000211391 http://togogenome.org/gene/10090:Defb38 ^@ http://purl.uniprot.org/uniprot/Q05A65|||http://purl.uniprot.org/uniprot/Q7TNV7 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 38 ^@ http://purl.uniprot.org/annotation/PRO_0000006950|||http://purl.uniprot.org/annotation/PRO_5014306681 http://togogenome.org/gene/10090:Saa2 ^@ http://purl.uniprot.org/uniprot/P05367 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide|||Strand ^@ Amyloid protein A|||Basic and acidic residues|||Disordered|||In strain: SJL/J.|||Serum amyloid A-2 protein ^@ http://purl.uniprot.org/annotation/PRO_0000031589|||http://purl.uniprot.org/annotation/PRO_0000031590 http://togogenome.org/gene/10090:Odf3b ^@ http://purl.uniprot.org/uniprot/Q5M8M2 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ Ciliary microtubule associated protein 1B|||Disordered|||STPGR ^@ http://purl.uniprot.org/annotation/PRO_0000346441 http://togogenome.org/gene/10090:Zfp65 ^@ http://purl.uniprot.org/uniprot/Q8BY64|||http://purl.uniprot.org/uniprot/Q91W94 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Fam180a ^@ http://purl.uniprot.org/uniprot/Q8BR21 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Protein FAM180A ^@ http://purl.uniprot.org/annotation/PRO_0000317517 http://togogenome.org/gene/10090:Eny2 ^@ http://purl.uniprot.org/uniprot/Q9JIX0 ^@ Chain|||Crosslink|||Modification|||Molecule Processing ^@ Chain|||Crosslink ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Transcription and mRNA export factor ENY2 ^@ http://purl.uniprot.org/annotation/PRO_0000314131 http://togogenome.org/gene/10090:Btg1b ^@ http://purl.uniprot.org/uniprot/Q3V0S2 ^@ Experimental Information|||Non-terminal Residue ^@ Non-terminal Residue ^@ ^@ http://togogenome.org/gene/10090:Tmem184a ^@ http://purl.uniprot.org/uniprot/G3X923|||http://purl.uniprot.org/uniprot/Q3UFJ6 ^@ 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|||Transmembrane protein 184A ^@ http://purl.uniprot.org/annotation/PRO_0000300468 http://togogenome.org/gene/10090:Camk1g ^@ http://purl.uniprot.org/uniprot/Q91VB2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region ^@ Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase type 1G|||Calmodulin-binding|||Disordered|||Loss of association to membranes.|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086085 http://togogenome.org/gene/10090:Zw10 ^@ http://purl.uniprot.org/uniprot/O54692 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Centromere/kinetochore protein zw10 homolog|||Interaction with RINT1|||Interaction with ZWINT|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000184958 http://togogenome.org/gene/10090:Oprk1 ^@ http://purl.uniprot.org/uniprot/A0A5F8MP90|||http://purl.uniprot.org/uniprot/P33534|||http://purl.uniprot.org/uniprot/Q14AL5|||http://purl.uniprot.org/uniprot/Q3UVW8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Non-terminal Residue|||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|||Kappa-type opioid receptor|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069968 http://togogenome.org/gene/10090:Dcaf1 ^@ http://purl.uniprot.org/uniprot/Q80TR8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Chromo|||DDB1- and CUL4-associated factor 1|||DWD box 1|||DWD box 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with NF2|||LisH|||Loss of interaction with DDB1 and strong decrease in TET2 monoubiquitination; when associated with A-1246.|||Loss of interaction with DDB1 and strong decrease in TET2 monoubiquitination; when associated with A-1282.|||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_0000287474|||http://purl.uniprot.org/annotation/VSP_025500|||http://purl.uniprot.org/annotation/VSP_025501|||http://purl.uniprot.org/annotation/VSP_025502|||http://purl.uniprot.org/annotation/VSP_025503|||http://purl.uniprot.org/annotation/VSP_025504 http://togogenome.org/gene/10090:Pcbd1 ^@ http://purl.uniprot.org/uniprot/P61458 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||Pterin-4-alpha-carbinolamine dehydratase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000063053 http://togogenome.org/gene/10090:Ammecr1 ^@ http://purl.uniprot.org/uniprot/Q9JHT5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ AMMECR1|||Disordered|||Nuclear protein AMMECR1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000142367 http://togogenome.org/gene/10090:Itprid1 ^@ http://purl.uniprot.org/uniprot/Q14B48 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Polar residues|||Protein ITPRID1 ^@ http://purl.uniprot.org/annotation/PRO_0000270964|||http://purl.uniprot.org/annotation/VSP_022256 http://togogenome.org/gene/10090:Ces2c ^@ http://purl.uniprot.org/uniprot/Q91WG0 ^@ Active Site|||Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Helix|||Motif|||Signal Peptide|||Strand|||Turn ^@ Acyl-ester intermediate|||Acylcarnitine hydrolase|||Charge relay system|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_5000396880 http://togogenome.org/gene/10090:Lingo3 ^@ http://purl.uniprot.org/uniprot/Q6GQU6 ^@ 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|||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_0000326530 http://togogenome.org/gene/10090:Kcnmb1 ^@ http://purl.uniprot.org/uniprot/Q5SQK1|||http://purl.uniprot.org/uniprot/Q8CAE3 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Calcium-activated potassium channel subunit beta-1|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000187047 http://togogenome.org/gene/10090:Gale ^@ http://purl.uniprot.org/uniprot/Q8R059 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Proton acceptor|||UDP-glucose 4-epimerase ^@ http://purl.uniprot.org/annotation/PRO_0000183190 http://togogenome.org/gene/10090:Chd5 ^@ http://purl.uniprot.org/uniprot/E9PYL1|||http://purl.uniprot.org/uniprot/E9PYU4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Chromo|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||PHD-type|||Polar residues ^@ http://togogenome.org/gene/10090:Aifm1 ^@ http://purl.uniprot.org/uniprot/B1AU25|||http://purl.uniprot.org/uniprot/Q9Z0X1 ^@ 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|||Site|||Splice Variant|||Strand|||Transit Peptide|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Splice Variant|||Strand|||Transit Peptide|||Transmembrane|||Turn ^@ Abolished DNA-binding without affecting binding to poly-ADP-ribose chains; when associated with A-254.|||Abolished DNA-binding without affecting binding to poly-ADP-ribose chains; when associated with A-264.|||Abolished binding to poly-ADP-ribose chains, preventing induction of parthanatos.|||Apoptosis-inducing factor 1, mitochondrial|||Disordered|||FAD-dependent oxidoreductase|||FAD/NAD(P)-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||Increases catalytic efficiency 30-fold. Increases affinity for NADH 20-fold.|||Increases catalytic efficiency.|||Increases redox potential, reacts faster to NADH and forms two-fold longer-lived CTC.|||Mitochondrial apoptosis-inducing factor C-terminal|||Mitochondrial localization signal|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein MGARP N-terminal|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000022031|||http://purl.uniprot.org/annotation/PRO_0000401936|||http://purl.uniprot.org/annotation/VSP_060486|||http://purl.uniprot.org/annotation/VSP_060487 http://togogenome.org/gene/10090:Pigq ^@ http://purl.uniprot.org/uniprot/Q3TD14|||http://purl.uniprot.org/uniprot/Q3TF56|||http://purl.uniprot.org/uniprot/Q9QYT7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q ^@ http://purl.uniprot.org/annotation/PRO_0000215665 http://togogenome.org/gene/10090:Lrriq4 ^@ http://purl.uniprot.org/uniprot/A6H6A4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant ^@ Basic residues|||Disordered|||IQ|||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 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_0000332139|||http://purl.uniprot.org/annotation/VSP_033339 http://togogenome.org/gene/10090:Or4c108 ^@ http://purl.uniprot.org/uniprot/A2ATG2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Usp17ld ^@ http://purl.uniprot.org/uniprot/G5E8G2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Loss of deubiquitinating activity.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein D ^@ http://purl.uniprot.org/annotation/PRO_0000438105 http://togogenome.org/gene/10090:Mov10 ^@ http://purl.uniprot.org/uniprot/E9PW39|||http://purl.uniprot.org/uniprot/P23249|||http://purl.uniprot.org/uniprot/Q3UD86 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes inhibition of retrotransposition.|||DEAG box|||DNA2/NAM7 helicase helicase|||DNA2/NAM7 helicase-like C-terminal|||Disordered|||Interaction with AGO2 and APOBEC3G|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Putative helicase MOV-10 ^@ http://purl.uniprot.org/annotation/PRO_0000080705 http://togogenome.org/gene/10090:1810010H24Rik ^@ http://purl.uniprot.org/uniprot/Q08AU9 ^@ 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 ^@ Basic and acidic residues|||Disordered|||NTR|||Polar residues|||UPF0450 protein C17orf58 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000279446 http://togogenome.org/gene/10090:Skint1 ^@ http://purl.uniprot.org/uniprot/A7TZE6 ^@ 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 C1-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In strain: FVB/NTac.|||N-linked (GlcNAc...) asparagine|||Selection and upkeep of intraepithelial T-cells protein 1 ^@ http://purl.uniprot.org/annotation/PRO_5000270102|||http://purl.uniprot.org/annotation/VSP_034871|||http://purl.uniprot.org/annotation/VSP_034872|||http://purl.uniprot.org/annotation/VSP_034873|||http://purl.uniprot.org/annotation/VSP_034874|||http://purl.uniprot.org/annotation/VSP_034875|||http://purl.uniprot.org/annotation/VSP_034876 http://togogenome.org/gene/10090:Tacr3 ^@ http://purl.uniprot.org/uniprot/P47937 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||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-K receptor|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069900 http://togogenome.org/gene/10090:BC053393 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1F6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015034597 http://togogenome.org/gene/10090:Khsrp ^@ http://purl.uniprot.org/uniprot/Q3U0V1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000298678 http://togogenome.org/gene/10090:Fcf1 ^@ http://purl.uniprot.org/uniprot/Q9CTH6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PINc|||rRNA-processing protein FCF1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089921 http://togogenome.org/gene/10090:Zfp459 ^@ http://purl.uniprot.org/uniprot/Q8BZ17 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Golph3l ^@ http://purl.uniprot.org/uniprot/H3BJ07|||http://purl.uniprot.org/uniprot/Q8R088 ^@ 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|||Beta-hairpin required for oligomerization|||Disordered|||Golgi phosphoprotein 3-like|||In isoform 2.|||In isoform 3.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000324137|||http://purl.uniprot.org/annotation/VSP_032151|||http://purl.uniprot.org/annotation/VSP_032152 http://togogenome.org/gene/10090:Dlg4 ^@ http://purl.uniprot.org/uniprot/Q62108 ^@ Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disks large homolog 4|||Disordered|||Guanylate kinase-like|||In isoform 2.|||In isoform 3.|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||S-palmitoyl cysteine|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000094561|||http://purl.uniprot.org/annotation/VSP_014930|||http://purl.uniprot.org/annotation/VSP_014931 http://togogenome.org/gene/10090:Zfand6 ^@ http://purl.uniprot.org/uniprot/Q9DCH6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ A20-type|||AN1-type|||AN1-type zinc finger protein 6|||Abolishes interaction with PEX6 and ubiquitin. Impairs interaction with PEX5.|||Disordered|||Impairs interaction with PEX6.|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000245236 http://togogenome.org/gene/10090:Ormdl2 ^@ http://purl.uniprot.org/uniprot/Q9CQZ0 ^@ 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.|||ORM1-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000215637|||http://purl.uniprot.org/annotation/VSP_016051 http://togogenome.org/gene/10090:Anln ^@ http://purl.uniprot.org/uniprot/Q8K298 ^@ 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 ^@ Anillin|||Basic and acidic residues|||Disordered|||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_0000227966 http://togogenome.org/gene/10090:Kmo ^@ http://purl.uniprot.org/uniprot/Q91WN4 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Kynurenine 3-monooxygenase ^@ http://purl.uniprot.org/annotation/PRO_0000229743|||http://purl.uniprot.org/annotation/VSP_051974 http://togogenome.org/gene/10090:Btbd35f9 ^@ http://purl.uniprot.org/uniprot/A2BFZ7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Manf ^@ http://purl.uniprot.org/uniprot/Q9CXI5 ^@ Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Turn ^@ Chain|||Disulfide Bond|||Helix|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Turn ^@ Mesencephalic astrocyte-derived neurotrophic factor|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000002306 http://togogenome.org/gene/10090:Grsf1 ^@ http://purl.uniprot.org/uniprot/E9Q179|||http://purl.uniprot.org/uniprot/Q8C5Q4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ G-rich sequence factor 1|||Mitochondrion|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000081598 http://togogenome.org/gene/10090:Fstl4 ^@ http://purl.uniprot.org/uniprot/Q5STE3 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||EF-hand 1|||EF-hand 2|||Follistatin-related protein 4|||Ig-like 1|||Ig-like 2|||Kazal-like|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000251926 http://togogenome.org/gene/10090:Spag16 ^@ http://purl.uniprot.org/uniprot/Q8K450 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Sperm-associated antigen 16 protein|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051224|||http://purl.uniprot.org/annotation/VSP_013503|||http://purl.uniprot.org/annotation/VSP_013504|||http://purl.uniprot.org/annotation/VSP_013505|||http://purl.uniprot.org/annotation/VSP_013506|||http://purl.uniprot.org/annotation/VSP_013507 http://togogenome.org/gene/10090:Il1rap ^@ http://purl.uniprot.org/uniprot/E9Q6I2|||http://purl.uniprot.org/uniprot/Q3UEL3|||http://purl.uniprot.org/uniprot/Q3V2X3|||http://purl.uniprot.org/uniprot/Q61730 ^@ Active Site|||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|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes interaction with MYD88 and IL-1-dependent activation of NF-kappa-B.|||Abolishes interaction with PTPRD; when associates with 69-A--A-71 Significantly reduces synaptogenesis; when associates with 82-A--A-85.|||Abolishes interaction with PTPRD; when associates with 82-A--A-85. Significantly reduces synaptogenesis; when associates with 82-A--A-85.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not affect affinity for PTPRD.|||Essential for interaction with PTPRD|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like domain-containing protein|||In isoform 2.|||In isoform 3.|||Interleukin-1 receptor accessory protein|||N-linked (GlcNAc...) asparagine|||Polar residues|||Reduces affinity for PTPRD.|||TIR ^@ http://purl.uniprot.org/annotation/PRO_0000015452|||http://purl.uniprot.org/annotation/PRO_5003244464|||http://purl.uniprot.org/annotation/PRO_5004229930|||http://purl.uniprot.org/annotation/PRO_5004230531|||http://purl.uniprot.org/annotation/VSP_008054|||http://purl.uniprot.org/annotation/VSP_008055|||http://purl.uniprot.org/annotation/VSP_058171 http://togogenome.org/gene/10090:Polr2k ^@ http://purl.uniprot.org/uniprot/Q63871 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Zinc Finger ^@ C4-type|||DNA-directed RNA polymerases I, II, and III subunit RPABC4 ^@ http://purl.uniprot.org/annotation/PRO_0000159751 http://togogenome.org/gene/10090:Inka1 ^@ http://purl.uniprot.org/uniprot/Q9CX62 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Inka box 1|||Inka box 2|||PAK4-inhibitor INKA1 ^@ http://purl.uniprot.org/annotation/PRO_0000239718 http://togogenome.org/gene/10090:Pus7l ^@ http://purl.uniprot.org/uniprot/Q8CE46 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Nucleophile|||Phosphoserine|||Pseudouridylate synthase PUS7L|||TRUD ^@ http://purl.uniprot.org/annotation/PRO_0000316786 http://togogenome.org/gene/10090:Sema6b ^@ http://purl.uniprot.org/uniprot/O54951|||http://purl.uniprot.org/uniprot/Q3UTK5 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Sema|||Semaphorin-6B ^@ http://purl.uniprot.org/annotation/PRO_0000032342|||http://purl.uniprot.org/annotation/PRO_5014309224 http://togogenome.org/gene/10090:Or5g9 ^@ http://purl.uniprot.org/uniprot/A2ALD4|||http://purl.uniprot.org/uniprot/Q8VFK1 ^@ 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 5G9 ^@ http://purl.uniprot.org/annotation/PRO_0000150859 http://togogenome.org/gene/10090:H2ac25 ^@ http://purl.uniprot.org/uniprot/A2AB79|||http://purl.uniprot.org/uniprot/Q8BFU2 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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 3|||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; 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_0000227513 http://togogenome.org/gene/10090:Fam174b ^@ http://purl.uniprot.org/uniprot/Q8K064 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Membrane protein FAM174B|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000326115 http://togogenome.org/gene/10090:Mnt ^@ http://purl.uniprot.org/uniprot/O08789 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Leucine-zipper|||Max-binding protein MNT|||N-acetylserine|||Pro residues|||Removed|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127282 http://togogenome.org/gene/10090:Mctp1 ^@ http://purl.uniprot.org/uniprot/E9PW38|||http://purl.uniprot.org/uniprot/Q8C8C0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C2|||Helical ^@ http://togogenome.org/gene/10090:Ccdc121rt2 ^@ http://purl.uniprot.org/uniprot/E9Q3K0|||http://purl.uniprot.org/uniprot/Q3V040 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF4515|||Disordered ^@ http://togogenome.org/gene/10090:Prelid3b ^@ http://purl.uniprot.org/uniprot/Q9CYY7 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ PRELI domain containing protein 3B|||PRELI/MSF1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000079430 http://togogenome.org/gene/10090:Caln1 ^@ http://purl.uniprot.org/uniprot/Q542R1|||http://purl.uniprot.org/uniprot/Q8CBJ9|||http://purl.uniprot.org/uniprot/Q9JJG7 ^@ 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_0000073530|||http://purl.uniprot.org/annotation/VSP_060874 http://togogenome.org/gene/10090:Gm10670 ^@ http://purl.uniprot.org/uniprot/K7N6B7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rdh7 ^@ http://purl.uniprot.org/uniprot/O88451 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Proton acceptor|||Retinol dehydrogenase 7 ^@ http://purl.uniprot.org/annotation/PRO_0000054761 http://togogenome.org/gene/10090:Ndufaf1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J081|||http://purl.uniprot.org/uniprot/Q9CWX2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Basic and acidic residues|||Complex I intermediate-associated protein 30, mitochondrial|||Disordered|||Mitochondrion|||NADH:ubiquinone oxidoreductase intermediate-associated protein 30|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000005465 http://togogenome.org/gene/10090:Acad10 ^@ http://purl.uniprot.org/uniprot/Q8K370 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Acyl-CoA dehydrogenase family member 10|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000284771 http://togogenome.org/gene/10090:Vmn1r76 ^@ http://purl.uniprot.org/uniprot/F8VQ63 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Chrna9 ^@ http://purl.uniprot.org/uniprot/G3X8Z7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_5015091808 http://togogenome.org/gene/10090:Ube2v2 ^@ http://purl.uniprot.org/uniprot/A6X925|||http://purl.uniprot.org/uniprot/Q4VBX4|||http://purl.uniprot.org/uniprot/Q9D2M8 ^@ 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.|||N-acetylalanine|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 variant 2 ^@ http://purl.uniprot.org/annotation/PRO_0000082603|||http://purl.uniprot.org/annotation/VSP_011529 http://togogenome.org/gene/10090:Or5d38 ^@ http://purl.uniprot.org/uniprot/Q7TR27 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc27a5 ^@ http://purl.uniprot.org/uniprot/Q3UNC6|||http://purl.uniprot.org/uniprot/Q4LDG0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ AMP-dependent synthetase/ligase|||AMP-dependent synthetase/ligase domain-containing protein|||Cytoplasmic|||Helical|||Long-chain fatty acid transport protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000193214|||http://purl.uniprot.org/annotation/PRO_5004230200 http://togogenome.org/gene/10090:Apoa4 ^@ http://purl.uniprot.org/uniprot/P06728 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ 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 strain: various strains.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000001977 http://togogenome.org/gene/10090:Hmgb2 ^@ http://purl.uniprot.org/uniprot/P30681 ^@ 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_0000048535 http://togogenome.org/gene/10090:Abo ^@ http://purl.uniprot.org/uniprot/P38649 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Histo-blood group ABO system transferase|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000157293 http://togogenome.org/gene/10090:Speer3 ^@ http://purl.uniprot.org/uniprot/Q9D4A3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Btbd35f5 ^@ http://purl.uniprot.org/uniprot/Q99N64 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Motif|||Sequence Conflict ^@ BTB|||Germ cell-less protein-like 2|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000087522 http://togogenome.org/gene/10090:Scrn3 ^@ http://purl.uniprot.org/uniprot/Q3TMH2 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Sequence Conflict ^@ Secernin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000262560 http://togogenome.org/gene/10090:Klc4 ^@ http://purl.uniprot.org/uniprot/Q9DBS5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Kinesin light chain 4|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7 ^@ http://purl.uniprot.org/annotation/PRO_0000215098 http://togogenome.org/gene/10090:Or13a20 ^@ http://purl.uniprot.org/uniprot/Q8VGL8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dhh ^@ http://purl.uniprot.org/uniprot/Q544P6|||http://purl.uniprot.org/uniprot/Q61488 ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Signal Peptide|||Site ^@ Cholesterol glycine ester|||Cleavage; by autolysis|||Desert hedgehog protein|||Desert hedgehog protein N-product|||Essential for auto-cleavage|||Hedgehog protein|||Hint|||Involved in auto-cleavage|||Involved in cholesterol transfer|||N-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000013247|||http://purl.uniprot.org/annotation/PRO_0000013248|||http://purl.uniprot.org/annotation/PRO_5010844018 http://togogenome.org/gene/10090:Stard13 ^@ http://purl.uniprot.org/uniprot/F8WIY7|||http://purl.uniprot.org/uniprot/Q3UWP1|||http://purl.uniprot.org/uniprot/Q923Q2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Rho-GAP|||SAM|||START|||StAR-related lipid transfer protein 13 ^@ http://purl.uniprot.org/annotation/PRO_0000220680 http://togogenome.org/gene/10090:Ap1s2 ^@ http://purl.uniprot.org/uniprot/Q3TIV9|||http://purl.uniprot.org/uniprot/Q8BW87|||http://purl.uniprot.org/uniprot/Q9DB50 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ AP complex mu/sigma subunit|||AP-1 complex subunit sigma-2 ^@ http://purl.uniprot.org/annotation/PRO_0000193800 http://togogenome.org/gene/10090:Prl7a1 ^@ http://purl.uniprot.org/uniprot/O54830 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prolactin-7A1 ^@ http://purl.uniprot.org/annotation/PRO_0000045211|||http://purl.uniprot.org/annotation/VSP_016678 http://togogenome.org/gene/10090:Lpar3 ^@ http://purl.uniprot.org/uniprot/Q544B4|||http://purl.uniprot.org/uniprot/Q9EQ31 ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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 3|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069434 http://togogenome.org/gene/10090:Slc9a4 ^@ http://purl.uniprot.org/uniprot/Q8BUE1 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Region|||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|||Polar residues|||Sodium/hydrogen exchanger 4 ^@ http://purl.uniprot.org/annotation/PRO_0000314666 http://togogenome.org/gene/10090:Or8d23 ^@ http://purl.uniprot.org/uniprot/Q9EQ99 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ifi47 ^@ http://purl.uniprot.org/uniprot/Q61635 ^@ Domain Extent|||Region ^@ Domain Extent ^@ IRG-type G ^@ http://togogenome.org/gene/10090:Esrra ^@ http://purl.uniprot.org/uniprot/O08580 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ AF-2 domain|||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|||N6-acetyllysine; by PCAF/KAT2B|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine|||Repressor domain|||Required for DNA-dependent dimerization|||Steroid hormone receptor ERR1 ^@ http://purl.uniprot.org/annotation/PRO_0000053661 http://togogenome.org/gene/10090:Plp1 ^@ http://purl.uniprot.org/uniprot/P60202|||http://purl.uniprot.org/uniprot/Q3UYM8 ^@ Chain|||Disulfide Bond|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Initiator Methionine|||Lipid Binding|||Modified 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 Jimpy MSD.|||In Rumpshaker.|||In isoform DM-20.|||Myelin proteolipid protein|||O-palmitoyl serine|||Phosphoserine|||Phosphothreonine|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000159007|||http://purl.uniprot.org/annotation/VSP_009194 http://togogenome.org/gene/10090:Or52e4 ^@ http://purl.uniprot.org/uniprot/Q8VF06 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Plag1 ^@ http://purl.uniprot.org/uniprot/Q9QYE0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Interaction with KPNA2|||Massively activates transcription|||Nuclear localization signal|||Polar residues|||Repression domain; contains 3 sumoylation motifs and massively decrease transcription activity|||Zinc finger protein PLAG1 ^@ http://purl.uniprot.org/annotation/PRO_0000295108 http://togogenome.org/gene/10090:Olfml1 ^@ http://purl.uniprot.org/uniprot/Q8BSH2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Olfactomedin-like ^@ http://purl.uniprot.org/annotation/PRO_5015099053 http://togogenome.org/gene/10090:Nprl3 ^@ http://purl.uniprot.org/uniprot/Q8BXG6|||http://purl.uniprot.org/uniprot/Q8VIJ8 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||GATOR1 complex protein NPRL3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000278089 http://togogenome.org/gene/10090:Bambi ^@ http://purl.uniprot.org/uniprot/Q9D0L6 ^@ 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 ^@ BMP and activin membrane-bound inhibitor homolog|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000020780 http://togogenome.org/gene/10090:Dek ^@ http://purl.uniprot.org/uniprot/Q3UR53|||http://purl.uniprot.org/uniprot/Q7TNV0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ ADP-ribosylserine|||Acidic residues|||Basic and acidic residues|||DEK-C|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Protein DEK|||SAP ^@ http://purl.uniprot.org/annotation/PRO_0000079859 http://togogenome.org/gene/10090:Or1e17 ^@ http://purl.uniprot.org/uniprot/Q7TRX4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Col17a1 ^@ http://purl.uniprot.org/uniprot/Q07563 ^@ 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 ^@ 120 kDa linear IgA disease antigen homolog|||Basic and acidic residues|||Collagen alpha-1(XVII) chain|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||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_0000059408|||http://purl.uniprot.org/annotation/PRO_0000342558|||http://purl.uniprot.org/annotation/VSP_009362 http://togogenome.org/gene/10090:Nadsyn1 ^@ http://purl.uniprot.org/uniprot/Q711T7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ CN hydrolase|||For glutaminase activity|||Glutamine-dependent NAD(+) synthetase|||Ligase|||Nucleophile; for glutaminase activity|||Proton acceptor; for glutaminase activity ^@ http://purl.uniprot.org/annotation/PRO_0000237579 http://togogenome.org/gene/10090:Clec5a ^@ http://purl.uniprot.org/uniprot/Q9R007 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 5 member A|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046633|||http://purl.uniprot.org/annotation/VSP_012840|||http://purl.uniprot.org/annotation/VSP_041577 http://togogenome.org/gene/10090:Eif2s1 ^@ http://purl.uniprot.org/uniprot/Q6ZWX6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ 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_0000137383 http://togogenome.org/gene/10090:Ucma ^@ http://purl.uniprot.org/uniprot/Q14BU0 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Ucma-N|||Unique cartilage matrix-associated protein|||Unique cartilage matrix-associated protein C-terminal fragment ^@ http://purl.uniprot.org/annotation/PRO_0000347065|||http://purl.uniprot.org/annotation/PRO_0000347066|||http://purl.uniprot.org/annotation/PRO_0000347067|||http://purl.uniprot.org/annotation/VSP_035051|||http://purl.uniprot.org/annotation/VSP_040807 http://togogenome.org/gene/10090:Atp2a1 ^@ http://purl.uniprot.org/uniprot/Q8R429 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||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|||Impaired interaction with DWORF and PLN; when associated with A-795 and A-809.|||Impaired interaction with DWORF and PLN; when associated with A-796 and A-802.|||Impaired interaction with DWORF and PLN; when associated with A-802 and A-809.|||Interaction with PLN|||Lumenal|||Phosphoserine|||Phosphothreonine|||Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000046188 http://togogenome.org/gene/10090:Shank1 ^@ http://purl.uniprot.org/uniprot/D3YZU1|||http://purl.uniprot.org/uniprot/D3YZU4|||http://purl.uniprot.org/uniprot/D3YZU5 ^@ 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|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||Disordered|||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_0000411019 http://togogenome.org/gene/10090:Dhcr24 ^@ http://purl.uniprot.org/uniprot/Q8VCH6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cleavage; by caspase|||Cytoplasmic|||Delta(24)-sterol reductase|||FAD-binding PCMH-type|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000320300 http://togogenome.org/gene/10090:Or4p20 ^@ http://purl.uniprot.org/uniprot/Q7TR18 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Prex1 ^@ http://purl.uniprot.org/uniprot/Q69ZK0 ^@ 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 ^@ DEP 1|||DEP 2|||DH|||Disordered|||In isoform 2.|||PDZ|||PH|||Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000292674|||http://purl.uniprot.org/annotation/VSP_026436 http://togogenome.org/gene/10090:Tex261 ^@ http://purl.uniprot.org/uniprot/Q62302 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Protein TEX261 ^@ http://purl.uniprot.org/annotation/PRO_0000247434 http://togogenome.org/gene/10090:Ccl22 ^@ http://purl.uniprot.org/uniprot/O88430|||http://purl.uniprot.org/uniprot/Q546S6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ C-C motif chemokine|||C-C motif chemokine 22|||Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_0000005228|||http://purl.uniprot.org/annotation/PRO_5014205870 http://togogenome.org/gene/10090:Rcl1 ^@ http://purl.uniprot.org/uniprot/Q9JJT0 ^@ Chain|||Molecule Processing ^@ Chain ^@ RNA 3'-terminal phosphate cyclase-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000156439 http://togogenome.org/gene/10090:Zbtb14 ^@ http://purl.uniprot.org/uniprot/Q08376|||http://purl.uniprot.org/uniprot/Q544H8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Motif|||Region|||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_0000047318 http://togogenome.org/gene/10090:Fxyd3 ^@ http://purl.uniprot.org/uniprot/Q3TLM3|||http://purl.uniprot.org/uniprot/Q61835 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Does not lead to glycosylation, suggesting that the non-cleavable signal sequence remains partly or entirely embedded in the membrane.|||Extracellular|||FXYD domain-containing ion transport regulator|||FXYD domain-containing ion transport regulator 3|||Helical|||Not cleaved ^@ http://purl.uniprot.org/annotation/PRO_0000010363|||http://purl.uniprot.org/annotation/PRO_5014205821 http://togogenome.org/gene/10090:Sprr3 ^@ http://purl.uniprot.org/uniprot/O09116 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat ^@ 1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||21 X 8 AA approximate tandem repeats|||3|||4|||5|||6|||7|||8|||9|||Disordered|||N-acetylserine|||Polar residues|||Pro residues|||Removed|||Small proline-rich protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000150004 http://togogenome.org/gene/10090:Srp54c ^@ http://purl.uniprot.org/uniprot/E9PXC0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ SRP54-type proteins GTP-binding ^@ http://togogenome.org/gene/10090:Tlr4 ^@ http://purl.uniprot.org/uniprot/L0CL36|||http://purl.uniprot.org/uniprot/Q9QUK6 ^@ 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|||In Lps-tolerant mice.|||In strain: A/J, BALB/cJ and SEA/GNJ.|||In strain: A/J, BALB/cJ, P/J, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK.|||In strain: A/J, BALB/cJ, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK.|||In strain: KK/HLJ.|||In strain: LP/J.|||In strain: P/J.|||In strain: SEA/GNJ.|||Interaction with SCIMP|||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 4 ^@ http://purl.uniprot.org/annotation/PRO_0000034723|||http://purl.uniprot.org/annotation/PRO_5011419740 http://togogenome.org/gene/10090:Lurap1 ^@ http://purl.uniprot.org/uniprot/A2A8F6|||http://purl.uniprot.org/uniprot/Q9D6I9 ^@ 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_0000271079 http://togogenome.org/gene/10090:Rbm8a ^@ http://purl.uniprot.org/uniprot/Q9CWZ3 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||RNA-binding protein 8A|||RRM|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000081764|||http://purl.uniprot.org/annotation/VSP_010251 http://togogenome.org/gene/10090:Or7a35 ^@ http://purl.uniprot.org/uniprot/Q8VGU6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp628 ^@ http://purl.uniprot.org/uniprot/Q8CJ78 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Splice Variant|||Zinc Finger ^@ 1|||2|||3|||4|||4 X 11 AA tandem repeats of VQLQP-[AL]-[QT]-[EG]-[VQ]-[ATV]-[ST]|||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.|||Interaction with TAF4B|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger protein 628 ^@ http://purl.uniprot.org/annotation/PRO_0000246071|||http://purl.uniprot.org/annotation/VSP_019825|||http://purl.uniprot.org/annotation/VSP_019826 http://togogenome.org/gene/10090:Aldh1l2 ^@ http://purl.uniprot.org/uniprot/Q8K009 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Aldehyde dehydrogenase domain|||Carrier|||Essential for catalytic activity|||Hydrolase domain|||Mitochondrial 10-formyltetrahydrofolate dehydrogenase|||Mitochondrion; not cleaved|||N6-acetyllysine|||N6-succinyllysine|||O-(pantetheine 4'-phosphoryl)serine|||Phosphoserine|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000316002 http://togogenome.org/gene/10090:Exoc3l4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0W9|||http://purl.uniprot.org/uniprot/Q6DIA2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Exocyst complex component 3-like protein 4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000274381 http://togogenome.org/gene/10090:Bpifb1 ^@ http://purl.uniprot.org/uniprot/Q61114 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ BPI fold-containing family B member 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017181 http://togogenome.org/gene/10090:Tlr8 ^@ http://purl.uniprot.org/uniprot/P58682 ^@ 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|||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 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 8 ^@ http://purl.uniprot.org/annotation/PRO_0000034736 http://togogenome.org/gene/10090:Gpalpp1 ^@ http://purl.uniprot.org/uniprot/Q69ZC8|||http://purl.uniprot.org/uniprot/Q9D4A1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Acidic residues|||Basic and acidic residues|||DUF3752|||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)|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000293715 http://togogenome.org/gene/10090:Rhox2a ^@ http://purl.uniprot.org/uniprot/G3UYY0|||http://purl.uniprot.org/uniprot/Q9D4Y3 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Zfp59 ^@ http://purl.uniprot.org/uniprot/P16373 ^@ 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|||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 59 ^@ http://purl.uniprot.org/annotation/PRO_0000047303 http://togogenome.org/gene/10090:Pnpla5 ^@ http://purl.uniprot.org/uniprot/Q32LZ8 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Motif|||Region|||Splice Variant ^@ DGA/G|||Disordered|||GXGXXG|||GXSXG|||In isoform 2.|||Nucleophile|||PNPLA|||Patatin-like phospholipase domain-containing protein 5|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000292022|||http://purl.uniprot.org/annotation/VSP_026374 http://togogenome.org/gene/10090:Dpysl2 ^@ http://purl.uniprot.org/uniprot/O08553 ^@ 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 ^@ Asymmetric dimethylarginine|||Delayed neurite degeneration.|||Dihydropyrimidinase-related protein 2|||Disordered|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by GSK3-beta|||Phosphothreonine; by ROCK2|||Phosphotyrosine|||Phosphotyrosine; by FYN|||Polar residues|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000165914 http://togogenome.org/gene/10090:Mrps31 ^@ http://purl.uniprot.org/uniprot/Q61733 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||Small ribosomal subunit protein mS31 ^@ http://purl.uniprot.org/annotation/PRO_0000030595 http://togogenome.org/gene/10090:Nlrp12 ^@ http://purl.uniprot.org/uniprot/E9Q5R7 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Domain Extent|||Repeat ^@ FISNA|||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_0000419758 http://togogenome.org/gene/10090:Chrm5 ^@ http://purl.uniprot.org/uniprot/Q920H4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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|||Muscarinic acetylcholine receptor M5|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069044 http://togogenome.org/gene/10090:Or6k6 ^@ http://purl.uniprot.org/uniprot/E9Q0M4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp664 ^@ http://purl.uniprot.org/uniprot/E9QPD3|||http://purl.uniprot.org/uniprot/Q4VA44 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Crosslink|||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|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 664 ^@ http://purl.uniprot.org/annotation/PRO_0000296274 http://togogenome.org/gene/10090:Syce3 ^@ http://purl.uniprot.org/uniprot/B5KM66|||http://purl.uniprot.org/uniprot/E7D6R1 ^@ Chain|||Coiled-Coil|||Helix|||Molecule Processing|||Region|||Secondary Structure ^@ Chain|||Coiled-Coil|||Helix ^@ Synaptonemal complex central element protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000367275 http://togogenome.org/gene/10090:Sema5a ^@ http://purl.uniprot.org/uniprot/Q3UPZ0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Sema ^@ http://purl.uniprot.org/annotation/PRO_5015097491 http://togogenome.org/gene/10090:Vmn1r167 ^@ http://purl.uniprot.org/uniprot/G3UW71 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cltrn ^@ http://purl.uniprot.org/uniprot/Q9ESG4 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cleavage by BACE2|||Collectrin|||Collectrin-like|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000245868 http://togogenome.org/gene/10090:Icmt ^@ http://purl.uniprot.org/uniprot/Q3U4N2|||http://purl.uniprot.org/uniprot/Q9EQK7 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Protein-S-isoprenylcysteine O-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000209895 http://togogenome.org/gene/10090:AI987944 ^@ http://purl.uniprot.org/uniprot/Q4KL68|||http://purl.uniprot.org/uniprot/Q7TPX5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Pam ^@ http://purl.uniprot.org/uniprot/A1L331|||http://purl.uniprot.org/uniprot/E9Q704|||http://purl.uniprot.org/uniprot/F8VQA4|||http://purl.uniprot.org/uniprot/P97467 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Copper type II ascorbate-dependent monooxygenase C-terminal|||Copper type II ascorbate-dependent monooxygenase N-terminal|||Cytoplasmic|||Disordered|||Helical|||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|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000006363|||http://purl.uniprot.org/annotation/PRO_0000006364|||http://purl.uniprot.org/annotation/PRO_5003245956|||http://purl.uniprot.org/annotation/PRO_5003379318 http://togogenome.org/gene/10090:Kcna2 ^@ http://purl.uniprot.org/uniprot/P63141 ^@ Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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 Pgu; chronic motor incoordination; decreases the number of functional channels at the cell surface.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphotyrosine|||Potassium voltage-gated channel subfamily A member 2|||S-palmitoyl cysteine|||S4-S5 linker|||Selectivity filter|||Tetramerization domain ^@ http://purl.uniprot.org/annotation/PRO_0000053973 http://togogenome.org/gene/10090:Ern1 ^@ http://purl.uniprot.org/uniprot/Q9EQY0 ^@ 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|||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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes endoribonuclease activity.|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Interacts with hydroxy-aryl-aldehyde inhibitors|||KEN|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor; for protein kinase activity|||Serine/threonine-protein kinase/endoribonuclease IRE1 ^@ http://purl.uniprot.org/annotation/PRO_0000024328|||http://purl.uniprot.org/annotation/VSP_050794|||http://purl.uniprot.org/annotation/VSP_050795 http://togogenome.org/gene/10090:Ndufv1 ^@ http://purl.uniprot.org/uniprot/Q91YT0 ^@ Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Strand|||Transit Peptide|||Turn ^@ Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial|||Omega-N-methylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000019978 http://togogenome.org/gene/10090:Tnfrsf19 ^@ http://purl.uniprot.org/uniprot/Q8BUM7|||http://purl.uniprot.org/uniprot/Q9JLL3 ^@ 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.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3; truncated|||TNFR-Cys domain-containing protein|||Tumor necrosis factor receptor superfamily member 19 ^@ http://purl.uniprot.org/annotation/PRO_0000034598|||http://purl.uniprot.org/annotation/PRO_5004307236|||http://purl.uniprot.org/annotation/VSP_006513|||http://purl.uniprot.org/annotation/VSP_006514|||http://purl.uniprot.org/annotation/VSP_006515|||http://purl.uniprot.org/annotation/VSP_006516|||http://purl.uniprot.org/annotation/VSP_006517|||http://purl.uniprot.org/annotation/VSP_006518 http://togogenome.org/gene/10090:Serpinb11 ^@ http://purl.uniprot.org/uniprot/Q9CQV3 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Region|||Sequence Conflict|||Site ^@ RCL|||Reactive bond|||Serpin B11 ^@ http://purl.uniprot.org/annotation/PRO_0000094118 http://togogenome.org/gene/10090:Dennd2d ^@ http://purl.uniprot.org/uniprot/Q91VV4|||http://purl.uniprot.org/uniprot/S4R219 ^@ 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 ^@ DENN domain-containing protein 2D|||Disordered|||In isoform 2.|||Polar residues|||UDENN|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000242687|||http://purl.uniprot.org/annotation/VSP_019472 http://togogenome.org/gene/10090:Krt9 ^@ http://purl.uniprot.org/uniprot/Q6RHW0 ^@ 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 ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type I cytoskeletal 9|||Linker 1|||Linker 12|||Phosphoserine|||Polar residues|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000308372 http://togogenome.org/gene/10090:Kctd20 ^@ http://purl.uniprot.org/uniprot/Q8CDD8 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ BTB|||BTB/POZ domain-containing protein KCTD20|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000255249|||http://purl.uniprot.org/annotation/VSP_021279 http://togogenome.org/gene/10090:Arhgap36 ^@ http://purl.uniprot.org/uniprot/B1AUC7 ^@ 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.|||In isoform 3.|||Rho GTPase-activating protein 36|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000394288|||http://purl.uniprot.org/annotation/VSP_039237|||http://purl.uniprot.org/annotation/VSP_039238 http://togogenome.org/gene/10090:Mbd3l1 ^@ http://purl.uniprot.org/uniprot/Q0P5Y0|||http://purl.uniprot.org/uniprot/Q9D9H3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Methyl-CpG binding protein 2/3 C-terminal|||Methyl-CpG-binding|||Methyl-CpG-binding domain protein 3-like 1|||Transcription repressor ^@ http://purl.uniprot.org/annotation/PRO_0000096252 http://togogenome.org/gene/10090:Tom1l2 ^@ http://purl.uniprot.org/uniprot/Q5SRX1 ^@ 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 ^@ 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_0000278791|||http://purl.uniprot.org/annotation/VSP_023393|||http://purl.uniprot.org/annotation/VSP_023394|||http://purl.uniprot.org/annotation/VSP_023395|||http://purl.uniprot.org/annotation/VSP_023396|||http://purl.uniprot.org/annotation/VSP_023397|||http://purl.uniprot.org/annotation/VSP_023398|||http://purl.uniprot.org/annotation/VSP_023399 http://togogenome.org/gene/10090:Rtl4 ^@ http://purl.uniprot.org/uniprot/Q3URY0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Sequence Conflict|||Zinc Finger ^@ CCHC-type|||Retrotransposon Gag-like protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000257495 http://togogenome.org/gene/10090:Fcer1g ^@ http://purl.uniprot.org/uniprot/P20491 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||High affinity immunoglobulin epsilon receptor subunit gamma|||ITAM|||Impairs IgE-induced mast cell activation in the presence of antigen; Impairs IgE-induced mast cell survival in the absence of antigen.|||Impairs IgE-induced mast cell activation in the presence of antigen; Impairs IgE-induced mast cell survival in the absence of antigen; when associated with P-65. Impairs IL3-induced production of IL4 by basophils; when associated with P-65.|||Impairs IgE-induced mast cell activation in the presence of antigen; Impairs IgE-induced mast cell survival in the absence of antigen; when associated with P-76. Impairs IL3-induced production of IL4 by basophils; when associated with P-76.|||Impairs interaction with CSF2RB. Impairs IL3-induced production of IL4 by basophils.|||Increases IL3-induced production of IL4 by basophils.|||Interchain|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000016503 http://togogenome.org/gene/10090:Arhgef4 ^@ http://purl.uniprot.org/uniprot/Q3TQN9|||http://purl.uniprot.org/uniprot/Q7TNR9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DH|||Disordered|||PH|||Rho guanine nucleotide exchange factor 4|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000080915 http://togogenome.org/gene/10090:Serpinb3c ^@ http://purl.uniprot.org/uniprot/A2RSF9|||http://purl.uniprot.org/uniprot/Q9D1E7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Gm1979 ^@ http://purl.uniprot.org/uniprot/E9QAN3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Vmn1r194 ^@ http://purl.uniprot.org/uniprot/J3JS27 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:AW551984 ^@ http://purl.uniprot.org/uniprot/Q8BGF0|||http://purl.uniprot.org/uniprot/Q8C1D4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ VIT|||VWFA ^@ http://togogenome.org/gene/10090:Slc35a3 ^@ http://purl.uniprot.org/uniprot/Q8R1T4 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Mutagenesis Site|||Sequence Conflict|||Transmembrane ^@ Abolishes protein expression.|||Almost completely inactive UDP-GlcNAc transport activity.|||Almost completely inactive UDP-GlcNAc transport activity. Does not affect membrane localization.|||Completely abolishes the biosynthesis of GlcNAc glycoconjugates.|||Decreases UDP-GlcNAc transport activity.|||Does not affect UDP-GlcNAc transport activity.|||Helical|||Increases UDP-GlcNAc transport activity.|||Severe impairment of UDP-GlcNAc transport activity.|||Severe impairment of UDP-GlcNAc transport activity. Does not affect membrane localization.|||UDP-N-acetylglucosamine transporter ^@ http://purl.uniprot.org/annotation/PRO_0000213358 http://togogenome.org/gene/10090:Tmem147 ^@ http://purl.uniprot.org/uniprot/B2RVQ1|||http://purl.uniprot.org/uniprot/Q9CQG6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ BOS complex subunit TMEM147|||Cytoplasmic|||Helical|||In isoform 2.|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000271702|||http://purl.uniprot.org/annotation/VSP_022328|||http://purl.uniprot.org/annotation/VSP_022329 http://togogenome.org/gene/10090:Fbxo6 ^@ http://purl.uniprot.org/uniprot/Q9QZN4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ F-box|||F-box only protein 6|||FBA|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000119883 http://togogenome.org/gene/10090:Capsl ^@ http://purl.uniprot.org/uniprot/Q6P8Y1 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Calcyphosin-like protein|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4 ^@ http://purl.uniprot.org/annotation/PRO_0000264474 http://togogenome.org/gene/10090:Or7h8 ^@ http://purl.uniprot.org/uniprot/Q7TRF0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gsg1 ^@ http://purl.uniprot.org/uniprot/Q8R1W2 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Germ cell-specific gene 1 protein|||Helical|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4. ^@ http://purl.uniprot.org/annotation/PRO_0000329462|||http://purl.uniprot.org/annotation/VSP_032998|||http://purl.uniprot.org/annotation/VSP_032999|||http://purl.uniprot.org/annotation/VSP_033000|||http://purl.uniprot.org/annotation/VSP_033001 http://togogenome.org/gene/10090:Phf21a ^@ http://purl.uniprot.org/uniprot/A0A498WGG5|||http://purl.uniprot.org/uniprot/A2AHG3|||http://purl.uniprot.org/uniprot/A2AHG4|||http://purl.uniprot.org/uniprot/D3Z764|||http://purl.uniprot.org/uniprot/Q6ZPK0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ A.T hook|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3, isoform 5, isoform 6, isoform 7, isoform 9 and isoform 8.|||In isoform 3, isoform 6 and isoform 8.|||In isoform 4, isoform 5, isoform 7 and isoform 9.|||In isoform 6, isoform 5 and isoform 4.|||In isoform 7 and isoform 8.|||PHD finger protein 21A|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000226768|||http://purl.uniprot.org/annotation/VSP_060156|||http://purl.uniprot.org/annotation/VSP_060157|||http://purl.uniprot.org/annotation/VSP_060158|||http://purl.uniprot.org/annotation/VSP_060159|||http://purl.uniprot.org/annotation/VSP_060160|||http://purl.uniprot.org/annotation/VSP_060161 http://togogenome.org/gene/10090:Rims2 ^@ http://purl.uniprot.org/uniprot/D9HP81|||http://purl.uniprot.org/uniprot/Q0VF51|||http://purl.uniprot.org/uniprot/Q9EQZ7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C2|||C2 1|||C2 2|||Disordered|||FYVE-type|||In isoform 2.|||In isoform 3.|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RabBD|||Regulating synaptic membrane exocytosis protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000190202|||http://purl.uniprot.org/annotation/VSP_008181|||http://purl.uniprot.org/annotation/VSP_008182|||http://purl.uniprot.org/annotation/VSP_008183|||http://purl.uniprot.org/annotation/VSP_008184 http://togogenome.org/gene/10090:Or2y11 ^@ http://purl.uniprot.org/uniprot/Q7TQT4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdc42bpb ^@ http://purl.uniprot.org/uniprot/Q7TT50 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ AGC-kinase C-terminal|||Basic and acidic residues|||CNH|||CRIB|||Disordered|||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_0000086395 http://togogenome.org/gene/10090:Dtx3l ^@ http://purl.uniprot.org/uniprot/Q3UIR3 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase DTX3L|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||RING-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000390470|||http://purl.uniprot.org/annotation/VSP_038533 http://togogenome.org/gene/10090:Zscan25 ^@ http://purl.uniprot.org/uniprot/B2RX31 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues|||SCAN box ^@ http://togogenome.org/gene/10090:H2bc13 ^@ http://purl.uniprot.org/uniprot/P10853 ^@ 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-F/J/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-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_0000071839 http://togogenome.org/gene/10090:Tdpoz9 ^@ http://purl.uniprot.org/uniprot/P0DMR6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ BTB|||MATH|||TD and POZ domain-containing protein 1-like ^@ http://purl.uniprot.org/annotation/PRO_0000431621 http://togogenome.org/gene/10090:Axin2 ^@ http://purl.uniprot.org/uniprot/O88566|||http://purl.uniprot.org/uniprot/Q3UQK5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Axin-2|||DIX|||Disordered|||Interaction with GSK3B|||Interaction with beta-catenin|||Polar residues|||RGS|||Tankyrase-binding motif ^@ http://purl.uniprot.org/annotation/PRO_0000220896 http://togogenome.org/gene/10090:Ptchd1 ^@ http://purl.uniprot.org/uniprot/Q14B62 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Patched domain-containing protein 1|||SSD ^@ http://purl.uniprot.org/annotation/PRO_0000280041|||http://purl.uniprot.org/annotation/VSP_023514 http://togogenome.org/gene/10090:Sypl ^@ http://purl.uniprot.org/uniprot/O09117|||http://purl.uniprot.org/uniprot/Q3TVX7 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||MARVEL|||N-linked (GlcNAc...) asparagine|||Synaptophysin-like protein 1|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000179165|||http://purl.uniprot.org/annotation/VSP_008558 http://togogenome.org/gene/10090:Adh4 ^@ http://purl.uniprot.org/uniprot/Q9QYY9 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn ^@ All-trans-retinol dehydrogenase [NAD(+)] ADH4|||No effect.|||Strongly increases NAD-retinol dehydrogenase activity.|||Strongly increases activity towards ethanol, increases KM for benzoquinone 10-fold. ^@ http://purl.uniprot.org/annotation/PRO_0000160682 http://togogenome.org/gene/10090:Prpf8 ^@ http://purl.uniprot.org/uniprot/Q3UNG1|||http://purl.uniprot.org/uniprot/Q99PV0 ^@ 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 ^@ Important for branch point selection|||Involved in interaction with pre-mRNA 5' splice site|||Linker|||MPN|||N-acetylalanine|||N6,N6-dimethyllysine|||N6-acetyllysine|||PRO8NT|||PROCN|||Phosphoserine|||Pre-mRNA-processing-splicing factor 8|||RNA recognition motif spliceosomal PrP8|||RNase H homology domain|||Removed|||Required for interaction with EFTUD2 and SNRNP200|||Restriction endonuclease homology domain|||Reverse transcriptase homology domain ^@ http://purl.uniprot.org/annotation/PRO_0000097041 http://togogenome.org/gene/10090:Egflam ^@ http://purl.uniprot.org/uniprot/Q4VBE4 ^@ 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 ^@ EGF-like 1|||EGF-like 2|||EGF-like 3|||Fibronectin type-III 1|||Fibronectin type-III 2|||In isoform 2.|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||N-linked (GlcNAc...) asparagine|||Pikachurin ^@ http://purl.uniprot.org/annotation/PRO_0000306804|||http://purl.uniprot.org/annotation/VSP_028482 http://togogenome.org/gene/10090:Fbxw20 ^@ http://purl.uniprot.org/uniprot/Q5U467 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Cd1d1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J090|||http://purl.uniprot.org/uniprot/P11609 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Antigen-presenting glycoprotein CD1d1|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Internalization signal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014591|||http://purl.uniprot.org/annotation/PRO_5015044285 http://togogenome.org/gene/10090:Parp9 ^@ http://purl.uniprot.org/uniprot/Q8CAS9 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||Macro 1|||Macro 2|||PARP catalytic|||Phosphoserine|||Protein mono-ADP-ribosyltransferase PARP9 ^@ http://purl.uniprot.org/annotation/PRO_0000211340|||http://purl.uniprot.org/annotation/VSP_008506|||http://purl.uniprot.org/annotation/VSP_008507 http://togogenome.org/gene/10090:L1cam ^@ http://purl.uniprot.org/uniprot/A2AFG8|||http://purl.uniprot.org/uniprot/Q6PGJ3 ^@ 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|||Fibronectin type-III|||Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5002642665|||http://purl.uniprot.org/annotation/PRO_5015098434 http://togogenome.org/gene/10090:Or51b6 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSF4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tshz2 ^@ http://purl.uniprot.org/uniprot/Q68FE9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||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|||Phosphoserine|||Polar residues|||Teashirt homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000047065 http://togogenome.org/gene/10090:Cd6 ^@ http://purl.uniprot.org/uniprot/Q61003 ^@ 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 ^@ Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Pro residues|||SRCR 1|||SRCR 2|||SRCR 3|||T-cell differentiation antigen CD6 ^@ http://purl.uniprot.org/annotation/PRO_0000033228|||http://purl.uniprot.org/annotation/VSP_006224|||http://purl.uniprot.org/annotation/VSP_006225|||http://purl.uniprot.org/annotation/VSP_006226 http://togogenome.org/gene/10090:Olfml3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J086|||http://purl.uniprot.org/uniprot/Q8BK62 ^@ 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 ^@ N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Olfactomedin-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000020093|||http://purl.uniprot.org/annotation/PRO_5006451954 http://togogenome.org/gene/10090:Sdr39u1 ^@ http://purl.uniprot.org/uniprot/Q5M8N4 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Epimerase family protein SDR39U1 ^@ http://purl.uniprot.org/annotation/PRO_0000279749 http://togogenome.org/gene/10090:Gykl1 ^@ http://purl.uniprot.org/uniprot/Q8C635 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Carbohydrate kinase FGGY C-terminal|||Carbohydrate kinase FGGY N-terminal|||Helical ^@ http://togogenome.org/gene/10090:Chrna6 ^@ http://purl.uniprot.org/uniprot/Q9R0W9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Associated with receptor activation|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-6|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000000361 http://togogenome.org/gene/10090:Polr2j ^@ http://purl.uniprot.org/uniprot/Q3TYI2|||http://purl.uniprot.org/uniprot/Q6PI63 ^@ Domain Extent|||Region ^@ Domain Extent ^@ DNA-directed RNA polymerase RBP11-like dimerisation ^@ http://togogenome.org/gene/10090:Crybg2 ^@ http://purl.uniprot.org/uniprot/A0A2I3BQG2|||http://purl.uniprot.org/uniprot/B7ZCC2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Beta/gamma crystallin 'Greek key'|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Vsig1 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1E9|||http://purl.uniprot.org/uniprot/Q9D2J4 ^@ 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|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||V-set and immunoglobulin domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000313574|||http://purl.uniprot.org/annotation/PRO_5002091785|||http://purl.uniprot.org/annotation/VSP_030028 http://togogenome.org/gene/10090:Adgre1 ^@ http://purl.uniprot.org/uniprot/Q3U9R0|||http://purl.uniprot.org/uniprot/Q61549 ^@ 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|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Adhesion G protein-coupled receptor E1|||Cell attachment site|||Cytoplasmic|||EGF-like|||EGF-like 1|||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|||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_0000012874|||http://purl.uniprot.org/annotation/PRO_5014309184 http://togogenome.org/gene/10090:Usp42 ^@ http://purl.uniprot.org/uniprot/B2RQC2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 42 ^@ http://purl.uniprot.org/annotation/PRO_0000404199 http://togogenome.org/gene/10090:Trmt44 ^@ http://purl.uniprot.org/uniprot/Q9D2Q2 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ C3H1-type|||Disordered|||Phosphoserine|||Probable tRNA (uracil-O(2)-)-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000249895 http://togogenome.org/gene/10090:Ccn2 ^@ http://purl.uniprot.org/uniprot/P29268 ^@ 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 ^@ CCN family member 2|||CTCK|||Heparin-binding|||IGFBP N-terminal|||TSP type-1|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000014403 http://togogenome.org/gene/10090:Slc39a2 ^@ http://purl.uniprot.org/uniprot/G3X943 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Critical for the pH sensitivity|||Cytoplasmic|||Extracellular|||Helical|||Zinc transporter ZIP2 ^@ http://purl.uniprot.org/annotation/PRO_0000458161 http://togogenome.org/gene/10090:Slc22a18 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0P7|||http://purl.uniprot.org/uniprot/Q78KK3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ Helical|||Major facilitator superfamily (MFS) profile|||Solute carrier family 22 member 18 ^@ http://purl.uniprot.org/annotation/PRO_0000220510 http://togogenome.org/gene/10090:Hic1 ^@ http://purl.uniprot.org/uniprot/Q9R1Y5|||http://purl.uniprot.org/uniprot/Z4YJP0 ^@ 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|||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 SUMO); alternate|||Hypermethylated in cancer 1 protein|||Interaction with CTBP1|||Mediates HDAC-dependent transcriptional repression|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000046943 http://togogenome.org/gene/10090:Nup153 ^@ http://purl.uniprot.org/uniprot/E9Q3G8|||http://purl.uniprot.org/uniprot/Q3V3W1|||http://purl.uniprot.org/uniprot/Q8BRF6 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||RanBP2-type ^@ http://togogenome.org/gene/10090:Galnt3 ^@ http://purl.uniprot.org/uniprot/P70419 ^@ 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|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 3|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059107 http://togogenome.org/gene/10090:Or51a24 ^@ http://purl.uniprot.org/uniprot/Q7TRQ1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp951 ^@ http://purl.uniprot.org/uniprot/A0A087WRH0|||http://purl.uniprot.org/uniprot/Q3V1G7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Gzmk ^@ http://purl.uniprot.org/uniprot/O35205 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Granzyme K|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027417|||http://purl.uniprot.org/annotation/PRO_0000027418 http://togogenome.org/gene/10090:Minpp1 ^@ http://purl.uniprot.org/uniprot/Q9Z2L6 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Loss of phosphatase activity.|||Multiple inositol polyphosphate phosphatase 1|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000019583 http://togogenome.org/gene/10090:Gpbar1 ^@ http://purl.uniprot.org/uniprot/Q14AA9|||http://purl.uniprot.org/uniprot/Q80SS6 ^@ 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 bile acid 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-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069501 http://togogenome.org/gene/10090:Fuca2 ^@ http://purl.uniprot.org/uniprot/Q505Q3|||http://purl.uniprot.org/uniprot/Q99KR8 ^@ 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|||Sequence Conflict|||Signal Peptide|||Site ^@ Alpha-L-fucosidase|||Alpha-L-fucosidase C-terminal|||May be important for catalysis|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Plasma alpha-L-fucosidase ^@ http://purl.uniprot.org/annotation/PRO_0000010313|||http://purl.uniprot.org/annotation/PRO_5014309461 http://togogenome.org/gene/10090:Ptprc ^@ http://purl.uniprot.org/uniprot/P06800|||http://purl.uniprot.org/uniprot/Q8C6Q7|||http://purl.uniprot.org/uniprot/S4R1M0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||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|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Receptor-type tyrosine-protein phosphatase C|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2|||protein-tyrosine-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000025471|||http://purl.uniprot.org/annotation/PRO_5004304345|||http://purl.uniprot.org/annotation/PRO_5004522286|||http://purl.uniprot.org/annotation/VSP_059410|||http://purl.uniprot.org/annotation/VSP_059411 http://togogenome.org/gene/10090:Msmp ^@ http://purl.uniprot.org/uniprot/B1AWI6 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Region|||Signal Peptide ^@ Disordered|||Prostate-associated microseminoprotein ^@ http://purl.uniprot.org/annotation/PRO_0000338649 http://togogenome.org/gene/10090:Rfwd3 ^@ http://purl.uniprot.org/uniprot/Q8CIK8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RFWD3|||Phosphoserine; by ATM and ATR|||Polar residues|||RING-type; degenerate|||WD 1|||WD 2|||WD 3 ^@ http://purl.uniprot.org/annotation/PRO_0000278235 http://togogenome.org/gene/10090:Bcam ^@ http://purl.uniprot.org/uniprot/Q9R069 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basal cell adhesion molecule|||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 V-type 1|||Ig-like V-type 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000383338 http://togogenome.org/gene/10090:Fancc ^@ http://purl.uniprot.org/uniprot/P50652|||http://purl.uniprot.org/uniprot/Q3UI88 ^@ 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|||Disordered|||Fanconi anemia group C protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000087185 http://togogenome.org/gene/10090:Psmb6 ^@ http://purl.uniprot.org/uniprot/Q60692 ^@ 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_0000026615|||http://purl.uniprot.org/annotation/PRO_0000026616 http://togogenome.org/gene/10090:Trim34a ^@ http://purl.uniprot.org/uniprot/Q99PP6 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM34A|||In isoform Beta.|||In isoform Gamma.|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056249|||http://purl.uniprot.org/annotation/VSP_011923|||http://purl.uniprot.org/annotation/VSP_011924|||http://purl.uniprot.org/annotation/VSP_011925|||http://purl.uniprot.org/annotation/VSP_011926 http://togogenome.org/gene/10090:Ccdc74a ^@ http://purl.uniprot.org/uniprot/E9Q9U8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||CCDC92/74 N-terminal|||Coiled coil protein 74 C-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Pus3 ^@ http://purl.uniprot.org/uniprot/Q9JI38 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ N-acetylalanine|||Nucleophile|||Removed|||tRNA pseudouridine(38/39) synthase ^@ http://purl.uniprot.org/annotation/PRO_0000057521 http://togogenome.org/gene/10090:Ccni ^@ http://purl.uniprot.org/uniprot/Q8C7E2|||http://purl.uniprot.org/uniprot/Q9Z2V9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Cyclin-I|||Cyclin-like|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000080477 http://togogenome.org/gene/10090:Rps11 ^@ http://purl.uniprot.org/uniprot/P62281|||http://purl.uniprot.org/uniprot/Q3UC02 ^@ Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue ^@ Citrulline|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Removed|||S-palmitoyl cysteine|||Small ribosomal subunit protein uS17|||Small ribosomal subunit protein uS17 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000128511 http://togogenome.org/gene/10090:Map3k4 ^@ http://purl.uniprot.org/uniprot/O08648 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Disordered|||In isoform B.|||Loss of kinase activity.|||Mitogen-activated protein kinase kinase kinase 4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086248|||http://purl.uniprot.org/annotation/VSP_004885 http://togogenome.org/gene/10090:Wnt6 ^@ http://purl.uniprot.org/uniprot/P22727 ^@ 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|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-6 ^@ http://purl.uniprot.org/annotation/PRO_0000041441 http://togogenome.org/gene/10090:Obsl1 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1L4|||http://purl.uniprot.org/uniprot/D3YYU8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ 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.|||Interaction with TTN|||Obscurin-like protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000430250|||http://purl.uniprot.org/annotation/VSP_055905|||http://purl.uniprot.org/annotation/VSP_055906|||http://purl.uniprot.org/annotation/VSP_055907 http://togogenome.org/gene/10090:Braf ^@ http://purl.uniprot.org/uniprot/P28028 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 1.|||N-acetylalanine|||Omega-N-methylarginine; by PRMT5|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||RBD|||Removed|||Serine/threonine-protein kinase B-raf ^@ http://purl.uniprot.org/annotation/PRO_0000085666|||http://purl.uniprot.org/annotation/VSP_060878|||http://purl.uniprot.org/annotation/VSP_060879|||http://purl.uniprot.org/annotation/VSP_060880 http://togogenome.org/gene/10090:Vezt ^@ http://purl.uniprot.org/uniprot/D3Z4E6|||http://purl.uniprot.org/uniprot/Q3ZK22 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Myosin-binding|||Polar residues|||Vezatin ^@ http://purl.uniprot.org/annotation/PRO_0000349248|||http://purl.uniprot.org/annotation/VSP_035268|||http://purl.uniprot.org/annotation/VSP_035269|||http://purl.uniprot.org/annotation/VSP_035270|||http://purl.uniprot.org/annotation/VSP_035271|||http://purl.uniprot.org/annotation/VSP_035272|||http://purl.uniprot.org/annotation/VSP_035273|||http://purl.uniprot.org/annotation/VSP_035274 http://togogenome.org/gene/10090:Aen ^@ http://purl.uniprot.org/uniprot/Q9CZI9 ^@ 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 ^@ Apoptosis-enhancing nuclease|||Basic residues|||Disordered|||Exonuclease|||In isoform 2.|||Nuclear localization signal|||Nucleolar localization signal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000324089|||http://purl.uniprot.org/annotation/VSP_032133 http://togogenome.org/gene/10090:Sltm ^@ http://purl.uniprot.org/uniprot/B9EI57|||http://purl.uniprot.org/uniprot/Q8CH25 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||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)|||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_0000307799|||http://purl.uniprot.org/annotation/VSP_028834 http://togogenome.org/gene/10090:Cx3cr1 ^@ http://purl.uniprot.org/uniprot/Q543X3|||http://purl.uniprot.org/uniprot/Q9Z0D9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Abolished activity without affecting avility to bind CX3CL1.|||CX3C chemokine 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 DR/NN; abolished activity without affecting avility to bind CX3CL1.|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000069327 http://togogenome.org/gene/10090:Ugt2a1 ^@ http://purl.uniprot.org/uniprot/Q80X89 ^@ 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|||N6-succinyllysine|||UDP-glucuronosyltransferase 2A1 ^@ http://purl.uniprot.org/annotation/PRO_0000299143 http://togogenome.org/gene/10090:Ttc32 ^@ http://purl.uniprot.org/uniprot/Q9DAC7 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 32 ^@ http://purl.uniprot.org/annotation/PRO_0000263101 http://togogenome.org/gene/10090:Hyal6 ^@ http://purl.uniprot.org/uniprot/Q9D4E9 ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Transmembrane ^@ Helical|||Hyaluronidase|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_5015099682 http://togogenome.org/gene/10090:Plpp3 ^@ http://purl.uniprot.org/uniprot/Q99JY8 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dityrosine basolateral targeting motif|||Extracellular|||Helical|||Integrin-binding motif|||Mediates interaction with CTNND1|||N-linked (GlcNAc...) asparagine|||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_0000220913 http://togogenome.org/gene/10090:Harbi1 ^@ http://purl.uniprot.org/uniprot/Q8BR93 ^@ 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 ^@ DDE Tnp4|||In isoform 2.|||In isoform 3.|||Putative nuclease HARBI1 ^@ http://purl.uniprot.org/annotation/PRO_0000263615|||http://purl.uniprot.org/annotation/VSP_021876|||http://purl.uniprot.org/annotation/VSP_021877|||http://purl.uniprot.org/annotation/VSP_021878|||http://purl.uniprot.org/annotation/VSP_021879 http://togogenome.org/gene/10090:Rtraf ^@ http://purl.uniprot.org/uniprot/Q9CQE8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ N6-acetyllysine|||RNA transcription, translation and transport factor protein ^@ http://purl.uniprot.org/annotation/PRO_0000089957 http://togogenome.org/gene/10090:Pea15a ^@ http://purl.uniprot.org/uniprot/Q62048 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Turn ^@ Abolishes inhibitory effect on FAS-mediated apoptosis. Does not change effect on TNFRSF1A-mediated apoptosis.|||Astrocytic phosphoprotein PEA-15|||DED|||In isoform 2.|||Microtubule-binding|||Phosphoserine|||Phosphoserine; by CaMK2|||Phosphoserine; by PKC ^@ http://purl.uniprot.org/annotation/PRO_0000191283|||http://purl.uniprot.org/annotation/VSP_007736|||http://purl.uniprot.org/annotation/VSP_007737 http://togogenome.org/gene/10090:Edem3 ^@ http://purl.uniprot.org/uniprot/A0A087WQK5|||http://purl.uniprot.org/uniprot/A0A087WR24|||http://purl.uniprot.org/uniprot/B7ZNP0|||http://purl.uniprot.org/uniprot/Q2HXL6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||ER degradation-enhancing alpha-mannosidase-like protein 3|||Loss of ERAD activity.|||N-linked (GlcNAc...) asparagine|||PA|||Polar residues|||Prevents secretion from ER|||Proton donor|||alpha-1,2-Mannosidase ^@ http://purl.uniprot.org/annotation/PRO_0000316958|||http://purl.uniprot.org/annotation/PRO_5001831788|||http://purl.uniprot.org/annotation/PRO_5001831840|||http://purl.uniprot.org/annotation/PRO_5015087444 http://togogenome.org/gene/10090:Ints6 ^@ http://purl.uniprot.org/uniprot/Q6PCM2 ^@ 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.|||In isoform 3.|||Integrator complex subunit 6|||Phosphoserine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000259544|||http://purl.uniprot.org/annotation/VSP_021459|||http://purl.uniprot.org/annotation/VSP_021460|||http://purl.uniprot.org/annotation/VSP_021461|||http://purl.uniprot.org/annotation/VSP_021462 http://togogenome.org/gene/10090:Or1j20 ^@ http://purl.uniprot.org/uniprot/Q8VGJ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or8g18 ^@ http://purl.uniprot.org/uniprot/P34983 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||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|||Olfactory receptor 8G18 ^@ http://purl.uniprot.org/annotation/PRO_0000150821 http://togogenome.org/gene/10090:Sfxn5 ^@ http://purl.uniprot.org/uniprot/Q925N0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Sideroflexin-5 ^@ http://purl.uniprot.org/annotation/PRO_0000177044 http://togogenome.org/gene/10090:Nifk ^@ http://purl.uniprot.org/uniprot/Q91VE6 ^@ 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 ^@ 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|||In isoform 2.|||MKI67 FHA domain-interacting nucleolar phosphoprotein|||N-acetylalanine|||Omega-N-methylarginine|||Omega-N-methylated arginine|||Phosphoserine|||Phosphothreonine|||RRM|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000081630|||http://purl.uniprot.org/annotation/VSP_014634 http://togogenome.org/gene/10090:Kcnk12 ^@ http://purl.uniprot.org/uniprot/Q76M80 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Potassium channel ^@ http://togogenome.org/gene/10090:Stx2 ^@ http://purl.uniprot.org/uniprot/Q3TJ55|||http://purl.uniprot.org/uniprot/Q80W45 ^@ Coiled-Coil|||Domain Extent|||Region|||Transmembrane ^@ Coiled-Coil|||Domain Extent|||Transmembrane ^@ Helical|||T-SNARE coiled-coil homology ^@ http://togogenome.org/gene/10090:Kcnk10 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VJZ9|||http://purl.uniprot.org/uniprot/F6YU65|||http://purl.uniprot.org/uniprot/Q3LS20|||http://purl.uniprot.org/uniprot/Q8BUW1|||http://purl.uniprot.org/uniprot/Q8BZB0|||http://purl.uniprot.org/uniprot/Q9CX88 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Potassium channel|||Potassium channel domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5004303846|||http://purl.uniprot.org/annotation/PRO_5015099077 http://togogenome.org/gene/10090:Prrc2b ^@ http://purl.uniprot.org/uniprot/F8WHT3|||http://purl.uniprot.org/uniprot/Q7TPM1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ BAT2 N-terminal|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein PRRC2B ^@ http://purl.uniprot.org/annotation/PRO_0000274482|||http://purl.uniprot.org/annotation/VSP_022764|||http://purl.uniprot.org/annotation/VSP_022765 http://togogenome.org/gene/10090:Npc2 ^@ http://purl.uniprot.org/uniprot/Q9Z0J0 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Signal Peptide ^@ Decreased cholesterol binding. Nearly abolishes cholesterol transport activity.|||Decreased cholesterol binding. Strongly decreased cholesterol transport activity.|||Loss of cholesterol binding. Abolishes cholesterol transport activity.|||Loss of cholesterol binding. Abolishes cholesterol transport activity. Abolishes stimulation of biliary cholesterol secretion.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||NPC intracellular cholesterol transporter 2|||No effect on cholesterol binding. Strongly decreased cholesterol transport activity.|||No significant effect on biliary cholesterol secretion.|||Strongly decreased cholesterol export. ^@ http://purl.uniprot.org/annotation/PRO_0000019856 http://togogenome.org/gene/10090:Ssxb5 ^@ http://purl.uniprot.org/uniprot/Q6XAS2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB|||KRAB-related ^@ http://togogenome.org/gene/10090:3300002I08Rik ^@ http://purl.uniprot.org/uniprot/Q9CXH3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB ^@ http://togogenome.org/gene/10090:Or9g3 ^@ http://purl.uniprot.org/uniprot/Q8VFJ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Xpnpep3 ^@ http://purl.uniprot.org/uniprot/B7ZMP1 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Region|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Interaction with TNFRSF1B|||Mitochondrion|||Xaa-Pro aminopeptidase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000401208|||http://purl.uniprot.org/annotation/VSP_040145|||http://purl.uniprot.org/annotation/VSP_040146 http://togogenome.org/gene/10090:Cyp11b1 ^@ http://purl.uniprot.org/uniprot/Q3TG86|||http://purl.uniprot.org/uniprot/Q3UQH5 ^@ Binding Site|||Site ^@ Binding Site ^@ axial binding residue ^@ http://togogenome.org/gene/10090:Cfap43 ^@ http://purl.uniprot.org/uniprot/E9Q7R9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Cilia- and flagella-associated protein 43|||Disordered|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000445512 http://togogenome.org/gene/10090:Fn3k ^@ http://purl.uniprot.org/uniprot/Q9ER35 ^@ 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_0000216338 http://togogenome.org/gene/10090:Ier3ip1 ^@ http://purl.uniprot.org/uniprot/Q9CR20 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Immediate early response 3-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000257962 http://togogenome.org/gene/10090:Mro ^@ http://purl.uniprot.org/uniprot/E9PUF9|||http://purl.uniprot.org/uniprot/E9QNX2|||http://purl.uniprot.org/uniprot/Q7TNB4 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||HEAT|||Protein maestro ^@ http://purl.uniprot.org/annotation/PRO_0000248199 http://togogenome.org/gene/10090:Cdsn ^@ http://purl.uniprot.org/uniprot/Q7TPC1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide ^@ Corneodesmosin|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000020914 http://togogenome.org/gene/10090:Rsrp1 ^@ http://purl.uniprot.org/uniprot/Q3UC65 ^@ 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 ^@ Arginine/serine-rich protein 1|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000297619|||http://purl.uniprot.org/annotation/VSP_027308|||http://purl.uniprot.org/annotation/VSP_027309|||http://purl.uniprot.org/annotation/VSP_027310 http://togogenome.org/gene/10090:Nlrp5 ^@ http://purl.uniprot.org/uniprot/Q9R1M5 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In strain: 129/Sv and CBA/J.|||In strain: 129/Sv; requires 2 nucleotide substitutions.|||In strain: A/J.|||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 5|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080891|||http://purl.uniprot.org/annotation/VSP_024726|||http://purl.uniprot.org/annotation/VSP_024727|||http://purl.uniprot.org/annotation/VSP_024728|||http://purl.uniprot.org/annotation/VSP_024729|||http://purl.uniprot.org/annotation/VSP_024730|||http://purl.uniprot.org/annotation/VSP_024731|||http://purl.uniprot.org/annotation/VSP_024732|||http://purl.uniprot.org/annotation/VSP_024733 http://togogenome.org/gene/10090:Ceacam15 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1L0 ^@ 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 ^@ Carcinoembryonic antigen-related cell adhesion molecule 15|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000442297 http://togogenome.org/gene/10090:Trio ^@ http://purl.uniprot.org/uniprot/Q0KL02 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Abolishes Rac1 activation; when associated with A-1427.|||Abolishes Rac1 activation; when associated with E-1435.|||Basic and acidic residues|||CRAL-TRIO|||DH 1|||DH 2|||Disordered|||Ig-like C2-type|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||SH3 1|||SH3 2|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Triple functional domain protein ^@ http://purl.uniprot.org/annotation/PRO_0000278474|||http://purl.uniprot.org/annotation/VSP_023308|||http://purl.uniprot.org/annotation/VSP_023309|||http://purl.uniprot.org/annotation/VSP_037863|||http://purl.uniprot.org/annotation/VSP_037864|||http://purl.uniprot.org/annotation/VSP_037865 http://togogenome.org/gene/10090:Rpl29 ^@ http://purl.uniprot.org/uniprot/P47915|||http://purl.uniprot.org/uniprot/Q5M8M8 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ 1|||2|||2 X 8 AA tandem repeats of A-X-A-K-A-P-A-[KQ]|||Basic residues|||Disordered|||Large ribosomal subunit protein eL29|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000219136 http://togogenome.org/gene/10090:Nsmce4a ^@ http://purl.uniprot.org/uniprot/G3XA30 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Non-structural maintenance of chromosome element 4 C-terminal|||Nse4/EID protein Nse3/MAGE-binding ^@ http://togogenome.org/gene/10090:Tigit ^@ http://purl.uniprot.org/uniprot/A0A0B4J1G6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5002092569 http://togogenome.org/gene/10090:Pih1d2 ^@ http://purl.uniprot.org/uniprot/Q8CHR9 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||PIH1 domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000307335|||http://purl.uniprot.org/annotation/VSP_028718|||http://purl.uniprot.org/annotation/VSP_028719 http://togogenome.org/gene/10090:Vmn2r56 ^@ http://purl.uniprot.org/uniprot/E9Q4U5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://togogenome.org/gene/10090:Cpeb4 ^@ http://purl.uniprot.org/uniprot/Q3TSF0|||http://purl.uniprot.org/uniprot/Q5SU48|||http://purl.uniprot.org/uniprot/Q7TN98 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Site|||Splice Variant ^@ Basic residues|||Cytoplasmic polyadenylation element-binding protein 4|||Disordered|||Important for the positionning of RRM1 relative to RRM2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA-binding|||RRM|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000269265|||http://purl.uniprot.org/annotation/VSP_022043|||http://purl.uniprot.org/annotation/VSP_022044|||http://purl.uniprot.org/annotation/VSP_022045|||http://purl.uniprot.org/annotation/VSP_022046 http://togogenome.org/gene/10090:Twist2 ^@ http://purl.uniprot.org/uniprot/A5D6P6|||http://purl.uniprot.org/uniprot/Q9D030 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abrogates transcriptional repression of MYOD1.|||BHLH|||Disordered|||Twist-related protein 2|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127490 http://togogenome.org/gene/10090:Chrna7 ^@ http://purl.uniprot.org/uniprot/P49582|||http://purl.uniprot.org/uniprot/Q53YJ9|||http://purl.uniprot.org/uniprot/Q8CC01 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Associated with receptor activation|||Cytoplasmic|||Essential for TMEM35A/NACHO-mediated proper subunit assembly and trafficking to cell membrane|||Extracellular|||Helical|||Impairs TMEM35A/NACHO-mediated proper subunit assembly and trafficking to cell membrane.|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-7|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel ligand-binding domain-containing protein|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000368|||http://purl.uniprot.org/annotation/PRO_5010843962|||http://purl.uniprot.org/annotation/PRO_5010846972 http://togogenome.org/gene/10090:Incenp ^@ http://purl.uniprot.org/uniprot/Q9WU62 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||IN box|||In isoform 2.|||Inner centromere protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by AURKB|||Polar residues|||SAH ^@ http://purl.uniprot.org/annotation/PRO_0000084202|||http://purl.uniprot.org/annotation/VSP_007233 http://togogenome.org/gene/10090:Actn4 ^@ http://purl.uniprot.org/uniprot/P57780|||http://purl.uniprot.org/uniprot/Q3ULT2 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat ^@ Actin-binding|||Alpha-actinin-4|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||Interaction with VCL|||LXXLL motif|||Mediates interaction with MICALL2|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polyphosphoinositide (PIP2)-binding|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4 ^@ http://purl.uniprot.org/annotation/PRO_0000073441 http://togogenome.org/gene/10090:4930519G04Rik ^@ http://purl.uniprot.org/uniprot/Q9CPT7|||http://purl.uniprot.org/uniprot/Q9DAB8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Gfra1 ^@ http://purl.uniprot.org/uniprot/P97785 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 1|||2|||3|||GDNF family receptor alpha-1|||GPI-anchor amidated serine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000010779|||http://purl.uniprot.org/annotation/PRO_0000010780|||http://purl.uniprot.org/annotation/VSP_041630 http://togogenome.org/gene/10090:Tyw1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0L2|||http://purl.uniprot.org/uniprot/Q8BJM7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Flavodoxin-like|||Helical|||In isoform 2.|||Radical SAM core|||S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase TYW1 ^@ http://purl.uniprot.org/annotation/PRO_0000281828|||http://purl.uniprot.org/annotation/VSP_024068|||http://purl.uniprot.org/annotation/VSP_024070 http://togogenome.org/gene/10090:Pcdhb19 ^@ http://purl.uniprot.org/uniprot/Q3UH89|||http://purl.uniprot.org/uniprot/Q91Y01 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Cadherin domain-containing protein|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5004230130|||http://purl.uniprot.org/annotation/PRO_5015099503 http://togogenome.org/gene/10090:Smg9 ^@ http://purl.uniprot.org/uniprot/Q9DB90 ^@ 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.|||N-acetylserine|||Nonsense-mediated mRNA decay factor SMG9|||Phosphoserine|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000289164|||http://purl.uniprot.org/annotation/VSP_025947 http://togogenome.org/gene/10090:Snrnp48 ^@ http://purl.uniprot.org/uniprot/Q9D361 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Splice Variant|||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.|||In isoform 3.|||U11/U12 small nuclear ribonucleoprotein 48 kDa protein ^@ http://purl.uniprot.org/annotation/PRO_0000089545|||http://purl.uniprot.org/annotation/VSP_014642|||http://purl.uniprot.org/annotation/VSP_014643|||http://purl.uniprot.org/annotation/VSP_014644 http://togogenome.org/gene/10090:Plaat1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J130|||http://purl.uniprot.org/uniprot/Q9QZU4 ^@ 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_0000152482|||http://purl.uniprot.org/annotation/VSP_060191 http://togogenome.org/gene/10090:P4ha3 ^@ http://purl.uniprot.org/uniprot/H7BX23 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Fe2OG dioxygenase|||procollagen-proline 4-dioxygenase ^@ http://purl.uniprot.org/annotation/PRO_5003608416 http://togogenome.org/gene/10090:Lipe ^@ http://purl.uniprot.org/uniprot/P54310 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Hormone-sensitive lipase|||In isoform 2.|||Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000071548|||http://purl.uniprot.org/annotation/VSP_053335 http://togogenome.org/gene/10090:Tigar ^@ http://purl.uniprot.org/uniprot/B2RWB7|||http://purl.uniprot.org/uniprot/Q8BZA9 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Site ^@ Fructose-2,6-bisphosphatase TIGAR|||Proton donor/acceptor|||Tele-phosphohistidine intermediate|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000179958 http://togogenome.org/gene/10090:Or51a25 ^@ http://purl.uniprot.org/uniprot/Q8VH14 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Scgb1b7 ^@ http://purl.uniprot.org/uniprot/D2XZ31 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Signal Peptide ^@ Chain|||Non-terminal Residue|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015088473 http://togogenome.org/gene/10090:Spag17 ^@ http://purl.uniprot.org/uniprot/Q5S003 ^@ 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 pcdo.|||Polar residues|||Sperm-associated antigen 17 ^@ http://purl.uniprot.org/annotation/PRO_0000331446 http://togogenome.org/gene/10090:Atosa ^@ http://purl.uniprot.org/uniprot/Q69ZK7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant ^@ Atos homolog protein A|||Basic and acidic residues|||Disordered|||In isoform 2.|||Required for macropage invasion|||Transactivation domain 1 (TAD1)|||Transactivation domain 2 (TAD2) ^@ http://purl.uniprot.org/annotation/PRO_0000315614|||http://purl.uniprot.org/annotation/VSP_030582 http://togogenome.org/gene/10090:Tbc1d24 ^@ http://purl.uniprot.org/uniprot/Q3UUG6 ^@ 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 ^@ In isoform 2.|||Phosphoserine|||Rab-GAP TBC|||TBC1 domain family member 24|||TLDc ^@ http://purl.uniprot.org/annotation/PRO_0000288505|||http://purl.uniprot.org/annotation/VSP_025702 http://togogenome.org/gene/10090:Efhd1 ^@ http://purl.uniprot.org/uniprot/Q9D4J1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand|||Turn ^@ Disordered|||EF-hand 1|||EF-hand 2|||EF-hand domain-containing protein D1|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000073644 http://togogenome.org/gene/10090:Rab44 ^@ http://purl.uniprot.org/uniprot/A0A2Y9CZI3|||http://purl.uniprot.org/uniprot/Q8CB87 ^@ 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|||Ras-related protein Rab-44|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000333078 http://togogenome.org/gene/10090:Ugt1a6b ^@ http://purl.uniprot.org/uniprot/K9J7B2 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||UDP-glucuronosyltransferase ^@ http://purl.uniprot.org/annotation/PRO_5015019930 http://togogenome.org/gene/10090:Sugct ^@ http://purl.uniprot.org/uniprot/Q3TV98|||http://purl.uniprot.org/uniprot/Q7TNE1 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Chain|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||N6-acetyllysine|||Nucleophile|||Succinate--hydroxymethylglutarate CoA-transferase ^@ http://purl.uniprot.org/annotation/PRO_0000194727 http://togogenome.org/gene/10090:Defa26 ^@ http://purl.uniprot.org/uniprot/Q3L180 ^@ Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Compositionally Biased Region|||Disulfide Bond|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Alpha-defensin 26|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000300078|||http://purl.uniprot.org/annotation/PRO_0000300079 http://togogenome.org/gene/10090:Znrd2 ^@ http://purl.uniprot.org/uniprot/P56873|||http://purl.uniprot.org/uniprot/Q545N1|||http://purl.uniprot.org/uniprot/Q9D002 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Protein ZNRD2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000072202 http://togogenome.org/gene/10090:Larp6 ^@ http://purl.uniprot.org/uniprot/Q8BN59 ^@ 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|||HTH La-type RNA-binding|||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_0000281142 http://togogenome.org/gene/10090:Tmem97 ^@ http://purl.uniprot.org/uniprot/Q8VD00 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EXPERA|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Sigma intracellular receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000254569 http://togogenome.org/gene/10090:Ythdc2 ^@ http://purl.uniprot.org/uniprot/B2RR83 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat ^@ 3'-5' RNA helicase YTHDC2|||ANK 1|||ANK 2|||Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In ketu; homozygotes mice are both male- and female-sterile. In the testis, mutant germ cells carry out an abortive attempt at meiosis: They express hallmark meiotic proteins and initiate recombination, but fail to fully extinguish the spermatogonial mitotic division program, proceed prematurely to an aberrant metaphase-like state, and undergo apoptosis. The mutation probably causes misfolding or protein aggregation. Slightly reduced helicase activity.|||Phosphoserine|||Polar residues|||R3H|||YTH ^@ http://purl.uniprot.org/annotation/PRO_0000378275 http://togogenome.org/gene/10090:Nup93 ^@ http://purl.uniprot.org/uniprot/Q8BJ71 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Nuclear pore complex protein Nup93|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000124783|||http://purl.uniprot.org/annotation/VSP_010089 http://togogenome.org/gene/10090:Emc3 ^@ http://purl.uniprot.org/uniprot/Q99KI3 ^@ Chain|||Initiator Methionine|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||ER membrane protein complex subunit 3|||Helical|||Lumenal|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000211407 http://togogenome.org/gene/10090:Htatip2 ^@ http://purl.uniprot.org/uniprot/Q3U816|||http://purl.uniprot.org/uniprot/Q9Z2G9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand ^@ In isoform 2.|||N-acetylalanine|||Oxidoreductase HTATIP2|||Proton acceptor|||Removed|||Semialdehyde dehydrogenase NAD-binding ^@ http://purl.uniprot.org/annotation/PRO_0000072545|||http://purl.uniprot.org/annotation/PRO_5015097470|||http://purl.uniprot.org/annotation/VSP_051866|||http://purl.uniprot.org/annotation/VSP_051867 http://togogenome.org/gene/10090:Erg28 ^@ http://purl.uniprot.org/uniprot/Q9ERY9 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Ergosterol biosynthetic protein 28 homolog|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000193904 http://togogenome.org/gene/10090:Plcb3 ^@ http://purl.uniprot.org/uniprot/P51432|||http://purl.uniprot.org/uniprot/Q8CI86 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3|||C2|||Disordered|||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_0000088492 http://togogenome.org/gene/10090:Antxr2 ^@ http://purl.uniprot.org/uniprot/Q3TCL6|||http://purl.uniprot.org/uniprot/Q6DFX2 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Anthrax toxin receptor|||Anthrax toxin receptor 2|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000002695|||http://purl.uniprot.org/annotation/PRO_5014309140 http://togogenome.org/gene/10090:Cenpk ^@ http://purl.uniprot.org/uniprot/A0A0R4J037|||http://purl.uniprot.org/uniprot/Q9ESN5 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant ^@ Centromere protein K|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000249483|||http://purl.uniprot.org/annotation/VSP_020437|||http://purl.uniprot.org/annotation/VSP_020438|||http://purl.uniprot.org/annotation/VSP_020439 http://togogenome.org/gene/10090:Scgb1b12 ^@ http://purl.uniprot.org/uniprot/A0A087WP21 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015029572 http://togogenome.org/gene/10090:Or51ac3 ^@ http://purl.uniprot.org/uniprot/Q3KPB0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp236 ^@ http://purl.uniprot.org/uniprot/B2RR24|||http://purl.uniprot.org/uniprot/Q3UAV3 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or14j9 ^@ http://purl.uniprot.org/uniprot/Q8C0S2|||http://purl.uniprot.org/uniprot/Q8C1J3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lep ^@ http://purl.uniprot.org/uniprot/P41160|||http://purl.uniprot.org/uniprot/Q544U0 ^@ 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 ^@ In 30% the clones.|||Leptin ^@ http://purl.uniprot.org/annotation/PRO_0000017687|||http://purl.uniprot.org/annotation/PRO_5014309631 http://togogenome.org/gene/10090:Neil2 ^@ http://purl.uniprot.org/uniprot/Q1LZM6|||http://purl.uniprot.org/uniprot/Q6R2P8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Endonuclease 8-like 2|||FPG-type|||Formamidopyrimidine-DNA glycosylase catalytic|||N6-acetyllysine|||Phosphoserine|||Proton donor|||Proton donor; for beta-elimination activity|||Proton donor; for delta-elimination activity|||Removed|||Schiff-base intermediate with DNA ^@ http://purl.uniprot.org/annotation/PRO_0000170909 http://togogenome.org/gene/10090:Bhlhe41 ^@ http://purl.uniprot.org/uniprot/D3Z2G6|||http://purl.uniprot.org/uniprot/Q6L8F5|||http://purl.uniprot.org/uniprot/Q99PV5 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Region ^@ BHLH|||Class E basic helix-loop-helix protein 41|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Orange|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127148 http://togogenome.org/gene/10090:Ddx1 ^@ http://purl.uniprot.org/uniprot/Q91VR5 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region ^@ ATP-dependent RNA helicase DDX1|||B30.2/SPRY|||DEAD box|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||Interaction with dsRNA|||N6-acetyllysine|||N6-acetyllysine; alternate|||Necessary for interaction with HNRNPK|||Necessary for interaction with RELA|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000054987 http://togogenome.org/gene/10090:Cyba ^@ http://purl.uniprot.org/uniprot/B3VQI8|||http://purl.uniprot.org/uniprot/Q61462 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Crosslink|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Cytochrome b-245 light chain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000144908|||http://purl.uniprot.org/annotation/VSP_001248 http://togogenome.org/gene/10090:Astn2 ^@ http://purl.uniprot.org/uniprot/Q80Z10 ^@ 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 ^@ Astrotactin-2|||Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Fibronectin type-III|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000308253|||http://purl.uniprot.org/annotation/VSP_028938|||http://purl.uniprot.org/annotation/VSP_058454 http://togogenome.org/gene/10090:Aldh1a1 ^@ http://purl.uniprot.org/uniprot/P24549 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ Aldehyde dehydrogenase 1A1|||Mediates interaction with PRMT3|||N-acetylserine|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||Removed|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000056417 http://togogenome.org/gene/10090:Lrp2 ^@ http://purl.uniprot.org/uniprot/A2ARV4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6|||Endocytosis signal|||Extracellular|||Helical|||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 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 36|||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|||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_0000309845 http://togogenome.org/gene/10090:Tle1 ^@ http://purl.uniprot.org/uniprot/Q5SQA2|||http://purl.uniprot.org/uniprot/Q5SQA3|||http://purl.uniprot.org/uniprot/Q5SQA4|||http://purl.uniprot.org/uniprot/Q62440|||http://purl.uniprot.org/uniprot/Q6PFG2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||CcN domain|||Disordered|||GP domain|||Groucho/TLE N-terminal Q-rich|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 8.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by CK2|||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_0000051277|||http://purl.uniprot.org/annotation/VSP_006987|||http://purl.uniprot.org/annotation/VSP_006988|||http://purl.uniprot.org/annotation/VSP_006989|||http://purl.uniprot.org/annotation/VSP_006990|||http://purl.uniprot.org/annotation/VSP_006991|||http://purl.uniprot.org/annotation/VSP_006992|||http://purl.uniprot.org/annotation/VSP_006993|||http://purl.uniprot.org/annotation/VSP_006994|||http://purl.uniprot.org/annotation/VSP_006995 http://togogenome.org/gene/10090:Rhbdl2 ^@ http://purl.uniprot.org/uniprot/A2AGA4 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Transmembrane ^@ Abolishes protease activity.|||Basic and acidic residues|||Disordered|||Helical|||Nucleophile|||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_0000408511|||http://purl.uniprot.org/annotation/PRO_0000408512|||http://purl.uniprot.org/annotation/PRO_0000408513 http://togogenome.org/gene/10090:Myo1b ^@ http://purl.uniprot.org/uniprot/E9QNH6|||http://purl.uniprot.org/uniprot/P46735|||http://purl.uniprot.org/uniprot/Q3TTZ3|||http://purl.uniprot.org/uniprot/Q7TQD7 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||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|||In isoform 2.|||Myosin motor|||Phosphoserine|||TH1|||Unconventional myosin-Ib ^@ http://purl.uniprot.org/annotation/PRO_0000123443|||http://purl.uniprot.org/annotation/VSP_003347 http://togogenome.org/gene/10090:Col15a1 ^@ http://purl.uniprot.org/uniprot/O35206 ^@ 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 ^@ Collagen alpha-1(XV) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Disordered|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nonhelical region 1 (NC1)|||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)|||O-linked (Xyl...) (chondroitin sulfate) serine|||Polar residues|||Pro residues|||Restin|||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) ^@ http://purl.uniprot.org/annotation/PRO_0000005790|||http://purl.uniprot.org/annotation/PRO_0000005791 http://togogenome.org/gene/10090:Macrod2 ^@ http://purl.uniprot.org/uniprot/Q3UYG8|||http://purl.uniprot.org/uniprot/Q9D117 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region ^@ ADP-ribose glycohydrolase MACROD2|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Macro|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000300462 http://togogenome.org/gene/10090:Ube2f ^@ http://purl.uniprot.org/uniprot/Q9CY34 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl thioester intermediate|||Interaction with UBA3|||N-acetylmethionine|||NEDD8-conjugating enzyme UBE2F|||UBC core ^@ http://purl.uniprot.org/annotation/PRO_0000263078 http://togogenome.org/gene/10090:Sftpb ^@ http://purl.uniprot.org/uniprot/P50405|||http://purl.uniprot.org/uniprot/S4R2L6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Signal Peptide ^@ Interchain|||N-linked (GlcNAc...) asparagine|||Pulmonary surfactant-associated protein B|||Saposin A-type|||Saposin B-type|||Saposin B-type 1|||Saposin B-type 2|||Saposin B-type 3 ^@ http://purl.uniprot.org/annotation/PRO_0000031650|||http://purl.uniprot.org/annotation/PRO_0000031651|||http://purl.uniprot.org/annotation/PRO_0000031652|||http://purl.uniprot.org/annotation/PRO_5004522661 http://togogenome.org/gene/10090:Slc25a37 ^@ http://purl.uniprot.org/uniprot/Q920G8|||http://purl.uniprot.org/uniprot/Q9CQG7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||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 3.|||In isoform 4.|||In isoform 5.|||Mitoferrin-1|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000235252|||http://purl.uniprot.org/annotation/VSP_018405|||http://purl.uniprot.org/annotation/VSP_018406|||http://purl.uniprot.org/annotation/VSP_018407|||http://purl.uniprot.org/annotation/VSP_018408|||http://purl.uniprot.org/annotation/VSP_018409|||http://purl.uniprot.org/annotation/VSP_018410|||http://purl.uniprot.org/annotation/VSP_018411|||http://purl.uniprot.org/annotation/VSP_018412 http://togogenome.org/gene/10090:Hspb1 ^@ http://purl.uniprot.org/uniprot/P14602|||http://purl.uniprot.org/uniprot/Q545F4 ^@ 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 ^@ Heat shock protein beta-1|||In isoform B.|||In isoform C.|||Interaction with TGFB1I1|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by MAPKAPK2, MAPKAPK3, MAPKAPK5, PKA and PKC|||Phosphoserine; by MAPKAPK2, MAPKAPK3, PKA and PKC|||Phosphothreonine|||SHSP|||sHSP ^@ http://purl.uniprot.org/annotation/PRO_0000125928|||http://purl.uniprot.org/annotation/VSP_002422|||http://purl.uniprot.org/annotation/VSP_002423 http://togogenome.org/gene/10090:Bex4 ^@ http://purl.uniprot.org/uniprot/Q14BB8|||http://purl.uniprot.org/uniprot/Q9CWT2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Interaction with SIRT2|||Interaction with alpha-tubulin|||Protein BEX4 ^@ http://purl.uniprot.org/annotation/PRO_0000229784 http://togogenome.org/gene/10090:Gm11992 ^@ http://purl.uniprot.org/uniprot/B2RVL0|||http://purl.uniprot.org/uniprot/Q5SS90 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Uncharacterized protein C7orf57 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000310992 http://togogenome.org/gene/10090:Gpx3 ^@ http://purl.uniprot.org/uniprot/P46412 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Molecule Processing|||Non standard residue|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Non standard residue|||Sequence Conflict|||Signal Peptide ^@ Glutathione peroxidase 3|||Selenocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000013063 http://togogenome.org/gene/10090:Sh3bp5 ^@ http://purl.uniprot.org/uniprot/Q9Z131 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||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_0000064369|||http://purl.uniprot.org/annotation/VSP_010882|||http://purl.uniprot.org/annotation/VSP_022572 http://togogenome.org/gene/10090:Pag1 ^@ http://purl.uniprot.org/uniprot/A6H659|||http://purl.uniprot.org/uniprot/Q3U1F9 ^@ 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 ^@ Abolishes interaction with NHERF1 and effect on synapse formation.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Enhances TCR-mediated signaling.|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||Interaction with CSK|||Interaction with NHERF1|||Phosphoprotein associated with glycosphingolipid-enriched microdomains 1|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by FYN|||Phosphotyrosine; by LYN|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000083339 http://togogenome.org/gene/10090:Mybpc2 ^@ http://purl.uniprot.org/uniprot/Q5XKE0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000253051 http://togogenome.org/gene/10090:Defb46 ^@ http://purl.uniprot.org/uniprot/Q4QY34 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015097643 http://togogenome.org/gene/10090:Arhgap12 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ95|||http://purl.uniprot.org/uniprot/B2RUJ8|||http://purl.uniprot.org/uniprot/Q8C0D4|||http://purl.uniprot.org/uniprot/S4R203|||http://purl.uniprot.org/uniprot/S4R221 ^@ 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|||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_0000056715 http://togogenome.org/gene/10090:Spns2 ^@ http://purl.uniprot.org/uniprot/Q91VM4 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Sphingosine-1-phosphate transporter SPNS2 ^@ http://purl.uniprot.org/annotation/PRO_0000305044|||http://purl.uniprot.org/annotation/VSP_036390|||http://purl.uniprot.org/annotation/VSP_036391 http://togogenome.org/gene/10090:Ppp1r3e ^@ http://purl.uniprot.org/uniprot/H3BJB2 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ CBM21|||Disordered ^@ http://togogenome.org/gene/10090:Kif2b ^@ http://purl.uniprot.org/uniprot/A2RSC8|||http://purl.uniprot.org/uniprot/Q8C0N1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Kinesin motor|||Kinesin-like protein KIF2B|||Phosphoserine; by PLK1|||Phosphothreonine; by PLK1 ^@ http://purl.uniprot.org/annotation/PRO_0000253717 http://togogenome.org/gene/10090:Or6c205 ^@ http://purl.uniprot.org/uniprot/Q7TRI4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Esp24 ^@ http://purl.uniprot.org/uniprot/A8R0V6 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015086688 http://togogenome.org/gene/10090:Cadps2 ^@ http://purl.uniprot.org/uniprot/A4PI80|||http://purl.uniprot.org/uniprot/A4PI81|||http://purl.uniprot.org/uniprot/A4PI82|||http://purl.uniprot.org/uniprot/A4PI83|||http://purl.uniprot.org/uniprot/A4PI84|||http://purl.uniprot.org/uniprot/Q8BYR5 ^@ 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 ^@ Acidic residues|||C2|||Calcium-dependent secretion activator 2|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with DRD2|||MHD1|||PH|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000053869|||http://purl.uniprot.org/annotation/VSP_016819|||http://purl.uniprot.org/annotation/VSP_016820|||http://purl.uniprot.org/annotation/VSP_016821|||http://purl.uniprot.org/annotation/VSP_016822|||http://purl.uniprot.org/annotation/VSP_016823|||http://purl.uniprot.org/annotation/VSP_016824|||http://purl.uniprot.org/annotation/VSP_016825|||http://purl.uniprot.org/annotation/VSP_016826|||http://purl.uniprot.org/annotation/VSP_016827 http://togogenome.org/gene/10090:Pacrgl ^@ http://purl.uniprot.org/uniprot/Q9D3X5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||PACRG-like protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000278244 http://togogenome.org/gene/10090:Pdgfra ^@ http://purl.uniprot.org/uniprot/P26618 ^@ 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|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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|||Ig-like C2-type 5|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Platelet-derived growth factor receptor alpha|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000016761|||http://purl.uniprot.org/annotation/VSP_031877|||http://purl.uniprot.org/annotation/VSP_031878 http://togogenome.org/gene/10090:Ly6d ^@ http://purl.uniprot.org/uniprot/P35459 ^@ 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 serine|||Lymphocyte antigen 6D|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036136|||http://purl.uniprot.org/annotation/PRO_0000036137 http://togogenome.org/gene/10090:Nfkbil1 ^@ http://purl.uniprot.org/uniprot/O88995 ^@ 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|||Basic and acidic residues|||Disordered|||NF-kappa-B inhibitor-like protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000067011 http://togogenome.org/gene/10090:Emx1 ^@ http://purl.uniprot.org/uniprot/Q04742 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein EMX1 ^@ http://purl.uniprot.org/annotation/PRO_0000048867 http://togogenome.org/gene/10090:Myf5 ^@ http://purl.uniprot.org/uniprot/A2RSK4|||http://purl.uniprot.org/uniprot/P24699 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Disordered|||Myogenic factor 5|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127345 http://togogenome.org/gene/10090:Cpq ^@ http://purl.uniprot.org/uniprot/Q9WVJ3 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Carboxypeptidase Q|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000312260|||http://purl.uniprot.org/annotation/PRO_0000312261 http://togogenome.org/gene/10090:Rps6ka2 ^@ http://purl.uniprot.org/uniprot/Q7TPD5|||http://purl.uniprot.org/uniprot/Q9WUT3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ AGC-kinase C-terminal|||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_0000086202 http://togogenome.org/gene/10090:Vmn1r100 ^@ http://purl.uniprot.org/uniprot/Q9EPS5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clec1a ^@ http://purl.uniprot.org/uniprot/A0A0N4SV03|||http://purl.uniprot.org/uniprot/Q8BWY2|||http://purl.uniprot.org/uniprot/Q8BZ31 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 1 member A|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046610 http://togogenome.org/gene/10090:6430550D23Rik ^@ http://purl.uniprot.org/uniprot/A3KGJ9 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Sult3a1 ^@ http://purl.uniprot.org/uniprot/Q059N0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Mphosph6 ^@ http://purl.uniprot.org/uniprot/Q9D1Q1 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Crosslink|||Modified Residue|||Motif ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||M-phase phosphoprotein 6|||Nuclear localization signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000122438 http://togogenome.org/gene/10090:Ttyh3 ^@ http://purl.uniprot.org/uniprot/Q6P5F7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||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|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein tweety homolog 3 ^@ http://purl.uniprot.org/annotation/PRO_0000312252|||http://purl.uniprot.org/annotation/VSP_029771|||http://purl.uniprot.org/annotation/VSP_029772 http://togogenome.org/gene/10090:Adam10 ^@ http://purl.uniprot.org/uniprot/O35598|||http://purl.uniprot.org/uniprot/Q6NZC0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cleavage; by furin and PCSK7|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 10|||Disordered|||Extracellular|||Helical|||Interaction with AP2A1, AP2A2 and AP2M1|||Loss of binding to AP2A1 and AP2A2. Decreased localization to the plasma membrane.|||Loss of catalytic activity.|||N-linked (GlcNAc...) asparagine|||No loss of binding to AP2A1 and AP2A2.|||Peptidase M12B|||Phosphothreonine|||Pro residues|||SH3-binding|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029068|||http://purl.uniprot.org/annotation/PRO_0000029069|||http://purl.uniprot.org/annotation/PRO_5004277941 http://togogenome.org/gene/10090:Septin11 ^@ http://purl.uniprot.org/uniprot/A0A0J9YUL3|||http://purl.uniprot.org/uniprot/Q8C1B7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Septin-11|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173543|||http://purl.uniprot.org/annotation/VSP_011041|||http://purl.uniprot.org/annotation/VSP_011042 http://togogenome.org/gene/10090:Gm5169 ^@ http://purl.uniprot.org/uniprot/Q5M8P2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Prps1l1 ^@ http://purl.uniprot.org/uniprot/Q8C5R8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ribose-phosphate pyrophosphokinase N-terminal ^@ http://togogenome.org/gene/10090:Wdr62 ^@ http://purl.uniprot.org/uniprot/E9QK36 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Anaphase-promoting complex subunit 4-like WD40|||Disordered|||Polar residues|||WD ^@ http://togogenome.org/gene/10090:Dcdc2c ^@ http://purl.uniprot.org/uniprot/Q9D1B8 ^@ 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|||Doublecortin 1|||Doublecortin 2|||Doublecortin domain-containing protein 2C|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000344450|||http://purl.uniprot.org/annotation/VSP_040534 http://togogenome.org/gene/10090:Epb42 ^@ http://purl.uniprot.org/uniprot/P49222 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Band 3 binding|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||Protein 4.2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213721 http://togogenome.org/gene/10090:Sorbs3 ^@ http://purl.uniprot.org/uniprot/Q8K0M3|||http://purl.uniprot.org/uniprot/Q9R1Z8 ^@ 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|||Binds to SOS|||Binds to vinculin|||Disordered|||Phosphoserine|||Phosphoserine; by MAPK1|||Polar residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SoHo|||Vinexin ^@ http://purl.uniprot.org/annotation/PRO_0000065831 http://togogenome.org/gene/10090:Xrcc2 ^@ http://purl.uniprot.org/uniprot/Q9CX47 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Modified Residue|||Mutagenesis Site ^@ DNA repair protein XRCC2|||Mutant male mice exhibit meiotic arrest, azoospermia and infertility. Females exhibit infertility or low reproductive capacity.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000122949 http://togogenome.org/gene/10090:Map3k6 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ82 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Protein kinase ^@ http://togogenome.org/gene/10090:Dennd5b ^@ http://purl.uniprot.org/uniprot/A2RSQ0 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ DENN domain-containing protein 5B|||Helical|||N-acetylserine|||PLAT|||Phosphoserine|||Phosphothreonine|||RUN 1|||RUN 2|||Removed|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000326532 http://togogenome.org/gene/10090:Swsap1 ^@ http://purl.uniprot.org/uniprot/Q8VCI7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ ATPase SWSAP1|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000294241 http://togogenome.org/gene/10090:Polr3g ^@ http://purl.uniprot.org/uniprot/Q6NXY9 ^@ 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|||DNA-directed RNA polymerase III subunit RPC7|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000073979|||http://purl.uniprot.org/annotation/VSP_012672|||http://purl.uniprot.org/annotation/VSP_012673 http://togogenome.org/gene/10090:Or5h26 ^@ http://purl.uniprot.org/uniprot/E9PYP4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Usp36 ^@ http://purl.uniprot.org/uniprot/B1AQJ2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 36 ^@ http://purl.uniprot.org/annotation/PRO_0000378494 http://togogenome.org/gene/10090:Myh13 ^@ http://purl.uniprot.org/uniprot/B1AR69 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Actin-binding|||Disordered|||Myosin N-terminal SH3-like|||Myosin motor|||Polar residues ^@ http://togogenome.org/gene/10090:Epb41l3 ^@ http://purl.uniprot.org/uniprot/A0A3B2WD96|||http://purl.uniprot.org/uniprot/A7YY80|||http://purl.uniprot.org/uniprot/Q9WV92 ^@ 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 ^@ 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 5.|||In isoform 2, isoform 3, isoform 5, isoform 6 and isoform 7.|||In isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 7 and isoform 8.|||In isoform 7.|||In isoform 8.|||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_0000219400|||http://purl.uniprot.org/annotation/PRO_0000423195|||http://purl.uniprot.org/annotation/VSP_000487|||http://purl.uniprot.org/annotation/VSP_000488|||http://purl.uniprot.org/annotation/VSP_000489|||http://purl.uniprot.org/annotation/VSP_000490|||http://purl.uniprot.org/annotation/VSP_000491|||http://purl.uniprot.org/annotation/VSP_023063 http://togogenome.org/gene/10090:Mill1 ^@ http://purl.uniprot.org/uniprot/Q8HWE7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Disordered|||GPI-anchor amidated serine|||Ig-like C1-type|||MHC class I-like protein MILL1|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000452205|||http://purl.uniprot.org/annotation/PRO_5015099152 http://togogenome.org/gene/10090:Tmem19 ^@ http://purl.uniprot.org/uniprot/A0A1W2P7R5|||http://purl.uniprot.org/uniprot/Q91W52 ^@ 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_0000284795|||http://purl.uniprot.org/annotation/VSP_024661 http://togogenome.org/gene/10090:Btn2a2 ^@ http://purl.uniprot.org/uniprot/A4QPC6|||http://purl.uniprot.org/uniprot/B9EJ60 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ B30.2/SPRY|||Butyrophilin subfamily 2 member A2|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000367054|||http://purl.uniprot.org/annotation/PRO_5015087493|||http://purl.uniprot.org/annotation/VSP_036621|||http://purl.uniprot.org/annotation/VSP_036622 http://togogenome.org/gene/10090:Notch2 ^@ http://purl.uniprot.org/uniprot/O35516 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Cytoplasmic|||Decreased NICD processing.|||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|||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; incomplete|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Essential for O-xylosylation|||Extracellular|||Helical|||In isoform 2.|||LNR 1|||LNR 2|||LNR 3|||N-linked (GlcNAc...) asparagine|||Negative regulatory region (NRR)|||Neurogenic locus notch homolog protein 2|||No effect on NICD processing.|||No effect on O-glycosylation by POGLUT1. Loss of O-xylosylation.|||Notch 2 extracellular truncation|||Notch 2 intracellular domain|||O-linked (Glc...) serine; alternate|||O-linked (Xyl...) serine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000007686|||http://purl.uniprot.org/annotation/PRO_0000007687|||http://purl.uniprot.org/annotation/PRO_0000007688|||http://purl.uniprot.org/annotation/VSP_001405 http://togogenome.org/gene/10090:Rbmxl1 ^@ http://purl.uniprot.org/uniprot/Q91VM5 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Pro residues|||RNA binding motif protein, X-linked-like-1|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000408006 http://togogenome.org/gene/10090:Pck2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0G0|||http://purl.uniprot.org/uniprot/Q8BH04 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ 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_0000023569 http://togogenome.org/gene/10090:Angptl1 ^@ http://purl.uniprot.org/uniprot/Q640P2 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ Angiopoietin-related protein 1|||Fibrinogen C-terminal|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009119|||http://purl.uniprot.org/annotation/VSP_013722|||http://purl.uniprot.org/annotation/VSP_013723 http://togogenome.org/gene/10090:Vmn1r235 ^@ http://purl.uniprot.org/uniprot/Q8R297 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Galnt16 ^@ http://purl.uniprot.org/uniprot/Q9JJ61 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Polypeptide N-acetylgalactosaminyltransferase 16|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059136 http://togogenome.org/gene/10090:Sptlc2 ^@ http://purl.uniprot.org/uniprot/P97363|||http://purl.uniprot.org/uniprot/Q542D6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Transmembrane ^@ Aminotransferase class I/classII|||Helical|||N6-(pyridoxal phosphate)lysine|||Serine palmitoyltransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000163859 http://togogenome.org/gene/10090:Chek2 ^@ http://purl.uniprot.org/uniprot/Q543W6|||http://purl.uniprot.org/uniprot/Q9Z265 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||Does not inhibit cell survival upon DNA damage. Not phosphorylates p53/TP53.|||FHA|||Phosphoserine|||Phosphoserine; by PLK3|||Phosphoserine; by autocatalysis|||Phosphothreonine; by ATM and MAP3K20|||Phosphothreonine; by 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_0000085859 http://togogenome.org/gene/10090:Or2w3 ^@ http://purl.uniprot.org/uniprot/Q5NCC8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or2ag17 ^@ http://purl.uniprot.org/uniprot/Q7TRN3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kbtbd12 ^@ http://purl.uniprot.org/uniprot/Q9D618 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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_0000324767|||http://purl.uniprot.org/annotation/VSP_032356|||http://purl.uniprot.org/annotation/VSP_032357 http://togogenome.org/gene/10090:Stfa1 ^@ http://purl.uniprot.org/uniprot/P35175 ^@ Chain|||Molecule Processing|||Motif|||Region|||Site ^@ Chain|||Motif|||Site ^@ Reactive site|||Secondary area of contact|||Stefin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000207148 http://togogenome.org/gene/10090:Defb9 ^@ http://purl.uniprot.org/uniprot/Q32MD8|||http://purl.uniprot.org/uniprot/Q8R2I6 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 9 ^@ http://purl.uniprot.org/annotation/PRO_0000006937|||http://purl.uniprot.org/annotation/PRO_5014309020 http://togogenome.org/gene/10090:Usp28 ^@ http://purl.uniprot.org/uniprot/Q5I043 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||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.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||UIM|||USP|||Ubiquitin carboxyl-terminal hydrolase 28 ^@ http://purl.uniprot.org/annotation/PRO_0000080658|||http://purl.uniprot.org/annotation/VSP_015581 http://togogenome.org/gene/10090:2210418O10Rik ^@ http://purl.uniprot.org/uniprot/A2ARL4|||http://purl.uniprot.org/uniprot/D3YYR3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Skint5 ^@ http://purl.uniprot.org/uniprot/A7XUY5 ^@ 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 C1-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Selection and upkeep of intraepithelial T-cells protein 5 ^@ http://purl.uniprot.org/annotation/PRO_5000271637|||http://purl.uniprot.org/annotation/VSP_034883|||http://purl.uniprot.org/annotation/VSP_034884|||http://purl.uniprot.org/annotation/VSP_034885 http://togogenome.org/gene/10090:Aldoa ^@ http://purl.uniprot.org/uniprot/A6ZI44|||http://purl.uniprot.org/uniprot/P05064 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Disordered|||Fructose-bisphosphate aldolase|||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|||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|||Polar residues|||Proton acceptor|||Removed|||Schiff-base intermediate with dihydroxyacetone-P ^@ http://purl.uniprot.org/annotation/PRO_0000216937|||http://purl.uniprot.org/annotation/PRO_5015086548 http://togogenome.org/gene/10090:Dnaja2 ^@ http://purl.uniprot.org/uniprot/Q9QYJ0 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Repeat|||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_0000071012|||http://purl.uniprot.org/annotation/PRO_0000396758 http://togogenome.org/gene/10090:Fam205a4 ^@ http://purl.uniprot.org/uniprot/C0HKD1|||http://purl.uniprot.org/uniprot/C0HKD2|||http://purl.uniprot.org/uniprot/C0HKD3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Protein SPATA31F1-2|||Protein SPATA31F1-3|||Protein SPATA31F1-4 ^@ http://purl.uniprot.org/annotation/PRO_0000341305|||http://purl.uniprot.org/annotation/PRO_0000444751|||http://purl.uniprot.org/annotation/PRO_0000444752 http://togogenome.org/gene/10090:Gorab ^@ http://purl.uniprot.org/uniprot/Q8BRM2 ^@ 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.|||Necessary for interaction with RCHY1|||Polar residues|||RAB6-interacting golgin ^@ http://purl.uniprot.org/annotation/PRO_0000252445|||http://purl.uniprot.org/annotation/VSP_020979 http://togogenome.org/gene/10090:Rpl18a ^@ http://purl.uniprot.org/uniprot/P62717 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Crosslink|||Modified Residue ^@ 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_0000213926 http://togogenome.org/gene/10090:Zfp1 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLC5|||http://purl.uniprot.org/uniprot/P08042|||http://purl.uniprot.org/uniprot/Q3UI68 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Crosslink|||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; degenerate|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000047280|||http://purl.uniprot.org/annotation/VSP_012683 http://togogenome.org/gene/10090:Dlgap4 ^@ http://purl.uniprot.org/uniprot/B1AZP2|||http://purl.uniprot.org/uniprot/B7ZNS2|||http://purl.uniprot.org/uniprot/E9PUF2|||http://purl.uniprot.org/uniprot/Q3UCF7 ^@ 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|||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_0000345018|||http://purl.uniprot.org/annotation/VSP_034907|||http://purl.uniprot.org/annotation/VSP_034908|||http://purl.uniprot.org/annotation/VSP_034909 http://togogenome.org/gene/10090:Gnb5 ^@ http://purl.uniprot.org/uniprot/P62881|||http://purl.uniprot.org/uniprot/Q3UG14 ^@ Chain|||Coiled-Coil|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Helix|||Repeat|||Splice Variant|||Strand|||Turn ^@ Guanine nucleotide-binding protein subunit beta-5|||In isoform 2.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000127706|||http://purl.uniprot.org/annotation/VSP_008766 http://togogenome.org/gene/10090:Ano4 ^@ http://purl.uniprot.org/uniprot/Q8C5H1|||http://purl.uniprot.org/uniprot/S4R1L3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Anoctamin dimerisation|||Anoctamin-4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000353190|||http://purl.uniprot.org/annotation/VSP_052960|||http://purl.uniprot.org/annotation/VSP_052961|||http://purl.uniprot.org/annotation/VSP_052962|||http://purl.uniprot.org/annotation/VSP_052963 http://togogenome.org/gene/10090:Patl1 ^@ http://purl.uniprot.org/uniprot/Q3TC46 ^@ 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 ^@ Acidic residues|||Asymmetric dimethylarginine|||Disordered|||Involved in RNA-binding|||Involved in nuclear foci localization|||Involved in nuclear speckle localization|||Nuclear export signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||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_0000320964 http://togogenome.org/gene/10090:Rnf4 ^@ http://purl.uniprot.org/uniprot/Q9QZS2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ Abolishes homodimerization. Loss of E3 ubiquitin ligase activity.|||Abolishes homodimerization. Strongly reduced E3 ubiquitin ligase activity.|||Disordered|||E3 ubiquitin-protein ligase RNF4|||Mediates interaction with TRPS1|||No effect.|||Phosphoserine|||Polar residues|||RING-type|||Required for ubiquitination activity|||SUMO interaction motif 1; mediates the binding to polysumoylated substrates|||SUMO interaction motif 2; mediates the binding to polysumoylated substrates|||SUMO interaction motif 3; mediates the binding to polysumoylated substrates|||SUMO interaction motif 4; mediates the binding to polysumoylated substrates ^@ http://purl.uniprot.org/annotation/PRO_0000056044 http://togogenome.org/gene/10090:Gadd45gip1 ^@ http://purl.uniprot.org/uniprot/Q9CR59 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Large ribosomal subunit protein mL64|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000228621 http://togogenome.org/gene/10090:Spam1 ^@ http://purl.uniprot.org/uniprot/P48794|||http://purl.uniprot.org/uniprot/Q5D1J0 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Hyaluronidase PH-20|||N-linked (GlcNAc...) asparagine|||Proton donor|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000012093|||http://purl.uniprot.org/annotation/PRO_0000012094 http://togogenome.org/gene/10090:Il20 ^@ http://purl.uniprot.org/uniprot/Q2NKI0|||http://purl.uniprot.org/uniprot/Q2THG5|||http://purl.uniprot.org/uniprot/Q9JKV9 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Interleukin-20 ^@ http://purl.uniprot.org/annotation/PRO_0000015382 http://togogenome.org/gene/10090:Tmx1 ^@ http://purl.uniprot.org/uniprot/Q8VBT0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Polar residues|||Redox-active|||Thioredoxin|||Thioredoxin-related transmembrane protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000034154 http://togogenome.org/gene/10090:Prl8a8 ^@ http://purl.uniprot.org/uniprot/A0A0M6L0I6|||http://purl.uniprot.org/uniprot/Q9DAS4 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prolactin-8A8 ^@ http://purl.uniprot.org/annotation/PRO_0000045332|||http://purl.uniprot.org/annotation/PRO_5005806234|||http://purl.uniprot.org/annotation/VSP_016781 http://togogenome.org/gene/10090:Qrfpr ^@ http://purl.uniprot.org/uniprot/P83861|||http://purl.uniprot.org/uniprot/Q4VA00 ^@ 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|||Pyroglutamylated RF-amide peptide receptor ^@ http://purl.uniprot.org/annotation/PRO_0000070098 http://togogenome.org/gene/10090:Or8g19 ^@ http://purl.uniprot.org/uniprot/Q9EQ90 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r124 ^@ http://purl.uniprot.org/uniprot/K7N789 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908834 http://togogenome.org/gene/10090:Col9a3 ^@ http://purl.uniprot.org/uniprot/A2ACT7|||http://purl.uniprot.org/uniprot/Q8BSX1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Collagen alpha-3(IX) chain|||Disordered|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5004304241|||http://purl.uniprot.org/annotation/PRO_5015086012 http://togogenome.org/gene/10090:Unc5cl ^@ http://purl.uniprot.org/uniprot/E9QLC2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Death|||ZU5 ^@ http://togogenome.org/gene/10090:Slain1 ^@ http://purl.uniprot.org/uniprot/Q68FF7 ^@ 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 ^@ Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||SLAIN motif-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000316963|||http://purl.uniprot.org/annotation/VSP_030833 http://togogenome.org/gene/10090:Fam184a ^@ http://purl.uniprot.org/uniprot/E9PW83 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disordered|||Protein FAM184A/B N-terminal ^@ http://togogenome.org/gene/10090:Mras ^@ http://purl.uniprot.org/uniprot/O08989 ^@ Binding Site|||Chain|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Site|||Strand ^@ Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Strand ^@ Cysteine methyl ester|||Effector region|||Ras-related protein M-Ras|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000082655|||http://purl.uniprot.org/annotation/PRO_0000281305 http://togogenome.org/gene/10090:Mcur1 ^@ http://purl.uniprot.org/uniprot/Q9CXD6 ^@ 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 ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Mitochondrial calcium uniporter regulator 1|||Mitochondrial intermembrane|||Mitochondrial matrix|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000295693|||http://purl.uniprot.org/annotation/VSP_027000|||http://purl.uniprot.org/annotation/VSP_027001|||http://purl.uniprot.org/annotation/VSP_027002 http://togogenome.org/gene/10090:Fmn2 ^@ http://purl.uniprot.org/uniprot/Q9JL04 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ 1|||10|||11|||12|||12 X 11 AA tandem repeats of [MV]-G-I-P-P-P-P-P-L-P-G|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||FH1|||FH2|||Formin-2|||Important for interaction with SPIRE1|||Phosphoserine|||Polar residues|||Pro residues|||Strongly reduced interaction with SPIRE1. ^@ http://purl.uniprot.org/annotation/PRO_0000194889 http://togogenome.org/gene/10090:Ccdc127 ^@ http://purl.uniprot.org/uniprot/Q3TC33 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant ^@ Coiled-coil domain-containing protein 127|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000263751|||http://purl.uniprot.org/annotation/VSP_021885|||http://purl.uniprot.org/annotation/VSP_021886 http://togogenome.org/gene/10090:Prl2c2 ^@ http://purl.uniprot.org/uniprot/A0A0M6L0W4|||http://purl.uniprot.org/uniprot/P04095 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prolactin-2C2 ^@ http://purl.uniprot.org/annotation/PRO_0000032967|||http://purl.uniprot.org/annotation/PRO_5005806172|||http://purl.uniprot.org/annotation/VSP_043544 http://togogenome.org/gene/10090:Cand2 ^@ http://purl.uniprot.org/uniprot/Q6ZQ73 ^@ 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 ^@ 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|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089298 http://togogenome.org/gene/10090:Gpatch11 ^@ http://purl.uniprot.org/uniprot/A0A0R4J215|||http://purl.uniprot.org/uniprot/Q3UFS4 ^@ 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|||G patch domain-containing protein 11|||G-patch|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000279753 http://togogenome.org/gene/10090:4933405O20Rik ^@ http://purl.uniprot.org/uniprot/Q8BPC6 ^@ Binding Site|||Chain|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Transit Peptide ^@ Mitochondrion|||Probable isocitrate dehydrogenase [NAD] gamma 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000401933 http://togogenome.org/gene/10090:Dmbx1 ^@ http://purl.uniprot.org/uniprot/Q91ZK4 ^@ 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 ^@ Basic and acidic residues|||Diencephalon/mesencephalon homeobox protein 1|||Disordered|||Homeobox|||In isoform 2.|||Interaction with OTX2 and is required for repressor activity|||OAR ^@ http://purl.uniprot.org/annotation/PRO_0000262955|||http://purl.uniprot.org/annotation/VSP_052252 http://togogenome.org/gene/10090:Zfp810 ^@ http://purl.uniprot.org/uniprot/Q99K45 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Gm1110 ^@ http://purl.uniprot.org/uniprot/F6Y113 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Beta-galactosidase|||Glycoside hydrolase 35 catalytic ^@ http://purl.uniprot.org/annotation/PRO_5009690933 http://togogenome.org/gene/10090:Recql4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0J3|||http://purl.uniprot.org/uniprot/Q75NR7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ATP-dependent DNA helicase Q4|||CCHC-type|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000205054|||http://purl.uniprot.org/annotation/VSP_015177 http://togogenome.org/gene/10090:Ndufb11 ^@ http://purl.uniprot.org/uniprot/O09111 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Transit Peptide|||Transmembrane|||Turn ^@ Chain|||Helix|||Region|||Transit Peptide|||Transmembrane|||Turn ^@ Disordered|||Helical|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000020058 http://togogenome.org/gene/10090:Arhgap11a ^@ http://purl.uniprot.org/uniprot/Q80Y19 ^@ 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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho GTPase-activating protein 11A|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000267214 http://togogenome.org/gene/10090:Vmn1r82 ^@ http://purl.uniprot.org/uniprot/Q8R283 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp937 ^@ http://purl.uniprot.org/uniprot/A2ANU7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Asmt ^@ http://purl.uniprot.org/uniprot/A0A0R4J285|||http://purl.uniprot.org/uniprot/D3KU66 ^@ 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 ^@ Acetylserotonin O-methyltransferase|||Acetylserotonin O-methyltransferase dimerisation|||Disordered|||In strain: C57BL/6J, 129/Sv, BALB/c, FVB/N and more; reduces protein expression.|||O-methyltransferase|||Polar residues|||Proton acceptor|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000414794 http://togogenome.org/gene/10090:Taf6l ^@ http://purl.uniprot.org/uniprot/H3BJR2|||http://purl.uniprot.org/uniprot/H3BK01|||http://purl.uniprot.org/uniprot/Q8R2K4 ^@ 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.|||Phosphoserine|||Polar residues|||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_0000118880|||http://purl.uniprot.org/annotation/VSP_010158 http://togogenome.org/gene/10090:Gapt ^@ http://purl.uniprot.org/uniprot/Q8CB93 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Protein GAPT ^@ http://purl.uniprot.org/annotation/PRO_0000271124 http://togogenome.org/gene/10090:Slc34a2 ^@ http://purl.uniprot.org/uniprot/Q9DBP0 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||Sodium-dependent phosphate transport protein 2B ^@ http://purl.uniprot.org/annotation/PRO_0000068614 http://togogenome.org/gene/10090:Chst15 ^@ http://purl.uniprot.org/uniprot/Q91XQ5 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 15|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000225624 http://togogenome.org/gene/10090:Aprt ^@ http://purl.uniprot.org/uniprot/P08030 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Adenine phosphoribosyltransferase|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000149506 http://togogenome.org/gene/10090:Acaa1a ^@ http://purl.uniprot.org/uniprot/Q921H8 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Chain|||Modified Residue|||Region|||Transit Peptide ^@ 3-ketoacyl-CoA thiolase A, peroxisomal|||Acyl-thioester intermediate|||N6-acetyllysine|||PTS2-type peroxisomal targeting signal|||Peroxisome|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000034068 http://togogenome.org/gene/10090:Kcnip3 ^@ http://purl.uniprot.org/uniprot/A2AHT3|||http://purl.uniprot.org/uniprot/Q3YAA9|||http://purl.uniprot.org/uniprot/Q3YAB0|||http://purl.uniprot.org/uniprot/Q9QXT8 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Strand ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand ^@ Abolishes calcium-binding.|||Calsenilin|||Disordered|||EF-hand|||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 isoform 2.|||In isoform 3.|||In strain: 129/Ola, BALB/c and FVB/NJ.|||Interaction with KCND2|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000073815|||http://purl.uniprot.org/annotation/PRO_5015097543|||http://purl.uniprot.org/annotation/VSP_015041|||http://purl.uniprot.org/annotation/VSP_015042 http://togogenome.org/gene/10090:Gm6176 ^@ http://purl.uniprot.org/uniprot/J3QK59 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Fip1l1 ^@ http://purl.uniprot.org/uniprot/Q9D824 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant ^@ Arg/Asp/Glu-rich domain|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 4.|||Necessary for stimulating PAPOLA activity|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pre-mRNA 3'-end-processing factor FIP1|||Pro residues|||Sufficient for interaction with AHCYL1|||Sufficient for interaction with CPSF1 and CSTF3|||Sufficient for interaction with CPSF4|||Sufficient for interaction with PAPOLA ^@ http://purl.uniprot.org/annotation/PRO_0000215038|||http://purl.uniprot.org/annotation/VSP_016733|||http://purl.uniprot.org/annotation/VSP_016734|||http://purl.uniprot.org/annotation/VSP_016735|||http://purl.uniprot.org/annotation/VSP_016736 http://togogenome.org/gene/10090:Ccdc152 ^@ http://purl.uniprot.org/uniprot/E9PX14 ^@ Coiled-Coil|||Region ^@ Coiled-Coil ^@ ^@ http://togogenome.org/gene/10090:Traf3 ^@ http://purl.uniprot.org/uniprot/Q3UHJ1|||http://purl.uniprot.org/uniprot/Q60803 ^@ 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 ^@ Abolished ubiquitination by the SCF(FBXL2) complex.|||Abolishes inhibition of NFKB2 processing; when associated with A-52.|||Abolishes inhibition of NFKB2 processing; when associated with A-55.|||Decreased interaction with FBXL2.|||Disordered|||Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Loss of interaction with MAVS.|||MATH|||RING-type|||Reduces 'Lys-48'-linked polyubiquitination; when associated with R-106.|||Reduces 'Lys-48'-linked polyubiquitination; when associated with R-155.|||Strongly reduces 'Lys-63'-linked ubiquitination; when associated with A-69. Abolishes inhibition of NFKB2 processing; when associated with A-67.|||Strongly reduces 'Lys-63'-linked ubiquitination; when associated with A-69. Abolishes inhibition of NFKB2 processing; when associated with A-69.|||TNF receptor-associated factor 3|||TRAF-type|||TRAF-type 1|||TRAF-type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000056402 http://togogenome.org/gene/10090:Osbpl3 ^@ http://purl.uniprot.org/uniprot/D3YTT6|||http://purl.uniprot.org/uniprot/D3Z194|||http://purl.uniprot.org/uniprot/F8WH20|||http://purl.uniprot.org/uniprot/Q9DBS9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||FFAT 1|||FFAT 2|||Oxysterol-binding protein-related protein 3|||PH|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000100372 http://togogenome.org/gene/10090:Klf8 ^@ http://purl.uniprot.org/uniprot/Q8BLM0 ^@ Chain|||Crosslink|||Modification|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Crosslink|||Motif|||Region|||Zinc Finger ^@ 9aaTAD; inactive|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Krueppel-like factor 8 ^@ http://purl.uniprot.org/annotation/PRO_0000294168 http://togogenome.org/gene/10090:Krt79 ^@ http://purl.uniprot.org/uniprot/Q8VED5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Chain|||Domain Extent|||Region|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type II cytoskeletal 79|||Linker 1|||Linker 12|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000314894 http://togogenome.org/gene/10090:Maff ^@ http://purl.uniprot.org/uniprot/A0A1S6GWH7|||http://purl.uniprot.org/uniprot/O54791|||http://purl.uniprot.org/uniprot/Q3U0G5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ BZIP|||Basic motif|||Disordered|||Leucine-zipper|||Polar residues|||Transcription factor MafF|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076498 http://togogenome.org/gene/10090:Rraga ^@ http://purl.uniprot.org/uniprot/Q80X95 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Site ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Mutagenesis Site ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Maintains GTP-bound state, leading to activate mTORC1. Knockin mice develop normally, but die within 1 day postpartum because of constitutive activation of mTORC1 that prevents response to fasting. Inhibition of mTORC1 is required for neonatal autophagy and thus nutrient homeostasis.|||Phosphoserine|||Ras-related GTP-binding protein A ^@ http://purl.uniprot.org/annotation/PRO_0000239946 http://togogenome.org/gene/10090:Gm21190 ^@ http://purl.uniprot.org/uniprot/A0A0G2JGJ6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Sapcd2 ^@ http://purl.uniprot.org/uniprot/Q9D818 ^@ 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.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Suppressor APC domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000286597|||http://purl.uniprot.org/annotation/VSP_025112|||http://purl.uniprot.org/annotation/VSP_025113 http://togogenome.org/gene/10090:Dlx2 ^@ http://purl.uniprot.org/uniprot/P40764|||http://purl.uniprot.org/uniprot/Q52KJ2 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Homeobox|||Homeobox protein DLX-2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049024 http://togogenome.org/gene/10090:Ap3m2 ^@ http://purl.uniprot.org/uniprot/Q8R2R9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ AP-3 complex subunit mu-2|||MHD ^@ http://purl.uniprot.org/annotation/PRO_0000193785 http://togogenome.org/gene/10090:Slco5a1 ^@ http://purl.uniprot.org/uniprot/E9PVD9|||http://purl.uniprot.org/uniprot/Q8BY69 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Kazal-like|||Major facilitator superfamily (MFS) profile|||Polar residues ^@ http://togogenome.org/gene/10090:Gm21761 ^@ http://purl.uniprot.org/uniprot/J3QK00 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tnnc2 ^@ http://purl.uniprot.org/uniprot/P20801 ^@ 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|||EF-hand 4|||N-acetylthreonine|||Removed|||Troponin C, skeletal muscle ^@ http://purl.uniprot.org/annotation/PRO_0000073704 http://togogenome.org/gene/10090:Ctsh ^@ http://purl.uniprot.org/uniprot/P49935 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cathepsin H|||Cathepsin H heavy chain|||Cathepsin H light chain|||Cathepsin H mini chain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000026212|||http://purl.uniprot.org/annotation/PRO_0000026213|||http://purl.uniprot.org/annotation/PRO_0000026214|||http://purl.uniprot.org/annotation/PRO_0000026215|||http://purl.uniprot.org/annotation/PRO_0000026216|||http://purl.uniprot.org/annotation/PRO_0000026217 http://togogenome.org/gene/10090:Slc6a7 ^@ http://purl.uniprot.org/uniprot/Q6PGE7 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||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_0000214771 http://togogenome.org/gene/10090:Trim14 ^@ http://purl.uniprot.org/uniprot/Q14AR3|||http://purl.uniprot.org/uniprot/Q3V0E0|||http://purl.uniprot.org/uniprot/Q8BVW3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ B box-type|||B30.2/SPRY|||In isoform 2.|||In isoform 3.|||Loss of inhibition of SPI1-mediated transcriptional activation.|||Tripartite motif-containing protein 14 ^@ http://purl.uniprot.org/annotation/PRO_0000220371|||http://purl.uniprot.org/annotation/VSP_012053|||http://purl.uniprot.org/annotation/VSP_012054|||http://purl.uniprot.org/annotation/VSP_012055|||http://purl.uniprot.org/annotation/VSP_012056 http://togogenome.org/gene/10090:Herc6 ^@ http://purl.uniprot.org/uniprot/F2Z461 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||E3 ISG15--protein ligase Herc6|||Glycyl thioester intermediate|||HECT|||Polar residues|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5 ^@ http://purl.uniprot.org/annotation/PRO_0000418833 http://togogenome.org/gene/10090:C1qtnf9 ^@ http://purl.uniprot.org/uniprot/Q4ZJN1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant ^@ 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 9|||Disordered|||In isoform 2.|||No change in the interaction with ADIPOQ.|||O-linked (Gal...) hydroxylysine ^@ http://purl.uniprot.org/annotation/PRO_0000291752|||http://purl.uniprot.org/annotation/VSP_026218 http://togogenome.org/gene/10090:H2-Q7 ^@ http://purl.uniprot.org/uniprot/E9PWT4|||http://purl.uniprot.org/uniprot/L7N260|||http://purl.uniprot.org/uniprot/P14429 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Extracellular|||H-2 class I histocompatibility antigen, Q7 alpha chain|||Helical|||Ig-like|||Ig-like C1-type|||MHC class I-like antigen recognition-like|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000018933|||http://purl.uniprot.org/annotation/PRO_5003243004|||http://purl.uniprot.org/annotation/PRO_5003982391 http://togogenome.org/gene/10090:Dyrk3 ^@ http://purl.uniprot.org/uniprot/Q922Y0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Disordered|||Dual specificity tyrosine-phosphorylation-regulated kinase 3|||Loss of kinase activity.|||Minimal loss of kinase activity.|||Minimal loss of kinase activity; when associated with E-366.|||Minimal loss of kinase activity; when associated with E-368.|||Nuclear localization signal|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000291537 http://togogenome.org/gene/10090:Pde4c ^@ http://purl.uniprot.org/uniprot/Q3UEI1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||PDEase|||Phosphoserine|||Proton donor|||cAMP-specific 3',5'-cyclic phosphodiesterase 4C ^@ http://purl.uniprot.org/annotation/PRO_0000198812|||http://purl.uniprot.org/annotation/VSP_016663 http://togogenome.org/gene/10090:Or13p3 ^@ http://purl.uniprot.org/uniprot/Q7TQV4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp607b ^@ http://purl.uniprot.org/uniprot/G3X9H3|||http://purl.uniprot.org/uniprot/Q3URA4|||http://purl.uniprot.org/uniprot/Q6P9L8 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ift56 ^@ http://purl.uniprot.org/uniprot/Q8BS45 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ Disordered|||Intraflagellar transport protein 56|||TPR 1|||TPR 2|||TPR 3|||TPR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000289084 http://togogenome.org/gene/10090:Dexi ^@ http://purl.uniprot.org/uniprot/Q9WUQ7 ^@ Chain|||Molecule Processing ^@ Chain ^@ Dexamethasone-induced protein ^@ http://purl.uniprot.org/annotation/PRO_0000096670 http://togogenome.org/gene/10090:Bcan ^@ http://purl.uniprot.org/uniprot/Q3TSQ8|||http://purl.uniprot.org/uniprot/Q61361 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Brevican core protein|||C-type lectin|||Disordered|||EGF-like|||Ig-like V-type|||Link 1|||Link 2|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Polar residues|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_0000017512 http://togogenome.org/gene/10090:Hoxb13 ^@ http://purl.uniprot.org/uniprot/P70321 ^@ Chain|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Region ^@ Homeobox|||Homeobox protein Hox-B13|||Interaction with 5-mCpG DNA|||Interaction with DNA ^@ http://purl.uniprot.org/annotation/PRO_0000200161 http://togogenome.org/gene/10090:Col28a1 ^@ http://purl.uniprot.org/uniprot/Q2UY11 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||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|||Disordered|||In isoform 2.|||VWFA 1|||VWFA 2 ^@ http://purl.uniprot.org/annotation/PRO_5000074665|||http://purl.uniprot.org/annotation/VSP_031095|||http://purl.uniprot.org/annotation/VSP_031096 http://togogenome.org/gene/10090:Pcna ^@ http://purl.uniprot.org/uniprot/P17918|||http://purl.uniprot.org/uniprot/Q542J9 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ 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|||N6-acetyllysine|||Phosphotyrosine; by EGFR|||Proliferating cell nuclear antigen|||Proliferating cell nuclear antigen PCNA C-terminal|||Proliferating cell nuclear antigen PCNA N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000149160 http://togogenome.org/gene/10090:Cdh23 ^@ http://purl.uniprot.org/uniprot/K4DI74|||http://purl.uniprot.org/uniprot/Q99PF4 ^@ Chain|||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|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||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|||Extracellular|||Helical|||In isoform 2, isoform B2 and isoform C2.|||In isoform B2 and isoform B1.|||In isoform C1 and isoform C2.|||In isoform C1.|||In strain: CAST/Ei.|||In waltzer.|||N-linked (GlcNAc...) asparagine|||Strongly reduced affinity for PCDH15.|||Strongly reduced interaction with PCDH15. ^@ http://purl.uniprot.org/annotation/PRO_0000003825|||http://purl.uniprot.org/annotation/PRO_5003875023|||http://purl.uniprot.org/annotation/VSP_000648|||http://purl.uniprot.org/annotation/VSP_059242|||http://purl.uniprot.org/annotation/VSP_059243|||http://purl.uniprot.org/annotation/VSP_059244 http://togogenome.org/gene/10090:Atp6v0a2 ^@ http://purl.uniprot.org/uniprot/P15920 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform 2.|||Phosphoserine|||V-type proton ATPase 116 kDa subunit a 2|||Vacuolar ^@ http://purl.uniprot.org/annotation/PRO_0000119217|||http://purl.uniprot.org/annotation/VSP_032088 http://togogenome.org/gene/10090:Trim12c ^@ http://purl.uniprot.org/uniprot/D3Z3L3 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ B box-type|||B30.2/SPRY|||RING-type ^@ http://togogenome.org/gene/10090:Tnfsf13 ^@ http://purl.uniprot.org/uniprot/Q5F2A4|||http://purl.uniprot.org/uniprot/Q9D777 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn ^@ Cleavage; by furin|||Helical|||N-linked (GlcNAc...) asparagine|||TNF family profile|||Tumor necrosis factor ligand superfamily member 13 ^@ http://purl.uniprot.org/annotation/PRO_0000034526|||http://purl.uniprot.org/annotation/PRO_0000034527 http://togogenome.org/gene/10090:Reg4 ^@ http://purl.uniprot.org/uniprot/Q9D8G5 ^@ 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 ^@ C-type lectin|||N-linked (GlcNAc...) asparagine|||Regenerating islet-derived protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000017438 http://togogenome.org/gene/10090:G0s2 ^@ http://purl.uniprot.org/uniprot/Q545U0|||http://purl.uniprot.org/uniprot/Q61585 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ G0/G1 switch protein 2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000087406 http://togogenome.org/gene/10090:Lsm6 ^@ http://purl.uniprot.org/uniprot/P62313|||http://purl.uniprot.org/uniprot/Q542U7 ^@ 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_0000125576 http://togogenome.org/gene/10090:Cdh15 ^@ http://purl.uniprot.org/uniprot/P33146 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-15|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000003807|||http://purl.uniprot.org/annotation/PRO_0000003808 http://togogenome.org/gene/10090:Tm2d2 ^@ http://purl.uniprot.org/uniprot/Q8R0I4 ^@ 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|||TM2 domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000298983 http://togogenome.org/gene/10090:Zfp747 ^@ http://purl.uniprot.org/uniprot/Q8BHM7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Gpr45 ^@ http://purl.uniprot.org/uniprot/Q148B5|||http://purl.uniprot.org/uniprot/Q8C6N9|||http://purl.uniprot.org/uniprot/Q8CA29|||http://purl.uniprot.org/uniprot/Q9EQQ4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||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|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Probable G-protein coupled receptor 45 ^@ http://purl.uniprot.org/annotation/PRO_0000069575 http://togogenome.org/gene/10090:Slco6d1 ^@ http://purl.uniprot.org/uniprot/Q14DL2|||http://purl.uniprot.org/uniprot/Q9D5W6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Kazal-like ^@ http://togogenome.org/gene/10090:Alkbh5 ^@ http://purl.uniprot.org/uniprot/Q3TSG4 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||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|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RNA demethylase ALKBH5|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000239284 http://togogenome.org/gene/10090:Tmem170 ^@ http://purl.uniprot.org/uniprot/Q9D342 ^@ 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 170A ^@ http://purl.uniprot.org/annotation/PRO_0000291760 http://togogenome.org/gene/10090:Gpc4 ^@ http://purl.uniprot.org/uniprot/P51655 ^@ Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ GPI-anchor amidated serine|||Glypican-4|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Phosphoserine|||Removed in mature form|||Secreted glypican-4 ^@ http://purl.uniprot.org/annotation/PRO_0000012317|||http://purl.uniprot.org/annotation/PRO_0000012318|||http://purl.uniprot.org/annotation/PRO_0000333848 http://togogenome.org/gene/10090:Zfpm1 ^@ http://purl.uniprot.org/uniprot/O35615 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn|||Zinc Finger ^@ Able to partially restore the interaction with the G-205 GATA1 mutant, which is usually unable to interact with ZFPM1.|||Abolishes interaction with CTBP2.|||Abolishes interaction with CTBP2; it however does not abolish the corepressor activity in erythropoiesis.|||Abolishes interaction with GATA1.|||Abolishes interaction with TACC3.|||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|||Does not affect the interaction with GATA1.|||Impairs interaction with GATA1.|||Impairs interaction with GATA1. Strongly impairs interaction with GATA1; when associated with A-277; A-612 and/or A-985.|||Impairs interaction with GATA1. Strongly impairs interaction with GATA1; when associated with A-277; A-718 and/or A-985.|||Impairs interaction with GATA1. Strongly impairs interaction with GATA1; when associated with A-612; A-718 and/or A-985.|||Impairs interaction with TACC3.|||Interaction with CTBP2|||Interaction with TACC3|||No effect on interaction with TACC3.|||Phosphoserine|||Polar residues|||Pro residues|||Slightly affects the interaction with GATA1.|||Slightly affects the interaction with GATA1. Strongly impairs interaction with GATA1; when associated with A-277; A-612 and/or A-718.|||Transforms the C2HC-type zinc finger into a C2H2-type, leading to abolition of interaction with GATA1.|||Zinc finger protein ZFPM1 ^@ http://purl.uniprot.org/annotation/PRO_0000221042 http://togogenome.org/gene/10090:Mccc1 ^@ http://purl.uniprot.org/uniprot/Q99MR8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ ATP-grasp|||Biotin carboxylation|||Biotinyl-binding|||Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-biotinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000002834 http://togogenome.org/gene/10090:Or4f14d ^@ http://purl.uniprot.org/uniprot/Q8VG12 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Drap1 ^@ http://purl.uniprot.org/uniprot/D3YY09|||http://purl.uniprot.org/uniprot/Q4FJW2|||http://purl.uniprot.org/uniprot/Q9D6N5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Dr1-associated corepressor|||Histone-fold|||Pro residues|||Transcription factor CBF/NF-Y/archaeal histone ^@ http://purl.uniprot.org/annotation/PRO_0000080002 http://togogenome.org/gene/10090:Eci2 ^@ http://purl.uniprot.org/uniprot/Q9WUR2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ ACB|||Disordered|||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_0000214028|||http://purl.uniprot.org/annotation/VSP_037855 http://togogenome.org/gene/10090:Dbx2 ^@ http://purl.uniprot.org/uniprot/F8VQH7|||http://purl.uniprot.org/uniprot/Q8BZD0 ^@ DNA Binding|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ DNA Binding|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Mrrf ^@ http://purl.uniprot.org/uniprot/Q9D6S7 ^@ Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Strand|||Transit Peptide|||Turn ^@ Mitochondrion|||Ribosome-recycling factor, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000031081 http://togogenome.org/gene/10090:Or7g12 ^@ http://purl.uniprot.org/uniprot/Q7TRG8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp687 ^@ http://purl.uniprot.org/uniprot/Q9D2D7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||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 isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger protein 687 ^@ http://purl.uniprot.org/annotation/PRO_0000234006|||http://purl.uniprot.org/annotation/VSP_018170|||http://purl.uniprot.org/annotation/VSP_018171|||http://purl.uniprot.org/annotation/VSP_018172|||http://purl.uniprot.org/annotation/VSP_018173 http://togogenome.org/gene/10090:Hsd17b4 ^@ http://purl.uniprot.org/uniprot/P51660 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ (3R)-hydroxyacyl-CoA dehydrogenase|||Enoyl-CoA hydratase 2|||MaoC-like|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Peroxisomal multifunctional enzyme type 2|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||SCP2 ^@ http://purl.uniprot.org/annotation/PRO_0000054584|||http://purl.uniprot.org/annotation/PRO_0000400084|||http://purl.uniprot.org/annotation/PRO_0000400085 http://togogenome.org/gene/10090:H2bc3 ^@ http://purl.uniprot.org/uniprot/Q64475 ^@ 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-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-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_0000244830 http://togogenome.org/gene/10090:Prdm1 ^@ http://purl.uniprot.org/uniprot/Q60636 ^@ 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 ^@ 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); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with PIAS1|||PR domain zinc finger protein 1|||Polar residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000047758|||http://purl.uniprot.org/annotation/VSP_039189|||http://purl.uniprot.org/annotation/VSP_041570|||http://purl.uniprot.org/annotation/VSP_041571|||http://purl.uniprot.org/annotation/VSP_041572 http://togogenome.org/gene/10090:Igflr1 ^@ http://purl.uniprot.org/uniprot/Q3U4N7 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||IGF-like family receptor 1|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000290358|||http://purl.uniprot.org/annotation/VSP_026146 http://togogenome.org/gene/10090:Vwa5a ^@ http://purl.uniprot.org/uniprot/Q99KC8 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Phosphotyrosine|||VIT|||VWFA|||von Willebrand factor A domain-containing protein 5A ^@ http://purl.uniprot.org/annotation/PRO_0000084412 http://togogenome.org/gene/10090:Castor1 ^@ http://purl.uniprot.org/uniprot/Q9CWQ8 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ ACT 1|||ACT 2|||Cytosolic arginine sensor for mTORC1 subunit 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000348591 http://togogenome.org/gene/10090:Kcnh3 ^@ http://purl.uniprot.org/uniprot/Q9WVJ0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||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|||Pro residues|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054006 http://togogenome.org/gene/10090:Vmn1r65 ^@ http://purl.uniprot.org/uniprot/Q9EPS7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Prmt8 ^@ http://purl.uniprot.org/uniprot/Q6PAK3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region ^@ Asymmetric dimethylarginine; by PRMT8|||Disordered|||N-myristoyl glycine|||Omega-N-methylarginine; by PRMT8|||Protein arginine N-methyltransferase 8|||Removed|||SAM-dependent MTase PRMT-type|||SH3-binding 1|||SH3-binding 2 ^@ http://purl.uniprot.org/annotation/PRO_0000212330 http://togogenome.org/gene/10090:Carm1 ^@ http://purl.uniprot.org/uniprot/Q9WVG6 ^@ 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|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Abolishes dimerization.|||Abolishes dimethylation. Impairs transcription coactivator activity and regulation of alternative splicing. No effect on methyltransferase activity.|||Abolishes histone methyltransferase activity and coactivator activity.|||Abolishes histone methyltransferase activity and reduces coactivator activity.|||Dimethylated arginine|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Histone-arginine methyltransferase CARM1|||In isoform 2.|||Interaction with C9orf72|||Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity.|||Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity. Localized in the cytosol.|||Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity. Localized in the nucleus.|||Loss of protein methyltransferase activity.|||Phosphoserine|||Reduces protein methyltransferase activity.|||Required for nuclear translocation|||SAM-dependent MTase PRMT-type|||Transactivation domain ^@ http://purl.uniprot.org/annotation/PRO_0000212339|||http://purl.uniprot.org/annotation/VSP_012508 http://togogenome.org/gene/10090:Pign ^@ http://purl.uniprot.org/uniprot/A0A087WQ32|||http://purl.uniprot.org/uniprot/G3X9F1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ GPI ethanolamine phosphate transferase 1 C-terminal|||Helical ^@ http://togogenome.org/gene/10090:Setd5 ^@ http://purl.uniprot.org/uniprot/Q5XJV7 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Histone-lysine N-methyltransferase SETD5|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000281906|||http://purl.uniprot.org/annotation/VSP_024096|||http://purl.uniprot.org/annotation/VSP_024097 http://togogenome.org/gene/10090:Ndufs8 ^@ http://purl.uniprot.org/uniprot/Q3UY05|||http://purl.uniprot.org/uniprot/Q5M9P5|||http://purl.uniprot.org/uniprot/Q8K3J1 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Strand|||Transit Peptide|||Turn ^@ 4Fe-4S ferredoxin-type|||4Fe-4S ferredoxin-type 1|||4Fe-4S ferredoxin-type 2|||Mitochondrion|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000020014 http://togogenome.org/gene/10090:Hipk4 ^@ http://purl.uniprot.org/uniprot/Q3V016 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Homeodomain-interacting protein kinase 4|||In isoform 2.|||Loss of activity.|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000277604|||http://purl.uniprot.org/annotation/VSP_023035 http://togogenome.org/gene/10090:Fam98b ^@ http://purl.uniprot.org/uniprot/Q80VD1 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Protein FAM98B ^@ http://purl.uniprot.org/annotation/PRO_0000187189 http://togogenome.org/gene/10090:Tomm6 ^@ http://purl.uniprot.org/uniprot/Q9CQN3 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Mitochondrial import receptor subunit TOM6 homolog|||N-acetylalanine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000302857 http://togogenome.org/gene/10090:Mbnl1 ^@ http://purl.uniprot.org/uniprot/A0A0A6YWB0|||http://purl.uniprot.org/uniprot/G3X9Q0|||http://purl.uniprot.org/uniprot/Q3U570|||http://purl.uniprot.org/uniprot/Q3U581|||http://purl.uniprot.org/uniprot/Q4VA08|||http://purl.uniprot.org/uniprot/Q9JKP5 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Zinc Finger ^@ C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||Muscleblind-like protein 1|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000089179 http://togogenome.org/gene/10090:Rtn2 ^@ http://purl.uniprot.org/uniprot/O70622|||http://purl.uniprot.org/uniprot/Q3TUZ6|||http://purl.uniprot.org/uniprot/Q6IM74|||http://purl.uniprot.org/uniprot/Q6IM75 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues|||Reticulon|||Reticulon-2 ^@ http://purl.uniprot.org/annotation/PRO_0000168162|||http://purl.uniprot.org/annotation/VSP_005650|||http://purl.uniprot.org/annotation/VSP_005651 http://togogenome.org/gene/10090:Lyrm2 ^@ http://purl.uniprot.org/uniprot/Q8R033 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ LYR motif-containing protein 2|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000251176 http://togogenome.org/gene/10090:Otud1 ^@ http://purl.uniprot.org/uniprot/Q9CUB6 ^@ 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 1|||UIM|||Variable-loop ^@ http://purl.uniprot.org/annotation/PRO_0000271019 http://togogenome.org/gene/10090:Vmn1r207 ^@ http://purl.uniprot.org/uniprot/A0A494BA14 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cfh ^@ http://purl.uniprot.org/uniprot/E9Q8I0|||http://purl.uniprot.org/uniprot/P06909 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand ^@ Basic and acidic residues|||Complement factor H|||Disordered|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||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_0000005895|||http://purl.uniprot.org/annotation/PRO_5003243130 http://togogenome.org/gene/10090:Slc35b3 ^@ http://purl.uniprot.org/uniprot/F8WGD7|||http://purl.uniprot.org/uniprot/Q922Q5 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Transmembrane ^@ Adenosine 3'-phospho 5'-phosphosulfate transporter 2|||Basic and acidic residues|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000213380 http://togogenome.org/gene/10090:Aadacl2fm3 ^@ http://purl.uniprot.org/uniprot/J3QPI0 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Signal Peptide ^@ Alpha/beta hydrolase fold-3 ^@ http://purl.uniprot.org/annotation/PRO_5038497724 http://togogenome.org/gene/10090:Fxyd5 ^@ http://purl.uniprot.org/uniprot/F8WJA1|||http://purl.uniprot.org/uniprot/P97808|||http://purl.uniprot.org/uniprot/Q3TDW1 ^@ 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|||FXYD domain-containing ion transport regulator|||FXYD domain-containing ion transport regulator 5|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000388996|||http://purl.uniprot.org/annotation/PRO_5011326941|||http://purl.uniprot.org/annotation/PRO_5011332401 http://togogenome.org/gene/10090:Gsn ^@ http://purl.uniprot.org/uniprot/P13020|||http://purl.uniprot.org/uniprot/Q6PAC1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Actin-actin interfilament contact point|||Actin-binding, Ca-sensitive|||Actin-severing|||Basic and acidic residues|||Disordered|||Gelsolin|||Gelsolin-like|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||Gelsolin-like 6|||In isoform 1|||In isoform 2.|||N-acetylmethionine; alternate|||N6-acetyllysine|||Phosphothreonine|||Phosphotyrosine|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000036387|||http://purl.uniprot.org/annotation/VSP_018960 http://togogenome.org/gene/10090:Slc3a2 ^@ http://purl.uniprot.org/uniprot/P10852 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Amino acid transporter heavy chain SLC3A2|||Basic and acidic residues|||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|||In isoform 2.|||Interchain (with C-164 in SLC7A5; C-158 in SLC7A11 and C-153 in SLC7A8)|||Loss of interchain disulfide bond. No effect on guidance of SLC7A5 to the plasma membrane.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000064384|||http://purl.uniprot.org/annotation/VSP_054953 http://togogenome.org/gene/10090:Sfrp5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J001|||http://purl.uniprot.org/uniprot/Q9WU66 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ FZ|||NTR|||Secreted frizzled-related protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000032556|||http://purl.uniprot.org/annotation/PRO_5015044276 http://togogenome.org/gene/10090:Phf6 ^@ http://purl.uniprot.org/uniprot/Q9D4J7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Splice Variant|||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 isoform 2.|||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_0000059294|||http://purl.uniprot.org/annotation/VSP_009375 http://togogenome.org/gene/10090:Prnd ^@ http://purl.uniprot.org/uniprot/Q544A3|||http://purl.uniprot.org/uniprot/Q9QUG3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Cu(2+) binding|||Flexible tail|||GPI-anchor amidated glycine|||Globular|||N-linked (GlcNAc...) asparagine|||Prion-like protein doppel|||Prion/Doppel protein beta-ribbon|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000025747|||http://purl.uniprot.org/annotation/PRO_0000025748|||http://purl.uniprot.org/annotation/PRO_5014309570 http://togogenome.org/gene/10090:Or2y1d ^@ http://purl.uniprot.org/uniprot/Q8VGX0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mmp11 ^@ http://purl.uniprot.org/uniprot/Q02853|||http://purl.uniprot.org/uniprot/Q3UQT3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Propeptide|||Repeat|||Signal Peptide|||Strand ^@ Activation peptide|||Cysteine switch|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Peptidase metallopeptidase|||Peptidase metallopeptidase domain-containing protein|||Stromelysin-3|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028772|||http://purl.uniprot.org/annotation/PRO_0000028773|||http://purl.uniprot.org/annotation/PRO_5010843486 http://togogenome.org/gene/10090:Smgc ^@ http://purl.uniprot.org/uniprot/Q6JHY2 ^@ 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|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Submandibular gland protein C ^@ http://purl.uniprot.org/annotation/PRO_5000092417|||http://purl.uniprot.org/annotation/VSP_034523|||http://purl.uniprot.org/annotation/VSP_034524|||http://purl.uniprot.org/annotation/VSP_034525|||http://purl.uniprot.org/annotation/VSP_034526 http://togogenome.org/gene/10090:Or8g2b ^@ http://purl.uniprot.org/uniprot/Q9EQ96 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zscan4c ^@ http://purl.uniprot.org/uniprot/Q80VJ6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||SCAN box|||Zinc finger and SCAN domain containing protein 4C ^@ http://purl.uniprot.org/annotation/PRO_0000394244 http://togogenome.org/gene/10090:Duoxa1 ^@ http://purl.uniprot.org/uniprot/Q8VE49 ^@ Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dual oxidase maturation factor 1|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000264242 http://togogenome.org/gene/10090:Syn1 ^@ http://purl.uniprot.org/uniprot/O88935 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ A|||Asymmetric dimethylarginine|||B; linker|||C; actin-binding and synaptic-vesicle binding|||D; Pro-rich linker|||Disordered|||E|||In isoform 3.|||In isoform Ib.|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) serine; alternate|||O-linked (GlcNAc) threonine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by CaMK2|||Phosphoserine; by PDPK1|||Phosphotyrosine|||Polar residues|||Pro residues|||Synapsin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000183019|||http://purl.uniprot.org/annotation/VSP_015205|||http://purl.uniprot.org/annotation/VSP_015206|||http://purl.uniprot.org/annotation/VSP_015207 http://togogenome.org/gene/10090:Ptger4 ^@ http://purl.uniprot.org/uniprot/P32240|||http://purl.uniprot.org/uniprot/Q91VE4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Prostaglandin E2 receptor EP4 subtype ^@ http://purl.uniprot.org/annotation/PRO_0000070065 http://togogenome.org/gene/10090:Mxd3 ^@ http://purl.uniprot.org/uniprot/Q80US8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Interaction with SIN3A and SIN3B|||Max dimerization protein 3|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000253708 http://togogenome.org/gene/10090:Rnf152 ^@ http://purl.uniprot.org/uniprot/Q8BG47 ^@ Chain|||Molecule Processing|||Region|||Transmembrane|||Zinc Finger ^@ Chain|||Region|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNF152|||Helical|||Necessary for interaction with RRAGA|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056112 http://togogenome.org/gene/10090:Psph ^@ http://purl.uniprot.org/uniprot/Q99LS3 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ N-acetylmethionine|||Nucleophile|||Phosphoserine phosphatase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000156880 http://togogenome.org/gene/10090:Zc3h14 ^@ http://purl.uniprot.org/uniprot/Q8BJ05 ^@ 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 ^@ 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 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||N-acetylmethionine|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||Zinc finger CCCH domain-containing protein 14 ^@ http://purl.uniprot.org/annotation/PRO_0000331313|||http://purl.uniprot.org/annotation/VSP_033177|||http://purl.uniprot.org/annotation/VSP_033178|||http://purl.uniprot.org/annotation/VSP_033179|||http://purl.uniprot.org/annotation/VSP_033180 http://togogenome.org/gene/10090:Cntnap5b ^@ http://purl.uniprot.org/uniprot/Q0V8T8 ^@ 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 ^@ Contactin-associated protein like 5-2|||Cytoplasmic|||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_0000317379|||http://purl.uniprot.org/annotation/VSP_030943 http://togogenome.org/gene/10090:Fbxw27 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLI0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Reg3a ^@ http://purl.uniprot.org/uniprot/O09037|||http://purl.uniprot.org/uniprot/Q794C6 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Region|||Signal Peptide ^@ C-type lectin|||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_0000017430|||http://purl.uniprot.org/annotation/PRO_0000422743|||http://purl.uniprot.org/annotation/PRO_0000422744|||http://purl.uniprot.org/annotation/PRO_5014310822 http://togogenome.org/gene/10090:Cd22 ^@ http://purl.uniprot.org/uniprot/P35329 ^@ 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 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 Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes binding to GRB2.|||B-cell receptor CD22|||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|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In strain: BXSB and MRL/MpJ.|||In strain: BXSB.|||In strain: DBA/2J and BXSB.|||In strain: DBA/2J and NZW/LacJ.|||In strain: DBA/2J, BXSB and NZW/LacJ.|||In strain: DBA/2J.|||In strain: DBA/2J; BXSB and MRL/MpJ.|||In strain: MRL/MpJ.|||In strain: NZW/LacJ.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014874|||http://purl.uniprot.org/annotation/VSP_002532|||http://purl.uniprot.org/annotation/VSP_002533 http://togogenome.org/gene/10090:Nr2c2ap ^@ http://purl.uniprot.org/uniprot/Q3TV70 ^@ Chain|||Molecule Processing ^@ Chain ^@ Nuclear receptor 2C2-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000295586 http://togogenome.org/gene/10090:Snx25 ^@ http://purl.uniprot.org/uniprot/Q3ZT31 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||PX|||PXA|||Phosphoserine|||RGS|||Sorting nexin-25 ^@ http://purl.uniprot.org/annotation/PRO_0000352799 http://togogenome.org/gene/10090:Or6a2 ^@ http://purl.uniprot.org/uniprot/Q80WD6|||http://purl.uniprot.org/uniprot/Q9QWU6 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Domain Extent|||Non-terminal Residue|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cd74 ^@ http://purl.uniprot.org/uniprot/P04441|||http://purl.uniprot.org/uniprot/Q3U4Q8|||http://purl.uniprot.org/uniprot/Q545Y5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Class-II-associated invariant chain peptide|||Cytoplasmic|||Disordered|||Extracellular|||H-2 class II histocompatibility antigen gamma chain|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform Short.|||MHC class II-associated invariant chain trimerisation|||MHC class II-associated invariant chain/CLIP MHC II-interacting|||N-linked (GlcNAc...) asparagine|||No addition of glycosaminoglycan; no effect on the synthesis of the protein.|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000067955|||http://purl.uniprot.org/annotation/PRO_0000448887|||http://purl.uniprot.org/annotation/VSP_005332 http://togogenome.org/gene/10090:Chst13 ^@ http://purl.uniprot.org/uniprot/D3Z6E3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Carbohydrate sulfotransferase ^@ http://purl.uniprot.org/annotation/PRO_5003053264 http://togogenome.org/gene/10090:Acd ^@ http://purl.uniprot.org/uniprot/B2RS36|||http://purl.uniprot.org/uniprot/Q5EE38 ^@ 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 ^@ Adrenocortical dysplasia protein|||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 POT1|||PWI|||Phosphoserine|||Polar residues|||Shelterin complex subunit TPP1/Est3 ^@ http://purl.uniprot.org/annotation/PRO_0000239020|||http://purl.uniprot.org/annotation/VSP_019067|||http://purl.uniprot.org/annotation/VSP_019068|||http://purl.uniprot.org/annotation/VSP_019069|||http://purl.uniprot.org/annotation/VSP_019070|||http://purl.uniprot.org/annotation/VSP_019071|||http://purl.uniprot.org/annotation/VSP_019072|||http://purl.uniprot.org/annotation/VSP_019073|||http://purl.uniprot.org/annotation/VSP_019074|||http://purl.uniprot.org/annotation/VSP_019075 http://togogenome.org/gene/10090:Pcmt1 ^@ http://purl.uniprot.org/uniprot/E0CYV0|||http://purl.uniprot.org/uniprot/E9PWE0|||http://purl.uniprot.org/uniprot/P23506 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||N-acetylalanine|||Polar residues|||Protein-L-isoaspartate(D-aspartate) O-methyltransferase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000111876|||http://purl.uniprot.org/annotation/VSP_004717 http://togogenome.org/gene/10090:Zxdb ^@ http://purl.uniprot.org/uniprot/A2CE44 ^@ 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 ^@ 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|||Omega-N-methylarginine|||Pro residues|||Required for interaction with ZXDC|||Required for transcriptional activation|||Zinc finger X-linked protein ZXDB ^@ http://purl.uniprot.org/annotation/PRO_0000292802 http://togogenome.org/gene/10090:Tecpr1 ^@ http://purl.uniprot.org/uniprot/Q80VP0 ^@ 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|||Disordered|||In isoform 2.|||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_0000337061|||http://purl.uniprot.org/annotation/VSP_033862 http://togogenome.org/gene/10090:Gm428 ^@ http://purl.uniprot.org/uniprot/Q3UTE2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Or11h7 ^@ http://purl.uniprot.org/uniprot/E9Q840 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vsnl1 ^@ http://purl.uniprot.org/uniprot/P62761|||http://purl.uniprot.org/uniprot/Q4W4C9 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding ^@ EF-hand|||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_0000073764 http://togogenome.org/gene/10090:Csad ^@ http://purl.uniprot.org/uniprot/Q9DBE0 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ Cysteine sulfinic acid decarboxylase|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_0000147007 http://togogenome.org/gene/10090:Casq1 ^@ http://purl.uniprot.org/uniprot/O09165|||http://purl.uniprot.org/uniprot/Q6P3C3|||http://purl.uniprot.org/uniprot/Q8C7M8 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide ^@ Calsequestrin|||Calsequestrin-1|||Disordered|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000412170|||http://purl.uniprot.org/annotation/PRO_5004277714 http://togogenome.org/gene/10090:Adgrf5 ^@ http://purl.uniprot.org/uniprot/G5E8Q8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Adhesion G protein-coupled receptor F5|||Cleavage|||Cleavage; by furin|||Cytoplasmic|||Disordered|||Extracellular|||GPS|||Helical|||Ig-like 1|||Ig-like 2|||Ig-like 3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||SEA ^@ http://purl.uniprot.org/annotation/PRO_0000433564 http://togogenome.org/gene/10090:Art3 ^@ http://purl.uniprot.org/uniprot/E9QNU1|||http://purl.uniprot.org/uniprot/Q8R2G4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Ecto-ADP-ribosyltransferase 3|||GPI-anchor amidated serine|||In isoform 5.|||In isoform 7.|||NAD(P)(+)--arginine ADP-ribosyltransferase|||Removed in mature form|||TR mART core ^@ http://purl.uniprot.org/annotation/PRO_0000019327|||http://purl.uniprot.org/annotation/PRO_0000019328|||http://purl.uniprot.org/annotation/PRO_5005128622|||http://purl.uniprot.org/annotation/VSP_036193|||http://purl.uniprot.org/annotation/VSP_036199 http://togogenome.org/gene/10090:Klhl12 ^@ http://purl.uniprot.org/uniprot/Q8BZM0 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Repeat|||Splice Variant ^@ BACK|||BTB|||In isoform 2.|||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_0000234350|||http://purl.uniprot.org/annotation/VSP_018280 http://togogenome.org/gene/10090:Rbm4 ^@ http://purl.uniprot.org/uniprot/B7ZN14|||http://purl.uniprot.org/uniprot/Q5CZX8|||http://purl.uniprot.org/uniprot/Q8C7Q4 ^@ 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 ^@ CCHC-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with TNPO3|||Phosphoserine|||RNA-binding protein 4|||RRM|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081755|||http://purl.uniprot.org/annotation/VSP_013417|||http://purl.uniprot.org/annotation/VSP_013418 http://togogenome.org/gene/10090:Vmn1r11 ^@ http://purl.uniprot.org/uniprot/Q3SXA2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Higd1b ^@ http://purl.uniprot.org/uniprot/Q99JY6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||HIG1|||HIG1 domain family member 1B|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000215775 http://togogenome.org/gene/10090:Ccne1 ^@ http://purl.uniprot.org/uniprot/Q61457 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||G1/S-specific cyclin-E1|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000080450 http://togogenome.org/gene/10090:Vmn1r22 ^@ http://purl.uniprot.org/uniprot/Q8R2D1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Srsf9 ^@ http://purl.uniprot.org/uniprot/Q9D0B0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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_0000081936 http://togogenome.org/gene/10090:Nxph4 ^@ http://purl.uniprot.org/uniprot/G3X9N5|||http://purl.uniprot.org/uniprot/Q8BTD1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Neurexophilin ^@ http://purl.uniprot.org/annotation/PRO_5004304245|||http://purl.uniprot.org/annotation/PRO_5015091832 http://togogenome.org/gene/10090:Chadl ^@ http://purl.uniprot.org/uniprot/E9Q7T7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide ^@ Chondroadherin-like protein|||Disordered|||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_0000432866 http://togogenome.org/gene/10090:Tsr2 ^@ http://purl.uniprot.org/uniprot/H7BWY8|||http://purl.uniprot.org/uniprot/Q8C8T8|||http://purl.uniprot.org/uniprot/Z4YL87 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pre-rRNA-processing protein TSR2 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000285588 http://togogenome.org/gene/10090:Sec24a ^@ http://purl.uniprot.org/uniprot/A2AA71|||http://purl.uniprot.org/uniprot/Q3U2P1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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_0000205154|||http://purl.uniprot.org/annotation/VSP_016990|||http://purl.uniprot.org/annotation/VSP_016991 http://togogenome.org/gene/10090:Ddx47 ^@ http://purl.uniprot.org/uniprot/Q4VBG1|||http://purl.uniprot.org/uniprot/Q9CWX9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Probable ATP-dependent RNA helicase DDX47|||Q motif|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000055051 http://togogenome.org/gene/10090:Tdrd6 ^@ http://purl.uniprot.org/uniprot/B7ZNI0|||http://purl.uniprot.org/uniprot/E9PZ50|||http://purl.uniprot.org/uniprot/F2Z429|||http://purl.uniprot.org/uniprot/P61407 ^@ 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|||Phosphothreonine|||Tudor|||Tudor 1|||Tudor 2|||Tudor 3|||Tudor 4|||Tudor 5|||Tudor 6|||Tudor domain-containing protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000183168 http://togogenome.org/gene/10090:H2-DMb1 ^@ http://purl.uniprot.org/uniprot/Q31094 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097375 http://togogenome.org/gene/10090:Gm44501 ^@ http://purl.uniprot.org/uniprot/A8R0T9 ^@ 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_5015086676 http://togogenome.org/gene/10090:Daam1 ^@ http://purl.uniprot.org/uniprot/Q8BPM0|||http://purl.uniprot.org/uniprot/Q8BTF1 ^@ 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 ^@ Actin-binding|||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_0000194908|||http://purl.uniprot.org/annotation/VSP_027771|||http://purl.uniprot.org/annotation/VSP_027772|||http://purl.uniprot.org/annotation/VSP_027773 http://togogenome.org/gene/10090:Fut1 ^@ http://purl.uniprot.org/uniprot/O09160|||http://purl.uniprot.org/uniprot/Q32MG3 ^@ 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|||Galactoside alpha-(1,2)-fucosyltransferase 1|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000149098 http://togogenome.org/gene/10090:Ptprk ^@ http://purl.uniprot.org/uniprot/P35822 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Helical|||Ig-like C2-type|||MAM|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Receptor-type tyrosine-protein phosphatase kappa|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000025447 http://togogenome.org/gene/10090:Mst1r ^@ http://purl.uniprot.org/uniprot/Q62190 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||Macrophage-stimulating protein receptor|||Macrophage-stimulating protein receptor alpha chain|||Macrophage-stimulating protein receptor beta chain|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Sema ^@ http://purl.uniprot.org/annotation/PRO_0000024455|||http://purl.uniprot.org/annotation/PRO_0000024456|||http://purl.uniprot.org/annotation/PRO_0000024457 http://togogenome.org/gene/10090:Rho ^@ http://purl.uniprot.org/uniprot/P15409 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ 'Ionic lock' involved in activated form stabilization|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Interaction with SAG|||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_0000197687 http://togogenome.org/gene/10090:Zdhhc8 ^@ http://purl.uniprot.org/uniprot/Q2TGE7|||http://purl.uniprot.org/uniprot/Q5Y5T5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||DHHC|||Disordered|||Helical|||Lumenal|||Omega-N-methylarginine|||Palmitoyltransferase DHHC|||Palmitoyltransferase ZDHHC8|||Phosphoserine|||Polar residues|||Pro residues|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212878 http://togogenome.org/gene/10090:Crygn ^@ http://purl.uniprot.org/uniprot/Q8VHL5 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Gamma-crystallin N ^@ http://purl.uniprot.org/annotation/PRO_0000311282 http://togogenome.org/gene/10090:Ssr2 ^@ http://purl.uniprot.org/uniprot/Q9CPW5 ^@ 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...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Translocon-associated protein subunit beta ^@ http://purl.uniprot.org/annotation/PRO_0000033291 http://togogenome.org/gene/10090:Bend5 ^@ http://purl.uniprot.org/uniprot/Q8C6D4 ^@ 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 ^@ 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_0000274280|||http://purl.uniprot.org/annotation/VSP_022696 http://togogenome.org/gene/10090:Cyp27b1 ^@ http://purl.uniprot.org/uniprot/O35084|||http://purl.uniprot.org/uniprot/Q66JY8 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Mutagenesis Site|||Transit Peptide ^@ 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial|||Impaired 1-alpha hydroxylase activity toward 25-hydroxyvitamin D3.|||Impaired 1-alpha hydroxylase activity toward 25-hydroxyvitamin D3. Impaired heme binding.|||Mitochondrion|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000003623 http://togogenome.org/gene/10090:Psmc3ip ^@ http://purl.uniprot.org/uniprot/C4PFH5|||http://purl.uniprot.org/uniprot/O35047 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Alters PSMC3/MND1 formation.|||DNA-binding|||Homologous-pairing protein 2 homolog|||Homologous-pairing protein 2 winged helix|||Leucine zipper with capping helix ^@ http://purl.uniprot.org/annotation/PRO_0000314136 http://togogenome.org/gene/10090:Bcl3 ^@ http://purl.uniprot.org/uniprot/Q9Z2F6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||B-cell lymphoma 3 protein homolog|||Disordered|||Phosphoserine|||Phosphoserine; by GSK3|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000066977 http://togogenome.org/gene/10090:Il17rd ^@ http://purl.uniprot.org/uniprot/Q8JZL1 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interleukin-17 receptor D|||N-linked (GlcNAc...) asparagine|||Polar residues|||SEFIR ^@ http://purl.uniprot.org/annotation/PRO_0000041872|||http://purl.uniprot.org/annotation/VSP_015585 http://togogenome.org/gene/10090:Emg1 ^@ http://purl.uniprot.org/uniprot/O35130|||http://purl.uniprot.org/uniprot/Q542P8 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Site ^@ Disordered|||Interaction with substrate rRNA|||Phosphoserine|||Ribosomal RNA small subunit methyltransferase NEP1|||Stabilizes Arg-84 ^@ http://purl.uniprot.org/annotation/PRO_0000158607 http://togogenome.org/gene/10090:Brwd1 ^@ http://purl.uniprot.org/uniprot/Q3TSA7|||http://purl.uniprot.org/uniprot/Q921C3 ^@ 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 ^@ Basic and acidic residues|||Bromo 1|||Bromo 2|||Bromodomain and WD repeat-containing protein 1|||Disordered|||In isoform B.|||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_0000235986|||http://purl.uniprot.org/annotation/VSP_018552|||http://purl.uniprot.org/annotation/VSP_018553 http://togogenome.org/gene/10090:Tmem108 ^@ http://purl.uniprot.org/uniprot/Q8BHE4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Interaction with CYFIP2|||Interaction with DST (isoform 1)|||Interaction with SH3GL2|||Polar residues|||Transmembrane protein 108 ^@ http://purl.uniprot.org/annotation/PRO_0000243914 http://togogenome.org/gene/10090:Xdh ^@ http://purl.uniprot.org/uniprot/Q00519|||http://purl.uniprot.org/uniprot/Q9CVF2 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Non-terminal Residue|||Sequence Conflict ^@ 2Fe-2S ferredoxin-type|||Aldehyde oxidase/xanthine dehydrogenase second molybdopterin binding|||FAD-binding PCMH-type|||In oxidase form|||Proton acceptor|||Removed|||Xanthine dehydrogenase/oxidase ^@ http://purl.uniprot.org/annotation/PRO_0000166085 http://togogenome.org/gene/10090:D430019H16Rik ^@ http://purl.uniprot.org/uniprot/J3QPM6 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Bud13 ^@ http://purl.uniprot.org/uniprot/Q8R149 ^@ 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 ^@ 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_0000287689|||http://purl.uniprot.org/annotation/VSP_025591 http://togogenome.org/gene/10090:Tbccd1 ^@ http://purl.uniprot.org/uniprot/Q640P7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ C-CAP/cofactor C-like|||In isoform 2.|||TBCC domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000304945|||http://purl.uniprot.org/annotation/VSP_028139|||http://purl.uniprot.org/annotation/VSP_028140 http://togogenome.org/gene/10090:Lgals7 ^@ http://purl.uniprot.org/uniprot/Q9CRB1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Galectin ^@ http://togogenome.org/gene/10090:Cxcl9 ^@ http://purl.uniprot.org/uniprot/P18340 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic residues|||C-X-C motif chemokine 9|||Disordered|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000005100 http://togogenome.org/gene/10090:Pstpip2 ^@ http://purl.uniprot.org/uniprot/Q99M15 ^@ 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 ^@ Disordered|||F-BAR|||Phosphotyrosine|||Proline-serine-threonine phosphatase-interacting protein 2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000058542 http://togogenome.org/gene/10090:Unc5d ^@ http://purl.uniprot.org/uniprot/A0A1B0GSR6|||http://purl.uniprot.org/uniprot/A6H5Z5|||http://purl.uniprot.org/uniprot/B7ZMT2|||http://purl.uniprot.org/uniprot/C5IAW8|||http://purl.uniprot.org/uniprot/Q8K1S2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cleavage; by caspase-3|||Cytoplasmic|||Death|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Important for interaction with FLRT2|||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_0000036080|||http://purl.uniprot.org/annotation/PRO_5015086520|||http://purl.uniprot.org/annotation/PRO_5015087434|||http://purl.uniprot.org/annotation/PRO_5015087990|||http://purl.uniprot.org/annotation/PRO_5025092865 http://togogenome.org/gene/10090:Siah3 ^@ http://purl.uniprot.org/uniprot/B2RWG3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Seven-in-absentia protein TRAF-like ^@ http://togogenome.org/gene/10090:Rwdd3 ^@ http://purl.uniprot.org/uniprot/E9Q1R6|||http://purl.uniprot.org/uniprot/Q3UYX7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ RWD ^@ http://togogenome.org/gene/10090:Irx1 ^@ http://purl.uniprot.org/uniprot/P81068 ^@ 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_0000049152 http://togogenome.org/gene/10090:Upf3b ^@ http://purl.uniprot.org/uniprot/Q3ULL6|||http://purl.uniprot.org/uniprot/Q80UI8 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||UPF3 ^@ http://togogenome.org/gene/10090:Sh3tc2 ^@ http://purl.uniprot.org/uniprot/Q3UPD8|||http://purl.uniprot.org/uniprot/Q6DFU9|||http://purl.uniprot.org/uniprot/Q80VA5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||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_0000106357|||http://purl.uniprot.org/annotation/VSP_009887|||http://purl.uniprot.org/annotation/VSP_009888|||http://purl.uniprot.org/annotation/VSP_009889|||http://purl.uniprot.org/annotation/VSP_009890|||http://purl.uniprot.org/annotation/VSP_009891|||http://purl.uniprot.org/annotation/VSP_009892 http://togogenome.org/gene/10090:Gmppa ^@ http://purl.uniprot.org/uniprot/Q922H4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Mannose-1-phosphate guanyltransferase alpha ^@ http://purl.uniprot.org/annotation/PRO_0000327873 http://togogenome.org/gene/10090:Dglucy ^@ http://purl.uniprot.org/uniprot/Q8BH86 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ D-glutamate cyclase, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000036293|||http://purl.uniprot.org/annotation/VSP_010512|||http://purl.uniprot.org/annotation/VSP_010513 http://togogenome.org/gene/10090:Or6b2b ^@ http://purl.uniprot.org/uniprot/Q7TQS4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hip1r ^@ http://purl.uniprot.org/uniprot/Q9JKY5 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||ENTH|||Huntingtin-interacting protein 1-related protein|||I/LWEQ|||Important for actin binding|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000083985 http://togogenome.org/gene/10090:Gpr34 ^@ http://purl.uniprot.org/uniprot/Q3YL73|||http://purl.uniprot.org/uniprot/Q9R1K6 ^@ 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 34 ^@ http://purl.uniprot.org/annotation/PRO_0000069560 http://togogenome.org/gene/10090:Cyp26b1 ^@ http://purl.uniprot.org/uniprot/A0A0N4SUV4|||http://purl.uniprot.org/uniprot/Q811W2 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Cytochrome P450 26B1|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000416905 http://togogenome.org/gene/10090:Xpot ^@ http://purl.uniprot.org/uniprot/A0A1W2P7Q6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Importin N-terminal ^@ http://togogenome.org/gene/10090:Flt4 ^@ http://purl.uniprot.org/uniprot/P35917|||http://purl.uniprot.org/uniprot/Q5SU94 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||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|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC|||Phosphotyrosine; by autocatalysis|||Phosphotyrosine; by autocatalysis and SRC|||Protein kinase|||Proton acceptor|||Vascular endothelial growth factor receptor 3|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000016777|||http://purl.uniprot.org/annotation/PRO_5014309960 http://togogenome.org/gene/10090:Fbxw26 ^@ http://purl.uniprot.org/uniprot/Q8BI58 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Cfap90 ^@ http://purl.uniprot.org/uniprot/Q9DAR0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Cilia- and flagella-associated protein 90|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000336091 http://togogenome.org/gene/10090:Ifit1 ^@ http://purl.uniprot.org/uniprot/Q64282 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Chain|||Region|||Repeat|||Sequence Conflict|||Site ^@ Interaction with PPP-RNA|||Interaction with the 5'-triphosphate group of PPP-RNA|||Interferon-induced protein with tetratricopeptide repeats 1|||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_0000106345 http://togogenome.org/gene/10090:Nmd3 ^@ http://purl.uniprot.org/uniprot/Q99L48 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Modified Residue|||Motif|||Region|||Splice Variant ^@ 60S ribosomal export protein NMD3|||In isoform 2.|||N-acetylmethionine|||Necessary for the nuclear export of the 60S ribosomal subunit|||Nuclear and nucleolar localization signal|||Nuclear export signal|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000323562|||http://purl.uniprot.org/annotation/VSP_032020|||http://purl.uniprot.org/annotation/VSP_032021 http://togogenome.org/gene/10090:Cep120 ^@ http://purl.uniprot.org/uniprot/Q7TSG1 ^@ 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 ^@ Basic and acidic residues|||C2 1|||C2 2|||Centrosomal protein of 120 kDa|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000348263|||http://purl.uniprot.org/annotation/VSP_035126|||http://purl.uniprot.org/annotation/VSP_035127|||http://purl.uniprot.org/annotation/VSP_035128|||http://purl.uniprot.org/annotation/VSP_035129|||http://purl.uniprot.org/annotation/VSP_035130 http://togogenome.org/gene/10090:Fads2b ^@ http://purl.uniprot.org/uniprot/Q0VAX3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytochrome b5 heme-binding|||Cytoplasmic|||Disordered|||Fatty acid desaturase 2-like protein FADS2B|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Lumenal|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000348958 http://togogenome.org/gene/10090:Mc5r ^@ http://purl.uniprot.org/uniprot/P41149|||http://purl.uniprot.org/uniprot/Q496T0 ^@ 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 ^@ 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|||Melanocortin receptor 5|||N-linked (GlcNAc...) asparagine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069729 http://togogenome.org/gene/10090:Casp9 ^@ http://purl.uniprot.org/uniprot/A2AS93|||http://purl.uniprot.org/uniprot/Q8C3Q9 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Propeptide|||Region ^@ CARD|||Caspase family p20|||Caspase-9 subunit p10|||Caspase-9 subunit p35|||Disordered|||Phosphoserine|||Phosphothreonine; by MAPK1|||Phosphotyrosine; by ABL1 ^@ http://purl.uniprot.org/annotation/PRO_0000421172|||http://purl.uniprot.org/annotation/PRO_0000421173|||http://purl.uniprot.org/annotation/PRO_0000421174|||http://purl.uniprot.org/annotation/PRO_0000421175 http://togogenome.org/gene/10090:Mmp17 ^@ http://purl.uniprot.org/uniprot/Q9R0S3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Cysteine switch|||Disordered|||GPI-anchor amidated serine|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Loss of activity.|||Matrix metalloproteinase-17|||N-linked (GlcNAc...) asparagine|||Pro residues|||Removed in mature form|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028821|||http://purl.uniprot.org/annotation/PRO_0000028822|||http://purl.uniprot.org/annotation/PRO_0000028823 http://togogenome.org/gene/10090:Timm17b ^@ http://purl.uniprot.org/uniprot/Q545H3|||http://purl.uniprot.org/uniprot/Q9Z0V7 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Disulfide Bond|||Region|||Transmembrane ^@ Disordered|||Helical|||Mitochondrial import inner membrane translocase subunit Tim17-B ^@ http://purl.uniprot.org/annotation/PRO_0000210288 http://togogenome.org/gene/10090:Bicra ^@ http://purl.uniprot.org/uniprot/F8VPZ9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ BRD4-interacting chromatin-remodeling complex-associated protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000445345 http://togogenome.org/gene/10090:Pip5k1b ^@ http://purl.uniprot.org/uniprot/P70181 ^@ 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 ^@ Almost complete loss of 1-phosphatidylinositol-4-phosphate 5-kinase activity.|||Disordered|||In isoform 2.|||PIPK|||Phosphatidylinositol 4-phosphate 5-kinase type-1 beta|||Phosphoserine|||Reduced 1-phosphatidylinositol-4-phosphate 5-kinase activity by 98%. Loss of actin-remodeling activity. ^@ http://purl.uniprot.org/annotation/PRO_0000185459|||http://purl.uniprot.org/annotation/VSP_016012 http://togogenome.org/gene/10090:Try10 ^@ http://purl.uniprot.org/uniprot/Q792Z1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015098643 http://togogenome.org/gene/10090:4930578I06Rik ^@ http://purl.uniprot.org/uniprot/Q80ZQ3 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Uncharacterized protein C8orf74 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000270932 http://togogenome.org/gene/10090:Lactb2 ^@ http://purl.uniprot.org/uniprot/Q99KR3 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Endoribonuclease LACTB2|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000315744 http://togogenome.org/gene/10090:Gga3 ^@ http://purl.uniprot.org/uniprot/A2A9W7|||http://purl.uniprot.org/uniprot/Q8BMI3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ ADP-ribosylation factor-binding protein GGA3|||Autoinhibitory|||Disordered|||GAE|||GAT|||Phosphoserine|||Polar residues|||Pro residues|||Unstructured hinge|||VHS ^@ http://purl.uniprot.org/annotation/PRO_0000212685 http://togogenome.org/gene/10090:Sgca ^@ http://purl.uniprot.org/uniprot/P82350 ^@ 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 ^@ Alpha-sarcoglycan|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000031675 http://togogenome.org/gene/10090:U2surp ^@ http://purl.uniprot.org/uniprot/Q6NV83 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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_0000280071|||http://purl.uniprot.org/annotation/VSP_023525|||http://purl.uniprot.org/annotation/VSP_023526 http://togogenome.org/gene/10090:Cela3a ^@ http://purl.uniprot.org/uniprot/A2A9U8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015086009 http://togogenome.org/gene/10090:Alk ^@ http://purl.uniprot.org/uniprot/P97793 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ ALK tyrosine kinase receptor|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||Heparin-binding region|||LDL-receptor class A|||MAM 1|||MAM 2|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000016741 http://togogenome.org/gene/10090:Snrpf ^@ http://purl.uniprot.org/uniprot/P62307|||http://purl.uniprot.org/uniprot/Q497K3|||http://purl.uniprot.org/uniprot/Q6NZQ3 ^@ 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-acetylserine|||Removed|||Sm|||Small nuclear ribonucleoprotein F ^@ http://purl.uniprot.org/annotation/PRO_0000125537 http://togogenome.org/gene/10090:Erich3 ^@ http://purl.uniprot.org/uniprot/F6QRE9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glutamate rich 3|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000458848|||http://purl.uniprot.org/annotation/VSP_061973|||http://purl.uniprot.org/annotation/VSP_061974|||http://purl.uniprot.org/annotation/VSP_061975 http://togogenome.org/gene/10090:Tma7 ^@ http://purl.uniprot.org/uniprot/Q14A47|||http://purl.uniprot.org/uniprot/Q8K003 ^@ 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_0000235682 http://togogenome.org/gene/10090:Mgat1 ^@ http://purl.uniprot.org/uniprot/P27808|||http://purl.uniprot.org/uniprot/Q544F0 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Topological Domain|||Transmembrane ^@ Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000191385 http://togogenome.org/gene/10090:Scgb2b11 ^@ http://purl.uniprot.org/uniprot/A0A087WR49 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015029549 http://togogenome.org/gene/10090:Spata24 ^@ http://purl.uniprot.org/uniprot/Q6P926 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes binding to GMNN.|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Required for interaction with CBX5 and TBPL1|||Spermatogenesis-associated protein 24 ^@ http://purl.uniprot.org/annotation/PRO_0000328981|||http://purl.uniprot.org/annotation/VSP_032868|||http://purl.uniprot.org/annotation/VSP_032869 http://togogenome.org/gene/10090:Egr4 ^@ http://purl.uniprot.org/uniprot/Q3URA9|||http://purl.uniprot.org/uniprot/Q9WUF2 ^@ 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|||Disordered|||Early growth response protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000047129 http://togogenome.org/gene/10090:Snap91 ^@ http://purl.uniprot.org/uniprot/E9Q9A3|||http://purl.uniprot.org/uniprot/Q3TWS4|||http://purl.uniprot.org/uniprot/Q61548|||http://purl.uniprot.org/uniprot/Q7TT20 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Splice Variant ^@ Asymmetric dimethylarginine; alternate|||Clathrin coat assembly protein AP180|||Disordered|||ENTH|||In isoform 3.|||In isoform Short and isoform 3.|||O-linked (GlcNAc) threonine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000193865|||http://purl.uniprot.org/annotation/VSP_000172|||http://purl.uniprot.org/annotation/VSP_022635 http://togogenome.org/gene/10090:Itfg1 ^@ http://purl.uniprot.org/uniprot/Q99KW9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ FG-GAP 1; atypical|||FG-GAP 2; atypical|||FG-GAP 3; atypical|||Helical|||N-linked (GlcNAc...) asparagine|||T-cell immunomodulatory protein ^@ http://purl.uniprot.org/annotation/PRO_0000034355 http://togogenome.org/gene/10090:Gm7073 ^@ http://purl.uniprot.org/uniprot/E9QAS1|||http://purl.uniprot.org/uniprot/Q3UXG0 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Region|||Signal Peptide ^@ Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015090370 http://togogenome.org/gene/10090:Defa33 ^@ http://purl.uniprot.org/uniprot/Q8C1N9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Alpha-defensin N-terminal|||Beta/alpha-defensin C-terminal|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015099048 http://togogenome.org/gene/10090:Zswim7 ^@ http://purl.uniprot.org/uniprot/Q9CWQ2 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Zinc Finger ^@ SWIM-type|||Zinc finger SWIM domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000307404 http://togogenome.org/gene/10090:Phldb2 ^@ http://purl.uniprot.org/uniprot/Q8K1N2 ^@ 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.|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology-like domain family B member 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053895|||http://purl.uniprot.org/annotation/VSP_016746 http://togogenome.org/gene/10090:Elf3 ^@ http://purl.uniprot.org/uniprot/Q3UPW2 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn ^@ Abolishes nuclear localization.|||Abrogates nuclear localization activity.|||Basic and acidic residues|||Clear and exclusive nuclear accumulation.|||Disordered|||ETS|||ETS-related transcription factor Elf-3|||In isoform 2.|||PNT|||Polar residues|||Significant loss of transactivation activity.|||Slight reduction in transactivation activity. ^@ http://purl.uniprot.org/annotation/PRO_0000287682|||http://purl.uniprot.org/annotation/VSP_052434 http://togogenome.org/gene/10090:Lca5 ^@ http://purl.uniprot.org/uniprot/G5E886|||http://purl.uniprot.org/uniprot/G5E887|||http://purl.uniprot.org/uniprot/Q80ST9 ^@ 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.|||Lebercilin|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089547|||http://purl.uniprot.org/annotation/VSP_014944|||http://purl.uniprot.org/annotation/VSP_014945 http://togogenome.org/gene/10090:Or3a1c ^@ http://purl.uniprot.org/uniprot/Q8VFX8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nutf2 ^@ http://purl.uniprot.org/uniprot/P61971 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ N6-acetyllysine|||NTF2|||Nuclear transport factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000194776 http://togogenome.org/gene/10090:Odf3 ^@ http://purl.uniprot.org/uniprot/Q920N1 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ Ciliary microtubule associated protein 1A|||Disordered|||STPGR 1|||STPGR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000299465 http://togogenome.org/gene/10090:Entrep2 ^@ http://purl.uniprot.org/uniprot/Q6A044 ^@ 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|||Protein ENTREP2 ^@ http://purl.uniprot.org/annotation/PRO_0000314456|||http://purl.uniprot.org/annotation/VSP_032011 http://togogenome.org/gene/10090:Htr3a ^@ http://purl.uniprot.org/uniprot/P23979|||http://purl.uniprot.org/uniprot/Q8K1F4 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 5-hydroxytryptamine receptor 3A|||Cytoplasmic|||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 5-HT3R-AS.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000409|||http://purl.uniprot.org/annotation/PRO_5015099257|||http://purl.uniprot.org/annotation/VSP_000079 http://togogenome.org/gene/10090:Eri3 ^@ http://purl.uniprot.org/uniprot/Q8C460 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Splice Variant ^@ ERI1 exoribonuclease 3|||Exonuclease|||In isoform 2.|||In isoform 3.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000317627|||http://purl.uniprot.org/annotation/VSP_031105|||http://purl.uniprot.org/annotation/VSP_031106|||http://purl.uniprot.org/annotation/VSP_031107 http://togogenome.org/gene/10090:Plch1 ^@ http://purl.uniprot.org/uniprot/H3BKK4|||http://purl.uniprot.org/uniprot/Q4KWH5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1|||Basic and acidic residues|||Basic residues|||C2|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000329008|||http://purl.uniprot.org/annotation/VSP_032907|||http://purl.uniprot.org/annotation/VSP_032908|||http://purl.uniprot.org/annotation/VSP_032909|||http://purl.uniprot.org/annotation/VSP_032910|||http://purl.uniprot.org/annotation/VSP_032911|||http://purl.uniprot.org/annotation/VSP_032912|||http://purl.uniprot.org/annotation/VSP_032913|||http://purl.uniprot.org/annotation/VSP_032914|||http://purl.uniprot.org/annotation/VSP_032915 http://togogenome.org/gene/10090:Apon ^@ http://purl.uniprot.org/uniprot/G3X9D6 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015091846 http://togogenome.org/gene/10090:Or51b6b ^@ http://purl.uniprot.org/uniprot/E9Q382 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r12 ^@ http://purl.uniprot.org/uniprot/G5E8G1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Adgrv1 ^@ http://purl.uniprot.org/uniprot/B8JJE0 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Transmembrane ^@ Disordered|||EAR|||G-protein coupled receptors family 2 profile 2|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Adamdec1 ^@ http://purl.uniprot.org/uniprot/Q3U0T4|||http://purl.uniprot.org/uniprot/Q9R0X2 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Signal Peptide ^@ ADAM DEC1|||Disintegrin|||N-linked (GlcNAc...) asparagine|||Peptidase M12B ^@ http://purl.uniprot.org/annotation/PRO_0000029148|||http://purl.uniprot.org/annotation/PRO_0000029149|||http://purl.uniprot.org/annotation/PRO_5009970814 http://togogenome.org/gene/10090:Timm21 ^@ http://purl.uniprot.org/uniprot/Q8CCM6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Mitochondrial import inner membrane translocase subunit Tim21|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000043229|||http://purl.uniprot.org/annotation/VSP_060547|||http://purl.uniprot.org/annotation/VSP_060548 http://togogenome.org/gene/10090:Nhlrc3 ^@ http://purl.uniprot.org/uniprot/Q8CCH2 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Glycosylation Site|||Repeat|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL repeat-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000317195 http://togogenome.org/gene/10090:Cald1 ^@ http://purl.uniprot.org/uniprot/E9QA16|||http://purl.uniprot.org/uniprot/Q3TUS1|||http://purl.uniprot.org/uniprot/Q8VCQ8 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Lhb ^@ http://purl.uniprot.org/uniprot/G3X9G6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Glycoprotein hormone subunit beta ^@ http://purl.uniprot.org/annotation/PRO_5015091825 http://togogenome.org/gene/10090:Cfap44 ^@ http://purl.uniprot.org/uniprot/E9Q5M6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Acidic residues|||Basic and acidic residues|||Cilia- and flagella-associated protein 44|||Disordered|||Phosphoserine|||Polar residues|||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_0000445514 http://togogenome.org/gene/10090:Mtch2 ^@ http://purl.uniprot.org/uniprot/A2AFW6|||http://purl.uniprot.org/uniprot/Q791V5|||http://purl.uniprot.org/uniprot/Q9D050 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial carrier homolog 2|||Mitochondrial intermembrane|||N-acetylalanine|||Removed|||Solcar|||Solcar 1|||Solcar 2 ^@ http://purl.uniprot.org/annotation/PRO_0000090638 http://togogenome.org/gene/10090:Atf7ip2 ^@ http://purl.uniprot.org/uniprot/Q3UL97 ^@ 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 ^@ Activating transcription factor 7-interacting protein 2|||Disordered|||Fibronectin type-III|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000281785|||http://purl.uniprot.org/annotation/VSP_024044|||http://purl.uniprot.org/annotation/VSP_024045|||http://purl.uniprot.org/annotation/VSP_024046|||http://purl.uniprot.org/annotation/VSP_024047|||http://purl.uniprot.org/annotation/VSP_024048|||http://purl.uniprot.org/annotation/VSP_024049 http://togogenome.org/gene/10090:Greb1l ^@ http://purl.uniprot.org/uniprot/B9EJV3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||GREB1-like protein|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000416127 http://togogenome.org/gene/10090:Zfp449 ^@ http://purl.uniprot.org/uniprot/Q8CB76 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||SCAN box ^@ http://togogenome.org/gene/10090:Cyp4f18 ^@ http://purl.uniprot.org/uniprot/Q99N16 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Cytochrome P450 4F3|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000238924 http://togogenome.org/gene/10090:Tle6 ^@ http://purl.uniprot.org/uniprot/D3Z5E1|||http://purl.uniprot.org/uniprot/Q9WVB3 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Nuclear localization signal|||Phosphoserine|||Transducin-like enhancer protein 6|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8 ^@ http://purl.uniprot.org/annotation/PRO_0000051287 http://togogenome.org/gene/10090:Lrrc1 ^@ http://purl.uniprot.org/uniprot/G3X9W3|||http://purl.uniprot.org/uniprot/Q571M3|||http://purl.uniprot.org/uniprot/Q80VQ1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||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 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_0000084490|||http://purl.uniprot.org/annotation/VSP_010914|||http://purl.uniprot.org/annotation/VSP_010915|||http://purl.uniprot.org/annotation/VSP_010916 http://togogenome.org/gene/10090:Rhoc ^@ http://purl.uniprot.org/uniprot/Q62159 ^@ 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|||Removed in mature form|||Rho-related GTP-binding protein RhoC|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000042024|||http://purl.uniprot.org/annotation/PRO_0000042025 http://togogenome.org/gene/10090:Cldn12 ^@ http://purl.uniprot.org/uniprot/Q9ET43 ^@ 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_0000144766 http://togogenome.org/gene/10090:Myo7a ^@ http://purl.uniprot.org/uniprot/A0A0R4J113|||http://purl.uniprot.org/uniprot/P97479|||http://purl.uniprot.org/uniprot/Q5MJ56 ^@ 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 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn ^@ Actin-binding|||FERM|||FERM 1|||FERM 2|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||In isoform 2.|||In sh-1.|||MyTH4|||MyTH4 1|||MyTH4 2|||Myosin motor|||Phosphoserine|||Phosphothreonine|||Reduced affinity for USH1G.|||SAH|||SH3|||Strongly reduced affinity for USH1G.|||Unconventional myosin-VIIa ^@ http://purl.uniprot.org/annotation/PRO_0000123467|||http://purl.uniprot.org/annotation/VSP_042238 http://togogenome.org/gene/10090:Nxt1 ^@ http://purl.uniprot.org/uniprot/Q9QZV9 ^@ 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|||NTF2|||NTF2-related export protein 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194794 http://togogenome.org/gene/10090:Gpt2 ^@ http://purl.uniprot.org/uniprot/Q8BGT5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Alanine aminotransferase 2|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000247533 http://togogenome.org/gene/10090:Iqck ^@ http://purl.uniprot.org/uniprot/E9PUC1|||http://purl.uniprot.org/uniprot/Q3UUI0 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Mrpl57 ^@ http://purl.uniprot.org/uniprot/Q9CQF8 ^@ Chain|||Molecule Processing ^@ Chain ^@ Large ribosomal subunit protein mL63 ^@ http://purl.uniprot.org/annotation/PRO_0000253542 http://togogenome.org/gene/10090:Ube2k ^@ http://purl.uniprot.org/uniprot/A0A0J9YU07|||http://purl.uniprot.org/uniprot/P61087|||http://purl.uniprot.org/uniprot/Q6ZWQ6 ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ 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 thioester intermediate|||N-acetylalanine|||N6-acetyllysine; alternate|||Phosphoserine|||Removed|||UBA|||UBC core|||Ubiquitin-conjugating enzyme E2 K ^@ http://purl.uniprot.org/annotation/PRO_0000082444 http://togogenome.org/gene/10090:Abca4 ^@ http://purl.uniprot.org/uniprot/O35600 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ ABC transporter 1|||ABC transporter 2|||Cleavage; by trypsin|||Cytoplasmic|||Disordered|||Essential for ATP binding and ATPase activity|||Extracellular|||Helical|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Retinal-specific phospholipid-transporting ATPase ABCA4 ^@ http://purl.uniprot.org/annotation/PRO_0000093302 http://togogenome.org/gene/10090:Sgk1 ^@ http://purl.uniprot.org/uniprot/E9Q1B0|||http://purl.uniprot.org/uniprot/E9Q8C1|||http://purl.uniprot.org/uniprot/Q9WVC6 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ AGC-kinase C-terminal|||Disordered|||In isoform 2.|||In isoform 3.|||Interchain (with C-193)|||Interchain (with C-258)|||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_0000086643|||http://purl.uniprot.org/annotation/VSP_037788|||http://purl.uniprot.org/annotation/VSP_037789 http://togogenome.org/gene/10090:Ap1s1 ^@ http://purl.uniprot.org/uniprot/P61967 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ AP-1 complex subunit sigma-1A|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000193798 http://togogenome.org/gene/10090:Ankrd13a ^@ http://purl.uniprot.org/uniprot/Q80UP5 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Modified Residue|||Repeat ^@ ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein 13A|||Phosphoserine|||UIM 1|||UIM 2|||UIM 3|||UIM 4 ^@ http://purl.uniprot.org/annotation/PRO_0000066910 http://togogenome.org/gene/10090:Isoc2a ^@ http://purl.uniprot.org/uniprot/B2RY90|||http://purl.uniprot.org/uniprot/P85094 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Isochorismatase domain-containing protein 2A|||Isochorismatase-like|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000282952 http://togogenome.org/gene/10090:Fbxl13 ^@ http://purl.uniprot.org/uniprot/B7ZNK1|||http://purl.uniprot.org/uniprot/B7ZNK2|||http://purl.uniprot.org/uniprot/Q8CDU4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant ^@ F-box|||F-box and leucine-rich repeat protein 13|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6 ^@ http://purl.uniprot.org/annotation/PRO_0000119860|||http://purl.uniprot.org/annotation/VSP_013006|||http://purl.uniprot.org/annotation/VSP_013007|||http://purl.uniprot.org/annotation/VSP_013008 http://togogenome.org/gene/10090:Plekhg6 ^@ http://purl.uniprot.org/uniprot/Q8R0J1 ^@ 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|||DH|||Disordered|||PH|||Pleckstrin homology domain-containing family G member 6|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000307913 http://togogenome.org/gene/10090:Gramd1c ^@ http://purl.uniprot.org/uniprot/A0A3P9AQ15|||http://purl.uniprot.org/uniprot/Q8CI52 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand|||Transmembrane|||Turn ^@ Basic and acidic residues|||Disordered|||GRAM|||Helical|||Polar residues|||Protein Aster-C|||VASt ^@ http://purl.uniprot.org/annotation/PRO_0000287452 http://togogenome.org/gene/10090:Rab8a ^@ http://purl.uniprot.org/uniprot/P55258 ^@ 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|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-8A|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121132|||http://purl.uniprot.org/annotation/PRO_0000370795 http://togogenome.org/gene/10090:Vmn1r43 ^@ http://purl.uniprot.org/uniprot/Q8VIC9 ^@ 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|||Vomeronasal type-1 receptor 43 ^@ http://purl.uniprot.org/annotation/PRO_0000239960 http://togogenome.org/gene/10090:Ehf ^@ http://purl.uniprot.org/uniprot/O70273 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||ETS|||ETS homologous factor|||In isoform 2.|||In isoform 3.|||PNT ^@ http://purl.uniprot.org/annotation/PRO_0000257970|||http://purl.uniprot.org/annotation/VSP_052191|||http://purl.uniprot.org/annotation/VSP_052192|||http://purl.uniprot.org/annotation/VSP_052193 http://togogenome.org/gene/10090:Pnck ^@ http://purl.uniprot.org/uniprot/Q3TYC1|||http://purl.uniprot.org/uniprot/Q3UYI0|||http://purl.uniprot.org/uniprot/Q9QYK9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Calcium/calmodulin-dependent protein kinase type 1B|||Calmodulin-binding|||Disordered|||Phosphoserine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086080 http://togogenome.org/gene/10090:Pptc7 ^@ http://purl.uniprot.org/uniprot/Q6NVE9 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Mitochondrion|||PPM-type phosphatase|||Protein phosphatase PTC7 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000328746|||http://purl.uniprot.org/annotation/VSP_032772 http://togogenome.org/gene/10090:N4bp2l1 ^@ http://purl.uniprot.org/uniprot/Q3V2Q8 ^@ 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.|||NEDD4-binding protein 2-like 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000318959|||http://purl.uniprot.org/annotation/VSP_031320 http://togogenome.org/gene/10090:Gm14308 ^@ http://purl.uniprot.org/uniprot/A2ART4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Slc13a3 ^@ http://purl.uniprot.org/uniprot/Q3UUJ6|||http://purl.uniprot.org/uniprot/Q91Y63 ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Na(+)/dicarboxylate cotransporter 3 ^@ http://purl.uniprot.org/annotation/PRO_0000172493 http://togogenome.org/gene/10090:Degs2 ^@ http://purl.uniprot.org/uniprot/Q8R2F2 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Initiator Methionine|||Lipid Binding|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In isoform 2.|||N-myristoyl glycine|||Removed|||Required for C4-hydroxylase activity|||Sphingolipid delta(4)-desaturase/C4-monooxygenase DES2 ^@ http://purl.uniprot.org/annotation/PRO_0000312817|||http://purl.uniprot.org/annotation/VSP_052629 http://togogenome.org/gene/10090:Or56a3 ^@ http://purl.uniprot.org/uniprot/Q8VGV0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Spopfm2 ^@ http://purl.uniprot.org/uniprot/Q3UTC4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB|||MATH ^@ http://togogenome.org/gene/10090:Ppp2r2a ^@ http://purl.uniprot.org/uniprot/Q6P1F6 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat ^@ 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_0000071417 http://togogenome.org/gene/10090:Rassf1 ^@ http://purl.uniprot.org/uniprot/A9YZW8|||http://purl.uniprot.org/uniprot/Q3UIV8|||http://purl.uniprot.org/uniprot/Q99MK9 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform C.|||MOAP1-binding|||Mediates interaction with E4F1|||N-acetylserine|||Phorbol-ester/DAG-type|||Phosphoserine|||Ras association domain-containing protein 1|||Ras-associating|||Removed|||SARAH ^@ http://purl.uniprot.org/annotation/PRO_0000068892|||http://purl.uniprot.org/annotation/VSP_050779|||http://purl.uniprot.org/annotation/VSP_050780 http://togogenome.org/gene/10090:Zbtb40 ^@ http://purl.uniprot.org/uniprot/Q6PCS8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB|||Basic and acidic residues|||C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Crb3 ^@ http://purl.uniprot.org/uniprot/Q8QZT4 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with EPB41L5|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Polar residues|||Protein crumbs homolog 3 ^@ http://purl.uniprot.org/annotation/PRO_0000021006|||http://purl.uniprot.org/annotation/VSP_013990 http://togogenome.org/gene/10090:Or6c211 ^@ http://purl.uniprot.org/uniprot/Q8VEU1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:St6galnac2 ^@ http://purl.uniprot.org/uniprot/P70277 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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_0000149273 http://togogenome.org/gene/10090:2310030G06Rik ^@ http://purl.uniprot.org/uniprot/Q9D8L0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Uncharacterized protein C11orf52 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000263610|||http://purl.uniprot.org/annotation/VSP_021875 http://togogenome.org/gene/10090:Acsm4 ^@ http://purl.uniprot.org/uniprot/Q80W40 ^@ Binding Site|||Chain|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Transit Peptide ^@ Acyl-coenzyme A synthetase ACSM4, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000306104 http://togogenome.org/gene/10090:Vmn1r17 ^@ http://purl.uniprot.org/uniprot/Q8R2D8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Esp38 ^@ http://purl.uniprot.org/uniprot/A8R0X1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015086680 http://togogenome.org/gene/10090:Gins4 ^@ http://purl.uniprot.org/uniprot/Q99LZ3 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ DNA replication complex GINS protein SLD5|||DNA replication complex GINS protein SLD5, N-terminally processed|||Important for GINS complex assembly|||N-acetylmethionine|||N-acetylthreonine; in DNA replication complex GINS protein SLD5, N-terminally processed|||Phosphoserine|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000327621|||http://purl.uniprot.org/annotation/PRO_0000421795 http://togogenome.org/gene/10090:Ncald ^@ http://purl.uniprot.org/uniprot/Q91X97 ^@ 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 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||N-myristoyl glycine|||Neurocalcin-delta|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073783 http://togogenome.org/gene/10090:Hdgf ^@ http://purl.uniprot.org/uniprot/P51859 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes disulfide bond formation.|||Abolishes secretion.|||Acidic residues|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Does not affect secretion.|||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|||N6-acetyllysine|||Nuclear localization signal|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000191701 http://togogenome.org/gene/10090:Slc30a2 ^@ http://purl.uniprot.org/uniprot/D3Z5N1|||http://purl.uniprot.org/uniprot/Q2HJ10 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform 2.|||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_0000415850|||http://purl.uniprot.org/annotation/VSP_061730 http://togogenome.org/gene/10090:Dock1 ^@ http://purl.uniprot.org/uniprot/Q8BUR4 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 1|||Disordered|||In isoform 2.|||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_0000189985|||http://purl.uniprot.org/annotation/VSP_022205|||http://purl.uniprot.org/annotation/VSP_022206 http://togogenome.org/gene/10090:Lynx1 ^@ http://purl.uniprot.org/uniprot/P0DP60 ^@ 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|||Ly-6/neurotoxin-like protein 1|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036158|||http://purl.uniprot.org/annotation/PRO_0000440643 http://togogenome.org/gene/10090:Nfxl1 ^@ http://purl.uniprot.org/uniprot/E9Q8I7 ^@ Coiled-Coil|||Domain Extent|||Region|||Transmembrane ^@ Coiled-Coil|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||RING-type ^@ http://togogenome.org/gene/10090:Or5ak20 ^@ http://purl.uniprot.org/uniprot/Q7TRA1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp568 ^@ http://purl.uniprot.org/uniprot/E9PYI1 ^@ 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 ^@ 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|||Decreases transcriptional repression.|||Disordered|||In chato; probable null mutation. Almost abolishes transcriptional repression. No effect on interaction with THRIM28. Embryonic development arrests at stage 9 dpc. Widespread morphogenetic defects are found in all germ layers, associated with defective convergent extension movements. The anterior-posterior axis is abnormally shortened, somites are mediolaterally expanded, and the neural tube fails to close normally. Morphogenesis of most mesodermal tissues is also defective. The definitive endoderm fails to narrow and elongate leading to an open gut tube. Extraembryonic tissues are also abnormal with bubble-like protrusions in the yolk sac, aberrant migration of extraembryonic mesoderm, and incomplete placental development. Abolishes interaction with TRIM28; when associated with P-154.|||In isoform 2.|||Increases transcriptional repression. No effect on interaction with THRIM28.|||KRAB 1|||KRAB 2|||No effect on transcriptional repression.|||No effect on transcriptional repression. Abolishes interaction with TRIM28; when associated with P-64.|||No effect on transcriptional repression. No effect on interaction with THRIM28.|||Strongly decreases transcriptional repression. No effect on interaction with THRIM28. No effect on interaction with THRIM28.|||Zinc finger protein 568 ^@ http://purl.uniprot.org/annotation/PRO_0000438106|||http://purl.uniprot.org/annotation/VSP_058610 http://togogenome.org/gene/10090:Gpr27 ^@ http://purl.uniprot.org/uniprot/O54897 ^@ 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 27 ^@ http://purl.uniprot.org/annotation/PRO_0000069549 http://togogenome.org/gene/10090:Sult2a7 ^@ http://purl.uniprot.org/uniprot/K7N6K8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Cpxm2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0C4|||http://purl.uniprot.org/uniprot/Q9D2L5 ^@ 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 ^@ Basic and acidic residues|||Disordered|||F5/8 type C|||Inactive carboxypeptidase-like protein X2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000004410|||http://purl.uniprot.org/annotation/PRO_5015044290 http://togogenome.org/gene/10090:Rrm1 ^@ http://purl.uniprot.org/uniprot/P07742 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000187191 http://togogenome.org/gene/10090:Clec2l ^@ http://purl.uniprot.org/uniprot/P0C7M9 ^@ 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_0000339386 http://togogenome.org/gene/10090:Gga1 ^@ http://purl.uniprot.org/uniprot/Q8R0H9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ ADP-ribosylation factor-binding protein GGA1|||Autoinhibitory|||Disordered|||GAE|||GAT|||Interaction with ARF3|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||Unstructured hinge|||VHS ^@ http://purl.uniprot.org/annotation/PRO_0000212681 http://togogenome.org/gene/10090:8030474K03Rik ^@ http://purl.uniprot.org/uniprot/F6R3T1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Kif13b ^@ http://purl.uniprot.org/uniprot/A0A286YCV9|||http://purl.uniprot.org/uniprot/E9Q4K7 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||CAP-Gly|||Disordered|||Kinesin motor|||Polar residues ^@ http://togogenome.org/gene/10090:Foxr2 ^@ http://purl.uniprot.org/uniprot/Q3UM89 ^@ Chain|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||DNA Binding ^@ Fork-head|||Forkhead box protein R2 ^@ http://purl.uniprot.org/annotation/PRO_0000253781 http://togogenome.org/gene/10090:Adam24 ^@ http://purl.uniprot.org/uniprot/Q8CDV3|||http://purl.uniprot.org/uniprot/Q9R160 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||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|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 24|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029122|||http://purl.uniprot.org/annotation/PRO_0000029123|||http://purl.uniprot.org/annotation/PRO_5004304023 http://togogenome.org/gene/10090:Ppp2r5a ^@ http://purl.uniprot.org/uniprot/Q6PD03 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform ^@ http://purl.uniprot.org/annotation/PRO_0000071449 http://togogenome.org/gene/10090:Mapt ^@ http://purl.uniprot.org/uniprot/P10637|||http://purl.uniprot.org/uniprot/Q3UH19|||http://purl.uniprot.org/uniprot/Q547J4|||http://purl.uniprot.org/uniprot/Q8C5K4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and 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 isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E.|||In isoform Tau-B and isoform Tau-C.|||In isoform Tau-B, isoform Tau-C, isoform Tau-D and isoform Tau-E.|||In isoform Tau-B.|||In isoform Tau-E.|||Microtubule-associated protein tau|||N-acetylalanine|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||O-linked (GlcNAc...) serine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FYN|||Polar residues|||Removed|||Tau/MAP 1|||Tau/MAP 2|||Tau/MAP 3|||Tau/MAP 4 ^@ http://purl.uniprot.org/annotation/PRO_0000072742|||http://purl.uniprot.org/annotation/VSP_003185|||http://purl.uniprot.org/annotation/VSP_003186|||http://purl.uniprot.org/annotation/VSP_003187|||http://purl.uniprot.org/annotation/VSP_003188|||http://purl.uniprot.org/annotation/VSP_003189|||http://purl.uniprot.org/annotation/VSP_003190 http://togogenome.org/gene/10090:Tnc ^@ http://purl.uniprot.org/uniprot/Q148T5|||http://purl.uniprot.org/uniprot/Q80YX1|||http://purl.uniprot.org/uniprot/Q8C9Z1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 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 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 isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tenascin ^@ http://purl.uniprot.org/annotation/PRO_0000248607|||http://purl.uniprot.org/annotation/PRO_5014306905|||http://purl.uniprot.org/annotation/VSP_052144|||http://purl.uniprot.org/annotation/VSP_052145|||http://purl.uniprot.org/annotation/VSP_052146|||http://purl.uniprot.org/annotation/VSP_052147 http://togogenome.org/gene/10090:Rps6ka3 ^@ http://purl.uniprot.org/uniprot/B1AXN9|||http://purl.uniprot.org/uniprot/P18654 ^@ 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|||Region|||Strand|||Turn ^@ AGC-kinase C-terminal|||Attenuates activation by MAPK1/ERK1 and MAPK3/ERK2.|||Disordered|||Loss of interaction with PDPK1 and phosphorylation at S-227.|||Loss of phosphorylation and activation by PDPK1.|||Loss of phosphorylation by PDPK1; loss of activation by PDPK1 and EGF.|||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_0000086204 http://togogenome.org/gene/10090:Prr32 ^@ http://purl.uniprot.org/uniprot/A2AFE9 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Proline-rich protein 32 ^@ http://purl.uniprot.org/annotation/PRO_0000336103 http://togogenome.org/gene/10090:Epha8 ^@ http://purl.uniprot.org/uniprot/O09127 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 8|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Kinase-dead. Loss of autophosphorylation but has no effect on regulation of cell adhesion.|||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|||Reduced phosphorylation and reduced association with FYN.|||Reduced phosphorylation.|||Reduced tyrosine kinase activity.|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000016823 http://togogenome.org/gene/10090:Gm15093 ^@ http://purl.uniprot.org/uniprot/A2BI72 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Vars ^@ http://purl.uniprot.org/uniprot/Q790I0|||http://purl.uniprot.org/uniprot/Q9Z1Q9 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 'HIGH' region|||'KMSKS' region|||Basic and acidic residues|||Disordered|||GST C-terminal|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed|||Valine--tRNA ligase ^@ http://purl.uniprot.org/annotation/PRO_0000106254 http://togogenome.org/gene/10090:Syf2 ^@ http://purl.uniprot.org/uniprot/Q9D198 ^@ 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 SUMO2)|||N-acetylalanine|||Pre-mRNA-splicing factor SYF2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000250377 http://togogenome.org/gene/10090:Rac1 ^@ http://purl.uniprot.org/uniprot/P63001 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide ^@ Constitutively active. Interacts with PARD6 proteins.|||Cysteine methyl ester|||Effector region|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Polybasic region; required for nuclear import|||Ras-related C3 botulinum toxin substrate 1|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000042038|||http://purl.uniprot.org/annotation/PRO_0000042039 http://togogenome.org/gene/10090:Myh6 ^@ http://purl.uniprot.org/uniprot/B2RQQ1|||http://purl.uniprot.org/uniprot/Q02566 ^@ 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|||Calmodulin-binding|||Disordered|||IQ|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-6|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000123403 http://togogenome.org/gene/10090:Usp43 ^@ http://purl.uniprot.org/uniprot/A6PWR8|||http://purl.uniprot.org/uniprot/Q8BUM9 ^@ 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|||Basic and acidic residues|||Disordered|||In isoform 2.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 43 ^@ http://purl.uniprot.org/annotation/PRO_0000249522|||http://purl.uniprot.org/annotation/VSP_020469|||http://purl.uniprot.org/annotation/VSP_020470 http://togogenome.org/gene/10090:Ago4 ^@ http://purl.uniprot.org/uniprot/Q8CJF8|||http://purl.uniprot.org/uniprot/Q9CS58 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||PAZ|||Piwi|||Protein argonaute-4 ^@ http://purl.uniprot.org/annotation/PRO_0000194064|||http://purl.uniprot.org/annotation/VSP_036487 http://togogenome.org/gene/10090:Pfkfb1 ^@ http://purl.uniprot.org/uniprot/A2AFM9|||http://purl.uniprot.org/uniprot/P70266 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ 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_0000179961|||http://purl.uniprot.org/annotation/VSP_022168 http://togogenome.org/gene/10090:Npc1 ^@ http://purl.uniprot.org/uniprot/O35604|||http://purl.uniprot.org/uniprot/Q7TMD4 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreased affinity for NPC2.|||Decreased affinity for NPC2. Loss of function in cholesterol transport. No effect on subcellular location. Strongly decreased affinity for NPC2; when associated with A-421.|||Di-leucine motif|||Helical|||Important for cholesterol binding|||Important for cholesterol binding and cholesterol transfer from NPC1 to liposomes|||In Npc1-nmf164; strongly decreased protein levels. Causes abnormal lipid storage in the spleen and liver, loss of cerebellar Purkinje cells and age-dependent ataxia.|||Loss of function giving rise to cholesterol accumulation in kidney, liver, lung and spleen. No effect on lysosomal location. Mice display age-dependent weight loss, neurodegeneration with loss of Purkinje cells, ataxia and premature death at a median age of 84 days.|||Lumenal|||N-linked (GlcNAc...) asparagine|||NPC intracellular cholesterol transporter 1|||No effect on affinity for NPC2.|||Required for location in lysosomes|||SSD|||Strongly decreased affinity for NPC2.|||Strongly decreased affinity for NPC2. No effect on lysosomal location.|||Strongly decreased affinity for NPC2; when associated with 503-A-A-504. ^@ http://purl.uniprot.org/annotation/PRO_0000023262|||http://purl.uniprot.org/annotation/PRO_5014311827 http://togogenome.org/gene/10090:Or2ag19 ^@ http://purl.uniprot.org/uniprot/Q9EPF5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dpp8 ^@ http://purl.uniprot.org/uniprot/Q80YA7 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Sequence Conflict ^@ Charge relay system|||Dipeptidyl peptidase 8 ^@ http://purl.uniprot.org/annotation/PRO_0000122414 http://togogenome.org/gene/10090:Zkscan3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1L3|||http://purl.uniprot.org/uniprot/Q91VW9 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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|||Phosphoserine|||Phosphothreonine|||SCAN box|||Zinc finger protein with KRAB and SCAN domains 3 ^@ http://purl.uniprot.org/annotation/PRO_0000394861 http://togogenome.org/gene/10090:Atp6v0b ^@ http://purl.uniprot.org/uniprot/Q3U889|||http://purl.uniprot.org/uniprot/Q91V37 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Essential for proton translocation|||Helical|||Lumenal|||V-ATPase proteolipid subunit C-like|||V-type proton ATPase 21 kDa proteolipid subunit c""" /id="PRO_0000071778 ^@ http://togogenome.org/gene/10090:Ifng ^@ http://purl.uniprot.org/uniprot/A0A7R8C347|||http://purl.uniprot.org/uniprot/P01580 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ Interferon gamma|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000016453|||http://purl.uniprot.org/annotation/PRO_5030781498 http://togogenome.org/gene/10090:Srp9 ^@ http://purl.uniprot.org/uniprot/P49962|||http://purl.uniprot.org/uniprot/Q3UIK3|||http://purl.uniprot.org/uniprot/Q5EAT0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ SRP9|||Signal recognition particle 9 kDa protein ^@ http://purl.uniprot.org/annotation/PRO_0000135183 http://togogenome.org/gene/10090:Or2y8 ^@ http://purl.uniprot.org/uniprot/Q7TQT6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or2av9 ^@ http://purl.uniprot.org/uniprot/Q5NC45 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kbtbd7 ^@ http://purl.uniprot.org/uniprot/G5E8C2|||http://purl.uniprot.org/uniprot/Q501K2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Sting1 ^@ http://purl.uniprot.org/uniprot/A0A2R3XZC4|||http://purl.uniprot.org/uniprot/Q3TBT3 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Crosslink|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolished ability to activate IRF3.|||Abolished inhibition by nitrofuran derivatives C-178 and C-176; abolished palmitoylation.|||Abolished palmitoylation.|||Abolished sumoylation by TRIM38, leading to decreased stability.|||C-terminal tail (CTT)|||Cyclic dinucleotide-binding domain (CBD)|||Cytoplasmic|||Decrease in cGAMP-binding.|||Decreased relocalization to autophagosomes and subsequent degradation.|||Does not affect palmitoylation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In isoform 2.|||In isoform 3.|||Induces a decrease in phosphorylation by TBK1, leading to reduced ability to activate IRF3.|||Lumenal|||Mediates interaction with ZDHHC1 and ZDHHC11|||Phosphoserine; by TBK1|||S-palmitoyl cysteine|||Stimulator of interferon genes protein|||Strong decrease in cGAMP-binding.|||Strongly decreases affinity for the synthetic compound 5,6-dimethylxanthenone 4-acetic acid (DMXAA).|||pLxIS motif ^@ http://purl.uniprot.org/annotation/PRO_0000271117|||http://purl.uniprot.org/annotation/VSP_022284|||http://purl.uniprot.org/annotation/VSP_022285 http://togogenome.org/gene/10090:Dlat ^@ http://purl.uniprot.org/uniprot/Q8BMF4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Catalytic|||Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial|||Disordered|||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_0000285717 http://togogenome.org/gene/10090:Alg11 ^@ http://purl.uniprot.org/uniprot/A0A077K846|||http://purl.uniprot.org/uniprot/Q3TZM9 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Splice Variant|||Transmembrane ^@ ALG11 mannosyltransferase N-terminal|||GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase|||Glycosyl transferase family 1|||Helical|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000295617|||http://purl.uniprot.org/annotation/VSP_026940|||http://purl.uniprot.org/annotation/VSP_026941 http://togogenome.org/gene/10090:Nqo1 ^@ http://purl.uniprot.org/uniprot/Q542Y0|||http://purl.uniprot.org/uniprot/Q64669 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn ^@ Flavodoxin-like fold|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Important for apoenzyme conformational stability|||N-acetylalanine|||NAD(P)H dehydrogenase [quinone] 1|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000071623 http://togogenome.org/gene/10090:Tmem215 ^@ http://purl.uniprot.org/uniprot/A7E1Z1|||http://purl.uniprot.org/uniprot/B7ZN35 ^@ 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_0000319325 http://togogenome.org/gene/10090:Cct5 ^@ http://purl.uniprot.org/uniprot/P80316 ^@ 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)|||N-acetylalanine|||Phosphoserine|||Removed|||T-complex protein 1 subunit epsilon ^@ http://purl.uniprot.org/annotation/PRO_0000128347 http://togogenome.org/gene/10090:Rpl36a ^@ http://purl.uniprot.org/uniprot/P83882|||http://purl.uniprot.org/uniprot/Q5M9P1 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Large ribosomal subunit protein eL42 ^@ http://purl.uniprot.org/annotation/PRO_0000149120 http://togogenome.org/gene/10090:Gnpda1 ^@ http://purl.uniprot.org/uniprot/O88958|||http://purl.uniprot.org/uniprot/Q3TKA0 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict ^@ For ring-opening step|||Glucosamine-6-phosphate isomerase 1|||Glucosamine/galactosamine-6-phosphate isomerase|||Phosphothreonine|||Proton acceptor; for enolization step|||Proton acceptor; for ring-opening step ^@ http://purl.uniprot.org/annotation/PRO_0000160124 http://togogenome.org/gene/10090:Tex13a ^@ http://purl.uniprot.org/uniprot/A2AFS9 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ RanBP2-type ^@ http://togogenome.org/gene/10090:Pcid2 ^@ http://purl.uniprot.org/uniprot/Q8BFV2 ^@ 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|||PCI|||PCI domain-containing protein 2|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000121030 http://togogenome.org/gene/10090:Rnf6 ^@ http://purl.uniprot.org/uniprot/Q9DBU5 ^@ 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|||Disordered|||E3 ubiquitin-protein ligase RNF6|||Phosphoserine|||Polar residues|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000395751 http://togogenome.org/gene/10090:Sgsm1 ^@ http://purl.uniprot.org/uniprot/B2RQR5|||http://purl.uniprot.org/uniprot/D3Z7V4|||http://purl.uniprot.org/uniprot/Q8BPQ7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Abolishes interaction with RAB9A.|||Basic and acidic residues|||Disordered|||Important for interaction with RAB9A and RAB9B|||In isoform 2.|||Mildly impaired interaction with RAB9A.|||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_0000284834|||http://purl.uniprot.org/annotation/VSP_024669|||http://purl.uniprot.org/annotation/VSP_024670 http://togogenome.org/gene/10090:Tnfrsf13b ^@ http://purl.uniprot.org/uniprot/A5D8Y6|||http://purl.uniprot.org/uniprot/Q9ET35 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||TACI cysteine-rich|||TNFR-Cys 1|||TNFR-Cys 2|||Tumor necrosis factor receptor superfamily member 13B ^@ http://purl.uniprot.org/annotation/PRO_0000058932 http://togogenome.org/gene/10090:P4htm ^@ http://purl.uniprot.org/uniprot/Q2M2M8|||http://purl.uniprot.org/uniprot/Q8BG58 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EF-hand 1|||EF-hand 2|||Fe2OG dioxygenase|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Transmembrane prolyl 4-hydroxylase ^@ http://purl.uniprot.org/annotation/PRO_0000206669|||http://purl.uniprot.org/annotation/VSP_007575|||http://purl.uniprot.org/annotation/VSP_007576 http://togogenome.org/gene/10090:Inpp5j ^@ http://purl.uniprot.org/uniprot/P59644 ^@ 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 ^@ Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Catalytic|||Disordered|||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_0000209739 http://togogenome.org/gene/10090:Wfdc18 ^@ http://purl.uniprot.org/uniprot/P62810 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ WAP|||WAP four-disulfide core domain protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000041376 http://togogenome.org/gene/10090:Vmn2r15 ^@ http://purl.uniprot.org/uniprot/A0A3B2WCV8|||http://purl.uniprot.org/uniprot/L7N2A0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982395|||http://purl.uniprot.org/annotation/PRO_5017332459 http://togogenome.org/gene/10090:Ush1g ^@ http://purl.uniprot.org/uniprot/Q0VBT9|||http://purl.uniprot.org/uniprot/Q80T11 ^@ 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|||ANK 1|||ANK 2|||ANK 3|||Disordered|||Phosphoserine|||Polar residues|||SAM|||pre-mRNA splicing regulator USH1G ^@ http://purl.uniprot.org/annotation/PRO_0000067078 http://togogenome.org/gene/10090:Commd5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0U7|||http://purl.uniprot.org/uniprot/Q8R395 ^@ 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 ^@ COMM|||COMM domain-containing protein 5|||Disordered|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000077396 http://togogenome.org/gene/10090:Capn10 ^@ http://purl.uniprot.org/uniprot/Q9ESK3 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Calpain catalytic|||Calpain-10|||Domain III 1|||Domain III 2 ^@ http://purl.uniprot.org/annotation/PRO_0000207727 http://togogenome.org/gene/10090:Slbp ^@ http://purl.uniprot.org/uniprot/P97440|||http://purl.uniprot.org/uniprot/Q3TSD8|||http://purl.uniprot.org/uniprot/Q3U4T7|||http://purl.uniprot.org/uniprot/Q8K2W7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone RNA hairpin-binding protein|||Histone RNA hairpin-binding protein RNA-binding|||Nuclear localization signal NLS1|||Nuclear localization signal NLS2|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphothreonine; by CK2|||Polar residues|||RNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000100357 http://togogenome.org/gene/10090:Foxb1 ^@ http://purl.uniprot.org/uniprot/Q64732 ^@ 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_0000091804 http://togogenome.org/gene/10090:Mrap ^@ http://purl.uniprot.org/uniprot/Q9D159 ^@ 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 ^@ Disordered|||Helical|||In isoform 2.|||Melanocortin-2 receptor accessory protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096571|||http://purl.uniprot.org/annotation/VSP_003865|||http://purl.uniprot.org/annotation/VSP_003866 http://togogenome.org/gene/10090:9530068E07Rik ^@ http://purl.uniprot.org/uniprot/Q3U339|||http://purl.uniprot.org/uniprot/Q8K201 ^@ 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_0000019580|||http://purl.uniprot.org/annotation/PRO_5015097463 http://togogenome.org/gene/10090:Gpbp1 ^@ http://purl.uniprot.org/uniprot/Q6NXH3 ^@ 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 and isoform 3.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Vasculin ^@ http://purl.uniprot.org/annotation/PRO_0000324111|||http://purl.uniprot.org/annotation/VSP_032138|||http://purl.uniprot.org/annotation/VSP_032139 http://togogenome.org/gene/10090:Dmpk ^@ http://purl.uniprot.org/uniprot/E9Q6J9|||http://purl.uniprot.org/uniprot/P54265 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane ^@ AGC-kinase C-terminal|||Cytoplasmic|||Helical; Anchor for type IV membrane protein|||In isoform 10.|||In isoform 2.|||In isoform 3, isoform 4, isoform 6 and isoform 9.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 7.|||In isoform 8 and isoform 9.|||Lumenal|||Myotonin-protein kinase|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085925|||http://purl.uniprot.org/annotation/VSP_004819|||http://purl.uniprot.org/annotation/VSP_004820|||http://purl.uniprot.org/annotation/VSP_004821|||http://purl.uniprot.org/annotation/VSP_004822|||http://purl.uniprot.org/annotation/VSP_004823|||http://purl.uniprot.org/annotation/VSP_004824|||http://purl.uniprot.org/annotation/VSP_004825|||http://purl.uniprot.org/annotation/VSP_004826|||http://purl.uniprot.org/annotation/VSP_004827|||http://purl.uniprot.org/annotation/VSP_004828|||http://purl.uniprot.org/annotation/VSP_004829 http://togogenome.org/gene/10090:Zfp825 ^@ http://purl.uniprot.org/uniprot/Q91VL6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ppp3cb ^@ http://purl.uniprot.org/uniprot/A0A6B9EQU3|||http://purl.uniprot.org/uniprot/E0CZ78|||http://purl.uniprot.org/uniprot/G3X8U7|||http://purl.uniprot.org/uniprot/P48453 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Autoinhibitory domain|||Autoinhibitory segment|||Calcineurin B binding|||Calmodulin-binding|||Catalytic|||Disordered|||In isoform 1.|||N-acetylalanine|||Phosphoserine|||Proton donor|||Removed|||SAPNY motif|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform ^@ http://purl.uniprot.org/annotation/PRO_0000058826|||http://purl.uniprot.org/annotation/VSP_011856 http://togogenome.org/gene/10090:Men1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1I3|||http://purl.uniprot.org/uniprot/O88559 ^@ 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.|||Interaction with FANCD2|||Menin|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096412|||http://purl.uniprot.org/annotation/VSP_041100 http://togogenome.org/gene/10090:Or6c3 ^@ http://purl.uniprot.org/uniprot/Q8VFI0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp941 ^@ http://purl.uniprot.org/uniprot/Q6NV92|||http://purl.uniprot.org/uniprot/Q6NZP7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Gbf1 ^@ http://purl.uniprot.org/uniprot/Q6DFZ1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||SEC7 ^@ http://togogenome.org/gene/10090:Tafa2 ^@ http://purl.uniprot.org/uniprot/Q7TPG7 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Chemokine-like protein TAFA-2 ^@ http://purl.uniprot.org/annotation/PRO_0000042724 http://togogenome.org/gene/10090:Asph ^@ http://purl.uniprot.org/uniprot/A2AL74|||http://purl.uniprot.org/uniprot/A2AL75|||http://purl.uniprot.org/uniprot/A2AL76|||http://purl.uniprot.org/uniprot/A2AL78|||http://purl.uniprot.org/uniprot/A2AL81|||http://purl.uniprot.org/uniprot/A2AL85|||http://purl.uniprot.org/uniprot/Q3TU40|||http://purl.uniprot.org/uniprot/Q8BQK0|||http://purl.uniprot.org/uniprot/Q8BSY0|||http://purl.uniprot.org/uniprot/Q8CBM2|||http://purl.uniprot.org/uniprot/Q9CR06|||http://purl.uniprot.org/uniprot/Q9D7J8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Aspartyl beta-hydroxylase/Triadin|||Aspartyl/asparaginy/proline hydroxylase|||Aspartyl/asparaginyl beta-hydroxylase|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5 ^@ http://purl.uniprot.org/annotation/PRO_0000254161|||http://purl.uniprot.org/annotation/PRO_5015099082|||http://purl.uniprot.org/annotation/VSP_056792|||http://purl.uniprot.org/annotation/VSP_056793|||http://purl.uniprot.org/annotation/VSP_056794|||http://purl.uniprot.org/annotation/VSP_060973|||http://purl.uniprot.org/annotation/VSP_060974|||http://purl.uniprot.org/annotation/VSP_060975 http://togogenome.org/gene/10090:Gap43 ^@ http://purl.uniprot.org/uniprot/P06837 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region ^@ Basic and acidic residues|||Disordered|||IQ|||Loss of palmitoylation; when associated with S-3.|||Loss of palmitoylation; when associated with S-4.|||Neuromodulin|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by PHK|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000159597 http://togogenome.org/gene/10090:Caly ^@ http://purl.uniprot.org/uniprot/Q9DCA7 ^@ 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|||Neuron-specific vesicular protein calcyon ^@ http://purl.uniprot.org/annotation/PRO_0000164369 http://togogenome.org/gene/10090:Tmem87b ^@ http://purl.uniprot.org/uniprot/Q8BKU8 ^@ 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|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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|||Transmembrane protein 87B ^@ http://purl.uniprot.org/annotation/PRO_0000291754|||http://purl.uniprot.org/annotation/VSP_026220|||http://purl.uniprot.org/annotation/VSP_026221 http://togogenome.org/gene/10090:Vmn2r23 ^@ http://purl.uniprot.org/uniprot/E9PXI5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003243013 http://togogenome.org/gene/10090:Atp5md ^@ http://purl.uniprot.org/uniprot/Q78IK2 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ ATP synthase membrane subunit K, mitochondrial|||Helical|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000231579 http://togogenome.org/gene/10090:Kcnj12 ^@ http://purl.uniprot.org/uniprot/B1ATI1|||http://purl.uniprot.org/uniprot/P52187|||http://purl.uniprot.org/uniprot/Q9D3L6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ ATP-sensitive inward rectifier potassium channel 12|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Interaction with phosphatidylinositides|||Interchain|||Inward rectifier potassium channel C-terminal|||PDZ-binding|||Polar residues|||Pore-forming|||Potassium channel inwardly rectifying Kir N-terminal|||Potassium channel inwardly rectifying transmembrane|||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_0000154963 http://togogenome.org/gene/10090:Zfp112 ^@ http://purl.uniprot.org/uniprot/Q0VAW7 ^@ 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 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.|||KRAB|||Zinc finger protein 112 ^@ http://purl.uniprot.org/annotation/PRO_0000351148|||http://purl.uniprot.org/annotation/VSP_052946 http://togogenome.org/gene/10090:Fam219a ^@ http://purl.uniprot.org/uniprot/A2ANP1|||http://purl.uniprot.org/uniprot/Q9D772 ^@ 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|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM219A ^@ http://purl.uniprot.org/annotation/PRO_0000089678 http://togogenome.org/gene/10090:Prim2 ^@ http://purl.uniprot.org/uniprot/P33610 ^@ 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 ^@ DNA primase large subunit|||Disordered|||Interacts with PRIM1|||Interdomain linker|||Phosphothreonine|||Polar residues|||RNA:DNA duplex binding ^@ http://purl.uniprot.org/annotation/PRO_0000046769 http://togogenome.org/gene/10090:Trak1 ^@ http://purl.uniprot.org/uniprot/Q6PD31 ^@ Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||HAP1 N-terminal|||In isoform 2.|||Interaction with HGS|||Interaction with OGT|||O-linked (GlcNAc) serine|||Phosphoserine|||Trafficking kinesin-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000394506|||http://purl.uniprot.org/annotation/VSP_039277|||http://purl.uniprot.org/annotation/VSP_039278|||http://purl.uniprot.org/annotation/VSP_039279 http://togogenome.org/gene/10090:Ccdc159 ^@ http://purl.uniprot.org/uniprot/Q8C963 ^@ 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 159|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000332997|||http://purl.uniprot.org/annotation/VSP_033427|||http://purl.uniprot.org/annotation/VSP_033428|||http://purl.uniprot.org/annotation/VSP_033429 http://togogenome.org/gene/10090:Hr ^@ http://purl.uniprot.org/uniprot/Q61645 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C6-type|||Disordered|||JmjC|||LXXLL motif 1|||LXXLL motif 2|||Lysine-specific demethylase hairless|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000083891 http://togogenome.org/gene/10090:Rtl3 ^@ http://purl.uniprot.org/uniprot/Q6P1Y1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Zinc Finger ^@ Basic and acidic residues|||CCHC-type|||Disordered|||Polar residues|||Retrotransposon Gag-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000440243 http://togogenome.org/gene/10090:Mageb4 ^@ http://purl.uniprot.org/uniprot/A2A9R3 ^@ 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|||10|||11|||12|||13|||14|||15|||15 X 15 AA approximate tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||MAGE|||Melanoma-associated antigen B4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000437174 http://togogenome.org/gene/10090:Sart3 ^@ http://purl.uniprot.org/uniprot/Q9JLI8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||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|||HAT 8|||HAT 9|||In isoform 2.|||Mediates interaction with PRPF3|||N-acetylalanine|||Necessary and sufficient for U6 snRNA binding|||Omega-N-methylarginine|||Phosphoserine|||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_0000223314|||http://purl.uniprot.org/annotation/VSP_017252|||http://purl.uniprot.org/annotation/VSP_017253 http://togogenome.org/gene/10090:A130010J15Rik ^@ http://purl.uniprot.org/uniprot/Q9DAE8 ^@ Chain|||Molecule Processing ^@ Chain ^@ UPF0739 protein C1orf74 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000271093 http://togogenome.org/gene/10090:Slc25a34 ^@ http://purl.uniprot.org/uniprot/A2ADF7 ^@ 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.|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 34 ^@ http://purl.uniprot.org/annotation/PRO_0000291790|||http://purl.uniprot.org/annotation/VSP_026235|||http://purl.uniprot.org/annotation/VSP_026236 http://togogenome.org/gene/10090:Mtrf1l ^@ http://purl.uniprot.org/uniprot/Q8BJU9 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Transit Peptide ^@ Chain|||Coiled-Coil|||Modified Residue|||Motif|||Region|||Transit Peptide ^@ GGQ|||GGQ domain|||Mitochondrion|||N5-methylglutamine|||Peptide chain release factor 1-like, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000330945 http://togogenome.org/gene/10090:Taok3 ^@ http://purl.uniprot.org/uniprot/B2RY27|||http://purl.uniprot.org/uniprot/Q8BYC6 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase TAO3 ^@ http://purl.uniprot.org/annotation/PRO_0000086738 http://togogenome.org/gene/10090:Klrk1 ^@ http://purl.uniprot.org/uniprot/O54709|||http://purl.uniprot.org/uniprot/Q3TCW7|||http://purl.uniprot.org/uniprot/Q4FJM0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||NKG2-D type II integral membrane protein ^@ http://purl.uniprot.org/annotation/PRO_0000046668|||http://purl.uniprot.org/annotation/VSP_053945 http://togogenome.org/gene/10090:Cttnbp2nl ^@ http://purl.uniprot.org/uniprot/Q99LJ0 ^@ 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 ^@ CTTNBP2 N-terminal-like protein|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000226998 http://togogenome.org/gene/10090:Cpt1b ^@ http://purl.uniprot.org/uniprot/Q924X2 ^@ 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 ^@ Carnitine O-palmitoyltransferase 1, muscle isoform|||Cytoplasmic|||Helical|||Mitochondrial intermembrane|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000210163 http://togogenome.org/gene/10090:Slc7a2 ^@ http://purl.uniprot.org/uniprot/P18581 ^@ 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 ^@ Cationic amino acid transporter 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000054265|||http://purl.uniprot.org/annotation/VSP_000025 http://togogenome.org/gene/10090:Trim44 ^@ http://purl.uniprot.org/uniprot/Q4KMS1|||http://purl.uniprot.org/uniprot/Q9QXA7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||B box-type|||Basic and acidic residues|||Disordered|||Phosphoserine|||Tripartite motif-containing protein 44 ^@ http://purl.uniprot.org/annotation/PRO_0000220373 http://togogenome.org/gene/10090:Hhex ^@ http://purl.uniprot.org/uniprot/P43120 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Hematopoietically-expressed homeobox protein Hhex|||Homeobox|||Interaction with SOX13|||Phosphoserine|||Polar residues|||Required for WNT signaling induction ^@ http://purl.uniprot.org/annotation/PRO_0000049075 http://togogenome.org/gene/10090:Fkrp ^@ http://purl.uniprot.org/uniprot/Q8CG64 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CDP-L-ribitol|||Cytoplasmic|||Does not alter dystroglycan processing in vitro.|||Helical|||Interchain|||Localized to the perinuclear region but not retained in or targeted to the medial part of the Golgi apparatus.|||Localizes mainly to the ER compartment.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Not properly targeted to the Golgi apparatus; strongly reduced secretion to the medium; localizes mainly to the ER compartment. Strongly impaired glycosylation of alpha-dystroglycan in muscles and brain.|||Reduced secretion to the medium.|||Reduced secretion to the medium; localizes mainly to the Golgi apparatus. Mild dystrophy with reduced alpha-dystroglycan glycosylation and no apparent brain defects.|||Ribitol 5-phosphate transferase FKRP|||Zinc finger loop ^@ http://purl.uniprot.org/annotation/PRO_0000204724 http://togogenome.org/gene/10090:COX2 ^@ http://purl.uniprot.org/uniprot/P00405|||http://purl.uniprot.org/uniprot/Q7JCZ1 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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|||Mitochondrial intermembrane|||Mitochondrial matrix|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000183635 http://togogenome.org/gene/10090:H2ab2 ^@ http://purl.uniprot.org/uniprot/S4R1M3 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Dzip1l ^@ http://purl.uniprot.org/uniprot/B2RR42|||http://purl.uniprot.org/uniprot/Q499E4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C2H2-type|||Cilium assembly protein DZIP1L|||Disordered|||In isoform 2.|||In wpy; widespread embryonic dysmorphologies, including highly penetrant polydactyly of all four limbs as well as craniofacial defects. Mice develop cystic kidney disease.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000331307|||http://purl.uniprot.org/annotation/VSP_033160 http://togogenome.org/gene/10090:Pde6d ^@ http://purl.uniprot.org/uniprot/O55057|||http://purl.uniprot.org/uniprot/Q3TDQ8 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Region|||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_0000221209 http://togogenome.org/gene/10090:Psd2 ^@ http://purl.uniprot.org/uniprot/Q6P1I6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||PH|||PH and SEC7 domain-containing protein 2|||Phosphoserine|||Polar residues|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000334163|||http://purl.uniprot.org/annotation/VSP_033639|||http://purl.uniprot.org/annotation/VSP_033640 http://togogenome.org/gene/10090:Rxfp3 ^@ http://purl.uniprot.org/uniprot/Q5Y988|||http://purl.uniprot.org/uniprot/Q8BGE9 ^@ 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|||Relaxin-3 receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000070105 http://togogenome.org/gene/10090:Txnl4a ^@ http://purl.uniprot.org/uniprot/P83877|||http://purl.uniprot.org/uniprot/Q9CQX6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N-acetyltransferase|||Phosphoserine|||Polar residues|||Thioredoxin-like protein 4A ^@ http://purl.uniprot.org/annotation/PRO_0000218288 http://togogenome.org/gene/10090:Or14a260 ^@ http://purl.uniprot.org/uniprot/Q8VFN8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pcdha12 ^@ http://purl.uniprot.org/uniprot/Q91Y18 ^@ 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|||Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099543 http://togogenome.org/gene/10090:Hoxb8 ^@ http://purl.uniprot.org/uniprot/A2A9Z8|||http://purl.uniprot.org/uniprot/P09632 ^@ 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_0000200149 http://togogenome.org/gene/10090:Igsf21 ^@ http://purl.uniprot.org/uniprot/Q7TNR6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Ig-like 1|||Ig-like 2|||Immunoglobulin superfamily member 21|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000223339 http://togogenome.org/gene/10090:Ccl26 ^@ http://purl.uniprot.org/uniprot/F8VQM2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_5003385261 http://togogenome.org/gene/10090:Mfng ^@ http://purl.uniprot.org/uniprot/O09008|||http://purl.uniprot.org/uniprot/Q3UPI0 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Beta-1,3-N-acetylglucosaminyltransferase manic fringe|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219183 http://togogenome.org/gene/10090:Cul2 ^@ http://purl.uniprot.org/uniprot/Q9D4H8 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Cullin-2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||In isoform 2.|||N6-acetyllysine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000119791|||http://purl.uniprot.org/annotation/VSP_008823 http://togogenome.org/gene/10090:Wipi2 ^@ http://purl.uniprot.org/uniprot/Q80W47 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Modified Residue|||Motif|||Repeat ^@ L/FRRG motif|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD repeat domain phosphoinositide-interacting protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000051441 http://togogenome.org/gene/10090:Cdkn2aipnl ^@ http://purl.uniprot.org/uniprot/Q9D211 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ CDKN2AIP N-terminal-like protein|||N-acetylmethionine|||XRN2-binding (XTBD) ^@ http://purl.uniprot.org/annotation/PRO_0000325927 http://togogenome.org/gene/10090:Fkbp11 ^@ http://purl.uniprot.org/uniprot/Q9D1M7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Helical|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP11 ^@ http://purl.uniprot.org/annotation/PRO_0000025520 http://togogenome.org/gene/10090:Pcsk4 ^@ http://purl.uniprot.org/uniprot/P29121 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||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.|||N-linked (GlcNAc...) asparagine|||P/Homo B|||Peptidase S8|||Proprotein convertase subtilisin/kexin type 4 ^@ http://purl.uniprot.org/annotation/PRO_0000027098|||http://purl.uniprot.org/annotation/PRO_0000027099|||http://purl.uniprot.org/annotation/VSP_011266|||http://purl.uniprot.org/annotation/VSP_011267|||http://purl.uniprot.org/annotation/VSP_011268|||http://purl.uniprot.org/annotation/VSP_011269|||http://purl.uniprot.org/annotation/VSP_011270|||http://purl.uniprot.org/annotation/VSP_011271|||http://purl.uniprot.org/annotation/VSP_011272 http://togogenome.org/gene/10090:Mosmo ^@ http://purl.uniprot.org/uniprot/Q8C784 ^@ 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_0000271083|||http://purl.uniprot.org/annotation/VSP_022277 http://togogenome.org/gene/10090:Cdh8 ^@ http://purl.uniprot.org/uniprot/E9PYB2|||http://purl.uniprot.org/uniprot/E9Q451|||http://purl.uniprot.org/uniprot/P97291|||http://purl.uniprot.org/uniprot/Q3UTL9|||http://purl.uniprot.org/uniprot/Q8BRK4|||http://purl.uniprot.org/uniprot/Q8C449 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin domain-containing protein|||Cadherin-8|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000003775|||http://purl.uniprot.org/annotation/PRO_0000003776|||http://purl.uniprot.org/annotation/PRO_5004304230 http://togogenome.org/gene/10090:Nhp2 ^@ http://purl.uniprot.org/uniprot/Q9CRB2 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Crosslink|||Modified Residue ^@ 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|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000136765 http://togogenome.org/gene/10090:Card11 ^@ http://purl.uniprot.org/uniprot/Q8CIS0 ^@ 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|||Splice Variant|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn ^@ CARD|||Caspase recruitment domain-containing protein 11|||Decreased interaction with BCL10.|||Disordered|||Guanylate kinase-like|||In isoform 2.|||Inhibitory domain (ID)|||Interchain|||Linker|||PDZ|||Phosphoserine|||Phosphoserine; by PKC/PRKCB and PKC/PRKCQ|||Polar residues|||Slightly decreased interaction with BCL10.|||Strongly decreased interaction with BCL10. ^@ http://purl.uniprot.org/annotation/PRO_0000320102|||http://purl.uniprot.org/annotation/VSP_031595 http://togogenome.org/gene/10090:Spdye4a ^@ http://purl.uniprot.org/uniprot/A0A0G2JEI8|||http://purl.uniprot.org/uniprot/B9EIX3|||http://purl.uniprot.org/uniprot/Q5IBH6|||http://purl.uniprot.org/uniprot/Q9D5G0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Speedy protein E4A|||Speedy/Ringo box; Required for CDK-binding ^@ http://purl.uniprot.org/annotation/PRO_0000234115 http://togogenome.org/gene/10090:Aox3 ^@ http://purl.uniprot.org/uniprot/G3X982|||http://purl.uniprot.org/uniprot/Q8C6Q4|||http://purl.uniprot.org/uniprot/Q9CW59 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Strand|||Turn ^@ 2Fe-2S ferredoxin-type|||Aldehyde oxidase 3|||Aldehyde oxidase/xanthine dehydrogenase a/b hammerhead|||CO dehydrogenase flavoprotein C-terminal|||FAD-binding PCMH-type|||Loss of activity with different N-heterocyclic compounds as substrates. 60% reduction of activity with benzaldehyde.|||No effect on kinetic constants with smaller substrates like benzaldehyde or phthalazine. Decreases substrate affinity and slightly increases catalytic efficiency for bulkier substrates like phenanthridine.|||No effect on substrate affinity but decreases catalytic efficiency for smaller substrates like benzaldehyde or phthalazine. Increases substrate affinity and activity for bulkier substrates like phenanthridine.|||Phosphoserine|||Proton acceptor|||Proton acceptor; for azaheterocycle hydroxylase activity|||Slightly decreases substrate affinity but no effect on activity with smaller substrates like benzaldehyde or phthalazine. Increases catalytic efficiency with bulkier substrates like phenanthridine or more charged substrates like N1-methylnicotinamide. ^@ http://purl.uniprot.org/annotation/PRO_0000425247 http://togogenome.org/gene/10090:Pik3r2 ^@ http://purl.uniprot.org/uniprot/O08908 ^@ 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|||Phosphatidylinositol 3-kinase regulatory subunit beta|||Phosphotyrosine|||Rho-GAP|||SH2 1|||SH2 2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000080764 http://togogenome.org/gene/10090:Adam8 ^@ http://purl.uniprot.org/uniprot/Q05910|||http://purl.uniprot.org/uniprot/Q3U1J7|||http://purl.uniprot.org/uniprot/Q3U7G2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 8|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000029061|||http://purl.uniprot.org/annotation/PRO_5010843354|||http://purl.uniprot.org/annotation/PRO_5015097473 http://togogenome.org/gene/10090:Hspa2 ^@ http://purl.uniprot.org/uniprot/P17156 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ 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_0000078259 http://togogenome.org/gene/10090:Bpifa1 ^@ http://purl.uniprot.org/uniprot/P97361 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Repeat|||Signal Peptide|||Strand ^@ 4 X 6 AA repeats of G-[LPQ]-[PL]-L-P-L|||BPI fold-containing family A member 1|||Important for surfactant activity and antibacterial properties|||N-linked (GlcNAc...) asparagine|||Repeat 1|||Repeat 2|||Repeat 3|||Repeat 4 ^@ http://purl.uniprot.org/annotation/PRO_0000017176 http://togogenome.org/gene/10090:Erc2 ^@ http://purl.uniprot.org/uniprot/Q3UHT7|||http://purl.uniprot.org/uniprot/Q6PH08 ^@ 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 residues|||Disordered|||ERC protein 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087003|||http://purl.uniprot.org/annotation/VSP_011466|||http://purl.uniprot.org/annotation/VSP_011467|||http://purl.uniprot.org/annotation/VSP_011468|||http://purl.uniprot.org/annotation/VSP_011469|||http://purl.uniprot.org/annotation/VSP_011470|||http://purl.uniprot.org/annotation/VSP_011471|||http://purl.uniprot.org/annotation/VSP_012306 http://togogenome.org/gene/10090:Tgif2lx2 ^@ http://purl.uniprot.org/uniprot/Q8K5B9 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Pelp1 ^@ http://purl.uniprot.org/uniprot/A0A158SIT8|||http://purl.uniprot.org/uniprot/Q9DBD5 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||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|||PELP1 middle|||Phosphoserine|||Phosphothreonine|||Polar residues|||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_0000252137 http://togogenome.org/gene/10090:Tob1 ^@ http://purl.uniprot.org/uniprot/Q61471 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Bipartite nuclear localization signal|||Disordered|||Important for nuclear localization|||Localizes to cytoplasm; when associated with 22-QQQ-24.|||Localizes to cytoplasm; when associated with 37-NNN-39.|||Not exported to the cytoplasm; when associated with A-234.|||Not exported to the cytoplasm; when associated with A-236.|||Nuclear export signal|||Phosphothreonine|||Polar residues|||Protein Tob1|||Required for interaction with CPEB3 ^@ http://purl.uniprot.org/annotation/PRO_0000143813 http://togogenome.org/gene/10090:Cdh9 ^@ http://purl.uniprot.org/uniprot/F8WHU6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015091378 http://togogenome.org/gene/10090:Il19 ^@ http://purl.uniprot.org/uniprot/Q14BK1|||http://purl.uniprot.org/uniprot/Q8CJ70 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Transmembrane ^@ Helical|||Interleukin-19|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015380 http://togogenome.org/gene/10090:Nat10 ^@ http://purl.uniprot.org/uniprot/Q8K224 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||N-acetyltransferase|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||RNA cytidine acetyltransferase|||Required for localization to the nucleolus and midbody ^@ http://purl.uniprot.org/annotation/PRO_0000327480 http://togogenome.org/gene/10090:Krt81 ^@ http://purl.uniprot.org/uniprot/Q9ERE2 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Region ^@ Coil 1A|||Coil 1B|||Coil 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Head|||IF rod|||Keratin, type II cuticular Hb1|||Linker 1|||Linker 12|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000361690 http://togogenome.org/gene/10090:Gata3 ^@ http://purl.uniprot.org/uniprot/P23772|||http://purl.uniprot.org/uniprot/Q3U0R5 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn|||Zinc Finger ^@ Disordered|||Dramatically decreased Th2 cell differentiation.|||Fails to induce Th2 cytokine production.|||Flexible linker|||GATA-type|||GATA-type 1|||GATA-type 2|||Interaction with TBX21|||Moderately decreased Th2 cell differentiation.|||Phosphoserine|||Trans-acting T-cell-specific transcription factor GATA-3|||YxKxHxxxRP ^@ http://purl.uniprot.org/annotation/PRO_0000083409 http://togogenome.org/gene/10090:Ifitm5 ^@ http://purl.uniprot.org/uniprot/O88728 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Abolishes expression at the cell membrane.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interferon-induced transmembrane protein 5|||No effect on location at the cell membrane. Abolishes palmitoylation; when associated with A-52 and A-53.|||S-palmitoyl cysteine|||Strongly reduces expression at the cell membrane. Reduces palmitoylation; when associated with A-52. Abolishes palmitoylation; when associated with A-52 and A-86.|||Strongly reduces expression at the cell membrane. Reduces palmitoylation; when associated with A-53. Abolishes palmitoylation; when associated with A-53 and A-86. ^@ http://purl.uniprot.org/annotation/PRO_0000397676 http://togogenome.org/gene/10090:Get3 ^@ http://purl.uniprot.org/uniprot/O54984 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ ATPase GET3|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000152254 http://togogenome.org/gene/10090:Rhag ^@ http://purl.uniprot.org/uniprot/A0A3B2WBH6|||http://purl.uniprot.org/uniprot/Q9QUT0 ^@ 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 ^@ Ammonium transporter AmtB-like|||Ammonium transporter Rh type A|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000380190 http://togogenome.org/gene/10090:Tapt1 ^@ http://purl.uniprot.org/uniprot/Q4VBD2 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Transmembrane anterior posterior transformation protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000328873 http://togogenome.org/gene/10090:Mcts2 ^@ http://purl.uniprot.org/uniprot/Q9CQ21 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Malignant T-cell-amplified sequence 2|||PUA ^@ http://purl.uniprot.org/annotation/PRO_0000344788 http://togogenome.org/gene/10090:Or4f54 ^@ http://purl.uniprot.org/uniprot/Q8VF39 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gm5862 ^@ http://purl.uniprot.org/uniprot/K7N5V5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ppp2r3c ^@ http://purl.uniprot.org/uniprot/Q9JK24 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ EF-hand 1|||EF-hand 2|||Serine/threonine-protein phosphatase 2A regulatory subunit B" subunit gamma ^@ http://purl.uniprot.org/annotation/PRO_0000277834 http://togogenome.org/gene/10090:Ddb1 ^@ http://purl.uniprot.org/uniprot/Q3U1J4 ^@ Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ DNA damage-binding protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with CDT1|||Interaction with CDT1 and CUL4A|||N-acetylserine|||N6-acetyllysine|||Phosphothreonine|||Removed|||WD repeat beta-propeller A|||WD repeat beta-propeller B; Interaction with CUL4A|||WD repeat beta-propeller C ^@ http://purl.uniprot.org/annotation/PRO_0000281036 http://togogenome.org/gene/10090:Nuak1 ^@ http://purl.uniprot.org/uniprot/Q641K5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Disordered|||GILK motif|||N-acetylmethionine|||NUAK family SNF1-like kinase 1|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphothreonine; by LKB1|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086454 http://togogenome.org/gene/10090:Wac ^@ http://purl.uniprot.org/uniprot/Q924H7 ^@ 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.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WW|||WW domain-containing adapter protein with coiled-coil ^@ http://purl.uniprot.org/annotation/PRO_0000254559|||http://purl.uniprot.org/annotation/VSP_021237|||http://purl.uniprot.org/annotation/VSP_021238 http://togogenome.org/gene/10090:Xlr3a ^@ http://purl.uniprot.org/uniprot/Q60595|||http://purl.uniprot.org/uniprot/Q78PE0|||http://purl.uniprot.org/uniprot/Q99L59 ^@ 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|||Polar residues|||X-linked lymphocyte-regulated protein 3A|||XLR/SYCP3/FAM9 ^@ http://purl.uniprot.org/annotation/PRO_0000223041 http://togogenome.org/gene/10090:Dnajc16 ^@ http://purl.uniprot.org/uniprot/Q80TN4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||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|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||DnaJ homolog subfamily C member 16|||Extracellular|||Helical; Anchor for type IV membrane protein|||In strain: Czech II.|||J|||N-linked (GlcNAc...) asparagine|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000236684 http://togogenome.org/gene/10090:Cblif ^@ http://purl.uniprot.org/uniprot/P52787 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Cobalamin binding intrinsic factor|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000005559 http://togogenome.org/gene/10090:Edar ^@ http://purl.uniprot.org/uniprot/Q9R187 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Death|||Disordered|||Extracellular|||Helical|||In recessive downless Jackson.|||N-linked (GlcNAc...) asparagine|||Polar residues|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member EDAR ^@ http://purl.uniprot.org/annotation/PRO_0000034609 http://togogenome.org/gene/10090:Vps35l ^@ http://purl.uniprot.org/uniprot/I1E4X5|||http://purl.uniprot.org/uniprot/Q8BWQ6 ^@ 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.|||Phosphoserine|||Polar residues|||VPS35 endosomal protein-sorting factor-like ^@ http://purl.uniprot.org/annotation/PRO_0000311353|||http://purl.uniprot.org/annotation/VSP_029539|||http://purl.uniprot.org/annotation/VSP_029540|||http://purl.uniprot.org/annotation/VSP_029541|||http://purl.uniprot.org/annotation/VSP_029542 http://togogenome.org/gene/10090:AI597479 ^@ http://purl.uniprot.org/uniprot/Q922M7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Ashwin|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000268860 http://togogenome.org/gene/10090:Cobl ^@ http://purl.uniprot.org/uniprot/G3UWY3|||http://purl.uniprot.org/uniprot/G5E8P4|||http://purl.uniprot.org/uniprot/Q5NBX1 ^@ 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|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||KKRRAP 1|||KKRRAP 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein cordon-bleu|||WH2|||WH2 1|||WH2 2|||WH2 3 ^@ http://purl.uniprot.org/annotation/PRO_0000260492|||http://purl.uniprot.org/annotation/VSP_021614|||http://purl.uniprot.org/annotation/VSP_021615|||http://purl.uniprot.org/annotation/VSP_021616|||http://purl.uniprot.org/annotation/VSP_021617|||http://purl.uniprot.org/annotation/VSP_021618|||http://purl.uniprot.org/annotation/VSP_021619|||http://purl.uniprot.org/annotation/VSP_021620 http://togogenome.org/gene/10090:Nectin2 ^@ http://purl.uniprot.org/uniprot/P32507|||http://purl.uniprot.org/uniprot/Q80XJ5|||http://purl.uniprot.org/uniprot/Q8C6F2 ^@ Chain|||Compositionally Biased Region|||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|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||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|||Ig-like domain-containing protein|||In isoform Alpha.|||N-linked (GlcNAc...) asparagine|||Nectin-2|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000015137|||http://purl.uniprot.org/annotation/PRO_5004297600|||http://purl.uniprot.org/annotation/PRO_5004307329|||http://purl.uniprot.org/annotation/VSP_002630|||http://purl.uniprot.org/annotation/VSP_002631 http://togogenome.org/gene/10090:Hlf ^@ http://purl.uniprot.org/uniprot/Q8BW74 ^@ 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 motif|||Disordered|||Hepatic leukemia factor|||Leucine-zipper|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076511 http://togogenome.org/gene/10090:Fbln7 ^@ http://purl.uniprot.org/uniprot/Q501P1 ^@ 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 ^@ EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||Fibulin-7|||N-linked (GlcNAc...) asparagine|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_0000313656 http://togogenome.org/gene/10090:Krt27 ^@ http://purl.uniprot.org/uniprot/Q9Z320 ^@ 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|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In Rex wavy coat; mice exhibit curly hair and vibrissae. The diameter of the hair shaft is irregular due to morphological abnormalities in all three layers of the irs.|||Keratin, type I cytoskeletal 27|||Linker 1|||Linker 12|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000312702 http://togogenome.org/gene/10090:2810408A11Rik ^@ http://purl.uniprot.org/uniprot/B1AR39|||http://purl.uniprot.org/uniprot/B1AR42|||http://purl.uniprot.org/uniprot/Q6NSU2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Pcdhgc4 ^@ http://purl.uniprot.org/uniprot/Q91XX0 ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Mafa ^@ http://purl.uniprot.org/uniprot/Q8CF90 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ Basic motif|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Leucine-zipper|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription factor MafA|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000320275 http://togogenome.org/gene/10090:Lmod3 ^@ http://purl.uniprot.org/uniprot/E9QA62 ^@ 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|||Leiomodin-3|||Polar residues|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000439646 http://togogenome.org/gene/10090:Oxct1 ^@ http://purl.uniprot.org/uniprot/Q9D0K2 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ 5-glutamyl coenzyme A thioester intermediate|||Mitochondrion|||N6-succinyllysine|||Phosphoserine|||Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000002414 http://togogenome.org/gene/10090:Chaf1a ^@ http://purl.uniprot.org/uniprot/Q9QWF0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Acidic residues|||Basic and acidic residues|||Binds CBX1 and CBX3 chromo shadow domains|||Binds PCNA|||Binds to p60|||Chromatin assembly factor 1 subunit A|||Disordered|||Necessary for homodimerization and competence for chromatin assembly|||Phosphoserine|||Phosphothreonine|||Polar residues|||Prevents binding to CBX1 and CBX5.|||PxVxL motif ^@ http://purl.uniprot.org/annotation/PRO_0000089277 http://togogenome.org/gene/10090:Zfp704 ^@ http://purl.uniprot.org/uniprot/Q9ERQ3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||C2H2-type|||CR1|||CR2|||Disordered|||Fails to bind to RE2 sequence motifs.|||Phosphoserine|||Polar residues|||Pro residues|||Sufficient for binding to RE2 sequence motifs|||Zinc finger protein 704 ^@ http://purl.uniprot.org/annotation/PRO_0000288825 http://togogenome.org/gene/10090:Rplp1 ^@ http://purl.uniprot.org/uniprot/P47955|||http://purl.uniprot.org/uniprot/Q58E35 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Large ribosomal subunit protein P1|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000157687 http://togogenome.org/gene/10090:Klhl20 ^@ http://purl.uniprot.org/uniprot/Q8VCK5 ^@ 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 20 ^@ http://purl.uniprot.org/annotation/PRO_0000119124 http://togogenome.org/gene/10090:Fyttd1 ^@ http://purl.uniprot.org/uniprot/Q91Z49 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Modified Residue|||Motif|||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 SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||UAP56-binding motif|||UAP56-interacting factor ^@ http://purl.uniprot.org/annotation/PRO_0000287442|||http://purl.uniprot.org/annotation/VSP_025462|||http://purl.uniprot.org/annotation/VSP_025463|||http://purl.uniprot.org/annotation/VSP_025464 http://togogenome.org/gene/10090:Slc38a11 ^@ http://purl.uniprot.org/uniprot/Q3USY0 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Putative sodium-coupled neutral amino acid transporter 11 ^@ http://purl.uniprot.org/annotation/PRO_0000326061|||http://purl.uniprot.org/annotation/VSP_032530|||http://purl.uniprot.org/annotation/VSP_032531 http://togogenome.org/gene/10090:Soat1 ^@ http://purl.uniprot.org/uniprot/Q61263 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||Lumenal|||Phosphoserine|||Sterol O-acyltransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000207642 http://togogenome.org/gene/10090:Sgo1 ^@ http://purl.uniprot.org/uniprot/Q9CXH7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||D-box|||Disordered|||In isoform 2.|||Necessary for interaction with PPP2CA and PPP2R1A|||PXVXL/I motif|||Phosphoserine|||Phosphoserine; by NEK2|||Polar residues|||Shugoshin 1 ^@ http://purl.uniprot.org/annotation/PRO_0000055437|||http://purl.uniprot.org/annotation/VSP_016796|||http://purl.uniprot.org/annotation/VSP_016797 http://togogenome.org/gene/10090:Prodh2 ^@ http://purl.uniprot.org/uniprot/Q8VCZ9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Hydroxyproline dehydrogenase|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000308624 http://togogenome.org/gene/10090:Smtnl2 ^@ http://purl.uniprot.org/uniprot/Q8CI12 ^@ 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 ^@ Calponin-homology (CH)|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Smoothelin-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000317279 http://togogenome.org/gene/10090:Or8g50 ^@ http://purl.uniprot.org/uniprot/Q60895 ^@ 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 8G50 ^@ http://purl.uniprot.org/annotation/PRO_0000150827 http://togogenome.org/gene/10090:Decr1 ^@ http://purl.uniprot.org/uniprot/Q9CQ62 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphothreonine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000031966 http://togogenome.org/gene/10090:Pik3r4 ^@ http://purl.uniprot.org/uniprot/Q8VD65 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||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_0000086525 http://togogenome.org/gene/10090:Hmgn3 ^@ http://purl.uniprot.org/uniprot/Q9DCB1 ^@ 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.|||In isoform 3.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000232575|||http://purl.uniprot.org/annotation/VSP_017909|||http://purl.uniprot.org/annotation/VSP_017910|||http://purl.uniprot.org/annotation/VSP_017911|||http://purl.uniprot.org/annotation/VSP_017912 http://togogenome.org/gene/10090:Rnf170 ^@ http://purl.uniprot.org/uniprot/Q8CBG9 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||E3 ubiquitin-protein ligase RNF170|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of E3 ligase activity.|||Lumenal|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000280701|||http://purl.uniprot.org/annotation/VSP_023858|||http://purl.uniprot.org/annotation/VSP_023859|||http://purl.uniprot.org/annotation/VSP_023860|||http://purl.uniprot.org/annotation/VSP_023861|||http://purl.uniprot.org/annotation/VSP_023862|||http://purl.uniprot.org/annotation/VSP_023863|||http://purl.uniprot.org/annotation/VSP_023864 http://togogenome.org/gene/10090:Zc3hc1 ^@ http://purl.uniprot.org/uniprot/Q80YV2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C3HC-type|||Disordered|||F-box-like|||In isoform 2.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Zinc finger C3HC-type protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000096850|||http://purl.uniprot.org/annotation/VSP_015219 http://togogenome.org/gene/10090:Gdf11 ^@ http://purl.uniprot.org/uniprot/Q9Z1W4 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage|||Cleavage; by FURIN|||Growth/differentiation factor 11|||Inhibits processing of prodomain.|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033988|||http://purl.uniprot.org/annotation/PRO_0000033989 http://togogenome.org/gene/10090:Col23a1 ^@ http://purl.uniprot.org/uniprot/Q8K4G2 ^@ 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 ^@ Basic and acidic residues|||Collagen alpha-1(XXIII) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000245227 http://togogenome.org/gene/10090:Iyd ^@ http://purl.uniprot.org/uniprot/Q9DCX8 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Helix|||Mutagenesis Site|||Strand|||Transmembrane|||Turn ^@ Helical|||Iodotyrosine deiodinase 1|||Loss of enzyme activity. ^@ http://purl.uniprot.org/annotation/PRO_0000230279 http://togogenome.org/gene/10090:Lhx9 ^@ http://purl.uniprot.org/uniprot/Q9WUH2 ^@ 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 1 and isoform 2.|||In isoform 2 and isoform 4.|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx9 ^@ http://purl.uniprot.org/annotation/PRO_0000075799|||http://purl.uniprot.org/annotation/VSP_036430|||http://purl.uniprot.org/annotation/VSP_036431 http://togogenome.org/gene/10090:Ndufaf3 ^@ http://purl.uniprot.org/uniprot/Q9JKL4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000281155 http://togogenome.org/gene/10090:Nr4a1 ^@ http://purl.uniprot.org/uniprot/P12813|||http://purl.uniprot.org/uniprot/Q545Q1 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ AF-2|||Binds lipopolysaccharide|||Disordered|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 4 group A member 1|||Phosphoserine; by PKA|||Phosphoserine; by PKA, RPS6KA1 and RPS6KA3|||Polar residues|||Pro residues|||Required for binding NBRE-containing DNA|||Required for nuclear import|||Required for the interaction with RXRA ^@ http://purl.uniprot.org/annotation/PRO_0000053716 http://togogenome.org/gene/10090:Igsf3 ^@ http://purl.uniprot.org/uniprot/A0A0A6YX40|||http://purl.uniprot.org/uniprot/Q6ZQA6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Acidic residues|||Cytoplasmic|||Disordered|||EWI motif|||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|||Immunoglobulin superfamily member 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000320135|||http://purl.uniprot.org/annotation/PRO_5002024356 http://togogenome.org/gene/10090:Snx5 ^@ http://purl.uniprot.org/uniprot/Q9D8U8 ^@ 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|||Region|||Strand|||Turn ^@ BAR|||Interaction with DOCK1|||Membrane-binding amphipathic helix|||N-acetylalanine|||N6-acetyllysine|||PX|||Phosphoserine|||Removed|||Sorting nexin-5 ^@ http://purl.uniprot.org/annotation/PRO_0000213845 http://togogenome.org/gene/10090:Tspoap1 ^@ http://purl.uniprot.org/uniprot/Q7TNF8 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Peripheral-type benzodiazepine receptor-associated protein 1|||Polar residues|||SH3 1|||SH3 2|||SH3 3 ^@ http://purl.uniprot.org/annotation/PRO_0000221381|||http://purl.uniprot.org/annotation/VSP_009206|||http://purl.uniprot.org/annotation/VSP_009207|||http://purl.uniprot.org/annotation/VSP_009208|||http://purl.uniprot.org/annotation/VSP_009209|||http://purl.uniprot.org/annotation/VSP_009210 http://togogenome.org/gene/10090:1700123O20Rik ^@ http://purl.uniprot.org/uniprot/Q9JJ93 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Uncharacterized protein C14orf119 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089930 http://togogenome.org/gene/10090:Acer3 ^@ http://purl.uniprot.org/uniprot/Q9D099 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Alkaline ceramidase 3|||Cytoplasmic|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000212464 http://togogenome.org/gene/10090:Pcp2 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZX8|||http://purl.uniprot.org/uniprot/A8IK50|||http://purl.uniprot.org/uniprot/P12660 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||GoLoco 1|||GoLoco 2|||Phosphoserine|||Polar residues|||Purkinje cell protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000058261 http://togogenome.org/gene/10090:Zzz3 ^@ http://purl.uniprot.org/uniprot/D3YTT9|||http://purl.uniprot.org/uniprot/Q6KAQ7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||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 isoform 2.|||In isoform 3.|||Myb-like|||N6-acetyllysine|||Phosphoserine|||Polar residues|||ZZ-type|||ZZ-type zinc finger-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000287496|||http://purl.uniprot.org/annotation/VSP_025514|||http://purl.uniprot.org/annotation/VSP_025515|||http://purl.uniprot.org/annotation/VSP_025516|||http://purl.uniprot.org/annotation/VSP_025517|||http://purl.uniprot.org/annotation/VSP_025518 http://togogenome.org/gene/10090:Lbp ^@ http://purl.uniprot.org/uniprot/Q61805 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Lipopolysaccharide-binding protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017159 http://togogenome.org/gene/10090:Tekt1 ^@ http://purl.uniprot.org/uniprot/Q5NBU4|||http://purl.uniprot.org/uniprot/Q9DAJ2 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Tektin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000184563 http://togogenome.org/gene/10090:Or12e10 ^@ http://purl.uniprot.org/uniprot/A2AVC7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gng13 ^@ http://purl.uniprot.org/uniprot/Q9JMF3 ^@ 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_0000012673|||http://purl.uniprot.org/annotation/PRO_0000012674 http://togogenome.org/gene/10090:Slc5a7 ^@ http://purl.uniprot.org/uniprot/Q8BGY9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dileucine-like motif|||Extracellular|||Helical|||High affinity choline transporter 1|||Mediates interaction with SEC14L1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000105392 http://togogenome.org/gene/10090:Cnot9 ^@ http://purl.uniprot.org/uniprot/Q9JKY0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ CCR4-NOT transcription complex subunit 9|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000327227 http://togogenome.org/gene/10090:Lgmn ^@ http://purl.uniprot.org/uniprot/A2RTI3|||http://purl.uniprot.org/uniprot/O89017|||http://purl.uniprot.org/uniprot/Q3UE99 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Signal Peptide|||Site|||Strand|||Turn ^@ 54% Loss of activity.|||Abolishes enzyme activity.|||Abolishes enzyme activity. Abolishes autocatalytic processing.|||Cleavage; by autolysis|||Complete loss of activity. Abolishes autocatalytic processing.|||Legumain|||N-linked (GlcNAc...) asparagine|||Nearly abolishes enzyme activity.|||No loss of activity.|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000026504|||http://purl.uniprot.org/annotation/PRO_0000026505|||http://purl.uniprot.org/annotation/PRO_5004229908|||http://purl.uniprot.org/annotation/PRO_5014296824 http://togogenome.org/gene/10090:Arx ^@ http://purl.uniprot.org/uniprot/O35085 ^@ 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|||Disordered|||Homeobox|||Homeobox protein ARX|||OAR|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048820 http://togogenome.org/gene/10090:Rbm47 ^@ http://purl.uniprot.org/uniprot/D3YXZ5|||http://purl.uniprot.org/uniprot/Q91WT8 ^@ 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; alternate|||Disordered|||In isoform 2.|||Omega-N-methylarginine; alternate|||Polar residues|||RNA-binding protein 47|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000307856|||http://purl.uniprot.org/annotation/VSP_028840|||http://purl.uniprot.org/annotation/VSP_028841 http://togogenome.org/gene/10090:Saxo2 ^@ http://purl.uniprot.org/uniprot/Q8BQB6 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Stabilizer of axonemal microtubules 2 ^@ http://purl.uniprot.org/annotation/PRO_0000321840 http://togogenome.org/gene/10090:Ssna1 ^@ http://purl.uniprot.org/uniprot/Q9JJ94 ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region ^@ Important for localization to the centrosome|||Microtubule nucleation factor SSNA1|||N-acetylthreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000114484 http://togogenome.org/gene/10090:Fhip1a ^@ http://purl.uniprot.org/uniprot/Q505K2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Acidic residues|||Disordered|||FHF complex subunit HOOK-interacting protein 1A|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000319579 http://togogenome.org/gene/10090:Trim67 ^@ http://purl.uniprot.org/uniprot/Q505D9|||http://purl.uniprot.org/uniprot/Q8BQ60 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Zinc Finger ^@ B box-type|||B box-type 1; degenerate|||B box-type 2|||B30.2/SPRY|||COS|||Disordered|||Fibronectin type-III|||RING-type; degenerate|||Tripartite motif-containing protein 67 ^@ http://purl.uniprot.org/annotation/PRO_0000256865 http://togogenome.org/gene/10090:Tstd2 ^@ http://purl.uniprot.org/uniprot/Q3U269 ^@ 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 ^@ Cysteine persulfide intermediate|||Phosphoserine|||Rhodanese|||Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000230674 http://togogenome.org/gene/10090:Mmp23 ^@ http://purl.uniprot.org/uniprot/O88676 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cleavage; by furin-like protease|||Cytoplasmic|||Helical|||Ig-like C2-type|||In isoform 2.|||Lumenal|||Matrix metalloproteinase-23|||Matrix metalloproteinase-23, soluble form|||N-linked (GlcNAc...) asparagine|||ShKT ^@ http://purl.uniprot.org/annotation/PRO_0000259915|||http://purl.uniprot.org/annotation/PRO_0000259916|||http://purl.uniprot.org/annotation/PRO_0000259917|||http://purl.uniprot.org/annotation/VSP_021561 http://togogenome.org/gene/10090:Chchd7 ^@ http://purl.uniprot.org/uniprot/Q8K2Q5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Domain Extent|||Motif ^@ CHCH|||Coiled-coil-helix-coiled-coil-helix domain-containing protein 7|||Cx9C motif 1|||Cx9C motif 2 ^@ http://purl.uniprot.org/annotation/PRO_0000129173 http://togogenome.org/gene/10090:Sec61a2 ^@ http://purl.uniprot.org/uniprot/Q9JLR1 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Protein transport protein Sec61 subunit alpha isoform 2 ^@ http://purl.uniprot.org/annotation/PRO_0000131796 http://togogenome.org/gene/10090:Slc8a3 ^@ http://purl.uniprot.org/uniprot/E9PX50|||http://purl.uniprot.org/uniprot/Q3UTP5|||http://purl.uniprot.org/uniprot/Q8BXN1|||http://purl.uniprot.org/uniprot/S4R2P9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||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|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Calx-beta|||Calx-beta 1|||Calx-beta 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Putative calmodulin-binding region|||Sodium/calcium exchanger 3 ^@ http://purl.uniprot.org/annotation/PRO_0000434797|||http://purl.uniprot.org/annotation/VSP_057981 http://togogenome.org/gene/10090:Krt34 ^@ http://purl.uniprot.org/uniprot/Q9D646 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Chain|||Domain Extent|||Region|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cuticular Ha4|||Linker 1|||Linker 12|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000361023 http://togogenome.org/gene/10090:Or2n1c ^@ http://purl.uniprot.org/uniprot/Q8VEY4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ppp1ca ^@ http://purl.uniprot.org/uniprot/P62137 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Disordered|||Dominant negative, severely disrupts circadian rhythmicity of transcription.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton donor|||Removed|||Serine/threonine-protein phosphatase PP1-alpha catalytic subunit ^@ http://purl.uniprot.org/annotation/PRO_0000058775 http://togogenome.org/gene/10090:Or6c6c ^@ http://purl.uniprot.org/uniprot/Q7TRH7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dach1 ^@ http://purl.uniprot.org/uniprot/Q3UTV2|||http://purl.uniprot.org/uniprot/Q80WU5|||http://purl.uniprot.org/uniprot/Q9QYB2 ^@ 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 ^@ DACHbox-C|||DACHbox-N|||Dachshund homolog 1|||Disordered|||In isoform 2.|||Interaction with SIN3A|||Interaction with SIX6 and HDAC3|||Phosphoserine|||Polar residues|||SKI/SNO/DAC ^@ http://purl.uniprot.org/annotation/PRO_0000095598|||http://purl.uniprot.org/annotation/VSP_009489 http://togogenome.org/gene/10090:Pja1 ^@ http://purl.uniprot.org/uniprot/B1AXU3|||http://purl.uniprot.org/uniprot/B1AXU4|||http://purl.uniprot.org/uniprot/O55176|||http://purl.uniprot.org/uniprot/Q05CG5|||http://purl.uniprot.org/uniprot/Q3UXQ1 ^@ 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 ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase Praja-1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of ubiquitination activity.|||No effect on MAGED1 binding. Decrease in ubiquitination of MAGED1. No inhibition of DLX5-dependent transcriptional activity.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056000|||http://purl.uniprot.org/annotation/VSP_007519|||http://purl.uniprot.org/annotation/VSP_007520|||http://purl.uniprot.org/annotation/VSP_007521|||http://purl.uniprot.org/annotation/VSP_022011 http://togogenome.org/gene/10090:Hpdl ^@ http://purl.uniprot.org/uniprot/Q8K248 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ 4-hydroxyphenylpyruvate dioxygenase-like protein|||VOC 1|||VOC 2 ^@ http://purl.uniprot.org/annotation/PRO_0000271120 http://togogenome.org/gene/10090:Ly9 ^@ http://purl.uniprot.org/uniprot/E9PX73|||http://purl.uniprot.org/uniprot/Q01965 ^@ 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|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITSM 1 (atypical)|||ITSM 2|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type 1|||Ig-like V-type 2|||In Ly9-1.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||T-lymphocyte surface antigen Ly-9 ^@ http://purl.uniprot.org/annotation/PRO_0000014852 http://togogenome.org/gene/10090:Or4g7 ^@ http://purl.uniprot.org/uniprot/Q7TQY0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cyp2b19 ^@ http://purl.uniprot.org/uniprot/O55071 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Cytochrome P450 2B19|||Phosphoserine; by PKA|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051689 http://togogenome.org/gene/10090:Ctf2 ^@ http://purl.uniprot.org/uniprot/P83714|||http://purl.uniprot.org/uniprot/Q0VB69 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ Cardiotrophin-2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015614|||http://purl.uniprot.org/annotation/PRO_5014306859 http://togogenome.org/gene/10090:Anks1b ^@ http://purl.uniprot.org/uniprot/A0A0R4J2A2|||http://purl.uniprot.org/uniprot/A0A0R4J2A6|||http://purl.uniprot.org/uniprot/A0A0R4J2A8|||http://purl.uniprot.org/uniprot/A0A140T8U6|||http://purl.uniprot.org/uniprot/E9QPP6|||http://purl.uniprot.org/uniprot/Q8BIZ1|||http://purl.uniprot.org/uniprot/Q8BZM2|||http://purl.uniprot.org/uniprot/S4R1H2|||http://purl.uniprot.org/uniprot/S4R2I2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Nuclear localization signal|||PID|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SAM|||SAM 1|||SAM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000327260|||http://purl.uniprot.org/annotation/VSP_032713|||http://purl.uniprot.org/annotation/VSP_032714|||http://purl.uniprot.org/annotation/VSP_032715|||http://purl.uniprot.org/annotation/VSP_032716|||http://purl.uniprot.org/annotation/VSP_032717|||http://purl.uniprot.org/annotation/VSP_032718|||http://purl.uniprot.org/annotation/VSP_032719 http://togogenome.org/gene/10090:Pnma5 ^@ http://purl.uniprot.org/uniprot/Q3URM0|||http://purl.uniprot.org/uniprot/Q5DTT8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Paraneoplastic antigen-like protein 5|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000311218 http://togogenome.org/gene/10090:Bcl2l1 ^@ http://purl.uniprot.org/uniprot/O35843|||http://purl.uniprot.org/uniprot/Q5HZH3|||http://purl.uniprot.org/uniprot/Q64373 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Turn ^@ Apoptosis regulator Bcl-2 family BH4|||BH1|||BH2|||BH3|||BH4|||Basic and acidic residues|||Bcl-2-like protein 1|||Disordered|||Helical|||In isoform Bcl-X(S).|||In isoform Bcl-X(beta).|||In isoform Bcl-X(delta-TM).|||Phosphoserine; by CDK1|||Phosphoserine; by PLK3 ^@ http://purl.uniprot.org/annotation/PRO_0000143063|||http://purl.uniprot.org/annotation/VSP_000517|||http://purl.uniprot.org/annotation/VSP_000518|||http://purl.uniprot.org/annotation/VSP_000519 http://togogenome.org/gene/10090:R3hcc1 ^@ http://purl.uniprot.org/uniprot/Q8BSI6 ^@ 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|||Disordered|||Phosphoserine|||Polar residues|||R3H|||R3H and coiled-coil domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000307390 http://togogenome.org/gene/10090:Or5ac19 ^@ http://purl.uniprot.org/uniprot/Q7TS38 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Uqcc1 ^@ http://purl.uniprot.org/uniprot/Q9CWU6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Ubiquinol-cytochrome c reductase complex assembly factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000206561|||http://purl.uniprot.org/annotation/VSP_000858|||http://purl.uniprot.org/annotation/VSP_000859 http://togogenome.org/gene/10090:Muc21 ^@ http://purl.uniprot.org/uniprot/F7C950 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Mucin catalytic TM and cytoplasmic tail|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003354889 http://togogenome.org/gene/10090:Chrac1 ^@ http://purl.uniprot.org/uniprot/Q9JKP8 ^@ 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 ^@ Acidic residues|||Chromatin accessibility complex protein 1|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089657 http://togogenome.org/gene/10090:Arih1 ^@ http://purl.uniprot.org/uniprot/Q9Z1K5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||Ariadne domain|||Disordered|||E3 ubiquitin-protein ligase ARIH1|||IBR-type|||N6-acetyllysine|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain|||UBA-like ^@ http://purl.uniprot.org/annotation/PRO_0000055753 http://togogenome.org/gene/10090:Slc5a9 ^@ http://purl.uniprot.org/uniprot/Q8VDT1 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Sodium/glucose cotransporter 4 ^@ http://purl.uniprot.org/annotation/PRO_0000333806 http://togogenome.org/gene/10090:Eml2 ^@ http://purl.uniprot.org/uniprot/Q7TNG5 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Echinoderm microtubule-associated protein-like 2|||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_0000284388|||http://purl.uniprot.org/annotation/VSP_024480|||http://purl.uniprot.org/annotation/VSP_061498 http://togogenome.org/gene/10090:Itpr2 ^@ http://purl.uniprot.org/uniprot/Q8CED6|||http://purl.uniprot.org/uniprot/Q9Z329 ^@ 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|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes PKA-mediated phosphorylation. No enhanced calcium release. Abolishes PKA-mediated phosphorylation: When associated with A-990; A-1190; A-1351 and A-1581.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Inositol 1,4,5-trisphosphate receptor type 2|||Ion transport|||Loss of binding activity.|||MIR 1|||MIR 2|||MIR 3|||MIR 4|||MIR 5|||No effect on PKA-mediated phosphorylation. Abolishes PKA-mediated phosphorylation: When associated with A-937; A-1190; A-1351 and A-1581.|||No effect on PKA-mediated phosphorylation. Abolishes PKA-mediated phosphorylation: When associated with A-937; A-990; A-1190 and A-1351.|||No effect on PKA-mediated phosphorylation. Abolishes PKA-mediated phosphorylation: When associated with A-937; A-990; A-1190 and A-1581.|||No effect on PKA-mediated phosphorylation. Abolishes PKA-mediated phosphorylation: When associated with A-937; A-990; A-1351 and A-1581.|||No effect on PKA-mediated phosphorylation. Enhanced calcium release on PKA activation.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000153925|||http://purl.uniprot.org/annotation/VSP_002701|||http://purl.uniprot.org/annotation/VSP_002702|||http://purl.uniprot.org/annotation/VSP_016026 http://togogenome.org/gene/10090:Tmem128 ^@ http://purl.uniprot.org/uniprot/Q9CZB9 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 128 ^@ http://purl.uniprot.org/annotation/PRO_0000254557 http://togogenome.org/gene/10090:Bsph2 ^@ http://purl.uniprot.org/uniprot/Q0Q236 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Binder of sperm protein homolog 2|||Fibronectin type-II 1|||Fibronectin type-II 2 ^@ http://purl.uniprot.org/annotation/PRO_5004175719 http://togogenome.org/gene/10090:Cdipt ^@ http://purl.uniprot.org/uniprot/A0A0U1RPV3|||http://purl.uniprot.org/uniprot/Q8VDP6 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Topological Domain|||Transmembrane ^@ CDP-diacylglycerol--inositol 3-phosphatidyltransferase|||Cytoplasmic|||Helical|||Lumenal|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000056803 http://togogenome.org/gene/10090:Myb ^@ http://purl.uniprot.org/uniprot/A0A087WPA7|||http://purl.uniprot.org/uniprot/P06876|||http://purl.uniprot.org/uniprot/Q3UUX5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand ^@ C-myb C-terminal|||Complete loss of TRAF7-mediated SUMOylatiom; when associated with R-499.|||Complete loss of TRAF7-mediated SUMOylatiom; when associated with R-523.|||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|||Interaction with HIPK2 and NLK|||Leucine-zipper|||Myb-like|||N6-acetyllysine|||N6-acetyllysine; alternate|||Negative regulatory domain|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcriptional activation domain|||Transcriptional activator Myb ^@ http://purl.uniprot.org/annotation/PRO_0000197049 http://togogenome.org/gene/10090:Gtpbp10 ^@ http://purl.uniprot.org/uniprot/Q8K013 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region ^@ Disordered|||GTP-binding protein 10|||OBG-type G|||Obg ^@ http://purl.uniprot.org/annotation/PRO_0000312631 http://togogenome.org/gene/10090:Mrgprb1 ^@ http://purl.uniprot.org/uniprot/Q3UG61 ^@ 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|||Mas-related G-protein coupled receptor member B1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000305585 http://togogenome.org/gene/10090:Serpinb1c ^@ http://purl.uniprot.org/uniprot/Q5SV42 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Chain|||Sequence Conflict|||Site ^@ Leukocyte elastase inhibitor C|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000289122 http://togogenome.org/gene/10090:Or10ak9 ^@ http://purl.uniprot.org/uniprot/K7N684 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Heatr3 ^@ http://purl.uniprot.org/uniprot/Q8BQM4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||HEAT 1|||HEAT 2|||HEAT repeat-containing protein 3|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000050822 http://togogenome.org/gene/10090:St13 ^@ http://purl.uniprot.org/uniprot/Q99L47 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Hsc70-interacting protein|||N6-acetyllysine|||Phosphoserine; by GRK5|||STI1|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000190812 http://togogenome.org/gene/10090:Jagn1 ^@ http://purl.uniprot.org/uniprot/A0A0N4SV89|||http://purl.uniprot.org/uniprot/Q5XKN4 ^@ 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|||Helical|||Lumenal|||Phosphoserine|||Protein jagunal homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000313609 http://togogenome.org/gene/10090:Clca3b ^@ http://purl.uniprot.org/uniprot/E9PUL3|||http://purl.uniprot.org/uniprot/Q91ZF5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Pro residues|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5003242970|||http://purl.uniprot.org/annotation/PRO_5010147422 http://togogenome.org/gene/10090:Ung ^@ http://purl.uniprot.org/uniprot/P97931|||http://purl.uniprot.org/uniprot/Q791V7 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 1.|||N6-acetyllysine|||Phosphoserine|||Proton acceptor|||Uracil-DNA glycosylase|||Uracil-DNA glycosylase-like ^@ http://purl.uniprot.org/annotation/PRO_0000176174|||http://purl.uniprot.org/annotation/VSP_008514 http://togogenome.org/gene/10090:Ptger1 ^@ http://purl.uniprot.org/uniprot/B2RS62|||http://purl.uniprot.org/uniprot/P35375 ^@ 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 ^@ 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|||Polar residues|||Prostaglandin E2 receptor EP1 subtype ^@ http://purl.uniprot.org/annotation/PRO_0000070051 http://togogenome.org/gene/10090:1110038F14Rik ^@ http://purl.uniprot.org/uniprot/Q3U6N9 ^@ 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 3.|||In isoform 2.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Removed|||UPF0488 protein C8orf33 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000304983|||http://purl.uniprot.org/annotation/VSP_028170|||http://purl.uniprot.org/annotation/VSP_028171 http://togogenome.org/gene/10090:Siglecf ^@ http://purl.uniprot.org/uniprot/B7ZN64|||http://purl.uniprot.org/uniprot/Q920G3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Polar residues|||SLAM-like motif|||Sialic acid-binding Ig-like lectin 5 ^@ http://purl.uniprot.org/annotation/PRO_0000014945|||http://purl.uniprot.org/annotation/PRO_5015087442 http://togogenome.org/gene/10090:Ak4 ^@ http://purl.uniprot.org/uniprot/Q3U489|||http://purl.uniprot.org/uniprot/Q9WUR9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Adenylate kinase 4, mitochondrial|||Adenylate kinase active site lid|||LID|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||NMP|||NMPbind ^@ http://purl.uniprot.org/annotation/PRO_0000158927 http://togogenome.org/gene/10090:Uqcrc1 ^@ http://purl.uniprot.org/uniprot/Q9CZ13 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Cytochrome b-c1 complex subunit 1, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000026787 http://togogenome.org/gene/10090:Fam118a ^@ http://purl.uniprot.org/uniprot/Q91YN1 ^@ 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.|||N-acetylmethionine|||Phosphoserine|||Protein FAM118A ^@ http://purl.uniprot.org/annotation/PRO_0000079573|||http://purl.uniprot.org/annotation/VSP_014460|||http://purl.uniprot.org/annotation/VSP_014461 http://togogenome.org/gene/10090:Gnao1 ^@ http://purl.uniprot.org/uniprot/P18872 ^@ 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 ^@ 5-glutamyl histamine|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(o) subunit alpha|||In isoform Alpha-2.|||N-myristoyl glycine|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000203704|||http://purl.uniprot.org/annotation/VSP_031251 http://togogenome.org/gene/10090:Rimklb ^@ http://purl.uniprot.org/uniprot/Q80WS1 ^@ 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 and isoform 3.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000282572|||http://purl.uniprot.org/annotation/VSP_024200|||http://purl.uniprot.org/annotation/VSP_024201|||http://purl.uniprot.org/annotation/VSP_024202|||http://purl.uniprot.org/annotation/VSP_024203 http://togogenome.org/gene/10090:Dhrs3 ^@ http://purl.uniprot.org/uniprot/O88876 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Proton acceptor|||Short-chain dehydrogenase/reductase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000054645|||http://purl.uniprot.org/annotation/VSP_050734|||http://purl.uniprot.org/annotation/VSP_050735 http://togogenome.org/gene/10090:Ppargc1a ^@ http://purl.uniprot.org/uniprot/O70343 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes AMPK-mediated phosphorylation; when associated with A-177.|||Abolishes AMPK-mediated phosphorylation; when associated with A-538.|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||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|||Strongly reduces coactivation of RORA activity. ^@ http://purl.uniprot.org/annotation/PRO_0000081733|||http://purl.uniprot.org/annotation/VSP_053275|||http://purl.uniprot.org/annotation/VSP_053276|||http://purl.uniprot.org/annotation/VSP_053277|||http://purl.uniprot.org/annotation/VSP_053278|||http://purl.uniprot.org/annotation/VSP_053279|||http://purl.uniprot.org/annotation/VSP_053280|||http://purl.uniprot.org/annotation/VSP_053281 http://togogenome.org/gene/10090:Or5b12b ^@ http://purl.uniprot.org/uniprot/Q8VFW9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rnf130 ^@ http://purl.uniprot.org/uniprot/A0A571BES6|||http://purl.uniprot.org/uniprot/Q5SVR5|||http://purl.uniprot.org/uniprot/Q8VEM1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||E3 ubiquitin-protein ligase RNF130|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||PA|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000030719|||http://purl.uniprot.org/annotation/PRO_5004262304|||http://purl.uniprot.org/annotation/PRO_5022073095 http://togogenome.org/gene/10090:Or5p60 ^@ http://purl.uniprot.org/uniprot/B2RQ97|||http://purl.uniprot.org/uniprot/Q8VFD3 ^@ 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 5P60 ^@ http://purl.uniprot.org/annotation/PRO_0000150842 http://togogenome.org/gene/10090:Fosl2 ^@ http://purl.uniprot.org/uniprot/P47930 ^@ 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.|||Leucine-zipper|||N-acetylmethionine|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076484|||http://purl.uniprot.org/annotation/VSP_042084 http://togogenome.org/gene/10090:C77080 ^@ http://purl.uniprot.org/uniprot/A2A7S8 ^@ 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|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Uncharacterized protein KIAA1522 ^@ http://purl.uniprot.org/annotation/PRO_0000311247|||http://purl.uniprot.org/annotation/VSP_029459|||http://purl.uniprot.org/annotation/VSP_029460|||http://purl.uniprot.org/annotation/VSP_029461 http://togogenome.org/gene/10090:Olig2 ^@ http://purl.uniprot.org/uniprot/Q542S0|||http://purl.uniprot.org/uniprot/Q9EQW6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ BHLH|||Disordered|||Oligodendrocyte transcription factor 2|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127415 http://togogenome.org/gene/10090:Vmn1r55 ^@ http://purl.uniprot.org/uniprot/E9Q8I6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnr2 ^@ http://purl.uniprot.org/uniprot/P47936 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000069324 http://togogenome.org/gene/10090:Mcpt1 ^@ http://purl.uniprot.org/uniprot/P11034|||http://purl.uniprot.org/uniprot/Q496V0 ^@ 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|||Mast cell protease 1|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027449|||http://purl.uniprot.org/annotation/PRO_0000027450|||http://purl.uniprot.org/annotation/PRO_5014309294 http://togogenome.org/gene/10090:Mmp8 ^@ http://purl.uniprot.org/uniprot/O70138 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Propeptide|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cysteine switch|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||N-linked (GlcNAc...) asparagine|||Neutrophil collagenase|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028746|||http://purl.uniprot.org/annotation/PRO_0000028747 http://togogenome.org/gene/10090:Tsc2 ^@ http://purl.uniprot.org/uniprot/A0A2I3BPP1|||http://purl.uniprot.org/uniprot/A0A2I3BRT5|||http://purl.uniprot.org/uniprot/Q3TQ10|||http://purl.uniprot.org/uniprot/Q3UG88|||http://purl.uniprot.org/uniprot/Q3UGI8|||http://purl.uniprot.org/uniprot/Q3UHB2|||http://purl.uniprot.org/uniprot/Q7TT21 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Rap-GAP ^@ http://togogenome.org/gene/10090:4930415L06Rik ^@ http://purl.uniprot.org/uniprot/Q3V0Y1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Protein PPP4R3C ^@ http://purl.uniprot.org/annotation/PRO_0000344448 http://togogenome.org/gene/10090:Zfp787 ^@ http://purl.uniprot.org/uniprot/Q8BIF9 ^@ 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|||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_0000287607 http://togogenome.org/gene/10090:Chic2 ^@ http://purl.uniprot.org/uniprot/Q9D9G3 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Motif|||Sequence Conflict ^@ CHIC motif (Cys-rich)|||Cysteine-rich hydrophobic domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000189557 http://togogenome.org/gene/10090:Syt8 ^@ http://purl.uniprot.org/uniprot/F2Z3W8|||http://purl.uniprot.org/uniprot/Q9R0N6 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Splice Variant|||Topological Domain|||Transmembrane ^@ C2|||C2 1|||C2 2|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||Synaptotagmin-8 ^@ http://purl.uniprot.org/annotation/PRO_0000183960|||http://purl.uniprot.org/annotation/VSP_009028|||http://purl.uniprot.org/annotation/VSP_009029 http://togogenome.org/gene/10090:Arpp21 ^@ http://purl.uniprot.org/uniprot/E9Q4A0|||http://purl.uniprot.org/uniprot/Q9DCB4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes methylation, no effect on subcellular location.|||Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In isoform 10.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 6 and isoform 9.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PKA|||Polar residues|||R3H|||Removed|||SUZ|||cAMP-regulated phosphoprotein 21 ^@ http://purl.uniprot.org/annotation/PRO_0000064683|||http://purl.uniprot.org/annotation/VSP_029477|||http://purl.uniprot.org/annotation/VSP_029478|||http://purl.uniprot.org/annotation/VSP_029479|||http://purl.uniprot.org/annotation/VSP_029480|||http://purl.uniprot.org/annotation/VSP_029481|||http://purl.uniprot.org/annotation/VSP_029482|||http://purl.uniprot.org/annotation/VSP_029483|||http://purl.uniprot.org/annotation/VSP_029484|||http://purl.uniprot.org/annotation/VSP_029485|||http://purl.uniprot.org/annotation/VSP_029486|||http://purl.uniprot.org/annotation/VSP_029487|||http://purl.uniprot.org/annotation/VSP_029488|||http://purl.uniprot.org/annotation/VSP_029489|||http://purl.uniprot.org/annotation/VSP_029490|||http://purl.uniprot.org/annotation/VSP_029491|||http://purl.uniprot.org/annotation/VSP_029492 http://togogenome.org/gene/10090:Foxf2 ^@ http://purl.uniprot.org/uniprot/O54743 ^@ 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 F2|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000322981 http://togogenome.org/gene/10090:Shbg ^@ http://purl.uniprot.org/uniprot/A0A158SIS9|||http://purl.uniprot.org/uniprot/P97497 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Laminin G|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Sex hormone-binding globulin ^@ http://purl.uniprot.org/annotation/PRO_0000032558|||http://purl.uniprot.org/annotation/PRO_5007632491 http://togogenome.org/gene/10090:Aloxe3 ^@ http://purl.uniprot.org/uniprot/Q14B96|||http://purl.uniprot.org/uniprot/Q9WV07 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Site ^@ Essential for stabilizing binding to COTL1|||Hydroperoxide isomerase ALOXE3|||Lipoxygenase|||PLAT ^@ http://purl.uniprot.org/annotation/PRO_0000220692 http://togogenome.org/gene/10090:Polm ^@ http://purl.uniprot.org/uniprot/Q9JIW4 ^@ 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|||Site|||Strand|||Turn ^@ BRCT|||DNA-directed DNA/RNA polymerase mu|||Disordered|||Involved in ssDNA binding|||Phosphoserine|||Responsible for the low discrimination between dNTP and rNTP ^@ http://purl.uniprot.org/annotation/PRO_0000218788 http://togogenome.org/gene/10090:Kat5 ^@ http://purl.uniprot.org/uniprot/A0A494BAP7|||http://purl.uniprot.org/uniprot/Q3UJQ1|||http://purl.uniprot.org/uniprot/Q8CHK4 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||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|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Abolished acetyltransferase activity.|||Abolished phosphorylation by GSK3 and decreased acetyltransferase activity. Impaired ability to activate the cGAS-STING antiviral response in knockin mice. Lean phenotype caused by impaired ability to promote the synthesis of diacylglycerol in knockin mice. Decreased ability to promote homologous recombination (HR)repair in response to DNA double-strand breaks (DSBs).|||C2HC MYST-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); alternate|||Histone acetyltransferase KAT5|||Impaired phosphorylation and decreased acetyltransferase activity, leading to decreased ability to promote homologous recombination (HR)repair in response to DNA double-strand breaks (DSBs).|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with ATF2|||MYST-type HAT|||Mimics phosphorylation; constitutively active mutant that shows constitutive protein acetyltransferase activity. Increased ability to promote homologous recombination (HR)repair in response to DNA double-strand breaks (DSBs).|||Mimics phosphorylation; constitutively active mutant that shows constitutive protein acetyltransferase and acyltransferase activities in knockin mice. Increased ability to promote homologous recombination (HR)repair in response to DNA double-strand breaks (DSBs).|||N6-acetyllysine|||N6-acetyllysine; by autocatalysis|||Phosphoserine|||Phosphoserine; by CDK1 and CDK9|||Proton donor/acceptor|||Tudor-knot ^@ http://purl.uniprot.org/annotation/PRO_0000051581|||http://purl.uniprot.org/annotation/VSP_009105|||http://purl.uniprot.org/annotation/VSP_009106|||http://purl.uniprot.org/annotation/VSP_009107|||http://purl.uniprot.org/annotation/VSP_061400|||http://purl.uniprot.org/annotation/VSP_061401 http://togogenome.org/gene/10090:Fermt2 ^@ http://purl.uniprot.org/uniprot/Q3TLE2|||http://purl.uniprot.org/uniprot/Q8CIB5 ^@ 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 interaction with integrins ITGB1 and ITGB3.|||Basic and acidic residues|||Disordered|||FERM|||Fermitin family homolog 2|||Interaction with membranes containing phosphatidylinositol phosphate|||PH|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000219457 http://togogenome.org/gene/10090:Adk ^@ http://purl.uniprot.org/uniprot/P55264|||http://purl.uniprot.org/uniprot/Q8BMC5 ^@ 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 ^@ Adenosine kinase|||Carbohydrate kinase PfkB|||In isoform 2.|||No effect on in vitro phosphorylation by PKC.|||Nuclear localization signal|||Phosphotyrosine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000080054|||http://purl.uniprot.org/annotation/VSP_014756 http://togogenome.org/gene/10090:Sncaip ^@ http://purl.uniprot.org/uniprot/E9Q4E2|||http://purl.uniprot.org/uniprot/G5E848|||http://purl.uniprot.org/uniprot/Q3TVI3|||http://purl.uniprot.org/uniprot/Q3V1N2|||http://purl.uniprot.org/uniprot/Q99ME3 ^@ 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|||ANK 6|||Basic and acidic residues|||Disordered|||Polar residues|||Synphilin-1|||Synphilin-1 alpha-Synuclein-binding ^@ http://purl.uniprot.org/annotation/PRO_0000320071 http://togogenome.org/gene/10090:Reep4 ^@ http://purl.uniprot.org/uniprot/A0A2I3BQJ3|||http://purl.uniprot.org/uniprot/Q8K072 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Receptor expression-enhancing protein|||Receptor expression-enhancing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000101831|||http://purl.uniprot.org/annotation/PRO_5014139443 http://togogenome.org/gene/10090:Plppr1 ^@ http://purl.uniprot.org/uniprot/Q8BFZ2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phospholipid phosphatase-related protein type 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000317533|||http://purl.uniprot.org/annotation/VSP_031009 http://togogenome.org/gene/10090:Pax9 ^@ http://purl.uniprot.org/uniprot/P47242|||http://purl.uniprot.org/uniprot/Q3V1K1 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Region ^@ Interaction with KDM5B|||PAI subdomain|||Paired|||Paired box protein Pax-9|||RED subdomain ^@ http://purl.uniprot.org/annotation/PRO_0000050208 http://togogenome.org/gene/10090:Stat2 ^@ http://purl.uniprot.org/uniprot/Q9QXJ2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ SH2 ^@ http://togogenome.org/gene/10090:Elk3 ^@ http://purl.uniprot.org/uniprot/G3UVW8|||http://purl.uniprot.org/uniprot/G3UVX2|||http://purl.uniprot.org/uniprot/P41971 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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_0000204098 http://togogenome.org/gene/10090:Exosc6 ^@ http://purl.uniprot.org/uniprot/Q8BTW3 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Exosome complex component MTR3 ^@ http://purl.uniprot.org/annotation/PRO_0000287479 http://togogenome.org/gene/10090:Tgtp1 ^@ http://purl.uniprot.org/uniprot/Q3T9E4|||http://purl.uniprot.org/uniprot/Q62293 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Turn ^@ IRG-type G|||T-cell-specific guanine nucleotide triphosphate-binding protein 1|||T-cell-specific guanine nucleotide triphosphate-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000437942|||http://purl.uniprot.org/annotation/PRO_0000437943 http://togogenome.org/gene/10090:Csta1 ^@ http://purl.uniprot.org/uniprot/B2RT71|||http://purl.uniprot.org/uniprot/P56567 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Site ^@ Cystatin|||Cystatin-A|||N-acetylmethionine|||Reactive site|||Secondary area of contact ^@ http://purl.uniprot.org/annotation/PRO_0000207149 http://togogenome.org/gene/10090:Rbak ^@ http://purl.uniprot.org/uniprot/Q8BQC8 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||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 2|||C2H2-type 3|||C2H2-type 4|||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)|||Interaction with AR|||KRAB|||RB-associated KRAB zinc finger protein|||Required for interaction with RB1 ^@ http://purl.uniprot.org/annotation/PRO_0000316977 http://togogenome.org/gene/10090:Tmem177 ^@ http://purl.uniprot.org/uniprot/Q8BPE4 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Transmembrane protein 177 ^@ http://purl.uniprot.org/annotation/PRO_0000282647 http://togogenome.org/gene/10090:Vmn1r124 ^@ http://purl.uniprot.org/uniprot/D3YTX4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tnfrsf4 ^@ http://purl.uniprot.org/uniprot/B1ASL3|||http://purl.uniprot.org/uniprot/P47741 ^@ 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|||Helical|||N-linked (GlcNAc...) asparagine|||TNFR-Cys|||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_0000034555|||http://purl.uniprot.org/annotation/PRO_5015087046 http://togogenome.org/gene/10090:Cd7 ^@ http://purl.uniprot.org/uniprot/P50283|||http://purl.uniprot.org/uniprot/Q3U4A8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like domain-containing protein|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||T-cell antigen CD7 ^@ http://purl.uniprot.org/annotation/PRO_0000014634|||http://purl.uniprot.org/annotation/PRO_5010843370 http://togogenome.org/gene/10090:Adra2a ^@ http://purl.uniprot.org/uniprot/Q01338 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Alpha-2A adrenergic receptor|||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|||Implicated in catechol agonist binding|||Implicated in ligand binding|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069081 http://togogenome.org/gene/10090:Vmn1r19 ^@ http://purl.uniprot.org/uniprot/Q8R2C7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zcrb1 ^@ http://purl.uniprot.org/uniprot/Q9CZ96 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||CCHC-type|||Disordered|||In isoform 2.|||Phosphoserine|||RRM|||Zinc finger CCHC-type and RNA-binding motif-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000252374|||http://purl.uniprot.org/annotation/VSP_020918 http://togogenome.org/gene/10090:Cfap61 ^@ http://purl.uniprot.org/uniprot/B7ZCD6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Cilia- and flagella-associated protein 61 N-terminal ^@ http://togogenome.org/gene/10090:Mterf1b ^@ http://purl.uniprot.org/uniprot/B9EJ57 ^@ Chain|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Chain|||Region|||Site|||Transit Peptide ^@ Interaction with DNA|||Mitochondrion|||Transcription termination factor 1b, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000430152 http://togogenome.org/gene/10090:Gria2 ^@ http://purl.uniprot.org/uniprot/Q4LG64 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Glutamate receptor|||Helical|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding ^@ http://purl.uniprot.org/annotation/PRO_5027156157 http://togogenome.org/gene/10090:Defb23 ^@ http://purl.uniprot.org/uniprot/Q30KP0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Beta-defensin|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015020006 http://togogenome.org/gene/10090:Zfp457 ^@ http://purl.uniprot.org/uniprot/L7N1X4|||http://purl.uniprot.org/uniprot/Q7M6X7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C2H2-type|||Helical|||KRAB ^@ http://togogenome.org/gene/10090:Hbegf ^@ http://purl.uniprot.org/uniprot/Q06186|||http://purl.uniprot.org/uniprot/Q5FW64 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic residues|||C-terminal|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||Heparin-binding EGF-like growth factor|||O-linked (GalNAc...) threonine|||Polar residues|||Proheparin-binding EGF-like growth factor ^@ http://purl.uniprot.org/annotation/PRO_0000007614|||http://purl.uniprot.org/annotation/PRO_0000007615|||http://purl.uniprot.org/annotation/PRO_0000007616|||http://purl.uniprot.org/annotation/PRO_0000302804|||http://purl.uniprot.org/annotation/PRO_5014309788 http://togogenome.org/gene/10090:D17H6S56E-5 ^@ http://purl.uniprot.org/uniprot/Q91UZ6 ^@ Coiled-Coil|||Region|||Transmembrane ^@ Coiled-Coil|||Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Spin2f ^@ http://purl.uniprot.org/uniprot/A0A571BGB0 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Oard1 ^@ http://purl.uniprot.org/uniprot/Q8R5F3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ ADP-ribose glycohydrolase OARD1|||Macro|||N-acetylalanine|||Nucleophile|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089530 http://togogenome.org/gene/10090:Etnk2 ^@ http://purl.uniprot.org/uniprot/A7MCT6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ Ethanolamine kinase 2|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000393962|||http://purl.uniprot.org/annotation/VSP_039099 http://togogenome.org/gene/10090:Sult6b1 ^@ http://purl.uniprot.org/uniprot/P0CC03 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Proton acceptor|||Sulfotransferase 6B1 ^@ http://purl.uniprot.org/annotation/PRO_0000389506 http://togogenome.org/gene/10090:Iqsec1 ^@ http://purl.uniprot.org/uniprot/A0A1D5RM83|||http://purl.uniprot.org/uniprot/E9PUA3|||http://purl.uniprot.org/uniprot/Q8R0S2 ^@ 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|||Basic residues|||Disordered|||IQ|||IQ motif and SEC7 domain-containing protein 1|||In isoform 2.|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000245607|||http://purl.uniprot.org/annotation/VSP_019759 http://togogenome.org/gene/10090:Atp5o ^@ http://purl.uniprot.org/uniprot/Q9DB20 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ ATP synthase subunit O, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000002647 http://togogenome.org/gene/10090:Tmem140 ^@ http://purl.uniprot.org/uniprot/Q8BGY5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Transmembrane protein 140 ^@ http://purl.uniprot.org/annotation/PRO_0000274358 http://togogenome.org/gene/10090:Ripply2 ^@ http://purl.uniprot.org/uniprot/Q2WG76 ^@ Chain|||Molecule Processing|||Motif|||Region ^@ Chain|||Motif|||Region ^@ Disordered|||Protein ripply2|||Ripply homology domain|||WRPW motif ^@ http://purl.uniprot.org/annotation/PRO_0000307760 http://togogenome.org/gene/10090:Ankrd23 ^@ http://purl.uniprot.org/uniprot/A0A0A6YW48|||http://purl.uniprot.org/uniprot/A2RT50|||http://purl.uniprot.org/uniprot/Q812A3|||http://purl.uniprot.org/uniprot/Q8K1D0 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Region|||Repeat ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 23|||Disordered|||Interaction with TTN ^@ http://purl.uniprot.org/annotation/PRO_0000240667 http://togogenome.org/gene/10090:Itch ^@ http://purl.uniprot.org/uniprot/Q8C863 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn ^@ Abolishes interaction with MAPK8.|||Almost complete loss of interaction with MAPK8.|||Basic and acidic residues|||C2|||Disordered|||E3 ubiquitin-protein ligase Itchy|||Glycyl thioester intermediate|||Greatly decreased interaction with MAPK8 and ligase activity.|||HECT|||In isoform 2.|||Inhibits in vitro interaction between ITCHHECT domain and PRR/WW motifs. More sensitive to in vitro proteolysis.|||Loss of ubiquitin protein ligase activity.|||MAP kinase docking site|||More sensitive to in vitro proteolysis.|||N-acetylserine|||No loss of MAPK8-mediated phosphorylation and no effect on ligase activity. Almost complete inactivation of ligase activity; when associated with A-199. Greatly reduced MAPK8-mediated phosphorylation; when associated with A-199 or A-222. Completely abolishes MAPK8-mediated phosphorylation; when associated with A-199 and A-222.|||No loss of MAPK8-mediated phosphorylation and no effect on ligase activity. Almost complete inactivation of ligase activity; when associated with A-232. Greatly reduced MAPK8-mediated phosphorylation; when associated with A-222 or A-232. Completely abolishes MAPK8-mediated phosphorylation; when associated with A-222 and A-232.|||No loss of MAPK8-mediated phosphorylation. Greatly reduced MAPK8-mediated phosphorylation; when associated with A-199 or A-232. Completely abolishes MAPK8-mediated phosphorylation; when associated with A-199 and A-232.|||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_0000120318|||http://purl.uniprot.org/annotation/VSP_008452|||http://purl.uniprot.org/annotation/VSP_008453 http://togogenome.org/gene/10090:Agtr2 ^@ http://purl.uniprot.org/uniprot/P35374|||http://purl.uniprot.org/uniprot/Q3US12 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||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|||Helix VIII|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKC|||Type-2 angiotensin II receptor ^@ http://purl.uniprot.org/annotation/PRO_0000069169 http://togogenome.org/gene/10090:Fbxl21 ^@ http://purl.uniprot.org/uniprot/G3X9Y3|||http://purl.uniprot.org/uniprot/Q8BFZ4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Mutagenesis Site|||Repeat|||Splice Variant ^@ F-box|||F-box/LRR-repeat protein 21|||In Past-time (Psttm) mutant; causes period shortening due to Cry1 and Cry2 destabilization.|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6 ^@ http://purl.uniprot.org/annotation/PRO_0000119874|||http://purl.uniprot.org/annotation/VSP_008415|||http://purl.uniprot.org/annotation/VSP_008416 http://togogenome.org/gene/10090:Tmem92 ^@ http://purl.uniprot.org/uniprot/B7ZWI3 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Transmembrane protein 92 ^@ http://purl.uniprot.org/annotation/PRO_0000416120|||http://purl.uniprot.org/annotation/VSP_042507 http://togogenome.org/gene/10090:Rad9a ^@ http://purl.uniprot.org/uniprot/Q9Z0F6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Cell cycle checkpoint control protein RAD9A|||Disordered|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Possesses 3'-5' exonuclease activity|||Sufficient for interaction with ABL1 ^@ http://purl.uniprot.org/annotation/PRO_0000225001 http://togogenome.org/gene/10090:Vmn1r50 ^@ http://purl.uniprot.org/uniprot/Q9EP51 ^@ 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|||Vomeronasal type-1 receptor 50 ^@ http://purl.uniprot.org/annotation/PRO_0000239973 http://togogenome.org/gene/10090:Lrrc3c ^@ http://purl.uniprot.org/uniprot/A0A1B0GRI5 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5008408556 http://togogenome.org/gene/10090:Gm14393 ^@ http://purl.uniprot.org/uniprot/A2ARW5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Socs4 ^@ http://purl.uniprot.org/uniprot/Q8C1K3|||http://purl.uniprot.org/uniprot/Q91ZA6 ^@ 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|||SH2|||SOCS box|||SOCS4/SOCS5|||Suppressor of cytokine signaling 4 ^@ http://purl.uniprot.org/annotation/PRO_0000181248 http://togogenome.org/gene/10090:Sinhcaf ^@ http://purl.uniprot.org/uniprot/Q8C8M1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||SIN3-HDAC complex-associated factor ^@ http://purl.uniprot.org/annotation/PRO_0000187087 http://togogenome.org/gene/10090:Patj ^@ http://purl.uniprot.org/uniprot/A2ADL9|||http://purl.uniprot.org/uniprot/Q63ZW7 ^@ 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 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||InaD-like protein|||L27|||PDZ|||PDZ 1|||PDZ 10|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||PDZ 7|||PDZ 8|||PDZ 9|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000094593|||http://purl.uniprot.org/annotation/VSP_014210|||http://purl.uniprot.org/annotation/VSP_014211|||http://purl.uniprot.org/annotation/VSP_014212|||http://purl.uniprot.org/annotation/VSP_014213|||http://purl.uniprot.org/annotation/VSP_014214|||http://purl.uniprot.org/annotation/VSP_014215|||http://purl.uniprot.org/annotation/VSP_014216|||http://purl.uniprot.org/annotation/VSP_014217|||http://purl.uniprot.org/annotation/VSP_014218 http://togogenome.org/gene/10090:Zmym5 ^@ http://purl.uniprot.org/uniprot/Q3U2E2 ^@ Chain|||Crosslink|||Modification|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Crosslink|||Region|||Zinc Finger ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||MYM-type 1|||MYM-type 2; degenerate|||MYM-type 4|||MYM-type 5|||Zinc finger MYM-type protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000343663 http://togogenome.org/gene/10090:Fam228a ^@ http://purl.uniprot.org/uniprot/Q8CDW1 ^@ 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|||Protein FAM228A ^@ http://purl.uniprot.org/annotation/PRO_0000348446|||http://purl.uniprot.org/annotation/VSP_035162|||http://purl.uniprot.org/annotation/VSP_035163 http://togogenome.org/gene/10090:Zc3h12d ^@ http://purl.uniprot.org/uniprot/E9QNR7|||http://purl.uniprot.org/uniprot/Q8BIY3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ C3H1-type|||Disordered|||Necessary for interaction with ZC3H12A|||Probable ribonuclease ZC3H12D|||RNase NYN ^@ http://purl.uniprot.org/annotation/PRO_0000348932 http://togogenome.org/gene/10090:Crebbp ^@ http://purl.uniprot.org/uniprot/A0A0U1RQB6|||http://purl.uniprot.org/uniprot/F8VPR5|||http://purl.uniprot.org/uniprot/Q6GQV9 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Site|||Zinc Finger ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||Bromo|||CBP/p300-type HAT|||Disordered|||KIX|||Polar residues|||Pro residues|||TAZ-type|||ZZ-type ^@ http://togogenome.org/gene/10090:Or10ag2 ^@ http://purl.uniprot.org/uniprot/A2AT85 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Star ^@ http://purl.uniprot.org/uniprot/P51557 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||Phosphoserine; by PKA|||START|||Steroidogenic acute regulatory protein, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000033318 http://togogenome.org/gene/10090:Adam1a ^@ http://purl.uniprot.org/uniprot/Q3V0H1|||http://purl.uniprot.org/uniprot/Q60813 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 1a|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B ^@ http://purl.uniprot.org/annotation/PRO_0000029032|||http://purl.uniprot.org/annotation/PRO_0000029033 http://togogenome.org/gene/10090:Tk2 ^@ http://purl.uniprot.org/uniprot/Q8BN51 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Region ^@ Deoxynucleoside kinase|||Disordered|||Proton acceptor ^@ http://togogenome.org/gene/10090:Dhx34 ^@ http://purl.uniprot.org/uniprot/A0A0R4J217|||http://purl.uniprot.org/uniprot/Q66JM5|||http://purl.uniprot.org/uniprot/Q9DBV3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Probable ATP-dependent RNA helicase DHX34 ^@ http://purl.uniprot.org/annotation/PRO_0000055167 http://togogenome.org/gene/10090:Gkn2 ^@ http://purl.uniprot.org/uniprot/Q9CQS6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ BRICHOS|||Gastrokine-2 ^@ http://purl.uniprot.org/annotation/PRO_0000252105 http://togogenome.org/gene/10090:Srsf12 ^@ http://purl.uniprot.org/uniprot/Q8C8K3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||Pro residues|||Serine/arginine-rich splicing factor 12 ^@ http://purl.uniprot.org/annotation/PRO_0000395111 http://togogenome.org/gene/10090:Kif23 ^@ http://purl.uniprot.org/uniprot/E9Q5G3 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Kinesin motor|||Kinesin-like protein KIF23|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000425085 http://togogenome.org/gene/10090:Ark2c ^@ http://purl.uniprot.org/uniprot/E9QAU8 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Region|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase ARK2C|||RING-type; atypical|||Ubiquitin binding ^@ http://purl.uniprot.org/annotation/PRO_0000415819 http://togogenome.org/gene/10090:Lyz2 ^@ http://purl.uniprot.org/uniprot/A0A077S2U6|||http://purl.uniprot.org/uniprot/P08905 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Strand|||Turn ^@ C-type lysozyme|||Glycosyl hydrolases family 22 (GH22)|||Lysozyme C-2 ^@ http://purl.uniprot.org/annotation/PRO_0000018472|||http://purl.uniprot.org/annotation/PRO_5014216937 http://togogenome.org/gene/10090:Ncaph2 ^@ http://purl.uniprot.org/uniprot/E9PY48|||http://purl.uniprot.org/uniprot/Q8BSP2 ^@ 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|||Condensin II complex subunit H2 N-terminal|||Condensin II complex subunit H2 middle|||Condensin-2 complex subunit H2|||Condensin-2 complex subunit H2 C-terminal|||Disordered|||In Nessy.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000326242|||http://purl.uniprot.org/annotation/VSP_032641|||http://purl.uniprot.org/annotation/VSP_032642 http://togogenome.org/gene/10090:Akap6 ^@ http://purl.uniprot.org/uniprot/E9Q9K8|||http://purl.uniprot.org/uniprot/Q3UHI8|||http://purl.uniprot.org/uniprot/Q3UHR2|||http://purl.uniprot.org/uniprot/Q6PGB9|||http://purl.uniprot.org/uniprot/Q6ZQD9 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Dock9 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLE0|||http://purl.uniprot.org/uniprot/A0A1D5RMM1|||http://purl.uniprot.org/uniprot/A0A5F8MPL9|||http://purl.uniprot.org/uniprot/E9QMR2|||http://purl.uniprot.org/uniprot/F8VPN7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Disordered|||PH ^@ http://togogenome.org/gene/10090:Pnpla6 ^@ http://purl.uniprot.org/uniprot/A0A140LI54|||http://purl.uniprot.org/uniprot/Q3TRM4 ^@ 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|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cyclic nucleotide-binding|||Cytoplasmic|||DGA/G|||Disordered|||GXGXXG|||GXSXG|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PNPLA|||Patatin-like phospholipase domain-containing protein 6|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000292200|||http://purl.uniprot.org/annotation/VSP_026390|||http://purl.uniprot.org/annotation/VSP_026391|||http://purl.uniprot.org/annotation/VSP_026392|||http://purl.uniprot.org/annotation/VSP_026393 http://togogenome.org/gene/10090:Mark2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0B1|||http://purl.uniprot.org/uniprot/A0A0R4J227|||http://purl.uniprot.org/uniprot/E9QMP6|||http://purl.uniprot.org/uniprot/Q05512|||http://purl.uniprot.org/uniprot/Q3T9A3 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||KA1|||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|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase MARK2|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000086302|||http://purl.uniprot.org/annotation/VSP_013341|||http://purl.uniprot.org/annotation/VSP_013342|||http://purl.uniprot.org/annotation/VSP_022597 http://togogenome.org/gene/10090:Trpm3 ^@ http://purl.uniprot.org/uniprot/B2RUS0|||http://purl.uniprot.org/uniprot/D3Z539|||http://purl.uniprot.org/uniprot/E9PUC8|||http://purl.uniprot.org/uniprot/J9SVL3|||http://purl.uniprot.org/uniprot/Q5F4S6|||http://purl.uniprot.org/uniprot/Q5F4S7|||http://purl.uniprot.org/uniprot/Q5F4S8|||http://purl.uniprot.org/uniprot/Q5F4S9|||http://purl.uniprot.org/uniprot/Q5F4T0|||http://purl.uniprot.org/uniprot/Q69ZE8|||http://purl.uniprot.org/uniprot/Q8BIH6 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Ion transport|||Polar residues|||TRPM SLOG|||TRPM tetramerisation ^@ http://togogenome.org/gene/10090:Or5au1 ^@ http://purl.uniprot.org/uniprot/B2RVX8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp583 ^@ http://purl.uniprot.org/uniprot/Q3V080 ^@ 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 583 ^@ http://purl.uniprot.org/annotation/PRO_0000047675 http://togogenome.org/gene/10090:Hnf1a ^@ http://purl.uniprot.org/uniprot/P22361|||http://purl.uniprot.org/uniprot/Q66JY7 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Dimerization|||Disordered|||HNF-p1|||Hepatocyte nuclear factor 1-alpha|||Homeobox|||Homeobox; HNF1-type|||Interaction with DNA|||Nuclear localization signal|||POU-specific atypical|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000049116 http://togogenome.org/gene/10090:Gpx5 ^@ http://purl.uniprot.org/uniprot/P21765|||http://purl.uniprot.org/uniprot/Q496Q2|||http://purl.uniprot.org/uniprot/Q8CC60|||http://purl.uniprot.org/uniprot/Q8CDQ5 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide ^@ Epididymal secretory glutathione peroxidase|||Glutathione peroxidase ^@ http://purl.uniprot.org/annotation/PRO_0000013078|||http://purl.uniprot.org/annotation/PRO_5004304423|||http://purl.uniprot.org/annotation/PRO_5014309315 http://togogenome.org/gene/10090:Gsdmc3 ^@ http://purl.uniprot.org/uniprot/Q8CB12 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Gasdermin-C3|||Gasdermin-C3, C-terminal|||Gasdermin-C3, N-terminal|||Triggers pyroptosis ^@ http://purl.uniprot.org/annotation/PRO_0000347332|||http://purl.uniprot.org/annotation/PRO_0000451680|||http://purl.uniprot.org/annotation/PRO_0000451681 http://togogenome.org/gene/10090:Cav2 ^@ http://purl.uniprot.org/uniprot/Q924U4|||http://purl.uniprot.org/uniprot/Q9WVC3 ^@ Chain|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Modified Residue|||Topological Domain|||Transmembrane ^@ Caveolin-2|||Cytoplasmic|||Helical|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by SRC ^@ http://purl.uniprot.org/annotation/PRO_0000144138 http://togogenome.org/gene/10090:Gmds ^@ http://purl.uniprot.org/uniprot/Q8K0C9 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ GDP-mannose 4,6 dehydratase|||N-acetylalanine|||Nucleophile|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000201706 http://togogenome.org/gene/10090:Vmp1 ^@ http://purl.uniprot.org/uniprot/Q99KU0 ^@ 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|||Extracellular|||Helical|||N-acetylalanine|||Removed|||VTT domain|||Vacuole membrane protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000284547 http://togogenome.org/gene/10090:Btk ^@ http://purl.uniprot.org/uniprot/P35991 ^@ 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|||Turn|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger ^@ Btk-type|||CAV1-binding|||Constitutive activation.|||Disordered|||In XID; prevents interaction with ARID3A.|||Inositol-(1,3,4,5)-tetrakisphosphate 1-binding|||Loss of activity and no phosphorylation.|||N-acetylalanine|||No autophosphorylation.|||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_0000088066 http://togogenome.org/gene/10090:Ubxn2b ^@ http://purl.uniprot.org/uniprot/Q0KL01 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||SEP|||UBX|||UBX domain-containing protein 2B ^@ http://purl.uniprot.org/annotation/PRO_0000315229 http://togogenome.org/gene/10090:Nkx2-9 ^@ http://purl.uniprot.org/uniprot/O70584 ^@ 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-2.8|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048944 http://togogenome.org/gene/10090:Nckap5l ^@ http://purl.uniprot.org/uniprot/Q6GQX2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ (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|||Basic and acidic residues|||Disordered|||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|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000288448 http://togogenome.org/gene/10090:Clrn3 ^@ http://purl.uniprot.org/uniprot/Q8BHH8 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Clarin-3|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000274699 http://togogenome.org/gene/10090:Helz ^@ http://purl.uniprot.org/uniprot/Q6DFV5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C3H1-type|||DEAA box|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Probable helicase with zinc finger domain ^@ http://purl.uniprot.org/annotation/PRO_0000354096|||http://purl.uniprot.org/annotation/VSP_035795|||http://purl.uniprot.org/annotation/VSP_035796|||http://purl.uniprot.org/annotation/VSP_035797 http://togogenome.org/gene/10090:Marchf3 ^@ http://purl.uniprot.org/uniprot/Q8BRX9 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Transmembrane|||Zinc Finger ^@ E3 ubiquitin-protein ligase MARCHF3|||Helical|||RING-CH-type ^@ http://purl.uniprot.org/annotation/PRO_0000055928 http://togogenome.org/gene/10090:Tnfaip8l3 ^@ http://purl.uniprot.org/uniprot/Q3TBL6 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Mutagenesis Site|||Region ^@ Binding to phosphoinositides|||Disordered|||Reduces binding to phosphoinositide.|||Reduces binding to phosphoinositide; when associated with Gln-109.|||Reduces binding to phosphoinositide; when associated with Gln-33; Gln-34 and Gln-38.|||Reduces binding to phosphoinositide; when associated with Gln-33; Gln-34 and Gln-42.|||Reduces binding to phosphoinositide; when associated with Gln-33; Gln-38 and Gln-42.|||Reduces binding to phosphoinositide; when associated with Gln-34; Gln-38 and Gln-42.|||Reduces binding to phosphoinositide; when associated with Gln-93.|||Tumor necrosis factor alpha-induced protein 8-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000331425 http://togogenome.org/gene/10090:Rps9 ^@ http://purl.uniprot.org/uniprot/Q6ZWN5 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||S4 RNA-binding|||Small ribosomal subunit protein uS4 ^@ http://purl.uniprot.org/annotation/PRO_0000132690 http://togogenome.org/gene/10090:Son ^@ http://purl.uniprot.org/uniprot/Q80TM4|||http://purl.uniprot.org/uniprot/Q8C9T5|||http://purl.uniprot.org/uniprot/Q9QX47 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||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]|||13 X 10 AA tandem repeats of L-A-[ST]-[NSG]-[TS]-MDSQM|||14 X 6 AA repeats of [ED]-R-S-M-M-S|||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; approximate|||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; approximate|||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 isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||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_0000072038|||http://purl.uniprot.org/annotation/VSP_004416|||http://purl.uniprot.org/annotation/VSP_004417|||http://purl.uniprot.org/annotation/VSP_041557|||http://purl.uniprot.org/annotation/VSP_041558 http://togogenome.org/gene/10090:Eif5a ^@ http://purl.uniprot.org/uniprot/P63242 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Eukaryotic translation initiation factor 5A-1|||Hypusine|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization regulation|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000142452 http://togogenome.org/gene/10090:Leng9 ^@ http://purl.uniprot.org/uniprot/Q8BTN6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger ^@ C3H1-type|||Disordered|||Leukocyte receptor cluster member 9|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000415826 http://togogenome.org/gene/10090:Eef1akmt4 ^@ http://purl.uniprot.org/uniprot/P0DPE0 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict ^@ EEF1A lysine methyltransferase 4|||Phosphotyrosine|||Required for methyltransferase activity ^@ http://purl.uniprot.org/annotation/PRO_0000443291 http://togogenome.org/gene/10090:Gm15127 ^@ http://purl.uniprot.org/uniprot/B1AVZ5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Oat ^@ http://purl.uniprot.org/uniprot/P29758 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Ornithine aminotransferase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000001264 http://togogenome.org/gene/10090:Vcam1 ^@ http://purl.uniprot.org/uniprot/Q3UPN1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097488 http://togogenome.org/gene/10090:Pced1b ^@ http://purl.uniprot.org/uniprot/Q8BGX1 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||PC-esterase domain-containing protein 1B ^@ http://purl.uniprot.org/annotation/PRO_0000331357 http://togogenome.org/gene/10090:Lrrn4 ^@ http://purl.uniprot.org/uniprot/P59383 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||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|||Leucine-rich repeat neuronal protein 4|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000021030 http://togogenome.org/gene/10090:Lce3f ^@ http://purl.uniprot.org/uniprot/Q6PAI4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Frmpd1 ^@ http://purl.uniprot.org/uniprot/A2AKB4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||FERM|||FERM and PDZ domain-containing protein 1|||Important for interaction with GPSM2|||PDZ|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000306806 http://togogenome.org/gene/10090:Or10s1 ^@ http://purl.uniprot.org/uniprot/Q8VGB3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc31a2 ^@ http://purl.uniprot.org/uniprot/Q4KL43|||http://purl.uniprot.org/uniprot/Q9CPU9|||http://purl.uniprot.org/uniprot/Q9D524 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Phosphoserine|||Phosphothreonine|||Protein SLC31A2 ^@ http://purl.uniprot.org/annotation/PRO_0000195044 http://togogenome.org/gene/10090:Pfkp ^@ http://purl.uniprot.org/uniprot/Q8C605|||http://purl.uniprot.org/uniprot/Q9WUA3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant ^@ ATP-dependent 6-phosphofructokinase, platelet type|||C-terminal regulatory PFK domain 2|||In isoform 2.|||In strain: C57BL/6.|||In strain: C57BL/6J.|||In strain: LG/J and NOD.|||In strain: NOD.|||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_0000112025|||http://purl.uniprot.org/annotation/VSP_016664|||http://purl.uniprot.org/annotation/VSP_016665 http://togogenome.org/gene/10090:Prkag1 ^@ http://purl.uniprot.org/uniprot/O54950|||http://purl.uniprot.org/uniprot/Q3TWR3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 5'-AMP-activated protein kinase subunit gamma-1|||AMPK pseudosubstrate|||CBS|||CBS 1|||CBS 2|||CBS 3|||CBS 4|||Disordered|||Phosphoserine; by ULK1|||Phosphothreonine; by ULK1 ^@ http://purl.uniprot.org/annotation/PRO_0000204378 http://togogenome.org/gene/10090:Lcn12 ^@ http://purl.uniprot.org/uniprot/Q2TA58|||http://purl.uniprot.org/uniprot/Q6JVL5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Epididymal-specific lipocalin-12|||Lipocalin/cytosolic fatty-acid binding|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017923|||http://purl.uniprot.org/annotation/PRO_5009970471 http://togogenome.org/gene/10090:Miip ^@ http://purl.uniprot.org/uniprot/A2A7Y5|||http://purl.uniprot.org/uniprot/C0KL25 ^@ 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.|||Migration and invasion-inhibitory protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000324323|||http://purl.uniprot.org/annotation/VSP_032215 http://togogenome.org/gene/10090:Or2aj6 ^@ http://purl.uniprot.org/uniprot/G5E8J1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Prm3 ^@ http://purl.uniprot.org/uniprot/Q62100 ^@ 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|||Basic and acidic residues|||Disordered|||Phosphoserine|||Protamine-3 ^@ http://purl.uniprot.org/annotation/PRO_0000106638 http://togogenome.org/gene/10090:Slc26a10 ^@ http://purl.uniprot.org/uniprot/F8WGV3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||STAS ^@ http://togogenome.org/gene/10090:Or8b4 ^@ http://purl.uniprot.org/uniprot/Q9EQA9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dpy19l2 ^@ http://purl.uniprot.org/uniprot/P0CW70 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Disordered|||Helical|||Nuclear|||Perinuclear space|||Probable C-mannosyltransferase DPY19L2 ^@ http://purl.uniprot.org/annotation/PRO_0000408327 http://togogenome.org/gene/10090:Igf2r ^@ http://purl.uniprot.org/uniprot/Q07113|||http://purl.uniprot.org/uniprot/Q8C6V9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cation-independent mannose-6-phosphate receptor|||Cytoplasmic|||Disordered|||Fibronectin type-II|||Helical|||Lumenal|||MRH|||MRH 1|||MRH 10|||MRH 11|||MRH 12|||MRH 13|||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_0000019230 http://togogenome.org/gene/10090:Atp6v1fnb ^@ http://purl.uniprot.org/uniprot/B9EJX3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Pro residues|||Protein SPMIP1 ^@ http://purl.uniprot.org/annotation/PRO_0000444982 http://togogenome.org/gene/10090:Mlx ^@ http://purl.uniprot.org/uniprot/A2BFB0|||http://purl.uniprot.org/uniprot/A2BFB1|||http://purl.uniprot.org/uniprot/A2BFB2|||http://purl.uniprot.org/uniprot/O08609|||http://purl.uniprot.org/uniprot/Q3UQB4 ^@ 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 ^@ BHLH|||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_0000127280|||http://purl.uniprot.org/annotation/VSP_002139|||http://purl.uniprot.org/annotation/VSP_002140 http://togogenome.org/gene/10090:Gm815 ^@ http://purl.uniprot.org/uniprot/Q3UWS2 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015097510 http://togogenome.org/gene/10090:Zap70 ^@ http://purl.uniprot.org/uniprot/P43404 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In ST; causes an absence of mature T-cells due to thymocyte development being arrested at the CD4+CD8+ stage.|||In isoform 2.|||In isoform 3.|||Interdomain A|||Interdomain B|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by LCK|||Polar residues|||Protein kinase|||Proton acceptor|||SH2 1|||SH2 2|||Tyrosine-protein kinase ZAP-70 ^@ http://purl.uniprot.org/annotation/PRO_0000088169|||http://purl.uniprot.org/annotation/VSP_031159|||http://purl.uniprot.org/annotation/VSP_031160|||http://purl.uniprot.org/annotation/VSP_031161 http://togogenome.org/gene/10090:Rxfp1 ^@ http://purl.uniprot.org/uniprot/Q6R6I7 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||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|||LDL-receptor class A|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-linked (GlcNAc...) asparagine|||Relaxin receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000303887 http://togogenome.org/gene/10090:Nos2 ^@ http://purl.uniprot.org/uniprot/P29477 ^@ 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 ^@ Calmodulin-binding|||DINNN-motif; mediates interaction with SPSB1, SPSB2 and SPSB4|||Disordered|||FAD-binding FR-type|||Flavodoxin-like|||In strain: BALB/CBYJ.|||In strain: NOD/LtJ.|||In strain: SJL/J.|||Loss of interaction with SPSB2.|||Nitric oxide synthase, inducible|||Phosphotyrosine|||Polar residues|||Reduced interaction with SPSB2.|||Significant loss of interaction with SPSB2.|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000170934 http://togogenome.org/gene/10090:Sms ^@ http://purl.uniprot.org/uniprot/P97355 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ N-acetylalanine|||PABS|||Phosphoserine|||Proton acceptor|||Removed|||Spermine synthase ^@ http://purl.uniprot.org/annotation/PRO_0000156539 http://togogenome.org/gene/10090:Nr2f2 ^@ http://purl.uniprot.org/uniprot/D3YYP4|||http://purl.uniprot.org/uniprot/P43135|||http://purl.uniprot.org/uniprot/Q3UST6 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Abolishes interaction with ZFPM2.|||COUP transcription factor 2|||Disordered|||Important for dimerization|||Interaction with ZFPM2|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000053607 http://togogenome.org/gene/10090:Abcd3 ^@ http://purl.uniprot.org/uniprot/P55096 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||ATP-binding cassette sub-family D member 3|||Helical|||Interaction with PEX19|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000093310 http://togogenome.org/gene/10090:H2al1n ^@ http://purl.uniprot.org/uniprot/Q497L1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Histone H2A/H2B/H3 ^@ http://togogenome.org/gene/10090:Tex29 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSS2|||http://purl.uniprot.org/uniprot/Q9DA77 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Pro residues|||Testis-expressed protein 29 ^@ http://purl.uniprot.org/annotation/PRO_0000358917 http://togogenome.org/gene/10090:Sh2b1 ^@ http://purl.uniprot.org/uniprot/Q91ZM2 ^@ 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.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||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_0000323594|||http://purl.uniprot.org/annotation/VSP_032029|||http://purl.uniprot.org/annotation/VSP_032030|||http://purl.uniprot.org/annotation/VSP_032031|||http://purl.uniprot.org/annotation/VSP_032032|||http://purl.uniprot.org/annotation/VSP_032033|||http://purl.uniprot.org/annotation/VSP_032034 http://togogenome.org/gene/10090:Pabpc4 ^@ http://purl.uniprot.org/uniprot/A3KFU5|||http://purl.uniprot.org/uniprot/A3KFU8|||http://purl.uniprot.org/uniprot/Q6PHQ9|||http://purl.uniprot.org/uniprot/Q91YZ8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PABC|||Polar residues|||RRM ^@ http://togogenome.org/gene/10090:Ip6k3 ^@ http://purl.uniprot.org/uniprot/Q8BWD2 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Inositol hexakisphosphate kinase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000066882 http://togogenome.org/gene/10090:Gja3 ^@ http://purl.uniprot.org/uniprot/A0A654ICY8|||http://purl.uniprot.org/uniprot/Q3UWF8|||http://purl.uniprot.org/uniprot/Q64448 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||INTRAMEM|||Initiator Methionine|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Initiator Methionine|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction alpha-3 protein|||Gap junction protein cysteine-rich|||Helical|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057811 http://togogenome.org/gene/10090:Rasgef1a ^@ http://purl.uniprot.org/uniprot/A0A0N4SVF2|||http://purl.uniprot.org/uniprot/A6H650|||http://purl.uniprot.org/uniprot/Q3TYC0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ N-terminal Ras-GEF|||Ras-GEF ^@ http://togogenome.org/gene/10090:Mlxip ^@ http://purl.uniprot.org/uniprot/B2RQ56|||http://purl.uniprot.org/uniprot/G5E8D8|||http://purl.uniprot.org/uniprot/Q2VPU4 ^@ 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 ^@ BHLH|||Disordered|||In isoform 2.|||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_0000298764|||http://purl.uniprot.org/annotation/VSP_052505|||http://purl.uniprot.org/annotation/VSP_052506 http://togogenome.org/gene/10090:Car3 ^@ http://purl.uniprot.org/uniprot/P16015 ^@ 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|||Region|||Sequence Conflict ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase 3|||Involved in proton transfer|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||S-glutathionyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000077427 http://togogenome.org/gene/10090:Prss1 ^@ http://purl.uniprot.org/uniprot/Q9Z1R9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015101037 http://togogenome.org/gene/10090:Usb1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0E0|||http://purl.uniprot.org/uniprot/Q91W78 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict ^@ Disordered|||Proton acceptor|||Proton donor|||Proton donor/acceptor|||U6 snRNA phosphodiesterase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000274392 http://togogenome.org/gene/10090:Rap2b ^@ http://purl.uniprot.org/uniprot/P61226 ^@ 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 association with membranes.|||No reduction of association with the recycling endosome membranes and does activate TNIK; when associated with G-176.|||No reduction of association with the recycling endosome membranes and does activate TNIK; when associated with G-177.|||Ras-related protein Rap-2b|||Removed in mature form|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000030217|||http://purl.uniprot.org/annotation/PRO_0000030218 http://togogenome.org/gene/10090:Cenpp ^@ http://purl.uniprot.org/uniprot/B2RVI6|||http://purl.uniprot.org/uniprot/Q9CZ92 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Centromere protein P|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000249507|||http://purl.uniprot.org/annotation/VSP_020449|||http://purl.uniprot.org/annotation/VSP_020450 http://togogenome.org/gene/10090:Sec22b ^@ http://purl.uniprot.org/uniprot/O08547 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Longin|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Vesicle-trafficking protein SEC22b|||v-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000206771 http://togogenome.org/gene/10090:Ces5a ^@ http://purl.uniprot.org/uniprot/Q6AW46 ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Acyl-ester intermediate|||Carboxylesterase 5A|||Charge relay system|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000308592 http://togogenome.org/gene/10090:Tmem67 ^@ http://purl.uniprot.org/uniprot/A2AJP5|||http://purl.uniprot.org/uniprot/E9QNI1|||http://purl.uniprot.org/uniprot/Q8BR76 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||INTRAMEM|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cysteine-rich|||Cytoplasmic|||Discontinuously helical; Name=4|||Discontinuously helical; Name=5|||Discontinuously helical; Name=6|||Disordered|||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 isoform 2.|||Meckelin|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000225690|||http://purl.uniprot.org/annotation/VSP_017417|||http://purl.uniprot.org/annotation/VSP_017418 http://togogenome.org/gene/10090:Mrnip ^@ http://purl.uniprot.org/uniprot/Q9D1F5 ^@ 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|||MRN complex-interacting protein|||Necessary for the association with the MRN complex|||Nuclear localization signal (NLS)|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000326120 http://togogenome.org/gene/10090:Ppp4r2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0U2|||http://purl.uniprot.org/uniprot/Q0VGB7 ^@ 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|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Serine/threonine-protein phosphatase 4 regulatory subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000299366 http://togogenome.org/gene/10090:Methig1 ^@ http://purl.uniprot.org/uniprot/Q76I26 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ HIG1|||Helical ^@ http://togogenome.org/gene/10090:Or6c65 ^@ http://purl.uniprot.org/uniprot/Q8VGI8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Camk2g ^@ http://purl.uniprot.org/uniprot/Q6ZWS7|||http://purl.uniprot.org/uniprot/Q8BW40|||http://purl.uniprot.org/uniprot/Q923T9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolished calmodulin-dependent protein kinase activity. Abolished ability to phosphorylate STAT1.|||Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase type II subunit gamma|||Calmodulin-binding|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086102|||http://purl.uniprot.org/annotation/VSP_004779|||http://purl.uniprot.org/annotation/VSP_004780 http://togogenome.org/gene/10090:Nfe2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Y5|||http://purl.uniprot.org/uniprot/Q07279 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes phosphorylation by PKA. No effect on ability to bind DNA nor on transactivation activity.|||BZIP|||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 SUMO1); alternate|||Leucine-zipper|||Loss of MAPK8-mediated phosphorylation and no protein degradation.|||Loss of transactivation activity. No induction of histone H3 'K-4' acetylation.|||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_0000320078 http://togogenome.org/gene/10090:Vmn2r29 ^@ http://purl.uniprot.org/uniprot/L7N2D4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982290 http://togogenome.org/gene/10090:Crybb2 ^@ http://purl.uniprot.org/uniprot/P62696 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Beta-crystallin B2|||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|||N-acetylalanine|||N-terminal arm|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057555 http://togogenome.org/gene/10090:Atp6v1e2 ^@ http://purl.uniprot.org/uniprot/Q9D593 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ V-type proton ATPase subunit E 2 ^@ http://purl.uniprot.org/annotation/PRO_0000282345 http://togogenome.org/gene/10090:Zfp296 ^@ http://purl.uniprot.org/uniprot/E9Q6W4 ^@ 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 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)|||Polar residues|||Zinc finger protein 296 ^@ http://purl.uniprot.org/annotation/PRO_0000436774 http://togogenome.org/gene/10090:Zftraf1 ^@ http://purl.uniprot.org/uniprot/P0DW87 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Region|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform 1.|||In isoform 6 and isoform 7.|||In isoform 6.|||RING-type; degenerate|||TRAF-type|||Zinc finger TRAF-type-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000328853|||http://purl.uniprot.org/annotation/VSP_061641|||http://purl.uniprot.org/annotation/VSP_061642|||http://purl.uniprot.org/annotation/VSP_061643 http://togogenome.org/gene/10090:Prkdc ^@ http://purl.uniprot.org/uniprot/P97313 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant ^@ Activation loop|||Catalytic loop|||Cleavage; by caspase-3|||DNA-dependent protein kinase catalytic subunit|||Disordered|||FAT|||FATC|||G-loop|||HEAT 1|||HEAT 2|||HEAT 3|||In SCID.|||In isoform 2.|||Interaction with C1D|||KIP-binding|||Lethal at 4-week-old; impaired hematopoiesis due to a decrease in hematopoietic stem and progenitor cells which causes a severe reduction in the numbers of erythrocytes, platelets, lymphocytes and neutrophils; reduced protein synthesis in bone marrow and fetal erythrocyte precursors; normal V(D)J recombination in B-cells; when associated with 2614-A--A-2616, A-2634 and A-2643.|||Lethal at 4-week-old; impaired hematopoiesis due to a decrease in hematopoietic stem and progenitor cells which causes a severe reduction in the numbers of erythrocytes, platelets, lymphocytes and neutrophils; reduced protein synthesis in bone marrow and fetal erythrocyte precursors; normal V(D)J recombination in B-cells; when associated with A-2605, 2614-A--A-2616 and A-2634.|||Lethal at 4-week-old; impaired hematopoiesis due to a decrease in hematopoietic stem and progenitor cells which causes a severe reduction in the numbers of erythrocytes, platelets, lymphocytes and neutrophils; reduced protein synthesis in bone marrow and fetal erythrocyte precursors; normal V(D)J recombination in B-cells; when associated with A-2605, 2614-A--A-2616 and A-2643.|||Lethal at 4-week-old; impaired hematopoiesis due to a decrease in hematopoietic stem and progenitor cells which causes a severe reduction in the numbers of erythrocytes, platelets, lymphocytes and neutrophils; reduced protein synthesis in bone marrow and fetal erythrocyte precursors; normal V(D)J recombination in B-cells; when associated with A-2605, A-2634 and A-2643.|||Leucine-zipper|||N6-acetyllysine|||Normal erythrocyte and platelet numbers; when associated with A-2026 and 2050-A--A-2053.|||Normal erythrocyte and platelet numbers; when associated with A-2026 and A-2038.|||Normal erythrocyte and platelet numbers; when associated with A-2038 and 2050-A--A-2053.|||PI3K/PI4K catalytic|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Probable loss of catalytic activity. Severe reduction in the number of hematopoietic stem and progenitor cells in fetal liver. Slight reduction in translation during erythrocyte development in fetal liver.|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000225599|||http://purl.uniprot.org/annotation/VSP_017361|||http://purl.uniprot.org/annotation/VSP_017362 http://togogenome.org/gene/10090:Nrg4 ^@ http://purl.uniprot.org/uniprot/Q9WTX4 ^@ 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_0000019487|||http://purl.uniprot.org/annotation/PRO_0000019488 http://togogenome.org/gene/10090:Vmn1r174 ^@ http://purl.uniprot.org/uniprot/E9PYW5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hs2st1 ^@ http://purl.uniprot.org/uniprot/Q8R3H7 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate 2-O-sulfotransferase 1|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000207675 http://togogenome.org/gene/10090:Supt20 ^@ http://purl.uniprot.org/uniprot/Q7TT00 ^@ 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|||Transcription factor SPT20 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000187040|||http://purl.uniprot.org/annotation/VSP_014880|||http://purl.uniprot.org/annotation/VSP_014881|||http://purl.uniprot.org/annotation/VSP_014882 http://togogenome.org/gene/10090:Psma7 ^@ http://purl.uniprot.org/uniprot/Q3UIT9|||http://purl.uniprot.org/uniprot/Q542H2|||http://purl.uniprot.org/uniprot/Q9Z2U0 ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Strand|||Turn ^@ 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_0000124143 http://togogenome.org/gene/10090:Tbl3 ^@ http://purl.uniprot.org/uniprot/Q8C4J7 ^@ Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ 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_0000362980 http://togogenome.org/gene/10090:A430005L14Rik ^@ http://purl.uniprot.org/uniprot/E9PUH0|||http://purl.uniprot.org/uniprot/Q80WR5 ^@ 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|||UPF0688 protein C1orf174 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000294245 http://togogenome.org/gene/10090:Slc25a43 ^@ http://purl.uniprot.org/uniprot/A2A3V2 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Repeat|||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 43 ^@ http://purl.uniprot.org/annotation/PRO_0000291824 http://togogenome.org/gene/10090:Myl6b ^@ http://purl.uniprot.org/uniprot/Q8CI43 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Myosin light chain 6B ^@ http://purl.uniprot.org/annotation/PRO_0000248833 http://togogenome.org/gene/10090:Tardbp ^@ http://purl.uniprot.org/uniprot/Q544R5|||http://purl.uniprot.org/uniprot/Q6VYI4|||http://purl.uniprot.org/uniprot/Q6VYI5|||http://purl.uniprot.org/uniprot/Q8BLD4|||http://purl.uniprot.org/uniprot/Q8BUM1|||http://purl.uniprot.org/uniprot/Q8R0B4|||http://purl.uniprot.org/uniprot/Q921F2 ^@ 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)|||Interaction with UBQLN2|||Omega-N-methylarginine|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||TAR DNA-binding protein 43 ^@ http://purl.uniprot.org/annotation/PRO_0000081973 http://togogenome.org/gene/10090:Kmt5a ^@ http://purl.uniprot.org/uniprot/A0A0G2JFK5|||http://purl.uniprot.org/uniprot/D3YXI6|||http://purl.uniprot.org/uniprot/E9QNB8|||http://purl.uniprot.org/uniprot/Q2YDW7|||http://purl.uniprot.org/uniprot/Q8C1L9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||N-lysine methyltransferase KMT5A|||Phosphoserine|||Phosphothreonine|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000228689 http://togogenome.org/gene/10090:Scube2 ^@ http://purl.uniprot.org/uniprot/D3YVM9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ CUB|||EGF-like ^@ http://purl.uniprot.org/annotation/PRO_5003052938 http://togogenome.org/gene/10090:Arf2 ^@ http://purl.uniprot.org/uniprot/Q8BSL7 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Strand|||Turn ^@ ADP-ribosylation factor 2|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207384 http://togogenome.org/gene/10090:Ctrl ^@ http://purl.uniprot.org/uniprot/Q9ER05 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015099720 http://togogenome.org/gene/10090:Flg2 ^@ http://purl.uniprot.org/uniprot/Q2VIS4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||Filaggrin 1|||Filaggrin 10|||Filaggrin 11|||Filaggrin 12|||Filaggrin 2|||Filaggrin 3|||Filaggrin 4|||Filaggrin 5|||Filaggrin 6|||Filaggrin 7|||Filaggrin 8|||Filaggrin 9|||Filaggrin-2|||Phosphoserine|||Polar residues|||S-100-like ^@ http://purl.uniprot.org/annotation/PRO_0000331455 http://togogenome.org/gene/10090:Rrm2b ^@ http://purl.uniprot.org/uniprot/Q6PEE3 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Region ^@ Disordered|||Ribonucleoside-diphosphate reductase subunit M2 B ^@ http://purl.uniprot.org/annotation/PRO_0000228152 http://togogenome.org/gene/10090:Nudt14 ^@ http://purl.uniprot.org/uniprot/A0A217FL49|||http://purl.uniprot.org/uniprot/Q9D142 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Motif|||Sequence Conflict ^@ Nudix box|||Nudix hydrolase|||Uridine diphosphate glucose pyrophosphatase NUDT14 ^@ http://purl.uniprot.org/annotation/PRO_0000057114 http://togogenome.org/gene/10090:Tube1 ^@ http://purl.uniprot.org/uniprot/Q9D6T1 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Tubulin epsilon chain ^@ http://purl.uniprot.org/annotation/PRO_0000233352 http://togogenome.org/gene/10090:Psg16 ^@ http://purl.uniprot.org/uniprot/D0VY58|||http://purl.uniprot.org/uniprot/Q60962|||http://purl.uniprot.org/uniprot/Q8K0U8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Samd4b ^@ http://purl.uniprot.org/uniprot/G5E8A7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Pro residues|||SAM ^@ http://togogenome.org/gene/10090:Tyr ^@ http://purl.uniprot.org/uniprot/P11344|||http://purl.uniprot.org/uniprot/Q91XK0 ^@ Binding Site|||Chain|||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|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In albino mice.|||In chinchilla mice.|||In strain: Himalayan.|||Lumenal, melanosome|||N-linked (GlcNAc...) asparagine|||Tyrosinase|||Tyrosinase copper-binding ^@ http://purl.uniprot.org/annotation/PRO_0000035880|||http://purl.uniprot.org/annotation/PRO_5014312448 http://togogenome.org/gene/10090:Acot4 ^@ http://purl.uniprot.org/uniprot/Q14DI6|||http://purl.uniprot.org/uniprot/Q8BWN8 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict ^@ Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase|||BAAT/Acyl-CoA thioester hydrolase C-terminal|||Charge relay system|||Microbody targeting signal|||N6-succinyllysine|||Peroxisomal succinyl-coenzyme A thioesterase ^@ http://purl.uniprot.org/annotation/PRO_0000202150 http://togogenome.org/gene/10090:Pelo ^@ http://purl.uniprot.org/uniprot/Q80X73 ^@ 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)|||Phosphoserine|||Protein pelota homolog ^@ http://purl.uniprot.org/annotation/PRO_0000143189 http://togogenome.org/gene/10090:Crispld2 ^@ http://purl.uniprot.org/uniprot/Q8BZQ2 ^@ 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 LCCL domain-containing 2|||In isoform 2.|||LCCL 1|||LCCL 2|||N-linked (GlcNAc...) asparagine|||SCP ^@ http://purl.uniprot.org/annotation/PRO_0000363885|||http://purl.uniprot.org/annotation/VSP_036331 http://togogenome.org/gene/10090:Ccn6 ^@ http://purl.uniprot.org/uniprot/D3Z5L9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ CTCK|||Cellular communication network factor 6|||IGFBP N-terminal|||N-linked (GlcNAc...) asparagine|||TSP type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000415855 http://togogenome.org/gene/10090:Mfsd14a ^@ http://purl.uniprot.org/uniprot/P70187 ^@ 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_0000084857 http://togogenome.org/gene/10090:Glmp ^@ http://purl.uniprot.org/uniprot/Q9JHJ3 ^@ Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes lysosomal localization and results in mislocalization to the cell surface. Localizes to lysosomes when expressed with wild-type MFSD1.|||Cytoplasmic|||Glycosylated lysosomal membrane protein|||Helical|||Lumenal|||Lysosomal targeting motif|||N-linked (GlcNAc...) asparagine|||No effect on glycosylation.|||Reduced glycosylation. ^@ http://purl.uniprot.org/annotation/PRO_0000284485 http://togogenome.org/gene/10090:Cul9 ^@ http://purl.uniprot.org/uniprot/S4R1Y1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Cullin family profile|||DOC|||Disordered|||Polar residues|||RING-type ^@ http://togogenome.org/gene/10090:Wnk2 ^@ http://purl.uniprot.org/uniprot/E9QM73|||http://purl.uniprot.org/uniprot/E9QMI8|||http://purl.uniprot.org/uniprot/E9QMI9|||http://purl.uniprot.org/uniprot/Q3UH66 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic residues|||Disordered|||In isoform 2.|||In isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7.|||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 6.|||In isoform 7.|||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_0000278774|||http://purl.uniprot.org/annotation/VSP_023366|||http://purl.uniprot.org/annotation/VSP_023367|||http://purl.uniprot.org/annotation/VSP_023368|||http://purl.uniprot.org/annotation/VSP_023369|||http://purl.uniprot.org/annotation/VSP_023370|||http://purl.uniprot.org/annotation/VSP_023371|||http://purl.uniprot.org/annotation/VSP_023372|||http://purl.uniprot.org/annotation/VSP_023373|||http://purl.uniprot.org/annotation/VSP_023374 http://togogenome.org/gene/10090:Cdyl2 ^@ http://purl.uniprot.org/uniprot/Q9D5D8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Chromo|||Chromodomain Y-like protein 2|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000424594 http://togogenome.org/gene/10090:Fah ^@ http://purl.uniprot.org/uniprot/P35505 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn ^@ Decrease in activity.|||Fumarylacetoacetase|||N-acetylserine|||Phosphoserine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000156826 http://togogenome.org/gene/10090:Lpar5 ^@ http://purl.uniprot.org/uniprot/G3X9K0|||http://purl.uniprot.org/uniprot/Q149R9 ^@ 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; 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 ^@ http://purl.uniprot.org/annotation/PRO_0000303236 http://togogenome.org/gene/10090:Nicn1 ^@ http://purl.uniprot.org/uniprot/Q9CQM0 ^@ Chain|||Molecule Processing ^@ Chain ^@ Nicolin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000096815 http://togogenome.org/gene/10090:Xlr5b ^@ http://purl.uniprot.org/uniprot/A2BI50 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Cc2d1b ^@ http://purl.uniprot.org/uniprot/Q8BRN9 ^@ 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 ^@ C2|||Coiled-coil and C2 domain-containing protein 1B|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288427 http://togogenome.org/gene/10090:Speer1 ^@ http://purl.uniprot.org/uniprot/F6X687 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:Atp9a ^@ http://purl.uniprot.org/uniprot/O70228|||http://purl.uniprot.org/uniprot/Q505G9|||http://purl.uniprot.org/uniprot/Q8C288|||http://purl.uniprot.org/uniprot/Q8C4G3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cytoplasmic|||Extracellular|||Helical|||N-acetylthreonine|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Probable phospholipid-transporting ATPase IIA|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000046376 http://togogenome.org/gene/10090:Tcf24 ^@ http://purl.uniprot.org/uniprot/V9GWT9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BHLH|||Disordered ^@ http://togogenome.org/gene/10090:Raly ^@ http://purl.uniprot.org/uniprot/Q3U3F6|||http://purl.uniprot.org/uniprot/Q64012 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||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 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_0000081747|||http://purl.uniprot.org/annotation/VSP_005805 http://togogenome.org/gene/10090:Vstm2l ^@ http://purl.uniprot.org/uniprot/A2ACD2|||http://purl.uniprot.org/uniprot/Q6PDS0 ^@ 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|||Ig-like|||Pro residues|||V-set and transmembrane domain-containing protein 2-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000015165|||http://purl.uniprot.org/annotation/PRO_5002642228 http://togogenome.org/gene/10090:Mrpl21 ^@ http://purl.uniprot.org/uniprot/Q9D1N9 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant|||Transit Peptide ^@ Chain|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Large ribosomal subunit protein bL21m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000252443|||http://purl.uniprot.org/annotation/VSP_020975 http://togogenome.org/gene/10090:Btc ^@ http://purl.uniprot.org/uniprot/Q05928|||http://purl.uniprot.org/uniprot/Q3TP84|||http://purl.uniprot.org/uniprot/Q543J8 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Betacellulin|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like domain-containing protein|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Probetacellulin|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000007492|||http://purl.uniprot.org/annotation/PRO_0000007493|||http://purl.uniprot.org/annotation/PRO_0000300686|||http://purl.uniprot.org/annotation/PRO_5004229545|||http://purl.uniprot.org/annotation/PRO_5014309610 http://togogenome.org/gene/10090:Hspb6 ^@ http://purl.uniprot.org/uniprot/Q5EBG6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Deamidated glutamine|||Heat shock protein beta-6|||Involved in stabilization of the HSPB1:HSBP6 heterodimer|||Phosphoserine|||sHSP ^@ http://purl.uniprot.org/annotation/PRO_0000246077 http://togogenome.org/gene/10090:Adamts15 ^@ http://purl.uniprot.org/uniprot/P59384 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ A disintegrin and metalloproteinase with thrombospondin motifs 15|||Basic and acidic residues|||Cleavage; by furin|||Cysteine switch|||Disintegrin|||Disordered|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Reduced glycosylation.|||Reduced propeptide cleavage.|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000078212|||http://purl.uniprot.org/annotation/PRO_0000270787 http://togogenome.org/gene/10090:Tram1l1 ^@ http://purl.uniprot.org/uniprot/Q8QZR0 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||TLC|||Translocating chain-associated membrane protein 1-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000313707 http://togogenome.org/gene/10090:Ercc8 ^@ http://purl.uniprot.org/uniprot/Q8CFD5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ DNA excision repair protein ERCC-8|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000050971 http://togogenome.org/gene/10090:Marcks ^@ http://purl.uniprot.org/uniprot/P26645 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Calmodulin-binding (PSD)|||Disordered|||Myristoylated alanine-rich C-kinase substrate|||N-myristoyl glycine|||Phosphoserine|||Phosphoserine; by MAPK|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues|||Poorly phosphorylated.|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000157149 http://togogenome.org/gene/10090:Tgtp2 ^@ http://purl.uniprot.org/uniprot/Q3T9E4|||http://purl.uniprot.org/uniprot/Q62293 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Turn ^@ IRG-type G|||T-cell-specific guanine nucleotide triphosphate-binding protein 1|||T-cell-specific guanine nucleotide triphosphate-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000437942|||http://purl.uniprot.org/annotation/PRO_0000437943 http://togogenome.org/gene/10090:Bcl2l2 ^@ http://purl.uniprot.org/uniprot/P70345 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant ^@ BH1|||BH2|||BH4|||Bcl-2-like protein 2|||In isoform 2.|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000143067|||http://purl.uniprot.org/annotation/VSP_014780 http://togogenome.org/gene/10090:Ccnh ^@ http://purl.uniprot.org/uniprot/E9PWD3|||http://purl.uniprot.org/uniprot/Q61458 ^@ 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|||Cyclin-H|||Cyclin-like|||Disordered|||Phosphoserine|||Phosphoserine; by CDK8|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000080472 http://togogenome.org/gene/10090:Trmt2a ^@ http://purl.uniprot.org/uniprot/E9PUQ7|||http://purl.uniprot.org/uniprot/Q8BNV1 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||Nucleophile|||Phosphoserine|||Proton acceptor|||RRM|||tRNA (uracil-5-)-methyltransferase homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000081615|||http://purl.uniprot.org/annotation/VSP_061469 http://togogenome.org/gene/10090:Gatd3a ^@ http://purl.uniprot.org/uniprot/Q9D172 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ Glutamine amidotransferase-like class 1 domain-containing protein 3, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000008545 http://togogenome.org/gene/10090:Scn8a ^@ http://purl.uniprot.org/uniprot/A0A0J9YUW5|||http://purl.uniprot.org/uniprot/A0A0R5RP22|||http://purl.uniprot.org/uniprot/F6U329|||http://purl.uniprot.org/uniprot/F7D6J5|||http://purl.uniprot.org/uniprot/F7D6K4|||http://purl.uniprot.org/uniprot/Q9WTU3 ^@ 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|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Decrease in sensitivity to the scorpion toxin BMKM1.|||Decreases interaction with CALM1 in the absence of calcium.|||Decreases interaction with CALM1 in the presence and absence of calcium and reduces rate of channel inactivation.|||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 isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In medjo.|||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|||Pore-forming|||Sodium channel protein type 8 subunit alpha|||Sodium ion transport-associated|||Voltage-gated Na+ ion channel cytoplasmic ^@ http://purl.uniprot.org/annotation/PRO_0000048501|||http://purl.uniprot.org/annotation/VSP_050594|||http://purl.uniprot.org/annotation/VSP_050595|||http://purl.uniprot.org/annotation/VSP_050596|||http://purl.uniprot.org/annotation/VSP_050597|||http://purl.uniprot.org/annotation/VSP_050598 http://togogenome.org/gene/10090:Or4f14 ^@ http://purl.uniprot.org/uniprot/A2BFL7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp426 ^@ http://purl.uniprot.org/uniprot/G5E8Y1|||http://purl.uniprot.org/uniprot/Q8R1D1 ^@ 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 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_0000284700 http://togogenome.org/gene/10090:Dse ^@ http://purl.uniprot.org/uniprot/Q8BLI4 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Critical for catalysis|||Cytoplasmic|||Dermatan-sulfate epimerase|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000223312 http://togogenome.org/gene/10090:Cyp2c55 ^@ http://purl.uniprot.org/uniprot/Q9D816 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Cytochrome P450 2C55|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000282959 http://togogenome.org/gene/10090:Emilin1 ^@ http://purl.uniprot.org/uniprot/Q99K41 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ C1q|||Collagen-like|||Disordered|||EMI|||EMILIN-1|||N-linked (GlcNAc...) asparagine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000007816 http://togogenome.org/gene/10090:Rit2 ^@ http://purl.uniprot.org/uniprot/P70425 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict ^@ Constitutively active. Dramatic reduction of the rate of GTP hydrolysis.|||Dominant negative. Loss of interaction with AFDN, RLF and RALGDS.|||GTP-binding protein Rit2|||Loss of interaction with AFDN, RLF and RALGDS; when associated with L-78. ^@ http://purl.uniprot.org/annotation/PRO_0000082728 http://togogenome.org/gene/10090:Tas2r130 ^@ http://purl.uniprot.org/uniprot/P59530 ^@ 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 7 ^@ http://purl.uniprot.org/annotation/PRO_0000082217 http://togogenome.org/gene/10090:Cyp4a32 ^@ http://purl.uniprot.org/uniprot/A2A8T1 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Adamtsl3 ^@ http://purl.uniprot.org/uniprot/G3UXC7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Ig-like|||PLAC ^@ http://purl.uniprot.org/annotation/PRO_5003457027 http://togogenome.org/gene/10090:Smim29 ^@ http://purl.uniprot.org/uniprot/Q8R043 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Small integral membrane protein 29 ^@ http://purl.uniprot.org/annotation/PRO_0000019540 http://togogenome.org/gene/10090:Hacd3 ^@ http://purl.uniprot.org/uniprot/Q8K2C9 ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CS|||Cytoplasmic|||Helical|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000313725 http://togogenome.org/gene/10090:Il36a ^@ http://purl.uniprot.org/uniprot/Q9JLA2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Propeptide ^@ Chain|||Modified Residue|||Propeptide ^@ 3'-nitrotyrosine|||Interleukin-36 alpha ^@ http://purl.uniprot.org/annotation/PRO_0000153645|||http://purl.uniprot.org/annotation/PRO_0000430546 http://togogenome.org/gene/10090:Ddi2 ^@ http://purl.uniprot.org/uniprot/A2ADY9 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein DDI1 homolog 2|||Ubiquitin-binding|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000287091 http://togogenome.org/gene/10090:Pgf ^@ http://purl.uniprot.org/uniprot/P49764|||http://purl.uniprot.org/uniprot/Q544A5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||Interchain|||N-linked (GlcNAc...) asparagine|||Placenta growth factor|||Platelet-derived growth factor (PDGF) family profile|||Platelet-derived growth factor (PDGF) family profile domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000023421|||http://purl.uniprot.org/annotation/PRO_5009971091 http://togogenome.org/gene/10090:Map2k4 ^@ http://purl.uniprot.org/uniprot/P47809|||http://purl.uniprot.org/uniprot/Q543X6|||http://purl.uniprot.org/uniprot/Q8K2U0 ^@ 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|||Region ^@ Asymmetric dimethylarginine; alternate|||D domain|||DVD domain|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 4|||Loss of ATP-binding.|||N-acetylalanine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000086382 http://togogenome.org/gene/10090:Or2d36 ^@ http://purl.uniprot.org/uniprot/Q9EPG6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nucb2 ^@ http://purl.uniprot.org/uniprot/P81117|||http://purl.uniprot.org/uniprot/Q3TV28 ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Binds to necdin|||Disordered|||EF-hand 1|||EF-hand 2|||GBA|||Nesfatin-1|||Nucleobindin-2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000004166|||http://purl.uniprot.org/annotation/PRO_0000419820|||http://purl.uniprot.org/annotation/PRO_5004229706 http://togogenome.org/gene/10090:Dner ^@ http://purl.uniprot.org/uniprot/Q8JZM4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||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|||Fails to be restricted to the somatodendritic compartment.|||Helical|||Interaction with AP1G1 and somatodendritic targeting|||Interaction with NOTCH1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000253558 http://togogenome.org/gene/10090:Eef1a1 ^@ http://purl.uniprot.org/uniprot/P10126|||http://purl.uniprot.org/uniprot/Q58E64 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 5-glutamyl glycerylphosphorylethanolamine|||Elongation factor 1-alpha 1|||G1|||G2|||G3|||G4|||G5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N,N,N-trimethylglycine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3|||N6,N6,N6-trimethyllysine; by EEF1AKMT1|||N6,N6,N6-trimethyllysine; by EEF1AKMT2|||N6,N6-dimethyllysine|||N6,N6-dimethyllysine; alternate|||N6,N6-dimethyllysine; alternate; by EEF1AKMT3|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||N6-methyllysine; alternate; by EEF1AKMT3|||N6-succinyllysine; alternate|||Phosphoserine; by TGFBR1|||Phosphothreonine; by PASK|||Removed|||Tr-type G|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000090886 http://togogenome.org/gene/10090:Il12rb1 ^@ http://purl.uniprot.org/uniprot/A0A1D5RL98|||http://purl.uniprot.org/uniprot/Q60837 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Interleukin-12 receptor subunit beta-1|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010918|||http://purl.uniprot.org/annotation/PRO_5008929766 http://togogenome.org/gene/10090:Abcg4 ^@ http://purl.uniprot.org/uniprot/Q91WA9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ABC transporter|||ATP-binding cassette subfamily G member 4|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6 ^@ http://purl.uniprot.org/annotation/PRO_0000453165 http://togogenome.org/gene/10090:Bola3 ^@ http://purl.uniprot.org/uniprot/Q8CEI1 ^@ Chain|||Molecule Processing ^@ Chain ^@ BolA-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000245502 http://togogenome.org/gene/10090:Gm14124 ^@ http://purl.uniprot.org/uniprot/A2AU83 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Vav3 ^@ http://purl.uniprot.org/uniprot/Q9R0C8 ^@ 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 ^@ Calponin-homology (CH)|||DH|||Guanine nucleotide exchange factor VAV3|||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_0000080987|||http://purl.uniprot.org/annotation/VSP_042360|||http://purl.uniprot.org/annotation/VSP_042361|||http://purl.uniprot.org/annotation/VSP_042362|||http://purl.uniprot.org/annotation/VSP_042363 http://togogenome.org/gene/10090:Abcc2 ^@ http://purl.uniprot.org/uniprot/Q8VI47 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000093357 http://togogenome.org/gene/10090:Tekt3 ^@ http://purl.uniprot.org/uniprot/Q6X6Z7 ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Modification|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Glycosylation Site ^@ N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Tektin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000184569 http://togogenome.org/gene/10090:Krt6b ^@ http://purl.uniprot.org/uniprot/Q3UV11 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||IF rod|||Polar residues ^@ http://togogenome.org/gene/10090:C9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J032|||http://purl.uniprot.org/uniprot/P06683 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Beta stranded|||Complement component C9|||EGF-like|||LDL-receptor class A|||MACPF|||N-linked (GlcNAc...) asparagine|||TSP type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000023605|||http://purl.uniprot.org/annotation/PRO_5015044281 http://togogenome.org/gene/10090:Yod1 ^@ http://purl.uniprot.org/uniprot/Q8CB27 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Strand|||Turn|||Zinc Finger ^@ C2H2-type|||Cys-loop|||His-loop|||Nucleophile|||OTU|||S2 site|||UBX-like|||Ubiquitin thioesterase OTU1|||Variable-loop ^@ http://purl.uniprot.org/annotation/PRO_0000282357 http://togogenome.org/gene/10090:Cep170b ^@ http://purl.uniprot.org/uniprot/Q80U49 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000282890|||http://purl.uniprot.org/annotation/VSP_024249 http://togogenome.org/gene/10090:Abtb2 ^@ http://purl.uniprot.org/uniprot/Q3T9J9|||http://purl.uniprot.org/uniprot/Q7TQI7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat and BTB/POZ domain-containing protein 2|||BTB ^@ http://purl.uniprot.org/annotation/PRO_0000066888 http://togogenome.org/gene/10090:Gpr25 ^@ http://purl.uniprot.org/uniprot/P0C5I1 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||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|||Probable G-protein coupled receptor 25 ^@ http://purl.uniprot.org/annotation/PRO_0000307093 http://togogenome.org/gene/10090:Samhd1 ^@ http://purl.uniprot.org/uniprot/Q60710 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ (Microbial infection) Phosphothreonine|||Deoxynucleoside triphosphate triphosphohydrolase SAMHD1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HD|||In LCH mutant; abolishes formation of the tetramer and deoxynucleoside triphosphate (dNTPase) activity; when associated with C-112 and H-143.|||In LCH mutant; abolishes formation of the tetramer and deoxynucleoside triphosphate (dNTPase) activity; when associated with L-109 and C-112.|||In LCH mutant; abolishes formation of the tetramer and deoxynucleoside triphosphate (dNTPase) activity; when associated with L-109 and H-143.|||In isoform 2.|||Increased ability to restrict LINE-1 retrotransposon activity.|||Mimicks phosphorylation state, reduced ability to restrict LINE-1 retrotransposon activity.|||Phosphoserine|||Phosphothreonine|||SAM|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000153733|||http://purl.uniprot.org/annotation/VSP_059661 http://togogenome.org/gene/10090:Rprm ^@ http://purl.uniprot.org/uniprot/Q9JJ72 ^@ 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|||Phosphoserine|||Protein reprimo ^@ http://purl.uniprot.org/annotation/PRO_0000312753 http://togogenome.org/gene/10090:Dnm3 ^@ http://purl.uniprot.org/uniprot/Q8BZ98 ^@ 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 ^@ Disordered|||Dynamin-3|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||GED|||In isoform 2.|||N6-acetyllysine|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000319951|||http://purl.uniprot.org/annotation/VSP_031548 http://togogenome.org/gene/10090:Sos1 ^@ http://purl.uniprot.org/uniprot/Q3USK4|||http://purl.uniprot.org/uniprot/Q62245 ^@ 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|||DH|||Disordered|||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_0000068895 http://togogenome.org/gene/10090:Colq ^@ http://purl.uniprot.org/uniprot/E9PVR3|||http://purl.uniprot.org/uniprot/O35348 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide ^@ Acetylcholinesterase collagenic tail peptide|||Basic and acidic residues|||Collagen-like 1|||Collagen-like 2|||Disordered|||Heparan sulfate proteoglycan binding|||Interchain|||Interchain (with T subunit)|||PRAD|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000059415|||http://purl.uniprot.org/annotation/PRO_5003244257 http://togogenome.org/gene/10090:Ipp ^@ http://purl.uniprot.org/uniprot/P28575 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ Actin-binding protein IPP|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6 ^@ http://purl.uniprot.org/annotation/PRO_0000119076 http://togogenome.org/gene/10090:Amotl1 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VM69|||http://purl.uniprot.org/uniprot/Q9D4H4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Angiomotin C-terminal|||Angiomotin-like protein 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||PDZ-binding|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000190671|||http://purl.uniprot.org/annotation/VSP_044080 http://togogenome.org/gene/10090:Tppp3 ^@ http://purl.uniprot.org/uniprot/Q9CRB6 ^@ Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand ^@ Basic and acidic residues|||Disordered|||N-acetylalanine|||Removed|||Tubulin polymerization-promoting protein family member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000221139 http://togogenome.org/gene/10090:Fam83h ^@ http://purl.uniprot.org/uniprot/Q148V8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Mediates interaction with CSNK1A1 and is required for FAM83H activity in keratin cytoskeleton organization|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein FAM83H ^@ http://purl.uniprot.org/annotation/PRO_0000324489 http://togogenome.org/gene/10090:Gabrp ^@ http://purl.uniprot.org/uniprot/Q8QZW7 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit pi|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000000493 http://togogenome.org/gene/10090:Rpl10 ^@ http://purl.uniprot.org/uniprot/Q6ZWV3 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Crosslink|||Modified Residue|||Sequence Conflict ^@ Citrulline|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Large ribosomal subunit protein uL16 ^@ http://purl.uniprot.org/annotation/PRO_0000147107 http://togogenome.org/gene/10090:Bpifb6 ^@ http://purl.uniprot.org/uniprot/Q8BU51 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ BPI fold-containing family B member 6|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017169 http://togogenome.org/gene/10090:Pimreg ^@ http://purl.uniprot.org/uniprot/Q8BFY7 ^@ 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|||D-box 1|||D-box 2|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphoserine; by Uhmk1; in vitro|||Polar residues|||Protein PIMREG ^@ http://purl.uniprot.org/annotation/PRO_0000281160|||http://purl.uniprot.org/annotation/VSP_023998 http://togogenome.org/gene/10090:Plin1 ^@ http://purl.uniprot.org/uniprot/Q8CGN5 ^@ 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.|||In isoform 3.|||In isoform 4.|||Perilipin-1|||Phosphoserine|||Phosphothreonine|||Required for interaction with CIDEC ^@ http://purl.uniprot.org/annotation/PRO_0000099885|||http://purl.uniprot.org/annotation/VSP_038204|||http://purl.uniprot.org/annotation/VSP_038205|||http://purl.uniprot.org/annotation/VSP_038206|||http://purl.uniprot.org/annotation/VSP_038207|||http://purl.uniprot.org/annotation/VSP_038208|||http://purl.uniprot.org/annotation/VSP_038209 http://togogenome.org/gene/10090:Nfs1 ^@ http://purl.uniprot.org/uniprot/Q9CTB2|||http://purl.uniprot.org/uniprot/Q9Z1J3 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Transit Peptide ^@ Cysteine desulfurase|||Cysteine persulfide|||Cysteine persulfide intermediate|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||via persulfide group ^@ http://purl.uniprot.org/annotation/PRO_0000001294 http://togogenome.org/gene/10090:Pkhd1 ^@ http://purl.uniprot.org/uniprot/E9PZ36|||http://purl.uniprot.org/uniprot/Q6T3A5|||http://purl.uniprot.org/uniprot/Q8CIS7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Almost completely blocks the ability to traffic to cilia. Disrupts interaction with RAB8A. Disrupts interaction with ARF4.|||Almost completely blocks the ability to traffic to the cilia; when associated with 3872-A-A-3873. Affects palmitoylation; when associated with 3872-A-A-3873. Disrupts interaction with RAB8A; when associated with 3872-A-A-3873. Disrupts interaction with ARF4; when associated with 3872-A-A-3873.|||Almost completely blocks the ability to traffic to the cilia; when associated with A-3869. Affetcs palmitoylation; when associated with A-3869. Disrupts interaction with RAB8A; when associated with A-3869. Disrupts interaction with ARF4; when associated with A-3869.|||Basic and acidic residues|||Ciliary targeting sequence (CST)|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Fibrocystin|||G8|||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|||Little affects the ability to traffic to the cilia. Does not affect interaction with RAB8A. Does not affect interaction with ARF4.|||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|||Prevents ciliary localizytion.|||Reduces the ability to traffic to the cilia.|||Reduces the ability to traffic to the cilia. Reduces interaction with RAB8A.|||Reduces the ability to traffic to the cilia. Reduces interaction with RAB8A. Does not affect interaction with ARF4. ^@ http://purl.uniprot.org/annotation/PRO_5003243036|||http://purl.uniprot.org/annotation/PRO_5004280003|||http://purl.uniprot.org/annotation/PRO_5004304482 http://togogenome.org/gene/10090:Hook1 ^@ http://purl.uniprot.org/uniprot/Q8BIL5 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Calponin-homology (CH)|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Protein Hook homolog 1|||Sufficient for interaction with AKTIP and VPS18|||Sufficient for interaction with microtubules ^@ http://purl.uniprot.org/annotation/PRO_0000219193|||http://purl.uniprot.org/annotation/VSP_009340|||http://purl.uniprot.org/annotation/VSP_009341 http://togogenome.org/gene/10090:Or52ae9 ^@ http://purl.uniprot.org/uniprot/Q0VBH3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Helb ^@ http://purl.uniprot.org/uniprot/Q6NVF4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Accumulation in the nucleus due to defects in nuclear export.|||Acidic residues|||Basic and acidic residues|||DNA helicase B|||Disordered|||No ATPase activity.|||Nuclear export signal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000338993 http://togogenome.org/gene/10090:Or4c125 ^@ http://purl.uniprot.org/uniprot/Q8VGN0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:EU599041 ^@ http://purl.uniprot.org/uniprot/B2M0R7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type ^@ http://togogenome.org/gene/10090:Batf2 ^@ http://purl.uniprot.org/uniprot/Q8R1H8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Basic leucine zipper transcriptional factor ATF-like 2|||Basic motif|||Disordered|||In isoform 2.|||Leucine-zipper|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000288682|||http://purl.uniprot.org/annotation/VSP_025753 http://togogenome.org/gene/10090:Lig3 ^@ http://purl.uniprot.org/uniprot/Q3UC82|||http://purl.uniprot.org/uniprot/Q80ZH7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ ATP-dependent DNA ligase family profile|||BRCT|||Disordered|||PARP-type|||Polar residues ^@ http://togogenome.org/gene/10090:Sox2 ^@ http://purl.uniprot.org/uniprot/P48432|||http://purl.uniprot.org/uniprot/Q60I23 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 9aaTAD|||Absence of sumoylation. Increased FGF4 activation. No effect on nuclear localization.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||HMG box|||N6-methyllysine|||Phosphoserine|||Polar residues|||Transcription factor SOX-2 ^@ http://purl.uniprot.org/annotation/PRO_0000048716 http://togogenome.org/gene/10090:Cox7a1 ^@ http://purl.uniprot.org/uniprot/P56392|||http://purl.uniprot.org/uniprot/Q792A4 ^@ 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_0000006150 http://togogenome.org/gene/10090:Ndufb11b ^@ http://purl.uniprot.org/uniprot/Q9CQ68 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_5015099655 http://togogenome.org/gene/10090:1700001F09Rik ^@ http://purl.uniprot.org/uniprot/Q9DAR5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ttc22 ^@ http://purl.uniprot.org/uniprot/Q8C159 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||Tetratricopeptide repeat protein 22 ^@ http://purl.uniprot.org/annotation/PRO_0000263099 http://togogenome.org/gene/10090:Naaladl2 ^@ http://purl.uniprot.org/uniprot/A0A0N4SUJ3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:1810065E05Rik ^@ http://purl.uniprot.org/uniprot/Q5NC41|||http://purl.uniprot.org/uniprot/Q9D8K1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5004260251|||http://purl.uniprot.org/annotation/PRO_5004324573 http://togogenome.org/gene/10090:H6pd ^@ http://purl.uniprot.org/uniprot/A2A7A7|||http://purl.uniprot.org/uniprot/Q8CFX1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 6-phosphogluconolactonase|||GDH/6PGL endoplasmic bifunctional protein|||Glucosamine/galactosamine-6-phosphate isomerase|||Glucose-6-phosphate dehydrogenase C-terminal|||Glucose-6-phosphate dehydrogenase NAD-binding|||Hexose-6-phosphate dehydrogenase|||Linker|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Proton acceptor|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000236794|||http://purl.uniprot.org/annotation/PRO_5002642186 http://togogenome.org/gene/10090:Bmp6 ^@ http://purl.uniprot.org/uniprot/P20722|||http://purl.uniprot.org/uniprot/Q3UXB2|||http://purl.uniprot.org/uniprot/Q8BRW3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Bone morphogenetic protein 6|||Disordered|||Interchain|||N-linked (GlcNAc...) asparagine|||Polar residues|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033872|||http://purl.uniprot.org/annotation/PRO_0000033873 http://togogenome.org/gene/10090:Lcn4 ^@ http://purl.uniprot.org/uniprot/Q24JQ8|||http://purl.uniprot.org/uniprot/Q62472 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding|||Vomeronasal secretory protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000017979|||http://purl.uniprot.org/annotation/PRO_5014308475 http://togogenome.org/gene/10090:Zfp493 ^@ http://purl.uniprot.org/uniprot/E9Q1L8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Cdk14 ^@ http://purl.uniprot.org/uniprot/O35495|||http://purl.uniprot.org/uniprot/Q6NVF8|||http://purl.uniprot.org/uniprot/Q8BFX6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Cyclin-dependent kinase 14|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086507|||http://purl.uniprot.org/annotation/VSP_038763|||http://purl.uniprot.org/annotation/VSP_038764 http://togogenome.org/gene/10090:Gng8 ^@ http://purl.uniprot.org/uniprot/P63078|||http://purl.uniprot.org/uniprot/Q3UMY0 ^@ 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-8|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000012651|||http://purl.uniprot.org/annotation/PRO_0000012652 http://togogenome.org/gene/10090:Slco1b2 ^@ http://purl.uniprot.org/uniprot/Q9JJL3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Disulfide Bond|||Domain Extent|||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.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Solute carrier organic anion transporter family member 1B2 ^@ http://purl.uniprot.org/annotation/PRO_0000191051|||http://purl.uniprot.org/annotation/VSP_006149 http://togogenome.org/gene/10090:Coa3 ^@ http://purl.uniprot.org/uniprot/Q9D2R6 ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytochrome c oxidase assembly factor 3 homolog, mitochondrial|||Disordered|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000239439 http://togogenome.org/gene/10090:Gja1 ^@ http://purl.uniprot.org/uniprot/A0A654ICD2|||http://purl.uniprot.org/uniprot/P23242|||http://purl.uniprot.org/uniprot/Q8C4N2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction alpha-1 protein|||Gap junction alpha-1 protein (Cx43) C-terminal|||Gap junction protein cysteine-rich|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||Interaction with NOV|||Interaction with UBQLN4|||Phosphoserine|||Phosphoserine; by PKC/PRKCG and PKC/PRKCD|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000057802 http://togogenome.org/gene/10090:Sbk3 ^@ http://purl.uniprot.org/uniprot/P0C5K0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Acidic residues|||Disordered|||In isoform 2.|||Protein kinase|||Proton acceptor|||Uncharacterized serine/threonine-protein kinase SBK3 ^@ http://purl.uniprot.org/annotation/PRO_0000308263|||http://purl.uniprot.org/annotation/VSP_053507 http://togogenome.org/gene/10090:Nrep ^@ http://purl.uniprot.org/uniprot/Q07475|||http://purl.uniprot.org/uniprot/Q542Q5 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Neuronal regeneration-related protein ^@ http://purl.uniprot.org/annotation/PRO_0000057938 http://togogenome.org/gene/10090:Fitm2 ^@ http://purl.uniprot.org/uniprot/P59266 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Acyl-coenzyme A diphosphatase FITM2|||Cytoplasmic|||Decreased specific binding to triglyceride. Decreased lipid droplet size. No change in protein expression levels and subcellular localization to the ER.|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000021036 http://togogenome.org/gene/10090:Il10ra ^@ http://purl.uniprot.org/uniprot/H3BKN6|||http://purl.uniprot.org/uniprot/Q3U6I9|||http://purl.uniprot.org/uniprot/Q3UDL4|||http://purl.uniprot.org/uniprot/Q3UDV8|||http://purl.uniprot.org/uniprot/Q3UE89|||http://purl.uniprot.org/uniprot/Q61727 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Complete loss of STAT3 activation; in association with F-443.|||Complete loss of STAT3 activation; in association with F-493.|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III domain-containing protein|||Helical|||Interleukin-10 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000011013|||http://purl.uniprot.org/annotation/PRO_5003581443|||http://purl.uniprot.org/annotation/PRO_5004229839|||http://purl.uniprot.org/annotation/PRO_5004230061|||http://purl.uniprot.org/annotation/PRO_5010843415 http://togogenome.org/gene/10090:Rer1 ^@ http://purl.uniprot.org/uniprot/Q9CQU3 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Transmembrane ^@ Helical|||N-acetylserine|||Phosphoserine|||Protein RER1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207590 http://togogenome.org/gene/10090:Pgap6 ^@ http://purl.uniprot.org/uniprot/Q9ESN3 ^@ 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|||EGF-like|||Extracellular|||Helical|||In isoform Beta.|||N-linked (GlcNAc...) asparagine|||Post-GPI attachment to proteins factor 6 ^@ http://purl.uniprot.org/annotation/PRO_0000022540|||http://purl.uniprot.org/annotation/VSP_004005 http://togogenome.org/gene/10090:Armc12 ^@ http://purl.uniprot.org/uniprot/Q80X86 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ ARM 1|||ARM 2|||ARM 3|||Armadillo repeat-containing protein 12|||Disordered|||Interaction with TBC1D15 ^@ http://purl.uniprot.org/annotation/PRO_0000230164 http://togogenome.org/gene/10090:Slc9a5 ^@ http://purl.uniprot.org/uniprot/B2RXE2 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||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|||Sodium/hydrogen exchanger 5 ^@ http://purl.uniprot.org/annotation/PRO_5015087168 http://togogenome.org/gene/10090:Fam131b ^@ http://purl.uniprot.org/uniprot/E9Q8P8|||http://purl.uniprot.org/uniprot/Q3TY60 ^@ 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|||Phosphothreonine|||Polar residues|||Protein FAM131B ^@ http://purl.uniprot.org/annotation/PRO_0000253033|||http://purl.uniprot.org/annotation/VSP_020994|||http://purl.uniprot.org/annotation/VSP_020995 http://togogenome.org/gene/10090:Or4d11 ^@ http://purl.uniprot.org/uniprot/Q8VFV0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Krt8 ^@ http://purl.uniprot.org/uniprot/P11679 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Asymmetric dimethylarginine; alternate|||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|||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 MAPK|||Phosphoserine; by PKC/PRKCE|||Phosphothreonine|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063741 http://togogenome.org/gene/10090:Polb ^@ http://purl.uniprot.org/uniprot/Q8K409 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ DNA polymerase beta|||DNA-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N6-acetyllysine|||Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity|||Omega-N-methylarginine; by PRMT6 ^@ http://purl.uniprot.org/annotation/PRO_0000218779 http://togogenome.org/gene/10090:Ppp1r2 ^@ http://purl.uniprot.org/uniprot/Q9DCL8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||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|||Required for binding the 'RVXF' binding groove of PPP1CC ^@ http://purl.uniprot.org/annotation/PRO_0000071482 http://togogenome.org/gene/10090:Cibar2 ^@ http://purl.uniprot.org/uniprot/Q3V2J0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ BAR-like|||CBY1-interacting BAR domain-containing protein 2|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000333005 http://togogenome.org/gene/10090:Smad9 ^@ http://purl.uniprot.org/uniprot/Q3UVC6|||http://purl.uniprot.org/uniprot/Q9JIW5 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant ^@ Disordered|||MH1|||MH2|||Mothers against decapentaplegic homolog 9 ^@ http://purl.uniprot.org/annotation/PRO_0000090876 http://togogenome.org/gene/10090:Pkdcc ^@ http://purl.uniprot.org/uniprot/Q5RJI4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||Complete loss of kinase activity.|||Complete loss of kinase activity. Phosphorylation is restored by co-transfection with wild-type protein.|||Disordered|||Does not affect kinase activity nor secretion to the extracellular medium.|||Extracellular tyrosine-protein kinase PKDCC|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000263011|||http://purl.uniprot.org/annotation/VSP_038822 http://togogenome.org/gene/10090:Dph5 ^@ http://purl.uniprot.org/uniprot/Q9CWQ0 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ Diphthine methyl ester synthase|||Most homozygous embryos are non-viable and show craniofacial, ophthalmologic, cardiac, visceral, and hemopoietic abnormalities.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000156134 http://togogenome.org/gene/10090:Lypd10 ^@ http://purl.uniprot.org/uniprot/Q810N3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_5015098933 http://togogenome.org/gene/10090:Gm10354 ^@ http://purl.uniprot.org/uniprot/K7N6A0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or4k35 ^@ http://purl.uniprot.org/uniprot/Q8VF41 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tuba1c ^@ http://purl.uniprot.org/uniprot/P68373|||http://purl.uniprot.org/uniprot/Q52L87 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Site ^@ 3'-nitrotyrosine|||Detyrosinated tubulin alpha-1C chain|||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_0000048124|||http://purl.uniprot.org/annotation/PRO_0000437395 http://togogenome.org/gene/10090:Eaf1 ^@ http://purl.uniprot.org/uniprot/Q9D4C5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||ELL-associated factor 1|||Necessary for transactivation activity|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000130335 http://togogenome.org/gene/10090:Rab11fip1 ^@ http://purl.uniprot.org/uniprot/E9Q8L9|||http://purl.uniprot.org/uniprot/Q9D620 ^@ 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|||C2|||Disordered|||FIP-RBD|||Necessary for interaction with RAB4A and RAB11A, subcellular location and endosomal recycling|||Phosphoserine|||Polar residues|||Rab11 family-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000097305 http://togogenome.org/gene/10090:Six3 ^@ http://purl.uniprot.org/uniprot/Q62233 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Bind to RHO promoter|||Disordered|||Homeobox|||Homeobox protein SIX3|||In isoform SIX3A.|||Interaction with TLE5|||Loss of interaction with TLE5 and TLE4.|||Polar residues|||Suppression of SIX3-binding to rhodopsin promoter. Impairs the ability of Six3 to stimulate RHO transcription. ^@ http://purl.uniprot.org/annotation/PRO_0000049300|||http://purl.uniprot.org/annotation/VSP_002291|||http://purl.uniprot.org/annotation/VSP_002292 http://togogenome.org/gene/10090:Uqcr10 ^@ http://purl.uniprot.org/uniprot/Q8R1I1 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Helix|||Topological Domain|||Transmembrane|||Turn ^@ Cytochrome b-c1 complex subunit 9|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix ^@ http://purl.uniprot.org/annotation/PRO_0000193554 http://togogenome.org/gene/10090:Mup11 ^@ http://purl.uniprot.org/uniprot/A2BIM8|||http://purl.uniprot.org/uniprot/P04938|||http://purl.uniprot.org/uniprot/Q9CXU6 ^@ 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 ^@ Lipocalin/cytosolic fatty-acid binding|||Lipocalin/cytosolic fatty-acid binding domain-containing protein|||Major urinary protein 11|||Major urinary protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000201023|||http://purl.uniprot.org/annotation/PRO_5004327944|||http://purl.uniprot.org/annotation/PRO_5005334073 http://togogenome.org/gene/10090:Smim11 ^@ http://purl.uniprot.org/uniprot/Q99J19 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Coiled-Coil|||Transmembrane ^@ Helical|||Small integral membrane protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000079518 http://togogenome.org/gene/10090:Zfp286 ^@ http://purl.uniprot.org/uniprot/Q8C0E6|||http://purl.uniprot.org/uniprot/Q8R0E0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Ddx19a ^@ http://purl.uniprot.org/uniprot/Q61655 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ ATP-dependent RNA helicase DDX19A|||C-terminal lobe|||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|||N-acetylalanine|||N-terminal helix|||N-terminal lobe|||Phosphothreonine|||Q motif|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000055023 http://togogenome.org/gene/10090:Apeh ^@ http://purl.uniprot.org/uniprot/Q8R146 ^@ 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 ^@ Acylamino-acid-releasing enzyme|||Charge relay system|||In isoform 2.|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000122431|||http://purl.uniprot.org/annotation/VSP_008866 http://togogenome.org/gene/10090:Krtap3-1 ^@ http://purl.uniprot.org/uniprot/A2A591 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Repeat ^@ 1|||2|||3|||4|||4 X 5 AA repeats of C-C-X(3)|||Keratin-associated protein 3-1|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000358594 http://togogenome.org/gene/10090:Mycbpap ^@ http://purl.uniprot.org/uniprot/Q5SUV2|||http://purl.uniprot.org/uniprot/Q8CDK4 ^@ 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.|||MYCBP-associated protein|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000302878|||http://purl.uniprot.org/annotation/VSP_052544|||http://purl.uniprot.org/annotation/VSP_052545 http://togogenome.org/gene/10090:Gucd1 ^@ http://purl.uniprot.org/uniprot/Q8BZI6 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Protein GUCD1 ^@ http://purl.uniprot.org/annotation/PRO_0000079575 http://togogenome.org/gene/10090:Hsf2 ^@ http://purl.uniprot.org/uniprot/A0A1W2P8F8|||http://purl.uniprot.org/uniprot/P38533|||http://purl.uniprot.org/uniprot/Q8BWK6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Region|||Splice Variant ^@ Disordered|||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 Beta.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000124570|||http://purl.uniprot.org/annotation/VSP_002417 http://togogenome.org/gene/10090:Spen ^@ http://purl.uniprot.org/uniprot/A2ADB0|||http://purl.uniprot.org/uniprot/A2ADB1|||http://purl.uniprot.org/uniprot/Q3UV27|||http://purl.uniprot.org/uniprot/Q62504 ^@ Chain|||Coiled-Coil|||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|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with MSX2|||Interaction with RBPSUH|||Msx2-interacting protein|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RID|||RRM|||RRM 1|||RRM 2|||RRM 3|||RRM 4|||SPOC ^@ http://purl.uniprot.org/annotation/PRO_0000081628|||http://purl.uniprot.org/annotation/VSP_008564|||http://purl.uniprot.org/annotation/VSP_013802|||http://purl.uniprot.org/annotation/VSP_013803|||http://purl.uniprot.org/annotation/VSP_013804 http://togogenome.org/gene/10090:Inpp5e ^@ http://purl.uniprot.org/uniprot/A2AIX0|||http://purl.uniprot.org/uniprot/Q9JII1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Repeat ^@ 1|||2|||3|||3 X 4 AA repeats of P-X-X-P|||Cysteine methyl ester|||Disordered|||Inositol polyphosphate-related phosphatase|||Phosphatidylinositol polyphosphate 5-phosphatase type IV|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000209748|||http://purl.uniprot.org/annotation/PRO_0000431689 http://togogenome.org/gene/10090:Rigi ^@ http://purl.uniprot.org/uniprot/A1L0V6|||http://purl.uniprot.org/uniprot/Q6Q899 ^@ Binding Site|||Chain|||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 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Antiviral innate immune response receptor RIG-I|||CARD 1|||CARD 2|||DECH box|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Greatly decreases 'K-48'-linked ubiquitination.|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ZC3HAV1|||Mediates interaction with RNF135|||N6-acetyllysine|||Phosphothreonine; by CK2|||RLR CTR ^@ http://purl.uniprot.org/annotation/PRO_0000144094|||http://purl.uniprot.org/annotation/VSP_016055|||http://purl.uniprot.org/annotation/VSP_016056|||http://purl.uniprot.org/annotation/VSP_016057|||http://purl.uniprot.org/annotation/VSP_016058|||http://purl.uniprot.org/annotation/VSP_016059|||http://purl.uniprot.org/annotation/VSP_016060 http://togogenome.org/gene/10090:Serpinb6d ^@ http://purl.uniprot.org/uniprot/Q3UWK8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Or10g3b ^@ http://purl.uniprot.org/uniprot/L7N457 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Helt ^@ http://purl.uniprot.org/uniprot/Q7TS99 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Hairy and enhancer of split-related protein HELT|||N6-acetyllysine|||Orange|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000349379 http://togogenome.org/gene/10090:St3gal6 ^@ http://purl.uniprot.org/uniprot/Q8VIB3 ^@ 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|||Type 2 lactosamine alpha-2,3-sialyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000149306 http://togogenome.org/gene/10090:Jaml ^@ http://purl.uniprot.org/uniprot/Q80UL9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||Junctional adhesion molecule-like|||Loss of interaction with CXADR.|||Loss of interaction with PI3 kinase.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with PI3 kinase.|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000015075 http://togogenome.org/gene/10090:Cnot3 ^@ http://purl.uniprot.org/uniprot/Q8K0V4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ CCR4-NOT transcription complex subunit 3|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Repressor domain ^@ http://purl.uniprot.org/annotation/PRO_0000198334 http://togogenome.org/gene/10090:Thg1l ^@ http://purl.uniprot.org/uniprot/Q9CQT0|||http://purl.uniprot.org/uniprot/Q9CY52 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Probable tRNA(His) guanylyltransferase|||Thg1 C-terminal|||tRNAHis guanylyltransferase catalytic ^@ http://purl.uniprot.org/annotation/PRO_0000284985 http://togogenome.org/gene/10090:Ptgr1 ^@ http://purl.uniprot.org/uniprot/Q91YR9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-acetyllysine; alternate|||Phosphothreonine|||Prostaglandin reductase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000218066 http://togogenome.org/gene/10090:Ccdc83 ^@ http://purl.uniprot.org/uniprot/D3YUZ0|||http://purl.uniprot.org/uniprot/Q9D4V3 ^@ 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 83|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288883|||http://purl.uniprot.org/annotation/VSP_025812|||http://purl.uniprot.org/annotation/VSP_025813|||http://purl.uniprot.org/annotation/VSP_025814 http://togogenome.org/gene/10090:Akap1 ^@ http://purl.uniprot.org/uniprot/O08715 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ A-kinase anchor protein 1, mitochondrial|||Basic and acidic residues|||Disordered|||In isoform 1 and isoform 2.|||In isoform 2 and isoform 4.|||In isoform 5.|||In isoform 6.|||KH|||Mitochondrion|||PKA-RII subunit binding domain|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tudor ^@ http://purl.uniprot.org/annotation/PRO_0000016660|||http://purl.uniprot.org/annotation/VSP_002847|||http://purl.uniprot.org/annotation/VSP_002848|||http://purl.uniprot.org/annotation/VSP_002849|||http://purl.uniprot.org/annotation/VSP_002850|||http://purl.uniprot.org/annotation/VSP_002851|||http://purl.uniprot.org/annotation/VSP_002852|||http://purl.uniprot.org/annotation/VSP_002853 http://togogenome.org/gene/10090:Ffar2 ^@ http://purl.uniprot.org/uniprot/Q8VCK6 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Free fatty acid receptor 2|||Gain of SCFA-independent constitutive G protein-coupled receptor activity.|||Helical; 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_0000228144 http://togogenome.org/gene/10090:Gm12888 ^@ http://purl.uniprot.org/uniprot/Q3UW77 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015097521 http://togogenome.org/gene/10090:Rgl2 ^@ http://purl.uniprot.org/uniprot/Q61193 ^@ 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|||Disordered|||N-terminal Ras-GEF|||Polar residues|||Ral guanine nucleotide dissociation stimulator-like 2|||Ras-GEF|||Ras-associating ^@ http://purl.uniprot.org/annotation/PRO_0000068889 http://togogenome.org/gene/10090:Neurl2 ^@ http://purl.uniprot.org/uniprot/A2A5J5 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||NHR|||SOCS box ^@ http://togogenome.org/gene/10090:Bcl2l13 ^@ http://purl.uniprot.org/uniprot/P59017 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ A|||A; approximate|||BH1|||BH2|||BH3|||BH4|||Basic and acidic residues|||Bcl-2-like protein 13|||Disordered|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000143074 http://togogenome.org/gene/10090:Guf1 ^@ http://purl.uniprot.org/uniprot/Q8C3X4 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Mitochondrion|||Translation factor Guf1, mitochondrial|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000256252|||http://purl.uniprot.org/annotation/VSP_021345 http://togogenome.org/gene/10090:Tas2r119 ^@ http://purl.uniprot.org/uniprot/A2VCK4|||http://purl.uniprot.org/uniprot/Q9JKT2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||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 119 ^@ http://purl.uniprot.org/annotation/PRO_0000082192 http://togogenome.org/gene/10090:Or5b95 ^@ http://purl.uniprot.org/uniprot/Q8VFW8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rnf144b ^@ http://purl.uniprot.org/uniprot/Q8BKD6 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ E3 ubiquitin-protein ligase RNF144B|||Helical|||IBR-type|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain ^@ http://purl.uniprot.org/annotation/PRO_0000055912 http://togogenome.org/gene/10090:Or5p68 ^@ http://purl.uniprot.org/uniprot/Q8VEW5 ^@ 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 5P68 ^@ http://purl.uniprot.org/annotation/PRO_0000150848 http://togogenome.org/gene/10090:Serpini1 ^@ http://purl.uniprot.org/uniprot/O35684 ^@ Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ N-linked (GlcNAc...) asparagine|||Neuroserpin|||O-linked (Xyl...) (chondroitin sulfate) serine|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000032522 http://togogenome.org/gene/10090:Ost4 ^@ http://purl.uniprot.org/uniprot/Q99LX8 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000328639 http://togogenome.org/gene/10090:G6pdx ^@ http://purl.uniprot.org/uniprot/Q00612|||http://purl.uniprot.org/uniprot/Q790Y8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Glucose-6-phosphate 1-dehydrogenase X|||Glucose-6-phosphate dehydrogenase C-terminal|||Glucose-6-phosphate dehydrogenase NAD-binding|||N-acetylalanine|||Phosphotyrosine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000068085 http://togogenome.org/gene/10090:Hpcal4 ^@ http://purl.uniprot.org/uniprot/B2RRY8|||http://purl.uniprot.org/uniprot/Q8BGZ1 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding ^@ 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_0000073778 http://togogenome.org/gene/10090:Cntn5 ^@ http://purl.uniprot.org/uniprot/E9PYK7|||http://purl.uniprot.org/uniprot/P68500|||http://purl.uniprot.org/uniprot/Q3TRE5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Signal Peptide|||Strand|||Turn ^@ Contactin-5|||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|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000014719|||http://purl.uniprot.org/annotation/PRO_0000014720|||http://purl.uniprot.org/annotation/PRO_5004229693|||http://purl.uniprot.org/annotation/PRO_5015090367 http://togogenome.org/gene/10090:Vmn1r7 ^@ http://purl.uniprot.org/uniprot/E9Q8T0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lctl ^@ http://purl.uniprot.org/uniprot/Q8K1F9 ^@ 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 3.|||Lactase-like protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000042252|||http://purl.uniprot.org/annotation/VSP_015833|||http://purl.uniprot.org/annotation/VSP_015834 http://togogenome.org/gene/10090:Thbs4 ^@ http://purl.uniprot.org/uniprot/B2RTL6|||http://purl.uniprot.org/uniprot/Q9Z1T2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||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_0000035853|||http://purl.uniprot.org/annotation/PRO_5014298384 http://togogenome.org/gene/10090:Dnajb14 ^@ http://purl.uniprot.org/uniprot/Q149L6 ^@ 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 ^@ Cytoplasmic|||Disordered|||DnaJ homolog subfamily B member 14|||Helical|||In isoform 2.|||In isoform 3.|||J|||Lumenal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000281479|||http://purl.uniprot.org/annotation/VSP_024008|||http://purl.uniprot.org/annotation/VSP_024009|||http://purl.uniprot.org/annotation/VSP_024010 http://togogenome.org/gene/10090:P2ry10b ^@ http://purl.uniprot.org/uniprot/Q8BY68 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Klrb1a ^@ http://purl.uniprot.org/uniprot/B7ZN67|||http://purl.uniprot.org/uniprot/E9Q0W1|||http://purl.uniprot.org/uniprot/G5E882|||http://purl.uniprot.org/uniprot/P27811 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Killer cell lectin-like receptor subfamily B member 1A|||LCK-binding motif ^@ http://purl.uniprot.org/annotation/PRO_0000046675 http://togogenome.org/gene/10090:Mepce ^@ http://purl.uniprot.org/uniprot/Q8K3A9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 7SK snRNA methylphosphate capping enzyme|||Bin3-type SAM|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000289263 http://togogenome.org/gene/10090:Mfsd2a ^@ http://purl.uniprot.org/uniprot/Q9DA75 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes LPC transport.|||Abolishes LPC transport. Abolishes LPC transport; when associated with A-92.|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||No effect on LPC transport.|||Significant reduction in LPC transport.|||Significant reduction in LPC transport. Abolishes LPC transport; when associated with A-96.|||Slightly increased LPC transport.|||Slightly reduced LPC transport.|||Sodium-dependent lysophosphatidylcholine symporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000273388 http://togogenome.org/gene/10090:App ^@ http://purl.uniprot.org/uniprot/A0A2I3BPT1|||http://purl.uniprot.org/uniprot/A0A2I3BQZ9|||http://purl.uniprot.org/uniprot/P12023|||http://purl.uniprot.org/uniprot/Q3TWF3|||http://purl.uniprot.org/uniprot/Q6GR78 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||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|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Acidic residues|||Almost complete loss of binding to G(o) alpha subunit. No inhibition of GTPase activity.|||Amyloid-beta A4 protein|||Amyloid-beta precursor protein|||Amyloid-beta protein 40|||Amyloid-beta protein 42|||BPTI/Kunitz inhibitor|||Basolateral sorting signal|||C31|||C80|||C83|||C99|||Cleavage; by ACE|||Cleavage; by a caspase|||Cleavage; by alpha-secretase|||Cleavage; by beta-secretase|||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|||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 impairs interaction with DAB2.|||Greatly promotes interaction with DAB2.|||Helical|||Heparin-binding|||Impairs interaction with DAB2.|||Implicated in free radical propagation|||In isoform APP695.|||In isoform APP751.|||Interaction with DAB2|||Interaction with G(o)-alpha|||Interaction with PSEN1|||N-APP|||N-linked (GlcNAc...) asparagine|||No MAPK8IP1 nor APBA1 nor APBB1 nor DAB1 binding.|||No MAPK8IP1 nor APBA1 nor Dab1 binding. No effect on APBB1 binding.|||No effect on MAPK8IP1 binding.|||OX-2|||P3(40)|||P3(42)|||Phosphoserine|||Phosphoserine; by APP-kinase I|||Phosphoserine; by CK1|||Phosphoserine; by CK2|||Phosphothreonine|||Phosphothreonine; by CDK5 and MAPK10 and LRRK2|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Polar residues|||Reactive bond|||Required for Cu(2+) reduction|||Required for the interaction with KIF5B and for anterograde transport in axons|||Soluble APP-alpha|||Soluble APP-beta|||Sulfotyrosine|||Susceptible to oxidation|||YENPXY motif; contains endocytosis signal|||Zinc-binding ^@ http://purl.uniprot.org/annotation/PRO_0000000114|||http://purl.uniprot.org/annotation/PRO_0000000115|||http://purl.uniprot.org/annotation/PRO_0000000116|||http://purl.uniprot.org/annotation/PRO_0000000117|||http://purl.uniprot.org/annotation/PRO_0000000118|||http://purl.uniprot.org/annotation/PRO_0000000119|||http://purl.uniprot.org/annotation/PRO_0000000120|||http://purl.uniprot.org/annotation/PRO_0000000121|||http://purl.uniprot.org/annotation/PRO_0000000122|||http://purl.uniprot.org/annotation/PRO_0000000123|||http://purl.uniprot.org/annotation/PRO_0000000124|||http://purl.uniprot.org/annotation/PRO_0000000125|||http://purl.uniprot.org/annotation/PRO_0000000126|||http://purl.uniprot.org/annotation/PRO_0000381968|||http://purl.uniprot.org/annotation/PRO_0000384576|||http://purl.uniprot.org/annotation/PRO_5014169811|||http://purl.uniprot.org/annotation/PRO_5014196347|||http://purl.uniprot.org/annotation/PRO_5014310460|||http://purl.uniprot.org/annotation/PRO_5015097453|||http://purl.uniprot.org/annotation/VSP_000012|||http://purl.uniprot.org/annotation/VSP_000013|||http://purl.uniprot.org/annotation/VSP_000014 http://togogenome.org/gene/10090:Ppil2 ^@ http://purl.uniprot.org/uniprot/Q9D787 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||PPIase cyclophilin-type|||Polar residues|||RING-type E3 ubiquitin-protein ligase PPIL2|||U-box ^@ http://purl.uniprot.org/annotation/PRO_0000064172 http://togogenome.org/gene/10090:Sprr4 ^@ http://purl.uniprot.org/uniprot/Q8CGN8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Small proline-rich protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000150007 http://togogenome.org/gene/10090:Meaf6 ^@ http://purl.uniprot.org/uniprot/Q2VPQ9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||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.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000272610|||http://purl.uniprot.org/annotation/VSP_022452 http://togogenome.org/gene/10090:Or5t15 ^@ http://purl.uniprot.org/uniprot/A3KPP7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp800 ^@ http://purl.uniprot.org/uniprot/B7ZMR9|||http://purl.uniprot.org/uniprot/Q0VEE6 ^@ 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|||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 SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 800 ^@ http://purl.uniprot.org/annotation/PRO_0000304411 http://togogenome.org/gene/10090:Foxm1 ^@ http://purl.uniprot.org/uniprot/Q6P1H7 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Fork-head|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Arsg ^@ http://purl.uniprot.org/uniprot/Q3TYD4 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 3-oxoalanine (Cys)|||Arylsulfatase G|||Faster electrophoretic migration typical of a size reduction probably due to glycosylation loss.|||Faster electrophoretic migration typical of a size reduction probably due to glycosylation loss. Abolishes proteolytic cleavage.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000238663|||http://purl.uniprot.org/annotation/VSP_018628|||http://purl.uniprot.org/annotation/VSP_018629 http://togogenome.org/gene/10090:Gm21171 ^@ http://purl.uniprot.org/uniprot/J3QNI1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Nat3 ^@ http://purl.uniprot.org/uniprot/P50296 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Acyl-thioester intermediate|||Arylamine N-acetyltransferase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000107910 http://togogenome.org/gene/10090:Tmem259 ^@ http://purl.uniprot.org/uniprot/Q8CIV2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Membralin|||N-acetylserine|||N-linked (GlcNAc...) asparagine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000096274|||http://purl.uniprot.org/annotation/VSP_014379 http://togogenome.org/gene/10090:Cabp2 ^@ http://purl.uniprot.org/uniprot/G3XA16|||http://purl.uniprot.org/uniprot/G3XA29|||http://purl.uniprot.org/uniprot/G5E8W3|||http://purl.uniprot.org/uniprot/Q9JLK4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Splice Variant ^@ Calcium-binding protein 2|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform S-CaBP2.|||N-myristoyl glycine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073518|||http://purl.uniprot.org/annotation/VSP_000735 http://togogenome.org/gene/10090:Gm5141 ^@ http://purl.uniprot.org/uniprot/A0A0J9YUW3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Polr2l ^@ http://purl.uniprot.org/uniprot/P62876 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ DNA-directed RNA polymerases I, II, and III subunit RPABC5 ^@ http://purl.uniprot.org/annotation/PRO_0000121334 http://togogenome.org/gene/10090:Katnal2 ^@ http://purl.uniprot.org/uniprot/Q9D3R6 ^@ 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 2.|||In isoform 3.|||Katanin p60 ATPase-containing subunit A-like 2|||LisH|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000333793|||http://purl.uniprot.org/annotation/VSP_033524|||http://purl.uniprot.org/annotation/VSP_033525|||http://purl.uniprot.org/annotation/VSP_033526|||http://purl.uniprot.org/annotation/VSP_033527|||http://purl.uniprot.org/annotation/VSP_033528 http://togogenome.org/gene/10090:Wrap73 ^@ http://purl.uniprot.org/uniprot/Q9JM98 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein WRAP73 ^@ http://purl.uniprot.org/annotation/PRO_0000051357 http://togogenome.org/gene/10090:Nrxn3 ^@ http://purl.uniprot.org/uniprot/Q6P9K9|||http://purl.uniprot.org/uniprot/Q8C985 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes heparan sulfate attachment.|||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-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_0000412557|||http://purl.uniprot.org/annotation/PRO_0000412558|||http://purl.uniprot.org/annotation/PRO_0000412559|||http://purl.uniprot.org/annotation/PRO_0000412560|||http://purl.uniprot.org/annotation/VSP_041710|||http://purl.uniprot.org/annotation/VSP_041711|||http://purl.uniprot.org/annotation/VSP_041712 http://togogenome.org/gene/10090:Defb14 ^@ http://purl.uniprot.org/uniprot/Q7TNV9 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 14 ^@ http://purl.uniprot.org/annotation/PRO_0000006942 http://togogenome.org/gene/10090:Hnrnpd ^@ http://purl.uniprot.org/uniprot/G3X9W0|||http://purl.uniprot.org/uniprot/G5E8G0|||http://purl.uniprot.org/uniprot/Q60668 ^@ 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 ^@ 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|||RRM 1|||RRM 2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000081850|||http://purl.uniprot.org/annotation/VSP_007940|||http://purl.uniprot.org/annotation/VSP_007941 http://togogenome.org/gene/10090:Slc17a8 ^@ http://purl.uniprot.org/uniprot/D3YTT3|||http://purl.uniprot.org/uniprot/Q3UE85|||http://purl.uniprot.org/uniprot/Q8BFU8 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Vesicular|||Vesicular glutamate transporter 3 ^@ http://purl.uniprot.org/annotation/PRO_0000331615 http://togogenome.org/gene/10090:Stip1 ^@ http://purl.uniprot.org/uniprot/Q60864 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ 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|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||STI1 1|||STI1 2|||Stress-induced-phosphoprotein 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_0000106373 http://togogenome.org/gene/10090:Mex3d ^@ http://purl.uniprot.org/uniprot/D3YTR3|||http://purl.uniprot.org/uniprot/Q3UE17 ^@ 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|||In isoform 2.|||KH 1|||KH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type|||RNA-binding protein MEX3D ^@ http://purl.uniprot.org/annotation/PRO_0000281676|||http://purl.uniprot.org/annotation/VSP_024020 http://togogenome.org/gene/10090:Faap100 ^@ http://purl.uniprot.org/uniprot/A2ACJ2 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Fanconi anemia core complex-associated protein 100 ^@ http://purl.uniprot.org/annotation/PRO_0000289131 http://togogenome.org/gene/10090:Sell ^@ http://purl.uniprot.org/uniprot/B1B506|||http://purl.uniprot.org/uniprot/P18337|||http://purl.uniprot.org/uniprot/Q3TCF3|||http://purl.uniprot.org/uniprot/Q3UV83 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||EGF-like|||Extracellular|||Helical|||L-selectin|||N-linked (GlcNAc...) asparagine|||Sushi|||Sushi 1|||Sushi 2 ^@ http://purl.uniprot.org/annotation/PRO_0000017479|||http://purl.uniprot.org/annotation/PRO_0000017480|||http://purl.uniprot.org/annotation/PRO_5002761934|||http://purl.uniprot.org/annotation/PRO_5014309231|||http://purl.uniprot.org/annotation/PRO_5015097433 http://togogenome.org/gene/10090:Or5m8 ^@ http://purl.uniprot.org/uniprot/Q7TR87 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tnfsf4 ^@ http://purl.uniprot.org/uniprot/B6DXE3|||http://purl.uniprot.org/uniprot/P43488 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||TNF family profile|||Tumor necrosis factor ligand superfamily member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000185494 http://togogenome.org/gene/10090:Or1j11 ^@ http://purl.uniprot.org/uniprot/Q8VGK8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cd93 ^@ http://purl.uniprot.org/uniprot/O89103 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000017368 http://togogenome.org/gene/10090:Zdhhc12 ^@ http://purl.uniprot.org/uniprot/Q8VC90 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Helical|||In isoform 2.|||Loss of protein-cysteine S-palmitoyltransferase activity.|||Lumenal|||Palmitoyltransferase ZDHHC12|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212885|||http://purl.uniprot.org/annotation/VSP_006946 http://togogenome.org/gene/10090:C6 ^@ http://purl.uniprot.org/uniprot/Q91X70 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ MACPF|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_5015099509 http://togogenome.org/gene/10090:Prr23a1 ^@ http://purl.uniprot.org/uniprot/G3UW32 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Katnb1 ^@ http://purl.uniprot.org/uniprot/Q8BG40 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Turn ^@ Abolishes localization to microtubules minus ends; decreases ASPM localization to microtubules minus ends; no enhancement of ASPM activity in blocking microtubule minus-end growth.|||Abolishes localization to microtubules.|||Basic and acidic residues|||Disordered|||Disrupts KATNA1:KATNB1 interaction with ASPM.|||Disrupts KATNA1:KATNB1 interaction with ASPM; abolishes localization to microtubules minus ends; decreases ASPM localization to microtubules minus ends; no enhancement of ASPM activity in blocking microtubule minus-end growth.|||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_0000051050 http://togogenome.org/gene/10090:Ttll4 ^@ http://purl.uniprot.org/uniprot/Q80UG8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site ^@ Acidic residues|||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_0000212443 http://togogenome.org/gene/10090:Or8s8 ^@ http://purl.uniprot.org/uniprot/Q8VET6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hcrt ^@ http://purl.uniprot.org/uniprot/O55241|||http://purl.uniprot.org/uniprot/Q547R2 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide ^@ Leucine amide|||Methionine amide|||Orexin|||Orexin-A|||Orexin-B|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000020264|||http://purl.uniprot.org/annotation/PRO_0000020265|||http://purl.uniprot.org/annotation/PRO_0000020266|||http://purl.uniprot.org/annotation/PRO_5014309591 http://togogenome.org/gene/10090:Tmem269 ^@ http://purl.uniprot.org/uniprot/Q9D4Y8 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 269 ^@ http://purl.uniprot.org/annotation/PRO_0000440586 http://togogenome.org/gene/10090:Ccdc6 ^@ http://purl.uniprot.org/uniprot/D3YZP9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat ^@ 1|||2|||3|||4; approximate|||5|||5 X 29 AA tandem repeats|||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_0000415808 http://togogenome.org/gene/10090:Mei1 ^@ http://purl.uniprot.org/uniprot/Q9D4I2 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Meiosis inhibitor protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000347265|||http://purl.uniprot.org/annotation/VSP_052892 http://togogenome.org/gene/10090:Masp1 ^@ http://purl.uniprot.org/uniprot/A0A2R8VHR3|||http://purl.uniprot.org/uniprot/P98064 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ (3R)-3-hydroxyasparagine|||CUB|||CUB 1|||CUB 2|||Charge relay system|||Cleavage; by autolysis|||EGF-like; calcium-binding|||Homodimerization|||In isoform 2.|||Interaction with FCN2|||Interaction with MBL1|||Interaction with MBL2|||Interchain (between heavy and light chains)|||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|||Peptidase S1|||Sushi|||Sushi 1|||Sushi 2 ^@ http://purl.uniprot.org/annotation/PRO_0000027595|||http://purl.uniprot.org/annotation/PRO_0000027596|||http://purl.uniprot.org/annotation/PRO_0000027597|||http://purl.uniprot.org/annotation/PRO_5030054819|||http://purl.uniprot.org/annotation/VSP_036814|||http://purl.uniprot.org/annotation/VSP_036815 http://togogenome.org/gene/10090:Btbd35f16 ^@ http://purl.uniprot.org/uniprot/A0A087WSN2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Tmem14c ^@ http://purl.uniprot.org/uniprot/Q8C297|||http://purl.uniprot.org/uniprot/Q9CQN6 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 14C ^@ http://purl.uniprot.org/annotation/PRO_0000221174 http://togogenome.org/gene/10090:Rlim ^@ http://purl.uniprot.org/uniprot/Q9WTV7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RLIM|||N-acetylmethionine|||PDZ-binding|||Phosphoserine|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056053 http://togogenome.org/gene/10090:Akap10 ^@ http://purl.uniprot.org/uniprot/O88845 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ A-kinase anchor protein 10, mitochondrial|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Mitochondrion|||PKA-RII subunit binding|||Phosphoserine|||Polar residues|||RGS 1|||RGS 2 ^@ http://purl.uniprot.org/annotation/PRO_0000030405|||http://purl.uniprot.org/annotation/VSP_014873|||http://purl.uniprot.org/annotation/VSP_014874|||http://purl.uniprot.org/annotation/VSP_014875|||http://purl.uniprot.org/annotation/VSP_014876 http://togogenome.org/gene/10090:Pcdha5 ^@ http://purl.uniprot.org/uniprot/Q91Y15 ^@ 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|||Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099507 http://togogenome.org/gene/10090:Opa3 ^@ http://purl.uniprot.org/uniprot/Q505D7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Mutagenesis Site|||Sequence Conflict ^@ Homozygous mice have their visual function which is severely reduced, consistent with significant loss of retinal ganglion cells and degeneration of axons in the optic nerve. They also display a severe multi-systemic disease characterized by reduced lifespan (<4 months), decreased weight, dilated cardiomyopathy, extrapyramidal dysfunction and gross neuro-muscular defects.|||Optic atrophy 3 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000326547 http://togogenome.org/gene/10090:Umod ^@ http://purl.uniprot.org/uniprot/Q91X17 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Beta hairpin|||Cleavage|||D10C|||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 alanine|||Internal hydrophobic patch (IHP)|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Uromodulin|||Uromodulin, secreted form|||ZP|||ZP-C|||ZP-N ^@ http://purl.uniprot.org/annotation/PRO_0000041673|||http://purl.uniprot.org/annotation/PRO_0000041674|||http://purl.uniprot.org/annotation/PRO_0000407910 http://togogenome.org/gene/10090:Myog ^@ http://purl.uniprot.org/uniprot/P12979 ^@ 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_0000127376 http://togogenome.org/gene/10090:Bag3 ^@ http://purl.uniprot.org/uniprot/Q9JLV1 ^@ 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 ^@ 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|||N-acetylserine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000088869 http://togogenome.org/gene/10090:Hpcal1 ^@ http://purl.uniprot.org/uniprot/P62748 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding ^@ 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_0000073772 http://togogenome.org/gene/10090:Acsl6 ^@ http://purl.uniprot.org/uniprot/Q5F2D0|||http://purl.uniprot.org/uniprot/Q5ICG4|||http://purl.uniprot.org/uniprot/Q5ICG5|||http://purl.uniprot.org/uniprot/Q8R1X1|||http://purl.uniprot.org/uniprot/Q91WC3 ^@ 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 2.|||Long-chain-fatty-acid--CoA ligase 6 ^@ http://purl.uniprot.org/annotation/PRO_0000193116|||http://purl.uniprot.org/annotation/VSP_037824 http://togogenome.org/gene/10090:Sirpa ^@ http://purl.uniprot.org/uniprot/E0CX65|||http://purl.uniprot.org/uniprot/P97797|||http://purl.uniprot.org/uniprot/Q6P6I8 ^@ 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 ^@ Almost complete loss of CD47 binding.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C1-type 1|||Ig-like C1-type 2|||Ig-like V-type|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by Tyr-kinases|||SH2-binding|||SH3-binding|||Tyrosine-protein phosphatase non-receptor type substrate 1 ^@ http://purl.uniprot.org/annotation/PRO_0000014942|||http://purl.uniprot.org/annotation/PRO_5003133251|||http://purl.uniprot.org/annotation/PRO_5015098419|||http://purl.uniprot.org/annotation/VSP_007031|||http://purl.uniprot.org/annotation/VSP_007032 http://togogenome.org/gene/10090:Rgl3 ^@ http://purl.uniprot.org/uniprot/Q3UYI5 ^@ 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.|||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_0000306800|||http://purl.uniprot.org/annotation/VSP_028471|||http://purl.uniprot.org/annotation/VSP_028472|||http://purl.uniprot.org/annotation/VSP_028473|||http://purl.uniprot.org/annotation/VSP_028474 http://togogenome.org/gene/10090:Zmynd15 ^@ http://purl.uniprot.org/uniprot/A2CFF1|||http://purl.uniprot.org/uniprot/Q5F2D4|||http://purl.uniprot.org/uniprot/Q6ZQM1|||http://purl.uniprot.org/uniprot/Q8C0R7 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||MYND-type|||Pro residues|||Zinc finger MYND domain-containing protein 15 ^@ http://purl.uniprot.org/annotation/PRO_0000414854|||http://purl.uniprot.org/annotation/VSP_042145|||http://purl.uniprot.org/annotation/VSP_042146 http://togogenome.org/gene/10090:Pax6 ^@ http://purl.uniprot.org/uniprot/P63015|||http://purl.uniprot.org/uniprot/Q8VBX9 ^@ 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 Pax6(4Neu); defective.|||In isoform 3.|||In isoform 5a.|||PAI subdomain|||Paired|||Paired box protein Pax-6|||Polar residues|||RED subdomain|||Required for suppression of NFATC1-mediated transcription ^@ http://purl.uniprot.org/annotation/PRO_0000050186|||http://purl.uniprot.org/annotation/VSP_011530|||http://purl.uniprot.org/annotation/VSP_054294 http://togogenome.org/gene/10090:H2-M11 ^@ http://purl.uniprot.org/uniprot/Q85ZX0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5004303644 http://togogenome.org/gene/10090:Fam3b ^@ http://purl.uniprot.org/uniprot/Q9D309 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ GG-type lectin|||N-linked (GlcNAc...) asparagine|||Protein FAM3B ^@ http://purl.uniprot.org/annotation/PRO_0000008751 http://togogenome.org/gene/10090:Kpna6 ^@ http://purl.uniprot.org/uniprot/O35345|||http://purl.uniprot.org/uniprot/Q8BH30 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ ARM|||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_0000120730 http://togogenome.org/gene/10090:Or10ak13 ^@ http://purl.uniprot.org/uniprot/A2ACY8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ckb ^@ http://purl.uniprot.org/uniprot/Q04447 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 3'-nitrotyrosine|||Abolished creatine kinase activity.|||Abolishes localization to mitochondria in fat cells.|||Basic and acidic residues|||Creatine kinase B-type|||Disordered|||Internal MTS-like signal|||Phosphagen kinase C-terminal|||Phosphagen kinase N-terminal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000211967 http://togogenome.org/gene/10090:Ss18 ^@ http://purl.uniprot.org/uniprot/Q62280|||http://purl.uniprot.org/uniprot/Q6P1I1|||http://purl.uniprot.org/uniprot/Q8BJJ6|||http://purl.uniprot.org/uniprot/Q8BKL1|||http://purl.uniprot.org/uniprot/Q8VHA8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||2 X 13 AA imperfect tandem repeats|||Disordered|||N-acetylserine|||Polar residues|||Protein SSXT|||Removed|||SH2-binding|||SH3-binding|||SS18 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000181824 http://togogenome.org/gene/10090:Arl3 ^@ http://purl.uniprot.org/uniprot/Q9WUL7 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Strand|||Turn ^@ ADP-ribosylation factor-like protein 3|||Does not inhibit interaction with PDE6D.|||Does not reduce the interaction with RP2.|||Inhibits RP2-dependent GTP-hydrolysis rate.|||Inhibits interaction with PDE6D.|||N-myristoyl glycine|||Phosphoserine|||Reduces the interaction with RP2; when associated with A-164.|||Reduces the interaction with RP2; when associated with A-168.|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207457 http://togogenome.org/gene/10090:Magea1 ^@ http://purl.uniprot.org/uniprot/O89006 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Rad51 ^@ http://purl.uniprot.org/uniprot/Q08297 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ DNA repair protein RAD51 homolog 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HhH|||Interaction with PALB2|||N-acetylalanine|||Nuclear export signal; masked by the interaction with BRCA2|||Phosphothreonine; by CHEK1|||Phosphotyrosine; by ABL1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000122933 http://togogenome.org/gene/10090:Npepl1 ^@ http://purl.uniprot.org/uniprot/Q3UD03|||http://purl.uniprot.org/uniprot/Q6NSR8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent ^@ Cytosol aminopeptidase|||Probable aminopeptidase NPEPL1 ^@ http://purl.uniprot.org/annotation/PRO_0000165829 http://togogenome.org/gene/10090:Ezhip ^@ http://purl.uniprot.org/uniprot/B1B0V2 ^@ 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|||EZH inhibitory protein|||In isoform 2.|||Necessary and sufficient for inhibition of PRC2/EED-EZH1 and PRC2/EED-EZH2 complex activity|||Phosphoserine|||Polar residues|||Sufficient for interaction with EZH2 ^@ http://purl.uniprot.org/annotation/PRO_0000450617|||http://purl.uniprot.org/annotation/VSP_060652 http://togogenome.org/gene/10090:Pogk ^@ http://purl.uniprot.org/uniprot/A0A0R4J1T0|||http://purl.uniprot.org/uniprot/E9Q3B2|||http://purl.uniprot.org/uniprot/Q6GQW2|||http://purl.uniprot.org/uniprot/Q80TC5 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Region|||Sequence Conflict ^@ DDE-1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HTH CENPB-type|||KRAB|||KRAB-related|||Pogo transposable element with KRAB domain ^@ http://purl.uniprot.org/annotation/PRO_0000126132 http://togogenome.org/gene/10090:Grap ^@ http://purl.uniprot.org/uniprot/Q9CX99 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ GRB2-related adapter protein|||SH2|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000088207 http://togogenome.org/gene/10090:Trpv3 ^@ http://purl.uniprot.org/uniprot/Q8K424 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||INTRAMEM|||Region|||Repeat|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ ANK 1|||ANK 2|||ANK 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues|||Pore-forming|||Transient receptor potential cation channel subfamily V member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000215346 http://togogenome.org/gene/10090:Mindy4 ^@ http://purl.uniprot.org/uniprot/A0A0N4SVL4|||http://purl.uniprot.org/uniprot/Q3UQI9 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Deubiquitinating enzyme MINDY-3/4 conserved|||Disordered|||In isoform 2.|||Nucleophile|||Phosphoserine|||Polar residues|||Probable ubiquitin carboxyl-terminal hydrolase MINDY-4|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000320591|||http://purl.uniprot.org/annotation/VSP_031672 http://togogenome.org/gene/10090:Or5aq1 ^@ http://purl.uniprot.org/uniprot/Q8VG38 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r1 ^@ http://purl.uniprot.org/uniprot/G3X8Y6|||http://purl.uniprot.org/uniprot/O70410 ^@ 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|||G-protein coupled receptors family 3 profile|||Helical|||N-linked (GlcNAc...) asparagine|||Vomeronasal type-2 receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000246126|||http://purl.uniprot.org/annotation/PRO_5015091803 http://togogenome.org/gene/10090:Abhd5 ^@ http://purl.uniprot.org/uniprot/Q9DBL9 ^@ Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Splice Variant|||Strand ^@ 1-acylglycerol-3-phosphate O-acyltransferase ABHD5|||AB hydrolase-1|||HXXXXD motif|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000080867|||http://purl.uniprot.org/annotation/VSP_015345 http://togogenome.org/gene/10090:Slc4a11 ^@ http://purl.uniprot.org/uniprot/A2AJN7 ^@ 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|||Solute carrier family 4 member 11 ^@ http://purl.uniprot.org/annotation/PRO_0000352350 http://togogenome.org/gene/10090:Cbfb ^@ http://purl.uniprot.org/uniprot/Q08024 ^@ 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|||Core-binding factor subunit beta|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interferes with heterodimerization.|||Phosphoserine; by CK2|||Phosphoserine; by PKC ^@ http://purl.uniprot.org/annotation/PRO_0000058302|||http://purl.uniprot.org/annotation/VSP_004358|||http://purl.uniprot.org/annotation/VSP_004359|||http://purl.uniprot.org/annotation/VSP_004360 http://togogenome.org/gene/10090:Gm37013 ^@ http://purl.uniprot.org/uniprot/O88689|||http://purl.uniprot.org/uniprot/Q8K492 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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|||Cadherin C-terminal catenin-binding|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||O-linked (Man) serine|||O-linked (Man) threonine|||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_0000240663|||http://purl.uniprot.org/annotation/VSP_019413|||http://purl.uniprot.org/annotation/VSP_019414|||http://purl.uniprot.org/annotation/VSP_019415 http://togogenome.org/gene/10090:Vps16 ^@ http://purl.uniprot.org/uniprot/G3X8X7|||http://purl.uniprot.org/uniprot/Q8BWV2|||http://purl.uniprot.org/uniprot/Q8C016 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ Vps16 C-terminal|||Vps16 N-terminal ^@ http://togogenome.org/gene/10090:Des ^@ http://purl.uniprot.org/uniprot/P31001|||http://purl.uniprot.org/uniprot/Q3V1K9 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Site ^@ ADP-ribosylarginine|||Asymmetric dimethylarginine; alternate|||Coil 1A|||Coil 1B|||Coil 2A|||Coil 2B|||Desmin|||Formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-60. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-32 and A-60.|||Formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-76. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-32 and A-76.|||Head|||IF rod|||Increases protein decay. forms subsarcolemmal aggregates. Changes the subcellular localization and turnover of its direct, extrasarcomeric binding partners. Knockin mice develop age-dependent desmin-positive protein aggregation pathology, skeletal muscle weakness, dilated cardiomyopathy, as well as cardiac arrhythmias and conduction defects. Knockin mice exhibit altered axial myofibrillar lattice arrangement in fast- and slow-twitch muscle fibers, increased axial stiffness and stretch-induced vulnerability in soleus muscle fiber bundles, reduced Ca(2+)-sensitivity in heterozygous fiber bundles and increased Ca(2+)-sensitivity in homozygous fiber bundles.|||Interaction with CRYAB|||Interaction with NEB|||Linker 1|||Linker 12|||Linker 2|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by AURKB|||Phosphoserine; by CDK1|||Phosphothreonine; by AURKB and ROCK1|||Phosphothreonine; by ROCK1|||Reduced phosphorylation and formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis. Almost complete loss of phosphorylation; when associated with A-7 and A-28. Increased formation of unusual long bridge-like intermediate filament structures between two daughter cells during cytokinesis; when associated with A-60 and A-76.|||Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with A-28 and A-32.|||Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with A-7 and A-32.|||Removed|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063773 http://togogenome.org/gene/10090:Bzw1 ^@ http://purl.uniprot.org/uniprot/Q9CQC6 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||W2|||eIF5-mimic protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000254610 http://togogenome.org/gene/10090:Ugt2a3 ^@ http://purl.uniprot.org/uniprot/Q8BWQ1 ^@ 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|||N6-succinyllysine|||UDP-glucuronosyltransferase 2A3 ^@ http://purl.uniprot.org/annotation/PRO_0000299147 http://togogenome.org/gene/10090:Cnga2 ^@ http://purl.uniprot.org/uniprot/A3KGE1|||http://purl.uniprot.org/uniprot/Q62398 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||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|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000219313 http://togogenome.org/gene/10090:Ncoa4 ^@ http://purl.uniprot.org/uniprot/Q5U4H9|||http://purl.uniprot.org/uniprot/Q8BSH1|||http://purl.uniprot.org/uniprot/Q9CXF3 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ Nuclear coactivator ^@ http://togogenome.org/gene/10090:Cnksr3 ^@ http://purl.uniprot.org/uniprot/Q8BMA3 ^@ 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 ^@ CRIC|||Connector enhancer of kinase suppressor of ras 3|||DUF1170|||Disordered|||In isoform 2.|||PDZ|||Phosphoserine|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000311106|||http://purl.uniprot.org/annotation/VSP_029391|||http://purl.uniprot.org/annotation/VSP_029615 http://togogenome.org/gene/10090:Herc2 ^@ http://purl.uniprot.org/uniprot/Q4U2R1 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Acidic residues|||Cytochrome b5 heme-binding|||DOC|||Disordered|||E3 ubiquitin-protein ligase HERC2|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||MIB/HERC2|||Phosphoserine|||Phosphothreonine|||Polar residues|||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_0000229740|||http://purl.uniprot.org/annotation/VSP_051975 http://togogenome.org/gene/10090:Taar7d ^@ http://purl.uniprot.org/uniprot/Q5QD10 ^@ 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|||Trace amine-associated receptor 7d ^@ http://purl.uniprot.org/annotation/PRO_0000070167 http://togogenome.org/gene/10090:Pttg1ip2 ^@ http://purl.uniprot.org/uniprot/D3YUK8 ^@ 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|||PTTG1IP family member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000452021 http://togogenome.org/gene/10090:Ndst4 ^@ http://purl.uniprot.org/uniprot/Q9EQW8 ^@ 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|||Topological Domain|||Transmembrane ^@ Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4|||Cytoplasmic|||For sulfotransferase activity|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate N-deacetylase 4|||Heparan sulfate N-sulfotransferase 4|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000225662 http://togogenome.org/gene/10090:Angpt4 ^@ http://purl.uniprot.org/uniprot/Q3V0P7|||http://purl.uniprot.org/uniprot/Q9WVH6 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Angiopoietin-4|||Disordered|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009117|||http://purl.uniprot.org/annotation/PRO_5014309207 http://togogenome.org/gene/10090:Pcdhb10 ^@ http://purl.uniprot.org/uniprot/Q91VE5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099490 http://togogenome.org/gene/10090:1700017N19Rik ^@ http://purl.uniprot.org/uniprot/D3YX67 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Zinc-finger CCCH ^@ http://togogenome.org/gene/10090:Rtcb ^@ http://purl.uniprot.org/uniprot/Q99LF4 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Modified Residue|||Sequence Conflict ^@ 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_0000255243 http://togogenome.org/gene/10090:Elavl2 ^@ http://purl.uniprot.org/uniprot/B1AXZ4|||http://purl.uniprot.org/uniprot/B1AXZ5|||http://purl.uniprot.org/uniprot/Q3UR02|||http://purl.uniprot.org/uniprot/Q564D8|||http://purl.uniprot.org/uniprot/Q60899|||http://purl.uniprot.org/uniprot/Q80UJ0|||http://purl.uniprot.org/uniprot/Q80Y51 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||ELAV-like protein 2|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000081580 http://togogenome.org/gene/10090:Lhfpl1 ^@ http://purl.uniprot.org/uniprot/Q80SV1 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Signal Peptide|||Transmembrane ^@ Helical|||LHFPL tetraspan subfamily member 1 protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000244761 http://togogenome.org/gene/10090:Fgf22 ^@ http://purl.uniprot.org/uniprot/A0A7U3JW52|||http://purl.uniprot.org/uniprot/Q9ESS2 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Fibroblast growth factor|||Fibroblast growth factor 22 ^@ http://purl.uniprot.org/annotation/PRO_0000008997|||http://purl.uniprot.org/annotation/PRO_5031608420 http://togogenome.org/gene/10090:Oca2 ^@ http://purl.uniprot.org/uniprot/Q62052 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||P protein ^@ http://purl.uniprot.org/annotation/PRO_0000172510 http://togogenome.org/gene/10090:Tpcn1 ^@ http://purl.uniprot.org/uniprot/Q9EQJ0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||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.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Two pore calcium channel protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000276854|||http://purl.uniprot.org/annotation/VSP_023006|||http://purl.uniprot.org/annotation/VSP_023007 http://togogenome.org/gene/10090:Cdc25a ^@ http://purl.uniprot.org/uniprot/P48964 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||KEN box|||M-phase inducer phosphatase 1|||Phosphodegron|||Phosphoserine|||Phosphoserine; by CHEK1|||Phosphoserine; by CHEK1 and CHEK2|||Phosphoserine; by NEK11|||Phosphoserine; by PLK3|||Phosphothreonine; by CHEK1|||Rhodanese ^@ http://purl.uniprot.org/annotation/PRO_0000198642 http://togogenome.org/gene/10090:Rusc1 ^@ http://purl.uniprot.org/uniprot/Q3TDG5|||http://purl.uniprot.org/uniprot/Q8BG26 ^@ 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 ^@ AP-4 complex accessory subunit RUSC1|||Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with IKBKG|||Interaction with TRAF6|||Polar residues|||Pro residues|||RUN|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000097533|||http://purl.uniprot.org/annotation/VSP_010856|||http://purl.uniprot.org/annotation/VSP_010857 http://togogenome.org/gene/10090:Rnaseh2b ^@ http://purl.uniprot.org/uniprot/Q80ZV0 ^@ 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-acetyllysine|||Phosphoserine|||Removed|||Ribonuclease H2 subunit B ^@ http://purl.uniprot.org/annotation/PRO_0000248379 http://togogenome.org/gene/10090:Pcgf6 ^@ http://purl.uniprot.org/uniprot/Q99NA9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polycomb group RING finger protein 6|||Pro residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055990 http://togogenome.org/gene/10090:Ltv1 ^@ http://purl.uniprot.org/uniprot/Q6NSQ7 ^@ 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|||Disordered|||Phosphoserine|||Protein LTV1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000302814 http://togogenome.org/gene/10090:Kif2a ^@ http://purl.uniprot.org/uniprot/P28740|||http://purl.uniprot.org/uniprot/Q9D481 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Globular|||In isoform 1 and isoform 2.|||In isoform 1.|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF2A|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000125415|||http://purl.uniprot.org/annotation/VSP_028377|||http://purl.uniprot.org/annotation/VSP_028378|||http://purl.uniprot.org/annotation/VSP_028379 http://togogenome.org/gene/10090:Frs2 ^@ http://purl.uniprot.org/uniprot/Q8C180 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolishes myristoylation and membrane association.|||Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-306; F-349 and F-392.|||Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-306; F-349 and F-436.|||Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-306; F-392 and F-436.|||Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-196; F-349; F-392 and F-436.|||Abolishes tyrosine phosphorylation and interactions with GRB2 and PTPN11; when associated with F-306; F-349; F-392 and F-436.|||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_0000087345 http://togogenome.org/gene/10090:Or11g24 ^@ http://purl.uniprot.org/uniprot/E9Q1P0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Csn1s2b ^@ http://purl.uniprot.org/uniprot/A0A0G2JDP4|||http://purl.uniprot.org/uniprot/P02664|||http://purl.uniprot.org/uniprot/Q3TP31 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Sequence Conflict|||Signal Peptide ^@ Alpha-S2-casein-like B ^@ http://purl.uniprot.org/annotation/PRO_0000004466|||http://purl.uniprot.org/annotation/PRO_5012700823|||http://purl.uniprot.org/annotation/PRO_5015097454 http://togogenome.org/gene/10090:Ogdh ^@ http://purl.uniprot.org/uniprot/Q60597|||http://purl.uniprot.org/uniprot/Z4YJV4 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ 2-oxoglutarate dehydrogenase complex component E1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Recognized by alloreactive CD8 cytotoxic T-lymphocytes in association with a class I MHC protein|||Transketolase-like pyrimidine-binding ^@ http://purl.uniprot.org/annotation/PRO_0000020434|||http://purl.uniprot.org/annotation/VSP_024799|||http://purl.uniprot.org/annotation/VSP_024800|||http://purl.uniprot.org/annotation/VSP_024801 http://togogenome.org/gene/10090:Cmtm3 ^@ http://purl.uniprot.org/uniprot/Q99LJ5 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ CKLF-like MARVEL transmembrane domain-containing protein 3|||Disordered|||Helical|||MARVEL ^@ http://purl.uniprot.org/annotation/PRO_0000186102 http://togogenome.org/gene/10090:Prkcb ^@ http://purl.uniprot.org/uniprot/P68404 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ AGC-kinase C-terminal|||Basic and acidic residues|||C2|||Disordered|||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|||Protein kinase|||Protein kinase C beta type|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000055685|||http://purl.uniprot.org/annotation/VSP_041812 http://togogenome.org/gene/10090:Slc31a1 ^@ http://purl.uniprot.org/uniprot/Q8K211 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Bis-His motif|||Cleavage|||Cysteine sulfenic acid (-SOH)|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||High affinity copper uptake protein 1|||Inhibition of VEGF-induced VEGFR2 signaling. Inhibition of endothelial cell migration.|||Interchain (with C-1208 in KDR)|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphothreonine|||Polar residues|||Truncated CTR1 form ^@ http://purl.uniprot.org/annotation/PRO_0000195041|||http://purl.uniprot.org/annotation/PRO_0000458009 http://togogenome.org/gene/10090:Catsper1 ^@ http://purl.uniprot.org/uniprot/Q91ZR5 ^@ Chain|||Compositionally Biased Region|||Helix|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||INTRAMEM|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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|||In strain: 2, 47 and 58.|||In strain: 47.|||In strain: 72.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295675 http://togogenome.org/gene/10090:Pros1 ^@ http://purl.uniprot.org/uniprot/Q08761|||http://purl.uniprot.org/uniprot/Q3TR66 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||Gla|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Thrombin-sensitive|||Vitamin K-dependent protein S ^@ http://purl.uniprot.org/annotation/PRO_0000022123|||http://purl.uniprot.org/annotation/PRO_0000022124|||http://purl.uniprot.org/annotation/PRO_5014309118 http://togogenome.org/gene/10090:Or8b46 ^@ http://purl.uniprot.org/uniprot/Q8VG76 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wdr4 ^@ http://purl.uniprot.org/uniprot/E9Q156|||http://purl.uniprot.org/uniprot/Q9EP82 ^@ 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 ^@ Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4 ^@ http://purl.uniprot.org/annotation/PRO_0000051349 http://togogenome.org/gene/10090:Ctbp1 ^@ http://purl.uniprot.org/uniprot/A0A0J9YU62|||http://purl.uniprot.org/uniprot/O88712 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ 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 isoform 2.|||In isoform 3.|||Interaction with GLIS2 1|||Interaction with GLIS2 2|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000076042|||http://purl.uniprot.org/annotation/VSP_024737|||http://purl.uniprot.org/annotation/VSP_024738 http://togogenome.org/gene/10090:Arrb1 ^@ http://purl.uniprot.org/uniprot/Q8BWG8 ^@ 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|||Beta-arrestin-1|||Disordered|||In isoform 1B.|||Interaction with CHRM2|||Interaction with SRC|||Interaction with TRAF6|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000205195|||http://purl.uniprot.org/annotation/VSP_019545 http://togogenome.org/gene/10090:Agfg1 ^@ http://purl.uniprot.org/uniprot/A0A087WNV1|||http://purl.uniprot.org/uniprot/A0A087WSR7|||http://purl.uniprot.org/uniprot/Q8K2K6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Arf-GAP|||Arf-GAP domain and FG repeat-containing protein 1|||C4-type|||Disordered|||In isoform 1.|||In isoform 2.|||In isoform 3.|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204905|||http://purl.uniprot.org/annotation/VSP_010664|||http://purl.uniprot.org/annotation/VSP_010665|||http://purl.uniprot.org/annotation/VSP_017602 http://togogenome.org/gene/10090:Phtf1 ^@ http://purl.uniprot.org/uniprot/Q5IBN5|||http://purl.uniprot.org/uniprot/Q80YS3|||http://purl.uniprot.org/uniprot/Q8C2F6|||http://purl.uniprot.org/uniprot/Q9QZ09 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||PHTF|||PHTF1/2 N-terminal|||Phosphoserine|||Polar residues|||Protein PHTF1 ^@ http://purl.uniprot.org/annotation/PRO_0000127424 http://togogenome.org/gene/10090:H1f4 ^@ http://purl.uniprot.org/uniprot/P43274 ^@ 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 ^@ ADP-ribosylserine|||Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.4|||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_0000195917 http://togogenome.org/gene/10090:Or4a39 ^@ http://purl.uniprot.org/uniprot/Q8VG59 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zbed6 ^@ http://purl.uniprot.org/uniprot/D2EAC2|||http://purl.uniprot.org/uniprot/G0LE24 ^@ Binding Site|||Chain|||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|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ BED-type|||BED-type 1|||BED-type 2|||Basic and acidic residues|||Disordered|||HATC (Hobo-Ac-Tam3) domain|||In isoform 2.|||Phosphoserine|||Polar residues|||Required for nucleolar localization|||Zinc finger BED domain-containing protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000392574|||http://purl.uniprot.org/annotation/VSP_053206 http://togogenome.org/gene/10090:Vmn2r37 ^@ http://purl.uniprot.org/uniprot/F8VQD3|||http://purl.uniprot.org/uniprot/O35202 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003379246|||http://purl.uniprot.org/annotation/PRO_5004158334 http://togogenome.org/gene/10090:Dusp4 ^@ http://purl.uniprot.org/uniprot/Q8BFV3 ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Dual specificity protein phosphatase 4|||N-acetylvaline|||Phosphocysteine intermediate|||Phosphoserine; by MAPK|||Removed|||Rhodanese|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094799 http://togogenome.org/gene/10090:B3gnt6 ^@ http://purl.uniprot.org/uniprot/Q3USF0 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000289219 http://togogenome.org/gene/10090:Ldb1 ^@ http://purl.uniprot.org/uniprot/P70662 ^@ 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 and isoform 3.|||In isoform 2.|||LIM domain-binding protein 1|||LIM interaction domain (LID)|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000084385|||http://purl.uniprot.org/annotation/VSP_027833|||http://purl.uniprot.org/annotation/VSP_027834|||http://purl.uniprot.org/annotation/VSP_027835 http://togogenome.org/gene/10090:Or2bd2 ^@ http://purl.uniprot.org/uniprot/Q7TQV3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tas2r109 ^@ http://purl.uniprot.org/uniprot/Q7M707 ^@ 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 109 ^@ http://purl.uniprot.org/annotation/PRO_0000248254 http://togogenome.org/gene/10090:Nova2 ^@ http://purl.uniprot.org/uniprot/A0A1W2P872 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Crosslink|||Domain Extent|||Motif|||Splice Variant ^@ Bipartite nuclear localization signal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KH 1|||KH 2|||KH 3|||RNA-binding protein Nova-2 ^@ http://purl.uniprot.org/annotation/PRO_0000453422|||http://purl.uniprot.org/annotation/VSP_061137 http://togogenome.org/gene/10090:Ifi214 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1R5|||http://purl.uniprot.org/uniprot/Q504N7 ^@ 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 residues|||Disordered|||HIN-200|||In isoform 2.|||Polar residues|||Pyrin|||Pyrin and HIN domain-containing protein 1-like ^@ http://purl.uniprot.org/annotation/PRO_0000334526|||http://purl.uniprot.org/annotation/VSP_033661|||http://purl.uniprot.org/annotation/VSP_033662 http://togogenome.org/gene/10090:Smyd4 ^@ http://purl.uniprot.org/uniprot/Q8BTK5 ^@ 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 ^@ In isoform 2.|||In strain: Czech II.|||MYND-type|||SET|||SET and MYND domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000227785|||http://purl.uniprot.org/annotation/VSP_017580 http://togogenome.org/gene/10090:Hesx1 ^@ http://purl.uniprot.org/uniprot/Q61658 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Region|||Sequence Conflict ^@ Disordered|||Homeobox|||Homeobox expressed in ES cells 1 ^@ http://purl.uniprot.org/annotation/PRO_0000048923 http://togogenome.org/gene/10090:Tex24 ^@ http://purl.uniprot.org/uniprot/Q5DP50 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Protein Tex24 ^@ http://purl.uniprot.org/annotation/PRO_0000435468 http://togogenome.org/gene/10090:Tnfrsf26 ^@ http://purl.uniprot.org/uniprot/P83626|||http://purl.uniprot.org/uniprot/Q3U3N2 ^@ 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|||N-linked (GlcNAc...) asparagine|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 26 ^@ http://purl.uniprot.org/annotation/PRO_0000034607|||http://purl.uniprot.org/annotation/PRO_5014309183 http://togogenome.org/gene/10090:Abhd10 ^@ http://purl.uniprot.org/uniprot/Q6PE15 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ AB hydrolase-1|||Charge relay system|||In isoform 2.|||Mitochondrion|||Palmitoyl-protein thioesterase ABHD10, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000280734|||http://purl.uniprot.org/annotation/VSP_023893|||http://purl.uniprot.org/annotation/VSP_023894 http://togogenome.org/gene/10090:Gal3st2b ^@ http://purl.uniprot.org/uniprot/J3QMJ1|||http://purl.uniprot.org/uniprot/Q6XQH0 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Galactose-3-O-sulfotransferase 2|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000085204 http://togogenome.org/gene/10090:Qki ^@ http://purl.uniprot.org/uniprot/Q9QYS9 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Abolishes nuclear localization; when associated with A-324.|||Abolishes nuclear localization; when associated with A-330.|||Abolishes phosphorylation and RNA-binding; when associated with F-285; F-288; F-290 and F-292.|||Abolishes phosphorylation and RNA-binding; when associated with F-285; F-288; F-290 and F-303.|||Abolishes phosphorylation and RNA-binding; when associated with F-285; F-288; F-292 and F-303.|||Abolishes phosphorylation and RNA-binding; when associated with F-285; F-290; F-292 and F-303.|||Abolishes phosphorylation and RNA-binding; when associated with F-288; F-290; F-292 and F-303.|||Asymmetric dimethylarginine; by CARM1; alternate|||Does not affect nuclear localization.|||Impaired homodimerization.|||In isoform 6.|||In isoform QKI5A.|||In isoform QKI6.|||In isoform QKI7.|||In isoform QKI7B and isoform 6.|||In isoform QKID.|||In isoform QKIG.|||In qk-Kt4; induces embryonic lethality possibly due to its inability to homodimerize.|||In qk-k24; induces embryonic lethality possibly due to blood vessel defects; prevents RNA-binding but not homodimerization.|||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|||Strongly impairs phosphorylation. ^@ http://purl.uniprot.org/annotation/PRO_0000239374|||http://purl.uniprot.org/annotation/VSP_019192|||http://purl.uniprot.org/annotation/VSP_019193|||http://purl.uniprot.org/annotation/VSP_019194|||http://purl.uniprot.org/annotation/VSP_019195|||http://purl.uniprot.org/annotation/VSP_019196|||http://purl.uniprot.org/annotation/VSP_019197|||http://purl.uniprot.org/annotation/VSP_019198|||http://purl.uniprot.org/annotation/VSP_019199 http://togogenome.org/gene/10090:Acsbg1 ^@ http://purl.uniprot.org/uniprot/Q99PU5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes enzyme activity; when associated with A-281.|||Abolishes enzyme activity; when associated with M-287.|||Disordered|||Long-chain-fatty-acid--CoA ligase ACSBG1|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315810 http://togogenome.org/gene/10090:Gm884 ^@ http://purl.uniprot.org/uniprot/E9Q472|||http://purl.uniprot.org/uniprot/Q3V3Y5 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||LRRC37A/B like protein 1 C-terminal|||Leucine-rich repeat-containing protein 37 N-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Slc29a4 ^@ http://purl.uniprot.org/uniprot/Q8R139 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Equilibrative nucleoside transporter 4|||Essential for cation selectivity|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000326252 http://togogenome.org/gene/10090:Slc1a4 ^@ http://purl.uniprot.org/uniprot/O35874|||http://purl.uniprot.org/uniprot/Q3US35|||http://purl.uniprot.org/uniprot/Q3UTP8 ^@ 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-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Neutral amino acid transporter A|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000202080 http://togogenome.org/gene/10090:Lcn11 ^@ http://purl.uniprot.org/uniprot/A2BHR2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5002642813 http://togogenome.org/gene/10090:Gjb6 ^@ http://purl.uniprot.org/uniprot/P70689|||http://purl.uniprot.org/uniprot/Q3URC5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Topological Domain|||Transmembrane ^@ Connexin N-terminal|||Cytoplasmic|||Extracellular|||Gap junction beta-6 protein|||Gap junction protein cysteine-rich|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000057872 http://togogenome.org/gene/10090:Safb2 ^@ http://purl.uniprot.org/uniprot/Q80YR5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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|||N-acetylalanine|||N6-acetyllysine; alternate|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||Removed|||SAP|||Scaffold attachment factor B2 ^@ http://purl.uniprot.org/annotation/PRO_0000081908 http://togogenome.org/gene/10090:Vasn ^@ http://purl.uniprot.org/uniprot/Q9CZT5 ^@ 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|||Region|||Repeat|||Sequence Conflict|||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...) asparagine|||Vasorin ^@ http://purl.uniprot.org/annotation/PRO_0000232631 http://togogenome.org/gene/10090:Rasl11b ^@ http://purl.uniprot.org/uniprot/Q922H7 ^@ 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.|||Ras-like protein family member 11B|||Small GTPase-like ^@ http://purl.uniprot.org/annotation/PRO_0000308366|||http://purl.uniprot.org/annotation/VSP_052585|||http://purl.uniprot.org/annotation/VSP_052586 http://togogenome.org/gene/10090:Fam216b ^@ http://purl.uniprot.org/uniprot/Q8CC14 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein FAM216B ^@ http://purl.uniprot.org/annotation/PRO_0000350568 http://togogenome.org/gene/10090:Cep20 ^@ http://purl.uniprot.org/uniprot/Q9CZS3 ^@ 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|||Centrosomal protein 20|||Disordered|||LisH|||Necessary and sufficient for homooligomerization and localization to centrosomes and pericentriolar satellites|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000264466 http://togogenome.org/gene/10090:Gm20883 ^@ http://purl.uniprot.org/uniprot/A0A087WRK1|||http://purl.uniprot.org/uniprot/A0A087WSR0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Cfap221 ^@ http://purl.uniprot.org/uniprot/A9Q751 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Cilia- and flagella-associated protein 221|||Interaction with calmodulin ^@ http://purl.uniprot.org/annotation/PRO_0000395000 http://togogenome.org/gene/10090:Selplg ^@ http://purl.uniprot.org/uniprot/Q3TA56 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015097431 http://togogenome.org/gene/10090:Dcaf17 ^@ http://purl.uniprot.org/uniprot/Q3TUL7 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ DDB1- and CUL4-associated factor 17|||Helical|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000300119|||http://purl.uniprot.org/annotation/VSP_027789|||http://purl.uniprot.org/annotation/VSP_027790|||http://purl.uniprot.org/annotation/VSP_027791 http://togogenome.org/gene/10090:Or10a49 ^@ http://purl.uniprot.org/uniprot/Q7TRU4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Chil4 ^@ http://purl.uniprot.org/uniprot/Q91Z98 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ Chitinase-like protein 4|||GH18 ^@ http://purl.uniprot.org/annotation/PRO_0000011971 http://togogenome.org/gene/10090:Aimp1 ^@ http://purl.uniprot.org/uniprot/Q3UZG4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||TRNA-binding ^@ http://togogenome.org/gene/10090:Pigw ^@ http://purl.uniprot.org/uniprot/B7ZN11|||http://purl.uniprot.org/uniprot/Q8C398 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Topological Domain|||Transmembrane ^@ Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphatidylinositol-glycan biosynthesis class W protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000246283 http://togogenome.org/gene/10090:Glt8d2 ^@ http://purl.uniprot.org/uniprot/Q640P4 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||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_0000271384 http://togogenome.org/gene/10090:Lrsam1 ^@ http://purl.uniprot.org/uniprot/Q80ZI6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Zinc Finger ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase LRSAM1|||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_0000055924 http://togogenome.org/gene/10090:Or4c112 ^@ http://purl.uniprot.org/uniprot/Q8VGG1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Csf2 ^@ http://purl.uniprot.org/uniprot/P01587|||http://purl.uniprot.org/uniprot/Q5SX78 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ 25-fold reduction in bioactivity.|||450-fold reduction in bioactivity.|||50-fold reduction in bioactivity.|||5500-fold reduction in bioactivity.|||Granulocyte-macrophage colony-stimulating factor|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Reduction in bioactivity. ^@ http://purl.uniprot.org/annotation/PRO_0000005866|||http://purl.uniprot.org/annotation/PRO_5010844583 http://togogenome.org/gene/10090:Zfyve26 ^@ http://purl.uniprot.org/uniprot/Q5DU37 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||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|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||Disordered|||FYVE-type|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Zinc finger FYVE domain-containing protein 26 ^@ http://purl.uniprot.org/annotation/PRO_0000314613|||http://purl.uniprot.org/annotation/VSP_030342|||http://purl.uniprot.org/annotation/VSP_030343|||http://purl.uniprot.org/annotation/VSP_030344|||http://purl.uniprot.org/annotation/VSP_030345|||http://purl.uniprot.org/annotation/VSP_030346 http://togogenome.org/gene/10090:Bad ^@ http://purl.uniprot.org/uniprot/Q3U9H3|||http://purl.uniprot.org/uniprot/Q61337 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure ^@ Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Asymmetric dimethylarginine; by PRMT1|||BH3|||Bcl2-associated agonist of cell death|||Disordered|||Enhances pro-apoptotic activity.|||Enhances pro-apoptotic activity; no phosphorylation.|||Enhances pro-apoptotic activity; no phosphorylation; interacts with Bcl-X(L).|||No phosphorylation.|||No pro-apoptotic activity, no interaction with Bcl-X(L).|||No pro-apoptotic activity; even when associated with A-112.|||Phosphoserine|||Phosphoserine; by PKA and PKB|||Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ|||Phosphoserine; by PKA, PKB, PIM2, PIM3, PAK1, PAK2, PAK4, PAK5, RPS6KA1 and RAF1 ^@ http://purl.uniprot.org/annotation/PRO_0000143104 http://togogenome.org/gene/10090:Kif5b ^@ http://purl.uniprot.org/uniprot/Q61768|||http://purl.uniprot.org/uniprot/Q9CUT6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||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|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000125352 http://togogenome.org/gene/10090:Zfp566 ^@ http://purl.uniprot.org/uniprot/Q8VCI1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Vmn1r181 ^@ http://purl.uniprot.org/uniprot/Q0P547 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mrpl33 ^@ http://purl.uniprot.org/uniprot/Q9CQP0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein bL33m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000238626 http://togogenome.org/gene/10090:Kdm7a ^@ http://purl.uniprot.org/uniprot/Q3UWM4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Abolishes enzymatic activity.|||Basic and acidic residues|||Disordered|||Has no effect on enzymatic activity.|||JmjC|||Linker|||Lysine-specific demethylase 7A|||PHD-type|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000226772 http://togogenome.org/gene/10090:Susd1 ^@ http://purl.uniprot.org/uniprot/E9Q3H4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ EGF-like|||Helical|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_5003243067 http://togogenome.org/gene/10090:Tdpoz1 ^@ http://purl.uniprot.org/uniprot/P0DMR5|||http://purl.uniprot.org/uniprot/Q05AE5 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ BTB|||MATH|||TD and POZ domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000191623 http://togogenome.org/gene/10090:Mturn ^@ http://purl.uniprot.org/uniprot/Q8CGA4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Maturin|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000294234 http://togogenome.org/gene/10090:Gsdma2 ^@ http://purl.uniprot.org/uniprot/Q32M21 ^@ Binding Site|||Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Region|||Splice Variant|||Transmembrane ^@ Beta stranded|||Gasdermin-A2|||Gasdermin-A2, C-terminal|||Gasdermin-A2, N-terminal|||In isoform 2.|||In isoform 3.|||Triggers pyroptosis ^@ http://purl.uniprot.org/annotation/PRO_0000347271|||http://purl.uniprot.org/annotation/PRO_0000451668|||http://purl.uniprot.org/annotation/PRO_0000451669|||http://purl.uniprot.org/annotation/VSP_052880|||http://purl.uniprot.org/annotation/VSP_052881|||http://purl.uniprot.org/annotation/VSP_052882 http://togogenome.org/gene/10090:Insm1 ^@ http://purl.uniprot.org/uniprot/Q05BD7|||http://purl.uniprot.org/uniprot/Q63ZV0 ^@ 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; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||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_0000047269 http://togogenome.org/gene/10090:Senp2 ^@ http://purl.uniprot.org/uniprot/Q91ZX6 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes protease activity.|||Disordered|||In isoform 2.|||In isoform 3.|||Nuclear export signal|||Nuclear localization signal|||Nucleophile|||Phosphoserine|||Polar residues|||Protease|||Sentrin-specific protease 2 ^@ http://purl.uniprot.org/annotation/PRO_0000101719|||http://purl.uniprot.org/annotation/VSP_005273|||http://purl.uniprot.org/annotation/VSP_021942 http://togogenome.org/gene/10090:Sdhc ^@ http://purl.uniprot.org/uniprot/Q9CZB0 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Succinate dehydrogenase cytochrome b560 subunit, mitochondrial|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000003635 http://togogenome.org/gene/10090:Ctsll3 ^@ http://purl.uniprot.org/uniprot/Q3ULP7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Cathepsin propeptide inhibitor|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_5015020015 http://togogenome.org/gene/10090:Rsad1 ^@ http://purl.uniprot.org/uniprot/Q5SUV1 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Transit Peptide ^@ Mitochondrion|||Radical S-adenosyl methionine domain-containing protein 1, mitochondrial|||Radical SAM core ^@ http://purl.uniprot.org/annotation/PRO_0000284610 http://togogenome.org/gene/10090:Nudt3 ^@ http://purl.uniprot.org/uniprot/B2KF67|||http://purl.uniprot.org/uniprot/Q9JI46 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site ^@ Diphosphoinositol polyphosphate phosphohydrolase 1|||Loss of diphosphoinositol polyphosphate phosphohydrolase activity, but retains ability to regulate the ERK1/2 pathway.|||N-acetylmethionine|||Nudix box|||Nudix hydrolase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000057056 http://togogenome.org/gene/10090:Dusp18 ^@ http://purl.uniprot.org/uniprot/Q8BWD7|||http://purl.uniprot.org/uniprot/Q8VE01 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Non-terminal Residue|||Region ^@ Dual specificity protein phosphatase 18|||Phosphocysteine intermediate|||Sufficient for mitochondrial localization|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094829 http://togogenome.org/gene/10090:Txn2 ^@ http://purl.uniprot.org/uniprot/P97493 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Site|||Transit Peptide ^@ 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_0000034151 http://togogenome.org/gene/10090:Adgrf1 ^@ http://purl.uniprot.org/uniprot/Q8VEC3 ^@ 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 ^@ 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|||N-linked (GlcNAc...) asparagine|||SEA ^@ http://purl.uniprot.org/annotation/PRO_0000012892 http://togogenome.org/gene/10090:Crlf3 ^@ http://purl.uniprot.org/uniprot/Q9Z2L7 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand ^@ Chain|||Coiled-Coil|||Domain Extent|||Splice Variant|||Strand ^@ Cytokine receptor-like factor 3|||Fibronectin type-III|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000288937|||http://purl.uniprot.org/annotation/VSP_025847|||http://purl.uniprot.org/annotation/VSP_025848 http://togogenome.org/gene/10090:Acbd7 ^@ http://purl.uniprot.org/uniprot/Q9D258 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ ACB|||Acyl-CoA-binding domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000288025 http://togogenome.org/gene/10090:Slc28a1 ^@ http://purl.uniprot.org/uniprot/E9PXX9 ^@ 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|||Sodium/nucleoside cotransporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000455292 http://togogenome.org/gene/10090:Pex12 ^@ http://purl.uniprot.org/uniprot/Q5SWQ8|||http://purl.uniprot.org/uniprot/Q8VC48 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||Helical; Name=TM1|||Helical; Name=TM2|||Helical; Name=TM3|||Helical; Name=TM4|||Helical; Name=TM5|||Peroxisomal matrix|||Peroxisome assembly protein 12|||Pex N-terminal|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000218611 http://togogenome.org/gene/10090:ND3 ^@ http://purl.uniprot.org/uniprot/P03899|||http://purl.uniprot.org/uniprot/Q7GIP5 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ Chain|||Helix|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ Helical|||NADH-ubiquinone oxidoreductase chain 3 ^@ http://purl.uniprot.org/annotation/PRO_0000117765 http://togogenome.org/gene/10090:Impg1 ^@ http://purl.uniprot.org/uniprot/Q8R1W8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||Heparin- and hyaluronan-binding|||In isoform 2.|||In isoform 3.|||Interphotoreceptor matrix proteoglycan 1|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Polar residues|||SEA 1|||SEA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000252239|||http://purl.uniprot.org/annotation/VSP_052171|||http://purl.uniprot.org/annotation/VSP_052172 http://togogenome.org/gene/10090:Or5e1 ^@ http://purl.uniprot.org/uniprot/Q8VFZ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ube4b ^@ http://purl.uniprot.org/uniprot/Q3V426|||http://purl.uniprot.org/uniprot/Q9ES00 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ Basic and acidic residues|||Cleavage; by caspase-3 and caspase-7|||Cleavage; by caspase-6 and granzyme B|||Disordered|||Loss of E3 ubiquitin protein ligase activity.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||U-box|||Ubiquitin conjugation factor E4 B ^@ http://purl.uniprot.org/annotation/PRO_0000194994 http://togogenome.org/gene/10090:Fbp2 ^@ http://purl.uniprot.org/uniprot/P70695|||http://purl.uniprot.org/uniprot/Q3TKP4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ Fructose-1,6-bisphosphatase isozyme 2|||Fructose-1-6-bisphosphatase class 1 C-terminal|||Fructose-1-6-bisphosphatase class I N-terminal|||Important for interaction with ALDOA|||Important for the conversion from active R-state to inactive T-state in the presence of AMP|||Nuclear localization signal|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000200505 http://togogenome.org/gene/10090:Selenoi ^@ http://purl.uniprot.org/uniprot/Q80TA1 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non standard residue|||Region|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Non standard residue|||Transmembrane ^@ Ethanolaminephosphotransferase 1|||Helical|||N-acetylalanine|||Removed|||Selenocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000056814 http://togogenome.org/gene/10090:Pgm2 ^@ http://purl.uniprot.org/uniprot/Q7TSV4 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ Phosphopentomutase|||Phosphoserine|||Phosphoserine intermediate|||via phosphate group ^@ http://purl.uniprot.org/annotation/PRO_0000147782 http://togogenome.org/gene/10090:Cxcl10 ^@ http://purl.uniprot.org/uniprot/P17515|||http://purl.uniprot.org/uniprot/Q548V9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Signal Peptide|||Strand|||Turn ^@ C-X-C motif chemokine|||C-X-C motif chemokine 10|||Chemokine interleukin-8-like|||Citrulline ^@ http://purl.uniprot.org/annotation/PRO_0000005104|||http://purl.uniprot.org/annotation/PRO_5014205874 http://togogenome.org/gene/10090:Lpin2 ^@ http://purl.uniprot.org/uniprot/E9PWN0|||http://purl.uniprot.org/uniprot/Q99PI5 ^@ 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 phosphatidate phosphatase activity but does not prevent membrane association nor coactivator activity.|||Abolishes phosphatidate phosphatase activity but does not prevent membrane association.|||Basic and acidic residues|||C-LIP|||DXDXT motif|||Disordered|||In isoform 2.|||LNS2/PITP|||LXXIL motif|||N-LIP|||Nuclear localization signal|||Phosphatidate phosphatase LPIN2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000209882|||http://purl.uniprot.org/annotation/VSP_010387|||http://purl.uniprot.org/annotation/VSP_010388 http://togogenome.org/gene/10090:Or2l13 ^@ http://purl.uniprot.org/uniprot/Q8VGX2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mkks ^@ http://purl.uniprot.org/uniprot/Q9JI70 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Region|||Sequence Conflict ^@ Molecular chaperone MKKS|||Substrate-binding apical domain ^@ http://purl.uniprot.org/annotation/PRO_0000128416 http://togogenome.org/gene/10090:Nscme3l ^@ http://purl.uniprot.org/uniprot/Q99PB1|||http://purl.uniprot.org/uniprot/Q9DA56 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Atxn1 ^@ http://purl.uniprot.org/uniprot/J3QPR1|||http://purl.uniprot.org/uniprot/P54254 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ AXH|||Abolishes nuclear localization. Inhibits development of ataxia.|||Ataxin-1|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Interaction with USP7|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA-binding|||Self-association ^@ http://purl.uniprot.org/annotation/PRO_0000064752 http://togogenome.org/gene/10090:Tcf7l1 ^@ http://purl.uniprot.org/uniprot/A1A549|||http://purl.uniprot.org/uniprot/A1A550|||http://purl.uniprot.org/uniprot/Q9Z1J1 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes DNA-binding and transactivator/repressor activity; when associated with I-407.|||Abolishes DNA-binding and transactivator/repressor activity; when associated with P-383.|||Basic and acidic residues|||CTNNB1-binding|||Disordered|||HMG box|||Nuclear localization signal|||Polar residues|||Pro residues|||Transcription factor 7-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000048615 http://togogenome.org/gene/10090:Psmd10 ^@ http://purl.uniprot.org/uniprot/A2AG83|||http://purl.uniprot.org/uniprot/Q9Z2X2 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Helix|||Repeat|||Sequence Conflict|||Strand ^@ 26S proteasome non-ATPase regulatory subunit 10|||ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7 ^@ http://purl.uniprot.org/annotation/PRO_0000067046 http://togogenome.org/gene/10090:Vxn ^@ http://purl.uniprot.org/uniprot/Q8BG31 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Vexin ^@ http://purl.uniprot.org/annotation/PRO_0000271015 http://togogenome.org/gene/10090:Mrpl39 ^@ http://purl.uniprot.org/uniprot/Q9JKF7 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Large ribosomal subunit protein mL39|||N6-acetyllysine|||TGS ^@ http://purl.uniprot.org/annotation/PRO_0000087685 http://togogenome.org/gene/10090:Pnpla7 ^@ http://purl.uniprot.org/uniprot/A2AJ88 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DGA/G|||Disordered|||GXGXXG|||GXSXG|||Helical|||In isoform 2.|||In isoform 3.|||Involved in the binding to lipid droplets|||Lumenal|||Nucleophile|||PNPLA|||Patatin-like phospholipase domain-containing protein 7|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000293490|||http://purl.uniprot.org/annotation/VSP_026506|||http://purl.uniprot.org/annotation/VSP_026507|||http://purl.uniprot.org/annotation/VSP_053967|||http://purl.uniprot.org/annotation/VSP_053968 http://togogenome.org/gene/10090:Spsb1 ^@ http://purl.uniprot.org/uniprot/Q9D5L7 ^@ 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 ^@ B30.2/SPRY|||In isoform 2.|||Phosphotyrosine|||SOCS box|||SPRY domain-containing SOCS box protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000238473|||http://purl.uniprot.org/annotation/VSP_018612 http://togogenome.org/gene/10090:Lrg1 ^@ http://purl.uniprot.org/uniprot/Q91XL1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ LRRCT ^@ http://purl.uniprot.org/annotation/PRO_5015099491 http://togogenome.org/gene/10090:Trmt9b ^@ http://purl.uniprot.org/uniprot/Q80WQ4 ^@ 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.|||In isoform 3.|||Phosphoserine|||Probable tRNA methyltransferase 9B ^@ http://purl.uniprot.org/annotation/PRO_0000328793|||http://purl.uniprot.org/annotation/VSP_032795|||http://purl.uniprot.org/annotation/VSP_032796|||http://purl.uniprot.org/annotation/VSP_032797 http://togogenome.org/gene/10090:Ccnt1 ^@ http://purl.uniprot.org/uniprot/Q9QWV9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ ADP-ribosylhistidine|||ADP-ribosylserine|||Basic and acidic residues|||Basic residues|||Binding to HIV-1 Tat similar to human CCNT1.|||Cyclin-T1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histidine-rich domain (HRD)|||N6-(ADP-ribosyl)lysine|||N6-acetyllysine|||No effect.|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000080493 http://togogenome.org/gene/10090:Ifit3b ^@ http://purl.uniprot.org/uniprot/Q8BPC3 ^@ Coiled-Coil|||Region ^@ Coiled-Coil ^@ ^@ http://togogenome.org/gene/10090:Etfbkmt ^@ http://purl.uniprot.org/uniprot/Q80ZM3 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Electron transfer flavoprotein beta subunit lysine methyltransferase|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000318710 http://togogenome.org/gene/10090:Plpp7 ^@ http://purl.uniprot.org/uniprot/Q91WB2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Inactive phospholipid phosphatase 7|||Interaction with MTOR|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000239402 http://togogenome.org/gene/10090:Sco2 ^@ http://purl.uniprot.org/uniprot/Q8VCL2 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Protein SCO2 homolog, mitochondrial|||Redox-active|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000354068 http://togogenome.org/gene/10090:Or52h7 ^@ http://purl.uniprot.org/uniprot/B9EHE6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp442 ^@ http://purl.uniprot.org/uniprot/A2AQA0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Or4k37 ^@ http://purl.uniprot.org/uniprot/Q7TQY6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mydgf ^@ http://purl.uniprot.org/uniprot/Q9CPT4 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Myeloid-derived growth factor ^@ http://purl.uniprot.org/annotation/PRO_0000021009 http://togogenome.org/gene/10090:Plcg1 ^@ http://purl.uniprot.org/uniprot/Q62077 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1|||C2|||Disordered|||EF-hand|||N-acetylalanine|||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 1|||SH2 2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000088499 http://togogenome.org/gene/10090:Gmpr2 ^@ http://purl.uniprot.org/uniprot/Q99L27 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ GMP reductase 2|||N6-acetyllysine|||Proton donor/acceptor|||Thioimidate intermediate|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000093727 http://togogenome.org/gene/10090:Oog3 ^@ http://purl.uniprot.org/uniprot/Q3UWY1 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Repeat|||Splice Variant ^@ In isoform 2.|||LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Oogenesin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000440973|||http://purl.uniprot.org/annotation/VSP_059016 http://togogenome.org/gene/10090:Eps8l2 ^@ http://purl.uniprot.org/uniprot/Q99K30 ^@ 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|||Epidermal growth factor receptor kinase substrate 8-like protein 2|||In isoform 2.|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000239085|||http://purl.uniprot.org/annotation/VSP_019093|||http://purl.uniprot.org/annotation/VSP_019094 http://togogenome.org/gene/10090:Poc1b ^@ http://purl.uniprot.org/uniprot/Q8BHD1 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Repeat ^@ POC1 centriolar protein homolog B|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051411 http://togogenome.org/gene/10090:Cyp4f17 ^@ http://purl.uniprot.org/uniprot/G3UW78 ^@ Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Signal Peptide ^@ axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_5015091580 http://togogenome.org/gene/10090:Wdr41 ^@ http://purl.uniprot.org/uniprot/Q3UDP0 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 41 ^@ http://purl.uniprot.org/annotation/PRO_0000051391|||http://purl.uniprot.org/annotation/VSP_016182|||http://purl.uniprot.org/annotation/VSP_016183 http://togogenome.org/gene/10090:Adarb2 ^@ http://purl.uniprot.org/uniprot/Q3UY54|||http://purl.uniprot.org/uniprot/Q6PB89|||http://purl.uniprot.org/uniprot/Q8BQZ3|||http://purl.uniprot.org/uniprot/Q9JI20 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ A to I editase|||Basic residues|||DRBM|||DRBM 1|||DRBM 2|||Disordered|||Double-stranded RNA-specific editase B2|||Polar residues|||Proton donor|||R-domain (ssRNA-binding) ^@ http://purl.uniprot.org/annotation/PRO_0000171783 http://togogenome.org/gene/10090:Bbof1 ^@ http://purl.uniprot.org/uniprot/Q3V079 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basal body-orientation factor 1|||Basic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000281125 http://togogenome.org/gene/10090:Or4b1d ^@ http://purl.uniprot.org/uniprot/Q7TQZ0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pde12 ^@ http://purl.uniprot.org/uniprot/Q3TIU4 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ 2',5'-phosphodiesterase 12|||Disordered|||Mitochondrion|||Phosphoserine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000324313 http://togogenome.org/gene/10090:Clint1 ^@ http://purl.uniprot.org/uniprot/Q3UPG6|||http://purl.uniprot.org/uniprot/Q5SUH6|||http://purl.uniprot.org/uniprot/Q5SUH7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||ENTH|||Polar residues ^@ http://togogenome.org/gene/10090:Nalf1 ^@ http://purl.uniprot.org/uniprot/Q8CCS2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||NALCN channel auxiliary factor 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000339374|||http://purl.uniprot.org/annotation/VSP_034162|||http://purl.uniprot.org/annotation/VSP_034163 http://togogenome.org/gene/10090:Spef1 ^@ http://purl.uniprot.org/uniprot/Q99JL1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Calponin-homology (CH)|||Disruption of its microtubule-binding and microtubule bundling activities. Failure to rescue ciliary central apparatus formation in SPEF1-depleted ependymal cilia.|||Essential for homodimerization and microtubule bundling activity|||Sperm flagellar protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000079422 http://togogenome.org/gene/10090:Plk4 ^@ http://purl.uniprot.org/uniprot/Q64702 ^@ 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 ^@ Activating mutant.|||Basic and acidic residues|||Cryptic POLO box 1 (CPB1)|||Cryptic POLO box 2 (CPB2)|||Disordered|||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_0000086568|||http://purl.uniprot.org/annotation/VSP_011369|||http://purl.uniprot.org/annotation/VSP_011370|||http://purl.uniprot.org/annotation/VSP_011371 http://togogenome.org/gene/10090:Eif1ad6 ^@ http://purl.uniprot.org/uniprot/Q3UT53 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||S1-like ^@ http://togogenome.org/gene/10090:Eif3i ^@ http://purl.uniprot.org/uniprot/Q9QZD9 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Crosslink|||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 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000051037 http://togogenome.org/gene/10090:Map3k11 ^@ http://purl.uniprot.org/uniprot/Q80XI6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Leucine-zipper 1|||Leucine-zipper 2|||Mitogen-activated protein kinase kinase kinase 11|||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_0000277828 http://togogenome.org/gene/10090:Or52d3 ^@ http://purl.uniprot.org/uniprot/E9PVA0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ufl1 ^@ http://purl.uniprot.org/uniprot/Q8CCJ3 ^@ 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|||E3 UFM1-protein ligase 1|||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|||Removed|||Required for E3 UFM1-protein ligase activity ^@ http://purl.uniprot.org/annotation/PRO_0000050772|||http://purl.uniprot.org/annotation/VSP_014249|||http://purl.uniprot.org/annotation/VSP_014250|||http://purl.uniprot.org/annotation/VSP_014251 http://togogenome.org/gene/10090:Scube3 ^@ http://purl.uniprot.org/uniprot/A0A3B2WCG9|||http://purl.uniprot.org/uniprot/Q66PY1 ^@ 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 ^@ CUB|||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|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Signal peptide, CUB and EGF-like domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000250617|||http://purl.uniprot.org/annotation/PRO_5017451241|||http://purl.uniprot.org/annotation/VSP_052168|||http://purl.uniprot.org/annotation/VSP_052169 http://togogenome.org/gene/10090:Or4x18 ^@ http://purl.uniprot.org/uniprot/A2ATW2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Il1a ^@ http://purl.uniprot.org/uniprot/P01582|||http://purl.uniprot.org/uniprot/Q3U0Y6 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region ^@ Interleukin-1 alpha|||Interleukin-1 propeptide|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Nuclear localization signal (NLS)|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000015273|||http://purl.uniprot.org/annotation/PRO_0000015274 http://togogenome.org/gene/10090:Bphl ^@ http://purl.uniprot.org/uniprot/Q8R164 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site ^@ AB hydrolase-1|||Binding of alpha-amino group of substrate|||Charge relay system|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Valacyclovir hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000017842 http://togogenome.org/gene/10090:Gm14288 ^@ http://purl.uniprot.org/uniprot/A2BDM8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB ^@ http://togogenome.org/gene/10090:Ranbp3 ^@ http://purl.uniprot.org/uniprot/A0A3B2WCL5|||http://purl.uniprot.org/uniprot/Q9CT10 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ran-binding protein 3|||RanBD1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000097167 http://togogenome.org/gene/10090:Exosc5 ^@ http://purl.uniprot.org/uniprot/Q9CRA8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Exosome complex component RRP46|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000139976 http://togogenome.org/gene/10090:Vegfa ^@ http://purl.uniprot.org/uniprot/Q00731 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||Disordered|||In isoform VEGF-1 and isoform L-VEGF-1.|||In isoform VEGF-1, isoform VEGF-2, isoform VEGF-3, isoform VEGF-4 and isoform VEGF-5.|||In isoform VEGF-2.|||In isoform VEGF-4.|||In isoform VEGF-5.|||Interchain|||N-VEGF|||N-linked (GlcNAc...) asparagine|||VEGFA|||Vascular endothelial growth factor A, long form ^@ http://purl.uniprot.org/annotation/PRO_0000458067|||http://purl.uniprot.org/annotation/PRO_0000458068|||http://purl.uniprot.org/annotation/PRO_0000458069|||http://purl.uniprot.org/annotation/VSP_061904|||http://purl.uniprot.org/annotation/VSP_061905|||http://purl.uniprot.org/annotation/VSP_061906|||http://purl.uniprot.org/annotation/VSP_061907|||http://purl.uniprot.org/annotation/VSP_061908|||http://purl.uniprot.org/annotation/VSP_061909|||http://purl.uniprot.org/annotation/VSP_061910|||http://purl.uniprot.org/annotation/VSP_061911 http://togogenome.org/gene/10090:Abhd14b ^@ http://purl.uniprot.org/uniprot/E9QN99 ^@ Domain Extent|||Region ^@ Domain Extent ^@ AB hydrolase-1 ^@ http://togogenome.org/gene/10090:Trib2 ^@ http://purl.uniprot.org/uniprot/Q8K4K3 ^@ 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|||Protein kinase|||Tribbles homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000131864 http://togogenome.org/gene/10090:Zbtb20 ^@ http://purl.uniprot.org/uniprot/Q8K0L9 ^@ 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|||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 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|||Phosphothreonine|||Polar residues|||Zinc finger and BTB domain-containing protein 20 ^@ http://purl.uniprot.org/annotation/PRO_0000325961|||http://purl.uniprot.org/annotation/VSP_032504 http://togogenome.org/gene/10090:Cyrib ^@ http://purl.uniprot.org/uniprot/Q921M7 ^@ Chain|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing ^@ Chain|||Crosslink|||Initiator Methionine|||Lipid Binding ^@ CYFIP-related Rac1 interactor B|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000187061 http://togogenome.org/gene/10090:Anapc10 ^@ http://purl.uniprot.org/uniprot/Q8K2H6 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Anaphase-promoting complex subunit 10|||DOC|||N-acetylthreonine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000174012 http://togogenome.org/gene/10090:Cep43 ^@ http://purl.uniprot.org/uniprot/Q66JX5 ^@ 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|||Centrosomal protein 43|||Disordered|||In isoform 2.|||In strain: C57BL/6J.|||LisH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000233295|||http://purl.uniprot.org/annotation/VSP_018122 http://togogenome.org/gene/10090:Ms4a19 ^@ http://purl.uniprot.org/uniprot/Q9D9Y7 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Gpr55 ^@ http://purl.uniprot.org/uniprot/Q14BV9|||http://purl.uniprot.org/uniprot/Q3UJF0 ^@ 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 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_0000233978 http://togogenome.org/gene/10090:Srrd ^@ http://purl.uniprot.org/uniprot/Q8K2M3 ^@ 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.|||SRR1-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000186124|||http://purl.uniprot.org/annotation/VSP_038445 http://togogenome.org/gene/10090:Setd1a ^@ http://purl.uniprot.org/uniprot/E9PYH6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||HCFC1-binding motif (HBM)|||Histone-lysine N-methyltransferase SETD1A|||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_0000445151 http://togogenome.org/gene/10090:Or7c19 ^@ http://purl.uniprot.org/uniprot/Q8VGB8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Stx11 ^@ http://purl.uniprot.org/uniprot/Q3U5V8|||http://purl.uniprot.org/uniprot/Q9D3G5 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent ^@ Syntaxin-11|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000210222 http://togogenome.org/gene/10090:Exosc10 ^@ http://purl.uniprot.org/uniprot/P56960 ^@ 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|||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|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000087134 http://togogenome.org/gene/10090:Bptf ^@ http://purl.uniprot.org/uniprot/E9Q6A7|||http://purl.uniprot.org/uniprot/Q6P9L3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Bromo|||DDT|||Disordered|||PHD-type|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Tm6sf1 ^@ http://purl.uniprot.org/uniprot/D3YX52|||http://purl.uniprot.org/uniprot/P58749 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||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|||Transmembrane 6 superfamily member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000181834 http://togogenome.org/gene/10090:Rhox2f ^@ http://purl.uniprot.org/uniprot/A2ANE0 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Pdia5 ^@ http://purl.uniprot.org/uniprot/Q921X9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Motif|||Signal Peptide ^@ Prevents secretion from ER|||Protein disulfide-isomerase A5|||Redox-active|||Thioredoxin 1|||Thioredoxin 2|||Thioredoxin 3 ^@ http://purl.uniprot.org/annotation/PRO_0000034234 http://togogenome.org/gene/10090:Cox5a ^@ http://purl.uniprot.org/uniprot/P12787 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Cytochrome c oxidase subunit 5A, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000006101 http://togogenome.org/gene/10090:Iqcf1 ^@ http://purl.uniprot.org/uniprot/Q9D9K8 ^@ 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|||IQ 1|||IQ 2|||IQ domain-containing protein F1|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000282557|||http://purl.uniprot.org/annotation/VSP_024186 http://togogenome.org/gene/10090:Amt ^@ http://purl.uniprot.org/uniprot/A2RSW6|||http://purl.uniprot.org/uniprot/Q8CFA2 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Aminomethyltransferase folate-binding|||Aminomethyltransferase, mitochondrial|||Glycine cleavage T-protein C-terminal barrel|||Mitochondrion|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000010756 http://togogenome.org/gene/10090:Fam91a1 ^@ http://purl.uniprot.org/uniprot/B6YY24|||http://purl.uniprot.org/uniprot/Q3UVG3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||FAM91 C-terminal|||FAM91 N-terminal|||Phosphoserine|||Polar residues|||Protein FAM91A1 ^@ http://purl.uniprot.org/annotation/PRO_0000282553 http://togogenome.org/gene/10090:Glcci1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Z9|||http://purl.uniprot.org/uniprot/E9QKK4|||http://purl.uniprot.org/uniprot/Q8K3I9 ^@ 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|||Glucocorticoid-induced transcript 1 protein|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000256129|||http://purl.uniprot.org/annotation/VSP_021321|||http://purl.uniprot.org/annotation/VSP_021322|||http://purl.uniprot.org/annotation/VSP_021323 http://togogenome.org/gene/10090:Rinl ^@ http://purl.uniprot.org/uniprot/Q80UW3 ^@ 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.|||Polar residues|||Ras and Rab interactor-like protein|||VPS9 ^@ http://purl.uniprot.org/annotation/PRO_0000318974|||http://purl.uniprot.org/annotation/VSP_031892|||http://purl.uniprot.org/annotation/VSP_031893 http://togogenome.org/gene/10090:Nlrp4a ^@ http://purl.uniprot.org/uniprot/B2RUQ7|||http://purl.uniprot.org/uniprot/Q8BU40 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Domain Extent|||Repeat ^@ LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||NACHT|||NACHT, LRR and PYD domains-containing protein 4A|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000286329 http://togogenome.org/gene/10090:Setbp1 ^@ http://purl.uniprot.org/uniprot/Q9Z180 ^@ 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 ^@ A.T hook 1|||A.T hook 2|||A.T hook 3|||Basic and acidic residues|||Basic residues|||Disordered|||N6-acetyllysine|||Polar residues|||Pro residues|||SET-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000097699 http://togogenome.org/gene/10090:Plcg2 ^@ http://purl.uniprot.org/uniprot/Q8CIH5 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2|||C2|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Phosphotyrosine|||Phosphotyrosine; by BTK|||SH2 1|||SH2 2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000342364 http://togogenome.org/gene/10090:Nid1 ^@ http://purl.uniprot.org/uniprot/P10493 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Cell attachment site|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6|||Involved in perlecan binding|||LDL-receptor class B 1|||LDL-receptor class B 2|||LDL-receptor class B 3|||LDL-receptor class B 4|||N-linked (GlcNAc...) asparagine|||NIDO|||Nidogen G2 beta-barrel|||Nidogen-1|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; partial|||Sulfotyrosine|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000007670 http://togogenome.org/gene/10090:Sergef ^@ http://purl.uniprot.org/uniprot/Q80YD6 ^@ 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|||Phosphoserine|||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_0000206650 http://togogenome.org/gene/10090:Vmn1r173 ^@ http://purl.uniprot.org/uniprot/E9Q8V7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cma2 ^@ http://purl.uniprot.org/uniprot/Q91VB1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015099489 http://togogenome.org/gene/10090:Itpr3 ^@ http://purl.uniprot.org/uniprot/P70227 ^@ 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|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Inositol 1,4,5-trisphosphate receptor type 3|||Loss of binding activity.|||Loss of calcium flux.|||MIR 1|||MIR 2|||MIR 3|||MIR 4|||MIR 5|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000153929 http://togogenome.org/gene/10090:AU040320 ^@ http://purl.uniprot.org/uniprot/Q8K135|||http://purl.uniprot.org/uniprot/Z4YK56 ^@ 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 ^@ Cytoplasmic|||Disordered|||Dyslexia-associated protein KIAA0319-like protein|||Extracellular|||Helical|||In isoform 2.|||MANSC|||N-linked (GlcNAc...) asparagine|||PKD|||PKD 1|||PKD 2|||PKD 3|||PKD 4|||PKD 5|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000329065|||http://purl.uniprot.org/annotation/VSP_032956 http://togogenome.org/gene/10090:Shcbp1l ^@ http://purl.uniprot.org/uniprot/Q3TTP0 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Repeat ^@ Disordered|||N6-acetyllysine|||O-acetylserine|||PbH1 1|||PbH1 2|||PbH1 3|||PbH1 4|||Phosphoserine|||Testicular spindle-associated protein SHCBP1L ^@ http://purl.uniprot.org/annotation/PRO_0000284839 http://togogenome.org/gene/10090:Pank4 ^@ http://purl.uniprot.org/uniprot/Q80YV4 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ 3'-nitrotyrosine|||4'-phosphopantetheine phosphatase|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Pantothenate kinase|||Phosphoserine|||Phosphothreonine|||Removed|||Subfamily II EGMGR motif ^@ http://purl.uniprot.org/annotation/PRO_0000249248|||http://purl.uniprot.org/annotation/VSP_020379|||http://purl.uniprot.org/annotation/VSP_020380|||http://purl.uniprot.org/annotation/VSP_020381 http://togogenome.org/gene/10090:Zfp995 ^@ http://purl.uniprot.org/uniprot/E9Q6M3 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Esm1 ^@ http://purl.uniprot.org/uniprot/B9EJX9|||http://purl.uniprot.org/uniprot/Q9QYY7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||Endothelial cell-specific molecule 1|||IGFBP N-terminal|||O-linked (Xyl...) (chondroitin sulfate) serine ^@ http://purl.uniprot.org/annotation/PRO_0000014395|||http://purl.uniprot.org/annotation/PRO_5014300278 http://togogenome.org/gene/10090:Nipal2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0G3|||http://purl.uniprot.org/uniprot/Q91WC7 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||NIPA-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000242149 http://togogenome.org/gene/10090:Cpa6 ^@ http://purl.uniprot.org/uniprot/Q5U901 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Signal Peptide|||Splice Variant ^@ Activation peptide|||Carboxypeptidase A6|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004367|||http://purl.uniprot.org/annotation/PRO_0000004368|||http://purl.uniprot.org/annotation/VSP_017081 http://togogenome.org/gene/10090:Sp1 ^@ http://purl.uniprot.org/uniprot/G3X8Q0|||http://purl.uniprot.org/uniprot/O89090 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ 9aaTAD|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Cleavage|||Disordered|||Domain D|||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.|||N-acetylserine|||N6-acetyllysine|||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|||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_0000047138|||http://purl.uniprot.org/annotation/VSP_007376 http://togogenome.org/gene/10090:Dennd5a ^@ http://purl.uniprot.org/uniprot/A0A0R4J1B6|||http://purl.uniprot.org/uniprot/Q6PAL8 ^@ 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 the interaction with RAP6A and localization to Golgi membrane.|||Abolishes the interaction with RAP6A and localization to Golgi membrane; when associated with Ala-935.|||Abolishes the interaction with RAP6A and localization to Golgi membrane; when associated with Ser-932.|||DENN domain-containing protein 5A|||PLAT|||Phosphoserine|||Phosphothreonine|||RUN|||RUN 1|||RUN 2|||UDENN|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000097143 http://togogenome.org/gene/10090:Arhgap44 ^@ http://purl.uniprot.org/uniprot/Q5SSM3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant ^@ BAR|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Interaction with BST2|||PDZ-binding|||Phosphoserine|||Polar residues|||Pro residues|||Reduces GRIA1 recycling. Abolishes the increase of spine density and size, as well as reduces the increase of GRIA1 expression in surface associated with long-term potentiation.|||Rho GTPase-activating protein 44|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000280481|||http://purl.uniprot.org/annotation/VSP_023737|||http://purl.uniprot.org/annotation/VSP_023738|||http://purl.uniprot.org/annotation/VSP_023739|||http://purl.uniprot.org/annotation/VSP_023740|||http://purl.uniprot.org/annotation/VSP_023741 http://togogenome.org/gene/10090:Kdf1 ^@ http://purl.uniprot.org/uniprot/A2A9F4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Keratinocyte differentiation factor 1|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000289049 http://togogenome.org/gene/10090:Bnc1 ^@ http://purl.uniprot.org/uniprot/F8VPY0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Wwtr1 ^@ http://purl.uniprot.org/uniprot/Q9EPK5 ^@ 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 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Loss of SLC9A3R2 binding and reduced nuclear localization. Partial recovery of nuclear accumulation; when associated with A-89.|||Loss of YWHAZ binding with increased nuclear localization. Partial recovery of nuclear accumulation; when associated with deletion of 392-L--L-395.|||PDZ-binding|||Phosphoserine|||Phosphoserine; by LATS2|||Polar residues|||Required for interaction with PALS1|||WW|||WW domain-containing transcription regulator protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000076070|||http://purl.uniprot.org/annotation/VSP_026137 http://togogenome.org/gene/10090:Fem1a ^@ http://purl.uniprot.org/uniprot/Q9Z2G1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Decreased ability to promote PGE2-EP4-mediated inhibition of inflammation; when associated with A-108.|||Decreased ability to promote PGE2-EP4-mediated inhibition of inflammation; when associated with A-608.|||Disordered|||Phosphoserine|||Polar residues|||Protein fem-1 homolog A-A|||TPR 1|||TPR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000324526 http://togogenome.org/gene/10090:Spata6 ^@ http://purl.uniprot.org/uniprot/Q3U6K5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Spermatogenesis-associated protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000278442|||http://purl.uniprot.org/annotation/VSP_023278|||http://purl.uniprot.org/annotation/VSP_023279|||http://purl.uniprot.org/annotation/VSP_023280 http://togogenome.org/gene/10090:Arhgef9 ^@ http://purl.uniprot.org/uniprot/Q3UTH8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ DH|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with GPHN|||PH|||Phosphoserine|||Rho guanine nucleotide exchange factor 9|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000253896|||http://purl.uniprot.org/annotation/VSP_021143|||http://purl.uniprot.org/annotation/VSP_021144|||http://purl.uniprot.org/annotation/VSP_021145|||http://purl.uniprot.org/annotation/VSP_021146 http://togogenome.org/gene/10090:Trip6 ^@ http://purl.uniprot.org/uniprot/B2RS30|||http://purl.uniprot.org/uniprot/Q9Z1Y4 ^@ 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 ^@ Asymmetric dimethylarginine; alternate|||Disordered|||Interaction with MAGI1 and PTPN13|||Interacts with PDLIM4. Loss of interaction with PTPN13.|||LIM zinc-binding|||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|||Thyroid receptor-interacting protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000274689 http://togogenome.org/gene/10090:Gjb5 ^@ http://purl.uniprot.org/uniprot/Q02739|||http://purl.uniprot.org/uniprot/Q542M8 ^@ 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_0000057869 http://togogenome.org/gene/10090:Gm3159 ^@ http://purl.uniprot.org/uniprot/K7N6T3 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:Tceal9 ^@ http://purl.uniprot.org/uniprot/Q9DD24 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Transcription elongation factor A protein-like 9 ^@ http://purl.uniprot.org/annotation/PRO_0000274047 http://togogenome.org/gene/10090:Man2b1 ^@ http://purl.uniprot.org/uniprot/O09159 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Lysosomal alpha-mannosidase|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000012076 http://togogenome.org/gene/10090:Car11 ^@ http://purl.uniprot.org/uniprot/O70354|||http://purl.uniprot.org/uniprot/Q541E9 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase-related protein 11|||Disordered|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000004246|||http://purl.uniprot.org/annotation/PRO_5014309533 http://togogenome.org/gene/10090:Thoc2l ^@ http://purl.uniprot.org/uniprot/E9Q5E2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||THO complex subunit 2 N-terminal|||THO complex subunitTHOC2 C-terminal|||THO complex subunitTHOC2 N-terminal ^@ http://togogenome.org/gene/10090:Ret ^@ http://purl.uniprot.org/uniprot/P35546 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||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|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes interaction with DOK proteins.|||Cadherin|||Cleavage; by caspase-3|||Cytoplasmic|||Extracellular|||Extracellular cell-membrane anchored RET cadherin 120 kDa fragment|||Helical|||In isoform 2.|||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_0000024451|||http://purl.uniprot.org/annotation/PRO_0000415294|||http://purl.uniprot.org/annotation/PRO_0000415295|||http://purl.uniprot.org/annotation/VSP_011304 http://togogenome.org/gene/10090:Pgm2l1 ^@ http://purl.uniprot.org/uniprot/Q8CAA7 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ Glucose 1,6-bisphosphate synthase|||Phosphoserine|||Phosphoserine intermediate|||via phosphate group ^@ http://purl.uniprot.org/annotation/PRO_0000147785 http://togogenome.org/gene/10090:Arpc5 ^@ http://purl.uniprot.org/uniprot/Q9CPW4 ^@ 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|||Actin-related protein 2/3 complex subunit 5|||Disordered|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000124055 http://togogenome.org/gene/10090:Cdh24 ^@ http://purl.uniprot.org/uniprot/Q6PFX6 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-24|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000320100|||http://purl.uniprot.org/annotation/PRO_0000320101 http://togogenome.org/gene/10090:Zc3h10 ^@ http://purl.uniprot.org/uniprot/Q8R205 ^@ 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 ^@ C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||Omega-N-methylarginine|||Polar residues|||Pro residues|||Zinc finger CCCH domain-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000281146 http://togogenome.org/gene/10090:Gcsam ^@ http://purl.uniprot.org/uniprot/Q6RFH4 ^@ 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|||Germinal center-associated signaling and motility protein|||In isoform 2.|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000256229|||http://purl.uniprot.org/annotation/VSP_021334 http://togogenome.org/gene/10090:Tacr2 ^@ http://purl.uniprot.org/uniprot/P30549|||http://purl.uniprot.org/uniprot/Q3KP20|||http://purl.uniprot.org/uniprot/Q8BZV9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Substance-K receptor ^@ http://purl.uniprot.org/annotation/PRO_0000069895 http://togogenome.org/gene/10090:Cilp ^@ http://purl.uniprot.org/uniprot/A0A0R4J0F8|||http://purl.uniprot.org/uniprot/Q66K08 ^@ 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 1|||Cartilage intermediate layer protein 1 C1|||Cartilage intermediate layer protein 1 C2|||Disordered|||Ig-like|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||TSP type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000014674|||http://purl.uniprot.org/annotation/PRO_0000014675|||http://purl.uniprot.org/annotation/PRO_0000014676|||http://purl.uniprot.org/annotation/PRO_5006451957 http://togogenome.org/gene/10090:Adora3 ^@ http://purl.uniprot.org/uniprot/Q3U4C5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Smc3 ^@ http://purl.uniprot.org/uniprot/Q1HL32|||http://purl.uniprot.org/uniprot/Q3TMK9|||http://purl.uniprot.org/uniprot/Q9CW03 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolishes interaction with MXI1.|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RecF/RecN/SMC N-terminal|||SMC hinge|||Structural maintenance of chromosomes protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000119002 http://togogenome.org/gene/10090:Ehbp1 ^@ http://purl.uniprot.org/uniprot/Q69ZW3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||C2 NT-type|||CAAX motif|||Calponin-homology (CH)|||Disordered|||EH domain-binding protein 1|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||bMERB ^@ http://purl.uniprot.org/annotation/PRO_0000285203|||http://purl.uniprot.org/annotation/VSP_024836 http://togogenome.org/gene/10090:Dr1 ^@ http://purl.uniprot.org/uniprot/Q91WV0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Disordered|||Histone-fold|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein Dr1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000072441 http://togogenome.org/gene/10090:Tubb5 ^@ http://purl.uniprot.org/uniprot/P99024 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 5-glutamyl polyglutamate|||5-glutamyl polyglycine|||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|||Loss of CDK1-mediated phosphorylation.|||MREI motif|||Mimics phosphorylation, unable to incorporate into microtubules.|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Tubulin beta-5 chain ^@ http://purl.uniprot.org/annotation/PRO_0000048246 http://togogenome.org/gene/10090:Pate11 ^@ http://purl.uniprot.org/uniprot/B3GLJ6 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015087269 http://togogenome.org/gene/10090:Ebp ^@ http://purl.uniprot.org/uniprot/P70245 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Transmembrane ^@ 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase|||EXPERA|||Helical|||In Td.|||N-acetylthreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000174343 http://togogenome.org/gene/10090:Or10a2 ^@ http://purl.uniprot.org/uniprot/Q7TRN0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ddx39a ^@ http://purl.uniprot.org/uniprot/Q3UAF1|||http://purl.uniprot.org/uniprot/Q8VDW0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||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.|||N-acetylalanine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Q motif|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000055068|||http://purl.uniprot.org/annotation/VSP_013064 http://togogenome.org/gene/10090:Zfp324 ^@ http://purl.uniprot.org/uniprot/Q78F42 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB|||KRAB-related|||Polar residues ^@ http://togogenome.org/gene/10090:Gzmd ^@ http://purl.uniprot.org/uniprot/P11033 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Granzyme D|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027405|||http://purl.uniprot.org/annotation/PRO_0000027406 http://togogenome.org/gene/10090:Aplf ^@ http://purl.uniprot.org/uniprot/Q9D842 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Acidic residues|||Aprataxin and PNK-like factor|||Disordered|||FHA-like|||Flexible linker|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||KBM|||NAP1L motif|||PBZ-type 1|||PBZ-type 2|||Phosphoserine|||Phosphoserine; by ATM|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089343|||http://purl.uniprot.org/annotation/VSP_014982|||http://purl.uniprot.org/annotation/VSP_014983|||http://purl.uniprot.org/annotation/VSP_014984 http://togogenome.org/gene/10090:Pou3f2 ^@ http://purl.uniprot.org/uniprot/P31360 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||POU domain, class 3, transcription factor 2|||POU-specific|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000100723 http://togogenome.org/gene/10090:Hspa1b ^@ http://purl.uniprot.org/uniprot/P17879 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Heat shock 70 kDa protein 1B|||N-acetylalanine|||N6,N6,N6-trimethyllysine; by METTL21A; alternate|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||Nucleotide-binding domain (NBD)|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Removed|||Substrate-binding domain (SBD) ^@ http://purl.uniprot.org/annotation/PRO_0000078251 http://togogenome.org/gene/10090:Insig2 ^@ http://purl.uniprot.org/uniprot/A0A087WQP7|||http://purl.uniprot.org/uniprot/Q91WG1 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Modified Residue|||Motif|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cysteine sulfenic acid (-SOH); alternate|||Cytoplasmic|||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|||Lumenal|||Phosphoserine|||Required for the recognition of 25-hydroxycholesterol ^@ http://purl.uniprot.org/annotation/PRO_0000286798 http://togogenome.org/gene/10090:Trpd52l3 ^@ http://purl.uniprot.org/uniprot/Q9CQ14 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rnase9 ^@ http://purl.uniprot.org/uniprot/P60154|||http://purl.uniprot.org/uniprot/Q5QJV3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Inactive ribonuclease-like protein 9|||N-linked (GlcNAc...) asparagine|||Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_0000030956|||http://purl.uniprot.org/annotation/PRO_5010140281 http://togogenome.org/gene/10090:Lyzl6 ^@ http://purl.uniprot.org/uniprot/A0A077S2U3|||http://purl.uniprot.org/uniprot/Q9DA11 ^@ 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 ^@ C-type lysozyme|||Glycosyl hydrolases family 22 (GH22)|||Lysozyme-like protein 6|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000240641|||http://purl.uniprot.org/annotation/PRO_5014216938 http://togogenome.org/gene/10090:Vgll4 ^@ http://purl.uniprot.org/uniprot/Q80V24 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Helix|||Modified Residue|||Region|||Strand ^@ Disordered|||Phosphoserine|||Transcription cofactor vestigial-like protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000191352 http://togogenome.org/gene/10090:Slc22a27 ^@ http://purl.uniprot.org/uniprot/Q76M72 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 27 ^@ http://purl.uniprot.org/annotation/PRO_0000436775|||http://purl.uniprot.org/annotation/VSP_058421 http://togogenome.org/gene/10090:Gas6 ^@ http://purl.uniprot.org/uniprot/Q61592 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ 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|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000007590 http://togogenome.org/gene/10090:Tmem266 ^@ http://purl.uniprot.org/uniprot/Q8BZB3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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_0000244096|||http://purl.uniprot.org/annotation/VSP_019514|||http://purl.uniprot.org/annotation/VSP_019515|||http://purl.uniprot.org/annotation/VSP_022109|||http://purl.uniprot.org/annotation/VSP_022110 http://togogenome.org/gene/10090:Or56a3b ^@ http://purl.uniprot.org/uniprot/Q3SXH8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ptpn9 ^@ http://purl.uniprot.org/uniprot/O35239|||http://purl.uniprot.org/uniprot/Q2M4G8 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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_0000094765 http://togogenome.org/gene/10090:Ccl28 ^@ http://purl.uniprot.org/uniprot/Q9JIL2 ^@ 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 ^@ Basic residues|||C-C motif chemokine 28|||Disordered|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000005243 http://togogenome.org/gene/10090:Gpr88 ^@ http://purl.uniprot.org/uniprot/B2RXU4|||http://purl.uniprot.org/uniprot/Q9EPB7 ^@ 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 88 ^@ http://purl.uniprot.org/annotation/PRO_0000069598 http://togogenome.org/gene/10090:Dnajc4 ^@ http://purl.uniprot.org/uniprot/Q9D844 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||DnaJ homolog subfamily C member 4|||Helical|||J|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000071050 http://togogenome.org/gene/10090:Rgs11 ^@ http://purl.uniprot.org/uniprot/G3X8W6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ DEP|||Disordered|||Polar residues|||RGS ^@ http://togogenome.org/gene/10090:Misp ^@ http://purl.uniprot.org/uniprot/Q9D279 ^@ 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|||Mitotic interactor and substrate of PLK1|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphothreonine; by CDK1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079382 http://togogenome.org/gene/10090:Nf2 ^@ http://purl.uniprot.org/uniprot/P46662|||http://purl.uniprot.org/uniprot/Q3TIW4|||http://purl.uniprot.org/uniprot/Q9D3K3 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Disordered|||FERM|||In isoform 2.|||Merlin|||Phosphoserine|||Phosphoserine; by PAK|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000219413|||http://purl.uniprot.org/annotation/VSP_000493 http://togogenome.org/gene/10090:Bloc1s3 ^@ http://purl.uniprot.org/uniprot/Q5U5M8 ^@ 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_0000234549 http://togogenome.org/gene/10090:Gvin3 ^@ http://purl.uniprot.org/uniprot/Q3TBC0 ^@ Experimental Information|||Non-terminal Residue ^@ Non-terminal Residue ^@ ^@ http://togogenome.org/gene/10090:3110040N11Rik ^@ http://purl.uniprot.org/uniprot/Q9CRC3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||UPF0235 protein C15orf40 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000139476 http://togogenome.org/gene/10090:Tbcd ^@ http://purl.uniprot.org/uniprot/Q8BYA0 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||Tubulin-specific chaperone D ^@ http://purl.uniprot.org/annotation/PRO_0000080050 http://togogenome.org/gene/10090:Gpr107 ^@ http://purl.uniprot.org/uniprot/Q148Z6|||http://purl.uniprot.org/uniprot/Q8BUV8 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||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|||Phosphoserine|||Protein GPR107 ^@ http://purl.uniprot.org/annotation/PRO_0000021341|||http://purl.uniprot.org/annotation/PRO_5015097029 http://togogenome.org/gene/10090:Sesn1 ^@ http://purl.uniprot.org/uniprot/P58006 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ C-terminal domain; mediates TORC1 regulation|||Cysteine sulfenic acid (-SOH) intermediate|||N-terminal domain; may mediate the alkylhydroperoxide reductase activity|||Phosphoserine|||Sestrin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000221179 http://togogenome.org/gene/10090:Otop2 ^@ http://purl.uniprot.org/uniprot/Q80SX5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Proton channel OTOP2 ^@ http://purl.uniprot.org/annotation/PRO_0000313821 http://togogenome.org/gene/10090:Hs3st3a1 ^@ http://purl.uniprot.org/uniprot/Q52KJ0|||http://purl.uniprot.org/uniprot/Q8BKN6 ^@ 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|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||For sulfotransferase activity|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate glucosamine 3-O-sulfotransferase 3A1|||Lumenal|||N-linked (GlcNAc...) asparagine|||Sulfotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000085218 http://togogenome.org/gene/10090:Fancl ^@ http://purl.uniprot.org/uniprot/Q9CR14 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ E3 ubiquitin-protein ligase FANCL|||In isoform 2.|||RING-type; degenerate|||UBC-RWD region (URD) ^@ http://purl.uniprot.org/annotation/PRO_0000055909|||http://purl.uniprot.org/annotation/VSP_008552 http://togogenome.org/gene/10090:Ccdc8 ^@ http://purl.uniprot.org/uniprot/D3YZV8 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 8 homolog|||Disordered|||Phosphoserine|||Polar residues|||PxLPxI/L motif; mediates interaction with ANKRA2 ^@ http://purl.uniprot.org/annotation/PRO_0000415807 http://togogenome.org/gene/10090:Trim39 ^@ http://purl.uniprot.org/uniprot/E9QLN4|||http://purl.uniprot.org/uniprot/Q570Z1|||http://purl.uniprot.org/uniprot/Q9ESN2 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM39|||In isoform 2.|||In isoform 3.|||Interaction with CDKN1A|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056258|||http://purl.uniprot.org/annotation/VSP_012063|||http://purl.uniprot.org/annotation/VSP_012064|||http://purl.uniprot.org/annotation/VSP_012065 http://togogenome.org/gene/10090:Lpcat3 ^@ http://purl.uniprot.org/uniprot/Q91V01 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Transmembrane ^@ Di-lysine motif|||Helical|||Loss of O-acyltransferase activity.|||Lysophospholipid acyltransferase 5|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000233383 http://togogenome.org/gene/10090:Pycrl ^@ http://purl.uniprot.org/uniprot/Q9DCC4 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ N-acetylalanine|||Pyrroline-5-carboxylate reductase 3|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000324563 http://togogenome.org/gene/10090:P3h4 ^@ http://purl.uniprot.org/uniprot/Q8K2B0 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide ^@ Acidic residues|||Disordered|||Endoplasmic reticulum protein SC65|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000320294 http://togogenome.org/gene/10090:Dnajc1 ^@ http://purl.uniprot.org/uniprot/Q61712 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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_0000071043 http://togogenome.org/gene/10090:Cd164l2 ^@ http://purl.uniprot.org/uniprot/Q3TYL8|||http://purl.uniprot.org/uniprot/Q9D6W7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||CD164 sialomucin-like 2 protein|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000045780 http://togogenome.org/gene/10090:Klre1 ^@ http://purl.uniprot.org/uniprot/Q8CJC7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Killer cell lectin-like receptor subfamily E member 1|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000442197 http://togogenome.org/gene/10090:Mfsd5 ^@ http://purl.uniprot.org/uniprot/Q921Y4 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Molybdate-anion transporter ^@ http://purl.uniprot.org/annotation/PRO_0000273402 http://togogenome.org/gene/10090:Map4k2 ^@ http://purl.uniprot.org/uniprot/Q14B83|||http://purl.uniprot.org/uniprot/Q61161 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ CNH|||Disordered|||Mitogen-activated protein kinase kinase kinase kinase 2|||PEST1|||PEST2|||PEST3|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||non-specific serine/threonine protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000086276|||http://purl.uniprot.org/annotation/PRO_5004182986 http://togogenome.org/gene/10090:Rps26 ^@ http://purl.uniprot.org/uniprot/P62855|||http://purl.uniprot.org/uniprot/Q497N1 ^@ 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|||Small ribosomal subunit protein eS26 ^@ http://purl.uniprot.org/annotation/PRO_0000204511 http://togogenome.org/gene/10090:Mgst3 ^@ http://purl.uniprot.org/uniprot/Q9CPU4 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Lipid Binding|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Glutathione S-transferase 3, mitochondrial|||Helical|||Mitochondrial intermembrane|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000217742 http://togogenome.org/gene/10090:Aqp8 ^@ http://purl.uniprot.org/uniprot/A0A0X1KG59|||http://purl.uniprot.org/uniprot/P56404|||http://purl.uniprot.org/uniprot/Q3UJ16 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Aquaporin-8|||Cysteine persulfide|||Cysteine sulfenic acid (-SOH)|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000063962 http://togogenome.org/gene/10090:Ppm1b ^@ http://purl.uniprot.org/uniprot/P36993|||http://purl.uniprot.org/uniprot/Q546R1|||http://purl.uniprot.org/uniprot/Q99NF7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-myristoyl glycine|||PPM-type phosphatase|||Phosphoserine|||Protein phosphatase 1B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057747|||http://purl.uniprot.org/annotation/VSP_005090|||http://purl.uniprot.org/annotation/VSP_005091|||http://purl.uniprot.org/annotation/VSP_005092 http://togogenome.org/gene/10090:Sspo ^@ http://purl.uniprot.org/uniprot/E9Q0I4 ^@ 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 ^@ CTCK|||Disordered|||F5/8 type C|||Polar residues|||SCO-spondin|||VWFC|||VWFD ^@ http://purl.uniprot.org/annotation/PRO_5003245575 http://togogenome.org/gene/10090:Med13 ^@ http://purl.uniprot.org/uniprot/Q5SWW4 ^@ 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|||LXXLL motif 1|||LXXLL motif 2|||Mediator of RNA polymerase II transcription subunit 13|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314240 http://togogenome.org/gene/10090:Or5w10 ^@ http://purl.uniprot.org/uniprot/Q7TR47 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r61 ^@ http://purl.uniprot.org/uniprot/L7N2B8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982397 http://togogenome.org/gene/10090:Myzap ^@ http://purl.uniprot.org/uniprot/Q3UIJ9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Myocardial zonula adherens protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000326226 http://togogenome.org/gene/10090:Actr3b ^@ http://purl.uniprot.org/uniprot/Q641P0 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ Actin-related protein 3B|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000342359|||http://purl.uniprot.org/annotation/VSP_034419 http://togogenome.org/gene/10090:Smad2 ^@ http://purl.uniprot.org/uniprot/Q62432 ^@ 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 ^@ Disordered|||In isoform Short.|||MH1|||MH2|||Mothers against decapentaplegic homolog 2|||N-acetylserine|||N6-acetyllysine|||PY-motif|||Phosphoserine|||Phosphoserine; by CAMK2|||Phosphoserine; by TGFBR1|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000090853|||http://purl.uniprot.org/annotation/VSP_021571 http://togogenome.org/gene/10090:Ttc9c ^@ http://purl.uniprot.org/uniprot/Q810A3 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 9C ^@ http://purl.uniprot.org/annotation/PRO_0000294467 http://togogenome.org/gene/10090:Cacna1b ^@ http://purl.uniprot.org/uniprot/A2AIR9|||http://purl.uniprot.org/uniprot/A2AIS0|||http://purl.uniprot.org/uniprot/O55017 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Basic 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 isoform NB2.|||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_0000053922|||http://purl.uniprot.org/annotation/VSP_000883 http://togogenome.org/gene/10090:Nck2 ^@ http://purl.uniprot.org/uniprot/O55033|||http://purl.uniprot.org/uniprot/Q8BQ28 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Cytoplasmic protein NCK2|||Disordered|||N-acetylthreonine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||SH2|||SH3|||SH3 1|||SH3 2|||SH3 3 ^@ http://purl.uniprot.org/annotation/PRO_0000415287 http://togogenome.org/gene/10090:Icosl ^@ http://purl.uniprot.org/uniprot/Q544C7|||http://purl.uniprot.org/uniprot/Q9JHJ8 ^@ 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|||Helical|||ICOS ligand|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014804|||http://purl.uniprot.org/annotation/VSP_002521 http://togogenome.org/gene/10090:Haus8 ^@ http://purl.uniprot.org/uniprot/Q99L00 ^@ 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|||HAUS augmin-like complex subunit 8|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000319938|||http://purl.uniprot.org/annotation/VSP_031544 http://togogenome.org/gene/10090:Eef1akmt2 ^@ http://purl.uniprot.org/uniprot/D3Z7D0|||http://purl.uniprot.org/uniprot/Q9D853 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||EEF1A lysine methyltransferase 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000325883 http://togogenome.org/gene/10090:Zfp958 ^@ http://purl.uniprot.org/uniprot/Q99LG7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Peg3 ^@ http://purl.uniprot.org/uniprot/Q3URU2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 1-1|||1-10|||1-2|||1-3|||1-4|||1-5|||1-6|||1-7|||1-8|||1-9|||10 X 5 AA repeat of P-H-X-X-E|||2-1|||2-2|||2-3|||3 X 5 AA repeat of P-H-D-D-K|||Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 10; degenerate|||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.|||Paternally-expressed gene 3 protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000249229|||http://purl.uniprot.org/annotation/VSP_020375|||http://purl.uniprot.org/annotation/VSP_020376|||http://purl.uniprot.org/annotation/VSP_020377 http://togogenome.org/gene/10090:Atat1 ^@ http://purl.uniprot.org/uniprot/Q8K341 ^@ 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|||Site|||Splice Variant ^@ Alpha-tubulin N-acetyltransferase 1|||Asymmetric dimethylarginine|||Basic and acidic residues|||Crucial for catalytic activity|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||Loss of activity, but function in microtubule stability not affected; when associated with W-134 and P-139.|||Loss of activity, but function in microtubule stability not affected; when associated with W-134 and W-136.|||Loss of catalytic activity, but function in microtubule stability not affected; when associated with W-136 and P-139.|||N-acetyltransferase|||N6-acetyllysine; by autocatalysis|||Omega-N-methylarginine|||Phosphoserine|||Pro residues|||Required for AP2A2-binding|||Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-146; R-233 and R-244.|||Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-56; R-146 and R-233.|||Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-56; R-146 and R-244.|||Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-56; R-233 and R-244. ^@ http://purl.uniprot.org/annotation/PRO_0000348067|||http://purl.uniprot.org/annotation/VSP_052905|||http://purl.uniprot.org/annotation/VSP_052906|||http://purl.uniprot.org/annotation/VSP_052907|||http://purl.uniprot.org/annotation/VSP_052908|||http://purl.uniprot.org/annotation/VSP_052909 http://togogenome.org/gene/10090:Or8k35 ^@ http://purl.uniprot.org/uniprot/A0A1L1SUC9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Jtb ^@ http://purl.uniprot.org/uniprot/O88824|||http://purl.uniprot.org/uniprot/Q542D4|||http://purl.uniprot.org/uniprot/Q9D0T9 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Abolishes N-terminal proteolytic processing.|||Cytoplasmic|||Extracellular|||Helical|||Protein JTB ^@ http://purl.uniprot.org/annotation/PRO_0000021536|||http://purl.uniprot.org/annotation/PRO_5004325855|||http://purl.uniprot.org/annotation/PRO_5014309594 http://togogenome.org/gene/10090:Nkap ^@ http://purl.uniprot.org/uniprot/Q9D0F4 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000259646 http://togogenome.org/gene/10090:Or1m1 ^@ http://purl.uniprot.org/uniprot/Q8VFM9 ^@ 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_0000352790 http://togogenome.org/gene/10090:Hnrnph3 ^@ http://purl.uniprot.org/uniprot/D3YWT1|||http://purl.uniprot.org/uniprot/D3Z3N4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ RRM ^@ http://togogenome.org/gene/10090:Kctd12b ^@ http://purl.uniprot.org/uniprot/Q8C7J6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Stx8 ^@ http://purl.uniprot.org/uniprot/O88983 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||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_0000210218 http://togogenome.org/gene/10090:Kcnk6 ^@ http://purl.uniprot.org/uniprot/Q3TBV4|||http://purl.uniprot.org/uniprot/Q3TQ68|||http://purl.uniprot.org/uniprot/Q3V1G1 ^@ Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Non-terminal Residue|||Region|||Transmembrane ^@ Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Potassium channel ^@ http://togogenome.org/gene/10090:Prrt1 ^@ http://purl.uniprot.org/uniprot/A2CG20|||http://purl.uniprot.org/uniprot/O35449 ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Pro residues|||Proline-rich transmembrane protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000135698 http://togogenome.org/gene/10090:Stk32a ^@ http://purl.uniprot.org/uniprot/Q8BGW6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||N-myristoyl glycine|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase 32A ^@ http://purl.uniprot.org/annotation/PRO_0000232412|||http://purl.uniprot.org/annotation/VSP_051996 http://togogenome.org/gene/10090:4930579F01Rik ^@ http://purl.uniprot.org/uniprot/A0A0G2JEX5|||http://purl.uniprot.org/uniprot/E9Q3L6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Slc20a1 ^@ http://purl.uniprot.org/uniprot/Q61609 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ A|||Confers virus infectibility.|||Disordered|||Helical|||Phosphoserine|||Sodium-dependent phosphate transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000080772 http://togogenome.org/gene/10090:Or9k2b ^@ http://purl.uniprot.org/uniprot/Q8VFU6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Micall1 ^@ http://purl.uniprot.org/uniprot/Q8BGT6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Calponin-homology (CH)|||Disordered|||In isoform 2.|||In isoform 3.|||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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||bMERB ^@ http://purl.uniprot.org/annotation/PRO_0000075849|||http://purl.uniprot.org/annotation/VSP_009851|||http://purl.uniprot.org/annotation/VSP_009852|||http://purl.uniprot.org/annotation/VSP_009853 http://togogenome.org/gene/10090:Fndc11 ^@ http://purl.uniprot.org/uniprot/Q80WB0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Fibronectin type III domain-containing protein 11|||Fibronectin type-III|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000232868 http://togogenome.org/gene/10090:Plaur ^@ http://purl.uniprot.org/uniprot/P35456|||http://purl.uniprot.org/uniprot/Q545X5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ GPI-anchor amidated glycine|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6|||UPAR/Ly6 1|||UPAR/Ly6 2|||UPAR/Ly6 3|||UPAR/Ly6 domain-containing protein|||Urokinase plasminogen activator surface receptor ^@ http://purl.uniprot.org/annotation/PRO_0000036096|||http://purl.uniprot.org/annotation/PRO_0000036097|||http://purl.uniprot.org/annotation/PRO_5010844044|||http://purl.uniprot.org/annotation/VSP_031837|||http://purl.uniprot.org/annotation/VSP_031838 http://togogenome.org/gene/10090:Ceacam12 ^@ http://purl.uniprot.org/uniprot/Q3UKP4|||http://purl.uniprot.org/uniprot/Q3V2Q3|||http://purl.uniprot.org/uniprot/Q9DAS5|||http://purl.uniprot.org/uniprot/Q9DAZ3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Immunoglobulin V-set ^@ http://togogenome.org/gene/10090:Rtl8c ^@ http://purl.uniprot.org/uniprot/Q9D6I0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ DUF4939 ^@ http://togogenome.org/gene/10090:Cpb2 ^@ http://purl.uniprot.org/uniprot/Q9JHH6 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Activation peptide|||Carboxypeptidase B2|||Cleavage; by thrombin|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004379|||http://purl.uniprot.org/annotation/PRO_0000004380 http://togogenome.org/gene/10090:Rpl34 ^@ http://purl.uniprot.org/uniprot/Q9D1R9 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Crosslink|||Modified Residue ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL34|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000131832 http://togogenome.org/gene/10090:Nsun5 ^@ http://purl.uniprot.org/uniprot/Q8K4F6 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 28S rRNA (cytosine-C(5))-methyltransferase|||Disordered|||N-acetylglycine|||Nucleophile|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000261670 http://togogenome.org/gene/10090:Cacng4 ^@ http://purl.uniprot.org/uniprot/A2AAU2|||http://purl.uniprot.org/uniprot/Q9JJV4 ^@ 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_0000164679 http://togogenome.org/gene/10090:Prr5 ^@ http://purl.uniprot.org/uniprot/Q812A5 ^@ 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.|||Interaction with RICTOR|||Phosphoserine|||Polar residues|||Proline-rich protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000308163|||http://purl.uniprot.org/annotation/VSP_052580 http://togogenome.org/gene/10090:Uchl1 ^@ http://purl.uniprot.org/uniprot/Q9R0P9 ^@ Active Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Abolishes enzymatic activity and ubiquitin binding.|||Abolishes enzymatic activity, but does not affect ubiquitin binding.|||Important for enzyme activity|||Interaction with ubiquitin|||Nucleophile|||Phosphoserine|||Proton donor|||Removed in mature form|||S-farnesyl cysteine|||Ubiquitin carboxyl-terminal hydrolase isozyme L1 ^@ http://purl.uniprot.org/annotation/PRO_0000211058|||http://purl.uniprot.org/annotation/PRO_0000414313 http://togogenome.org/gene/10090:Cpne3 ^@ http://purl.uniprot.org/uniprot/Q8BT60 ^@ 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 ^@ C2 1|||C2 2|||Copine-3|||Phosphoserine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000144839 http://togogenome.org/gene/10090:Or9a4 ^@ http://purl.uniprot.org/uniprot/Q8VF31 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Aldh3b2 ^@ http://purl.uniprot.org/uniprot/E9Q3E1 ^@ Active Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Site ^@ Active Site|||Chain|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide ^@ Aldehyde dehydrogenase family 3 member B2|||Cysteine methyl ester|||Reduces lipid droplet localization.|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000436528|||http://purl.uniprot.org/annotation/PRO_0000436529 http://togogenome.org/gene/10090:Inha ^@ http://purl.uniprot.org/uniprot/Q04997 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage|||Inhibin alpha N-terminal region|||Inhibin alpha chain|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033688|||http://purl.uniprot.org/annotation/PRO_0000033689|||http://purl.uniprot.org/annotation/PRO_0000033690 http://togogenome.org/gene/10090:Cideb ^@ http://purl.uniprot.org/uniprot/O70303|||http://purl.uniprot.org/uniprot/Q3V4D3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ Abolished interaction with PREB.|||CIDE-N|||Lipid transferase CIDEB|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000144721 http://togogenome.org/gene/10090:Tmem38b ^@ http://purl.uniprot.org/uniprot/Q9DAV9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||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|||Lumenal|||Polar residues|||Trimeric intracellular cation channel type B ^@ http://purl.uniprot.org/annotation/PRO_0000291525 http://togogenome.org/gene/10090:Ccdc65 ^@ http://purl.uniprot.org/uniprot/Q8VHI7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant ^@ Dynein regulatory complex subunit 2|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000284780|||http://purl.uniprot.org/annotation/VSP_024645 http://togogenome.org/gene/10090:Meis1 ^@ http://purl.uniprot.org/uniprot/Q60954 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant ^@ Disordered|||Homeobox protein Meis1|||Homeobox; TALE-type|||In isoform 2.|||In isoform 3.|||Interaction with DNA|||Loss of binding to other proteins.|||MEIS N-terminal|||No effect on cooperative binding with PBX1 to CYP17.|||Polar residues|||Required for transcriptional activation ^@ http://purl.uniprot.org/annotation/PRO_0000049106|||http://purl.uniprot.org/annotation/VSP_002240|||http://purl.uniprot.org/annotation/VSP_017056 http://togogenome.org/gene/10090:Pcdhb3 ^@ http://purl.uniprot.org/uniprot/Q91XZ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Cadherin|||Helical ^@ http://togogenome.org/gene/10090:Smim15 ^@ http://purl.uniprot.org/uniprot/Q3UTD9 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Transmembrane ^@ Disordered|||Helical|||Small integral membrane protein 15 ^@ http://purl.uniprot.org/annotation/PRO_0000326076 http://togogenome.org/gene/10090:Lipo2 ^@ http://purl.uniprot.org/uniprot/D3YY49 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Signal Peptide ^@ Charge relay system|||Lipase|||Nucleophile|||Partial AB-hydrolase lipase ^@ http://purl.uniprot.org/annotation/PRO_5013243321 http://togogenome.org/gene/10090:Or51a6 ^@ http://purl.uniprot.org/uniprot/Q8VH16 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Atp13a3 ^@ http://purl.uniprot.org/uniprot/Q5XF89 ^@ Active Site|||Binding Site|||Chain|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||INTRAMEM|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Phosphoserine|||Polyamine-transporting ATPase 13A3 ^@ http://purl.uniprot.org/annotation/PRO_0000363358|||http://purl.uniprot.org/annotation/VSP_036301 http://togogenome.org/gene/10090:Tbc1d32 ^@ http://purl.uniprot.org/uniprot/Q3URV1 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ In isoform 2.|||Protein broad-minded|||Rab-GAP TBC ^@ http://purl.uniprot.org/annotation/PRO_0000393609|||http://purl.uniprot.org/annotation/VSP_039021 http://togogenome.org/gene/10090:Rabep1 ^@ http://purl.uniprot.org/uniprot/J3QJV7|||http://purl.uniprot.org/uniprot/O35551 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Rab GTPase-binding effector protein 1|||Rabaptin GTPase-Rab5 binding|||Rabaptin coiled-coil|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000187557|||http://purl.uniprot.org/annotation/VSP_010452|||http://purl.uniprot.org/annotation/VSP_010453|||http://purl.uniprot.org/annotation/VSP_010454|||http://purl.uniprot.org/annotation/VSP_010455|||http://purl.uniprot.org/annotation/VSP_010456|||http://purl.uniprot.org/annotation/VSP_010457|||http://purl.uniprot.org/annotation/VSP_025444 http://togogenome.org/gene/10090:Or10ak12 ^@ http://purl.uniprot.org/uniprot/B2RVY8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ugt2b35 ^@ http://purl.uniprot.org/uniprot/Q8BJL9 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||UDP-glucuronosyltransferase ^@ http://purl.uniprot.org/annotation/PRO_5015020114 http://togogenome.org/gene/10090:Naa30 ^@ http://purl.uniprot.org/uniprot/Q8CES0 ^@ 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-acetyltransferase|||N-alpha-acetyltransferase 30|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000320033|||http://purl.uniprot.org/annotation/VSP_031582|||http://purl.uniprot.org/annotation/VSP_031583 http://togogenome.org/gene/10090:Baz1a ^@ http://purl.uniprot.org/uniprot/G3UWZ0 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Bromo|||DDT|||Disordered|||PHD-type|||Polar residues|||WAC ^@ http://togogenome.org/gene/10090:Actg1 ^@ http://purl.uniprot.org/uniprot/P63260 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Actin, cytoplasmic 2|||Actin, cytoplasmic 2, N-terminally processed|||Methionine (R)-sulfoxide|||N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed|||N-acetylmethionine|||N6-methyllysine|||Removed; alternate|||Tele-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000000833|||http://purl.uniprot.org/annotation/PRO_0000367101 http://togogenome.org/gene/10090:Tbc1d10a ^@ http://purl.uniprot.org/uniprot/P58802 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site ^@ Arginine finger|||Binding to the PDZ domain of EBP50|||Disordered|||Glutamine finger|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 10A ^@ http://purl.uniprot.org/annotation/PRO_0000208036 http://togogenome.org/gene/10090:Prl2c1 ^@ http://purl.uniprot.org/uniprot/Q5SVM0 ^@ Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5004261895 http://togogenome.org/gene/10090:Rhebl1 ^@ http://purl.uniprot.org/uniprot/Q9D8T3 ^@ 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 RhebL1|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000324294|||http://purl.uniprot.org/annotation/PRO_0000324295 http://togogenome.org/gene/10090:Krt15 ^@ http://purl.uniprot.org/uniprot/B1AQ77|||http://purl.uniprot.org/uniprot/Q61414 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||Keratin, type I cytoskeletal 15|||Linker 1|||Linker 12|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063658 http://togogenome.org/gene/10090:Raver2 ^@ http://purl.uniprot.org/uniprot/Q7TPD6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||RRM 1|||RRM 2|||RRM 3|||Ribonucleoprotein PTB-binding 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081491 http://togogenome.org/gene/10090:Scgb1b24 ^@ http://purl.uniprot.org/uniprot/B1B0N6 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015087048 http://togogenome.org/gene/10090:Or1i2 ^@ http://purl.uniprot.org/uniprot/Q7TQU7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp26 ^@ http://purl.uniprot.org/uniprot/G3XA08|||http://purl.uniprot.org/uniprot/P10076|||http://purl.uniprot.org/uniprot/Q8C4J2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||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 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; 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 26 ^@ http://purl.uniprot.org/annotation/PRO_0000047287 http://togogenome.org/gene/10090:Clca3a2 ^@ http://purl.uniprot.org/uniprot/Q9EQR4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ VWFA ^@ http://purl.uniprot.org/annotation/PRO_5015099727 http://togogenome.org/gene/10090:Fthl17a ^@ http://purl.uniprot.org/uniprot/Q9DAX0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ferritin-like diiron ^@ http://togogenome.org/gene/10090:Defb15 ^@ http://purl.uniprot.org/uniprot/Q8R2I5 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 15 ^@ http://purl.uniprot.org/annotation/PRO_0000006943 http://togogenome.org/gene/10090:Ranbp2 ^@ http://purl.uniprot.org/uniprot/Q9ERU9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ 1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||2 X 50 AA approximate repeats|||20|||20 X 2 AA repeats of F-G|||3|||4|||5|||6|||7|||8|||9|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||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|||Interaction with BICD2|||Interaction with SUMO1|||Interaction with UBE2I|||Interaction with sumoylated RANGAP1|||N6-acetyllysine|||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|||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_0000204914 http://togogenome.org/gene/10090:Cylc2 ^@ http://purl.uniprot.org/uniprot/A0A571BEE2|||http://purl.uniprot.org/uniprot/B1AWN8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Cylicin N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Nploc4 ^@ http://purl.uniprot.org/uniprot/P60670|||http://purl.uniprot.org/uniprot/Q3UDU9 ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ In isoform 2.|||MPN|||N-acetylalanine|||N6-acetyllysine|||Nuclear protein localization protein 4 homolog|||RanBP2-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057942|||http://purl.uniprot.org/annotation/VSP_009790 http://togogenome.org/gene/10090:Csnk1g2 ^@ http://purl.uniprot.org/uniprot/Q8BVP5|||http://purl.uniprot.org/uniprot/Q99K78 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ 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_0000192843 http://togogenome.org/gene/10090:Grpel1 ^@ http://purl.uniprot.org/uniprot/Q99LP6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||GrpE protein homolog 1, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000013050 http://togogenome.org/gene/10090:Vmn2r103 ^@ http://purl.uniprot.org/uniprot/E9PWW0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003242998 http://togogenome.org/gene/10090:Col4a1 ^@ http://purl.uniprot.org/uniprot/P02463 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ 3-hydroxyproline|||4-hydroxyproline|||Arresten|||Basic and acidic residues|||Collagen IV NC1|||Collagen alpha-1(IV) chain|||Disordered|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide (7S domain)|||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|||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_0000005750|||http://purl.uniprot.org/annotation/PRO_0000005751|||http://purl.uniprot.org/annotation/PRO_0000390483 http://togogenome.org/gene/10090:Slc4a5 ^@ http://purl.uniprot.org/uniprot/D3YVG0 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Band 3 cytoplasmic|||Bicarbonate transporter-like transmembrane|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Abi3bp ^@ http://purl.uniprot.org/uniprot/A0A338P6S8|||http://purl.uniprot.org/uniprot/A0A338P6W9|||http://purl.uniprot.org/uniprot/E9Q8E3|||http://purl.uniprot.org/uniprot/Q59IW5|||http://purl.uniprot.org/uniprot/Q59IW6|||http://purl.uniprot.org/uniprot/Q59IW7|||http://purl.uniprot.org/uniprot/Q59IW8|||http://purl.uniprot.org/uniprot/Q59IW9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Basic residues|||Disordered|||Fibronectin type-III|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5003244503|||http://purl.uniprot.org/annotation/PRO_5004252785|||http://purl.uniprot.org/annotation/PRO_5015097831|||http://purl.uniprot.org/annotation/PRO_5015097832|||http://purl.uniprot.org/annotation/PRO_5015097833|||http://purl.uniprot.org/annotation/PRO_5016254240|||http://purl.uniprot.org/annotation/PRO_5016313719|||http://purl.uniprot.org/annotation/PRO_5040057983 http://togogenome.org/gene/10090:Dio1 ^@ http://purl.uniprot.org/uniprot/Q61153 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Molecule Processing|||Non standard residue|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Chain|||Non standard residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Selenocysteine|||Type I iodothyronine deiodinase ^@ http://purl.uniprot.org/annotation/PRO_0000154312 http://togogenome.org/gene/10090:Slc28a3 ^@ http://purl.uniprot.org/uniprot/Q9ERH8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||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|||Polar residues|||Solute carrier family 28 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000324147 http://togogenome.org/gene/10090:Zfp740 ^@ http://purl.uniprot.org/uniprot/D3Z4S9|||http://purl.uniprot.org/uniprot/Q6NZQ6 ^@ 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; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Zinc finger protein 740 ^@ http://purl.uniprot.org/annotation/PRO_0000251402|||http://purl.uniprot.org/annotation/VSP_020756|||http://purl.uniprot.org/annotation/VSP_020757|||http://purl.uniprot.org/annotation/VSP_020758 http://togogenome.org/gene/10090:Htr1f ^@ http://purl.uniprot.org/uniprot/Q02284|||http://purl.uniprot.org/uniprot/Q543V2 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Topological Domain|||Transmembrane ^@ 5-hydroxytryptamine receptor 1F|||Cytoplasmic|||DRY motif; important for ligand-induced conformation changes|||Extracellular|||G-protein coupled receptors family 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_0000068938 http://togogenome.org/gene/10090:Synpo2l ^@ http://purl.uniprot.org/uniprot/B2RQK7|||http://purl.uniprot.org/uniprot/D3YU08|||http://purl.uniprot.org/uniprot/Q8BWB1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Synaptopodin 2-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000187676 http://togogenome.org/gene/10090:Bglap2 ^@ http://purl.uniprot.org/uniprot/P86547 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Gla|||Osteocalcin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000395312|||http://purl.uniprot.org/annotation/PRO_0000395313 http://togogenome.org/gene/10090:Taar8c ^@ http://purl.uniprot.org/uniprot/Q5QD05 ^@ 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|||Trace amine-associated receptor 8c ^@ http://purl.uniprot.org/annotation/PRO_0000070179 http://togogenome.org/gene/10090:Wdr45b ^@ http://purl.uniprot.org/uniprot/Q9CR39 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Motif|||Repeat|||Sequence Conflict ^@ L/FRRG motif|||WD 1|||WD 2|||WD repeat domain phosphoinositide-interacting protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000051446 http://togogenome.org/gene/10090:Pum3 ^@ http://purl.uniprot.org/uniprot/A0A0N4SUH4|||http://purl.uniprot.org/uniprot/Q8BKS9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||N6-acetyllysine|||Nuclear localization signal|||PUM-HD|||Polar residues|||Pumilio|||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_0000075930 http://togogenome.org/gene/10090:Ndufa6 ^@ http://purl.uniprot.org/uniprot/Q9CQZ5 ^@ Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Strand|||Turn ^@ NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 ^@ http://purl.uniprot.org/annotation/PRO_0000174303 http://togogenome.org/gene/10090:Ropn1 ^@ http://purl.uniprot.org/uniprot/Q9ESG2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Interaction with RHPN1|||Phosphoserine|||RIIa|||Ropporin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000307395 http://togogenome.org/gene/10090:Scgn ^@ http://purl.uniprot.org/uniprot/Q91WD9 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ 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_0000073637 http://togogenome.org/gene/10090:Fgfr1op2 ^@ http://purl.uniprot.org/uniprot/Q9CRA9 ^@ 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|||FGFR1 oncogene partner 2 homolog|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000299042|||http://purl.uniprot.org/annotation/VSP_027541 http://togogenome.org/gene/10090:Klf13 ^@ http://purl.uniprot.org/uniprot/Q9JJZ6 ^@ 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 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 13|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000047185 http://togogenome.org/gene/10090:Tph1 ^@ http://purl.uniprot.org/uniprot/P17532|||http://purl.uniprot.org/uniprot/Q3TZH2|||http://purl.uniprot.org/uniprot/Q3UK52|||http://purl.uniprot.org/uniprot/Q9JHZ8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue ^@ ACT|||Biopterin-dependent aromatic amino acid hydroxylase family profile|||Phosphoserine; by PKA|||Tryptophan 5-hydroxylase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000205569 http://togogenome.org/gene/10090:Rxfp2 ^@ http://purl.uniprot.org/uniprot/A0A0J9YV81|||http://purl.uniprot.org/uniprot/B7ZMU5|||http://purl.uniprot.org/uniprot/E9Q0U9|||http://purl.uniprot.org/uniprot/Q91ZZ5 ^@ 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|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||LDL-receptor class A|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-linked (GlcNAc...) asparagine|||Relaxin receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000069703|||http://purl.uniprot.org/annotation/PRO_5002866973|||http://purl.uniprot.org/annotation/PRO_5003245779|||http://purl.uniprot.org/annotation/PRO_5005326354 http://togogenome.org/gene/10090:Rnf115 ^@ http://purl.uniprot.org/uniprot/Q9D0C1 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNF115|||Loss of E3 ubiquitin protein ligase activity.|||Loss of interaction with EGFR and FLT3. No effect on E3 ubiquitin protein ligase activity; when associated with A-22.|||Loss of interaction with EGFR and FLT3. No effect on E3 ubiquitin protein ligase activity; when associated with A-25.|||N-acetylalanine|||RING-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056315 http://togogenome.org/gene/10090:Eno1b ^@ http://purl.uniprot.org/uniprot/P17182|||http://purl.uniprot.org/uniprot/Q5FW97 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Alpha-enolase|||Enolase C-terminal TIM barrel|||Enolase N-terminal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000134098 http://togogenome.org/gene/10090:Palm3 ^@ http://purl.uniprot.org/uniprot/A2TJV2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Propeptide|||Region ^@ 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_0000332173|||http://purl.uniprot.org/annotation/PRO_0000332174 http://togogenome.org/gene/10090:Ogg1 ^@ http://purl.uniprot.org/uniprot/O08760|||http://purl.uniprot.org/uniprot/Q3UIL3 ^@ 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|||Strand|||Turn ^@ HhH-GPD|||N-glycosylase/DNA lyase|||Schiff-base intermediate with DNA ^@ http://purl.uniprot.org/annotation/PRO_0000058592 http://togogenome.org/gene/10090:Cnep1r1 ^@ http://purl.uniprot.org/uniprot/Q3UJ81 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Modified Residue|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Nuclear envelope phosphatase-regulatory subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000286616|||http://purl.uniprot.org/annotation/VSP_025129|||http://purl.uniprot.org/annotation/VSP_025130|||http://purl.uniprot.org/annotation/VSP_025131 http://togogenome.org/gene/10090:Pdk1 ^@ http://purl.uniprot.org/uniprot/Q8BFP9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Histidine kinase|||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_0000023438 http://togogenome.org/gene/10090:Ccdc117 ^@ http://purl.uniprot.org/uniprot/Q6PB51 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Coiled-coil domain-containing protein 117|||Disordered|||Omega-N-methylarginine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000254139 http://togogenome.org/gene/10090:Tex55 ^@ http://purl.uniprot.org/uniprot/A6X8Z9 ^@ 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|||Testis-specific expressed protein 55 ^@ http://purl.uniprot.org/annotation/PRO_0000446513 http://togogenome.org/gene/10090:Or1e1 ^@ http://purl.uniprot.org/uniprot/Q7TRX9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ctcfl ^@ http://purl.uniprot.org/uniprot/A2APF3 ^@ 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 ^@ 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.|||Transcriptional repressor CTCFL ^@ http://purl.uniprot.org/annotation/PRO_0000373924|||http://purl.uniprot.org/annotation/VSP_037281 http://togogenome.org/gene/10090:Atad3a ^@ http://purl.uniprot.org/uniprot/Q925I1 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ ATPase family AAA domain-containing protein 3|||Disordered|||Helical|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Removed|||Required for interaction with the inner surface of the mitochondrial outer membrane|||S100B-binding ^@ http://purl.uniprot.org/annotation/PRO_0000084801|||http://purl.uniprot.org/annotation/VSP_015643 http://togogenome.org/gene/10090:Agpat1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J263|||http://purl.uniprot.org/uniprot/O35083 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Motif|||Sequence Conflict|||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_0000208191 http://togogenome.org/gene/10090:Pi4kb ^@ http://purl.uniprot.org/uniprot/Q8BKC8 ^@ 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 ^@ Activation loop|||Catalytic loop|||Disordered|||G-loop|||In isoform 2.|||In isoform 3.|||Interaction with ACBD3|||N-acetylglycine|||PI3K/PI4K catalytic|||PIK helical|||Phosphatidylinositol 4-kinase beta|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000088830|||http://purl.uniprot.org/annotation/VSP_037134|||http://purl.uniprot.org/annotation/VSP_037135 http://togogenome.org/gene/10090:H2al2a ^@ http://purl.uniprot.org/uniprot/Q9CQ70 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Histone H2A-Bbd type 1 ^@ http://purl.uniprot.org/annotation/PRO_0000419684 http://togogenome.org/gene/10090:Myod1 ^@ http://purl.uniprot.org/uniprot/P10085 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Myoblast determination protein 1|||N6-methyllysine; by EHMT2|||Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127361 http://togogenome.org/gene/10090:Or4a70 ^@ http://purl.uniprot.org/uniprot/Q8VGM6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sv2c ^@ http://purl.uniprot.org/uniprot/Q69ZS6 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with SYT1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Synaptic vesicle glycoprotein 2C ^@ http://purl.uniprot.org/annotation/PRO_0000239772 http://togogenome.org/gene/10090:Dxo ^@ http://purl.uniprot.org/uniprot/A0A0R4J288|||http://purl.uniprot.org/uniprot/O70348 ^@ 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 the decapping activity on both incomplete m7G cap and NAD-cap RNAs.|||Abolishes the decapping activity on both incomplete m7G cap and NAD-cap RNAs. Abolishes the 5'-3' exoribonuclease activity.|||Adenosine 3',5'-bisphosphate; inhibitor|||Basic and acidic residues|||Decapping and exoribonuclease protein|||Disordered|||Phosphoserine|||Phosphothreonine|||RAI1-like ^@ http://purl.uniprot.org/annotation/PRO_0000249823 http://togogenome.org/gene/10090:Or2h2c ^@ http://purl.uniprot.org/uniprot/L7N475 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ldhb ^@ http://purl.uniprot.org/uniprot/A0A6I8MX27|||http://purl.uniprot.org/uniprot/P16125 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ 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_0000168461 http://togogenome.org/gene/10090:B4galt1 ^@ http://purl.uniprot.org/uniprot/P15535|||http://purl.uniprot.org/uniprot/Q3U478 ^@ 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 ^@ Beta-1,4-galactosyltransferase 1|||Cytoplasmic|||Disordered|||Galactosyltransferase C-terminal|||Galactosyltransferase N-terminal|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform Short.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues|||Processed beta-1,4-galactosyltransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000012280|||http://purl.uniprot.org/annotation/PRO_0000296230|||http://purl.uniprot.org/annotation/VSP_018803 http://togogenome.org/gene/10090:Mpp2 ^@ http://purl.uniprot.org/uniprot/Q9WV34 ^@ 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 ^@ Guanylate kinase-like|||In isoform 2.|||L27 1|||L27 2|||MAGUK p55 subfamily member 2|||PDZ|||Phosphoserine|||Phosphothreonine|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000094574|||http://purl.uniprot.org/annotation/VSP_022952 http://togogenome.org/gene/10090:Tubgcp2 ^@ http://purl.uniprot.org/uniprot/Q3UIT6|||http://purl.uniprot.org/uniprot/Q921G8 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Gamma tubulin complex component C-terminal|||Gamma tubulin complex component protein N-terminal|||Gamma-tubulin complex component 2|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000078114 http://togogenome.org/gene/10090:Septin6 ^@ http://purl.uniprot.org/uniprot/Q9R1T4 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform I.|||In isoform V.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Septin-6|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173526|||http://purl.uniprot.org/annotation/VSP_006055|||http://purl.uniprot.org/annotation/VSP_006056 http://togogenome.org/gene/10090:Hgd ^@ http://purl.uniprot.org/uniprot/O09173 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Homogentisate 1,2-dioxygenase|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000220241 http://togogenome.org/gene/10090:Tex33 ^@ http://purl.uniprot.org/uniprot/E9QA37|||http://purl.uniprot.org/uniprot/Q3KNN2|||http://purl.uniprot.org/uniprot/Q9D9J2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Ciliary microtubule inner protein 4|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000086903 http://togogenome.org/gene/10090:Bahd1 ^@ http://purl.uniprot.org/uniprot/Z4YJL0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BAH|||Basic and acidic residues|||Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tnni3k ^@ http://purl.uniprot.org/uniprot/Q5GIG6 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 10|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Disordered|||In isoform 2.|||N-myristoyl glycine|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase TNNI3K ^@ http://purl.uniprot.org/annotation/PRO_0000086758|||http://purl.uniprot.org/annotation/VSP_051886|||http://purl.uniprot.org/annotation/VSP_051887 http://togogenome.org/gene/10090:Atrn ^@ http://purl.uniprot.org/uniprot/Q9WU60 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Attractin|||C-type lectin|||CUB|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000007484|||http://purl.uniprot.org/annotation/PRO_0000394772 http://togogenome.org/gene/10090:Gm5347 ^@ http://purl.uniprot.org/uniprot/Q7M765 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Disintegrin|||EGF-like|||Helical|||Peptidase M12B ^@ http://purl.uniprot.org/annotation/PRO_5010143563 http://togogenome.org/gene/10090:Wdr83os ^@ http://purl.uniprot.org/uniprot/Q6ZWX0 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylserine|||PAT complex subunit Asterix|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000071606 http://togogenome.org/gene/10090:Sox17 ^@ http://purl.uniprot.org/uniprot/A0A0A6YXS3|||http://purl.uniprot.org/uniprot/Q61473 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Motif|||Region|||Splice Variant|||Strand ^@ 9aaTAD|||Disordered|||HMG box|||In isoform 2.|||Polar residues|||Pro residues|||Sox C-terminal|||Transcription factor SOX-17 ^@ http://purl.uniprot.org/annotation/PRO_0000048766|||http://purl.uniprot.org/annotation/VSP_002204 http://togogenome.org/gene/10090:Yeats4 ^@ http://purl.uniprot.org/uniprot/Q9CR11 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Region|||Site ^@ Diacetylated histone H3 binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with MLLT10|||Interaction with TACC1|||Interacts with diacetylated histone H3|||YEATS|||YEATS domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000066205 http://togogenome.org/gene/10090:Qser1 ^@ http://purl.uniprot.org/uniprot/A0A338P6K9 ^@ 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|||Glutamine and serine-rich protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000453804|||http://purl.uniprot.org/annotation/VSP_061204 http://togogenome.org/gene/10090:Galk2 ^@ http://purl.uniprot.org/uniprot/Q3U3H5|||http://purl.uniprot.org/uniprot/Q68FH4|||http://purl.uniprot.org/uniprot/Q8BUU7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Site ^@ GHMP kinase C-terminal|||GHMP kinase N-terminal|||Galactokinase N-terminal|||N-acetylgalactosamine kinase|||Proton acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000184648 http://togogenome.org/gene/10090:Mastl ^@ http://purl.uniprot.org/uniprot/Q8C0P0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ AGC-kinase C-terminal|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase greatwall ^@ http://purl.uniprot.org/annotation/PRO_0000086316|||http://purl.uniprot.org/annotation/VSP_014576|||http://purl.uniprot.org/annotation/VSP_014577 http://togogenome.org/gene/10090:Cdc37 ^@ http://purl.uniprot.org/uniprot/Q61081 ^@ 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|||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_0000195058|||http://purl.uniprot.org/annotation/PRO_0000423198 http://togogenome.org/gene/10090:Gm904 ^@ http://purl.uniprot.org/uniprot/Q3V2L5 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Slc5a11 ^@ http://purl.uniprot.org/uniprot/Q8K0E3 ^@ 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.|||Sodium/myo-inositol cotransporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000331569|||http://purl.uniprot.org/annotation/VSP_052788 http://togogenome.org/gene/10090:Slc25a20 ^@ http://purl.uniprot.org/uniprot/Q9Z2Z6 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||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_0000090630 http://togogenome.org/gene/10090:Dhrs13 ^@ http://purl.uniprot.org/uniprot/Q5SS80 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Dehydrogenase/reductase SDR family member 13|||Disordered|||In isoform 2.|||Polar residues|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000311921|||http://purl.uniprot.org/annotation/VSP_029641 http://togogenome.org/gene/10090:Homer3 ^@ http://purl.uniprot.org/uniprot/Q99JP6 ^@ 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|||Homer protein homolog 3|||In isoform 2.|||Phosphoserine|||Polar residues|||Required for interaction with NFATC2|||WH1 ^@ http://purl.uniprot.org/annotation/PRO_0000191012|||http://purl.uniprot.org/annotation/VSP_009078 http://togogenome.org/gene/10090:Pomc ^@ http://purl.uniprot.org/uniprot/P01193 ^@ Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Beta-endorphin|||Corticotropin|||Corticotropin-like intermediary peptide|||Disordered|||Lipotropin beta|||Lipotropin gamma|||Melanocyte-stimulating hormone alpha|||Melanocyte-stimulating hormone beta|||Melanotropin gamma|||Met-enkephalin|||N-acetylserine; in Corticotropin|||N-linked (GlcNAc...) asparagine|||NPP|||Phenylalanine amide|||Phosphoserine|||Valine amide ^@ http://purl.uniprot.org/annotation/PRO_0000024996|||http://purl.uniprot.org/annotation/PRO_0000024997|||http://purl.uniprot.org/annotation/PRO_0000024998|||http://purl.uniprot.org/annotation/PRO_0000024999|||http://purl.uniprot.org/annotation/PRO_0000025000|||http://purl.uniprot.org/annotation/PRO_0000025001|||http://purl.uniprot.org/annotation/PRO_0000025002|||http://purl.uniprot.org/annotation/PRO_0000025003|||http://purl.uniprot.org/annotation/PRO_0000025004|||http://purl.uniprot.org/annotation/PRO_0000025005|||http://purl.uniprot.org/annotation/PRO_0000025006 http://togogenome.org/gene/10090:Samd1 ^@ http://purl.uniprot.org/uniprot/D3YXK1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Pro residues|||SAM|||SAMD1-like winged helix (WH)|||Sterile alpha motif domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000416118 http://togogenome.org/gene/10090:Or5k14 ^@ http://purl.uniprot.org/uniprot/E9Q7W1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Magee2 ^@ http://purl.uniprot.org/uniprot/Q52KG3|||http://purl.uniprot.org/uniprot/Q8CBC3 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Fam72a ^@ http://purl.uniprot.org/uniprot/Q8BFZ8 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Protein FAM72A ^@ http://purl.uniprot.org/annotation/PRO_0000340260 http://togogenome.org/gene/10090:Epha10 ^@ http://purl.uniprot.org/uniprot/Q8BYG9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Eph LBD|||Ephrin type-A receptor 10|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein kinase|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000280444|||http://purl.uniprot.org/annotation/VSP_023676|||http://purl.uniprot.org/annotation/VSP_023677 http://togogenome.org/gene/10090:Mmgt1 ^@ http://purl.uniprot.org/uniprot/Q8K273 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||ER membrane protein complex subunit 5|||Helical|||Lumenal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000286436 http://togogenome.org/gene/10090:Tmem200b ^@ http://purl.uniprot.org/uniprot/D3Z0P8 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Bub1 ^@ http://purl.uniprot.org/uniprot/A0A8I4YXJ8|||http://purl.uniprot.org/uniprot/A2APR8|||http://purl.uniprot.org/uniprot/O08901|||http://purl.uniprot.org/uniprot/Q8K1K8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ BUB1 N-terminal|||Disordered|||Essential for loading of BUBR1, MAD1L1 and MAD2L1 to kinetochores|||KEN box 1|||KEN box 2|||Mitotic checkpoint serine/threonine-protein kinase BUB1|||Necessary for interaction with BUB3|||Necessary for interaction with KNL1|||Necessary for kinetochore localization|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine; by CDK1|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085672 http://togogenome.org/gene/10090:Rc3h1 ^@ http://purl.uniprot.org/uniprot/Q4VGL6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn|||Zinc Finger ^@ Abolishes the formation of a preferential cleavage product. Abolishes protein cleavage; when associated with G-579.|||Abolishes the formation of an alternative cleavage product. Abolishes protein cleavage; when associated with G-510.|||C3H1-type|||Cleavage; by MALT1|||Decreases CDE and ADERNA-binding.|||Decreases CDERNA-binding.|||Decreases CDERNA-binding. Increases target-mRNA expression.|||Disordered|||Failed to reduce poly(A) tailed ICOS mRNA. Failed to regulate the production of inflammatory cytokines.|||HEPN-C|||HEPN-N|||In sanroque; partial loss of ICOS regulation, no effect on localization to stress granules, no effect on RNA-binding.|||No effect on CDERNA-binding.|||No effect on RNA-binding.|||No effect on cleavage.|||No effect on localization to stress granules, reduces RNA-binding.|||No effect on localization to stress granules.|||Phosphoserine|||Polar residues|||Pro residues|||RING-type; degenerate|||ROQ|||Roquin-1|||Slightly decreases CDE and ADERNA-binding.|||Strongly decreases CDE and ADERNA-binding.|||Strongly decreases CDE and ADERNA-binding. Increases target-mRNA expression. Abolishes CDERNA-binding and highly increases target-mRNA expression; when associated with A-239. Increases target-mRNA expression. Increases ICOS surface expression; when associated with A-220 and A-239.|||Strongly decreases CDE and ADERNA-binding. Increases target-mRNA expression. Abolishes CDERNA-binding and highly increases target-mRNA expression; when associated with A-260. Increases target-mRNA expression. Increases ICOS surface expression; when associated with A-220 and A-260.|||Strongly decreases CDE and ADERNA-binding. Increases target-mRNA expression. Increases ICOS surface expression; when associated with A-239 and A-260. ^@ http://purl.uniprot.org/annotation/PRO_0000055966 http://togogenome.org/gene/10090:Pcsk1n ^@ http://purl.uniprot.org/uniprot/Q9QXV0 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Motif|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Abolishes inhibition of PCSK1.|||Big LEN|||Big PEN-LEN|||Big SAAS|||C-terminal inhibitory domain; interacts with PCSK1|||Disordered|||KEP|||Little LEN|||Little SAAS|||PEN|||PEN-19|||PEN-20|||ProSAAS|||ProSAAS(1-180)|||Sufficient for inhibition of PCSK1 ^@ http://purl.uniprot.org/annotation/PRO_0000259681|||http://purl.uniprot.org/annotation/PRO_0000259682|||http://purl.uniprot.org/annotation/PRO_0000259683|||http://purl.uniprot.org/annotation/PRO_0000259684|||http://purl.uniprot.org/annotation/PRO_0000259685|||http://purl.uniprot.org/annotation/PRO_0000259686|||http://purl.uniprot.org/annotation/PRO_0000259687|||http://purl.uniprot.org/annotation/PRO_0000259688|||http://purl.uniprot.org/annotation/PRO_0000259689|||http://purl.uniprot.org/annotation/PRO_0000259690 http://togogenome.org/gene/10090:Dcbld1 ^@ http://purl.uniprot.org/uniprot/Q9D4J3 ^@ 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|||Helical|||In isoform 2.|||LCCL|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000021077|||http://purl.uniprot.org/annotation/VSP_010783 http://togogenome.org/gene/10090:Ankrd2 ^@ http://purl.uniprot.org/uniprot/Q9WV06 ^@ 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 2|||Disordered|||Phosphoserine|||Phosphoserine; by PKB/AKT2 ^@ http://purl.uniprot.org/annotation/PRO_0000066898 http://togogenome.org/gene/10090:Cd24a ^@ http://purl.uniprot.org/uniprot/P24807|||http://purl.uniprot.org/uniprot/Q3THW4|||http://purl.uniprot.org/uniprot/Q8CEU3 ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Lipid Binding|||Peptide|||Propeptide|||Region|||Signal Peptide|||Site ^@ Disordered|||GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) serine; partial|||O-linked (GalNAc...) threonine; partial|||Removed in mature form|||Signal transducer CD24 ^@ http://purl.uniprot.org/annotation/PRO_0000020895|||http://purl.uniprot.org/annotation/PRO_0000020896|||http://purl.uniprot.org/annotation/PRO_5004307397|||http://purl.uniprot.org/annotation/PRO_5014309135 http://togogenome.org/gene/10090:Vmn1r27 ^@ http://purl.uniprot.org/uniprot/K7N688 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Extl1 ^@ http://purl.uniprot.org/uniprot/Q3TSP4|||http://purl.uniprot.org/uniprot/Q9JKV7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Exostosin GT47|||Exostosin-like 1|||Glycosyl transferase 64|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149654 http://togogenome.org/gene/10090:Chrna3 ^@ http://purl.uniprot.org/uniprot/Q0VBK4|||http://purl.uniprot.org/uniprot/Q8R4G9 ^@ 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|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Associated with receptor activation|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-3|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000000347|||http://purl.uniprot.org/annotation/PRO_5015096999 http://togogenome.org/gene/10090:Galt ^@ http://purl.uniprot.org/uniprot/A2AMS3|||http://purl.uniprot.org/uniprot/Q03249|||http://purl.uniprot.org/uniprot/Q3TQJ2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Galactose-1-phosphate uridyl transferase C-terminal|||Galactose-1-phosphate uridyl transferase N-terminal|||Galactose-1-phosphate uridylyltransferase|||Tele-UMP-histidine intermediate|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000169883 http://togogenome.org/gene/10090:Chil5 ^@ http://purl.uniprot.org/uniprot/A0A0G2JDS2|||http://purl.uniprot.org/uniprot/A0JP54|||http://purl.uniprot.org/uniprot/Q08EE2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ GH18 ^@ http://purl.uniprot.org/annotation/PRO_5002546038 http://togogenome.org/gene/10090:Pik3cd ^@ http://purl.uniprot.org/uniprot/O35904|||http://purl.uniprot.org/uniprot/Q3T9Y0|||http://purl.uniprot.org/uniprot/Q3TBW3|||http://purl.uniprot.org/uniprot/Q3UDT3|||http://purl.uniprot.org/uniprot/Q8BS14|||http://purl.uniprot.org/uniprot/Q8CI98 ^@ 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 ^@ Activation loop|||C2 PI3K-type|||Catalytic loop|||Disordered|||G-loop|||In isoform 2.|||Inhibits lipid kinase activity. Mice are viable and fertile but display defective adaptive and innate immune responses Signaling defects in B-cells, T-cells, mast cells and natural killer cells. Reduced B and T-cell receptor signaling. Affects development and differentiation of B -ells. Reduced memory T-cell number. Affects B- and T-cell proliferation. Attenuates immune responses in vivo. Induces inflammatory bowel disease development. Lost TCR-induced migration and localization to antigenic tissue. Affects natural killer cell maturation and cytokine production.|||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_0000088791|||http://purl.uniprot.org/annotation/VSP_044411|||http://purl.uniprot.org/annotation/VSP_044412 http://togogenome.org/gene/10090:Lsm14a ^@ http://purl.uniprot.org/uniprot/Q8K2F8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||DFDF|||Disordered|||FFD box|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein LSM14 homolog A|||Removed|||Sm|||TFG box ^@ http://purl.uniprot.org/annotation/PRO_0000187091 http://togogenome.org/gene/10090:Rb1cc1 ^@ http://purl.uniprot.org/uniprot/Q9ESK9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||FFAT|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||RB1-inducible coiled-coil protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000097184 http://togogenome.org/gene/10090:Usp32 ^@ http://purl.uniprot.org/uniprot/F8VPZ3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region ^@ Cysteine methyl ester|||DUSP|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||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_0000458839|||http://purl.uniprot.org/annotation/PRO_0000458840 http://togogenome.org/gene/10090:Chtf8 ^@ http://purl.uniprot.org/uniprot/P0CG14|||http://purl.uniprot.org/uniprot/P0CG15 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Chromosome transmission fidelity protein 8 homolog|||Decreased expression in renal and prostate cancer protein|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000326397|||http://purl.uniprot.org/annotation/PRO_0000327254 http://togogenome.org/gene/10090:Or4c118 ^@ http://purl.uniprot.org/uniprot/A0A1L1SU13 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:2410004B18Rik ^@ http://purl.uniprot.org/uniprot/Q9CWU4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||UPF0690 protein C1orf52 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000254631 http://togogenome.org/gene/10090:Skor2 ^@ http://purl.uniprot.org/uniprot/A7M7C7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||Pro residues|||SKI family transcriptional corepressor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000334612 http://togogenome.org/gene/10090:Klf3 ^@ http://purl.uniprot.org/uniprot/Q545J5|||http://purl.uniprot.org/uniprot/Q60980 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn|||Zinc Finger ^@ 9aaTAD; inactive|||C2H2-type|||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 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|||Krueppel-like factor 3|||Little change in DNA-binding ability.|||Phosphoserine|||Reduced sumoylation levels. No effect on DNA-binding and slight reduction of transcriptional repression. Abolishes sumoylation. No effect on DNA-binding but great reduction in transcriptional repression; when associated with A-197.|||Reduced sumoylation levels. No effect on DNA-binding and slight reduction of transcriptional repression. Abolishes sumoylation. No effect on DNA-binding but great reduction of transcriptional repression; when associated with A-10.|||Repressor domain|||Slight reduction of transcriptional repression. Great reduction of transcriptional repression; when associated with A-199. ^@ http://purl.uniprot.org/annotation/PRO_0000047166 http://togogenome.org/gene/10090:Dnajc18 ^@ http://purl.uniprot.org/uniprot/Q9CZJ9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ DnaJ homolog subfamily C member 18|||Helical|||J ^@ http://purl.uniprot.org/annotation/PRO_0000244087 http://togogenome.org/gene/10090:Serpina3c ^@ http://purl.uniprot.org/uniprot/P29621 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide|||Site ^@ N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond|||Serine protease inhibitor A3C ^@ http://purl.uniprot.org/annotation/PRO_0000032416 http://togogenome.org/gene/10090:Zfp652 ^@ http://purl.uniprot.org/uniprot/Q5DU09 ^@ 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 ^@ Acidic residues|||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; degenerate|||Disordered|||In isoform 2.|||Mediates interaction with CBFA2T3|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 652 ^@ http://purl.uniprot.org/annotation/PRO_0000280429|||http://purl.uniprot.org/annotation/VSP_023669|||http://purl.uniprot.org/annotation/VSP_023670 http://togogenome.org/gene/10090:Gpa33 ^@ http://purl.uniprot.org/uniprot/A0A0R4J209|||http://purl.uniprot.org/uniprot/Q9JKA5 ^@ 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 ^@ Basic and acidic residues|||Cell surface A33 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014771|||http://purl.uniprot.org/annotation/PRO_5015044304 http://togogenome.org/gene/10090:Zfp119b ^@ http://purl.uniprot.org/uniprot/A0A087WPI5|||http://purl.uniprot.org/uniprot/Q8K0G9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Anp32a ^@ http://purl.uniprot.org/uniprot/O35381 ^@ 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 ^@ Acidic leucine-rich nuclear phosphoprotein 32 family member A|||Acidic residues|||Disordered|||Interaction with E4F1|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Necessary for tumor-suppressive function|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000137593 http://togogenome.org/gene/10090:Muc13 ^@ http://purl.uniprot.org/uniprot/P19467|||http://purl.uniprot.org/uniprot/Q3V1S6 ^@ 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|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Extracellular|||Helical|||Mucin-13|||N-linked (GlcNAc...) asparagine|||Polar residues|||SEA ^@ http://purl.uniprot.org/annotation/PRO_0000019285|||http://purl.uniprot.org/annotation/PRO_5014309240 http://togogenome.org/gene/10090:Gsg1l ^@ http://purl.uniprot.org/uniprot/D3Z7H4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Germ cell-specific gene 1-like protein|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000420684 http://togogenome.org/gene/10090:Dnah11 ^@ http://purl.uniprot.org/uniprot/E9Q7N9 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ AAA+ ATPase|||Disordered ^@ http://togogenome.org/gene/10090:Spata1 ^@ http://purl.uniprot.org/uniprot/Q9D5R4 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Splice Variant ^@ In isoform 2.|||Spermatogenesis-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000349216|||http://purl.uniprot.org/annotation/VSP_035225|||http://purl.uniprot.org/annotation/VSP_035226 http://togogenome.org/gene/10090:Il34 ^@ http://purl.uniprot.org/uniprot/Q8R1R4 ^@ 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 ^@ In isoform 2.|||In isoform 3.|||Interleukin-34|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000294349|||http://purl.uniprot.org/annotation/VSP_026632|||http://purl.uniprot.org/annotation/VSP_035080 http://togogenome.org/gene/10090:Galnt5 ^@ http://purl.uniprot.org/uniprot/Q14B51|||http://purl.uniprot.org/uniprot/Q8C102 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Polypeptide N-acetylgalactosaminyltransferase 5|||Ricin B lectin|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059111 http://togogenome.org/gene/10090:Iqcd ^@ http://purl.uniprot.org/uniprot/B2RPX1|||http://purl.uniprot.org/uniprot/Q9D3V1 ^@ 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|||Dynein regulatory complex protein 10|||IQ|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000282550|||http://purl.uniprot.org/annotation/VSP_024181 http://togogenome.org/gene/10090:Rab2b ^@ http://purl.uniprot.org/uniprot/P59279|||http://purl.uniprot.org/uniprot/Q0PD64 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Motif|||Mutagenesis Site|||Region ^@ Constitutively active. Interacts with GARIN1B.|||Constitutively inactive. Loss of Golgi apparatus location. Loss of interaction with GARIN1B.|||Disordered|||Effector region|||Polar residues|||Ras-related protein Rab-2B|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121072 http://togogenome.org/gene/10090:Or8g24 ^@ http://purl.uniprot.org/uniprot/Q9EQ93 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gm5157 ^@ http://purl.uniprot.org/uniprot/A0A087WRH8 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Fam204a ^@ http://purl.uniprot.org/uniprot/Q8C6C7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||Protein FAM204A ^@ http://purl.uniprot.org/annotation/PRO_0000089809 http://togogenome.org/gene/10090:Ccdc142 ^@ http://purl.uniprot.org/uniprot/Q8CAI1 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Splice Variant ^@ Coiled-coil domain-containing protein 142|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000311261|||http://purl.uniprot.org/annotation/VSP_029500|||http://purl.uniprot.org/annotation/VSP_029501 http://togogenome.org/gene/10090:Rela ^@ http://purl.uniprot.org/uniprot/Q04207|||http://purl.uniprot.org/uniprot/Q548Y4 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ 9aaTAD|||Abolishes DNA-binding and transcriptional activity.|||Abolishes monomethylation by SETD6 and interaction with EHMT1.|||Abolishes sulfhydration and impairs interaction with RPS3.|||Cysteine persulfide; alternate|||Disordered|||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 p65 delta.|||Loss of interaction with ZBTB7A.|||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|||Polar residues|||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_0000205170|||http://purl.uniprot.org/annotation/VSP_005589 http://togogenome.org/gene/10090:Ndufb9 ^@ http://purl.uniprot.org/uniprot/Q9CQJ8 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn ^@ N-acetylalanine|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000174307 http://togogenome.org/gene/10090:Arhgef37 ^@ http://purl.uniprot.org/uniprot/A1IGU4|||http://purl.uniprot.org/uniprot/E9Q5R6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ BAR|||Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||Rho guanine nucleotide exchange factor 37|||SH3|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000337051|||http://purl.uniprot.org/annotation/VSP_033856 http://togogenome.org/gene/10090:Acpp ^@ http://purl.uniprot.org/uniprot/Q8CE08 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Important for substrate specificity|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Prostatic acid phosphatase|||Proton donor|||Required for dimerization|||Required for structural stability ^@ http://purl.uniprot.org/annotation/PRO_0000356293|||http://purl.uniprot.org/annotation/VSP_036024 http://togogenome.org/gene/10090:Vmn1r89 ^@ http://purl.uniprot.org/uniprot/Q8R256 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or52a5 ^@ http://purl.uniprot.org/uniprot/E9PYY2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc6a3 ^@ http://purl.uniprot.org/uniprot/Q61327 ^@ 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|||Region|||Site|||Topological Domain|||Transmembrane ^@ Contributes to high-affinity binding to cocaine|||Cytoplasmic|||Extracellular|||Functional dopamine transporter with 4-fold decrease in cocaine sensitivity.|||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|||Interaction with TGFB1I1|||Interchain|||N-linked (GlcNAc...) asparagine|||Reduced sensitivity to cocaine.|||Retention of dopamine transporter activity and high sensitivity to cocaine.|||Sodium-dependent dopamine transporter|||Very low dopamine transporter activity. ^@ http://purl.uniprot.org/annotation/PRO_0000214753 http://togogenome.org/gene/10090:Ubn1 ^@ http://purl.uniprot.org/uniprot/Q4G0F8 ^@ 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.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ubinuclein-1 ^@ http://purl.uniprot.org/annotation/PRO_0000370691|||http://purl.uniprot.org/annotation/VSP_036972|||http://purl.uniprot.org/annotation/VSP_036973 http://togogenome.org/gene/10090:Cers6 ^@ http://purl.uniprot.org/uniprot/H3BL08|||http://purl.uniprot.org/uniprot/Q8C172 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Site|||Topological Domain|||Transmembrane ^@ Ceramide synthase 6|||Cytoplasmic|||Disordered|||Helical|||Homeobox|||Homeobox-like|||Lumenal|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||Polar residues|||TLC ^@ http://purl.uniprot.org/annotation/PRO_0000185517 http://togogenome.org/gene/10090:Arf4 ^@ http://purl.uniprot.org/uniprot/P61750 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict ^@ ADP-ribosylation factor 4|||N-myristoyl glycine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207392 http://togogenome.org/gene/10090:Semg1 ^@ http://purl.uniprot.org/uniprot/Q8BS30|||http://purl.uniprot.org/uniprot/Q8CBV5 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Disordered|||Polar residues|||Seminal vesicle secretory protein 2 ^@ http://purl.uniprot.org/annotation/PRO_5004307384|||http://purl.uniprot.org/annotation/PRO_5015099030 http://togogenome.org/gene/10090:Cxcr6 ^@ http://purl.uniprot.org/uniprot/Q9EQ16 ^@ 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 ^@ C-X-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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000303230 http://togogenome.org/gene/10090:Gm6676 ^@ http://purl.uniprot.org/uniprot/K7N6G4 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:Tbca ^@ http://purl.uniprot.org/uniprot/P48428|||http://purl.uniprot.org/uniprot/Q5I0U7 ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||Removed|||Tubulin-specific chaperone A ^@ http://purl.uniprot.org/annotation/PRO_0000080040 http://togogenome.org/gene/10090:Mlc1 ^@ http://purl.uniprot.org/uniprot/Q8VHK5 ^@ 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|||Membrane protein MLC1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000096498 http://togogenome.org/gene/10090:Dmac2 ^@ http://purl.uniprot.org/uniprot/Q9D7K5 ^@ Chain|||Molecule Processing ^@ Chain ^@ Distal membrane-arm assembly complex protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000318697 http://togogenome.org/gene/10090:Osbpl9 ^@ http://purl.uniprot.org/uniprot/A0A0A6YXH3|||http://purl.uniprot.org/uniprot/A2A8Z1|||http://purl.uniprot.org/uniprot/E9PXZ2|||http://purl.uniprot.org/uniprot/Q5FWX7|||http://purl.uniprot.org/uniprot/Q8R0G3 ^@ 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|||Disordered|||In isoform 2.|||N-acetylalanine|||Oxysterol-binding protein-related protein 9|||PH|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000366289|||http://purl.uniprot.org/annotation/VSP_036572|||http://purl.uniprot.org/annotation/VSP_036573 http://togogenome.org/gene/10090:Klhdc8a ^@ http://purl.uniprot.org/uniprot/Q91XA8 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ 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_0000229002 http://togogenome.org/gene/10090:Krtap19-9b ^@ http://purl.uniprot.org/uniprot/Q99NG9 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ 12 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 19-9b ^@ http://purl.uniprot.org/annotation/PRO_0000356211 http://togogenome.org/gene/10090:Ap5m1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0K9|||http://purl.uniprot.org/uniprot/Q8BJ63 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ AP-5 complex subunit mu-1|||In isoform 2.|||In isoform 3.|||MHD ^@ http://purl.uniprot.org/annotation/PRO_0000193796|||http://purl.uniprot.org/annotation/VSP_008409|||http://purl.uniprot.org/annotation/VSP_008410|||http://purl.uniprot.org/annotation/VSP_008411|||http://purl.uniprot.org/annotation/VSP_008412 http://togogenome.org/gene/10090:Stau1 ^@ http://purl.uniprot.org/uniprot/A2A5R8|||http://purl.uniprot.org/uniprot/A2A5S3|||http://purl.uniprot.org/uniprot/Q3TU43|||http://purl.uniprot.org/uniprot/Q3TWA1|||http://purl.uniprot.org/uniprot/Q3U7A6|||http://purl.uniprot.org/uniprot/Q3UKX3|||http://purl.uniprot.org/uniprot/Q3UTC8|||http://purl.uniprot.org/uniprot/Q9DBE7|||http://purl.uniprot.org/uniprot/Q9Z108 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Signal Peptide ^@ Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||DRBM|||DRBM 1|||DRBM 2|||DRBM domain-containing protein|||Disordered|||Double-stranded RNA-binding protein Staufen homolog 1|||Omega-N-methylarginine; alternate|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000072244|||http://purl.uniprot.org/annotation/PRO_5004229645 http://togogenome.org/gene/10090:Gabrr1 ^@ http://purl.uniprot.org/uniprot/P56475 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Gamma-aminobutyric acid receptor subunit rho-1|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000000486 http://togogenome.org/gene/10090:Lrpprc ^@ http://purl.uniprot.org/uniprot/Q6PB66 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ Leucine-rich PPR motif-containing protein, mitochondrial|||Mitochondrion|||N6-acetyllysine|||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|||Phosphoserine|||RNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000295546 http://togogenome.org/gene/10090:Ifnar2 ^@ http://purl.uniprot.org/uniprot/O35664|||http://purl.uniprot.org/uniprot/Q923Z6|||http://purl.uniprot.org/uniprot/Q9D1R7 ^@ 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 ^@ Cytoplasmic|||Disordered|||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|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000011007|||http://purl.uniprot.org/annotation/PRO_5014312470|||http://purl.uniprot.org/annotation/PRO_5014312705|||http://purl.uniprot.org/annotation/VSP_050345|||http://purl.uniprot.org/annotation/VSP_050346|||http://purl.uniprot.org/annotation/VSP_050347|||http://purl.uniprot.org/annotation/VSP_050348 http://togogenome.org/gene/10090:Ets1 ^@ http://purl.uniprot.org/uniprot/E9PWI8|||http://purl.uniprot.org/uniprot/P27577|||http://purl.uniprot.org/uniprot/Q540Q5|||http://purl.uniprot.org/uniprot/Q8BVW8|||http://purl.uniprot.org/uniprot/Q8K3Q9 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Activation domain; required for transcription activation|||Decreased phosphorylation, leading to decreased autoinhibition. Strongly decreased phosphorylation, leading to stongly decreased autoinhibition; when associated with 282-A--A-285.|||Decreased phosphorylation, leading to decreased autoinhibition. Strongly decreased phosphorylation, leading to stongly decreased autoinhibition; when associated with A-251.|||Does not affect phosphorylation and autoinhibition.|||ETS|||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|||Helix H4|||Helix H5|||Helix HI-1|||Helix HI-2|||N6-acetyllysine|||N6-acetyllysine; alternate|||PNT|||Phosphoserine|||Phosphoserine; by CaMK2|||Phosphothreonine|||Phosphothreonine; by MAPK|||Phosphotyrosine|||Protein C-ets-1|||Reduced autoinhibition. ^@ http://purl.uniprot.org/annotation/PRO_0000204070 http://togogenome.org/gene/10090:Pls3 ^@ http://purl.uniprot.org/uniprot/B1AX58|||http://purl.uniprot.org/uniprot/Q3UJG9|||http://purl.uniprot.org/uniprot/Q3UKB1|||http://purl.uniprot.org/uniprot/Q99K51 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||Phosphoserine|||Phosphothreonine|||Plastin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000073748 http://togogenome.org/gene/10090:Msh6 ^@ http://purl.uniprot.org/uniprot/P54276 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||DNA mismatch repair protein Msh6|||Disordered|||N6-acetyllysine|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000115208 http://togogenome.org/gene/10090:Or5d18 ^@ http://purl.uniprot.org/uniprot/Q920P2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Plekhj1 ^@ http://purl.uniprot.org/uniprot/Q9D240 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ PH|||Pleckstrin homology domain-containing family J member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000309231 http://togogenome.org/gene/10090:Or52n2 ^@ http://purl.uniprot.org/uniprot/Q8VH00 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or10al4 ^@ http://purl.uniprot.org/uniprot/Q8VFQ2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tctn1 ^@ http://purl.uniprot.org/uniprot/Q8BZ64 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Polar residues|||Tectonic-1 ^@ http://purl.uniprot.org/annotation/PRO_0000229797|||http://purl.uniprot.org/annotation/VSP_017764|||http://purl.uniprot.org/annotation/VSP_017765 http://togogenome.org/gene/10090:Rapgefl1 ^@ http://purl.uniprot.org/uniprot/Q68EF8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||Rap guanine nucleotide exchange factor-like 1|||Ras-GEF ^@ http://purl.uniprot.org/annotation/PRO_0000349203 http://togogenome.org/gene/10090:Pold4 ^@ http://purl.uniprot.org/uniprot/Q547B4|||http://purl.uniprot.org/uniprot/Q9CWP8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Motif|||Region ^@ Basic and acidic residues|||DNA polymerase delta subunit 4|||Disordered|||PCNA-interaction protein motif (PIP box) ^@ http://purl.uniprot.org/annotation/PRO_0000186052 http://togogenome.org/gene/10090:Znrf4 ^@ http://purl.uniprot.org/uniprot/Q9DAH2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||Disordered|||E3 ubiquitin-protein ligase ZNRF4|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_5004325102 http://togogenome.org/gene/10090:Wfikkn2 ^@ http://purl.uniprot.org/uniprot/Q7TQN3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Site|||Strand ^@ BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||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_0000307821 http://togogenome.org/gene/10090:Bccip ^@ http://purl.uniprot.org/uniprot/Q9CWI3 ^@ 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|||BRCA2 and CDKN1A-interacting protein|||Disordered|||Interaction with BRCA2|||Interaction with CDKN1A|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000249688 http://togogenome.org/gene/10090:Zfp62 ^@ http://purl.uniprot.org/uniprot/Q8C827 ^@ 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 ^@ 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 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|||Polar residues|||Zinc finger protein 62 ^@ http://purl.uniprot.org/annotation/PRO_0000047306|||http://purl.uniprot.org/annotation/VSP_010137|||http://purl.uniprot.org/annotation/VSP_010138 http://togogenome.org/gene/10090:Lrrc71 ^@ http://purl.uniprot.org/uniprot/Q9D3W5 ^@ 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|||Leucine-rich repeat-containing protein 71|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284543 http://togogenome.org/gene/10090:Nap1l1 ^@ http://purl.uniprot.org/uniprot/P28656 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict ^@ 5-glutamyl polyglycine|||Acidic residues|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||N-acetylalanine|||N6-acetyllysine|||NAP1L motif|||Nuclear localization signal|||Nucleosome assembly protein 1-like 1|||Phosphoserine|||Phosphothreonine|||Reduced polyglycylation.|||Removed|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000185653|||http://purl.uniprot.org/annotation/PRO_0000396686 http://togogenome.org/gene/10090:Clk1 ^@ http://purl.uniprot.org/uniprot/P22518 ^@ 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|||Basic residues|||Disordered|||Dual specificity protein kinase CLK1|||In isoform Short.|||Loss of kinase activity and changed localization in the nucleus.|||Nuclear localization signal|||Phosphoserine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085867|||http://purl.uniprot.org/annotation/VSP_004854|||http://purl.uniprot.org/annotation/VSP_004855 http://togogenome.org/gene/10090:Spink12 ^@ http://purl.uniprot.org/uniprot/A0A0R4J109|||http://purl.uniprot.org/uniprot/Q9D256 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Site ^@ Kazal-like|||Reactive bond|||Serine protease inhibitor Kazal-type 12 ^@ http://purl.uniprot.org/annotation/PRO_0000302143 http://togogenome.org/gene/10090:Fbxl22 ^@ http://purl.uniprot.org/uniprot/Q8C7B6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ F-box|||F-box and leucine-rich protein 22|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6 ^@ http://purl.uniprot.org/annotation/PRO_0000247150 http://togogenome.org/gene/10090:Elovl7 ^@ http://purl.uniprot.org/uniprot/Q9D2Y9 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Di-lysine motif|||Elongation of very long chain fatty acids protein 7|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||HxxHH motif|||Lumenal|||N-acetylalanine|||Nucleophile|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000311989 http://togogenome.org/gene/10090:Ugt2b36 ^@ http://purl.uniprot.org/uniprot/Q3UEP4 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||UDP-glucuronosyltransferase ^@ http://purl.uniprot.org/annotation/PRO_5015020013 http://togogenome.org/gene/10090:Sdccag8 ^@ http://purl.uniprot.org/uniprot/Q80UF4 ^@ 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|||Phosphoserine|||Serologically defined colon cancer antigen 8 homolog|||Sufficient for homodimerization ^@ http://purl.uniprot.org/annotation/PRO_0000076311 http://togogenome.org/gene/10090:Or51m1 ^@ http://purl.uniprot.org/uniprot/F8VPJ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fam3d ^@ http://purl.uniprot.org/uniprot/P97805 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ GG-type lectin|||N-linked (GlcNAc...) asparagine|||Protein FAM3D ^@ http://purl.uniprot.org/annotation/PRO_0000008755 http://togogenome.org/gene/10090:Tnip3 ^@ http://purl.uniprot.org/uniprot/Q3SXA6 ^@ Coiled-Coil|||Region ^@ Coiled-Coil|||Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Retnlb ^@ http://purl.uniprot.org/uniprot/A0A0R4J042|||http://purl.uniprot.org/uniprot/Q99P86 ^@ Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Fails to homodimerize.|||Interchain|||Resistin-like beta ^@ http://purl.uniprot.org/annotation/PRO_0000030346|||http://purl.uniprot.org/annotation/PRO_5015044279 http://togogenome.org/gene/10090:Zbtb33 ^@ http://purl.uniprot.org/uniprot/A2A3Z3|||http://purl.uniprot.org/uniprot/Q8BN78 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Abrogates nuclear localization.|||BTB|||C2H2-type|||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|||Polar residues|||Required for DNA-binding|||Self-association|||Transcriptional regulator Kaiso ^@ http://purl.uniprot.org/annotation/PRO_0000046989 http://togogenome.org/gene/10090:Cyth1 ^@ http://purl.uniprot.org/uniprot/Q3TZ02|||http://purl.uniprot.org/uniprot/Q570Y7|||http://purl.uniprot.org/uniprot/Q8K3E8|||http://purl.uniprot.org/uniprot/Q9QX11 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ C-terminal autoinhibitory region|||Cytohesin-1|||Disordered|||Impairs autoinhibition; when associated with A-385. Impairs translocation to the cell membrane.|||Impairs autoinhibition; when associated with A-389. Impairs translocation to the cell membrane.|||Impairs epithelium polarity.|||In isoform 2.|||Increases guanine exchange factor activity.|||N-acetylmethionine|||Necessary for localization at adherens junction|||PH|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000120195|||http://purl.uniprot.org/annotation/VSP_006035 http://togogenome.org/gene/10090:F2rl1 ^@ http://purl.uniprot.org/uniprot/P55086|||http://purl.uniprot.org/uniprot/Q3TU81 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cleavage; by trypsin|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||G-protein coupled receptors family 1 profile domain-containing protein|||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|||Proteinase-activated receptor 2|||Removed for receptor activation|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000012752|||http://purl.uniprot.org/annotation/PRO_0000012753|||http://purl.uniprot.org/annotation/PRO_5010843305 http://togogenome.org/gene/10090:Kdm3a ^@ http://purl.uniprot.org/uniprot/Q6PCM1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C6-type|||Disordered|||In isoform 2.|||JmjC|||LXXLL motif|||Lysine-specific demethylase 3A|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084286|||http://purl.uniprot.org/annotation/VSP_018296|||http://purl.uniprot.org/annotation/VSP_018297 http://togogenome.org/gene/10090:Ang ^@ http://purl.uniprot.org/uniprot/P21570|||http://purl.uniprot.org/uniprot/Q3TBG7 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Signal Peptide|||Strand|||Turn ^@ Angiogenin|||Nucleolar localization signal|||Proton acceptor|||Proton donor|||Pyrrolidone carboxylic acid|||Ribonuclease A-domain|||Ribonuclease A-domain domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000030857|||http://purl.uniprot.org/annotation/PRO_5014205820 http://togogenome.org/gene/10090:Bhlhe22 ^@ http://purl.uniprot.org/uniprot/A0A0R4J056|||http://purl.uniprot.org/uniprot/Q8C6A8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ BHLH|||Class E basic helix-loop-helix protein 22|||Disordered|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000274286 http://togogenome.org/gene/10090:Lsr ^@ http://purl.uniprot.org/uniprot/Q99KG5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Decreased phosphorylation levels.|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||Lipolysis-stimulated lipoprotein receptor|||Phosphoserine|||Phosphoserine; by MAPK8 and MAPK9|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000245309|||http://purl.uniprot.org/annotation/VSP_019695|||http://purl.uniprot.org/annotation/VSP_019696 http://togogenome.org/gene/10090:Vmn1r143 ^@ http://purl.uniprot.org/uniprot/E9PUW9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Srrt ^@ http://purl.uniprot.org/uniprot/Q99MR6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||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 B and isoform C.|||In isoform C and isoform D.|||N-acetylglycine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Serrate RNA effector molecule homolog ^@ http://purl.uniprot.org/annotation/PRO_0000220966|||http://purl.uniprot.org/annotation/VSP_000325|||http://purl.uniprot.org/annotation/VSP_000326 http://togogenome.org/gene/10090:Tmbim4 ^@ http://purl.uniprot.org/uniprot/Q9DA39 ^@ Chain|||INTRAMEM|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Protein lifeguard 4 ^@ http://purl.uniprot.org/annotation/PRO_0000179093 http://togogenome.org/gene/10090:Sh2d7 ^@ http://purl.uniprot.org/uniprot/Q8BI17 ^@ 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.|||Polar residues|||SH2|||SH2 domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000341255|||http://purl.uniprot.org/annotation/VSP_034233 http://togogenome.org/gene/10090:Map7d1 ^@ http://purl.uniprot.org/uniprot/A2AJI0|||http://purl.uniprot.org/uniprot/A2AJI1|||http://purl.uniprot.org/uniprot/A8Y5P4 ^@ 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.|||MAP7 domain-containing protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000306808|||http://purl.uniprot.org/annotation/VSP_028489 http://togogenome.org/gene/10090:Zfp786 ^@ http://purl.uniprot.org/uniprot/B2RSK4|||http://purl.uniprot.org/uniprot/Q8BV42 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||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; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 786 ^@ http://purl.uniprot.org/annotation/PRO_0000293695 http://togogenome.org/gene/10090:Or7e169 ^@ http://purl.uniprot.org/uniprot/Q8VFF7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Amigo3 ^@ http://purl.uniprot.org/uniprot/Q8C2S7 ^@ 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 ^@ Amphoterin-induced protein 3|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014514 http://togogenome.org/gene/10090:Tmem210 ^@ http://purl.uniprot.org/uniprot/Q9D2F0 ^@ 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|||Pro residues|||Transmembrane protein 210 ^@ http://purl.uniprot.org/annotation/PRO_0000329081 http://togogenome.org/gene/10090:Brd1 ^@ http://purl.uniprot.org/uniprot/A7MCW6|||http://purl.uniprot.org/uniprot/G5E8P1|||http://purl.uniprot.org/uniprot/Q3UE68 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Bromo|||Bromodomain-containing protein 1|||C2HC pre-PHD-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with KAT7/HBO1 and histones|||N6-acetyllysine|||PHD-type|||PHD-type 1|||PHD-type 2|||PWWP|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000449610|||http://purl.uniprot.org/annotation/VSP_060568 http://togogenome.org/gene/10090:Gpr137c ^@ http://purl.uniprot.org/uniprot/A0A2I3BPD5|||http://purl.uniprot.org/uniprot/E9Q343 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||G protein-coupled receptor 137C|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000448977 http://togogenome.org/gene/10090:Rhox3f ^@ http://purl.uniprot.org/uniprot/A2ANE1|||http://purl.uniprot.org/uniprot/A6H657 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Gstcd ^@ http://purl.uniprot.org/uniprot/Q5RL51 ^@ 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|||GST C-terminal|||Glutathione S-transferase C-terminal domain-containing protein|||In isoform 2.|||In isoform 3.|||In isoform 4. ^@ http://purl.uniprot.org/annotation/PRO_0000316954|||http://purl.uniprot.org/annotation/VSP_030823|||http://purl.uniprot.org/annotation/VSP_030824|||http://purl.uniprot.org/annotation/VSP_030825|||http://purl.uniprot.org/annotation/VSP_030826|||http://purl.uniprot.org/annotation/VSP_030827 http://togogenome.org/gene/10090:Drd4 ^@ http://purl.uniprot.org/uniprot/P51436 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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|||N-linked (GlcNAc...) asparagine|||Pro residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069402 http://togogenome.org/gene/10090:Ripor1 ^@ http://purl.uniprot.org/uniprot/Q68FE6 ^@ 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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho family-interacting cell polarization regulator 1 ^@ http://purl.uniprot.org/annotation/PRO_0000289111 http://togogenome.org/gene/10090:Exoc5 ^@ http://purl.uniprot.org/uniprot/Q3TPX4 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Exocyst complex component 5|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118944 http://togogenome.org/gene/10090:Nlrp9a ^@ http://purl.uniprot.org/uniprot/D3Z7F5|||http://purl.uniprot.org/uniprot/E9QKM4|||http://purl.uniprot.org/uniprot/Q66X03 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||NACHT|||NACHT, LRR and PYD domains-containing protein 9A|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000286335|||http://purl.uniprot.org/annotation/VSP_025022|||http://purl.uniprot.org/annotation/VSP_025023 http://togogenome.org/gene/10090:Ms4a4d ^@ http://purl.uniprot.org/uniprot/Q99N05 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Membrane-spanning 4-domains subfamily A member 4D ^@ http://purl.uniprot.org/annotation/PRO_0000158635 http://togogenome.org/gene/10090:Or8b42 ^@ http://purl.uniprot.org/uniprot/Q7TRD1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp7 ^@ http://purl.uniprot.org/uniprot/Q3TFZ4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:H3c11 ^@ http://purl.uniprot.org/uniprot/P68433 ^@ Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||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|||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; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoarginine|||Phosphoarginine; 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|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000221249 http://togogenome.org/gene/10090:Itgax ^@ http://purl.uniprot.org/uniprot/Q9QXH4 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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-X|||N-linked (GlcNAc...) asparagine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000016295 http://togogenome.org/gene/10090:Fbxo30 ^@ http://purl.uniprot.org/uniprot/Q8BJL1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||F-box|||F-box only protein 30|||Phosphoserine|||TRAF-type ^@ http://purl.uniprot.org/annotation/PRO_0000119919 http://togogenome.org/gene/10090:Prdm14 ^@ http://purl.uniprot.org/uniprot/E9Q3T6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Zinc Finger ^@ C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Impairs interaction with CBFA2T2.|||Interaction with CBFA2T2|||PR domain zinc finger protein 14|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000417666 http://togogenome.org/gene/10090:Il17rc ^@ http://purl.uniprot.org/uniprot/Q8BPI5|||http://purl.uniprot.org/uniprot/Q8K4C2 ^@ 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|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interleukin-17 receptor C|||N-linked (GlcNAc...) asparagine|||SEFIR ^@ http://purl.uniprot.org/annotation/PRO_0000011035|||http://purl.uniprot.org/annotation/VSP_058139|||http://purl.uniprot.org/annotation/VSP_058140|||http://purl.uniprot.org/annotation/VSP_058141|||http://purl.uniprot.org/annotation/VSP_058142 http://togogenome.org/gene/10090:Cmklr1 ^@ http://purl.uniprot.org/uniprot/P97468|||http://purl.uniprot.org/uniprot/Q497D3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Topological Domain|||Transmembrane ^@ Chemerin-like 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|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000069308 http://togogenome.org/gene/10090:AW554918 ^@ http://purl.uniprot.org/uniprot/Q6NZK5 ^@ 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 ^@ Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein hinderin ^@ http://purl.uniprot.org/annotation/PRO_0000312299|||http://purl.uniprot.org/annotation/VSP_029816|||http://purl.uniprot.org/annotation/VSP_029817 http://togogenome.org/gene/10090:Shisa5 ^@ http://purl.uniprot.org/uniprot/Q9D7I0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Pro residues|||Protein shisa-5 ^@ http://purl.uniprot.org/annotation/PRO_0000312879|||http://purl.uniprot.org/annotation/VSP_029957|||http://purl.uniprot.org/annotation/VSP_029958|||http://purl.uniprot.org/annotation/VSP_029959|||http://purl.uniprot.org/annotation/VSP_029960|||http://purl.uniprot.org/annotation/VSP_029961 http://togogenome.org/gene/10090:Or7g17 ^@ http://purl.uniprot.org/uniprot/Q8VGX1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfpm2 ^@ http://purl.uniprot.org/uniprot/Q8CCH7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||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 isoform 2.|||In isoform 3.|||Interaction with CTBP2|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Zinc finger protein ZFPM2 ^@ http://purl.uniprot.org/annotation/PRO_0000221044|||http://purl.uniprot.org/annotation/VSP_009703|||http://purl.uniprot.org/annotation/VSP_009704|||http://purl.uniprot.org/annotation/VSP_009705 http://togogenome.org/gene/10090:Pappa2 ^@ http://purl.uniprot.org/uniprot/E9PZ87|||http://purl.uniprot.org/uniprot/Q505G3|||http://purl.uniprot.org/uniprot/Q8BJG6 ^@ 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 ^@ Disordered|||LNR|||LamG-like jellyroll fold|||Polar residues|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_5003243037 http://togogenome.org/gene/10090:Etfdh ^@ http://purl.uniprot.org/uniprot/Q921G7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ 4Fe-4S ferredoxin-type|||Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000008662 http://togogenome.org/gene/10090:Nod2 ^@ http://purl.uniprot.org/uniprot/Q80SY9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ CARD|||NACHT ^@ http://togogenome.org/gene/10090:Prr14l ^@ http://purl.uniprot.org/uniprot/E9Q7C4|||http://purl.uniprot.org/uniprot/Q3UYV6|||http://purl.uniprot.org/uniprot/Q6UDR4 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Tantalus-like ^@ http://togogenome.org/gene/10090:Carns1 ^@ http://purl.uniprot.org/uniprot/E9PX09 ^@ Domain Extent|||Region ^@ Domain Extent ^@ ATP-grasp ^@ http://togogenome.org/gene/10090:Depdc5 ^@ http://purl.uniprot.org/uniprot/E9QAT3|||http://purl.uniprot.org/uniprot/P61460|||http://purl.uniprot.org/uniprot/Q6GQV2|||http://purl.uniprot.org/uniprot/Q8BVE2 ^@ 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|||DEP|||Disordered|||GATOR1 complex protein DEPDC5|||In isoform 2.|||Mimics phosphorylation; knockin mice show a significant level of resistance to PIM1 inhibitors.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079866|||http://purl.uniprot.org/annotation/VSP_046542 http://togogenome.org/gene/10090:Cftr ^@ http://purl.uniprot.org/uniprot/P26361 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||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|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||Abolishes normal maturation.|||Basic and acidic residues|||Cystic fibrosis transmembrane conductance regulator|||Cytoplasmic|||Discontinuously helical; Name=8|||Disordered|||Disordered R region|||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=9|||Impairs protein folding, due to small local changes that probably disrupt crucial interactions with the transmembrane domain. Abolishes normal maturation. Impairs trafficking to the apical cell membrane.|||In isoform 2.|||In isoform 3.|||Interaction with GORASP2|||Mildly impairs protein maturation.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes normal maturation.|||No effect on protein maturation.|||PDZ-binding|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000093424|||http://purl.uniprot.org/annotation/VSP_000062|||http://purl.uniprot.org/annotation/VSP_000063|||http://purl.uniprot.org/annotation/VSP_000064|||http://purl.uniprot.org/annotation/VSP_000065 http://togogenome.org/gene/10090:Arhgap9 ^@ http://purl.uniprot.org/uniprot/Q1HDU4|||http://purl.uniprot.org/uniprot/Q78T58|||http://purl.uniprot.org/uniprot/Q8QZW8 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||PH|||Rho-GAP|||SH3 ^@ http://togogenome.org/gene/10090:Mboat4 ^@ http://purl.uniprot.org/uniprot/P0C7A3 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Mutagenesis Site|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ 44,4 kDa fragment|||Abolished ability to acylate ghrelin.|||Abolished ability to acylate ghrelin. Does not affect proteic cleavage. loss of serine O-acyltransferase activity.|||Cleavage|||Cytoplasmic|||Does not affect protein cleavage.|||Does not glycosylated.|||Ghrelin O-acyltransferase|||Helical|||Loss of 44,4 kDa form.|||Loss of 44,4 kDa fragment.|||Lumenal|||No effect on ability to acylate ghrelin. ^@ http://purl.uniprot.org/annotation/PRO_0000329073|||http://purl.uniprot.org/annotation/PRO_0000454294 http://togogenome.org/gene/10090:Topaz1 ^@ http://purl.uniprot.org/uniprot/E5FYH1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Protein TOPAZ1 ^@ http://purl.uniprot.org/annotation/PRO_0000416061 http://togogenome.org/gene/10090:Rubcnl ^@ http://purl.uniprot.org/uniprot/F8WGX2 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Rubicon Homology ^@ http://togogenome.org/gene/10090:Nme8 ^@ http://purl.uniprot.org/uniprot/Q715T0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||NDK 1|||NDK 2|||NDK 3|||Redox-active|||Thioredoxin|||Thioredoxin domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000120157|||http://purl.uniprot.org/annotation/VSP_014330|||http://purl.uniprot.org/annotation/VSP_014331 http://togogenome.org/gene/10090:Fgf14 ^@ http://purl.uniprot.org/uniprot/A0A0R4J063|||http://purl.uniprot.org/uniprot/O89096|||http://purl.uniprot.org/uniprot/P70379 ^@ 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|||Fibroblast growth factor 14|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000147611|||http://purl.uniprot.org/annotation/VSP_001530 http://togogenome.org/gene/10090:Mfsd4b5 ^@ http://purl.uniprot.org/uniprot/E9PYY6|||http://purl.uniprot.org/uniprot/Q3TN71|||http://purl.uniprot.org/uniprot/Q8C3P4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:Trmt10b ^@ http://purl.uniprot.org/uniprot/Q9D075 ^@ 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 ^@ Basic residues|||Disordered|||SAM-dependent MTase TRM10-type|||tRNA methyltransferase 10 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000311322 http://togogenome.org/gene/10090:Vmn1r238 ^@ http://purl.uniprot.org/uniprot/E9Q373 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Aadacl4fm5 ^@ http://purl.uniprot.org/uniprot/B1ASB3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Alpha/beta hydrolase fold-3|||Helical ^@ http://togogenome.org/gene/10090:Slc35f5 ^@ http://purl.uniprot.org/uniprot/Q8R314 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ EamA|||Helical|||Phosphoserine|||Solute carrier family 35 member F5 ^@ http://purl.uniprot.org/annotation/PRO_0000311958 http://togogenome.org/gene/10090:9530002B09Rik ^@ http://purl.uniprot.org/uniprot/Q9EPV7 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099716 http://togogenome.org/gene/10090:Tcp11x2 ^@ http://purl.uniprot.org/uniprot/A2AEI7|||http://purl.uniprot.org/uniprot/Q9DAK1 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Map3k19 ^@ http://purl.uniprot.org/uniprot/E9Q3S4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Mitogen-activated protein kinase kinase kinase 19|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000421022 http://togogenome.org/gene/10090:Card19 ^@ http://purl.uniprot.org/uniprot/B2RV71|||http://purl.uniprot.org/uniprot/Q9D1I2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Transmembrane ^@ CARD|||Caspase recruitment domain-containing protein 19|||Helical|||Redox-active ^@ http://purl.uniprot.org/annotation/PRO_0000064928 http://togogenome.org/gene/10090:Hip1 ^@ http://purl.uniprot.org/uniprot/Q8VD75 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||ENTH|||Huntingtin-interacting protein 1|||I/LWEQ|||Important for actin binding|||Phosphoserine|||pDED ^@ http://purl.uniprot.org/annotation/PRO_0000361654 http://togogenome.org/gene/10090:Slc44a2 ^@ http://purl.uniprot.org/uniprot/Q8BY89 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane ^@ Choline transporter-like protein 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000191718|||http://purl.uniprot.org/annotation/VSP_015432 http://togogenome.org/gene/10090:Phka2 ^@ http://purl.uniprot.org/uniprot/A2AHQ7|||http://purl.uniprot.org/uniprot/Q8BWJ3 ^@ Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region ^@ Calmodulin-binding|||Disordered|||GH15-like|||Phosphorylase b kinase regulatory subunit alpha, liver isoform|||Phosphorylase b kinase regulatory subunit alpha/beta C-terminal|||Phosphoserine|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000057731 http://togogenome.org/gene/10090:Or2z9 ^@ http://purl.uniprot.org/uniprot/E9Q4J3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ceacam19 ^@ http://purl.uniprot.org/uniprot/Q3TQ88 ^@ 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 V-set|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5015097448 http://togogenome.org/gene/10090:Dusp12 ^@ http://purl.uniprot.org/uniprot/Q4KL39|||http://purl.uniprot.org/uniprot/Q9D0T2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Dual specificity protein phosphatase 12|||N-acetylmethionine|||Phosphocysteine intermediate|||Phosphoserine|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094819 http://togogenome.org/gene/10090:Zswim8 ^@ http://purl.uniprot.org/uniprot/Q3UHH1 ^@ 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.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SWIM-type|||Zinc finger SWIM domain-containing protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000311803|||http://purl.uniprot.org/annotation/VSP_029592|||http://purl.uniprot.org/annotation/VSP_029593|||http://purl.uniprot.org/annotation/VSP_029594|||http://purl.uniprot.org/annotation/VSP_029595|||http://purl.uniprot.org/annotation/VSP_029596|||http://purl.uniprot.org/annotation/VSP_029597|||http://purl.uniprot.org/annotation/VSP_029598|||http://purl.uniprot.org/annotation/VSP_029599|||http://purl.uniprot.org/annotation/VSP_029600 http://togogenome.org/gene/10090:B3galnt2 ^@ http://purl.uniprot.org/uniprot/Q8BG28 ^@ 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; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000248363|||http://purl.uniprot.org/annotation/VSP_020253|||http://purl.uniprot.org/annotation/VSP_020254 http://togogenome.org/gene/10090:Syndig1 ^@ http://purl.uniprot.org/uniprot/A2ANU3 ^@ Chain|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Phosphoserine|||Synapse differentiation-inducing gene protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000394033 http://togogenome.org/gene/10090:Pth1r ^@ http://purl.uniprot.org/uniprot/P41593 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||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|||Important for interaction with G proteins|||N-linked (GlcNAc...) asparagine|||Parathyroid hormone/parathyroid hormone-related peptide receptor ^@ http://purl.uniprot.org/annotation/PRO_0000012846 http://togogenome.org/gene/10090:Mmp10 ^@ http://purl.uniprot.org/uniprot/A1L3D0|||http://purl.uniprot.org/uniprot/O55123 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Propeptide|||Repeat|||Signal Peptide ^@ Activation peptide|||Cysteine switch|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Peptidase metallopeptidase|||Phosphotyrosine; by PKDCC|||Stromelysin-2|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028766|||http://purl.uniprot.org/annotation/PRO_0000028767|||http://purl.uniprot.org/annotation/PRO_5014296758 http://togogenome.org/gene/10090:Mycs ^@ http://purl.uniprot.org/uniprot/Q9Z304 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Leucine-zipper|||Phosphotyrosine; by Tyr-kinases|||Protein S-Myc|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127341 http://togogenome.org/gene/10090:Adrb1 ^@ http://purl.uniprot.org/uniprot/P34971 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Beta-1 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|||In knockin mouse model, decreases protein levels. Mice exhibit a short sleep phenotype. Changes the electrophysiological properties of dorsal pons neurons.|||N-linked (GlcNAc...) asparagine|||PDZ-Binding|||Phosphoserine|||Phosphoserine; by PKA|||Polar residues|||Pro residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069122 http://togogenome.org/gene/10090:Pttg1ip ^@ http://purl.uniprot.org/uniprot/F6TFF2|||http://purl.uniprot.org/uniprot/Q8R143 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphotyrosine|||Pituitary tumor-transforming gene 1 protein-interacting protein ^@ http://purl.uniprot.org/annotation/PRO_0000022185 http://togogenome.org/gene/10090:Ehmt2 ^@ http://purl.uniprot.org/uniprot/A2CG76|||http://purl.uniprot.org/uniprot/Q9Z148 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Site|||Splice Variant ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Abolishes histone methyltransferase activity and subsequent repression. In GM3; does not form heterodimer with EHMT1 and is defective in mediating both H3K9me and DNA methylation.|||Acidic residues|||Asymmetric dimethylarginine|||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|||In GM4; defective in methyltransferase activity without affecting DNA methylation.|||In GM6; does not form heterodimer with EHMT1 and is defective in mediating H3K9me.|||In GM7; defective in methyltransferase activity without affecting DNA methylation; when associated with F-1207.|||In GM7; defective in methyltransferase activity without affecting DNA methylation; when associated with V-1120.|||In isoform 2 and isoform 3.|||In isoform 2.|||Interaction with histone H3|||N6,N6,N6-trimethyllysine; by EHMT2; alternate|||N6,N6-dimethyllysine; by EHMT2; alternate|||Phosphoserine|||Phosphothreonine|||Post-SET|||Pre-SET|||SET|||Strongly reduces histone methyltransferase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000186069|||http://purl.uniprot.org/annotation/VSP_002214|||http://purl.uniprot.org/annotation/VSP_002215|||http://purl.uniprot.org/annotation/VSP_002216 http://togogenome.org/gene/10090:Fcer2a ^@ http://purl.uniprot.org/uniprot/P20693|||http://purl.uniprot.org/uniprot/Q8VH32|||http://purl.uniprot.org/uniprot/Q8VH33 ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Low affinity immunoglobulin epsilon Fc receptor|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000046640|||http://purl.uniprot.org/annotation/VSP_003058|||http://purl.uniprot.org/annotation/VSP_003059 http://togogenome.org/gene/10090:Cd2bp2 ^@ http://purl.uniprot.org/uniprot/Q9CWK3 ^@ 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|||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_0000089438 http://togogenome.org/gene/10090:Orm1 ^@ http://purl.uniprot.org/uniprot/Q60590 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Signal Peptide ^@ Alpha-1-acid glycoprotein 1|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000017862 http://togogenome.org/gene/10090:Tmem40 ^@ http://purl.uniprot.org/uniprot/E9Q6I9|||http://purl.uniprot.org/uniprot/Q4FJU9 ^@ 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|||Transmembrane protein 40 ^@ http://purl.uniprot.org/annotation/PRO_0000280359 http://togogenome.org/gene/10090:Or10a5 ^@ http://purl.uniprot.org/uniprot/Q920G5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cd84 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0K5|||http://purl.uniprot.org/uniprot/A0A0R4J1S4|||http://purl.uniprot.org/uniprot/E9Q9E8|||http://purl.uniprot.org/uniprot/Q18PI6 ^@ 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|||Helical|||ITSM 1|||ITSM 2|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||Immunoglobulin V-set|||In isoform 2.|||In isoform 3.|||Modulates macrophage cytokine secretion.|||N-linked (GlcNAc...) asparagine|||No effect on macrophage cytokine secretion.|||Phosphotyrosine|||Phosphotyrosine; by LYN|||SLAM family member 5 ^@ http://purl.uniprot.org/annotation/PRO_0000252030|||http://purl.uniprot.org/annotation/PRO_5003243136|||http://purl.uniprot.org/annotation/PRO_5006452011|||http://purl.uniprot.org/annotation/PRO_5015044292|||http://purl.uniprot.org/annotation/VSP_020857|||http://purl.uniprot.org/annotation/VSP_020858|||http://purl.uniprot.org/annotation/VSP_020859 http://togogenome.org/gene/10090:Nxf7 ^@ http://purl.uniprot.org/uniprot/Q80SZ6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||NTF2|||Polar residues|||TAP-C ^@ http://togogenome.org/gene/10090:H1f0 ^@ http://purl.uniprot.org/uniprot/P10922 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ ADP-ribosylserine|||Basic and acidic residues|||Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.0|||Histone H1.0, N-terminally processed|||N-acetylmethionine|||N-acetylthreonine; in Histone H1.0, N-terminally processed|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000195913|||http://purl.uniprot.org/annotation/PRO_0000423208 http://togogenome.org/gene/10090:Ppib ^@ http://purl.uniprot.org/uniprot/P24369|||http://purl.uniprot.org/uniprot/Q9DCY1 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Signal Peptide ^@ N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase B|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000025480 http://togogenome.org/gene/10090:Armc5 ^@ http://purl.uniprot.org/uniprot/Q5EBP3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||Armadillo repeat-containing protein 5|||BTB|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284406 http://togogenome.org/gene/10090:Tcea3 ^@ http://purl.uniprot.org/uniprot/P23881 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||TFIIS N-terminal|||TFIIS central|||TFIIS-type|||Transcription elongation factor A protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000121453 http://togogenome.org/gene/10090:Vtcn1 ^@ http://purl.uniprot.org/uniprot/Q7TSP5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ GPI-anchor amidated glycine|||Ig-like V-type 1|||Ig-like V-type 2|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||V-set domain containing T-cell activation inhibitor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000339238|||http://purl.uniprot.org/annotation/PRO_0000339239 http://togogenome.org/gene/10090:Csf2rb2 ^@ http://purl.uniprot.org/uniprot/A0A2R8VHE8|||http://purl.uniprot.org/uniprot/P26954|||http://purl.uniprot.org/uniprot/Q3U1Z1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||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 domain-containing protein|||Helical|||Interleukin-3 receptor class 2 subunit beta|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010885|||http://purl.uniprot.org/annotation/PRO_5004229865|||http://purl.uniprot.org/annotation/PRO_5016321830 http://togogenome.org/gene/10090:Cbr1 ^@ http://purl.uniprot.org/uniprot/B2RXY7|||http://purl.uniprot.org/uniprot/P48758 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Carbonyl reductase [NADPH] 1|||Disordered|||N-acetylserine|||N6-1-carboxyethyl lysine|||Phosphoserine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000054603 http://togogenome.org/gene/10090:Adgrg6 ^@ http://purl.uniprot.org/uniprot/Q6F3F9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ ADGRG6 C-terminal fragment|||ADGRG6 N-terminal fragment|||Adhesion G-protein coupled receptor G6|||CUB|||Cleavage|||Cleavage; by furin like-convertase|||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|||Inhibits receptor signaling in absence of type IV collagen|||Mediates interaction with laminin-2|||Mediates interaction with type IV collagen|||N-linked (GlcNAc...) asparagine|||Pentraxin (PTX)|||Phosphoserine|||STACHEL ^@ http://purl.uniprot.org/annotation/PRO_0000303888|||http://purl.uniprot.org/annotation/PRO_0000438598|||http://purl.uniprot.org/annotation/PRO_0000438599 http://togogenome.org/gene/10090:Tsen15 ^@ http://purl.uniprot.org/uniprot/G3X8S8|||http://purl.uniprot.org/uniprot/Q8R3W5 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||tRNA-splicing endonuclease subunit Sen15 ^@ http://purl.uniprot.org/annotation/PRO_0000194024 http://togogenome.org/gene/10090:N4bp3 ^@ http://purl.uniprot.org/uniprot/Q8C7U1 ^@ 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|||NEDD4-binding protein 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096683 http://togogenome.org/gene/10090:Potefam3c ^@ http://purl.uniprot.org/uniprot/A0A0J9YUZ3 ^@ Region|||Repeat ^@ Region|||Repeat ^@ ANK|||Disordered ^@ http://togogenome.org/gene/10090:Virma ^@ http://purl.uniprot.org/uniprot/A2AIV2|||http://purl.uniprot.org/uniprot/E9PZY8 ^@ 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 ^@ Acidic residues|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein virilizer homolog|||Removed|||Virilizer N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000308606|||http://purl.uniprot.org/annotation/VSP_029022|||http://purl.uniprot.org/annotation/VSP_029023 http://togogenome.org/gene/10090:Ccr10 ^@ http://purl.uniprot.org/uniprot/Q9JL21 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-C chemokine receptor type 10|||Cytoplasmic|||Extracellular|||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_0000069294 http://togogenome.org/gene/10090:Slc22a5 ^@ http://purl.uniprot.org/uniprot/Q5SX17|||http://purl.uniprot.org/uniprot/Q9Z0E8 ^@ 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|||Sequence 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 JVS.|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Organic cation/carnitine transporter 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000220501 http://togogenome.org/gene/10090:Vmn1r29 ^@ http://purl.uniprot.org/uniprot/Q9EQ41 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ocrl ^@ http://purl.uniprot.org/uniprot/Q6NVF0 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Motif|||Region|||Splice Variant ^@ 5-phosphatase|||ASH|||Clathrin box 1|||Clathrin box 2|||Disordered|||In isoform 2.|||Inositol polyphosphate 5-phosphatase OCRL|||PH|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000421564|||http://purl.uniprot.org/annotation/VSP_045749|||http://purl.uniprot.org/annotation/VSP_045750 http://togogenome.org/gene/10090:Or5b121 ^@ http://purl.uniprot.org/uniprot/Q7TQQ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gprc5c ^@ http://purl.uniprot.org/uniprot/I7HPW4|||http://purl.uniprot.org/uniprot/J3JS84|||http://purl.uniprot.org/uniprot/Q8K3J9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000012968|||http://purl.uniprot.org/annotation/PRO_5015094047|||http://purl.uniprot.org/annotation/PRO_5015094050 http://togogenome.org/gene/10090:Sacs ^@ http://purl.uniprot.org/uniprot/Q9JLC8 ^@ 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|||HEPN|||In isoform 2.|||In isoform 3.|||J|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sacsin|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000097564|||http://purl.uniprot.org/annotation/VSP_022326|||http://purl.uniprot.org/annotation/VSP_022327 http://togogenome.org/gene/10090:Dnajc7 ^@ http://purl.uniprot.org/uniprot/Q9QYI3 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ DnaJ homolog subfamily C member 7|||J|||N-acetylalanine|||Phosphoserine|||Removed|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8 ^@ http://purl.uniprot.org/annotation/PRO_0000071059 http://togogenome.org/gene/10090:H2-Ob ^@ http://purl.uniprot.org/uniprot/O35424|||http://purl.uniprot.org/uniprot/Q3U1X7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like|||Ig-like domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5010843363|||http://purl.uniprot.org/annotation/PRO_5015096771 http://togogenome.org/gene/10090:Nkx2-3 ^@ http://purl.uniprot.org/uniprot/P97334 ^@ 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 Nkx-2.3 ^@ http://purl.uniprot.org/annotation/PRO_0000048934 http://togogenome.org/gene/10090:Gpr150 ^@ http://purl.uniprot.org/uniprot/Q8BL07 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||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|||Probable G-protein coupled receptor 150 ^@ http://purl.uniprot.org/annotation/PRO_0000069631 http://togogenome.org/gene/10090:Fuz ^@ http://purl.uniprot.org/uniprot/E9QL29|||http://purl.uniprot.org/uniprot/Q3UYI6 ^@ 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 ^@ FUZ/MON1/HPS1 first Longin|||FUZ/MON1/HPS1 second Longin|||FUZ/MON1/HPS1 third Longin|||In isoform 2.|||Protein fuzzy homolog ^@ http://purl.uniprot.org/annotation/PRO_0000312921|||http://purl.uniprot.org/annotation/VSP_029967|||http://purl.uniprot.org/annotation/VSP_029968 http://togogenome.org/gene/10090:Prss23 ^@ http://purl.uniprot.org/uniprot/Q9D6X6 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||N-linked (GlcNAc...) asparagine|||Serine protease 23 ^@ http://purl.uniprot.org/annotation/PRO_0000027848 http://togogenome.org/gene/10090:Rnf126 ^@ http://purl.uniprot.org/uniprot/Q3U3G2|||http://purl.uniprot.org/uniprot/Q91YL2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||C4-type|||Disordered|||E3 ubiquitin-protein ligase RNF126|||Loss of E3 ubiquitin protein ligase activity.|||Loss of interaction with EGFR and FLT3. No effect on E3 ubiquitin protein ligase activity but alters specificity for 'Lys-48'-linked chains; when associated with A-13.|||Loss of interaction with EGFR and FLT3. No effect on E3 ubiquitin protein ligase activity but alters specificity for 'Lys-48'-linked chains; when associated with A-16.|||N-acetylalanine|||Phosphoserine|||Polar residues|||RING-type|||Removed|||Required for interaction with BAG6|||Sufficient for interaction with AICDA ^@ http://purl.uniprot.org/annotation/PRO_0000056094 http://togogenome.org/gene/10090:Or9r3 ^@ http://purl.uniprot.org/uniprot/Q7TRH2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fars2 ^@ http://purl.uniprot.org/uniprot/G3X9Q4|||http://purl.uniprot.org/uniprot/Q8BW46|||http://purl.uniprot.org/uniprot/Q99M01 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Aminoacyl-transfer RNA synthetases class-II family profile|||FDX-ACB|||Mitochondrion|||N6-acetyllysine|||Phenylalanine--tRNA ligase, mitochondrial|||Phenylalanyl-tRNA synthetase ^@ http://purl.uniprot.org/annotation/PRO_0000035814 http://togogenome.org/gene/10090:Psmd7 ^@ http://purl.uniprot.org/uniprot/A1L3B8|||http://purl.uniprot.org/uniprot/P26516 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ 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_0000213944 http://togogenome.org/gene/10090:Trim45 ^@ http://purl.uniprot.org/uniprot/Q6PFY8 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ B box-type 1|||B box-type 2|||E3 ubiquitin-protein ligase TRIM45|||Filamin|||In isoform 2.|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056267|||http://purl.uniprot.org/annotation/VSP_012001 http://togogenome.org/gene/10090:Ccdc88a ^@ http://purl.uniprot.org/uniprot/Q5SNZ0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||GBA|||Girdin|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoinositide-binding|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH2-like; required for interaction with growth factor receptors ^@ http://purl.uniprot.org/annotation/PRO_0000287430|||http://purl.uniprot.org/annotation/VSP_052410|||http://purl.uniprot.org/annotation/VSP_052411 http://togogenome.org/gene/10090:Rp1 ^@ http://purl.uniprot.org/uniprot/P56716|||http://purl.uniprot.org/uniprot/Q4VA02|||http://purl.uniprot.org/uniprot/Q8BXN6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Doublecortin|||Doublecortin 1|||Doublecortin 2|||Oxygen-regulated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000097411 http://togogenome.org/gene/10090:Qdpr ^@ http://purl.uniprot.org/uniprot/Q8BVI4 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Dihydropteridine reductase|||N6-succinyllysine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054637 http://togogenome.org/gene/10090:Cd244a ^@ http://purl.uniprot.org/uniprot/Q07763 ^@ 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 ^@ Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-266, F-325 and F-344.|||Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-266, F-325 and F-369.|||Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-266, F-344 and F-369.|||Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-325, F-344 and F-369.|||Cytoplasmic|||Decreases downstream phosphorylation of CBL and VAV1.|||Disordered|||Extracellular|||Helical|||ITSM 1|||ITSM 2|||ITSM 3|||ITSM 4|||Ig-like 1|||Ig-like 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Natural killer cell receptor 2B4|||Phosphotyrosine|||Phosphotyrosine; by FYN|||Polar residues|||Weakly decreases downstream phosphorylation of CBL and VAV1; when associated with F-325 and F-344.|||Weakly decreases downstream phosphorylation of CBL and VAV1; when associated with F-325 and F-369.|||Weakly decreases downstream phosphorylation of CBL and VAV1; when associated with F-344 and F-369. ^@ http://purl.uniprot.org/annotation/PRO_0000014669|||http://purl.uniprot.org/annotation/VSP_010401|||http://purl.uniprot.org/annotation/VSP_010402 http://togogenome.org/gene/10090:Gm13288 ^@ http://purl.uniprot.org/uniprot/Q8CD73 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099103 http://togogenome.org/gene/10090:Ybx1 ^@ http://purl.uniprot.org/uniprot/P62960|||http://purl.uniprot.org/uniprot/Q3UBT1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||C5-methylcytosine binding|||CSD|||Cleavage; by 20S proteasomal protease|||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|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphotyrosine|||Polar residues|||Removed|||Y-box-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000100220 http://togogenome.org/gene/10090:Coq7 ^@ http://purl.uniprot.org/uniprot/P97478|||http://purl.uniprot.org/uniprot/Q3TYT1 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Repeat|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Region|||Repeat|||Transit Peptide ^@ 1|||2|||2 X approximate tandem repeats|||5-demethoxyubiquinone hydroxylase, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000079252 http://togogenome.org/gene/10090:Pard3b ^@ http://purl.uniprot.org/uniprot/Q05B96|||http://purl.uniprot.org/uniprot/Q3URJ9|||http://purl.uniprot.org/uniprot/Q8BKM8|||http://purl.uniprot.org/uniprot/Q9CSB4 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||PDZ 1|||PDZ 2|||PDZ 3|||Partitioning defective 3 homolog B|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000185073|||http://purl.uniprot.org/annotation/VSP_022017 http://togogenome.org/gene/10090:Tbpl2 ^@ http://purl.uniprot.org/uniprot/B7ZMZ6|||http://purl.uniprot.org/uniprot/Q6SJ95 ^@ 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|||TATA box-binding protein-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000318119 http://togogenome.org/gene/10090:Vmn2r67 ^@ http://purl.uniprot.org/uniprot/K7N6T2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908727 http://togogenome.org/gene/10090:Cyp11b2 ^@ http://purl.uniprot.org/uniprot/G3UWE4|||http://purl.uniprot.org/uniprot/P15539 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Sequence Conflict|||Transit Peptide ^@ Cytochrome P450 11B2, mitochondrial|||Mitochondrion|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000003600 http://togogenome.org/gene/10090:Smap1 ^@ http://purl.uniprot.org/uniprot/D3YVX4|||http://purl.uniprot.org/uniprot/Q91VZ6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ Arf-GAP|||Basic and acidic residues|||C4-type|||Disordered|||Interaction with clathrin heavy chains|||Loss of GTPase activation.|||Loss of interaction with clathrin heavy chains.|||Stromal membrane-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000235839 http://togogenome.org/gene/10090:Aard ^@ http://purl.uniprot.org/uniprot/Q811W1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Alanine and arginine-rich domain-containing protein|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000337037 http://togogenome.org/gene/10090:Acvrl1 ^@ http://purl.uniprot.org/uniprot/Q61288 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||GS|||Helical|||Mediates specificity for BMP ligand|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase receptor R3 ^@ http://purl.uniprot.org/annotation/PRO_0000024421 http://togogenome.org/gene/10090:Tuba8 ^@ http://purl.uniprot.org/uniprot/Q9JJZ2 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Motif|||Sequence Conflict ^@ Dephenylalaninated tubulin alpha-8 chain|||MREC motif|||Tubulin alpha-8 chain ^@ http://purl.uniprot.org/annotation/PRO_0000048125|||http://purl.uniprot.org/annotation/PRO_0000456435 http://togogenome.org/gene/10090:Gbe1 ^@ http://purl.uniprot.org/uniprot/Q9D6Y9 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ 1,4-alpha-glucan-branching enzyme|||N-acetylalanine|||Nucleophile|||Phosphotyrosine|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000188776 http://togogenome.org/gene/10090:Foxi3 ^@ http://purl.uniprot.org/uniprot/D3Z120 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ 9aaTAD|||Abolished localization to the nucleus.|||Disordered|||Does not affect nuclear localization.|||Does not affect transcription factor activity.|||Fork-head|||Forkhead box protein I3|||In Mut1; reduced transcription factor activity.|||In Mut2; strongly reduced transcription factor activity.|||Knockin mice are significantly smaller and die immediately after birth. They show a partially truncated mandible and fusion of the upper and lower jaws (syngnathia) and anomalies of various bones of the ear.|||Knockin mice hemizygous for L-218 mutant and a deletion of the wild-type Foxi3 allele fail to thrive after birth, are underweight, display respiratory abnormalities and die between birth and day 5.|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Reduced transcription factor activity. ^@ http://purl.uniprot.org/annotation/PRO_0000458754 http://togogenome.org/gene/10090:Hbb-bs ^@ http://purl.uniprot.org/uniprot/A8DUK4|||http://purl.uniprot.org/uniprot/P02088 ^@ 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 ^@ Asymmetric dimethylarginine|||Globin family profile|||Hemoglobin subunit beta-1|||In allele S and allele W1.|||In allele S.|||In allele W1.|||N-acetylvaline|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||distal binding residue|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000053024 http://togogenome.org/gene/10090:Snx15 ^@ http://purl.uniprot.org/uniprot/Q91WE1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||MIT|||Omega-N-methylarginine|||PX|||Phosphoserine|||Pro residues|||Sorting nexin-15 ^@ http://purl.uniprot.org/annotation/PRO_0000236202 http://togogenome.org/gene/10090:Zfp964 ^@ http://purl.uniprot.org/uniprot/B2RR88 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Eeig2 ^@ http://purl.uniprot.org/uniprot/E9Q4R1|||http://purl.uniprot.org/uniprot/Q8BQS4 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ C2 NT-type|||Disordered|||EEIG family member 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000236181 http://togogenome.org/gene/10090:Itgb1 ^@ http://purl.uniprot.org/uniprot/P09055 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ CX3CL1-binding|||Cytoplasmic|||Disordered|||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.|||Integrin beta-1|||Interaction with ITGB1BP1|||Interaction with TMEM182|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine; alternate|||PSI|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Reduced endocytosis; when associated with F-783.|||Reduced endocytosis; when associated with F-795.|||Signal for sorting from recycling endosomes; interaction with ACAP1|||VWFA|||in ADMIDAS binding site|||in LIMBS binding site|||in MIDAS binding site ^@ http://purl.uniprot.org/annotation/PRO_0000016335|||http://purl.uniprot.org/annotation/VSP_053581|||http://purl.uniprot.org/annotation/VSP_053582 http://togogenome.org/gene/10090:Atf6 ^@ http://purl.uniprot.org/uniprot/F6VAN0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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|||Interaction with THBS4|||Leucine-zipper|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Processed cyclic AMP-dependent transcription factor ATF-6 alpha|||Transcription activation|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000424336|||http://purl.uniprot.org/annotation/PRO_0000424337 http://togogenome.org/gene/10090:Simc1 ^@ http://purl.uniprot.org/uniprot/E9Q6E9|||http://purl.uniprot.org/uniprot/Q505H0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||Interaction with SLF2|||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_0000451959|||http://purl.uniprot.org/annotation/VSP_060887|||http://purl.uniprot.org/annotation/VSP_060888 http://togogenome.org/gene/10090:Poglut3 ^@ http://purl.uniprot.org/uniprot/G5E897 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Signal Peptide ^@ Chain|||Glycosylation Site|||Motif|||Repeat|||Signal Peptide ^@ Filamin|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Protein O-glucosyltransferase 3 ^@ http://purl.uniprot.org/annotation/PRO_5015091896 http://togogenome.org/gene/10090:Scgb2b19 ^@ http://purl.uniprot.org/uniprot/J3QM75 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015095467 http://togogenome.org/gene/10090:Kdm5b ^@ http://purl.uniprot.org/uniprot/Q80Y84 ^@ 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ ARID|||Abolishes enzymatic activity.|||Basic and acidic residues|||C5HC2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||JmjC|||JmjN|||Lysine-specific demethylase 5B|||N6-acetyllysine|||PHD-type 1|||PHD-type 2|||PHD-type 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000292413|||http://purl.uniprot.org/annotation/VSP_026409 http://togogenome.org/gene/10090:Stxbp6 ^@ http://purl.uniprot.org/uniprot/Q3TYA4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ V-SNARE coiled-coil homology ^@ http://togogenome.org/gene/10090:Kcnn1 ^@ http://purl.uniprot.org/uniprot/A0A140T8Q8|||http://purl.uniprot.org/uniprot/Q9EQR3 ^@ Chain|||Coiled-Coil|||Domain Extent|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||INTRAMEM|||Region|||Sequence Variant|||Splice Variant|||Transmembrane ^@ Calmodulin-binding|||Disordered|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||In isoform 2.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 4 and isoform 9.|||In isoform 5 and isoform 8.|||In isoform 6 and isoform 7.|||In strain: C57BL/6J, A/HeJ and SPRET/Ei.|||In strain: C57BL/6J.|||In strain: SWR/J, AKR/J, RBF/DNJ and P/J.|||Pore-forming; Name=Segment H5|||Segment S6|||Small conductance calcium-activated potassium channel protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000155008|||http://purl.uniprot.org/annotation/VSP_002809|||http://purl.uniprot.org/annotation/VSP_002810|||http://purl.uniprot.org/annotation/VSP_002811|||http://purl.uniprot.org/annotation/VSP_002812|||http://purl.uniprot.org/annotation/VSP_002813 http://togogenome.org/gene/10090:Zfp580 ^@ http://purl.uniprot.org/uniprot/Q9DB38 ^@ 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_0000047672 http://togogenome.org/gene/10090:Rabggta ^@ http://purl.uniprot.org/uniprot/Q9JHK4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Modified Residue|||Repeat|||Splice Variant ^@ Geranylgeranyl transferase type-2 subunit alpha|||In isoform 2.|||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_0000119758|||http://purl.uniprot.org/annotation/VSP_009113|||http://purl.uniprot.org/annotation/VSP_009114 http://togogenome.org/gene/10090:Strip1 ^@ http://purl.uniprot.org/uniprot/Q3UGC1|||http://purl.uniprot.org/uniprot/Q8C079 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Far11/STRP C-terminal|||Far11/STRP N-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Pro residues|||Striatin-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000187019|||http://purl.uniprot.org/annotation/VSP_014863|||http://purl.uniprot.org/annotation/VSP_014865|||http://purl.uniprot.org/annotation/VSP_014866 http://togogenome.org/gene/10090:Tcp11l2 ^@ http://purl.uniprot.org/uniprot/Q8K1H7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Polar residues|||T-complex protein 11-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000313751 http://togogenome.org/gene/10090:Xrn2 ^@ http://purl.uniprot.org/uniprot/Q9DBR1 ^@ 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 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000071397|||http://purl.uniprot.org/annotation/VSP_007235 http://togogenome.org/gene/10090:Cyp2c29 ^@ http://purl.uniprot.org/uniprot/Q3UEF2|||http://purl.uniprot.org/uniprot/Q64458 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Cytochrome P450 2C29|||N6-acetyllysine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051717 http://togogenome.org/gene/10090:Smarcd2 ^@ http://purl.uniprot.org/uniprot/Q3TXH6|||http://purl.uniprot.org/uniprot/Q99JR8 ^@ 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|||DM2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pro residues|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2|||SWIB/MDM2 ^@ http://purl.uniprot.org/annotation/PRO_0000071986|||http://purl.uniprot.org/annotation/VSP_040533 http://togogenome.org/gene/10090:Fnip2 ^@ http://purl.uniprot.org/uniprot/D3YUC5|||http://purl.uniprot.org/uniprot/Q80TD3 ^@ 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|||Folliculin-interacting protein 2|||Interaction with PRKAA1|||Phosphoserine|||Polar residues|||UDENN FNIP1/2-type|||cDENN FNIP1/2-type|||dDENN FNIP1/2-type|||uDENN FNIP1/2-type ^@ http://purl.uniprot.org/annotation/PRO_0000320554 http://togogenome.org/gene/10090:Ift172 ^@ http://purl.uniprot.org/uniprot/Q6VH22 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||In wim; embryos arrest at 10.5-11.5 dpc and display an open neural tube in the head that lack the normal groove on the ventral midline. They lack ventral neural cell types and display other phenotypes characteristic of defects in Sonic hedgehog signaling.|||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_0000328942|||http://purl.uniprot.org/annotation/VSP_032850 http://togogenome.org/gene/10090:Mrpl1 ^@ http://purl.uniprot.org/uniprot/Q99N96 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein uL1m|||Mitochondrion|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000252441 http://togogenome.org/gene/10090:Cebpb ^@ http://purl.uniprot.org/uniprot/P28033|||http://purl.uniprot.org/uniprot/Q3UPN9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Asymmetric dimethylarginine; by CARM1|||BZIP|||Basic motif|||CCAAT/enhancer-binding protein beta|||Disordered|||Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-184.|||Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-188.|||Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-184 and A-188.|||Dominant negative. Loss of transactivation activity. No effect on interaction with EP300.|||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|||Highly increases transactivation activity; when associated with A-180.|||Highly increases transactivation activity; when associated with A-181.|||In isoform 2.|||In isoform 3.|||Induces hepatocyte proliferation.|||Leucine-zipper|||Loss of hepatocyte proliferation induction by TGFA.|||N6-acetyllysine; alternate|||N6-acetyllysine; by KAT2A and KAT2B|||N6-acetyllysine; by KAT2A and KAT2B; alternate|||N6-methylated lysine; alternate|||No effect on interaction with EP300.|||No effect on transactivation activity.|||No effect on transactivation activity. Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-101 and R-102.|||Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-98 and R-102.|||Not acetylated and no increase of transactivation activity after glucocorticoid-stimulation; when associated with R-98 and R-101.|||Not sumoylated and not ubiquitinated.|||Not sumoylated. Decreases ubiquitination and increases stability. Loss of proliferation inhibition in T cells. No effect on transactivation activity.|||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|||Reduces phosphorylation in response to calcium.|||Required for Lys-133 sumoylation|||Required for MYC transcriptional repression|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076618|||http://purl.uniprot.org/annotation/VSP_053976|||http://purl.uniprot.org/annotation/VSP_053977 http://togogenome.org/gene/10090:Plod1 ^@ http://purl.uniprot.org/uniprot/Q9R0E2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Fe2OG dioxygenase|||N-linked (GlcNAc...) asparagine|||Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000024679 http://togogenome.org/gene/10090:Rufy2 ^@ http://purl.uniprot.org/uniprot/B2RQ36|||http://purl.uniprot.org/uniprot/Q8R4C2 ^@ 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 ^@ FYVE-type|||RUN|||RUN and FYVE domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000245831 http://togogenome.org/gene/10090:Cpsf2 ^@ http://purl.uniprot.org/uniprot/O35218|||http://purl.uniprot.org/uniprot/Q3UGU6 ^@ 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 ^@ Basic and acidic residues|||Beta-Casp|||Cleavage and polyadenylation specificity factor subunit 2|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000074394 http://togogenome.org/gene/10090:Cep68 ^@ http://purl.uniprot.org/uniprot/Q8C0D9 ^@ 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|||Centrosomal protein of 68 kDa|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089495|||http://purl.uniprot.org/annotation/VSP_013477 http://togogenome.org/gene/10090:Rpl3l ^@ http://purl.uniprot.org/uniprot/E9PWZ3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Basic residues|||Disordered|||In isoform 2.|||Large ribosomal subunit protein uL3-like ^@ http://purl.uniprot.org/annotation/PRO_0000457813|||http://purl.uniprot.org/annotation/VSP_061845 http://togogenome.org/gene/10090:Nt5c1b ^@ http://purl.uniprot.org/uniprot/Q6P906|||http://purl.uniprot.org/uniprot/Q91YE9 ^@ 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.|||Nucleophile|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000144797|||http://purl.uniprot.org/annotation/VSP_010204|||http://purl.uniprot.org/annotation/VSP_010205 http://togogenome.org/gene/10090:Dhx38 ^@ http://purl.uniprot.org/uniprot/Q80X98 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Birc2 ^@ http://purl.uniprot.org/uniprot/Q62210 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Zinc Finger ^@ BIR 1|||BIR 2|||BIR 3|||Baculoviral IAP repeat-containing protein 2|||CARD|||Omega-N-methylarginine|||Phosphoserine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000122348 http://togogenome.org/gene/10090:Timp4 ^@ http://purl.uniprot.org/uniprot/Q3USH7|||http://purl.uniprot.org/uniprot/Q9JHB3 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Involved in metalloproteinase-binding|||Metalloproteinase inhibitor 4|||NTR|||NTR domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000034350|||http://purl.uniprot.org/annotation/PRO_5014309165 http://togogenome.org/gene/10090:Klhl11 ^@ http://purl.uniprot.org/uniprot/Q14DU1|||http://purl.uniprot.org/uniprot/Q8CE33 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Repeat|||Signal Peptide|||Splice Variant ^@ BACK|||BTB|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch-like protein 11|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000243919|||http://purl.uniprot.org/annotation/VSP_019496 http://togogenome.org/gene/10090:Ugdh ^@ http://purl.uniprot.org/uniprot/O70475|||http://purl.uniprot.org/uniprot/Q3TS38 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Allosteric switch region|||Disordered|||Important for formation of active hexamer structure|||In lzme; causes arrest of embryonic development during gastrulation due to chondroitin sulfate and heparan sulfate deficiency, impaired FGF signaling and impaired migration of mesoderm and endoderm.|||N6-acetyllysine|||Nucleophile|||Phosphothreonine|||Proton donor/acceptor|||UDP-glucose 6-dehydrogenase|||UDP-glucose/GDP-mannose dehydrogenase C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000074061 http://togogenome.org/gene/10090:Cpped1 ^@ http://purl.uniprot.org/uniprot/Q8BFS6 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Region|||Splice Variant ^@ Catalytic|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Serine/threonine-protein phosphatase CPPED1 ^@ http://purl.uniprot.org/annotation/PRO_0000320557|||http://purl.uniprot.org/annotation/VSP_031659|||http://purl.uniprot.org/annotation/VSP_031660|||http://purl.uniprot.org/annotation/VSP_031661|||http://purl.uniprot.org/annotation/VSP_031662|||http://purl.uniprot.org/annotation/VSP_031663|||http://purl.uniprot.org/annotation/VSP_031664|||http://purl.uniprot.org/annotation/VSP_031665 http://togogenome.org/gene/10090:4931414P19Rik ^@ http://purl.uniprot.org/uniprot/Q8K2W9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Uncharacterized protein C14orf93 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000020951 http://togogenome.org/gene/10090:Inpp4a ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Q2|||http://purl.uniprot.org/uniprot/D3YUD3|||http://purl.uniprot.org/uniprot/D3Z230|||http://purl.uniprot.org/uniprot/E9Q9A0|||http://purl.uniprot.org/uniprot/E9QAD0|||http://purl.uniprot.org/uniprot/F6V2U0|||http://purl.uniprot.org/uniprot/Q3UEQ1|||http://purl.uniprot.org/uniprot/Q9EPW0 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ C2|||Disordered|||Helical|||In isoform 2.|||Inositol polyphosphate-4-phosphatase type I A|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000190233|||http://purl.uniprot.org/annotation/VSP_015243|||http://purl.uniprot.org/annotation/VSP_015244|||http://purl.uniprot.org/annotation/VSP_015245|||http://purl.uniprot.org/annotation/VSP_015246 http://togogenome.org/gene/10090:Aldoart1 ^@ http://purl.uniprot.org/uniprot/A6ZI46 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Clcn1 ^@ http://purl.uniprot.org/uniprot/Q64347 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CBS 1|||CBS 2|||Causes myotonia.|||Chloride channel protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Pro residues|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3 ^@ http://purl.uniprot.org/annotation/PRO_0000094430 http://togogenome.org/gene/10090:Ier5l ^@ http://purl.uniprot.org/uniprot/Q99J55 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Immediate early response gene 5-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000334657 http://togogenome.org/gene/10090:Lamb2 ^@ http://purl.uniprot.org/uniprot/Q3USI2|||http://purl.uniprot.org/uniprot/Q61292 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||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-2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000017069|||http://purl.uniprot.org/annotation/PRO_5004230174 http://togogenome.org/gene/10090:Ggps1 ^@ http://purl.uniprot.org/uniprot/Q9WTN0 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Site ^@ Binding Site|||Chain|||Modified Residue|||Mutagenesis Site ^@ Geranylgeranyl pyrophosphate synthase|||N-acetylmethionine|||Results in prenatal animals lethality. ^@ http://purl.uniprot.org/annotation/PRO_0000123963 http://togogenome.org/gene/10090:Celf5 ^@ http://purl.uniprot.org/uniprot/D3Z4C5|||http://purl.uniprot.org/uniprot/D3Z4T1|||http://purl.uniprot.org/uniprot/D3Z580|||http://purl.uniprot.org/uniprot/D3Z588 ^@ Domain Extent|||Region ^@ Domain Extent ^@ RRM ^@ http://togogenome.org/gene/10090:Uba1 ^@ http://purl.uniprot.org/uniprot/A0A1S6GWH5|||http://purl.uniprot.org/uniprot/B9EHN0|||http://purl.uniprot.org/uniprot/Q02053 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ 1-1|||1-2|||2 approximate repeats|||Disordered|||Glycyl thioester intermediate|||N-acetylserine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Ubiquitin-activating enzyme E1 C-terminal|||Ubiquitin-like modifier-activating enzyme 1 ^@ http://purl.uniprot.org/annotation/PRO_0000194935 http://togogenome.org/gene/10090:Pcdhb8 ^@ http://purl.uniprot.org/uniprot/Q91XZ2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (Man) serine|||O-linked (Man) threonine|||Protocadherin beta-8 ^@ http://purl.uniprot.org/annotation/PRO_5008429396 http://togogenome.org/gene/10090:Per1 ^@ http://purl.uniprot.org/uniprot/O35973 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolishes homodimerization.|||Abolishes nuclear accumulation.|||Basic residues|||CRY binding domain|||Disordered|||Interaction with BTRC|||LXXLL|||No effect on homodimerization. Abolishes homodimerization; when associated with E-444.|||No effect on nuclear import.|||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|||Reduced phosphorylation. No nuclear entry PER1, CRY1 nor CKSN1E; when associated with A-661.|||Reduced phosphorylation. No nuclear entry of PER1, CRY1 nor CKSN1E; when associated with A-663.|||Reduces homodimerization. Abolishes homodimerization; when associated with E-267.|||Required for phosphorylation by CSNK1E ^@ http://purl.uniprot.org/annotation/PRO_0000162628 http://togogenome.org/gene/10090:Lix1l ^@ http://purl.uniprot.org/uniprot/G3X9C8|||http://purl.uniprot.org/uniprot/Q8BQ89 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||LIX1-like protein|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000232873 http://togogenome.org/gene/10090:Aco2 ^@ http://purl.uniprot.org/uniprot/Q99KI0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Aconitate hydratase, mitochondrial|||Disordered|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000000542 http://togogenome.org/gene/10090:Mgme1 ^@ http://purl.uniprot.org/uniprot/Q9CXC3 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Chain|||Sequence Conflict|||Transit Peptide ^@ Mitochondrial genome maintenance exonuclease 1|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000079440 http://togogenome.org/gene/10090:Tmem120a ^@ http://purl.uniprot.org/uniprot/Q8C1E7 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Helix|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Ion channel TACAN ^@ http://purl.uniprot.org/annotation/PRO_0000309340 http://togogenome.org/gene/10090:Or1r1 ^@ http://purl.uniprot.org/uniprot/Q8VFY0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gm6408 ^@ http://purl.uniprot.org/uniprot/J3QNG1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Sgo2a ^@ http://purl.uniprot.org/uniprot/Q7TSY8 ^@ 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|||Polar residues|||Shugoshin 2 ^@ http://purl.uniprot.org/annotation/PRO_0000055440 http://togogenome.org/gene/10090:Gnai1 ^@ http://purl.uniprot.org/uniprot/B2RSH2 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Region|||Strand|||Turn ^@ G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(i) subunit alpha-1|||N-myristoyl glycine|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000408477 http://togogenome.org/gene/10090:Tbc1d8b ^@ http://purl.uniprot.org/uniprot/A3KGB4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Arginine finger|||Basic and acidic residues|||Disordered|||EF-hand|||GRAM 1|||GRAM 2|||Glutamine finger|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 8B ^@ http://purl.uniprot.org/annotation/PRO_0000337184 http://togogenome.org/gene/10090:Atp1b4 ^@ http://purl.uniprot.org/uniprot/B1APX1|||http://purl.uniprot.org/uniprot/Q99ME6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform B.|||Nuclear|||Perinuclear space|||Protein ATP1B4 ^@ http://purl.uniprot.org/annotation/PRO_0000219123|||http://purl.uniprot.org/annotation/VSP_000352 http://togogenome.org/gene/10090:Unc93a ^@ http://purl.uniprot.org/uniprot/Q710D3 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Protein unc-93 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000190037 http://togogenome.org/gene/10090:Defa38 ^@ http://purl.uniprot.org/uniprot/Q5ERJ0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Alpha-defensin N-terminal|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015097871 http://togogenome.org/gene/10090:Sphkap ^@ http://purl.uniprot.org/uniprot/E9PUC4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ A-kinase anchor 110kDa C-terminal|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Lce1d ^@ http://purl.uniprot.org/uniprot/Q9D731 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Epop ^@ http://purl.uniprot.org/uniprot/Q7TNS8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes interaction with the elongin BC complex.|||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_0000332155 http://togogenome.org/gene/10090:Htra4 ^@ http://purl.uniprot.org/uniprot/A2RT60 ^@ 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|||IGFBP N-terminal|||PDZ|||Serine protease|||Serine protease HTRA4 ^@ http://purl.uniprot.org/annotation/PRO_0000417600 http://togogenome.org/gene/10090:Erlin1 ^@ http://purl.uniprot.org/uniprot/Q91X78 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Erlin-1|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000002785 http://togogenome.org/gene/10090:Pld1 ^@ http://purl.uniprot.org/uniprot/D6RH77|||http://purl.uniprot.org/uniprot/Q3UWT7|||http://purl.uniprot.org/uniprot/Q6NVF2 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ PH|||PLD phosphodiesterase|||PX ^@ http://togogenome.org/gene/10090:Scgb1c1 ^@ http://purl.uniprot.org/uniprot/G5E8B5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015091904 http://togogenome.org/gene/10090:Or51f2 ^@ http://purl.uniprot.org/uniprot/E9Q554 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or2ag20 ^@ http://purl.uniprot.org/uniprot/Q9EPF6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Asb7 ^@ http://purl.uniprot.org/uniprot/C0H5Y0|||http://purl.uniprot.org/uniprot/Q91ZU0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankyrin repeat and SOCS box protein 7|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066937 http://togogenome.org/gene/10090:Garin5b ^@ http://purl.uniprot.org/uniprot/L7N480 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Golgi associated RAB2 interactor protein-like Rab2B-binding ^@ http://togogenome.org/gene/10090:Gm21560 ^@ http://purl.uniprot.org/uniprot/D3Z7A4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Nlgn3 ^@ http://purl.uniprot.org/uniprot/Q8BYM5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||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|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neuroligin-3|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Reduced presynaptic differentiation. ^@ http://purl.uniprot.org/annotation/PRO_0000008646 http://togogenome.org/gene/10090:Fundc2 ^@ http://purl.uniprot.org/uniprot/Q9D6K8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||FUN14 domain-containing protein 2|||Helical|||Mitochondrial intermembrane ^@ http://purl.uniprot.org/annotation/PRO_0000314617 http://togogenome.org/gene/10090:Depdc7 ^@ http://purl.uniprot.org/uniprot/Q91WS7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ DEP|||DEP domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000307739 http://togogenome.org/gene/10090:Calm5 ^@ http://purl.uniprot.org/uniprot/Q6W3E0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ EF-hand ^@ http://togogenome.org/gene/10090:Lin7b ^@ http://purl.uniprot.org/uniprot/O88951 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure ^@ Chain|||Domain Extent|||Helix|||Motif|||Region ^@ Disordered|||Kinase interacting site|||L27|||PDZ|||Protein lin-7 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000189627 http://togogenome.org/gene/10090:Pkd1l2 ^@ http://purl.uniprot.org/uniprot/E9Q4D4|||http://purl.uniprot.org/uniprot/Q7TN88 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||C-type lectin|||Disordered|||GPS|||Helical|||Interaction with GNAS and GNAI1|||N-linked (GlcNAc...) asparagine|||PKD|||PLAT|||Polar residues|||Polycystin-1-like protein 2|||REJ|||SUEL-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000322577|||http://purl.uniprot.org/annotation/PRO_5003243075 http://togogenome.org/gene/10090:Cyp19a1 ^@ http://purl.uniprot.org/uniprot/P28649 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Aromatase|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051957 http://togogenome.org/gene/10090:Atp5b ^@ http://purl.uniprot.org/uniprot/P56480 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ ATP synthase subunit beta, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000002444 http://togogenome.org/gene/10090:Lrrc19 ^@ http://purl.uniprot.org/uniprot/Q8BZT5 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||Leucine-rich repeat-containing protein 19|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000021611 http://togogenome.org/gene/10090:Myom2 ^@ http://purl.uniprot.org/uniprot/O55124|||http://purl.uniprot.org/uniprot/Q14BI5|||http://purl.uniprot.org/uniprot/Q3UQS9 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disordered|||Fibronectin type-III|||Ig-like ^@ http://togogenome.org/gene/10090:Col6a1 ^@ http://purl.uniprot.org/uniprot/B0LAD9|||http://purl.uniprot.org/uniprot/Q04857 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||C-terminal globular domain|||Cell attachment site|||Collagen alpha-1(VI) chain|||Disordered|||N-linked (GlcNAc...) asparagine|||N-terminal globular domain|||Triple-helical region|||VWFA|||VWFA 1|||VWFA 2|||VWFA 3 ^@ http://purl.uniprot.org/annotation/PRO_0000005759 http://togogenome.org/gene/10090:Or51af1 ^@ http://purl.uniprot.org/uniprot/E9Q4X7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ttc7 ^@ http://purl.uniprot.org/uniprot/Q8BGB2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ Phosphoserine|||Phosphothreonine|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||Tetratricopeptide repeat protein 7A ^@ http://purl.uniprot.org/annotation/PRO_0000106386 http://togogenome.org/gene/10090:Ube2ql1 ^@ http://purl.uniprot.org/uniprot/A0PJN4|||http://purl.uniprot.org/uniprot/E9QMD2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Glycyl thioester intermediate|||Polar residues|||UBC core|||Ubiquitin-conjugating enzyme E2Q-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000335812 http://togogenome.org/gene/10090:Abcc5 ^@ http://purl.uniprot.org/uniprot/Q6P8Q2|||http://purl.uniprot.org/uniprot/Q9R1X5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000093364 http://togogenome.org/gene/10090:Slc30a5 ^@ http://purl.uniprot.org/uniprot/Q8R4H9 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||His-rich loop; required for zinc transport|||Lumenal|||Mediates homodimerization with SLC30A6|||N-acetylmethionine|||Proton-coupled zinc antiporter SLC30A5 ^@ http://purl.uniprot.org/annotation/PRO_0000314294 http://togogenome.org/gene/10090:Iapp ^@ http://purl.uniprot.org/uniprot/P12968 ^@ Compositionally Biased Region|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||Islet amyloid polypeptide|||Polar residues|||Tyrosine amide ^@ http://purl.uniprot.org/annotation/PRO_0000004112|||http://purl.uniprot.org/annotation/PRO_0000004113|||http://purl.uniprot.org/annotation/PRO_0000004114 http://togogenome.org/gene/10090:Gm4871 ^@ http://purl.uniprot.org/uniprot/D3Z0W7 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Eif3e ^@ http://purl.uniprot.org/uniprot/P60229|||http://purl.uniprot.org/uniprot/Q3UIG0 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Eukaryotic translation initiation factor 3 subunit E|||N-acetylalanine|||PCI|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Sufficient for interaction with EPAS1|||Sufficient for interaction with MCM7|||Sufficient for interaction with TRIM27 ^@ http://purl.uniprot.org/annotation/PRO_0000123516 http://togogenome.org/gene/10090:Wdr64 ^@ http://purl.uniprot.org/uniprot/E9QM22 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ Disordered|||Polar residues|||WD ^@ http://togogenome.org/gene/10090:Dact2 ^@ http://purl.uniprot.org/uniprot/Q7TN08 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Dapper homolog 2|||Disordered|||Inhibition of Nodal signaling|||PDZ-binding|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000326200 http://togogenome.org/gene/10090:Spred1 ^@ http://purl.uniprot.org/uniprot/Q924S8 ^@ 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|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||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_0000076908|||http://purl.uniprot.org/annotation/VSP_012412|||http://purl.uniprot.org/annotation/VSP_012413 http://togogenome.org/gene/10090:Yju2 ^@ http://purl.uniprot.org/uniprot/Q9D6J3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Splicing factor YJU2 ^@ http://purl.uniprot.org/annotation/PRO_0000234019 http://togogenome.org/gene/10090:Ppp2r3d ^@ http://purl.uniprot.org/uniprot/Q3UPT6|||http://purl.uniprot.org/uniprot/Q4VA48|||http://purl.uniprot.org/uniprot/Q8K1A4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||EF-hand|||PP2A regulatory subunit B"" EF-hand|||Pro residues ^@ http://togogenome.org/gene/10090:Klhl28 ^@ http://purl.uniprot.org/uniprot/Q9CR40 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||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_0000119065|||http://purl.uniprot.org/annotation/VSP_009801 http://togogenome.org/gene/10090:Rttn ^@ http://purl.uniprot.org/uniprot/Q8R4Y8 ^@ 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.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Rotatin ^@ http://purl.uniprot.org/annotation/PRO_0000308613|||http://purl.uniprot.org/annotation/VSP_029032|||http://purl.uniprot.org/annotation/VSP_029033|||http://purl.uniprot.org/annotation/VSP_029034|||http://purl.uniprot.org/annotation/VSP_029035|||http://purl.uniprot.org/annotation/VSP_029036|||http://purl.uniprot.org/annotation/VSP_029037|||http://purl.uniprot.org/annotation/VSP_029038|||http://purl.uniprot.org/annotation/VSP_029039 http://togogenome.org/gene/10090:Or6c216 ^@ http://purl.uniprot.org/uniprot/Q8VG64 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Noa1 ^@ http://purl.uniprot.org/uniprot/Q9JJG9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ CP-type G|||Disordered|||Loss of ability to regulate activity of mitochondrial respiratory chain complexes.|||Nitric oxide-associated protein 1|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000232511 http://togogenome.org/gene/10090:Enox2 ^@ http://purl.uniprot.org/uniprot/Q3UUZ1|||http://purl.uniprot.org/uniprot/Q3UZA6|||http://purl.uniprot.org/uniprot/Q8R0Z2 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Splice Variant ^@ Ecto-NOX disulfide-thiol exchanger 2|||In isoform 2.|||In isoform 3.|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000079276|||http://purl.uniprot.org/annotation/VSP_051830|||http://purl.uniprot.org/annotation/VSP_051831 http://togogenome.org/gene/10090:Espl1 ^@ http://purl.uniprot.org/uniprot/P60330 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Site ^@ Cleavage; by autolysis|||Disordered|||Peptidase C50|||Phosphoserine|||Separin ^@ http://purl.uniprot.org/annotation/PRO_0000205901 http://togogenome.org/gene/10090:Papolb ^@ http://purl.uniprot.org/uniprot/A1L349|||http://purl.uniprot.org/uniprot/Q9WVP6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000051623 http://togogenome.org/gene/10090:Pdlim7 ^@ http://purl.uniprot.org/uniprot/Q3TJD7|||http://purl.uniprot.org/uniprot/Q8BVJ7 ^@ 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|||Disordered|||In isoform 2.|||In isoform 3.|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||PDZ|||PDZ and LIM domain protein 7|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000075882|||http://purl.uniprot.org/annotation/VSP_016517|||http://purl.uniprot.org/annotation/VSP_016518|||http://purl.uniprot.org/annotation/VSP_016519|||http://purl.uniprot.org/annotation/VSP_016520|||http://purl.uniprot.org/annotation/VSP_016521 http://togogenome.org/gene/10090:Mab21l2 ^@ http://purl.uniprot.org/uniprot/Q8BPP1 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Protein mab-21-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000312788 http://togogenome.org/gene/10090:Mob3b ^@ http://purl.uniprot.org/uniprot/Q8VE04 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ MOB kinase activator 3B ^@ http://purl.uniprot.org/annotation/PRO_0000193573 http://togogenome.org/gene/10090:Or1e22 ^@ http://purl.uniprot.org/uniprot/Q5SSP0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp184 ^@ http://purl.uniprot.org/uniprot/Q7TSH9 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||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 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 184 ^@ http://purl.uniprot.org/annotation/PRO_0000348469 http://togogenome.org/gene/10090:Cript ^@ http://purl.uniprot.org/uniprot/O70333 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Cysteine-rich PDZ-binding protein|||Disordered|||PDZ3-binding|||Polar residues|||Sufficient for interaction with DLG4 ^@ http://purl.uniprot.org/annotation/PRO_0000314564 http://togogenome.org/gene/10090:Naip5 ^@ http://purl.uniprot.org/uniprot/Q9R016 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ Abolishes production of IL1B in response to bacterial flagellin.|||BIR 1|||BIR 2|||BIR 3|||Baculoviral IAP repeat-containing protein 1e|||Mildly reduced interaction with flagellin.|||NACHT|||Nearly abolishes interaction with flagellin.|||No effect on production of IL1B in response to bacterial flagellin.|||Reduced interaction with flagellin.|||Strongly reduced interaction with flagellin.|||Strongly reduces production of IL1B in response to bacterial flagellin.|||Strongly reduces production of IL1B in response to bacterial flagellin; then associated with F-15.|||Strongly reduces production of IL1B in response to bacterial flagellin; then associated with I-11. ^@ http://purl.uniprot.org/annotation/PRO_0000122344 http://togogenome.org/gene/10090:S100a1 ^@ http://purl.uniprot.org/uniprot/P56565|||http://purl.uniprot.org/uniprot/Q91V77 ^@ 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 ^@ EF-hand|||EF-hand 1|||EF-hand 2|||Protein S100-A1|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000143962 http://togogenome.org/gene/10090:Clec4b1 ^@ http://purl.uniprot.org/uniprot/Q7TS58|||http://purl.uniprot.org/uniprot/Q9D8Q7 ^@ Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Disulfide Bond|||Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Spata31d1d ^@ http://purl.uniprot.org/uniprot/E9Q5W2|||http://purl.uniprot.org/uniprot/Q8C5W2 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||SPATA31|||SPATA31F3-like ^@ http://togogenome.org/gene/10090:9830107B12Rik ^@ http://purl.uniprot.org/uniprot/A0A3B2W4G3|||http://purl.uniprot.org/uniprot/A9Q7H1|||http://purl.uniprot.org/uniprot/D3Z5D6|||http://purl.uniprot.org/uniprot/Q3UV63 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like|||Immunoglobulin V-set|||Immunoglobulin V-set domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5004230226|||http://purl.uniprot.org/annotation/PRO_5010104456|||http://purl.uniprot.org/annotation/PRO_5015088526|||http://purl.uniprot.org/annotation/PRO_5017185105 http://togogenome.org/gene/10090:Swt1 ^@ http://purl.uniprot.org/uniprot/Q9DBQ9 ^@ 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.|||PINc|||Polar residues|||Transcriptional protein SWT1 ^@ http://purl.uniprot.org/annotation/PRO_0000251185|||http://purl.uniprot.org/annotation/VSP_020734|||http://purl.uniprot.org/annotation/VSP_020735|||http://purl.uniprot.org/annotation/VSP_020736 http://togogenome.org/gene/10090:Mpped1 ^@ http://purl.uniprot.org/uniprot/Q91ZG2 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Metallophosphoesterase domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000053404 http://togogenome.org/gene/10090:Tuft1 ^@ http://purl.uniprot.org/uniprot/O08970|||http://purl.uniprot.org/uniprot/Q3TAP8|||http://purl.uniprot.org/uniprot/Q3V1F5 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Splice Variant ^@ Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Tuftelin ^@ http://purl.uniprot.org/annotation/PRO_0000183187|||http://purl.uniprot.org/annotation/VSP_006687|||http://purl.uniprot.org/annotation/VSP_006688 http://togogenome.org/gene/10090:Adamts1 ^@ http://purl.uniprot.org/uniprot/P97857|||http://purl.uniprot.org/uniprot/Q3TQF7|||http://purl.uniprot.org/uniprot/Q3TTE6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ A disintegrin and metalloproteinase with thrombospondin motifs 1|||Cysteine switch|||Disintegrin|||Disordered|||Loss of activity.|||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_0000029152|||http://purl.uniprot.org/annotation/PRO_0000029153 http://togogenome.org/gene/10090:Serbp1 ^@ http://purl.uniprot.org/uniprot/Q3UEI6|||http://purl.uniprot.org/uniprot/Q3UMP4|||http://purl.uniprot.org/uniprot/Q9CY58 ^@ 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 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 3.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SERPINE1 mRNA-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000058183|||http://purl.uniprot.org/annotation/VSP_011632|||http://purl.uniprot.org/annotation/VSP_011633|||http://purl.uniprot.org/annotation/VSP_011634|||http://purl.uniprot.org/annotation/VSP_011635 http://togogenome.org/gene/10090:Orai2 ^@ http://purl.uniprot.org/uniprot/A5CVE1|||http://purl.uniprot.org/uniprot/Q14BR6|||http://purl.uniprot.org/uniprot/Q8BH10 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Protein orai-2 ^@ http://purl.uniprot.org/annotation/PRO_0000234392 http://togogenome.org/gene/10090:Gm5460 ^@ http://purl.uniprot.org/uniprot/A0A2I3BRZ9|||http://purl.uniprot.org/uniprot/Q3UQ97 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Pro residues|||VWFA ^@ http://togogenome.org/gene/10090:Prss3b ^@ http://purl.uniprot.org/uniprot/Q9CPN9|||http://purl.uniprot.org/uniprot/Q9D7Y7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1|||Peptidase S1 domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5012904024|||http://purl.uniprot.org/annotation/PRO_5015099658 http://togogenome.org/gene/10090:Wdr93 ^@ http://purl.uniprot.org/uniprot/Q402B2 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ Disordered|||WD|||WD repeat-containing protein 93 ^@ http://purl.uniprot.org/annotation/PRO_0000319604 http://togogenome.org/gene/10090:Erbb4 ^@ http://purl.uniprot.org/uniprot/Q61527 ^@ Active Site|||Binding Site|||Chain|||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 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||ERBB4 intracellular domain|||Extracellular|||In isoform JM-ACYT-2.|||In isoform JM-BCYT-2.|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||PDZ-binding|||PPxY motif 2|||PPxy motif 1|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Receptor tyrosine-protein kinase erbB-4 ^@ http://purl.uniprot.org/annotation/PRO_0000270146|||http://purl.uniprot.org/annotation/PRO_0000396798|||http://purl.uniprot.org/annotation/VSP_002896|||http://purl.uniprot.org/annotation/VSP_042131 http://togogenome.org/gene/10090:Sp2 ^@ http://purl.uniprot.org/uniprot/Q8BNQ4|||http://purl.uniprot.org/uniprot/Q8C5J0|||http://purl.uniprot.org/uniprot/Q9D2H6 ^@ 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|||C2H2-type|||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_0000269192|||http://purl.uniprot.org/annotation/VSP_022022 http://togogenome.org/gene/10090:Ahnak ^@ http://purl.uniprot.org/uniprot/E9Q616|||http://purl.uniprot.org/uniprot/G5E8K8|||http://purl.uniprot.org/uniprot/Q8BRB8|||http://purl.uniprot.org/uniprot/Q8R2L7 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||PDZ|||Polar residues ^@ http://togogenome.org/gene/10090:Hormad2 ^@ http://purl.uniprot.org/uniprot/Q5SQP1 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Splice Variant ^@ HORMA|||HORMA domain-containing protein 2|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000284670|||http://purl.uniprot.org/annotation/VSP_024605|||http://purl.uniprot.org/annotation/VSP_024606 http://togogenome.org/gene/10090:Spata2l ^@ http://purl.uniprot.org/uniprot/B2RTE8|||http://purl.uniprot.org/uniprot/Q8BNN1 ^@ 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.|||Phosphoserine|||Spermatogenesis-associated protein 2-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000297671|||http://purl.uniprot.org/annotation/VSP_027334|||http://purl.uniprot.org/annotation/VSP_027335 http://togogenome.org/gene/10090:Syt11 ^@ http://purl.uniprot.org/uniprot/Q3TPH5|||http://purl.uniprot.org/uniprot/Q9R0N3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C2|||C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||Phosphoserine|||Polar residues|||Synaptotagmin-11|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000183970 http://togogenome.org/gene/10090:Pop5 ^@ http://purl.uniprot.org/uniprot/Q9DB28 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Ribonuclease P/MRP protein subunit POP5 ^@ http://purl.uniprot.org/annotation/PRO_0000239008 http://togogenome.org/gene/10090:Rad21 ^@ http://purl.uniprot.org/uniprot/Q3TG35|||http://purl.uniprot.org/uniprot/Q61550 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ 64-kDa C-terminal product|||Acidic residues|||Cleavage; by ESPL1|||Cleavage; by caspase-3 or caspase-7|||Disordered|||Double-strand-break repair protein rad21 homolog|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with NIPBL|||Interaction with STAG1|||Interaction with WAPL and PDS5B|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rad21/Rec8-like protein C-terminal eukaryotic|||Rad21/Rec8-like protein N-terminal|||Required for interaction with SMARCA5 ^@ http://purl.uniprot.org/annotation/PRO_0000097873|||http://purl.uniprot.org/annotation/PRO_0000446318 http://togogenome.org/gene/10090:Or5k8 ^@ http://purl.uniprot.org/uniprot/A0A140T8K4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Myl12a ^@ http://purl.uniprot.org/uniprot/Q6ZWQ9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||EF-hand ^@ http://togogenome.org/gene/10090:Ust ^@ http://purl.uniprot.org/uniprot/Q3TRA2|||http://purl.uniprot.org/uniprot/Q8BUB6 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Uronyl 2-sulfotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000207682 http://togogenome.org/gene/10090:Mrpl34 ^@ http://purl.uniprot.org/uniprot/Q99N91 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ Large ribosomal subunit protein bL34m|||Mitochondrion|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000030521 http://togogenome.org/gene/10090:1700067K01Rik ^@ http://purl.uniprot.org/uniprot/A0A6E0D3Q4|||http://purl.uniprot.org/uniprot/Q8CF25 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Pro residues|||UPF0575 protein C19orf67 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000332938 http://togogenome.org/gene/10090:Tmed4 ^@ http://purl.uniprot.org/uniprot/Q8R1V4 ^@ Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Motif|||Signal Peptide|||Topological Domain|||Transmembrane ^@ COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||GOLD|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Transmembrane emp24 domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000010388 http://togogenome.org/gene/10090:Ephb2 ^@ http://purl.uniprot.org/uniprot/P54763 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||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 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cleavage; by a metalloproteinase|||Cleavage; by gamma-secretase/PS1|||Cytoplasmic|||Eph LBD|||EphB2/CTF1|||EphB2/CTF2|||Ephrin type-B receptor 2|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||No loss of interaction with SPSB4; when associated with F-596.|||No loss of interaction with SPSB4; when associated with F-602.|||PDZ-binding|||Protein kinase|||Proton acceptor|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000016828|||http://purl.uniprot.org/annotation/PRO_0000445963|||http://purl.uniprot.org/annotation/PRO_0000445964|||http://purl.uniprot.org/annotation/VSP_057932|||http://purl.uniprot.org/annotation/VSP_057933 http://togogenome.org/gene/10090:C130050O18Rik ^@ http://purl.uniprot.org/uniprot/Q497Y9|||http://purl.uniprot.org/uniprot/Q8C860 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Tfap4 ^@ http://purl.uniprot.org/uniprot/Q9JIZ5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rcbtb1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J025|||http://purl.uniprot.org/uniprot/Q6NXM2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ BTB|||BTB 1|||BTB 2|||RCC1|||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_0000206643 http://togogenome.org/gene/10090:Pdcd7 ^@ http://purl.uniprot.org/uniprot/Q3U2X6 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Anks3 ^@ http://purl.uniprot.org/uniprot/Q9CZK6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ 3-hydroxyasparagine|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SAM domain-containing protein 3|||Disordered|||Interaction with NEK7|||No effect on its interaction with NEK7.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000230778 http://togogenome.org/gene/10090:Vmn1r35 ^@ http://purl.uniprot.org/uniprot/Q8R2E2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp850 ^@ http://purl.uniprot.org/uniprot/J3QPC5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Gapdhs ^@ http://purl.uniprot.org/uniprot/A0A0R4J0X7|||http://purl.uniprot.org/uniprot/Q64467|||http://purl.uniprot.org/uniprot/S4R2G5 ^@ Active Site|||Binding 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|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ Activates thiol group during catalysis|||Disordered|||Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding|||Glyceraldehyde-3-phosphate dehydrogenase, testis-specific|||Nucleophile|||Phosphoserine|||Pro residues|||Testis-specific N-terminal extension ^@ http://purl.uniprot.org/annotation/PRO_0000145504 http://togogenome.org/gene/10090:St14 ^@ http://purl.uniprot.org/uniprot/P56677|||http://purl.uniprot.org/uniprot/Q543E3 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Topological Domain|||Transmembrane ^@ CUB|||CUB 1|||CUB 2|||Charge relay system|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||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|||Phosphoserine|||SEA|||Suppressor of tumorigenicity 14 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000088713 http://togogenome.org/gene/10090:Chmp3 ^@ http://purl.uniprot.org/uniprot/Q9CQ10 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ Acidic residues|||Charged multivesicular body protein 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Important for autoinhibitory function|||Interaction with STAMBP|||Interaction with VPS4A|||Intramolecular interaction with C-terminus|||Intramolecular interaction with N-terminus|||MIT-interacting motif|||N-myristoyl glycine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000211481 http://togogenome.org/gene/10090:Or4f60 ^@ http://purl.uniprot.org/uniprot/Q7TQW8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or2d3b ^@ http://purl.uniprot.org/uniprot/A0A0R4J8U2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kcnab1 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPA4|||http://purl.uniprot.org/uniprot/P63143|||http://purl.uniprot.org/uniprot/Q3U6C5 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ NADP-dependent oxidoreductase|||Proton donor/acceptor|||Voltage-gated potassium channel subunit beta-1 ^@ http://purl.uniprot.org/annotation/PRO_0000148740 http://togogenome.org/gene/10090:Stk3 ^@ http://purl.uniprot.org/uniprot/Q9JI10 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site|||Splice Variant ^@ Acidic residues|||Cleavage; by caspase-3|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||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_0000086690|||http://purl.uniprot.org/annotation/PRO_0000413715|||http://purl.uniprot.org/annotation/PRO_0000413716|||http://purl.uniprot.org/annotation/VSP_020047 http://togogenome.org/gene/10090:Rbpjl ^@ http://purl.uniprot.org/uniprot/O08674|||http://purl.uniprot.org/uniprot/Q3V2I2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Beta-trefoil DNA-binding|||DNA-binding|||Disordered|||IPT/TIG|||Polar residues|||RBP-J/Cbf11/Cbf12 DNA binding|||Recombining binding protein suppressor of hairless-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000208571 http://togogenome.org/gene/10090:Usp37 ^@ http://purl.uniprot.org/uniprot/A0A0R4J2D0|||http://purl.uniprot.org/uniprot/Q8C0R0 ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||D-box 1|||D-box 2|||D-box 3|||Disordered|||In isoform 2.|||KEN box 1|||KEN box 2|||KEN box 3|||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_0000259610|||http://purl.uniprot.org/annotation/VSP_052196 http://togogenome.org/gene/10090:Dnajc9 ^@ http://purl.uniprot.org/uniprot/Q91WN1 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ DnaJ homolog subfamily C member 9|||J|||Phosphoserine|||Required for histone binding ^@ http://purl.uniprot.org/annotation/PRO_0000071064 http://togogenome.org/gene/10090:Cib1 ^@ http://purl.uniprot.org/uniprot/A0A0U1RPF3|||http://purl.uniprot.org/uniprot/Q8C2K4|||http://purl.uniprot.org/uniprot/Q9Z0F4 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding ^@ Calcium and integrin-binding protein 1|||EF-hand|||EF-hand 1|||EF-hand 2|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073532 http://togogenome.org/gene/10090:2610042L04Rik ^@ http://purl.uniprot.org/uniprot/Q9D073 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Slain2 ^@ http://purl.uniprot.org/uniprot/Q8CI08 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Disordered|||Important for interaction with CLIP1|||In isoform 2.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||SLAIN motif-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000316967|||http://purl.uniprot.org/annotation/VSP_030834 http://togogenome.org/gene/10090:Doc2g ^@ http://purl.uniprot.org/uniprot/A0A0R4J053|||http://purl.uniprot.org/uniprot/Q9ESN1 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ C2|||C2 1|||C2 2|||Double C2-like domain-containing protein gamma ^@ http://purl.uniprot.org/annotation/PRO_0000079971 http://togogenome.org/gene/10090:Alkal1 ^@ http://purl.uniprot.org/uniprot/J3QPP8 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ ALK and LTK ligand 1 ^@ http://purl.uniprot.org/annotation/PRO_5003776676 http://togogenome.org/gene/10090:Pla2g12a ^@ http://purl.uniprot.org/uniprot/Q9EPR2 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Group XIIA secretory phospholipase A2|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000022771|||http://purl.uniprot.org/annotation/VSP_004509 http://togogenome.org/gene/10090:Tmem220 ^@ http://purl.uniprot.org/uniprot/Q8BP07 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||In isoform 3.|||Transmembrane protein 220 ^@ http://purl.uniprot.org/annotation/PRO_0000319425|||http://purl.uniprot.org/annotation/VSP_031478|||http://purl.uniprot.org/annotation/VSP_031479|||http://purl.uniprot.org/annotation/VSP_031480 http://togogenome.org/gene/10090:Gpatch2 ^@ http://purl.uniprot.org/uniprot/Q7TQC7 ^@ 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.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087567|||http://purl.uniprot.org/annotation/VSP_010529|||http://purl.uniprot.org/annotation/VSP_010530 http://togogenome.org/gene/10090:Rpl4 ^@ http://purl.uniprot.org/uniprot/Q564E8|||http://purl.uniprot.org/uniprot/Q9D8E6 ^@ 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|||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|||Large ribosomal subunit protein uL4 C-terminal|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000129351 http://togogenome.org/gene/10090:Zfp141 ^@ http://purl.uniprot.org/uniprot/G3UY09 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dcp1b ^@ http://purl.uniprot.org/uniprot/B9EIX0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||mRNA-decapping enzyme C-terminal ^@ http://togogenome.org/gene/10090:Gpd1 ^@ http://purl.uniprot.org/uniprot/P13707 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000138080 http://togogenome.org/gene/10090:Anxa4 ^@ http://purl.uniprot.org/uniprot/P97429 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A4|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000067483 http://togogenome.org/gene/10090:Lmbrd1 ^@ http://purl.uniprot.org/uniprot/Q8K0B2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis 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|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||Lysosomal cobalamin transport escort protein LMBD1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Significantly reduced interaction with adapter protein complex 2 and disruption of its function in clathrin-mediated endocytosis of INSR.|||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_0000260517|||http://purl.uniprot.org/annotation/VSP_021631|||http://purl.uniprot.org/annotation/VSP_021632|||http://purl.uniprot.org/annotation/VSP_021633 http://togogenome.org/gene/10090:Rnmt ^@ http://purl.uniprot.org/uniprot/Q9D0L8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Nuclear localization signal|||Phosphoserine|||mRNA cap 0 methyltransferase|||mRNA cap binding|||mRNA cap guanine-N7 methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000248323|||http://purl.uniprot.org/annotation/VSP_020242|||http://purl.uniprot.org/annotation/VSP_020243 http://togogenome.org/gene/10090:Dnase1l3 ^@ http://purl.uniprot.org/uniprot/O55070 ^@ Active Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Motif|||Region|||Sequence Variant|||Signal Peptide ^@ Bipartite nuclear localization signal|||Deoxyribonuclease gamma|||Essential for enzymatic activity|||In strain: DBA/2, NZB and NZW, in vitro decreases nuclease activity against free DNA by approximately twofold and decreases activity to establish a barrier to liposomal gene transfection by eightfold.|||Not required for free DNA-nuclease activity but required for activity towards liposome-coated DNA|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000007289 http://togogenome.org/gene/10090:Il6 ^@ http://purl.uniprot.org/uniprot/A0A0G2JGF4|||http://purl.uniprot.org/uniprot/A2RTD1|||http://purl.uniprot.org/uniprot/P08505 ^@ Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Strand|||Turn ^@ Interleukin-6 ^@ http://purl.uniprot.org/annotation/PRO_0000015588|||http://purl.uniprot.org/annotation/PRO_5002546142|||http://purl.uniprot.org/annotation/PRO_5014296817 http://togogenome.org/gene/10090:Tnxb ^@ http://purl.uniprot.org/uniprot/A0A5F8MPH8|||http://purl.uniprot.org/uniprot/E9Q2T3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Fibrinogen C-terminal|||Fibronectin type-III|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5003244385|||http://purl.uniprot.org/annotation/PRO_5023821762 http://togogenome.org/gene/10090:Rab6b ^@ http://purl.uniprot.org/uniprot/P61294 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif ^@ Cysteine methyl ester|||Effector region|||Ras-related protein Rab-6B|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121116 http://togogenome.org/gene/10090:Or8g33 ^@ http://purl.uniprot.org/uniprot/Q8VFD7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Usp48 ^@ http://purl.uniprot.org/uniprot/A2ALR9|||http://purl.uniprot.org/uniprot/Q3V0C5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||DUSP|||DUSP 1|||DUSP 2|||DUSP 3|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3 and isoform 5.|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 48|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000249524|||http://purl.uniprot.org/annotation/VSP_020482|||http://purl.uniprot.org/annotation/VSP_020483|||http://purl.uniprot.org/annotation/VSP_020484|||http://purl.uniprot.org/annotation/VSP_020485 http://togogenome.org/gene/10090:Cop1 ^@ http://purl.uniprot.org/uniprot/Q9R1A8 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Site|||Zinc Finger ^@ Chain|||Coiled-Coil|||Motif|||Mutagenesis Site|||Region|||Repeat|||Site|||Zinc Finger ^@ Abolishes nuclear export.|||Abolishes nuclear localization.|||Abolishes the nuclear speckle localization but not the nuclear localization.|||Disordered|||Does not affect the subcellular localization.|||E3 ubiquitin-protein ligase COP1|||Interaction with TRIB1|||Nuclear export signal|||Nuclear localization signal 1|||Nuclear localization signal 2|||RING-type|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000055880 http://togogenome.org/gene/10090:Slc11a2 ^@ http://purl.uniprot.org/uniprot/P49282 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 1 and isoform 3.|||In isoform 3 and isoform 4.|||In microcytic anemia.|||N-linked (GlcNAc...) asparagine|||Natural resistance-associated macrophage protein 2|||Phosphoserine|||Polar residues|||Required for early endosome targeting ^@ http://purl.uniprot.org/annotation/PRO_0000212595|||http://purl.uniprot.org/annotation/VSP_003596|||http://purl.uniprot.org/annotation/VSP_038145 http://togogenome.org/gene/10090:Foxj2 ^@ http://purl.uniprot.org/uniprot/Q9ES18 ^@ 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|||Fork-head|||Forkhead box protein J2|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000091854 http://togogenome.org/gene/10090:Tmem207 ^@ http://purl.uniprot.org/uniprot/P86045 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||Transmembrane protein 207 ^@ http://purl.uniprot.org/annotation/PRO_0000355136 http://togogenome.org/gene/10090:Klk1b8 ^@ http://purl.uniprot.org/uniprot/P07628 ^@ 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|||Kallikrein 1-related peptidase b8|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027977|||http://purl.uniprot.org/annotation/PRO_0000027978 http://togogenome.org/gene/10090:A430033K04Rik ^@ http://purl.uniprot.org/uniprot/E9Q8G5|||http://purl.uniprot.org/uniprot/Q3V466|||http://purl.uniprot.org/uniprot/Q7TPL8 ^@ 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 OBI1 ^@ http://purl.uniprot.org/annotation/PRO_0000454385 http://togogenome.org/gene/10090:Gpd2 ^@ http://purl.uniprot.org/uniprot/Q64521 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ EF-hand 1|||EF-hand 2|||Glycerol-3-phosphate dehydrogenase, mitochondrial|||Mitochondrion|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000010430 http://togogenome.org/gene/10090:Dmtf1 ^@ http://purl.uniprot.org/uniprot/Q8CE22 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||DNA Binding|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abrogates DNA-binding.|||Cyclin-D-binding Myb-like transcription factor 1|||Disordered|||H-T-H motif|||HTH myb-type|||In isoform 2 and isoform 3.|||In isoform 3.|||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_0000323730|||http://purl.uniprot.org/annotation/VSP_032094|||http://purl.uniprot.org/annotation/VSP_032095|||http://purl.uniprot.org/annotation/VSP_032096|||http://purl.uniprot.org/annotation/VSP_032097|||http://purl.uniprot.org/annotation/VSP_032098|||http://purl.uniprot.org/annotation/VSP_032099|||http://purl.uniprot.org/annotation/VSP_032100|||http://purl.uniprot.org/annotation/VSP_032101 http://togogenome.org/gene/10090:Gm11487 ^@ http://purl.uniprot.org/uniprot/Q5RIS0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Renbp ^@ http://purl.uniprot.org/uniprot/P82343 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Important for enzyme activity|||In isoform 2.|||Leucine-zipper|||N-acylglucosamine 2-epimerase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000208950|||http://purl.uniprot.org/annotation/VSP_039024 http://togogenome.org/gene/10090:Ndufv2 ^@ http://purl.uniprot.org/uniprot/Q9D6J6 ^@ Binding Site|||Chain|||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|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Disordered|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial|||Phosphotyrosine; by SRC ^@ http://purl.uniprot.org/annotation/PRO_0000020004|||http://purl.uniprot.org/annotation/VSP_025017 http://togogenome.org/gene/10090:Wfdc5 ^@ http://purl.uniprot.org/uniprot/Q4KXB6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ WAP ^@ http://purl.uniprot.org/annotation/PRO_5015097625 http://togogenome.org/gene/10090:Zfp946 ^@ http://purl.uniprot.org/uniprot/F6VWU8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Gchfr ^@ http://purl.uniprot.org/uniprot/P99025 ^@ Chain|||Initiator Methionine|||Molecule Processing ^@ Chain|||Initiator Methionine ^@ GTP cyclohydrolase 1 feedback regulatory protein|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000189676 http://togogenome.org/gene/10090:Tango2 ^@ http://purl.uniprot.org/uniprot/P54797 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Transport and Golgi organization 2 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000072396 http://togogenome.org/gene/10090:Clns1a ^@ http://purl.uniprot.org/uniprot/Q923F1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Aste1 ^@ http://purl.uniprot.org/uniprot/Q8BIR2 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Protein asteroid homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000310459|||http://purl.uniprot.org/annotation/VSP_029285|||http://purl.uniprot.org/annotation/VSP_029286 http://togogenome.org/gene/10090:Gbp2 ^@ http://purl.uniprot.org/uniprot/Q9Z0E6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict ^@ Cysteine methyl ester|||GB1/RHD3-type G|||GTPase domain (Globular)|||Guanylate-binding protein 2|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000190966|||http://purl.uniprot.org/annotation/PRO_0000370783 http://togogenome.org/gene/10090:Slfn1 ^@ http://purl.uniprot.org/uniprot/Q9Z0I7 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Schlafen family member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000457108 http://togogenome.org/gene/10090:Arhgdig ^@ http://purl.uniprot.org/uniprot/Q62160 ^@ Chain|||Molecule Processing ^@ Chain ^@ Rho GDP-dissociation inhibitor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000219019 http://togogenome.org/gene/10090:Kcnj5 ^@ http://purl.uniprot.org/uniprot/P48545 ^@ Chain|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||G protein-activated inward rectifier potassium channel 4|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||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_0000154935 http://togogenome.org/gene/10090:Fam228b ^@ http://purl.uniprot.org/uniprot/Q497Q6 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||Protein FAM228B ^@ http://purl.uniprot.org/annotation/PRO_0000348450|||http://purl.uniprot.org/annotation/VSP_035165|||http://purl.uniprot.org/annotation/VSP_035166 http://togogenome.org/gene/10090:Ccdc167 ^@ http://purl.uniprot.org/uniprot/Q9D162 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Splice Variant|||Transmembrane ^@ Coiled-coil domain-containing protein 167|||Helical|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000308551|||http://purl.uniprot.org/annotation/VSP_028985|||http://purl.uniprot.org/annotation/VSP_028986 http://togogenome.org/gene/10090:Trappc13 ^@ http://purl.uniprot.org/uniprot/Q3TIR1 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2 and isoform 3.|||In isoform 3.|||Trafficking protein particle complex subunit 13 ^@ http://purl.uniprot.org/annotation/PRO_0000321548|||http://purl.uniprot.org/annotation/VSP_031799|||http://purl.uniprot.org/annotation/VSP_031800 http://togogenome.org/gene/10090:Dmc1 ^@ http://purl.uniprot.org/uniprot/Q14AN8|||http://purl.uniprot.org/uniprot/Q61880|||http://purl.uniprot.org/uniprot/Q8C610 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Meiotic recombination protein DMC1/LIM15 homolog|||RecA family profile 1|||RecA family profile 2 ^@ http://purl.uniprot.org/annotation/PRO_0000122919 http://togogenome.org/gene/10090:Lao1 ^@ http://purl.uniprot.org/uniprot/B1ARV3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Amine oxidase ^@ http://purl.uniprot.org/annotation/PRO_5015087045 http://togogenome.org/gene/10090:Magi1 ^@ http://purl.uniprot.org/uniprot/A0A0N4SUZ0|||http://purl.uniprot.org/uniprot/A0A0N4SWH0|||http://purl.uniprot.org/uniprot/A0A0R4J0S6|||http://purl.uniprot.org/uniprot/E9PZ12|||http://purl.uniprot.org/uniprot/Q3TQ86|||http://purl.uniprot.org/uniprot/Q4H4B4|||http://purl.uniprot.org/uniprot/Q4H4B5|||http://purl.uniprot.org/uniprot/Q6RHR9|||http://purl.uniprot.org/uniprot/Q8CCP7 ^@ 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|||Site|||Splice Variant|||Strand ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Basic and acidic residues|||Disordered|||Guanylate kinase-like|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Interaction with FCHSD2|||Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||Phosphoserine|||Polar residues|||WW|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000094590|||http://purl.uniprot.org/annotation/VSP_011673|||http://purl.uniprot.org/annotation/VSP_011674|||http://purl.uniprot.org/annotation/VSP_011675|||http://purl.uniprot.org/annotation/VSP_011676|||http://purl.uniprot.org/annotation/VSP_011677|||http://purl.uniprot.org/annotation/VSP_011678|||http://purl.uniprot.org/annotation/VSP_011679 http://togogenome.org/gene/10090:Gadd45g ^@ http://purl.uniprot.org/uniprot/Q9R0S0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ribosomal protein eL8/eL30/eS12/Gadd45 ^@ http://togogenome.org/gene/10090:Apbb2 ^@ http://purl.uniprot.org/uniprot/E9PWH3|||http://purl.uniprot.org/uniprot/Q3T9N0|||http://purl.uniprot.org/uniprot/Q3TDW6|||http://purl.uniprot.org/uniprot/Q3TIZ5|||http://purl.uniprot.org/uniprot/Q3U674|||http://purl.uniprot.org/uniprot/Q8BSK4|||http://purl.uniprot.org/uniprot/Q9DBR4 ^@ 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 ^@ Amyloid beta precursor protein binding family B member 2|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||PID|||PID 1|||PID 2|||Phosphoserine|||Polar residues|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000076053|||http://purl.uniprot.org/annotation/VSP_011661|||http://purl.uniprot.org/annotation/VSP_011662 http://togogenome.org/gene/10090:Cubn ^@ http://purl.uniprot.org/uniprot/Q9JLB4 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ 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|||Interaction with AMN|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000046074|||http://purl.uniprot.org/annotation/PRO_0000046075 http://togogenome.org/gene/10090:Acly ^@ http://purl.uniprot.org/uniprot/Q3V117|||http://purl.uniprot.org/uniprot/Q91V92 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ ATP-citrate synthase|||ATP-grasp|||Abolished ubiquitination by the BCR(KLHL25)complex, leading to imapired differentiation of inducible regulatory T (iTreg) cells; when associated with R-530 and R-536.|||Abolished ubiquitination by the BCR(KLHL25)complex, leading to imapired differentiation of inducible regulatory T (iTreg) cells; when associated with R-530 and R-544.|||Abolished ubiquitination by the BCR(KLHL25)complex, leading to imapired differentiation of inducible regulatory T (iTreg) cells; when associated with R-536 and R-544.|||CoA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Tele-phosphohistidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000102782 http://togogenome.org/gene/10090:Slc7a7 ^@ http://purl.uniprot.org/uniprot/Q9Z1K8 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Y+L amino acid transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000304935 http://togogenome.org/gene/10090:Srfbp1 ^@ http://purl.uniprot.org/uniprot/Q9CZ91 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Serum response factor-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000320007 http://togogenome.org/gene/10090:Mt1 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLN7|||http://purl.uniprot.org/uniprot/P02802 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Alpha|||Beta|||Metallothionein-1|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000197206 http://togogenome.org/gene/10090:Trak2 ^@ http://purl.uniprot.org/uniprot/G3UYW9|||http://purl.uniprot.org/uniprot/Q6P9N8|||http://purl.uniprot.org/uniprot/Q8BKA2|||http://purl.uniprot.org/uniprot/Q8BZ57 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||HAP1 N-terminal|||Polar residues|||Pro residues|||Trafficking kinesin-binding protein C-terminal ^@ http://togogenome.org/gene/10090:H2al1c ^@ http://purl.uniprot.org/uniprot/Q5M8Q2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Histone H2A-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000440627 http://togogenome.org/gene/10090:E130311K13Rik ^@ http://purl.uniprot.org/uniprot/Q8BN57 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||N-acetylalanine|||Protein C3orf33 homolog|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000254578 http://togogenome.org/gene/10090:Pdgfa ^@ http://purl.uniprot.org/uniprot/G5E891|||http://purl.uniprot.org/uniprot/P20033|||http://purl.uniprot.org/uniprot/Q99L56 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform Short.|||Interchain|||N-linked (GlcNAc...) asparagine|||Platelet-derived growth factor (PDGF) family profile|||Platelet-derived growth factor subunit A|||Receptor binding site|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000023358|||http://purl.uniprot.org/annotation/PRO_0000023359|||http://purl.uniprot.org/annotation/PRO_5015091902|||http://purl.uniprot.org/annotation/PRO_5015099626|||http://purl.uniprot.org/annotation/VSP_004604|||http://purl.uniprot.org/annotation/VSP_004605 http://togogenome.org/gene/10090:Or14j2 ^@ http://purl.uniprot.org/uniprot/Q8VEU4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:5031410I06Rik ^@ http://purl.uniprot.org/uniprot/E9Q4E0 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Dgkb ^@ http://purl.uniprot.org/uniprot/Q6NS52 ^@ 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 ^@ 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|||Polar residues|||Required for association with membranes and function in neurite spine formation ^@ http://purl.uniprot.org/annotation/PRO_0000264623|||http://purl.uniprot.org/annotation/VSP_021900 http://togogenome.org/gene/10090:Zfp639 ^@ http://purl.uniprot.org/uniprot/Q99KZ6 ^@ 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 ^@ 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)|||Interaction with CTNNA2|||Phosphoserine|||Zinc finger protein 639 ^@ http://purl.uniprot.org/annotation/PRO_0000383573 http://togogenome.org/gene/10090:Dhx58 ^@ http://purl.uniprot.org/uniprot/Q99J87 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ ATP-dependent RNA helicase DHX58|||Abolishes IFNB1 production upon infection with various viruses.|||DECH box|||Helicase ATP-binding|||Helicase C-terminal|||RLR CTR|||RNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000102011 http://togogenome.org/gene/10090:Hoxc4 ^@ http://purl.uniprot.org/uniprot/Q08624 ^@ 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-C4|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000200165 http://togogenome.org/gene/10090:Imp4 ^@ http://purl.uniprot.org/uniprot/Q8VHZ7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Brix|||U3 small nucleolar ribonucleoprotein protein IMP4 ^@ http://purl.uniprot.org/annotation/PRO_0000120237 http://togogenome.org/gene/10090:Lsm1 ^@ http://purl.uniprot.org/uniprot/Q544C9|||http://purl.uniprot.org/uniprot/Q8VC85 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Phosphoserine|||Phosphothreonine|||Sm|||U6 snRNA-associated Sm-like protein LSm1 ^@ http://purl.uniprot.org/annotation/PRO_0000125555 http://togogenome.org/gene/10090:Omt2a ^@ http://purl.uniprot.org/uniprot/G3X9W2|||http://purl.uniprot.org/uniprot/G5E8X8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Fbxo45 ^@ http://purl.uniprot.org/uniprot/Q8K3B1 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ Allows binding to CUL1 and RBX1 and formation of an authentic SCF (SKP1-CUL1-F-box protein) complex.|||B30.2/SPRY|||F-box|||F-box/SPRY domain-containing protein 1|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000119947 http://togogenome.org/gene/10090:Fkbp2 ^@ http://purl.uniprot.org/uniprot/P45878|||http://purl.uniprot.org/uniprot/Q3TND1|||http://purl.uniprot.org/uniprot/Q3UND3 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Motif|||Signal Peptide ^@ PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP2|||Prevents secretion from ER|||peptidylprolyl isomerase ^@ http://purl.uniprot.org/annotation/PRO_0000025507|||http://purl.uniprot.org/annotation/PRO_5004230088|||http://purl.uniprot.org/annotation/PRO_5014309147 http://togogenome.org/gene/10090:Pde8a ^@ http://purl.uniprot.org/uniprot/O88502 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A|||PAC|||PAS|||PDEase|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000198839 http://togogenome.org/gene/10090:Mpc1 ^@ http://purl.uniprot.org/uniprot/P63030 ^@ 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 ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrial pyruvate carrier 1|||N-acetylalanine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000212798 http://togogenome.org/gene/10090:Cdhr1 ^@ http://purl.uniprot.org/uniprot/Q8VHP6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin-related family member 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000318499 http://togogenome.org/gene/10090:Apba3 ^@ http://purl.uniprot.org/uniprot/O88888|||http://purl.uniprot.org/uniprot/Q3TER1 ^@ 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 ^@ Amyloid-beta A4 precursor protein-binding family A member 3|||Disordered|||N-acetylmethionine|||PDZ|||PDZ 1|||PDZ 2|||PID|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000064621 http://togogenome.org/gene/10090:Pkd1 ^@ http://purl.uniprot.org/uniprot/O08852|||http://purl.uniprot.org/uniprot/Q5DU58 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cleavage; by autolysis|||Cytoplasmic|||Disordered|||Extracellular|||GPS|||Helical|||LDL-receptor class A; atypical|||LRR 1|||LRR 2|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||PKD|||PKD 1|||PKD 10|||PKD 11|||PKD 12|||PKD 13|||PKD 14|||PKD 15|||PKD 16|||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_0000354054 http://togogenome.org/gene/10090:Tnnt1 ^@ http://purl.uniprot.org/uniprot/O88346|||http://purl.uniprot.org/uniprot/Q3TVB8 ^@ 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 ^@ Acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine; by CK2|||Troponin T, slow skeletal muscle ^@ http://purl.uniprot.org/annotation/PRO_0000186169|||http://purl.uniprot.org/annotation/VSP_013786|||http://purl.uniprot.org/annotation/VSP_013787 http://togogenome.org/gene/10090:Cask ^@ http://purl.uniprot.org/uniprot/B9EJ23|||http://purl.uniprot.org/uniprot/O70589 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Calmodulin-binding|||Disordered|||Guanylate kinase-like|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||L27|||L27 1|||L27 2|||PDZ|||Peripheral plasma membrane protein CASK|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Protein kinase|||Required for interaction with NRXN1 (via C-terminal tail)|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000094569|||http://purl.uniprot.org/annotation/VSP_003152|||http://purl.uniprot.org/annotation/VSP_003153|||http://purl.uniprot.org/annotation/VSP_024614|||http://purl.uniprot.org/annotation/VSP_024615|||http://purl.uniprot.org/annotation/VSP_024616 http://togogenome.org/gene/10090:Rfk ^@ http://purl.uniprot.org/uniprot/Q8CFV9 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Nucleophile|||Riboflavin kinase ^@ http://purl.uniprot.org/annotation/PRO_0000194149 http://togogenome.org/gene/10090:Bloc1s6 ^@ http://purl.uniprot.org/uniprot/Q9R0C0 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Sequence Variant|||Splice Variant ^@ Biogenesis of lysosome-related organelles complex 1 subunit 6|||Disordered|||In isoform 2.|||In strain: BALB/c, CBA and C57BL/6J-pa mutants.|||In strain: C57BL/6J-pa mutants. ^@ http://purl.uniprot.org/annotation/PRO_0000058459|||http://purl.uniprot.org/annotation/VSP_009295|||http://purl.uniprot.org/annotation/VSP_009296 http://togogenome.org/gene/10090:Ltbp4 ^@ http://purl.uniprot.org/uniprot/Q3UGU1|||http://purl.uniprot.org/uniprot/Q8K4G1 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||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 isoform 2.|||In isoform 3.|||Interchain (with C-33 in TGFB1); in linked form|||Latent-transforming growth factor beta-binding protein 4|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Pro residues|||TB|||TB 1|||TB 2|||TB 3|||TB 4 ^@ http://purl.uniprot.org/annotation/PRO_0000007648|||http://purl.uniprot.org/annotation/VSP_009248|||http://purl.uniprot.org/annotation/VSP_009249|||http://purl.uniprot.org/annotation/VSP_009250 http://togogenome.org/gene/10090:Tpi1 ^@ http://purl.uniprot.org/uniprot/P17751 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant ^@ 3'-nitrotyrosine|||50% reduced activity.|||Electrophile|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||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_0000090116|||http://purl.uniprot.org/annotation/VSP_060724 http://togogenome.org/gene/10090:Vmn1r157 ^@ http://purl.uniprot.org/uniprot/E9Q069 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdk5r1 ^@ http://purl.uniprot.org/uniprot/P61809|||http://purl.uniprot.org/uniprot/Q542T9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Site ^@ Abolishes the binding to CDK5RAP1, CDK5RAP2, CDKRAP3, but not to CDK5.|||Cleavage; by calpain|||Cyclin-dependent kinase 5 activator 1, p25|||Cyclin-dependent kinase 5 activator 1, p35|||Disordered|||N-myristoyl glycine|||Phosphoserine; by CDK5|||Phosphothreonine; by CDK5|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000004796|||http://purl.uniprot.org/annotation/PRO_0000004797 http://togogenome.org/gene/10090:Ajm1 ^@ http://purl.uniprot.org/uniprot/A2AJA9 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant ^@ Apical junction component 1 homolog|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000392545|||http://purl.uniprot.org/annotation/VSP_038820 http://togogenome.org/gene/10090:Tmed10 ^@ http://purl.uniprot.org/uniprot/Q9D1D4 ^@ Chain|||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|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||Dimethylated arginine|||GOLD|||Helical|||In isoform 2.|||Interaction with ARF1 and IL1B|||Interaction with COPG1|||Lumenal|||N-linked (GlcNAc...) asparagine|||Required for TMED10 and TMED2 cis-Golgi network localization|||Required for interaction with STX17|||Transmembrane emp24 domain-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000010401|||http://purl.uniprot.org/annotation/VSP_013582 http://togogenome.org/gene/10090:Zfp874a ^@ http://purl.uniprot.org/uniprot/Q66JQ2|||http://purl.uniprot.org/uniprot/Q8BX23 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Mtmr2 ^@ http://purl.uniprot.org/uniprot/Q6P572|||http://purl.uniprot.org/uniprot/Q9Z2D1 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||GRAM|||Loss of activity. Does not affect the interaction with SBF2/MTMR13.|||Loss of interaction with SBF2/MTMR13 which results in a decrease in SBF2/MTMR13 localization to membranes.|||Myotubularin phosphatase|||Myotubularin-related protein 2|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Severely impaired interaction with membranes and strongly reduced catalytic activity.|||Tyrosine specific protein phosphatases ^@ http://purl.uniprot.org/annotation/PRO_0000094935 http://togogenome.org/gene/10090:Klf7 ^@ http://purl.uniprot.org/uniprot/Q99JB0 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Motif|||Sequence Conflict|||Zinc Finger ^@ 9aaTAD; inactive|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Krueppel-like factor 7|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000047175 http://togogenome.org/gene/10090:Shprh ^@ http://purl.uniprot.org/uniprot/Q7TPQ3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||DEAQ box|||Disordered|||E3 ubiquitin-protein ligase SHPRH|||H15|||Helicase ATP-binding; first part|||Helicase ATP-binding; second part|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PHD-type|||Phosphoserine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000284919|||http://purl.uniprot.org/annotation/VSP_024766|||http://purl.uniprot.org/annotation/VSP_024767|||http://purl.uniprot.org/annotation/VSP_024768|||http://purl.uniprot.org/annotation/VSP_024769|||http://purl.uniprot.org/annotation/VSP_024770 http://togogenome.org/gene/10090:Grm1 ^@ http://purl.uniprot.org/uniprot/P97772|||http://purl.uniprot.org/uniprot/Q3V0U2 ^@ Binding Site|||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|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 isoform 2.|||In isoform 3.|||Interchain|||Metabotropic glutamate receptor 1|||N-linked (GlcNAc...) asparagine|||Normal response to light but reduced retinal electrical activity in response to light in dark adapted retinas. Gross morphology is normal.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000012923|||http://purl.uniprot.org/annotation/VSP_007184|||http://purl.uniprot.org/annotation/VSP_007185|||http://purl.uniprot.org/annotation/VSP_007186|||http://purl.uniprot.org/annotation/VSP_007187 http://togogenome.org/gene/10090:Ankef1 ^@ http://purl.uniprot.org/uniprot/Q9D2J7 ^@ 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 and EF-hand domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000066900 http://togogenome.org/gene/10090:Tmem239 ^@ http://purl.uniprot.org/uniprot/Q9DA47 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 239 ^@ http://purl.uniprot.org/annotation/PRO_0000413695 http://togogenome.org/gene/10090:Gpr39 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1E4 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Stam ^@ http://purl.uniprot.org/uniprot/P70297|||http://purl.uniprot.org/uniprot/Q3TQ49 ^@ 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)|||ITAM|||Phosphoserine|||Phosphotyrosine|||SH3|||Signal transducing adapter molecule 1|||UIM|||VHS ^@ http://purl.uniprot.org/annotation/PRO_0000190146 http://togogenome.org/gene/10090:Med11 ^@ http://purl.uniprot.org/uniprot/Q9D8C6 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Mediator of RNA polymerase II transcription subunit 11|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000304309 http://togogenome.org/gene/10090:Gstp3 ^@ http://purl.uniprot.org/uniprot/Q8VC73 ^@ Domain Extent|||Region ^@ Domain Extent ^@ GST C-terminal|||GST N-terminal ^@ http://togogenome.org/gene/10090:Dsc2 ^@ http://purl.uniprot.org/uniprot/P55292|||http://purl.uniprot.org/uniprot/Q544V1 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin domain-containing protein|||Cytoplasmic|||Desmocollin-2|||Extracellular|||Helical|||In isoform 2B.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000003871|||http://purl.uniprot.org/annotation/PRO_0000003872|||http://purl.uniprot.org/annotation/PRO_5010844031|||http://purl.uniprot.org/annotation/VSP_000659|||http://purl.uniprot.org/annotation/VSP_000660 http://togogenome.org/gene/10090:Poteg ^@ http://purl.uniprot.org/uniprot/A5H0M4|||http://purl.uniprot.org/uniprot/Q9CUQ9|||http://purl.uniprot.org/uniprot/Q9D5D4 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat ^@ ANK|||Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Msmb ^@ http://purl.uniprot.org/uniprot/O08540 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-microseminoprotein ^@ http://purl.uniprot.org/annotation/PRO_0000019270 http://togogenome.org/gene/10090:Gpr152 ^@ http://purl.uniprot.org/uniprot/Q8BXS7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Polar residues|||Probable G-protein coupled receptor 152 ^@ http://purl.uniprot.org/annotation/PRO_0000069636 http://togogenome.org/gene/10090:Or8g4 ^@ http://purl.uniprot.org/uniprot/Q7TRA6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H3c4 ^@ http://purl.uniprot.org/uniprot/B9EI85|||http://purl.uniprot.org/uniprot/P84228 ^@ Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||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 H2A/H2B/H3|||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; 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_0000221250 http://togogenome.org/gene/10090:Itgb6 ^@ http://purl.uniprot.org/uniprot/Q9Z0T9 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||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_0000016351 http://togogenome.org/gene/10090:Fbxo39 ^@ http://purl.uniprot.org/uniprot/Q5NBU5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ F-box|||F-box only protein 39 ^@ http://purl.uniprot.org/annotation/PRO_0000119936 http://togogenome.org/gene/10090:Prdm6 ^@ http://purl.uniprot.org/uniprot/Q3UZD5 ^@ 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 ^@ C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; degenerate|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of function in histone modification.|||Loss of function in histone modification. Loss of nuclear localization.|||Pro residues|||Putative histone-lysine N-methyltransferase PRDM6|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000363959|||http://purl.uniprot.org/annotation/VSP_036371|||http://purl.uniprot.org/annotation/VSP_036372|||http://purl.uniprot.org/annotation/VSP_036373 http://togogenome.org/gene/10090:Ints3 ^@ http://purl.uniprot.org/uniprot/Q7TPD0 ^@ 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.|||Integrator complex subunit 3|||N-acetylmethionine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000259535|||http://purl.uniprot.org/annotation/VSP_038133|||http://purl.uniprot.org/annotation/VSP_038134 http://togogenome.org/gene/10090:Or7g28 ^@ http://purl.uniprot.org/uniprot/Q8VET8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wasf2 ^@ http://purl.uniprot.org/uniprot/Q8BH43 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Actin-binding protein WASF2|||Basic and acidic residues|||Disordered|||Phosphoserine|||Pro residues|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000188995 http://togogenome.org/gene/10090:Ccar1 ^@ http://purl.uniprot.org/uniprot/Q8CH18 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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 isoform 2.|||In isoform 3.|||Interaction with AR|||Interaction with GATA1|||Interaction with GATA2|||Phosphoserine|||Phosphothreonine|||SAP ^@ http://purl.uniprot.org/annotation/PRO_0000233149|||http://purl.uniprot.org/annotation/VSP_018054|||http://purl.uniprot.org/annotation/VSP_018055|||http://purl.uniprot.org/annotation/VSP_037737 http://togogenome.org/gene/10090:Vwa8 ^@ http://purl.uniprot.org/uniprot/Q8CC88 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with PEX7|||Loss of in vitro ATPase activity.|||Mitochondrion|||VWFA|||von Willebrand factor A domain-containing protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000343892|||http://purl.uniprot.org/annotation/VSP_034707|||http://purl.uniprot.org/annotation/VSP_034708 http://togogenome.org/gene/10090:Prss35 ^@ http://purl.uniprot.org/uniprot/Q8C0F9 ^@ 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 ^@ Basic residues|||Disordered|||Inactive serine protease 35|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000299360 http://togogenome.org/gene/10090:Cd300ld5 ^@ http://purl.uniprot.org/uniprot/A2A7W1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Immunoglobulin V-set ^@ http://purl.uniprot.org/annotation/PRO_5015086002 http://togogenome.org/gene/10090:Omp ^@ http://purl.uniprot.org/uniprot/Q64288 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn ^@ N-acetylalanine|||Olfactory marker protein|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000058045 http://togogenome.org/gene/10090:Cog5 ^@ http://purl.uniprot.org/uniprot/Q8C0L8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Conserved oligomeric Golgi complex subunit 5|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000320146 http://togogenome.org/gene/10090:Negr1 ^@ http://purl.uniprot.org/uniprot/A0A4W9|||http://purl.uniprot.org/uniprot/D3Z4T6|||http://purl.uniprot.org/uniprot/Q80Z24 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated glycine|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||N-linked (GlcNAc...) asparagine|||Neuronal growth regulator 1|||Phosphotyrosine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000015039|||http://purl.uniprot.org/annotation/PRO_0000015040|||http://purl.uniprot.org/annotation/PRO_5015085816|||http://purl.uniprot.org/annotation/PRO_5015088519 http://togogenome.org/gene/10090:Chchd5 ^@ http://purl.uniprot.org/uniprot/Q52KC5|||http://purl.uniprot.org/uniprot/Q9CQP3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif ^@ 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|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000129168 http://togogenome.org/gene/10090:Hmcn1 ^@ http://purl.uniprot.org/uniprot/D3YXG0 ^@ 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 ^@ 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 isoform 2.|||Nidogen G2 beta-barrel|||O-linked (GalNAc...) threonine|||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_5003053106|||http://purl.uniprot.org/annotation/VSP_058526 http://togogenome.org/gene/10090:Zranb2 ^@ http://purl.uniprot.org/uniprot/B2RRT9|||http://purl.uniprot.org/uniprot/D3Z4U0|||http://purl.uniprot.org/uniprot/Q9R020 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||RanBP2-type|||RanBP2-type 1|||RanBP2-type 2|||Required for nuclear targeting|||Zinc finger Ran-binding domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000066586|||http://purl.uniprot.org/annotation/VSP_024946 http://togogenome.org/gene/10090:Fbxo22 ^@ http://purl.uniprot.org/uniprot/Q3V492|||http://purl.uniprot.org/uniprot/Q78JE5 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ F-box|||F-box only protein 22|||FIST C-domain|||N-acetylmethionine|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000119907 http://togogenome.org/gene/10090:Tox ^@ http://purl.uniprot.org/uniprot/Q66JW3 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||HMG box|||In isoform 2.|||Nuclear localization signal|||Polar residues|||Thymocyte selection-associated high mobility group box protein TOX ^@ http://purl.uniprot.org/annotation/PRO_0000244570|||http://purl.uniprot.org/annotation/VSP_019598|||http://purl.uniprot.org/annotation/VSP_019599 http://togogenome.org/gene/10090:Mcam ^@ http://purl.uniprot.org/uniprot/Q8R2Y2 ^@ 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 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000045460|||http://purl.uniprot.org/annotation/VSP_016940 http://togogenome.org/gene/10090:Runx1 ^@ http://purl.uniprot.org/uniprot/G3UWD2|||http://purl.uniprot.org/uniprot/G3X9W7|||http://purl.uniprot.org/uniprot/Q3UM65|||http://purl.uniprot.org/uniprot/Q8BQ09 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Runt ^@ http://togogenome.org/gene/10090:Crocc2 ^@ http://purl.uniprot.org/uniprot/F6XLV1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Ciliary rootlet coiled-coil protein 2|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000452751 http://togogenome.org/gene/10090:Nmnat3 ^@ http://purl.uniprot.org/uniprot/Q99JR6 ^@ Binding Site|||Chain|||Helix|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Strand|||Turn ^@ Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000135017 http://togogenome.org/gene/10090:Man2a2 ^@ http://purl.uniprot.org/uniprot/Q197W7|||http://purl.uniprot.org/uniprot/Q7TPQ0|||http://purl.uniprot.org/uniprot/Q8BRK9 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Alpha-mannosidase 2x|||Cytoplasmic|||Glycoside hydrolase family 38 central|||Glycosyl hydrolase family 38 C-terminal|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000412634|||http://purl.uniprot.org/annotation/VSP_041735|||http://purl.uniprot.org/annotation/VSP_041736 http://togogenome.org/gene/10090:Pabir3 ^@ http://purl.uniprot.org/uniprot/Q9D5J5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Vmn1r244 ^@ http://purl.uniprot.org/uniprot/K7N6J2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccl1 ^@ http://purl.uniprot.org/uniprot/P10146|||http://purl.uniprot.org/uniprot/Q0VB35 ^@ 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 ^@ C-C motif chemokine|||C-C motif chemokine 1|||Chemokine interleukin-8-like|||In isoform 2.|||In strain: DBA/2J and SJL/J.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000005142|||http://purl.uniprot.org/annotation/PRO_5014205721|||http://purl.uniprot.org/annotation/VSP_001059 http://togogenome.org/gene/10090:Slc37a2 ^@ http://purl.uniprot.org/uniprot/Q9WU81 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Glucose-6-phosphate exchanger SLC37A2|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000308323|||http://purl.uniprot.org/annotation/VSP_028964 http://togogenome.org/gene/10090:Aar2 ^@ http://purl.uniprot.org/uniprot/Q9D2V5 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Protein AAR2 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000209707 http://togogenome.org/gene/10090:Chil3 ^@ http://purl.uniprot.org/uniprot/O35744 ^@ 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|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chitinase-like protein 3|||GH18 ^@ http://purl.uniprot.org/annotation/PRO_0000011970 http://togogenome.org/gene/10090:Asb10 ^@ http://purl.uniprot.org/uniprot/D3YU18|||http://purl.uniprot.org/uniprot/Q91ZT7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankyrin repeat and SOCS box protein 10|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066943 http://togogenome.org/gene/10090:Klhl26 ^@ http://purl.uniprot.org/uniprot/E9Q4C1|||http://purl.uniprot.org/uniprot/Q8BGY4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Splice Variant ^@ BACK|||BTB|||Disordered|||In isoform 2.|||In isoform 3.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 26|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000242689|||http://purl.uniprot.org/annotation/VSP_019473|||http://purl.uniprot.org/annotation/VSP_019474 http://togogenome.org/gene/10090:G3bp2 ^@ http://purl.uniprot.org/uniprot/P97379|||http://purl.uniprot.org/uniprot/Q3TEL4|||http://purl.uniprot.org/uniprot/Q3U541|||http://purl.uniprot.org/uniprot/Q3U6B1|||http://purl.uniprot.org/uniprot/Q542W3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic disordered region|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform B.|||N6-succinyllysine|||NTF2|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RG-rich region|||RRM|||Ras GTPase-activating protein-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000194801|||http://purl.uniprot.org/annotation/VSP_003606 http://togogenome.org/gene/10090:Slc41a2 ^@ http://purl.uniprot.org/uniprot/B2RQZ3|||http://purl.uniprot.org/uniprot/Q8BYR8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Phosphoserine|||SLC41A/MgtE integral membrane|||Solute carrier family 41 member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000295042 http://togogenome.org/gene/10090:Hivep2 ^@ http://purl.uniprot.org/uniprot/Q3UHF7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||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_0000047372 http://togogenome.org/gene/10090:Slc46a3 ^@ http://purl.uniprot.org/uniprot/Q9DC26 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||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_0000307254 http://togogenome.org/gene/10090:Sh3bgrl ^@ http://purl.uniprot.org/uniprot/Q9JJU8 ^@ Chain|||Molecule Processing|||Motif|||Region ^@ Chain|||Motif|||Region ^@ Adapter Sh3bgrl|||Required for interaction with HER2|||Required for interaction with PFN1, HER2, and ATG12|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000220746 http://togogenome.org/gene/10090:Phldb3 ^@ http://purl.uniprot.org/uniprot/E9QAF4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PH|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Prorsd1 ^@ http://purl.uniprot.org/uniprot/Q9D820 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||Prolyl-tRNA synthetase associated domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000329287|||http://purl.uniprot.org/annotation/VSP_032962 http://togogenome.org/gene/10090:Snupn ^@ http://purl.uniprot.org/uniprot/Q80W37 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site ^@ Basic and acidic residues|||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|||Snurportin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000191072 http://togogenome.org/gene/10090:Mcm6 ^@ http://purl.uniprot.org/uniprot/P97311|||http://purl.uniprot.org/uniprot/Q3ULG5|||http://purl.uniprot.org/uniprot/Q542I2|||http://purl.uniprot.org/uniprot/Q8C5L1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region ^@ Arginine finger|||DNA replication licensing factor MCM6|||Decreased MCM complex DNA helicase activity. Loss of ATP-binding. Decreased MCM complex ATPase activity. No effect on MCM complex formation.|||Disordered|||Loss of MCM complex DNA helicase activity. Loss of ATP-binding. No effect on MCM complex formation. No effect on MCM complex ATPase activity and ssDNA binding.|||MCM|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000194114 http://togogenome.org/gene/10090:Or3a1d ^@ http://purl.uniprot.org/uniprot/Q7TRW8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or8h10 ^@ http://purl.uniprot.org/uniprot/Q8VFM1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dusp16 ^@ http://purl.uniprot.org/uniprot/F6UIK0|||http://purl.uniprot.org/uniprot/Q6PCP3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Rhodanese|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://togogenome.org/gene/10090:Dele1 ^@ http://purl.uniprot.org/uniprot/Q9DCV6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Propeptide|||Region|||Repeat|||Site|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Propeptide|||Region|||Repeat|||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_0000050722|||http://purl.uniprot.org/annotation/PRO_0000450309|||http://purl.uniprot.org/annotation/PRO_0000459061 http://togogenome.org/gene/10090:Syne4 ^@ http://purl.uniprot.org/uniprot/H3BL35|||http://purl.uniprot.org/uniprot/Q8CII8 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||Interchain (with C-577 in SUN2); alternate|||Interchain (with C-759 in SUN1)|||KASH|||Nesprin-4|||Perinuclear space|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000306265 http://togogenome.org/gene/10090:Ptn ^@ http://purl.uniprot.org/uniprot/P63089 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Signal Peptide ^@ Basic and acidic residues|||Chondroitin sulfate A binding|||Chondroitin sulfate binding|||Disordered|||Pleiotrophin ^@ http://purl.uniprot.org/annotation/PRO_0000024660 http://togogenome.org/gene/10090:Rnf19a ^@ http://purl.uniprot.org/uniprot/P50636 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNF19A|||Helical|||IBR-type|||Interaction with CASR|||Phosphoserine|||Polar residues|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain ^@ http://purl.uniprot.org/annotation/PRO_0000056062 http://togogenome.org/gene/10090:Qprt ^@ http://purl.uniprot.org/uniprot/Q91X91 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region ^@ Important for hexamer formation|||Nicotinate-nucleotide pyrophosphorylase [carboxylating]|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000155955 http://togogenome.org/gene/10090:Zcchc18 ^@ http://purl.uniprot.org/uniprot/Q8VD24 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger ^@ CCHC-type|||Disordered|||Polar residues|||Zinc finger CCHC domain-containing protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000395362 http://togogenome.org/gene/10090:Dag1 ^@ http://purl.uniprot.org/uniprot/Q544G5|||http://purl.uniprot.org/uniprot/Q62165|||http://purl.uniprot.org/uniprot/Q8BPJ7|||http://purl.uniprot.org/uniprot/Q8CBE6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||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|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Alpha-dystroglycan|||Beta-dystroglycan|||Cleavage; by MMP9|||Cleavage; by autolysis|||Complete loss of ANK3-binding.|||Cytoplasmic|||Disordered|||Dystroglycan 1|||Extracellular|||Helical|||Major reduction in ANK3-binding.|||Mucin-like domain|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||O-glycosylated at one site|||O-glycosylated at seven sites with GalNAc|||O-linked (Man6P...) threonine|||PPXY motif|||Peptidase S72|||Phosphothreonine|||Phosphotyrosine; by SRC|||Polar residues|||Pro residues|||Required for binding DMD and UTRN|||Required for interaction with CAV3|||Required for laminin recognition ^@ http://purl.uniprot.org/annotation/PRO_0000021067|||http://purl.uniprot.org/annotation/PRO_0000021068|||http://purl.uniprot.org/annotation/PRO_5004304204|||http://purl.uniprot.org/annotation/PRO_5004306269|||http://purl.uniprot.org/annotation/PRO_5014309576 http://togogenome.org/gene/10090:Commd3 ^@ http://purl.uniprot.org/uniprot/Q63829 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ COMM|||COMM domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000077390 http://togogenome.org/gene/10090:Fcgrt ^@ http://purl.uniprot.org/uniprot/Q61559 ^@ 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 ^@ Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C1-type|||IgG receptor FcRn large subunit p51|||In strain: FVB/N.|||In strain: P/J.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000015159 http://togogenome.org/gene/10090:Jam2 ^@ http://purl.uniprot.org/uniprot/Q9JI59 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||Junctional adhesion molecule B|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015070 http://togogenome.org/gene/10090:Nr6a1 ^@ http://purl.uniprot.org/uniprot/Q64249 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Abolishes interaction with RXRIP110.|||Disordered|||Does not abolish interaction with RXRIP110.|||In isoform 2.|||In isoform 3.|||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_0000053742|||http://purl.uniprot.org/annotation/VSP_025928|||http://purl.uniprot.org/annotation/VSP_025929|||http://purl.uniprot.org/annotation/VSP_025930|||http://purl.uniprot.org/annotation/VSP_025931 http://togogenome.org/gene/10090:Iho1 ^@ http://purl.uniprot.org/uniprot/Q6PDM4 ^@ 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|||Basic residues|||Disordered|||Interactor of HORMAD1 protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000302876 http://togogenome.org/gene/10090:Soga1 ^@ http://purl.uniprot.org/uniprot/A2ACV6 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ DUF4482|||Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Elmod3 ^@ http://purl.uniprot.org/uniprot/Q91YP6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ ELMO|||ELMO domain-containing protein 3|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000274904|||http://purl.uniprot.org/annotation/VSP_022925|||http://purl.uniprot.org/annotation/VSP_022926 http://togogenome.org/gene/10090:Otx1 ^@ http://purl.uniprot.org/uniprot/P80205|||http://purl.uniprot.org/uniprot/Q5SS54 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||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_0000049208 http://togogenome.org/gene/10090:Nxt2 ^@ http://purl.uniprot.org/uniprot/Q3UNA4 ^@ 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.|||NTF2|||NTF2-related export protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000378200|||http://purl.uniprot.org/annotation/VSP_037528|||http://purl.uniprot.org/annotation/VSP_037529 http://togogenome.org/gene/10090:Pcx ^@ http://purl.uniprot.org/uniprot/E9QPD7|||http://purl.uniprot.org/uniprot/G5E8R3|||http://purl.uniprot.org/uniprot/Q3UFS6|||http://purl.uniprot.org/uniprot/Q8BP54 ^@ Active Site|||Binding Site|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Modified Residue|||Non-terminal Residue ^@ ATP-grasp|||Biotin carboxylation|||Lipoyl-binding|||N6-biotinyllysine|||N6-carboxylysine|||Pyruvate carboxyltransferase|||via carbamate group ^@ http://togogenome.org/gene/10090:Jrk ^@ http://purl.uniprot.org/uniprot/Q543Z9|||http://purl.uniprot.org/uniprot/Q60976 ^@ 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|||Jerky protein ^@ http://purl.uniprot.org/annotation/PRO_0000126129 http://togogenome.org/gene/10090:Telo2 ^@ http://purl.uniprot.org/uniprot/Q9DC40 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Disordered|||Does not inhibit interaction with TTI1 or TTI2. Inhibits weakly interaction with TTI1 or TTI2; when associated with E-407 or R-424. Inhibits interaction with TTI1 or TTI2; when associated with E-407 and R-424.|||Does not inhibit interaction with TTI1 or TTI2. Inhibits weakly interaction with TTI1 or TTI2; when associated with Q-395 or E-407. Inhibits interaction with TTI1 or TTI2; when associated with Q-395 and E-407.|||Does not inhibit interaction with TTI1 or TTI2. Inhibits weakly interaction with TTI1 or TTI2; when associated with Q-395 or R-424. Inhibits interaction with TTI1 or TTI2; when associated with Q-395 and R-424.|||Hydroxyproline|||In isoform 2.|||Interaction with PIH1D1|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by CK2|||Telomere length regulation protein TEL2 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000318516|||http://purl.uniprot.org/annotation/VSP_031207|||http://purl.uniprot.org/annotation/VSP_031208|||http://purl.uniprot.org/annotation/VSP_031209 http://togogenome.org/gene/10090:Erap1 ^@ http://purl.uniprot.org/uniprot/Q9EQH2 ^@ 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|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endoplasmic reticulum aminopeptidase 1|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000026752 http://togogenome.org/gene/10090:Asl ^@ http://purl.uniprot.org/uniprot/Q91YI0 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Site ^@ Argininosuccinate lyase|||Increases basicity of active site His|||N-acetylalanine|||N6-acetyllysine|||Proton acceptor|||Proton donor|||Removed|||in chain A|||in chain B|||in chain C ^@ http://purl.uniprot.org/annotation/PRO_0000137714 http://togogenome.org/gene/10090:Or12j5 ^@ http://purl.uniprot.org/uniprot/Q8VFE9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vwa5b2 ^@ http://purl.uniprot.org/uniprot/Q3UR50 ^@ 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.|||In isoform 3.|||Polar residues|||VIT|||VWFA|||von Willebrand factor A domain-containing protein 5B2 ^@ http://purl.uniprot.org/annotation/PRO_0000339303|||http://purl.uniprot.org/annotation/VSP_034141|||http://purl.uniprot.org/annotation/VSP_034144|||http://purl.uniprot.org/annotation/VSP_034145|||http://purl.uniprot.org/annotation/VSP_034146 http://togogenome.org/gene/10090:Csmd2 ^@ http://purl.uniprot.org/uniprot/V9GX34 ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ CUB|||Disordered|||Helical|||Pro residues|||Sushi ^@ http://togogenome.org/gene/10090:Tcl1b3 ^@ http://purl.uniprot.org/uniprot/P56842 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein TCL1B3 ^@ http://purl.uniprot.org/annotation/PRO_0000184493 http://togogenome.org/gene/10090:Adhfe1 ^@ http://purl.uniprot.org/uniprot/Q8R0N6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant|||Transit Peptide ^@ Chain|||Modified Residue|||Splice Variant|||Transit Peptide ^@ Hydroxyacid-oxoacid transhydrogenase, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000322997|||http://purl.uniprot.org/annotation/VSP_031987 http://togogenome.org/gene/10090:Lhx2 ^@ http://purl.uniprot.org/uniprot/F6Z9H5|||http://purl.uniprot.org/uniprot/Q543C6|||http://purl.uniprot.org/uniprot/Q9Z0S2 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Mutagenesis Site|||Region ^@ Disordered|||Homeobox|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx2|||Nuclear localization signal|||Polar residues|||Reduces transcriptional activation; when associated with A-53.|||Reduces transcriptional activation; when associated with A-56. ^@ http://purl.uniprot.org/annotation/PRO_0000075779 http://togogenome.org/gene/10090:Rbms1 ^@ http://purl.uniprot.org/uniprot/E9PZ21|||http://purl.uniprot.org/uniprot/Q3TTX8|||http://purl.uniprot.org/uniprot/Q3UKR8|||http://purl.uniprot.org/uniprot/Q91W59 ^@ 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 3.|||Phosphothreonine|||Polar residues|||RNA-binding motif, single-stranded-interacting protein 1|||RRM|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081799|||http://purl.uniprot.org/annotation/VSP_011931|||http://purl.uniprot.org/annotation/VSP_011932 http://togogenome.org/gene/10090:Ccr5 ^@ http://purl.uniprot.org/uniprot/P51682 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane ^@ C-C chemokine receptor type 5|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||O-linked (GalNAc...) serine|||Phosphoserine; by BARK1|||S-palmitoyl cysteine|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000069269 http://togogenome.org/gene/10090:Vmn1r44 ^@ http://purl.uniprot.org/uniprot/Q9EQ47 ^@ 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|||Vomeronasal type-1 receptor 44 ^@ http://purl.uniprot.org/annotation/PRO_0000239976 http://togogenome.org/gene/10090:Vmn1r231 ^@ http://purl.uniprot.org/uniprot/Q8R2A3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ssxb1 ^@ http://purl.uniprot.org/uniprot/Q9CPU1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB|||KRAB-related ^@ http://togogenome.org/gene/10090:Trpt1 ^@ http://purl.uniprot.org/uniprot/Q8K3A2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Polar residues|||tRNA 2'-phosphotransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000273364 http://togogenome.org/gene/10090:Ttc14 ^@ http://purl.uniprot.org/uniprot/A0A0G2JGX7|||http://purl.uniprot.org/uniprot/A0A8V5I5B0|||http://purl.uniprot.org/uniprot/A6H6N9|||http://purl.uniprot.org/uniprot/E9PXW3|||http://purl.uniprot.org/uniprot/Q9CSP9 ^@ 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|||Basic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 6.|||In isoform 7.|||Phosphoserine|||Polar residues|||S1 motif|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||Tetratricopeptide repeat protein 14 ^@ http://purl.uniprot.org/annotation/PRO_0000106400|||http://purl.uniprot.org/annotation/VSP_022193|||http://purl.uniprot.org/annotation/VSP_061584|||http://purl.uniprot.org/annotation/VSP_061585|||http://purl.uniprot.org/annotation/VSP_061586|||http://purl.uniprot.org/annotation/VSP_061587|||http://purl.uniprot.org/annotation/VSP_061588 http://togogenome.org/gene/10090:Mmrn1 ^@ http://purl.uniprot.org/uniprot/A0A0N4SVL8|||http://purl.uniprot.org/uniprot/B2RPV6|||http://purl.uniprot.org/uniprot/G3UVV6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||C1q|||Disordered|||EGF-like|||EMI|||In isoform 2.|||Multimerin-1|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000367039|||http://purl.uniprot.org/annotation/PRO_5005885433|||http://purl.uniprot.org/annotation/PRO_5015091556|||http://purl.uniprot.org/annotation/VSP_053049 http://togogenome.org/gene/10090:Secisbp2l ^@ http://purl.uniprot.org/uniprot/A2AQE2|||http://purl.uniprot.org/uniprot/Q8C7M0 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||Ribosomal protein eL8/eL30/eS12/Gadd45 ^@ http://togogenome.org/gene/10090:Samt4 ^@ http://purl.uniprot.org/uniprot/Q9D4X6 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:H2ac18 ^@ http://purl.uniprot.org/uniprot/B2RWH3|||http://purl.uniprot.org/uniprot/Q6GSS7 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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 2-A|||Histone H2A/H2B/H3|||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_0000055233 http://togogenome.org/gene/10090:B3glct ^@ http://purl.uniprot.org/uniprot/Q8BHT6 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Beta-1,3-glucosyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000252400|||http://purl.uniprot.org/annotation/VSP_020936 http://togogenome.org/gene/10090:Dhtkd1 ^@ http://purl.uniprot.org/uniprot/A2ATU0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ 2-oxoadipate dehydrogenase complex component E1|||Disordered|||Mitochondrion|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000307937 http://togogenome.org/gene/10090:Tspan7 ^@ http://purl.uniprot.org/uniprot/Q62283 ^@ 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-7 ^@ http://purl.uniprot.org/annotation/PRO_0000219249 http://togogenome.org/gene/10090:Idi1 ^@ http://purl.uniprot.org/uniprot/G3XA48|||http://purl.uniprot.org/uniprot/P58044 ^@ 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 ^@ Isopentenyl-diphosphate Delta-isomerase 1|||Microbody targeting signal|||N6-acetyllysine|||Nudix hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000205225 http://togogenome.org/gene/10090:Nkx2-2 ^@ http://purl.uniprot.org/uniprot/P42586|||http://purl.uniprot.org/uniprot/Q3URZ4|||http://purl.uniprot.org/uniprot/Q8BRS9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Mutagenesis Site|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Nkx-2.2|||Inhibits DNA-binding activity and transcriptional activation of NEUROD1 expression.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048931 http://togogenome.org/gene/10090:Vmn2r80 ^@ http://purl.uniprot.org/uniprot/E9Q1L0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245603 http://togogenome.org/gene/10090:Ccnj ^@ http://purl.uniprot.org/uniprot/Q3TZI6 ^@ 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-J|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000309317|||http://purl.uniprot.org/annotation/VSP_029129 http://togogenome.org/gene/10090:Cxcl3 ^@ http://purl.uniprot.org/uniprot/Q6W5C0 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ C-X-C motif chemokine 3 ^@ http://purl.uniprot.org/annotation/PRO_5000091636 http://togogenome.org/gene/10090:Pnp2 ^@ http://purl.uniprot.org/uniprot/Q9D8C9 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Nucleoside phosphorylase ^@ http://togogenome.org/gene/10090:Ptcra ^@ http://purl.uniprot.org/uniprot/A0A0R4J0F4|||http://purl.uniprot.org/uniprot/P0C6B2 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Interchain (with TCRB)|||N-linked (GlcNAc...) asparagine|||Pre T-cell antigen receptor alpha ^@ http://purl.uniprot.org/annotation/PRO_0000319109|||http://purl.uniprot.org/annotation/PRO_5015044310|||http://purl.uniprot.org/annotation/VSP_031447 http://togogenome.org/gene/10090:Or5ae1 ^@ http://purl.uniprot.org/uniprot/Q7TS13 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnnm4 ^@ http://purl.uniprot.org/uniprot/Q69ZF7 ^@ Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Topological Domain|||Transmembrane ^@ CBS 1|||CBS 2|||CNNM transmembrane|||Cytoplasmic|||Extracellular|||Helical|||Metal transporter CNNM4|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000295766 http://togogenome.org/gene/10090:Emp3 ^@ http://purl.uniprot.org/uniprot/O35912 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ Epithelial membrane protein 3|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000164661 http://togogenome.org/gene/10090:Mdh2 ^@ http://purl.uniprot.org/uniprot/P08249 ^@ 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 ^@ Malate dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000018629 http://togogenome.org/gene/10090:Tmem132e ^@ http://purl.uniprot.org/uniprot/Q6IEE6 ^@ 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 ^@ Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 132E ^@ http://purl.uniprot.org/annotation/PRO_0000287104 http://togogenome.org/gene/10090:Ywhaq ^@ http://purl.uniprot.org/uniprot/A3KML3|||http://purl.uniprot.org/uniprot/P68254 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant ^@ 14-3-3|||14-3-3 protein theta|||3'-nitrotyrosine|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Interaction with phosphoserine on interacting protein|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphoserine; by CK1 ^@ http://purl.uniprot.org/annotation/PRO_0000058637|||http://purl.uniprot.org/annotation/VSP_016340 http://togogenome.org/gene/10090:Parp10 ^@ http://purl.uniprot.org/uniprot/Q8CIE4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ ADP-ribosyl glutamic acid|||Basic and acidic residues|||Disordered|||Myc binding|||PARP catalytic|||PIP-box|||Phosphoserine|||Protein mono-ADP-ribosyltransferase PARP10|||Ubiquitin-interacting ^@ http://purl.uniprot.org/annotation/PRO_0000446172 http://togogenome.org/gene/10090:Krtdap ^@ http://purl.uniprot.org/uniprot/Q3V2T4 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Keratinocyte differentiation-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000317056|||http://purl.uniprot.org/annotation/VSP_052660 http://togogenome.org/gene/10090:Tbx15 ^@ http://purl.uniprot.org/uniprot/O70306 ^@ 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 ^@ Disordered|||Phosphothreonine|||Polar residues|||T-box|||T-box transcription factor TBX15 ^@ http://purl.uniprot.org/annotation/PRO_0000184445 http://togogenome.org/gene/10090:Oas3 ^@ http://purl.uniprot.org/uniprot/Q8VI93 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ 2'-5'-oligoadenylate synthase 3|||Disordered|||Interaction with dsRNA|||Linker|||N-acetylmethionine|||OAS domain 1|||OAS domain 2|||OAS domain 3 ^@ http://purl.uniprot.org/annotation/PRO_0000418630 http://togogenome.org/gene/10090:Arhgef25 ^@ http://purl.uniprot.org/uniprot/A0A0R4J211|||http://purl.uniprot.org/uniprot/G5E825|||http://purl.uniprot.org/uniprot/Q9CWR0 ^@ 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 ^@ DH|||Disordered|||Important for binding to Rho GTPases|||In isoform 2.|||PH|||Polar residues|||Rho guanine nucleotide exchange factor 25|||Sufficient to bind activated GNAQ ^@ http://purl.uniprot.org/annotation/PRO_0000322133|||http://purl.uniprot.org/annotation/VSP_031876 http://togogenome.org/gene/10090:Ptgs1 ^@ http://purl.uniprot.org/uniprot/P22437|||http://purl.uniprot.org/uniprot/Q543T1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Site ^@ Aspirin-acetylated serine|||EGF-like|||For cyclooxygenase activity|||N-linked (GlcNAc...) asparagine|||Prostaglandin G/H synthase 1|||Proton acceptor|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000023869|||http://purl.uniprot.org/annotation/PRO_5014309561 http://togogenome.org/gene/10090:Chd7 ^@ http://purl.uniprot.org/uniprot/A2AJK6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 7|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000289964|||http://purl.uniprot.org/annotation/VSP_026040|||http://purl.uniprot.org/annotation/VSP_026041|||http://purl.uniprot.org/annotation/VSP_026042 http://togogenome.org/gene/10090:1700001C19Rik ^@ http://purl.uniprot.org/uniprot/E9Q6U5|||http://purl.uniprot.org/uniprot/Q8K168|||http://purl.uniprot.org/uniprot/Q9DAS0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Socs5 ^@ http://purl.uniprot.org/uniprot/O54928 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Polar residues|||Required for interaction with IL4R|||SH2|||SOCS box|||Suppressor of cytokine signaling 5 ^@ http://purl.uniprot.org/annotation/PRO_0000181250 http://togogenome.org/gene/10090:Itih3 ^@ http://purl.uniprot.org/uniprot/Q61704 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Aspartate 1-(chondroitin 4-sulfate)-ester|||Inter-alpha-trypsin inhibitor heavy chain H3|||N-linked (GlcNAc...) asparagine|||VIT|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000016535|||http://purl.uniprot.org/annotation/PRO_0000016536|||http://purl.uniprot.org/annotation/PRO_0000016537 http://togogenome.org/gene/10090:Urm1 ^@ http://purl.uniprot.org/uniprot/Q9D2P4 ^@ 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 ^@ 1-thioglycine; alternate|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins); alternate|||Ubiquitin-related modifier 1 ^@ http://purl.uniprot.org/annotation/PRO_0000089715 http://togogenome.org/gene/10090:Slc13a4 ^@ http://purl.uniprot.org/uniprot/Q8BZ82 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Gnb1l ^@ http://purl.uniprot.org/uniprot/Q3TM20|||http://purl.uniprot.org/uniprot/Q3TZ04|||http://purl.uniprot.org/uniprot/Q9EQ15 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ Guanine nucleotide-binding protein subunit beta-like protein 1|||In isoform 2.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000051009|||http://purl.uniprot.org/annotation/VSP_006769|||http://purl.uniprot.org/annotation/VSP_006770 http://togogenome.org/gene/10090:Zfp763 ^@ http://purl.uniprot.org/uniprot/Q8BIC7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Cyp2c67 ^@ http://purl.uniprot.org/uniprot/Q569X9 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015097797 http://togogenome.org/gene/10090:Ydjc ^@ http://purl.uniprot.org/uniprot/Q14BV6 ^@ 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 ^@ Carbohydrate deacetylase|||In isoform 2.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000328775|||http://purl.uniprot.org/annotation/VSP_032788 http://togogenome.org/gene/10090:Cyp2g1 ^@ http://purl.uniprot.org/uniprot/Q9WV19 ^@ Binding Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Smc6 ^@ http://purl.uniprot.org/uniprot/Q924W5 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Flexible hinge|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Structural maintenance of chromosomes protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000270957|||http://purl.uniprot.org/annotation/VSP_022254|||http://purl.uniprot.org/annotation/VSP_022255 http://togogenome.org/gene/10090:Ift57 ^@ http://purl.uniprot.org/uniprot/B2RQZ0|||http://purl.uniprot.org/uniprot/Q8BXG3 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Intraflagellar transport protein 57 homolog|||pDED ^@ http://purl.uniprot.org/annotation/PRO_0000328885|||http://purl.uniprot.org/annotation/VSP_032843 http://togogenome.org/gene/10090:Or11h4 ^@ http://purl.uniprot.org/uniprot/E9Q438 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cfap69 ^@ http://purl.uniprot.org/uniprot/Q8BH53 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Splice Variant ^@ Cilia- and flagella-associated protein 69|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4. ^@ http://purl.uniprot.org/annotation/PRO_0000320597|||http://purl.uniprot.org/annotation/VSP_031677|||http://purl.uniprot.org/annotation/VSP_031678|||http://purl.uniprot.org/annotation/VSP_031679|||http://purl.uniprot.org/annotation/VSP_031680|||http://purl.uniprot.org/annotation/VSP_031681|||http://purl.uniprot.org/annotation/VSP_031682 http://togogenome.org/gene/10090:Hdac5 ^@ http://purl.uniprot.org/uniprot/B7ZDF5|||http://purl.uniprot.org/uniprot/B7ZDF7|||http://purl.uniprot.org/uniprot/Q3UJF1|||http://purl.uniprot.org/uniprot/Q6P9T4 ^@ Active Site|||Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Acidic residues|||Basic and acidic residues|||Contributes to catalysis|||Disordered|||Histone deacetylase|||Histone deacetylase glutamine rich N-terminal ^@ http://togogenome.org/gene/10090:Efr3a ^@ http://purl.uniprot.org/uniprot/Q8BG67 ^@ 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|||Protein EFR3 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000270766|||http://purl.uniprot.org/annotation/VSP_022219 http://togogenome.org/gene/10090:Ptpn22 ^@ http://purl.uniprot.org/uniprot/P29352 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Interaction with CSK|||Phosphocysteine intermediate|||Phosphoserine|||Phosphoserine; by PKC/PRKCD|||Polar residues|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 22 ^@ http://purl.uniprot.org/annotation/PRO_0000094776 http://togogenome.org/gene/10090:Msi1 ^@ http://purl.uniprot.org/uniprot/Q61474 ^@ 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 ^@ Abolishes RNA binding; when associated with L-63 and L-65.|||Abolishes RNA binding; when associated with L-63 and L-68.|||Abolishes RNA binding; when associated with L-65 and L-68.|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||RNA-binding protein Musashi homolog 1|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081650|||http://purl.uniprot.org/annotation/VSP_011166|||http://purl.uniprot.org/annotation/VSP_011167 http://togogenome.org/gene/10090:Klhl9 ^@ http://purl.uniprot.org/uniprot/Q6ZPT1 ^@ 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_0000119111 http://togogenome.org/gene/10090:Tiprl ^@ http://purl.uniprot.org/uniprot/Q8BH58 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Interaction with PPP2CA|||N6-acetyllysine|||Phosphoserine|||TIP41-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000301854 http://togogenome.org/gene/10090:Blcap ^@ http://purl.uniprot.org/uniprot/P62951 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Bladder cancer-associated protein|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000064851 http://togogenome.org/gene/10090:Mog ^@ http://purl.uniprot.org/uniprot/Q3UY21|||http://purl.uniprot.org/uniprot/Q61885|||http://purl.uniprot.org/uniprot/Q66JM2 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||Myelin-oligodendrocyte glycoprotein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014889|||http://purl.uniprot.org/annotation/PRO_5004268589|||http://purl.uniprot.org/annotation/PRO_5015097525 http://togogenome.org/gene/10090:Cd44 ^@ http://purl.uniprot.org/uniprot/A2APM1|||http://purl.uniprot.org/uniprot/A2APM2|||http://purl.uniprot.org/uniprot/A2APM3|||http://purl.uniprot.org/uniprot/A2APM4|||http://purl.uniprot.org/uniprot/P15379|||http://purl.uniprot.org/uniprot/Q3U8S1|||http://purl.uniprot.org/uniprot/Q80X37 ^@ 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 ^@ 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 ^@ CD44 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In Ly-24.2.|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 13.|||In isoform 2.|||In isoform 3 and isoform 8.|||In isoform 4.|||In isoform 5 and isoform 9.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Link|||Loss of interaction with EZR, MSN and RDX and co-localization to microvilli with EZR, MSN and RDX.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues|||Required for interaction with EZR, MSN and RDX and for the co-localization to microvilli|||Stem|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000026689|||http://purl.uniprot.org/annotation/PRO_5002642320|||http://purl.uniprot.org/annotation/PRO_5002642567|||http://purl.uniprot.org/annotation/PRO_5002642725|||http://purl.uniprot.org/annotation/PRO_5002642731|||http://purl.uniprot.org/annotation/PRO_5015097474|||http://purl.uniprot.org/annotation/PRO_5015098946|||http://purl.uniprot.org/annotation/VSP_005326|||http://purl.uniprot.org/annotation/VSP_005327|||http://purl.uniprot.org/annotation/VSP_005328|||http://purl.uniprot.org/annotation/VSP_005329|||http://purl.uniprot.org/annotation/VSP_007329|||http://purl.uniprot.org/annotation/VSP_007330|||http://purl.uniprot.org/annotation/VSP_007331|||http://purl.uniprot.org/annotation/VSP_007332|||http://purl.uniprot.org/annotation/VSP_007333|||http://purl.uniprot.org/annotation/VSP_007334|||http://purl.uniprot.org/annotation/VSP_007335|||http://purl.uniprot.org/annotation/VSP_007336|||http://purl.uniprot.org/annotation/VSP_007337|||http://purl.uniprot.org/annotation/VSP_007338|||http://purl.uniprot.org/annotation/VSP_007339 http://togogenome.org/gene/10090:Tsen34 ^@ http://purl.uniprot.org/uniprot/Q8BMZ5 ^@ 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 2.|||Polar residues|||tRNA-splicing endonuclease subunit Sen34 ^@ http://purl.uniprot.org/annotation/PRO_0000109464|||http://purl.uniprot.org/annotation/VSP_010987 http://togogenome.org/gene/10090:5430402E10Rik ^@ http://purl.uniprot.org/uniprot/Q9D3N5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5015099709 http://togogenome.org/gene/10090:Chmp4b ^@ http://purl.uniprot.org/uniprot/Q9D8B3 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Charged multivesicular body protein 4b|||Disordered|||Intramolecular interaction with C-terminus|||Intramolecular interaction with N-terminus|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000211490 http://togogenome.org/gene/10090:Lamtor2 ^@ http://purl.uniprot.org/uniprot/Q9JHS3 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Region|||Strand|||Turn ^@ Ragulator complex protein LAMTOR2|||Required for location at endosomes ^@ http://purl.uniprot.org/annotation/PRO_0000220961 http://togogenome.org/gene/10090:Foxn2 ^@ http://purl.uniprot.org/uniprot/E9Q7L6 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Fork-head ^@ http://togogenome.org/gene/10090:Siae ^@ http://purl.uniprot.org/uniprot/P70665 ^@ 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.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sialate O-acetylesterase large subunit|||Sialate O-acetylesterase small subunit ^@ http://purl.uniprot.org/annotation/PRO_0000022714|||http://purl.uniprot.org/annotation/PRO_0000022715|||http://purl.uniprot.org/annotation/VSP_004077|||http://purl.uniprot.org/annotation/VSP_018996|||http://purl.uniprot.org/annotation/VSP_018997 http://togogenome.org/gene/10090:Ubac1 ^@ http://purl.uniprot.org/uniprot/Q8VDI7 ^@ 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 strain: Czech II.|||N-acetylmethionine|||Polar residues|||STI1|||UBA 1|||UBA 2|||Ubiquitin-associated domain-containing protein 1|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000250450 http://togogenome.org/gene/10090:Cend1 ^@ http://purl.uniprot.org/uniprot/Q9JKC6 ^@ 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_0000064952 http://togogenome.org/gene/10090:Amacr ^@ http://purl.uniprot.org/uniprot/O09174 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Alpha-methylacyl-CoA racemase|||Disordered|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194706 http://togogenome.org/gene/10090:Irak1bp1 ^@ http://purl.uniprot.org/uniprot/Q9ESJ7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Interleukin-1 receptor-associated kinase 1-binding protein 1|||Phosphoserine|||Phosphothreonine|||Required for nuclear localization (NLS) ^@ http://purl.uniprot.org/annotation/PRO_0000313734 http://togogenome.org/gene/10090:Tmem132d ^@ http://purl.uniprot.org/uniprot/A0A0R4J0I2|||http://purl.uniprot.org/uniprot/Q76HP3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Transmembrane protein 132D|||Transmembrane protein TMEM132 C-terminal|||Transmembrane protein TMEM132 N-terminal|||Transmembrane protein family 132 middle ^@ http://purl.uniprot.org/annotation/PRO_0000287101|||http://purl.uniprot.org/annotation/PRO_5006451962 http://togogenome.org/gene/10090:Mia2 ^@ http://purl.uniprot.org/uniprot/A0A1W2P711|||http://purl.uniprot.org/uniprot/E9PY90|||http://purl.uniprot.org/uniprot/E9Q3S2|||http://purl.uniprot.org/uniprot/H3BK44|||http://purl.uniprot.org/uniprot/H3BK48 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_5010994076 http://togogenome.org/gene/10090:Sgsm2 ^@ http://purl.uniprot.org/uniprot/Q80U12 ^@ 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.|||Phosphoserine|||Polar residues|||RUN|||Rab-GAP TBC|||Small G protein signaling modulator 2 ^@ http://purl.uniprot.org/annotation/PRO_0000284663|||http://purl.uniprot.org/annotation/VSP_024599 http://togogenome.org/gene/10090:Adpgk ^@ http://purl.uniprot.org/uniprot/A0A1L1SSF2|||http://purl.uniprot.org/uniprot/Q8VDL4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ ADP-dependent glucokinase|||ADPK|||In isoform 2.|||In isoform 3.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000184777|||http://purl.uniprot.org/annotation/PRO_5009681993|||http://purl.uniprot.org/annotation/VSP_013555|||http://purl.uniprot.org/annotation/VSP_013556|||http://purl.uniprot.org/annotation/VSP_013557 http://togogenome.org/gene/10090:Snph ^@ http://purl.uniprot.org/uniprot/Q80U23 ^@ 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 ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Syntaphilin ^@ http://purl.uniprot.org/annotation/PRO_0000284137|||http://purl.uniprot.org/annotation/VSP_037439|||http://purl.uniprot.org/annotation/VSP_037440 http://togogenome.org/gene/10090:Pnma2 ^@ http://purl.uniprot.org/uniprot/Q8BHK0 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylalanine|||Paraneoplastic antigen Ma2 homolog|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000155204 http://togogenome.org/gene/10090:Tlcd1 ^@ http://purl.uniprot.org/uniprot/Q99JT6 ^@ Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||INTRAMEM|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||TLC|||TLC domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000285678|||http://purl.uniprot.org/annotation/VSP_024887|||http://purl.uniprot.org/annotation/VSP_024888|||http://purl.uniprot.org/annotation/VSP_024889|||http://purl.uniprot.org/annotation/VSP_024890 http://togogenome.org/gene/10090:Gm7592 ^@ http://purl.uniprot.org/uniprot/A0A668KLT6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Defa43 ^@ http://purl.uniprot.org/uniprot/D3YX03 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Alpha-defensin N-terminal|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015088520 http://togogenome.org/gene/10090:Foxd1 ^@ http://purl.uniprot.org/uniprot/Q61345 ^@ 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 D1|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000091812 http://togogenome.org/gene/10090:Spin2c ^@ http://purl.uniprot.org/uniprot/Q6NVE3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Region|||Site ^@ Basic residues|||Disordered|||Histone H3K4me3 and H3R8me2a binding|||Spindlin-2C|||Tudor-like domain 1|||Tudor-like domain 2|||Tudor-like domain 3 ^@ http://purl.uniprot.org/annotation/PRO_0000259590 http://togogenome.org/gene/10090:Erich5 ^@ http://purl.uniprot.org/uniprot/Q8K0S2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glutamate-rich protein 5|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000294434 http://togogenome.org/gene/10090:Hyal5 ^@ http://purl.uniprot.org/uniprot/Q812F3 ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Hyaluronidase-5|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000441636 http://togogenome.org/gene/10090:Ermardl2 ^@ http://purl.uniprot.org/uniprot/Q8C5D3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ DUF4209 ^@ http://togogenome.org/gene/10090:Plec ^@ http://purl.uniprot.org/uniprot/E9Q3W4|||http://purl.uniprot.org/uniprot/Q6S385|||http://purl.uniprot.org/uniprot/Q6S387|||http://purl.uniprot.org/uniprot/Q6S388|||http://purl.uniprot.org/uniprot/Q6S390|||http://purl.uniprot.org/uniprot/Q6S392|||http://purl.uniprot.org/uniprot/Q6S393|||http://purl.uniprot.org/uniprot/Q9QXS1 ^@ Chain|||Coiled-Coil|||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|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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 isoform PLEC-0,1C, isoform PLEC-0,1C,2A and isoform PLEC-0,1C,2A,3A.|||In isoform PLEC-0,1C, isoform PLEC-0,1C,2A,3A and isoform PLEC-0,1C,2A.|||In isoform PLEC-0,1C,2A,3A.|||In isoform PLEC-1, isoform PLEC-1A, isoform PLEC-1B, isoform PLEC-1D, isoform PLEC-1E, isoform PLEC-1G, isoform PLEC-1F and isoform PLEC-0,1C.|||In isoform PLEC-1A, isoform PLEC-1B and isoform PLEC-1B,2A.|||In isoform PLEC-1A.|||In isoform PLEC-1B and isoform PLEC-1B,2A.|||In isoform PLEC-1D and isoform PLEC-1D,2A.|||In isoform PLEC-1E and isoform PLEC-1E,2A.|||In isoform PLEC-1F.|||In isoform PLEC-1G.|||In isoform PLEC-1H.|||In isoform PLEC-1I.|||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_0000078136|||http://purl.uniprot.org/annotation/VSP_005032|||http://purl.uniprot.org/annotation/VSP_005033|||http://purl.uniprot.org/annotation/VSP_005034|||http://purl.uniprot.org/annotation/VSP_005035|||http://purl.uniprot.org/annotation/VSP_005036|||http://purl.uniprot.org/annotation/VSP_005037|||http://purl.uniprot.org/annotation/VSP_005038|||http://purl.uniprot.org/annotation/VSP_005039|||http://purl.uniprot.org/annotation/VSP_005040|||http://purl.uniprot.org/annotation/VSP_005041|||http://purl.uniprot.org/annotation/VSP_005042|||http://purl.uniprot.org/annotation/VSP_005043|||http://purl.uniprot.org/annotation/VSP_005044|||http://purl.uniprot.org/annotation/VSP_005045|||http://purl.uniprot.org/annotation/VSP_005046|||http://purl.uniprot.org/annotation/VSP_005047|||http://purl.uniprot.org/annotation/VSP_005048|||http://purl.uniprot.org/annotation/VSP_005049 http://togogenome.org/gene/10090:Rbfox1 ^@ http://purl.uniprot.org/uniprot/Q9JJ43 ^@ 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 ^@ Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||In isoform 3, isoform 6 and isoform 7.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 7.|||Interaction with RNA|||Omega-N-methylarginine|||Polar residues|||RNA binding protein fox-1 homolog 1|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081481|||http://purl.uniprot.org/annotation/VSP_030879|||http://purl.uniprot.org/annotation/VSP_030880|||http://purl.uniprot.org/annotation/VSP_030881|||http://purl.uniprot.org/annotation/VSP_030882|||http://purl.uniprot.org/annotation/VSP_030883|||http://purl.uniprot.org/annotation/VSP_030884 http://togogenome.org/gene/10090:Bhlhe23 ^@ http://purl.uniprot.org/uniprot/Q0VEJ8|||http://purl.uniprot.org/uniprot/Q8BGW3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ BHLH|||Basic and acidic residues|||Class E basic helix-loop-helix protein 23|||Disordered|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000245527 http://togogenome.org/gene/10090:Vmn1r129 ^@ http://purl.uniprot.org/uniprot/E9QA94 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or51g2 ^@ http://purl.uniprot.org/uniprot/Q8VH11 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tmem199 ^@ http://purl.uniprot.org/uniprot/B2RV69|||http://purl.uniprot.org/uniprot/Q5SYH2 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Transmembrane ^@ Helical|||N-acetylalanine|||Removed|||Transmembrane protein 199 ^@ http://purl.uniprot.org/annotation/PRO_0000079299 http://togogenome.org/gene/10090:Agk ^@ http://purl.uniprot.org/uniprot/Q9ESW4 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Acylglycerol kinase, mitochondrial|||DAGKc|||Disordered|||Hydrophobic|||In isoform 2.|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000252381|||http://purl.uniprot.org/annotation/VSP_020927 http://togogenome.org/gene/10090:Vmn1r197 ^@ http://purl.uniprot.org/uniprot/Q8R265 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Esrrb ^@ http://purl.uniprot.org/uniprot/E9QKA2|||http://purl.uniprot.org/uniprot/G5E8P8|||http://purl.uniprot.org/uniprot/Q61539|||http://purl.uniprot.org/uniprot/Q80VS1|||http://purl.uniprot.org/uniprot/Q8CCV5 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Disordered|||Essential for ESRRB transcriptional activity and interaction with NCOA3|||Important for stabilizing DNA-binding|||Interaction with NANOG|||Loss of self-renewal in embryonic stem cells in absence of LIF. Does not interact with NCOA3.|||Loss of self-renewal in embryonic stem cells in absence of LIF; when associated with A-424. Does not interact with NCOA3; when associated with A-424.|||Loss of self-renewal in embryonic stem cells in absence of LIF; when associated with A-425. Does not interact with NCOA3; when associated with A-425.|||NR C4-type|||NR LBD|||Nuclear receptor|||Polar residues|||Steroid hormone receptor ERR2 ^@ http://purl.uniprot.org/annotation/PRO_0000053663 http://togogenome.org/gene/10090:Lor ^@ http://purl.uniprot.org/uniprot/P18165 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Loricrin|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084459 http://togogenome.org/gene/10090:Nmrk1 ^@ http://purl.uniprot.org/uniprot/Q91W63 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Nicotinamide riboside kinase 1|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000215892 http://togogenome.org/gene/10090:Camk1d ^@ http://purl.uniprot.org/uniprot/B1AW58|||http://purl.uniprot.org/uniprot/Q3TDM2|||http://purl.uniprot.org/uniprot/Q3UH04|||http://purl.uniprot.org/uniprot/Q8BW96 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||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|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase type 1D|||Calmodulin-binding|||Catalytically inactive form.|||Constitutively active form; when associated with 289-A--A-292.|||Constitutively active form; when associated with A-301.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Nuclear export signal|||Phosphoserine|||Phosphothreonine; by CaMKK1 and CaMKK2|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086083|||http://purl.uniprot.org/annotation/VSP_012136|||http://purl.uniprot.org/annotation/VSP_012137 http://togogenome.org/gene/10090:Cfap74 ^@ http://purl.uniprot.org/uniprot/G3UWF6|||http://purl.uniprot.org/uniprot/Q3UY96 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Splice Variant ^@ Cilia- and flagella-associated protein 74|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000324665|||http://purl.uniprot.org/annotation/VSP_057371|||http://purl.uniprot.org/annotation/VSP_057372 http://togogenome.org/gene/10090:Mtfr1l ^@ http://purl.uniprot.org/uniprot/Q9CWE0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Mitochondrial fission regulator 1-like|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000341567|||http://purl.uniprot.org/annotation/VSP_034340 http://togogenome.org/gene/10090:Defb30 ^@ http://purl.uniprot.org/uniprot/Q30KN4 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 30 ^@ http://purl.uniprot.org/annotation/PRO_0000352710 http://togogenome.org/gene/10090:Zfp473 ^@ http://purl.uniprot.org/uniprot/Q4VA40|||http://purl.uniprot.org/uniprot/Q8BI67 ^@ 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 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 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 473 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000047605 http://togogenome.org/gene/10090:Dcaf12 ^@ http://purl.uniprot.org/uniprot/Q8BGZ3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ DDB1- and CUL4-associated factor 12|||Disordered|||Phosphoserine|||Required for nuclear location and interaction with MOV10|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000306842 http://togogenome.org/gene/10090:Ggta1 ^@ http://purl.uniprot.org/uniprot/P23336|||http://purl.uniprot.org/uniprot/Q3TXW0|||http://purl.uniprot.org/uniprot/Q8C2H7|||http://purl.uniprot.org/uniprot/Q91W00|||http://purl.uniprot.org/uniprot/Q9DBU1 ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 3.|||Lumenal|||N-acetyllactosaminide alpha-1,3-galactosyltransferase|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000157299|||http://purl.uniprot.org/annotation/VSP_001804|||http://purl.uniprot.org/annotation/VSP_001805 http://togogenome.org/gene/10090:Rpl37a ^@ http://purl.uniprot.org/uniprot/P61514 ^@ 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_0000139818 http://togogenome.org/gene/10090:Myrf ^@ http://purl.uniprot.org/uniprot/Q3UR85 ^@ 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|||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|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes DNA-binding.|||Abolishes nuclear localization.|||Cleavage; by autolysis|||Cytoplasmic|||Disordered|||Does not affect autocatalytic cleavage and generation of Myelin regulatory factor, N-terminal part.|||Does not affect subcellular location. Impaired DNA-binding.|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of trimerization; when associated with 439-E--L-441 DEL.|||Loss of trimerization; when associated with R-469.|||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|||Polar residues|||Prevents autocatalytic cleavage and generation of Myelin regulatory factor, N-terminal part.|||Pro residues|||Required for interaction with TMEM98 ^@ http://purl.uniprot.org/annotation/PRO_0000318920|||http://purl.uniprot.org/annotation/PRO_0000424312|||http://purl.uniprot.org/annotation/PRO_0000424313|||http://purl.uniprot.org/annotation/VSP_031303|||http://purl.uniprot.org/annotation/VSP_031304|||http://purl.uniprot.org/annotation/VSP_053374|||http://purl.uniprot.org/annotation/VSP_053992|||http://purl.uniprot.org/annotation/VSP_053993 http://togogenome.org/gene/10090:Cldn34b1 ^@ http://purl.uniprot.org/uniprot/B1AZQ8 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015087041 http://togogenome.org/gene/10090:Oasl2 ^@ http://purl.uniprot.org/uniprot/Q9Z2F2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ 2'-5'-oligoadenylate synthase-like protein 2|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000160267 http://togogenome.org/gene/10090:Exoc8 ^@ http://purl.uniprot.org/uniprot/Q6PGF7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Exocyst complex component 8|||PH|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000227551 http://togogenome.org/gene/10090:Sun1 ^@ http://purl.uniprot.org/uniprot/Q9D666 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Disordered|||EMD-binding|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interchain (with KASH domain-containing nesprins)|||LMNA-binding|||Nuclear|||Perinuclear space|||Phosphoserine|||Polar residues|||SUN|||SUN domain-containing protein 1|||SYNE2-binding|||Sufficient for interaction with SYNE1 and SYNE2 ^@ http://purl.uniprot.org/annotation/PRO_0000218912|||http://purl.uniprot.org/annotation/VSP_009346|||http://purl.uniprot.org/annotation/VSP_009347|||http://purl.uniprot.org/annotation/VSP_039552|||http://purl.uniprot.org/annotation/VSP_058699 http://togogenome.org/gene/10090:S1pr2 ^@ http://purl.uniprot.org/uniprot/P52592 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||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|||Sphingosine 1-phosphate receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000069428 http://togogenome.org/gene/10090:Ube2w ^@ http://purl.uniprot.org/uniprot/Q3V321|||http://purl.uniprot.org/uniprot/Q8VDW4 ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Mutagenesis Site|||Sequence Conflict ^@ Glycyl thioester intermediate|||Loss of in vitro ubiquitin-conjugating activity.|||Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)|||UBC core|||Ubiquitin-conjugating enzyme E2 W ^@ http://purl.uniprot.org/annotation/PRO_0000232690 http://togogenome.org/gene/10090:BC016579 ^@ http://purl.uniprot.org/uniprot/E9QP50|||http://purl.uniprot.org/uniprot/Q8C5C9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||TPA-induced transmembrane protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000248025 http://togogenome.org/gene/10090:Abt1 ^@ http://purl.uniprot.org/uniprot/Q9QYL7 ^@ 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 ^@ Activator of basal transcription 1|||Basic and acidic residues|||Disordered|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000233169 http://togogenome.org/gene/10090:Ctse ^@ http://purl.uniprot.org/uniprot/P70269 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cathepsin E|||Interchain|||N-linked (GlcNAc...) asparagine|||Peptidase A1 ^@ http://purl.uniprot.org/annotation/PRO_0000025976|||http://purl.uniprot.org/annotation/PRO_0000025977 http://togogenome.org/gene/10090:Itga6 ^@ http://purl.uniprot.org/uniprot/Q61739|||http://purl.uniprot.org/uniprot/Q6PEE8|||http://purl.uniprot.org/uniprot/Q8CC06 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Repeat|||Sequence Conflict|||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|||GFFKR motif|||Helical|||In isoform Alpha-6X1A.|||Integrin alpha-2|||Integrin alpha-2 domain-containing protein|||Integrin alpha-6|||Integrin alpha-6 heavy chain|||Integrin alpha-6 light chain|||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_0000016261|||http://purl.uniprot.org/annotation/PRO_0000016262|||http://purl.uniprot.org/annotation/PRO_0000016263|||http://purl.uniprot.org/annotation/PRO_0000448082|||http://purl.uniprot.org/annotation/PRO_5001426099|||http://purl.uniprot.org/annotation/PRO_5001426215|||http://purl.uniprot.org/annotation/VSP_002726 http://togogenome.org/gene/10090:Ankrd29 ^@ http://purl.uniprot.org/uniprot/D3YVV3|||http://purl.uniprot.org/uniprot/Q3TS37 ^@ Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Non-terminal Residue|||Repeat ^@ ANK ^@ http://togogenome.org/gene/10090:Fbxo11 ^@ http://purl.uniprot.org/uniprot/Q7TPD1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||F-box|||F-box only protein 11|||In Jeff mutant; heterozygotes are deaf with chronic proliferative otitis media, have a shortened snout and occipital region, and are smaller than wild-type littermates. Homozygotes demonstrate perinatal lethality due to respiratory problems, are born with upper eyelids open and show clefting of the hard or soft palate as well as facial clefting.|||In Mutt mutant; 13% of heterozygotes show a reduced startle response to a toneburst of 24 kHz and a mild craniofacial abnormality. 17% of homozygotes show perinatal lethality. Surviving homozygotes demonstrate a marked craniofacial abnormality and reduced hearing.|||In isoform 2 and isoform 3.|||In isoform 3.|||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_0000119891|||http://purl.uniprot.org/annotation/VSP_053353|||http://purl.uniprot.org/annotation/VSP_053354 http://togogenome.org/gene/10090:Tmod2 ^@ http://purl.uniprot.org/uniprot/Q9JKK7 ^@ 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|||Tropomodulin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000186132|||http://purl.uniprot.org/annotation/VSP_024895|||http://purl.uniprot.org/annotation/VSP_024896|||http://purl.uniprot.org/annotation/VSP_024897 http://togogenome.org/gene/10090:Ramp2 ^@ http://purl.uniprot.org/uniprot/Q9WUP0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Receptor activity-modifying protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000030173 http://togogenome.org/gene/10090:Wnt16 ^@ http://purl.uniprot.org/uniprot/Q8BRT3|||http://purl.uniprot.org/uniprot/Q8C6P4|||http://purl.uniprot.org/uniprot/Q9QYS1 ^@ 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|||Protein Wnt-16 ^@ http://purl.uniprot.org/annotation/PRO_0000041472|||http://purl.uniprot.org/annotation/PRO_5004303989|||http://purl.uniprot.org/annotation/PRO_5015099051 http://togogenome.org/gene/10090:Kcnk13 ^@ http://purl.uniprot.org/uniprot/Q3TYG8|||http://purl.uniprot.org/uniprot/Q8R1P5 ^@ Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||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|||Potassium channel subfamily K member 13 ^@ http://purl.uniprot.org/annotation/PRO_0000101763 http://togogenome.org/gene/10090:Elavl3 ^@ http://purl.uniprot.org/uniprot/Q60900 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn ^@ ELAV-like protein 3|||In isoform HuC-S.|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000081582|||http://purl.uniprot.org/annotation/VSP_005790 http://togogenome.org/gene/10090:Prkab2 ^@ http://purl.uniprot.org/uniprot/Q6PAM0 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ 5'-AMP-activated protein kinase subunit beta-2|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphoserine; by ULK1|||Phosphothreonine|||Phosphothreonine; by ULK1 ^@ http://purl.uniprot.org/annotation/PRO_0000204369 http://togogenome.org/gene/10090:Lrrc51 ^@ http://purl.uniprot.org/uniprot/Q9DAK8 ^@ 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|||LRRCT|||Leucine-rich repeat-containing protein 51 ^@ http://purl.uniprot.org/annotation/PRO_0000225501|||http://purl.uniprot.org/annotation/VSP_036897 http://togogenome.org/gene/10090:Gm14440 ^@ http://purl.uniprot.org/uniprot/A2BDM8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB ^@ http://togogenome.org/gene/10090:Tm9sf2 ^@ http://purl.uniprot.org/uniprot/P58021|||http://purl.uniprot.org/uniprot/Q542E4 ^@ 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_0000034366|||http://purl.uniprot.org/annotation/PRO_5014205863 http://togogenome.org/gene/10090:Sprtn ^@ http://purl.uniprot.org/uniprot/G3X912 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Basic and acidic residues|||Cleavage; by autolysis|||DNA-dependent metalloprotease SPRTN|||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|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization signal|||PIP-box|||Phosphoserine|||Polar residues|||SHP-box|||SprT-like|||UBZ4-type ^@ http://purl.uniprot.org/annotation/PRO_0000419484 http://togogenome.org/gene/10090:Or6c33 ^@ http://purl.uniprot.org/uniprot/Q8VFU5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Crip2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JF37|||http://purl.uniprot.org/uniprot/Q4FJU3|||http://purl.uniprot.org/uniprot/Q9DCT8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Cysteine-rich protein 2|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000075711 http://togogenome.org/gene/10090:Stmn3 ^@ http://purl.uniprot.org/uniprot/O70166|||http://purl.uniprot.org/uniprot/Q545T6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent|||Lipid Binding|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||S-palmitoyl cysteine|||SLD|||Stathmin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000182403 http://togogenome.org/gene/10090:Zdhhc14 ^@ http://purl.uniprot.org/uniprot/Q8BQQ1 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Disordered|||Helical|||In isoform 2.|||Lumenal|||Palmitoyltransferase ZDHHC14|||Phosphoserine|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212892|||http://purl.uniprot.org/annotation/VSP_016272 http://togogenome.org/gene/10090:Nop10 ^@ http://purl.uniprot.org/uniprot/Q9CQS2 ^@ Chain|||Molecule Processing ^@ Chain ^@ H/ACA ribonucleoprotein complex subunit 3 ^@ http://purl.uniprot.org/annotation/PRO_0000149002 http://togogenome.org/gene/10090:Adamts16 ^@ http://purl.uniprot.org/uniprot/Q69Z28 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ A disintegrin and metalloproteinase with thrombospondin motifs 16|||Cysteine switch|||Disintegrin|||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|||TSP type-1 6|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029196|||http://purl.uniprot.org/annotation/PRO_0000029197|||http://purl.uniprot.org/annotation/VSP_014991|||http://purl.uniprot.org/annotation/VSP_014992 http://togogenome.org/gene/10090:Tlr5 ^@ http://purl.uniprot.org/uniprot/A0A0A6YVY4|||http://purl.uniprot.org/uniprot/Q05AH3|||http://purl.uniprot.org/uniprot/Q8CB40|||http://purl.uniprot.org/uniprot/Q9JLF7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In strain: MOLF/Ei.|||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|||Phosphotyrosine|||TIR|||Toll-like receptor 5 ^@ http://purl.uniprot.org/annotation/PRO_0000034730 http://togogenome.org/gene/10090:Glipr1 ^@ http://purl.uniprot.org/uniprot/Q4QQK5|||http://purl.uniprot.org/uniprot/Q9CWG1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Glioma pathogenesis-related protein 1|||Helical|||SCP ^@ http://purl.uniprot.org/annotation/PRO_0000006271|||http://purl.uniprot.org/annotation/PRO_5014309400 http://togogenome.org/gene/10090:Ncf4 ^@ http://purl.uniprot.org/uniprot/P97369 ^@ 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 ^@ Neutrophil cytosol factor 4|||PB1|||PX|||Phosphoserine|||Phosphothreonine|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000096765 http://togogenome.org/gene/10090:Aldh4a1 ^@ http://purl.uniprot.org/uniprot/Q8CHT0 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Phosphoserine|||Proton acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000007174 http://togogenome.org/gene/10090:Grik1 ^@ http://purl.uniprot.org/uniprot/Q3UZT1|||http://purl.uniprot.org/uniprot/Q8BQZ0|||http://purl.uniprot.org/uniprot/Q8BRT2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding ^@ http://togogenome.org/gene/10090:Dok7 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0R2|||http://purl.uniprot.org/uniprot/Q18PE0 ^@ 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 ^@ Abolishes interaction with MUSK and function; when associated with A-158 and A-159.|||Abolishes interaction with MUSK and function; when associated with A-174.|||Basic and acidic residues|||Disordered|||IRS-type PTB|||In isoform 2.|||In isoform 3.|||PH|||Polar residues|||Protein Dok-7 ^@ http://purl.uniprot.org/annotation/PRO_0000250372|||http://purl.uniprot.org/annotation/VSP_020636|||http://purl.uniprot.org/annotation/VSP_020637 http://togogenome.org/gene/10090:Or5be3 ^@ http://purl.uniprot.org/uniprot/Q7TR58 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp207 ^@ http://purl.uniprot.org/uniprot/Q9JMD0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger ^@ Abolishes interaction and stabilization of BUB3.|||BUB3-interacting and GLEBS motif-containing protein ZNF207|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||GLEBS|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Microtubule-binding region|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000428733|||http://purl.uniprot.org/annotation/VSP_054255|||http://purl.uniprot.org/annotation/VSP_054256|||http://purl.uniprot.org/annotation/VSP_054257 http://togogenome.org/gene/10090:Zfp600 ^@ http://purl.uniprot.org/uniprot/A2A7V0|||http://purl.uniprot.org/uniprot/Q32P07 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Gulo ^@ http://purl.uniprot.org/uniprot/P58710 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ FAD-binding PCMH-type|||Helical|||L-gulonolactone oxidase|||Pros-8alpha-FAD histidine ^@ http://purl.uniprot.org/annotation/PRO_0000128159 http://togogenome.org/gene/10090:Crym ^@ http://purl.uniprot.org/uniprot/O54983 ^@ Binding Site|||Chain|||Helix|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Strand|||Turn ^@ Ketimine reductase mu-crystallin ^@ http://purl.uniprot.org/annotation/PRO_0000200679 http://togogenome.org/gene/10090:Grid1 ^@ http://purl.uniprot.org/uniprot/Q61627 ^@ 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 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes dimerization. Weakly interacts with C1q domain of CBLN1.|||Cytoplasmic|||Disordered|||Essential for dimerization|||Extracellular|||Glutamate receptor ionotropic, delta-1|||Helical|||Interaction with CBLN1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000011562 http://togogenome.org/gene/10090:St6galnac5 ^@ http://purl.uniprot.org/uniprot/Q6GTI0|||http://purl.uniprot.org/uniprot/Q9QYJ1 ^@ 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 5|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In strain: C57BL/6J.|||In strain: C57BL/6N and C57BL/6J.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000149281 http://togogenome.org/gene/10090:Gpsm3 ^@ http://purl.uniprot.org/uniprot/Q0VGT5|||http://purl.uniprot.org/uniprot/Q3U1Z5 ^@ 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|||G-protein-signaling modulator 3|||GoLoco 1|||GoLoco 2|||GoLoco 3|||In isoform 2.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000233718|||http://purl.uniprot.org/annotation/VSP_018153|||http://purl.uniprot.org/annotation/VSP_018154 http://togogenome.org/gene/10090:Ntn5 ^@ http://purl.uniprot.org/uniprot/Q3UQ22|||http://purl.uniprot.org/uniprot/S4R1A5|||http://purl.uniprot.org/uniprot/S4R1X6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 2|||N-linked (GlcNAc...) asparagine|||NTR|||Netrin-5 ^@ http://purl.uniprot.org/annotation/PRO_0000320576|||http://purl.uniprot.org/annotation/PRO_5004522284 http://togogenome.org/gene/10090:Impact ^@ http://purl.uniprot.org/uniprot/O55091 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Protein IMPACT|||RWD ^@ http://purl.uniprot.org/annotation/PRO_0000330851 http://togogenome.org/gene/10090:Nmt1 ^@ http://purl.uniprot.org/uniprot/O70310|||http://purl.uniprot.org/uniprot/Q3UJC3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycylpeptide N-tetradecanoyltransferase 1|||Glycylpeptide N-tetradecanoyltransferase C-terminal|||Glycylpeptide N-tetradecanoyltransferase N-terminal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000064222 http://togogenome.org/gene/10090:Htatsf1 ^@ http://purl.uniprot.org/uniprot/Q8BGC0 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HIV Tat-specific factor 1 homolog|||In isoform 2.|||Mediates interaction with the P-TEFb complex|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||RRM 1|||RRM 2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000248605|||http://purl.uniprot.org/annotation/VSP_020332|||http://purl.uniprot.org/annotation/VSP_020333 http://togogenome.org/gene/10090:Adh7 ^@ http://purl.uniprot.org/uniprot/Q64437|||http://purl.uniprot.org/uniprot/Q9D748 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ All-trans-retinol dehydrogenase [NAD(+)] ADH7|||Enoyl reductase (ER) ^@ http://purl.uniprot.org/annotation/PRO_0000160692 http://togogenome.org/gene/10090:Ostn ^@ http://purl.uniprot.org/uniprot/P61364 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Signal Peptide ^@ Chain|||Modified Residue|||Mutagenesis Site|||Peptide|||Signal Peptide ^@ Abolishes processing of the protein.|||Arginine amide|||Osteocrin|||Processed Osteocrin ^@ http://purl.uniprot.org/annotation/PRO_0000021968|||http://purl.uniprot.org/annotation/PRO_0000439030 http://togogenome.org/gene/10090:Tnfrsf22 ^@ http://purl.uniprot.org/uniprot/Q9ER62 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 22 ^@ http://purl.uniprot.org/annotation/PRO_0000058937|||http://purl.uniprot.org/annotation/VSP_007648 http://togogenome.org/gene/10090:Marchf8 ^@ http://purl.uniprot.org/uniprot/A0A0N4SV35|||http://purl.uniprot.org/uniprot/A0A0N4SVK0|||http://purl.uniprot.org/uniprot/Q9DBD2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase MARCHF8|||Helical|||Phosphoserine|||Polar residues|||RING-CH-type|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000274371 http://togogenome.org/gene/10090:Rragd ^@ http://purl.uniprot.org/uniprot/B1AWT2|||http://purl.uniprot.org/uniprot/Q7TT45 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Ras-related GTP-binding protein D ^@ http://purl.uniprot.org/annotation/PRO_0000239954 http://togogenome.org/gene/10090:Prxl2c ^@ http://purl.uniprot.org/uniprot/Q9D1A0 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Peroxiredoxin-like 2C ^@ http://purl.uniprot.org/annotation/PRO_0000221625 http://togogenome.org/gene/10090:Ets2 ^@ http://purl.uniprot.org/uniprot/P15037|||http://purl.uniprot.org/uniprot/Q3UP99 ^@ Chain|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||ETS|||PNT|||Phosphoserine|||Protein C-ets-2 ^@ http://purl.uniprot.org/annotation/PRO_0000204078 http://togogenome.org/gene/10090:Sox3 ^@ http://purl.uniprot.org/uniprot/A2AM37|||http://purl.uniprot.org/uniprot/Q5RKW0 ^@ DNA Binding|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ DNA Binding|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||HMG box ^@ http://togogenome.org/gene/10090:Lmntd1 ^@ http://purl.uniprot.org/uniprot/E9Q8Y6|||http://purl.uniprot.org/uniprot/Q9D4C1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||LTD|||Lamin tail domain-containing protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317249 http://togogenome.org/gene/10090:Vegfc ^@ http://purl.uniprot.org/uniprot/P97953 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ 1|||2|||3|||4|||4 X 16 AA repeats of C-X(10)-C-X-C-X(1,3)-C|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interchain|||N-linked (GlcNAc...) asparagine|||Vascular endothelial growth factor C ^@ http://purl.uniprot.org/annotation/PRO_0000023403|||http://purl.uniprot.org/annotation/PRO_0000023404|||http://purl.uniprot.org/annotation/PRO_0000023405|||http://purl.uniprot.org/annotation/VSP_053477|||http://purl.uniprot.org/annotation/VSP_053478|||http://purl.uniprot.org/annotation/VSP_053479|||http://purl.uniprot.org/annotation/VSP_053480|||http://purl.uniprot.org/annotation/VSP_053481|||http://purl.uniprot.org/annotation/VSP_053482 http://togogenome.org/gene/10090:2510039O18Rik ^@ http://purl.uniprot.org/uniprot/Q91X21 ^@ 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 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Uncharacterized protein KIAA2013 ^@ http://purl.uniprot.org/annotation/PRO_0000293469|||http://purl.uniprot.org/annotation/VSP_026488|||http://purl.uniprot.org/annotation/VSP_026489 http://togogenome.org/gene/10090:Tab1 ^@ http://purl.uniprot.org/uniprot/Q8CF89 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Disordered|||O-linked (GlcNAc) serine|||PPM-type phosphatase|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with MAP3K7|||TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000057798 http://togogenome.org/gene/10090:Rad51b ^@ http://purl.uniprot.org/uniprot/O35719 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Region|||Sequence Conflict|||Splice Variant ^@ DNA repair protein RAD51 homolog 2|||In isoform 2.|||Interaction with RAD51C ^@ http://purl.uniprot.org/annotation/PRO_0000122940|||http://purl.uniprot.org/annotation/VSP_008869|||http://purl.uniprot.org/annotation/VSP_008870 http://togogenome.org/gene/10090:Vangl1 ^@ http://purl.uniprot.org/uniprot/Q80Z96 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Phosphoserine|||Polar residues|||Vang-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000186194 http://togogenome.org/gene/10090:2610044O15Rik8 ^@ http://purl.uniprot.org/uniprot/Q8BG62 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB ^@ http://togogenome.org/gene/10090:Hectd2 ^@ http://purl.uniprot.org/uniprot/B2RPZ5|||http://purl.uniprot.org/uniprot/Q8CDU6 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl thioester intermediate|||HECT|||Phosphoserine|||Probable E3 ubiquitin-protein ligase HECTD2 ^@ http://purl.uniprot.org/annotation/PRO_0000240852 http://togogenome.org/gene/10090:Tmem150a ^@ http://purl.uniprot.org/uniprot/Q91WN2 ^@ 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 150A ^@ http://purl.uniprot.org/annotation/PRO_0000274776 http://togogenome.org/gene/10090:Frmd8 ^@ http://purl.uniprot.org/uniprot/Q3UFK8 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||FERM|||FERM domain-containing protein 8|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000295779 http://togogenome.org/gene/10090:Or2b28 ^@ http://purl.uniprot.org/uniprot/Q8VFG2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lenep ^@ http://purl.uniprot.org/uniprot/Q9WVB6 ^@ Chain|||Molecule Processing ^@ Chain ^@ Lens epithelial cell protein LEP503 ^@ http://purl.uniprot.org/annotation/PRO_0000084404 http://togogenome.org/gene/10090:Scarf1 ^@ http://purl.uniprot.org/uniprot/Q5ND28|||http://purl.uniprot.org/uniprot/Q68EF1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Scavenger receptor class F member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000407314|||http://purl.uniprot.org/annotation/PRO_5004269601 http://togogenome.org/gene/10090:Dpysl3 ^@ http://purl.uniprot.org/uniprot/E9PWE8|||http://purl.uniprot.org/uniprot/Q3TT92|||http://purl.uniprot.org/uniprot/Q62188 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Amidohydrolase-related|||Basic and acidic residues|||Dihydropyrimidinase-related protein 3|||Disordered|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphoserine; by GSK3|||Phosphothreonine|||Phosphothreonine; by GSK3|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000165918 http://togogenome.org/gene/10090:Zfp871 ^@ http://purl.uniprot.org/uniprot/G5E905|||http://purl.uniprot.org/uniprot/Q80T67|||http://purl.uniprot.org/uniprot/Q80XN4 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Igfbp6 ^@ http://purl.uniprot.org/uniprot/P47880 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||IGFBP N-terminal|||Insulin-like growth factor-binding protein 6|||Polar residues|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000014390 http://togogenome.org/gene/10090:Fscn2 ^@ http://purl.uniprot.org/uniprot/Q32M02 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant ^@ Chain|||Sequence Conflict|||Sequence Variant ^@ Fascin-2|||In prebycusis phenotype; when associated with waltzer cadherin 23 mutant. ^@ http://purl.uniprot.org/annotation/PRO_0000404202 http://togogenome.org/gene/10090:Med26 ^@ http://purl.uniprot.org/uniprot/Q7TN02 ^@ 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|||Mediator of RNA polymerase II transcription subunit 26|||Phosphoserine|||Polar residues|||Pro residues|||TFIIS N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000304959 http://togogenome.org/gene/10090:Or2i1 ^@ http://purl.uniprot.org/uniprot/Q6UAH0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ascl3 ^@ http://purl.uniprot.org/uniprot/Q9JJR7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Achaete-scute homolog 3|||Basic motif|||Disordered|||Helix-loop-helix motif|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127134 http://togogenome.org/gene/10090:Stk36 ^@ http://purl.uniprot.org/uniprot/Q69ZM6 ^@ 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|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 36 ^@ http://purl.uniprot.org/annotation/PRO_0000229021|||http://purl.uniprot.org/annotation/VSP_040760|||http://purl.uniprot.org/annotation/VSP_040761|||http://purl.uniprot.org/annotation/VSP_040762|||http://purl.uniprot.org/annotation/VSP_040763 http://togogenome.org/gene/10090:Kcnc3 ^@ http://purl.uniprot.org/uniprot/A0A140LIW8|||http://purl.uniprot.org/uniprot/Q63959 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ BTB|||Cytoplasmic|||Disordered|||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|||Important for normal N-type inactivation|||Loss of channel activity. Functions as dominant negative mutation that impairs function of wild-type channel subunits. Causes impaired Purkinje cell dendrite growth and premature death of cerebellar Purkinje cells.|||N-linked (GlcNAc...) asparagine|||No effect on voltage-dependent channel opening or current amplitude, but decreased rate of inactivation during prolonged depolarization.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Potassium voltage-gated channel subfamily C member 3|||Pro residues|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054056 http://togogenome.org/gene/10090:Dync1li1 ^@ http://purl.uniprot.org/uniprot/Q3TWG5|||http://purl.uniprot.org/uniprot/Q8R1Q8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Cytoplasmic dynein 1 light intermediate chain 1|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000114667 http://togogenome.org/gene/10090:Atr ^@ http://purl.uniprot.org/uniprot/A0A1L1SSL9|||http://purl.uniprot.org/uniprot/E9QPK4 ^@ Domain Extent|||Region|||Repeat ^@ Domain Extent|||Region|||Repeat ^@ Disordered|||FAT|||FATC|||HEAT|||PI3K/PI4K catalytic ^@ http://togogenome.org/gene/10090:Alkbh4 ^@ http://purl.uniprot.org/uniprot/Q9D8F1 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Splice Variant ^@ Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4|||Fe2OG dioxygenase|||In isoform 2.|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000239282|||http://purl.uniprot.org/annotation/VSP_019129 http://togogenome.org/gene/10090:Pla2g4a ^@ http://purl.uniprot.org/uniprot/P47713|||http://purl.uniprot.org/uniprot/Q3UMQ1|||http://purl.uniprot.org/uniprot/Q9DBX5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||C2|||Cytosolic phospholipase A2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nucleophile|||PLA2c|||Phospholipid binding|||Phosphoserine|||Phosphoserine; by MAPK|||Phosphothreonine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000187263 http://togogenome.org/gene/10090:Nt5e ^@ http://purl.uniprot.org/uniprot/Q0VEE0|||http://purl.uniprot.org/uniprot/Q61503 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide|||Site|||Transmembrane ^@ 5'-Nucleotidase C-terminal|||5'-nucleotidase|||Calcineurin-like phosphoesterase|||GPI-anchor amidated serine|||Helical|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000000017|||http://purl.uniprot.org/annotation/PRO_0000000018|||http://purl.uniprot.org/annotation/PRO_5014205724 http://togogenome.org/gene/10090:Tmem231 ^@ http://purl.uniprot.org/uniprot/Q3U284 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 231 ^@ http://purl.uniprot.org/annotation/PRO_0000317521 http://togogenome.org/gene/10090:Or4p22 ^@ http://purl.uniprot.org/uniprot/Q8VG86 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:5031439G07Rik ^@ http://purl.uniprot.org/uniprot/B1APX2|||http://purl.uniprot.org/uniprot/Q3UE31 ^@ 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|||Phosphothreonine|||Polar residues|||Uncharacterized protein KIAA0930 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000255939 http://togogenome.org/gene/10090:H2az2 ^@ http://purl.uniprot.org/uniprot/B2RVP5|||http://purl.uniprot.org/uniprot/Q3THW5|||http://purl.uniprot.org/uniprot/Q8R029 ^@ 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 ^@ Disordered|||Histone H2A C-terminal|||Histone H2A.V|||Histone H2A/H2B/H3|||N6-acetyllysine|||N6-lactoyllysine|||N6-lactoyllysine; alternate|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000239069 http://togogenome.org/gene/10090:Eepd1 ^@ http://purl.uniprot.org/uniprot/Q3TGW2 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Endonuclease/exonuclease/phosphatase family domain-containing protein 1|||HhH|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000317262 http://togogenome.org/gene/10090:Magt1 ^@ http://purl.uniprot.org/uniprot/A2ADH1|||http://purl.uniprot.org/uniprot/Q9CQY5 ^@ 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|||Helical|||In isoform 2.|||In isoform 3.|||Magnesium transporter protein 1|||N-linked (GlcNAc...) asparagine|||Redox-active|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000246058|||http://purl.uniprot.org/annotation/VSP_019822|||http://purl.uniprot.org/annotation/VSP_019823 http://togogenome.org/gene/10090:Bend3 ^@ http://purl.uniprot.org/uniprot/Q6PAL0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Strand ^@ BEN 1|||BEN 2|||BEN 3|||BEN 4|||BEN domain-containing protein 3|||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|||Nuclear localization signal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000290201 http://togogenome.org/gene/10090:Robo2 ^@ http://purl.uniprot.org/uniprot/Q19AB2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Fibronectin type-III|||Helical|||Ig-like|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015097045 http://togogenome.org/gene/10090:Sh2d2a ^@ http://purl.uniprot.org/uniprot/Q5D0E4|||http://purl.uniprot.org/uniprot/Q9QXK9 ^@ 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 ^@ Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||SH2|||SH2 domain-containing protein 2A|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000097727|||http://purl.uniprot.org/annotation/VSP_003967 http://togogenome.org/gene/10090:Tor3a ^@ http://purl.uniprot.org/uniprot/Q9ER38 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Torsin-3A ^@ http://purl.uniprot.org/annotation/PRO_0000228148 http://togogenome.org/gene/10090:Iqcj ^@ http://purl.uniprot.org/uniprot/Q8BPW0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||IQ|||IQ domain-containing protein J|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315662 http://togogenome.org/gene/10090:Cops4 ^@ http://purl.uniprot.org/uniprot/O88544|||http://purl.uniprot.org/uniprot/Q14AI7 ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn ^@ COP9 signalosome complex subunit 4|||N-acetylalanine|||N6-acetyllysine|||PCI|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000120988 http://togogenome.org/gene/10090:Usp6nl ^@ http://purl.uniprot.org/uniprot/Q80XC3 ^@ 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.|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Rab-GAP TBC|||USP6 N-terminal-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000208057|||http://purl.uniprot.org/annotation/VSP_011153 http://togogenome.org/gene/10090:Myl9 ^@ http://purl.uniprot.org/uniprot/Q9CQ19 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||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|||Prevents aberrant myotube formation in PIEZO1-deficient myoblast; when associated with D-19.|||Prevents aberrant myotube formation in PIEZO1-deficient myoblast; when associated with D-20.|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000198736 http://togogenome.org/gene/10090:Casp1 ^@ http://purl.uniprot.org/uniprot/P29452 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||CARD|||Caspase-1 subunit p10|||Caspase-1 subunit p20|||Cleavage; by autolysis|||Disordered|||In C47 mutant; does not affect ability to mediate inflammatory response and cell death; when associated with N-296.|||In C47 mutant; does not affect ability to mediate inflammatory response; when associated with 313-N-N-314.|||In C60 mutant; impaired cleavage and ability to generate caspase-1 subunits p10 and p20; abolished ability to process inflammatory cytokine interleukin-1 beta (IL1B) without affecting ability to induce programmed cell death.|||In C71 mutant; abolished cleavage and ability to generate caspase-1 subunits; abolished ability to process inflammatory cytokine interleukin-1 beta (IL1B) and ability to induce programmed cell death; when associated with N-103 and 296-N--N-314.|||In C71 mutant; abolished cleavage and ability to generate caspase-1 subunits; abolished ability to process inflammatory cytokine interleukin-1 beta (IL1B) and ability to induce programmed cell death; when associated with N-103 and N-122.|||In C71 mutant; abolished cleavage and ability to generate caspase-1 subunits; abolished ability to process inflammatory cytokine interleukin-1 beta (IL1B) and ability to induce programmed cell death; when associated with N-122 and 296-N--N-314.|||Loss of protease activity.|||Mediates autoprocessing but are unable to mediate cleavage of Gasdermin-D (GSDMD).|||Omega-N-methylarginine|||Phosphoserine|||Prevents autoprocessing. ^@ http://purl.uniprot.org/annotation/PRO_0000004525|||http://purl.uniprot.org/annotation/PRO_0000004526|||http://purl.uniprot.org/annotation/PRO_0000004527|||http://purl.uniprot.org/annotation/PRO_0000004528 http://togogenome.org/gene/10090:Slc12a6 ^@ http://purl.uniprot.org/uniprot/Q3V0N8|||http://purl.uniprot.org/uniprot/Q924N4 ^@ 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|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolished potassium-chloride cotransport.|||Amino acid permease/ SLC12A|||Basic and acidic residues|||Constitutively enhanced potassium-chloride cotransport activity. Significant locomotor deficits.|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Loss of potassium-chloride cotransport activity in Xenopus laevis oocytes.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Reduced potassium-chloride cotransport activity in Xenopus laevis oocytes.|||Reduced potassium-chloride cotransport.|||SLC12A transporter C-terminal|||Solute carrier family 12 member 6 ^@ http://purl.uniprot.org/annotation/PRO_0000178038|||http://purl.uniprot.org/annotation/VSP_006117|||http://purl.uniprot.org/annotation/VSP_006118 http://togogenome.org/gene/10090:Rcc1l ^@ http://purl.uniprot.org/uniprot/Q548B0|||http://purl.uniprot.org/uniprot/Q9CYF5 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transit Peptide ^@ Chain|||Region|||Repeat|||Transit Peptide ^@ Disordered|||Mitochondrion|||RCC1|||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_0000206657 http://togogenome.org/gene/10090:Mrpl14 ^@ http://purl.uniprot.org/uniprot/Q9D1I6 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein uL14m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000261135 http://togogenome.org/gene/10090:AA986860 ^@ http://purl.uniprot.org/uniprot/Q8BI29 ^@ 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|||Phosphothreonine|||Polar residues|||Specifically androgen-regulated gene protein ^@ http://purl.uniprot.org/annotation/PRO_0000318576|||http://purl.uniprot.org/annotation/VSP_031229 http://togogenome.org/gene/10090:Gpr101 ^@ http://purl.uniprot.org/uniprot/Q1WKE2|||http://purl.uniprot.org/uniprot/Q80T62 ^@ 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 ^@ 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|||Polar residues|||Probable G-protein coupled receptor 101 ^@ http://purl.uniprot.org/annotation/PRO_0000069602 http://togogenome.org/gene/10090:Rps25 ^@ http://purl.uniprot.org/uniprot/P62852|||http://purl.uniprot.org/uniprot/Q58EA6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Small ribosomal subunit protein eS25 ^@ http://purl.uniprot.org/annotation/PRO_0000192870 http://togogenome.org/gene/10090:Pdgfrb ^@ http://purl.uniprot.org/uniprot/P05622 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||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|||Ig-like C2-type 5|||In isoform 2.|||Increased autophosphorylation in the absence of PDGFB binding. Increased autophosphorylation in response to PDGFB binding. Constitutive interaction with PIK3R1, and constitutive AKT1 activation.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by ABL1 and ABL2|||Phosphotyrosine; by autocatalysis|||Platelet-derived growth factor receptor beta|||Polar residues|||Protein kinase|||Proton acceptor|||Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-750; F-1008 and F-1020.|||Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-750; F-770 and F-1008.|||Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-750; F-770 and F-1020.|||Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-770; F-1008 and F-1020.|||Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-750; F-770; F-1008 and F-1020.|||Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-739; F-750; F-770; F-1008 and F-1020.|||Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-715; F-739; F-750; F-770; F-1008 and F-1020. ^@ http://purl.uniprot.org/annotation/PRO_0000016758|||http://purl.uniprot.org/annotation/VSP_060195 http://togogenome.org/gene/10090:Dnaaf4 ^@ http://purl.uniprot.org/uniprot/E9Q973|||http://purl.uniprot.org/uniprot/Q8C5Z6|||http://purl.uniprot.org/uniprot/Q8R368|||http://purl.uniprot.org/uniprot/Q9CVZ5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||CS|||Disordered|||Dynein axonemal assembly factor 4|||Mediates interaction with ESR1 and STUB1|||TPR|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000106285 http://togogenome.org/gene/10090:Ppp6r3 ^@ http://purl.uniprot.org/uniprot/G5E8R4|||http://purl.uniprot.org/uniprot/Q922D4 ^@ 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.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Serine/threonine-protein phosphatase 6 regulatory subunit 3 ^@ http://purl.uniprot.org/annotation/PRO_0000046101|||http://purl.uniprot.org/annotation/VSP_017145|||http://purl.uniprot.org/annotation/VSP_017146|||http://purl.uniprot.org/annotation/VSP_017147|||http://purl.uniprot.org/annotation/VSP_017148|||http://purl.uniprot.org/annotation/VSP_017149 http://togogenome.org/gene/10090:Or1ad6 ^@ http://purl.uniprot.org/uniprot/Q8VGH0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mettl21a ^@ http://purl.uniprot.org/uniprot/Q9CQL0 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Protein N-lysine methyltransferase METTL21A ^@ http://purl.uniprot.org/annotation/PRO_0000292034 http://togogenome.org/gene/10090:Ndufaf4 ^@ http://purl.uniprot.org/uniprot/Q9D1H6 ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region ^@ Disordered|||N-myristoyl glycine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000220989 http://togogenome.org/gene/10090:Or6c69c ^@ http://purl.uniprot.org/uniprot/Q8VFU1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp952 ^@ http://purl.uniprot.org/uniprot/B0V2W4 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Gcgr ^@ http://purl.uniprot.org/uniprot/Q3UN81|||http://purl.uniprot.org/uniprot/Q61606 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Glucagon 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Results in impaired glucagon binding and glucagon-mediated signaling. Homozygous mice show hyperglucagonemia with alpha-cell hyperplasia and enlargement of the pancreas. ^@ http://purl.uniprot.org/annotation/PRO_0000012833|||http://purl.uniprot.org/annotation/PRO_5004230084 http://togogenome.org/gene/10090:Tap1 ^@ http://purl.uniprot.org/uniprot/P21958|||http://purl.uniprot.org/uniprot/Q3TBA3|||http://purl.uniprot.org/uniprot/Q3U6V4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||Antigen peptide transporter 1|||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|||Inter-subunit salt bridge with TAPBP|||Lumenal|||Part of the peptide-binding site ^@ http://purl.uniprot.org/annotation/PRO_0000093327 http://togogenome.org/gene/10090:Gen1 ^@ http://purl.uniprot.org/uniprot/Q8BMI4 ^@ 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 ^@ 5'-3' exonuclease domain|||Basic and acidic residues|||Chromodomain|||Disordered|||Flap endonuclease GEN homolog 1|||In isoform 2.|||Phosphoserine|||XPG-I domain|||XPG-N domain ^@ http://purl.uniprot.org/annotation/PRO_0000314147|||http://purl.uniprot.org/annotation/VSP_030216 http://togogenome.org/gene/10090:Asxl3 ^@ http://purl.uniprot.org/uniprot/Q8C4A5 ^@ 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 ^@ Basic and acidic residues|||DEUBAD|||Disordered|||HTH HARE-type|||In isoform 2.|||PHD-type; atypical|||Polar residues|||Pro residues|||Putative Polycomb group protein ASXL3 ^@ http://purl.uniprot.org/annotation/PRO_0000320671|||http://purl.uniprot.org/annotation/VSP_031720 http://togogenome.org/gene/10090:Proz ^@ http://purl.uniprot.org/uniprot/Q9CQW3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Signal Peptide ^@ (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||EGF-like 1|||EGF-like 2|||Gla|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Vitamin K-dependent protein Z ^@ http://purl.uniprot.org/annotation/PRO_0000028490|||http://purl.uniprot.org/annotation/PRO_0000028491 http://togogenome.org/gene/10090:Camsap1 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQE5|||http://purl.uniprot.org/uniprot/A2AHC3 ^@ 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|||CKK|||Calmodulin-regulated spectrin-associated protein 1|||Calponin-homology (CH)|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Sufficient for interaction with SPTBN1|||Sufficient for interaction with calmodulin ^@ http://purl.uniprot.org/annotation/PRO_0000316829|||http://purl.uniprot.org/annotation/VSP_030802|||http://purl.uniprot.org/annotation/VSP_030803|||http://purl.uniprot.org/annotation/VSP_030804 http://togogenome.org/gene/10090:Rgs9 ^@ http://purl.uniprot.org/uniprot/O54828|||http://purl.uniprot.org/uniprot/Q3UUR0 ^@ 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 ^@ DEP|||Disordered|||G protein gamma|||In isoform 1.|||RGS|||Regulator of G-protein signaling 9 ^@ http://purl.uniprot.org/annotation/PRO_0000204204|||http://purl.uniprot.org/annotation/VSP_005678|||http://purl.uniprot.org/annotation/VSP_005679 http://togogenome.org/gene/10090:Or8j3 ^@ http://purl.uniprot.org/uniprot/Q7TR80 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r33 ^@ http://purl.uniprot.org/uniprot/K7N705 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908940 http://togogenome.org/gene/10090:Bricd5 ^@ http://purl.uniprot.org/uniprot/Q8BV89 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BRICHOS ^@ http://togogenome.org/gene/10090:Ceacam5 ^@ http://purl.uniprot.org/uniprot/Q3UKK2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Carcinoembryonic antigen-related cell adhesion molecule 5|||Ig-like C2-type 1|||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|||Ig-like V-type 6|||Ig-like V-type 7|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000378506 http://togogenome.org/gene/10090:Zfp329 ^@ http://purl.uniprot.org/uniprot/B2RSV9|||http://purl.uniprot.org/uniprot/Q6GQR8 ^@ 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|||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_0000307289 http://togogenome.org/gene/10090:Fam236f ^@ http://purl.uniprot.org/uniprot/A2AI92 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Prl4a1 ^@ http://purl.uniprot.org/uniprot/A0A0M6L0M4|||http://purl.uniprot.org/uniprot/O35256 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prolactin-4A1 ^@ http://purl.uniprot.org/annotation/PRO_0000045168|||http://purl.uniprot.org/annotation/PRO_5015043316 http://togogenome.org/gene/10090:Trappc6b ^@ http://purl.uniprot.org/uniprot/Q9D289 ^@ Chain|||Molecule Processing ^@ Chain ^@ Trafficking protein particle complex subunit 6B ^@ http://purl.uniprot.org/annotation/PRO_0000211588 http://togogenome.org/gene/10090:Ccdc171 ^@ http://purl.uniprot.org/uniprot/E9Q1U1 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Splice Variant ^@ Coiled-coil domain-containing protein 171|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000417502|||http://purl.uniprot.org/annotation/VSP_043769 http://togogenome.org/gene/10090:Cldn7 ^@ http://purl.uniprot.org/uniprot/Q9Z261 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Claudin-7|||Cytoplasmic|||Extracellular|||Helical|||Interactions with TJP1, TJP2 and TJP3 ^@ http://purl.uniprot.org/annotation/PRO_0000144751 http://togogenome.org/gene/10090:Nipal1 ^@ http://purl.uniprot.org/uniprot/Q8BMW7 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Magnesium transporter NIPA3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000386645 http://togogenome.org/gene/10090:Hs6st2 ^@ http://purl.uniprot.org/uniprot/Q80UW0 ^@ 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|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Heparan-sulfate 6-O-sulfotransferase 2|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000190806|||http://purl.uniprot.org/annotation/VSP_015848|||http://purl.uniprot.org/annotation/VSP_015849 http://togogenome.org/gene/10090:A630073D07Rik ^@ http://purl.uniprot.org/uniprot/E9PWS6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003242997 http://togogenome.org/gene/10090:Slc25a51 ^@ http://purl.uniprot.org/uniprot/Q5HZI9 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial nicotinamide adenine dinucleotide transporter SLC25A51|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090712 http://togogenome.org/gene/10090:Pacs2 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VLZ7|||http://purl.uniprot.org/uniprot/E9Q7E9|||http://purl.uniprot.org/uniprot/Q3V3Q7 ^@ 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|||Phosphofurin acidic cluster sorting protein 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000259512 http://togogenome.org/gene/10090:Myo3a ^@ http://purl.uniprot.org/uniprot/F6QNG5 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Actin-binding|||Disordered|||Myosin motor|||Polar residues|||Protein kinase ^@ http://togogenome.org/gene/10090:Tas2r138 ^@ http://purl.uniprot.org/uniprot/Q7TQA6 ^@ 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 38 ^@ http://purl.uniprot.org/annotation/PRO_0000082279 http://togogenome.org/gene/10090:Kng2 ^@ http://purl.uniprot.org/uniprot/Q6S9I0|||http://purl.uniprot.org/uniprot/Q6S9I2|||http://purl.uniprot.org/uniprot/Q6S9I3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Basic residues|||Cystatin kininogen-type|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015098483|||http://purl.uniprot.org/annotation/PRO_5015098484|||http://purl.uniprot.org/annotation/PRO_5015098485 http://togogenome.org/gene/10090:Msantd2 ^@ http://purl.uniprot.org/uniprot/Q6NZR2 ^@ 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 ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Myb-like|||Myb/SANT-like DNA-binding domain-containing protein 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000274302|||http://purl.uniprot.org/annotation/VSP_022707 http://togogenome.org/gene/10090:Vmn2r24 ^@ http://purl.uniprot.org/uniprot/D3YUI0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015088509 http://togogenome.org/gene/10090:Sncg ^@ http://purl.uniprot.org/uniprot/Q5GQ64|||http://purl.uniprot.org/uniprot/Q9Z0F7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat ^@ 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_0000184039 http://togogenome.org/gene/10090:Atp1b1 ^@ http://purl.uniprot.org/uniprot/P14094|||http://purl.uniprot.org/uniprot/Q3TV47|||http://purl.uniprot.org/uniprot/Q545P0 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Sodium/potassium-transporting ATPase subunit beta-1|||immunoglobulin-like ^@ http://purl.uniprot.org/annotation/PRO_0000219098 http://togogenome.org/gene/10090:Slc8b1 ^@ http://purl.uniprot.org/uniprot/Q925Q3 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Cytoplasmic|||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 isoform 2.|||In isoform 3.|||Mitochondrial sodium/calcium exchanger protein|||Mitochondrion|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKA ^@ http://purl.uniprot.org/annotation/PRO_0000045757|||http://purl.uniprot.org/annotation/VSP_016997|||http://purl.uniprot.org/annotation/VSP_016998 http://togogenome.org/gene/10090:Acot12 ^@ http://purl.uniprot.org/uniprot/A2RSC2|||http://purl.uniprot.org/uniprot/Q9DBK0 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Acetyl-coenzyme A thioesterase|||HotDog ACOT-type|||HotDog ACOT-type 1|||HotDog ACOT-type 2|||N6-succinyllysine|||START ^@ http://purl.uniprot.org/annotation/PRO_0000053810 http://togogenome.org/gene/10090:Arfgef1 ^@ http://purl.uniprot.org/uniprot/G3X9K3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ 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|||Nuclear localization signal (NLS)|||Phosphoserine|||Polar residues|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000419330 http://togogenome.org/gene/10090:Flnc ^@ http://purl.uniprot.org/uniprot/Q8VHX6 ^@ 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 ^@ Actin-binding|||Basic and acidic residues|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||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; 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 isoform 2.|||Interaction with INPPL1|||Intradomain insert; mediate targeting to Z lines|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Self-association site, tail ^@ http://purl.uniprot.org/annotation/PRO_0000087302|||http://purl.uniprot.org/annotation/VSP_007580 http://togogenome.org/gene/10090:Btbd35f29 ^@ http://purl.uniprot.org/uniprot/J3QML3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:H2al1h ^@ http://purl.uniprot.org/uniprot/Q5M8Q2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Histone H2A-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000440627 http://togogenome.org/gene/10090:Slurp1 ^@ http://purl.uniprot.org/uniprot/Q9Z0K7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Secreted Ly-6/uPAR-related protein 1|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036168 http://togogenome.org/gene/10090:E2f8 ^@ http://purl.uniprot.org/uniprot/Q58FA4 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Loss of DNA-binding.|||Phosphoserine|||Polar residues|||Transcription factor E2F8 ^@ http://purl.uniprot.org/annotation/PRO_0000298910 http://togogenome.org/gene/10090:Psip1 ^@ http://purl.uniprot.org/uniprot/A2BI12|||http://purl.uniprot.org/uniprot/Q99JF8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Integrase-binding domain (IBD)|||Nuclear localization signal|||PC4 and SFRS1-interacting protein|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000191709|||http://purl.uniprot.org/annotation/VSP_014299|||http://purl.uniprot.org/annotation/VSP_014300 http://togogenome.org/gene/10090:Scara3 ^@ http://purl.uniprot.org/uniprot/Q8C850 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Collagen-like 1|||Collagen-like 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Pro residues|||Scavenger receptor class A member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000181634 http://togogenome.org/gene/10090:Tyw3 ^@ http://purl.uniprot.org/uniprot/E9PYE2|||http://purl.uniprot.org/uniprot/Q8BSA9 ^@ 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|||tRNA wybutosine-synthesizing protein|||tRNA wybutosine-synthesizing protein 3 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000281843 http://togogenome.org/gene/10090:Sbsn ^@ http://purl.uniprot.org/uniprot/A0A0R4J2A5|||http://purl.uniprot.org/uniprot/E9QPB2|||http://purl.uniprot.org/uniprot/Q8CIT9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 3.|||Polar residues|||Suprabasin ^@ http://purl.uniprot.org/annotation/PRO_0000317121|||http://purl.uniprot.org/annotation/PRO_5003246310|||http://purl.uniprot.org/annotation/PRO_5006452031|||http://purl.uniprot.org/annotation/VSP_030902 http://togogenome.org/gene/10090:Phlpp1 ^@ http://purl.uniprot.org/uniprot/Q8CHE4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||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 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-acetylmethionine|||PDZ-binding|||PH|||PH domain leucine-rich repeat-containing protein phosphatase 1|||PPM-type phosphatase|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000057782|||http://purl.uniprot.org/annotation/VSP_057810 http://togogenome.org/gene/10090:Insig1 ^@ http://purl.uniprot.org/uniprot/Q8BGI3 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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|||Insulin-induced gene 1 protein|||KxHxx|||Phosphoserine|||Required for the recognition of 25-hydroxycholesterol ^@ http://purl.uniprot.org/annotation/PRO_0000191676 http://togogenome.org/gene/10090:Hoxd10 ^@ http://purl.uniprot.org/uniprot/P28359 ^@ 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 ^@ Disordered|||Homeobox|||Homeobox protein Hox-D10|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000200227 http://togogenome.org/gene/10090:Ccnd3 ^@ http://purl.uniprot.org/uniprot/P30282|||http://purl.uniprot.org/uniprot/Q3TSW4|||http://purl.uniprot.org/uniprot/Q3TWY0|||http://purl.uniprot.org/uniprot/S4R216 ^@ 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 ^@ Cyclin C-terminal|||Cyclin N-terminal|||Disordered|||G1/S-specific cyclin-D3|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080443 http://togogenome.org/gene/10090:Slc66a1 ^@ http://purl.uniprot.org/uniprot/A6PWV7|||http://purl.uniprot.org/uniprot/Q8C4N4 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Di-leucine motif|||Helical|||In isoform 2.|||Lumenal|||Lysosomal amino acid transporter 1 homolog|||N-linked (GlcNAc...) asparagine|||PQ-loop 1|||PQ-loop 2 ^@ http://purl.uniprot.org/annotation/PRO_0000282435|||http://purl.uniprot.org/annotation/VSP_024153 http://togogenome.org/gene/10090:Wnt7a ^@ http://purl.uniprot.org/uniprot/P24383 ^@ 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-7a ^@ http://purl.uniprot.org/annotation/PRO_0000041443 http://togogenome.org/gene/10090:Cwc22 ^@ http://purl.uniprot.org/uniprot/B1AYU7|||http://purl.uniprot.org/uniprot/Q8C5N3 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||MI|||MIF4G|||Phosphoserine|||Polar residues|||Pre-mRNA-splicing factor CWC22 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000302006|||http://purl.uniprot.org/annotation/VSP_027905 http://togogenome.org/gene/10090:Prelid1 ^@ http://purl.uniprot.org/uniprot/Q8R107 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||PRELI domain-containing protein 1, mitochondrial|||PRELI/MSF1 ^@ http://purl.uniprot.org/annotation/PRO_0000097120 http://togogenome.org/gene/10090:Fktn ^@ http://purl.uniprot.org/uniprot/A0A1Y7VM91|||http://purl.uniprot.org/uniprot/Q8R507 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||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_0000204722 http://togogenome.org/gene/10090:Peg12 ^@ http://purl.uniprot.org/uniprot/Q9WVA7 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Nudt1 ^@ http://purl.uniprot.org/uniprot/P53368 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Strand|||Turn ^@ Nudix box|||Nudix hydrolase|||Oxidized purine nucleoside triphosphate hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000057100 http://togogenome.org/gene/10090:Ccdc144b ^@ http://purl.uniprot.org/uniprot/E9PVZ3|||http://purl.uniprot.org/uniprot/Q80W27 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ DUF3496 ^@ http://togogenome.org/gene/10090:Appbp2 ^@ http://purl.uniprot.org/uniprot/Q9DAX9 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ 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_0000106260 http://togogenome.org/gene/10090:Acat1 ^@ http://purl.uniprot.org/uniprot/Q8QZT1 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Site|||Transit Peptide ^@ Acetyl-CoA acetyltransferase, mitochondrial|||Acyl-thioester intermediate|||Increases nucleophilicity of active site Cys|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000034087 http://togogenome.org/gene/10090:Pla2g7 ^@ http://purl.uniprot.org/uniprot/Q60963 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Platelet-activating factor acetylhydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000017834 http://togogenome.org/gene/10090:C1qa ^@ http://purl.uniprot.org/uniprot/A0A3B0IP04|||http://purl.uniprot.org/uniprot/P98086 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 4-hydroxyproline|||5-hydroxylysine; alternate|||C1q|||Collagen-like|||Complement C1q subcomponent subunit A|||Disordered|||Interchain (with C-29 in B chain)|||N-linked (GlcNAc...) asparagine|||O-linked (Gal...) hydroxylysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000003518|||http://purl.uniprot.org/annotation/PRO_5017272240 http://togogenome.org/gene/10090:Htd2 ^@ http://purl.uniprot.org/uniprot/J3QMX0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ MaoC-like ^@ http://togogenome.org/gene/10090:Adamts6 ^@ http://purl.uniprot.org/uniprot/D3Z1A5 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ PLAC|||Peptidase M12B|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_5015088517 http://togogenome.org/gene/10090:Hrc ^@ http://purl.uniprot.org/uniprot/G5E8J6|||http://purl.uniprot.org/uniprot/Q9WVE4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5004336026|||http://purl.uniprot.org/annotation/PRO_5015091901 http://togogenome.org/gene/10090:Thegl ^@ http://purl.uniprot.org/uniprot/Q9DA15 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ 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_0000416827 http://togogenome.org/gene/10090:Bclaf3 ^@ http://purl.uniprot.org/uniprot/A2AG58 ^@ 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.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000287435|||http://purl.uniprot.org/annotation/VSP_025460 http://togogenome.org/gene/10090:Traf4 ^@ http://purl.uniprot.org/uniprot/Q61382 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Zinc Finger ^@ Abolished ubiquitination by the SCF(FBXL2) complex.|||Decreased interaction with FBXL2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||MATH|||Phosphoserine|||RING-type|||TNF receptor-associated factor 4|||TRAF-type 1|||TRAF-type 2|||TRAF-type 3 ^@ http://purl.uniprot.org/annotation/PRO_0000056404 http://togogenome.org/gene/10090:Cdkn2b ^@ http://purl.uniprot.org/uniprot/P55271|||http://purl.uniprot.org/uniprot/Q549R4 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Repeat|||Strand|||Turn ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cyclin-dependent kinase 4 inhibitor B|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000144185 http://togogenome.org/gene/10090:Rpa3 ^@ http://purl.uniprot.org/uniprot/Q9CQ71 ^@ Chain|||Crosslink|||Modification|||Molecule Processing ^@ Chain|||Crosslink ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Replication protein A 14 kDa subunit ^@ http://purl.uniprot.org/annotation/PRO_0000097277 http://togogenome.org/gene/10090:Gbp7 ^@ http://purl.uniprot.org/uniprot/Q91Z40 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region ^@ 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|||Loss of catalytic activity and localization to cytoplasmic vesicle.|||Loss of catalytic activity.|||Loss of localization to cytoplasmic vesicle. ^@ http://purl.uniprot.org/annotation/PRO_0000454379 http://togogenome.org/gene/10090:Lmod2 ^@ http://purl.uniprot.org/uniprot/Q3UHZ5 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Interaction with actin 1|||Interaction with actin 2|||Interaction with actin 3|||Interaction with tropomyosin alpha|||Leiomodin-2|||Phosphoserine|||Polar residues|||Pro residues|||WH2|||When expressed in constitutive LMOD2 knockout mice, the mutant reduces onset of cardiac dilation and dysfunction. ^@ http://purl.uniprot.org/annotation/PRO_0000311341 http://togogenome.org/gene/10090:Stap2 ^@ http://purl.uniprot.org/uniprot/Q8R0L1 ^@ 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 ^@ Disordered|||In isoform 2.|||PH|||Phosphotyrosine|||Phosphotyrosine; by PTK6|||Pro residues|||SH2|||Signal-transducing adaptor protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000072240|||http://purl.uniprot.org/annotation/VSP_013401|||http://purl.uniprot.org/annotation/VSP_013402 http://togogenome.org/gene/10090:Tbc1d10c ^@ http://purl.uniprot.org/uniprot/Q8C9V1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Site|||Splice Variant ^@ Arginine finger|||Carabin|||Disordered|||Glutamine finger|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with calcineurin|||Polar residues|||Rab-GAP TBC ^@ http://purl.uniprot.org/annotation/PRO_0000284468|||http://purl.uniprot.org/annotation/VSP_024536|||http://purl.uniprot.org/annotation/VSP_024537|||http://purl.uniprot.org/annotation/VSP_024538|||http://purl.uniprot.org/annotation/VSP_024539 http://togogenome.org/gene/10090:Slc6a11 ^@ http://purl.uniprot.org/uniprot/P31650 ^@ 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; 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|||Sodium- and chloride-dependent GABA transporter 3 ^@ http://purl.uniprot.org/annotation/PRO_0000214785 http://togogenome.org/gene/10090:Ro60 ^@ http://purl.uniprot.org/uniprot/O08848|||http://purl.uniprot.org/uniprot/Q3TJ75 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||RNA-binding|||RNA-binding protein Ro60|||TROVE|||VWFA-like domain ^@ http://purl.uniprot.org/annotation/PRO_0000174170 http://togogenome.org/gene/10090:Serpinc1 ^@ http://purl.uniprot.org/uniprot/P32261|||http://purl.uniprot.org/uniprot/Q543J5 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Site ^@ Antithrombin-III|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Reactive bond|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_0000032490|||http://purl.uniprot.org/annotation/PRO_5014309547 http://togogenome.org/gene/10090:Trap1a ^@ http://purl.uniprot.org/uniprot/P19473|||http://purl.uniprot.org/uniprot/Q3UIV7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Transmembrane ^@ Acidic residues|||Disordered|||Helical|||Nuclear localization signal|||Tumor rejection antigen P815A ^@ http://purl.uniprot.org/annotation/PRO_0000065697 http://togogenome.org/gene/10090:Fam171a1 ^@ http://purl.uniprot.org/uniprot/A2ATK9|||http://purl.uniprot.org/uniprot/A2ATL0|||http://purl.uniprot.org/uniprot/A2ATL1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015086033 http://togogenome.org/gene/10090:Hat1 ^@ http://purl.uniprot.org/uniprot/Q8BY71 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Site ^@ Histone acetyltransferase type B catalytic subunit|||Interaction with histone H4 N-terminus|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Proton donor/acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000227729 http://togogenome.org/gene/10090:Gm597 ^@ http://purl.uniprot.org/uniprot/E9Q8J5 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Ddr1 ^@ http://purl.uniprot.org/uniprot/Q03146|||http://purl.uniprot.org/uniprot/Q05BN5|||http://purl.uniprot.org/uniprot/Q544T2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||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|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DS-like domain|||Disordered|||Epithelial discoidin domain-containing receptor 1|||Extracellular|||F5/8 type C|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PPxY motif|||Phosphotyrosine; by autocatalysis|||Pro residues|||Protein kinase|||Proton acceptor|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000016743|||http://purl.uniprot.org/annotation/PRO_5004164722|||http://purl.uniprot.org/annotation/PRO_5010844023|||http://purl.uniprot.org/annotation/VSP_002954 http://togogenome.org/gene/10090:Wasl ^@ http://purl.uniprot.org/uniprot/Q3TXX8|||http://purl.uniprot.org/uniprot/Q6PDL3|||http://purl.uniprot.org/uniprot/Q91YD9|||http://purl.uniprot.org/uniprot/Q9CXQ9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region ^@ Abolishes phosphorylation. Protein preferentially localized in nucleus.|||Acidic residues|||Actin nucleation-promoting factor WASL|||CRIB|||Disordered|||N-acetylserine|||No effect on phosphorylation. Protein preferentially localized in cytoplasm.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by TNK2|||Phosphotyrosine; by FAK1 and TNK2|||Polar residues|||Pro residues|||Removed|||WH1|||WH2|||WH2 1|||WH2 2 ^@ http://purl.uniprot.org/annotation/PRO_0000189001 http://togogenome.org/gene/10090:Efnb3 ^@ http://purl.uniprot.org/uniprot/O35393|||http://purl.uniprot.org/uniprot/Q543Q7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Ephrin RBD|||Ephrin-B3|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||PDZ-binding|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000008396|||http://purl.uniprot.org/annotation/PRO_5014309548 http://togogenome.org/gene/10090:Dolk ^@ http://purl.uniprot.org/uniprot/Q8R2Y3 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ CTP-binding|||Cytoplasmic|||Dolichol kinase|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000355581 http://togogenome.org/gene/10090:Ccdc124 ^@ http://purl.uniprot.org/uniprot/Q9D8X2 ^@ 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|||Coiled-coil domain-containing protein 124|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000263736 http://togogenome.org/gene/10090:Col14a1 ^@ http://purl.uniprot.org/uniprot/B7ZNH7|||http://purl.uniprot.org/uniprot/Q80X19 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Cell attachment site|||Collagen alpha-1(XIV) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Disordered|||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|||In isoform 2.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nonhelical region (NC4)|||Pro residues|||Triple-helical region 1 (COL2)|||Triple-helical region 2 (COL1)|||VWFA|||VWFA 1|||VWFA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000005786|||http://purl.uniprot.org/annotation/PRO_5015087439|||http://purl.uniprot.org/annotation/VSP_051652 http://togogenome.org/gene/10090:Nek4 ^@ http://purl.uniprot.org/uniprot/Q3UED6|||http://purl.uniprot.org/uniprot/Q6GTE9|||http://purl.uniprot.org/uniprot/Q9Z1J2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||N6-methyllysine|||Phosphoserine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek4 ^@ http://purl.uniprot.org/annotation/PRO_0000086426|||http://purl.uniprot.org/annotation/VSP_007001 http://togogenome.org/gene/10090:Hmga2 ^@ http://purl.uniprot.org/uniprot/P52927|||http://purl.uniprot.org/uniprot/Q6NSP9 ^@ 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 ^@ A.T hook 1|||A.T hook 2|||A.T hook 3|||Disordered|||High mobility group protein HMGI-C|||Interaction with E4F1|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000206712 http://togogenome.org/gene/10090:Zscan21 ^@ http://purl.uniprot.org/uniprot/Q07231 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ 1-1|||1-2|||1-3|||3 X 39 AA approximate tandem repeats|||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)|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 21 ^@ http://purl.uniprot.org/annotation/PRO_0000047296 http://togogenome.org/gene/10090:Krtap14 ^@ http://purl.uniprot.org/uniprot/O08640 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1|||2|||2 X 17 AA approximate tandem repeats|||Keratin-associated protein 14 ^@ http://purl.uniprot.org/annotation/PRO_0000271176 http://togogenome.org/gene/10090:Fbxw4 ^@ http://purl.uniprot.org/uniprot/Q9JMJ2 ^@ 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 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000050991 http://togogenome.org/gene/10090:Orc6 ^@ http://purl.uniprot.org/uniprot/Q3TQX1|||http://purl.uniprot.org/uniprot/Q66JV6 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Hadha ^@ http://purl.uniprot.org/uniprot/Q8BMS1 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ For hydroxyacyl-coenzyme A dehydrogenase activity|||Important for hydroxyacyl-coenzyme A dehydrogenase activity|||Important for long-chain enoyl-CoA hydratase activity|||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_0000322639 http://togogenome.org/gene/10090:Tent4a ^@ http://purl.uniprot.org/uniprot/Q3U7R5|||http://purl.uniprot.org/uniprot/Q6PB75 ^@ 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 ^@ Disordered|||PAP-associated|||Polar residues|||Polymerase nucleotidyl transferase|||Terminal nucleotidyltransferase 4A ^@ http://purl.uniprot.org/annotation/PRO_0000120309 http://togogenome.org/gene/10090:Klc2 ^@ http://purl.uniprot.org/uniprot/Q91YS4 ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Polar residues|||TPR ^@ http://togogenome.org/gene/10090:Paf1 ^@ http://purl.uniprot.org/uniprot/Q8K2T8 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||RNA polymerase II-associated factor 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000326401 http://togogenome.org/gene/10090:Treml1 ^@ http://purl.uniprot.org/uniprot/A6XA75|||http://purl.uniprot.org/uniprot/Q8K558 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Modified Residue|||Motif|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM|||Ig-like V-type|||Immunoglobulin subtype|||In isoform 2.|||Phosphoserine|||Pro residues|||S-palmitoyl cysteine|||Trem-like transcript 1 protein ^@ http://purl.uniprot.org/annotation/PRO_0000253856|||http://purl.uniprot.org/annotation/PRO_5015086541|||http://purl.uniprot.org/annotation/VSP_021127 http://togogenome.org/gene/10090:Chrnb2 ^@ http://purl.uniprot.org/uniprot/Q9ERK7 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000000380 http://togogenome.org/gene/10090:Samt2b ^@ http://purl.uniprot.org/uniprot/Q9D519 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Asb18 ^@ http://purl.uniprot.org/uniprot/Q8VHA6 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and SOCS box protein 18|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000311876|||http://purl.uniprot.org/annotation/VSP_029624|||http://purl.uniprot.org/annotation/VSP_029625|||http://purl.uniprot.org/annotation/VSP_029626|||http://purl.uniprot.org/annotation/VSP_029627 http://togogenome.org/gene/10090:Klhl34 ^@ http://purl.uniprot.org/uniprot/A2AI76 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BTB|||Disordered ^@ http://togogenome.org/gene/10090:Ccdc183 ^@ http://purl.uniprot.org/uniprot/A2AJB1 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Splice Variant ^@ Coiled-coil domain-containing protein 183|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000293466|||http://purl.uniprot.org/annotation/VSP_026485|||http://purl.uniprot.org/annotation/VSP_026486 http://togogenome.org/gene/10090:Gabbr1 ^@ http://purl.uniprot.org/uniprot/Q9WV18 ^@ Binding Site|||Chain|||Coiled-Coil|||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 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Gamma-aminobutyric acid type B receptor subunit 1|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 1B.|||Interaction with ATF4|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues|||Pro residues|||Sushi 1|||Sushi 2 ^@ http://purl.uniprot.org/annotation/PRO_0000012950|||http://purl.uniprot.org/annotation/VSP_002041 http://togogenome.org/gene/10090:Tshr ^@ http://purl.uniprot.org/uniprot/P47750|||http://purl.uniprot.org/uniprot/Q78U67 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Repeat|||Sequence Conflict|||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|||In hypothyroidism.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Sulfotyrosine|||Thyrotropin receptor ^@ http://purl.uniprot.org/annotation/PRO_0000012787|||http://purl.uniprot.org/annotation/PRO_5015098650 http://togogenome.org/gene/10090:Shpk ^@ http://purl.uniprot.org/uniprot/Q9D5J6 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Mutagenesis Site ^@ Decreases sedoheptulose kinase activity.|||Decreases sedoheptulose kinase activity; when associated with K-15.|||Decreases sedoheptulose kinase activity; when associated with M-14.|||Sedoheptulokinase ^@ http://purl.uniprot.org/annotation/PRO_0000059565 http://togogenome.org/gene/10090:Sowaha ^@ http://purl.uniprot.org/uniprot/Q8BLS7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein SOWAHA|||Disordered|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000244374 http://togogenome.org/gene/10090:Mcrip2 ^@ http://purl.uniprot.org/uniprot/Q9CQB2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||MAPK regulated corepressor interacting protein 2|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000274329 http://togogenome.org/gene/10090:Slco1a4 ^@ http://purl.uniprot.org/uniprot/Q9EP96 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier organic anion transporter family member 1A4 ^@ http://purl.uniprot.org/annotation/PRO_0000191046 http://togogenome.org/gene/10090:Pip4k2a ^@ http://purl.uniprot.org/uniprot/O70172|||http://purl.uniprot.org/uniprot/Q544E3 ^@ 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 ^@ Acidic residues|||Disordered|||N-acetylalanine|||N6-acetyllysine|||PIPK|||Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Required for interaction with PIP5K1A ^@ http://purl.uniprot.org/annotation/PRO_0000185466 http://togogenome.org/gene/10090:Hs3st3b1 ^@ http://purl.uniprot.org/uniprot/Q9QZS6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000085220 http://togogenome.org/gene/10090:Zfp42 ^@ http://purl.uniprot.org/uniprot/E9QK22|||http://purl.uniprot.org/uniprot/P22227 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ 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 ubiquitin)|||Zinc finger protein 42 ^@ http://purl.uniprot.org/annotation/PRO_0000047300 http://togogenome.org/gene/10090:Zcwpw1 ^@ http://purl.uniprot.org/uniprot/Q6IR42 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||CW-type|||Disordered|||Knockin mice show impaired spermatogenesis, loss of histone H3K4me3 binding, severe disruption of chromosomal synapsis and DNA double-strand breaks repair in spermatocytes; when associated with I-247 and P-294.|||Knockin mice show impaired spermatogenesis, loss of histone H3K4me3 binding, severe disruption of chromosomal synapsis and DNA double-strand breaks repair in spermatocytes; when associated with I-247 and R-292.|||Knockin mice show impaired spermatogenesis, loss of histone H3K4me3 binding, severe disruption of chromosomal synapsis and DNA double-strand breaks repair in spermatocytes; when associated with R-292 and P-294.|||PWWP|||Phosphoserine|||Polar residues|||Zinc finger CW-type PWWP domain protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000066568 http://togogenome.org/gene/10090:Dapk3 ^@ http://purl.uniprot.org/uniprot/O54784|||http://purl.uniprot.org/uniprot/Q05A21 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Activation segment|||Death-associated protein kinase 3|||Decreased activity; when associated with A-422 and A-429.|||Decreased activity; when associated with A-422 and A-436.|||Decreased activity; when associated with A-429 and A-436.|||Interaction with CDC5L|||Leucine-zipper|||Loss of activity.|||Nuclear colocalization.|||Nuclear localization.|||Phosphoserine; by DAPK1|||Phosphoserine; by autocatalysis and DAPK1|||Phosphothreonine|||Phosphothreonine; by ROCK1|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085915 http://togogenome.org/gene/10090:Or4c31 ^@ http://purl.uniprot.org/uniprot/Q8VFF8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cox11 ^@ http://purl.uniprot.org/uniprot/Q6P8I6 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Cytochrome c oxidase assembly protein COX11, mitochondrial|||Disordered|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000006081 http://togogenome.org/gene/10090:Wbp2nl ^@ http://purl.uniprot.org/uniprot/Q9D529 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Repeat ^@ 1|||2|||3|||4|||5|||6|||6 X 7 AA tandem repeat of Y-G-X-P-P-X-G|||Disordered|||GRAM|||PPxY motif 1|||PPxY motif 2|||PPxY motif 3|||PPxY motif 4|||PPxY motif 5|||PPxY motif 6|||Polar residues|||Postacrosomal sheath WW domain-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000289128 http://togogenome.org/gene/10090:Ebf2 ^@ http://purl.uniprot.org/uniprot/O08792 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ C5-type|||Disordered|||IPT/TIG|||Interaction with DNA|||Transcription factor COE2 ^@ http://purl.uniprot.org/annotation/PRO_0000107829 http://togogenome.org/gene/10090:Josd1 ^@ http://purl.uniprot.org/uniprot/Q9DBJ6 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Josephin|||Josephin-1|||Nucleophile|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000053840 http://togogenome.org/gene/10090:Lima1 ^@ http://purl.uniprot.org/uniprot/Q8C3R7|||http://purl.uniprot.org/uniprot/Q8CD09|||http://purl.uniprot.org/uniprot/Q9ERG0 ^@ 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 ^@ Abolished phosphorylation by MAPK1/MAPK3.|||Basic and acidic residues|||Decreases interaction with NPC1L1.|||Disordered|||In isoform Alpha.|||LIM domain and actin-binding protein 1|||LIM zinc-binding|||N-acetylmethionine|||N6-succinyllysine|||Phosphoserine|||Polar residues|||Reduced phosphorylation by MAPK1/MAPK3.|||Required for interaction with MYO5B|||Required for interaction with NPC1L1 ^@ http://purl.uniprot.org/annotation/PRO_0000075731|||http://purl.uniprot.org/annotation/VSP_003118 http://togogenome.org/gene/10090:Bbox1 ^@ http://purl.uniprot.org/uniprot/Q924Y0 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Gamma-butyrobetaine dioxygenase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000207086 http://togogenome.org/gene/10090:Ndufc1 ^@ http://purl.uniprot.org/uniprot/Q9CQY9 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transit Peptide|||Transmembrane|||Turn ^@ Chain|||Helix|||Strand|||Transit Peptide|||Transmembrane|||Turn ^@ Helical|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000020050 http://togogenome.org/gene/10090:Cyp3a44 ^@ http://purl.uniprot.org/uniprot/Q9EQW4 ^@ Binding Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Transmembrane ^@ Helical|||axial binding residue ^@ http://togogenome.org/gene/10090:Ikzf1 ^@ http://purl.uniprot.org/uniprot/G5E8H3|||http://purl.uniprot.org/uniprot/Q3UQ33|||http://purl.uniprot.org/uniprot/Q5SWT9|||http://purl.uniprot.org/uniprot/Q5SWU0|||http://purl.uniprot.org/uniprot/Q8C5P6|||http://purl.uniprot.org/uniprot/Q8C9X3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:1700008O03Rik ^@ http://purl.uniprot.org/uniprot/D3Z070 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Putative uncharacterized protein C19orf81 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000413697 http://togogenome.org/gene/10090:Elovl2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1P7|||http://purl.uniprot.org/uniprot/Q543J1|||http://purl.uniprot.org/uniprot/Q9JLJ4 ^@ Chain|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Motif|||Transmembrane ^@ Di-lysine motif|||Elongation of very long chain fatty acids protein 2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000207539 http://togogenome.org/gene/10090:Urgcp ^@ http://purl.uniprot.org/uniprot/Q5NCI0|||http://purl.uniprot.org/uniprot/Q6NXN0 ^@ 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.|||Phosphoserine|||Up-regulator of cell proliferation|||VLIG-type G ^@ http://purl.uniprot.org/annotation/PRO_0000337149|||http://purl.uniprot.org/annotation/VSP_052800 http://togogenome.org/gene/10090:2210016L21Rik ^@ http://purl.uniprot.org/uniprot/A0A0R4J099|||http://purl.uniprot.org/uniprot/Q3UY34 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Disordered|||Nucleolar localization signal (NLS)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein CUSTOS ^@ http://purl.uniprot.org/annotation/PRO_0000276851 http://togogenome.org/gene/10090:Pdap1 ^@ http://purl.uniprot.org/uniprot/B2RTB0|||http://purl.uniprot.org/uniprot/Q3UHX2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ 28 kDa heat- and acid-stable phosphoprotein|||Basic and acidic residues|||Casein kinase substrate phosphoprotein PP28|||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_0000083898 http://togogenome.org/gene/10090:Lfng ^@ http://purl.uniprot.org/uniprot/B2RRW2|||http://purl.uniprot.org/uniprot/O09010 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Beta-1,3-N-acetylglucosaminyltransferase|||Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe|||Cleavage; by furin-like protease|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219177|||http://purl.uniprot.org/annotation/PRO_5015087147 http://togogenome.org/gene/10090:Katna1 ^@ http://purl.uniprot.org/uniprot/E9PZI6 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ AAA+ ATPase|||Basic and acidic residues|||Disordered|||Phosphoserine; by DYRK2|||Polar residues ^@ http://togogenome.org/gene/10090:Map4k5 ^@ http://purl.uniprot.org/uniprot/Q05BG3|||http://purl.uniprot.org/uniprot/Q8BPM2 ^@ 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 ^@ Basic and acidic residues|||CNH|||Disordered|||In isoform 2.|||Mitogen-activated protein kinase kinase kinase kinase 5|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086283|||http://purl.uniprot.org/annotation/VSP_050478 http://togogenome.org/gene/10090:Or13a18 ^@ http://purl.uniprot.org/uniprot/Q8VGJ4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdk5rap2 ^@ http://purl.uniprot.org/uniprot/Q0VGR5|||http://purl.uniprot.org/uniprot/Q8K389 ^@ 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|||CDK5 regulatory subunit-associated protein 2|||Centrosomin N-terminal motif 1|||Disordered|||Interaction with CDK5R1|||Interaction with NCKAP5L|||Interaction with PCNT|||Interaction with PCNT and AKAP9|||Phosphoserine|||Phosphothreonine|||Required for centrosomal attachment, Golgi localization and CALM1 interaction|||Required for centrosomal attachment, Golgi targeting and CALM1 interaction ^@ http://purl.uniprot.org/annotation/PRO_0000089837 http://togogenome.org/gene/10090:Gnpnat1 ^@ http://purl.uniprot.org/uniprot/Q9JK38 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Glucosamine 6-phosphate N-acetyltransferase|||N-acetyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000074554 http://togogenome.org/gene/10090:Zdhhc20 ^@ http://purl.uniprot.org/uniprot/Q5Y5T1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Helical|||Important for selectivity toward medium-length fatty acids|||In isoform 2.|||Lumenal|||Palmitoyltransferase ZDHHC20|||Phosphoserine|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212907|||http://purl.uniprot.org/annotation/VSP_016278 http://togogenome.org/gene/10090:Col20a1 ^@ http://purl.uniprot.org/uniprot/Q923P0 ^@ 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 ^@ Collagen alpha-1(XX) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||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.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000393005|||http://purl.uniprot.org/annotation/VSP_038879 http://togogenome.org/gene/10090:Lias ^@ http://purl.uniprot.org/uniprot/A0A0M3HEP3|||http://purl.uniprot.org/uniprot/Q99M04 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Transit Peptide ^@ Lipoyl synthase, mitochondrial|||Mitochondrion|||Radical SAM core ^@ http://purl.uniprot.org/annotation/PRO_0000017724 http://togogenome.org/gene/10090:Vmn1r236 ^@ http://purl.uniprot.org/uniprot/Q05A06 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nrip1 ^@ http://purl.uniprot.org/uniprot/Q8CBD1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes binding to RAR, RXR and RAR/RXR.|||Basic and acidic residues|||CTBP-binding|||CTBP-binding; principal site|||Disordered|||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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces binding to RAR, RXR and RAR/RXR.|||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_0000057952 http://togogenome.org/gene/10090:Ctnnd2 ^@ http://purl.uniprot.org/uniprot/E9QKH8|||http://purl.uniprot.org/uniprot/O35927|||http://purl.uniprot.org/uniprot/Q3U8L7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ ARM|||ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Catenin delta-2|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000064300|||http://purl.uniprot.org/annotation/VSP_006747 http://togogenome.org/gene/10090:Fndc9 ^@ http://purl.uniprot.org/uniprot/Q8BJN4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Transmembrane ^@ Fibronectin type III domain-containing protein 9|||Fibronectin type-III|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000299410 http://togogenome.org/gene/10090:Il12a ^@ http://purl.uniprot.org/uniprot/P43431|||http://purl.uniprot.org/uniprot/Q549G3 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Interchain (with C-197 in IL12B)|||Interleukin-12 subunit alpha|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015608|||http://purl.uniprot.org/annotation/PRO_5014205875 http://togogenome.org/gene/10090:Mns1 ^@ http://purl.uniprot.org/uniprot/Q61884 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue ^@ Meiosis-specific nuclear structural protein 1|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000298923 http://togogenome.org/gene/10090:Ttc23l ^@ http://purl.uniprot.org/uniprot/A6H6E9 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Tetratricopeptide repeat protein 23-like ^@ http://purl.uniprot.org/annotation/PRO_0000336081 http://togogenome.org/gene/10090:Selenoh ^@ http://purl.uniprot.org/uniprot/Q3UQA7 ^@ 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_0000318631 http://togogenome.org/gene/10090:Acox3 ^@ http://purl.uniprot.org/uniprot/Q3TAW3|||http://purl.uniprot.org/uniprot/Q9EPL9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict ^@ Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA oxidase C-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||Microbody targeting signal|||N6-succinyllysine|||Peroxisomal acyl-coenzyme A oxidase 3|||Phosphoserine|||Phosphothreonine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000204686 http://togogenome.org/gene/10090:Fam13b ^@ http://purl.uniprot.org/uniprot/Q8K2H3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM13B|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000058925 http://togogenome.org/gene/10090:Or5an1 ^@ http://purl.uniprot.org/uniprot/Q7TQR9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gm4724 ^@ http://purl.uniprot.org/uniprot/A2ART4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ppp1r7 ^@ http://purl.uniprot.org/uniprot/Q3UM45 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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|||LRRCT|||N-acetylalanine|||Phosphoserine|||Polar residues|||Protein phosphatase 1 regulatory subunit 7|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000239614 http://togogenome.org/gene/10090:Pkm ^@ http://purl.uniprot.org/uniprot/P52480 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ 4-hydroxyproline|||Abolishes amino-acid binding without affecting interaction with the translating ribosome.|||Abolishes pyruvate kinase activity without affecting interaction with the ribosome.|||Crucial for phosphotyrosine binding|||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 M1.|||Interaction with POU5F1|||Intersubunit contact|||N6,N6,N6-trimethyllysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pyruvate kinase PKM|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000112089|||http://purl.uniprot.org/annotation/VSP_025057 http://togogenome.org/gene/10090:Or5bh3 ^@ http://purl.uniprot.org/uniprot/Q8VF35 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lypla1 ^@ http://purl.uniprot.org/uniprot/P97823 ^@ 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 ^@ Abolishes lysophospholipase activity.|||Acyl-protein thioesterase 1|||Charge relay system|||In isoform 2.|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000102268|||http://purl.uniprot.org/annotation/VSP_009197 http://togogenome.org/gene/10090:Gm10408 ^@ http://purl.uniprot.org/uniprot/K7N693 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:Or4k47 ^@ http://purl.uniprot.org/uniprot/Q8VGE8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sorcs1 ^@ http://purl.uniprot.org/uniprot/A0A1B0GRC4|||http://purl.uniprot.org/uniprot/A0A1B0GRN1|||http://purl.uniprot.org/uniprot/A0A1B0GT94|||http://purl.uniprot.org/uniprot/Q8BSV0 ^@ 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|||PKD|||PKD domain-containing protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5004303770|||http://purl.uniprot.org/annotation/PRO_5008408545|||http://purl.uniprot.org/annotation/PRO_5008408589|||http://purl.uniprot.org/annotation/PRO_5008408599 http://togogenome.org/gene/10090:Pnrc1 ^@ http://purl.uniprot.org/uniprot/Q3TWH3 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Rab15 ^@ http://purl.uniprot.org/uniprot/D3YTZ8|||http://purl.uniprot.org/uniprot/Q3TYB1|||http://purl.uniprot.org/uniprot/Q3TYH2 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Ttll12 ^@ http://purl.uniprot.org/uniprot/Q3UDE2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ TTL|||Tubulin--tyrosine ligase-like protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000326166 http://togogenome.org/gene/10090:Vmn1r90 ^@ http://purl.uniprot.org/uniprot/A0A087WR36 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mup16 ^@ http://purl.uniprot.org/uniprot/A2CGB6|||http://purl.uniprot.org/uniprot/A9C496|||http://purl.uniprot.org/uniprot/P02762 ^@ 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 ^@ Lipocalin/cytosolic fatty-acid binding|||Major urinary protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000017932|||http://purl.uniprot.org/annotation/PRO_5002736258|||http://purl.uniprot.org/annotation/PRO_5014296800 http://togogenome.org/gene/10090:Mtrex ^@ http://purl.uniprot.org/uniprot/Q9CZU3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||DEIH box|||Disordered|||Exosome RNA helicase MTR4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000102095 http://togogenome.org/gene/10090:Or5ak24 ^@ http://purl.uniprot.org/uniprot/Q8VF73 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc11a1 ^@ http://purl.uniprot.org/uniprot/P41251 ^@ 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|||Found in strains resistant to unrelated intracellular parasites, such as Mycobacterium bovis, Salmonella typhimurium and Leishmania donovani; highly glycosylated; locates properly to macrophage late endosome/lysosome membranes; has divalent transition metal transporter activity.|||Helical|||N-linked (GlcNAc...) asparagine|||Natural resistance-associated macrophage protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000212589 http://togogenome.org/gene/10090:Csmd1 ^@ http://purl.uniprot.org/uniprot/Q5DTU1|||http://purl.uniprot.org/uniprot/Q923L3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||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 1|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||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_0000021026|||http://purl.uniprot.org/annotation/VSP_009036|||http://purl.uniprot.org/annotation/VSP_009037 http://togogenome.org/gene/10090:Snapin ^@ http://purl.uniprot.org/uniprot/Q9Z266 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ 3.5-fold increase in SNAP25 binding.|||In isoform 2.|||Inhibition of phosphorylation.|||Interaction with TOR1A|||N-acetylalanine|||No effect.|||Phosphoserine|||Phosphoserine; by PKA; in vitro|||Phosphothreonine|||Phosphotyrosine|||Removed|||SNARE-associated protein Snapin ^@ http://purl.uniprot.org/annotation/PRO_0000097557|||http://purl.uniprot.org/annotation/VSP_009165|||http://purl.uniprot.org/annotation/VSP_009166 http://togogenome.org/gene/10090:Endov ^@ http://purl.uniprot.org/uniprot/Q8C9A2 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Endonuclease V|||In isoform 2.|||Interaction with target DNA|||No effect on activity. ^@ http://purl.uniprot.org/annotation/PRO_0000349224|||http://purl.uniprot.org/annotation/VSP_041579 http://togogenome.org/gene/10090:Mep1b ^@ http://purl.uniprot.org/uniprot/Q61847 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||Interchain|||MAM|||MATH|||Mediates preference for acidic residues at subsite P1'|||Meprin A subunit beta|||N-linked (GlcNAc...) asparagine|||Peptidase M12A ^@ http://purl.uniprot.org/annotation/PRO_0000028885|||http://purl.uniprot.org/annotation/PRO_0000028886|||http://purl.uniprot.org/annotation/VSP_005460 http://togogenome.org/gene/10090:Btbd35f12 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQP3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Myh14 ^@ http://purl.uniprot.org/uniprot/Q6URW6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant ^@ Actin-binding|||Basic and acidic residues|||Disordered|||IQ|||In isoform 2 and isoform 3.|||In isoform 3.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-14|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000123432|||http://purl.uniprot.org/annotation/VSP_014633|||http://purl.uniprot.org/annotation/VSP_044759 http://togogenome.org/gene/10090:Gucy2c ^@ http://purl.uniprot.org/uniprot/Q3UWA6 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Guanylate cyclase|||Guanylyl cyclase C|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000280396|||http://purl.uniprot.org/annotation/VSP_023652 http://togogenome.org/gene/10090:Zfp711 ^@ http://purl.uniprot.org/uniprot/E9PUP8|||http://purl.uniprot.org/uniprot/Q8BYM9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||Transcriptional activator Zfx / Zfy ^@ http://togogenome.org/gene/10090:Or10v9 ^@ http://purl.uniprot.org/uniprot/Q7TQS3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Jhy ^@ http://purl.uniprot.org/uniprot/E9Q793 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Jhy protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000442261 http://togogenome.org/gene/10090:St6galnac6 ^@ http://purl.uniprot.org/uniprot/E9PUI0|||http://purl.uniprot.org/uniprot/Q9JM95 ^@ 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 ^@ Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000314796|||http://purl.uniprot.org/annotation/VSP_030360|||http://purl.uniprot.org/annotation/VSP_030361|||http://purl.uniprot.org/annotation/VSP_030362 http://togogenome.org/gene/10090:Ptpn13 ^@ http://purl.uniprot.org/uniprot/G5E8B1|||http://purl.uniprot.org/uniprot/Q3TPD6|||http://purl.uniprot.org/uniprot/Q3TTT8|||http://purl.uniprot.org/uniprot/Q64512|||http://purl.uniprot.org/uniprot/Q8BV52 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||Disordered|||FERM|||KIND|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 13 ^@ http://purl.uniprot.org/annotation/PRO_0000219436 http://togogenome.org/gene/10090:Cox15 ^@ http://purl.uniprot.org/uniprot/Q8BJ03 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Cytochrome c oxidase assembly protein COX15 homolog|||Helical|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000183932|||http://purl.uniprot.org/annotation/VSP_011282 http://togogenome.org/gene/10090:Cherp ^@ http://purl.uniprot.org/uniprot/A0A1D5RL92|||http://purl.uniprot.org/uniprot/Q8CGZ0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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_0000299493 http://togogenome.org/gene/10090:1700010I14Rik ^@ http://purl.uniprot.org/uniprot/Q3TTN6|||http://purl.uniprot.org/uniprot/Q7TPG0|||http://purl.uniprot.org/uniprot/Q9CVW1|||http://purl.uniprot.org/uniprot/Q9DAH6 ^@ Coiled-Coil|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Domain Extent|||Non-terminal Residue ^@ Translin-associated factor X-interacting protein 1 N-terminal ^@ http://togogenome.org/gene/10090:Akap4 ^@ http://purl.uniprot.org/uniprot/A1L3T6|||http://purl.uniprot.org/uniprot/Q60662 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||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|||Polar residues|||RII binding ^@ http://purl.uniprot.org/annotation/PRO_0000020659|||http://purl.uniprot.org/annotation/PRO_0000020660|||http://purl.uniprot.org/annotation/VSP_004100 http://togogenome.org/gene/10090:Usp27x ^@ http://purl.uniprot.org/uniprot/Q8CEG8 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict ^@ Loss of catalytic activity. No effect on BCL2L11-binding, BCL2L11 stabilization, nor on apoptosis.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 27 ^@ http://purl.uniprot.org/annotation/PRO_0000367515 http://togogenome.org/gene/10090:Slc39a13 ^@ http://purl.uniprot.org/uniprot/B2RQ45|||http://purl.uniprot.org/uniprot/Q8BZH0 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Partially rescue the unresponsiveness of osteoblasts and fibroblasts lacking Slc39a13 against BMP4 and TGFB1.|||XEXPHE-motif|||Zinc transporter ZIP13 ^@ http://purl.uniprot.org/annotation/PRO_0000312310|||http://purl.uniprot.org/annotation/PRO_5015087140|||http://purl.uniprot.org/annotation/VSP_029820|||http://purl.uniprot.org/annotation/VSP_029821|||http://purl.uniprot.org/annotation/VSP_029822 http://togogenome.org/gene/10090:Phf19 ^@ http://purl.uniprot.org/uniprot/Q9CXG9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Disordered|||Does not affect ability to promote H3K27me3 methylation; when associated with S-75.|||Does not affect ability to promote H3K27me3 methylation; when associated with S-78.|||Histone H3K36me3 binding|||Impairs ability to promote H3K27me3 methylation without affecting ability to associate with the PRC2 complex; when associated with A-48.|||Impairs ability to promote H3K27me3 methylation without affecting ability to associate with the PRC2 complex; when associated with A-54.|||Impairs ability to promote H3K27me3 methylation without affecting ability to associate with the PRC2 complex; when associated with A-72.|||Impairs ability to promote H3K27me3 methylation without affecting ability to associate with the PRC2 complex; when associated with A-74.|||Important for PRC2 dimer stability|||Interaction with SUZ12|||PHD finger protein 19|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Tudor ^@ http://purl.uniprot.org/annotation/PRO_0000318571 http://togogenome.org/gene/10090:Ntf5 ^@ http://purl.uniprot.org/uniprot/Q80VU4 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Neurotrophin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000019671|||http://purl.uniprot.org/annotation/PRO_0000019672 http://togogenome.org/gene/10090:Gm20736 ^@ http://purl.uniprot.org/uniprot/J3QNV4|||http://purl.uniprot.org/uniprot/Q497M4 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Rnf157 ^@ http://purl.uniprot.org/uniprot/A2AAN9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||RING-type ^@ http://togogenome.org/gene/10090:Or5p76 ^@ http://purl.uniprot.org/uniprot/Q8VG09 ^@ 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 5P76 ^@ http://purl.uniprot.org/annotation/PRO_0000150853 http://togogenome.org/gene/10090:Cyp46a1 ^@ http://purl.uniprot.org/uniprot/Q3US73|||http://purl.uniprot.org/uniprot/Q9WVK8 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Signal Peptide|||Transmembrane ^@ Cholesterol 24-hydroxylase|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051995|||http://purl.uniprot.org/annotation/PRO_5009970841 http://togogenome.org/gene/10090:Slamf8 ^@ http://purl.uniprot.org/uniprot/Q3UQA2|||http://purl.uniprot.org/uniprot/Q9D3G2 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||SLAM family member 8 ^@ http://purl.uniprot.org/annotation/PRO_0000014966|||http://purl.uniprot.org/annotation/PRO_5015097495 http://togogenome.org/gene/10090:Ddx10 ^@ http://purl.uniprot.org/uniprot/Q80Y44 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region ^@ 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|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Probable ATP-dependent RNA helicase DDX10|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000055084 http://togogenome.org/gene/10090:Timm10 ^@ http://purl.uniprot.org/uniprot/P62073 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Disulfide Bond|||Motif|||Sequence Conflict ^@ Mitochondrial import inner membrane translocase subunit Tim10|||Twin CX3C motif ^@ http://purl.uniprot.org/annotation/PRO_0000193613 http://togogenome.org/gene/10090:Cntnap5c ^@ http://purl.uniprot.org/uniprot/Q0V8T7 ^@ 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 ^@ Contactin-associated protein like 5-3|||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_0000317380 http://togogenome.org/gene/10090:Or13e8 ^@ http://purl.uniprot.org/uniprot/Q80ZX9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ptpn7 ^@ http://purl.uniprot.org/uniprot/Q8BUM3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Cysteine sulfenic acid (-SOH)|||Disordered|||Interaction with MAP kinases|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 7 ^@ http://purl.uniprot.org/annotation/PRO_0000094762 http://togogenome.org/gene/10090:Msl3l2 ^@ http://purl.uniprot.org/uniprot/G3X992 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||MRG ^@ http://togogenome.org/gene/10090:Rdh16f2 ^@ http://purl.uniprot.org/uniprot/Q8K3M0|||http://purl.uniprot.org/uniprot/Q8K3M1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5004309105|||http://purl.uniprot.org/annotation/PRO_5015099232 http://togogenome.org/gene/10090:Cd59a ^@ http://purl.uniprot.org/uniprot/A2BI31|||http://purl.uniprot.org/uniprot/O55186 ^@ 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 ^@ CD59A glycoprotein|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036112|||http://purl.uniprot.org/annotation/PRO_0000036113|||http://purl.uniprot.org/annotation/PRO_5014296794 http://togogenome.org/gene/10090:Ypel5 ^@ http://purl.uniprot.org/uniprot/P62700 ^@ 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_0000212397 http://togogenome.org/gene/10090:Fpr-rs4 ^@ http://purl.uniprot.org/uniprot/A4FUQ5 ^@ 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|||Formyl peptide receptor-related sequence 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 ^@ http://purl.uniprot.org/annotation/PRO_0000382024 http://togogenome.org/gene/10090:Chp2 ^@ http://purl.uniprot.org/uniprot/Q9D869 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict ^@ Calcineurin B homologous protein 2|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||N-myristoyl glycine|||Nuclear export signal|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073849 http://togogenome.org/gene/10090:Art5 ^@ http://purl.uniprot.org/uniprot/P70352|||http://purl.uniprot.org/uniprot/Q14AG6|||http://purl.uniprot.org/uniprot/Q3V0V9 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Ecto-ADP-ribosyltransferase 5|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||NAD(P)(+)--arginine ADP-ribosyltransferase|||TR mART core ^@ http://purl.uniprot.org/annotation/PRO_0000019334|||http://purl.uniprot.org/annotation/PRO_5005143238|||http://purl.uniprot.org/annotation/PRO_5014205732|||http://purl.uniprot.org/annotation/VSP_003380|||http://purl.uniprot.org/annotation/VSP_003381|||http://purl.uniprot.org/annotation/VSP_003382|||http://purl.uniprot.org/annotation/VSP_003383 http://togogenome.org/gene/10090:Gm21209 ^@ http://purl.uniprot.org/uniprot/J3QNI1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Sim1 ^@ http://purl.uniprot.org/uniprot/Q61045 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ 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_0000127440 http://togogenome.org/gene/10090:Anapc1 ^@ http://purl.uniprot.org/uniprot/P53995 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Anaphase-promoting complex subunit 1|||Disordered|||PC 1|||PC 2|||PC 3|||PC 4|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000215872 http://togogenome.org/gene/10090:Polr3k ^@ http://purl.uniprot.org/uniprot/Q3TSW1|||http://purl.uniprot.org/uniprot/Q9CQZ7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Zinc Finger ^@ C4-type|||DNA-directed RNA polymerase III subunit RPC10|||TFIIS-type ^@ http://purl.uniprot.org/annotation/PRO_0000121476 http://togogenome.org/gene/10090:Irf4 ^@ http://purl.uniprot.org/uniprot/Q5SUZ4|||http://purl.uniprot.org/uniprot/Q5SUZ5|||http://purl.uniprot.org/uniprot/Q64287 ^@ Chain|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand ^@ Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Splice Variant|||Strand ^@ IRF tryptophan pentad repeat|||In isoform 2.|||Interferon regulatory factor 4|||Phosphoserine; by ROCK2 ^@ http://purl.uniprot.org/annotation/PRO_0000154557|||http://purl.uniprot.org/annotation/VSP_002756 http://togogenome.org/gene/10090:Kbtbd2 ^@ http://purl.uniprot.org/uniprot/G3X9X1|||http://purl.uniprot.org/uniprot/Q6ZPP6 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat ^@ Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Repeat ^@ 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_0000457779 http://togogenome.org/gene/10090:Zfp334 ^@ http://purl.uniprot.org/uniprot/A2A4U6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Aebp1 ^@ http://purl.uniprot.org/uniprot/Q640N1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Adipocyte enhancer-binding protein 1|||Basic and acidic residues|||Disordered|||F5/8 type C|||Impairs DNA-binding and phosphorylation by MAPK1.|||Impairs DNA-binding.|||In isoform 2.|||Interaction with MAPK1 and MAPK3|||Interaction with PTEN|||N-linked (GlcNAc...) asparagine|||Polar residues|||Required for DNA-binding and interaction with NFKBIA|||Required for transcriptional repression ^@ http://purl.uniprot.org/annotation/PRO_0000333190|||http://purl.uniprot.org/annotation/VSP_033470 http://togogenome.org/gene/10090:Snrpn ^@ http://purl.uniprot.org/uniprot/P63163|||http://purl.uniprot.org/uniprot/Q3UN87 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||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_0000125524 http://togogenome.org/gene/10090:Pom121 ^@ http://purl.uniprot.org/uniprot/Q3U425|||http://purl.uniprot.org/uniprot/Q8K3Z9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Basic and acidic residues|||Cisternal side|||Cleavage; by caspase-3|||Disordered|||Helical|||Nuclear envelope pore membrane protein POM 121|||Phosphoserine|||Polar residues|||Pore side ^@ http://purl.uniprot.org/annotation/PRO_0000204907 http://togogenome.org/gene/10090:Tlcd5 ^@ http://purl.uniprot.org/uniprot/Q3TYE7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Transmembrane ^@ Helical|||TLC|||TLC domain-containing protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000285584 http://togogenome.org/gene/10090:Lrp11 ^@ http://purl.uniprot.org/uniprot/Q8CB67 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||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_0000017338 http://togogenome.org/gene/10090:Foxh1 ^@ http://purl.uniprot.org/uniprot/O88621|||http://purl.uniprot.org/uniprot/Q0VEP8 ^@ 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 ^@ Disordered|||Fast/FoxH1 motif 1 (FM1)|||Fast/FoxH1 motif 2 (FM2)|||Fork-head|||Forkhead box protein H1|||In isoform Short.|||Polar residues|||Pro residues|||SMAD interaction motif (SIM)|||SMAD-interaction domain (SID) ^@ http://purl.uniprot.org/annotation/PRO_0000091843|||http://purl.uniprot.org/annotation/VSP_001542 http://togogenome.org/gene/10090:Stk4 ^@ http://purl.uniprot.org/uniprot/Q9JI11 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Site ^@ Cleavage; by caspase-3|||Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||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_0000246627|||http://purl.uniprot.org/annotation/PRO_0000413741|||http://purl.uniprot.org/annotation/PRO_0000413742 http://togogenome.org/gene/10090:Fahd1 ^@ http://purl.uniprot.org/uniprot/Q8R0F8 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Acylpyruvase FAHD1, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000156830 http://togogenome.org/gene/10090:Gin1 ^@ http://purl.uniprot.org/uniprot/Q8K259 ^@ 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 ^@ Gypsy retrotransposon integrase-like protein 1|||In isoform 2.|||In isoform 3.|||Integrase catalytic|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000333018|||http://purl.uniprot.org/annotation/VSP_033440|||http://purl.uniprot.org/annotation/VSP_033441|||http://purl.uniprot.org/annotation/VSP_033442 http://togogenome.org/gene/10090:Gm9839 ^@ http://purl.uniprot.org/uniprot/Q6IE03 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Ubiquitin-like protease family profile ^@ http://togogenome.org/gene/10090:Sema4a ^@ http://purl.uniprot.org/uniprot/Q62178 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||PSI|||Sema|||Semaphorin-4A ^@ http://purl.uniprot.org/annotation/PRO_0000032323 http://togogenome.org/gene/10090:Or5p78 ^@ http://purl.uniprot.org/uniprot/Q7TRU6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rbl1 ^@ http://purl.uniprot.org/uniprot/Q3UI58|||http://purl.uniprot.org/uniprot/Q64701|||http://purl.uniprot.org/uniprot/Q6PAR4 ^@ 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 ^@ Cyclin-like|||Domain A|||Domain B|||In isoform Short.|||Phosphoserine|||Phosphothreonine|||Pocket; binds T and E1A|||Retinoblastoma-associated protein A-box|||Retinoblastoma-associated protein C-terminal|||Retinoblastoma-associated protein N-terminal|||Retinoblastoma-like protein 1|||Spacer ^@ http://purl.uniprot.org/annotation/PRO_0000167840|||http://purl.uniprot.org/annotation/VSP_005537|||http://purl.uniprot.org/annotation/VSP_005538 http://togogenome.org/gene/10090:Heatr6 ^@ http://purl.uniprot.org/uniprot/Q6P1G0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Region|||Repeat ^@ Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT repeat-containing protein 6|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000337174 http://togogenome.org/gene/10090:Vmn1r137 ^@ http://purl.uniprot.org/uniprot/D3YTY1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tmem26 ^@ http://purl.uniprot.org/uniprot/Q149T4|||http://purl.uniprot.org/uniprot/Q3UP23 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 26 ^@ http://purl.uniprot.org/annotation/PRO_0000245866 http://togogenome.org/gene/10090:Ahctf1 ^@ http://purl.uniprot.org/uniprot/Q8CJF7 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ A.T hook|||Abolishes nuclear pore localization; when associated with 272-GSGSGSGSG-280.|||Abolishes nuclear pore localization; when associated with S-284.|||Basic and acidic residues|||Disordered|||Important for nuclear localization|||Important for nuclear localization and chromatin binding|||Mediates transcriptional activity|||N6-acetyllysine|||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_0000246320 http://togogenome.org/gene/10090:Vmn1r202 ^@ http://purl.uniprot.org/uniprot/Q8R259 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dbndd1 ^@ http://purl.uniprot.org/uniprot/H3BK17|||http://purl.uniprot.org/uniprot/H3BKU0|||http://purl.uniprot.org/uniprot/Q9CZ00 ^@ 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.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000291747|||http://purl.uniprot.org/annotation/VSP_026215 http://togogenome.org/gene/10090:Kcnd1 ^@ http://purl.uniprot.org/uniprot/A2AEX0|||http://purl.uniprot.org/uniprot/Q03719 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ BTB|||Cytoplasmic|||Disordered|||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|||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_0000054062|||http://purl.uniprot.org/annotation/PRO_5014296787 http://togogenome.org/gene/10090:Mthfsd ^@ http://purl.uniprot.org/uniprot/Q3URQ7 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||Methenyltetrahydrofolate synthase domain-containing protein|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000295872|||http://purl.uniprot.org/annotation/VSP_027116|||http://purl.uniprot.org/annotation/VSP_027117|||http://purl.uniprot.org/annotation/VSP_027118 http://togogenome.org/gene/10090:Cfap97d2 ^@ http://purl.uniprot.org/uniprot/G3UW36 ^@ Chain|||Molecule Processing ^@ Chain ^@ Uncharacterized protein CFAP97D2 ^@ http://purl.uniprot.org/annotation/PRO_0000445067 http://togogenome.org/gene/10090:Defb43 ^@ http://purl.uniprot.org/uniprot/Q30KM9 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 43 ^@ http://purl.uniprot.org/annotation/PRO_0000352716 http://togogenome.org/gene/10090:Zfp512b ^@ http://purl.uniprot.org/uniprot/B7ZCR6|||http://purl.uniprot.org/uniprot/Q6ZPW1 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Hdc ^@ http://purl.uniprot.org/uniprot/P23738 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Histidine decarboxylase|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_0000146951 http://togogenome.org/gene/10090:Dcps ^@ http://purl.uniprot.org/uniprot/Q9DAR7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Histidine triad motif|||N-acetylalanine|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Removed|||m7GpppX diphosphatase|||nuclear export sequence (NES)|||nuclear localization signal (NLS) ^@ http://purl.uniprot.org/annotation/PRO_0000109795 http://togogenome.org/gene/10090:Mat2b ^@ http://purl.uniprot.org/uniprot/Q99LB6 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Methionine adenosyltransferase 2 subunit beta|||Phosphothreonine|||Required for interaction with MAT2A ^@ http://purl.uniprot.org/annotation/PRO_0000287521|||http://purl.uniprot.org/annotation/VSP_025541 http://togogenome.org/gene/10090:Zfp608 ^@ http://purl.uniprot.org/uniprot/B9EKR3|||http://purl.uniprot.org/uniprot/Q56A10 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||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.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 608 ^@ http://purl.uniprot.org/annotation/PRO_0000280421|||http://purl.uniprot.org/annotation/VSP_023665|||http://purl.uniprot.org/annotation/VSP_023666|||http://purl.uniprot.org/annotation/VSP_023667|||http://purl.uniprot.org/annotation/VSP_023668 http://togogenome.org/gene/10090:Faap24 ^@ http://purl.uniprot.org/uniprot/Q8BHL6 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Fanconi anemia core complex-associated protein 24 ^@ http://purl.uniprot.org/annotation/PRO_0000270962 http://togogenome.org/gene/10090:Supt4a ^@ http://purl.uniprot.org/uniprot/P63271 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ C4-type|||Interaction with SUPT5H|||N-acetylalanine|||Removed|||Transcription elongation factor SPT4-A ^@ http://purl.uniprot.org/annotation/PRO_0000210327 http://togogenome.org/gene/10090:Gm20834 ^@ http://purl.uniprot.org/uniprot/J3QM72 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Btbd35f21 ^@ http://purl.uniprot.org/uniprot/A0A140T8Q5|||http://purl.uniprot.org/uniprot/Q99N64 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Motif|||Sequence Conflict ^@ BTB|||Germ cell-less protein-like 2|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000087522 http://togogenome.org/gene/10090:Tmem156 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLR8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Bmerb1 ^@ http://purl.uniprot.org/uniprot/Q8R1Y2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||bMERB|||bMERB domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000079282 http://togogenome.org/gene/10090:Rmnd1 ^@ http://purl.uniprot.org/uniprot/Q8CI78 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||Required for meiotic nuclear division protein 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000229734 http://togogenome.org/gene/10090:Nat9 ^@ http://purl.uniprot.org/uniprot/Q3UG98 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Alpha/beta-tubulin-N-acetyltransferase 9|||N-acetyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000286875 http://togogenome.org/gene/10090:Cuzd1 ^@ http://purl.uniprot.org/uniprot/P70412 ^@ 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 ^@ CUB 1|||CUB 2|||CUB and zona pellucida-like domain-containing protein 1|||Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||ZP ^@ http://purl.uniprot.org/annotation/PRO_0000233332 http://togogenome.org/gene/10090:Itgae ^@ http://purl.uniprot.org/uniprot/Q60677|||http://purl.uniprot.org/uniprot/Q8BS01 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Integrin alpha-E|||Integrin alpha-E heavy chain|||Integrin alpha-E light chain|||N-linked (GlcNAc...) asparagine|||VWFA|||VWFA domain-containing protein|||X-domain (extra domain) ^@ http://purl.uniprot.org/annotation/PRO_0000016286|||http://purl.uniprot.org/annotation/PRO_0000016287|||http://purl.uniprot.org/annotation/PRO_0000016288|||http://purl.uniprot.org/annotation/PRO_5015020117 http://togogenome.org/gene/10090:Akr1a1 ^@ http://purl.uniprot.org/uniprot/Q540D7|||http://purl.uniprot.org/uniprot/Q80XJ7|||http://purl.uniprot.org/uniprot/Q9JII6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site|||Strand ^@ Aldo-keto reductase family 1 member A1|||Lowers pKa of active site Tyr|||N-acetylthreonine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||NADP-dependent oxidoreductase|||Phosphoserine|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000124618 http://togogenome.org/gene/10090:Ankrd35 ^@ http://purl.uniprot.org/uniprot/E9Q9D8 ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ ANK|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Fbxo21 ^@ http://purl.uniprot.org/uniprot/Q8VDH1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ F-box|||F-box only protein 21|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000119904|||http://purl.uniprot.org/annotation/VSP_011350 http://togogenome.org/gene/10090:Pcolce ^@ http://purl.uniprot.org/uniprot/Q3UIP2|||http://purl.uniprot.org/uniprot/Q3UN82|||http://purl.uniprot.org/uniprot/Q61398 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||CUB|||CUB 1|||CUB 2|||Disordered|||N-linked (GlcNAc...) asparagine|||NTR|||Phosphoserine|||Phosphothreonine|||Polar residues|||Procollagen C-endopeptidase enhancer 1 ^@ http://purl.uniprot.org/annotation/PRO_0000022024|||http://purl.uniprot.org/annotation/PRO_5004230233|||http://purl.uniprot.org/annotation/PRO_5010843422 http://togogenome.org/gene/10090:Tmprss11c ^@ http://purl.uniprot.org/uniprot/Q1JRP2 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Site|||Topological Domain|||Transmembrane ^@ Abolishes autocatalytic cleavage.|||Charge relay system|||Cleavage|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Reduced autocatalytic cleavage. Strongly reduced autocatalytic cleavage; when associated with A-196. Strongly reduced autocatalytic cleavage; when associated with A-196 and 190-A-A-191.|||SEA|||Strongly reduced autocatalytic cleavage; when associated with A-196 and A-199. Slightly reduced autocatalytic cleavage; when associated with A-196.|||Strongly reduced autocatalytic cleavage; when associated with A-199. Strongly reduced autocatalytic cleavage; when associated with A-199 and 190-A-A-191. Slightly reduced autocatalytic cleavage; when associated with 190-A-A-191.|||Transmembrane protease serine 11C catalytic chain|||Transmembrane protease serine 11C non-catalytic chain ^@ http://purl.uniprot.org/annotation/PRO_0000436381|||http://purl.uniprot.org/annotation/PRO_0000436382 http://togogenome.org/gene/10090:Cant1 ^@ http://purl.uniprot.org/uniprot/Q8VCF1 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Important for dimer formation|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Soluble calcium-activated nucleotidase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000209926|||http://purl.uniprot.org/annotation/VSP_013762|||http://purl.uniprot.org/annotation/VSP_013763|||http://purl.uniprot.org/annotation/VSP_013764 http://togogenome.org/gene/10090:Rars ^@ http://purl.uniprot.org/uniprot/Q9D0I9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 'HIGH' region|||Arginine--tRNA ligase, cytoplasmic|||Could be involved in the assembly of the multisynthetase complex|||Interaction with tRNA|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000151659 http://togogenome.org/gene/10090:Unc13c ^@ http://purl.uniprot.org/uniprot/Q8K0T7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||C2 1|||C2 2|||Disordered|||MHD1|||MHD2|||Omega-N-methylarginine|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Protein unc-13 homolog C ^@ http://purl.uniprot.org/annotation/PRO_0000188579 http://togogenome.org/gene/10090:Proser1 ^@ http://purl.uniprot.org/uniprot/Q5PRE5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Polar residues|||Proline and serine-rich protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000274310 http://togogenome.org/gene/10090:Lrrc61 ^@ http://purl.uniprot.org/uniprot/Q8R2R5 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ LRR 1|||LRR 2|||LRR 3|||LRRCT|||Leucine-rich repeat-containing protein 61 ^@ http://purl.uniprot.org/annotation/PRO_0000236797 http://togogenome.org/gene/10090:Yipf6 ^@ http://purl.uniprot.org/uniprot/Q8BR70 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||N-acetylalanine|||Phosphoserine|||Protein YIPF6|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000242669 http://togogenome.org/gene/10090:Vsx1 ^@ http://purl.uniprot.org/uniprot/A2AQX5|||http://purl.uniprot.org/uniprot/Q91V10 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region ^@ Basic and acidic residues|||CVC|||Disordered|||Homeobox|||Nuclear localization signal|||Octapeptide motif|||Polar residues|||Visual system homeobox 1 ^@ http://purl.uniprot.org/annotation/PRO_0000049356 http://togogenome.org/gene/10090:1700020A23Rik ^@ http://purl.uniprot.org/uniprot/Q9DA59 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Sirt1 ^@ http://purl.uniprot.org/uniprot/Q3UNI1|||http://purl.uniprot.org/uniprot/Q3USJ2|||http://purl.uniprot.org/uniprot/Q3USY7|||http://purl.uniprot.org/uniprot/Q53Z05|||http://purl.uniprot.org/uniprot/Q923E4 ^@ Active Site|||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|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant ^@ Abolished ADP-ribosyltransferase activity in vitro without affecting the NAD-dependent protein deacetylase activity.|||Abolishes in vitro phosphorylation by CaMK2; when associated with A-154; A-649 and A-651.|||Abolishes in vitro phosphorylation by CaMK2; when associated with A-154; A-649 and A-683.|||Abolishes in vitro phosphorylation by CaMK2; when associated with A-154; A-651 and A-683.|||Abolishes in vitro phosphorylation by CaMK2; when associated with A-649; A-651 and A-683.|||Abolishes nuclear export; when associated with A-138; A-139; A-140; A-144 and A-145.|||Abolishes nuclear export; when associated with A-425; A-427; A-428; A-429; A-430 and A-431.|||Abolishes nuclear localization; when associated with A-227; A-228; A-229 and A-230.|||Abolishes nuclear localization; when associated with A-37 and A-38.|||Acidic residues|||Basic and acidic residues|||Deacetylase sirtuin-type|||Decreased acetylation, leading to increased protein deacetylase activity.|||Disordered|||Does not affect S-nitrosylation.|||Does not affect protein deacetylase activity.|||Impairs S-nitrosylation. Abolishes S-nitrosylation; when associated with S-387.|||Impairs S-nitrosylation. Abolishes S-nitrosylation; when associated with S-390.|||In isoform 2.|||Increased deacetylase activity toward p53/TP53 and increases resistance to genotoxic stress (mimicks residue phosphorylation).|||Interaction with CCAR2|||Interaction with CLOCK|||Interaction with H1-4|||Loss of deacetylation activity. Loss of inhibition of E2F1 and loss of coactivation of FOXO1-mediated transcription.|||N-acetylalanine|||N6-acetyllysine|||NAD-dependent protein deacetylase sirtuin-1|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CaMK2|||Phosphoserine; by MAPK8|||Phosphothreonine|||Phosphothreonine; by DYRK1A, DYRK3 and MAPK8|||Polar residues|||Proton acceptor|||Reduces phosphorylation. Impairs deacetylase activity toward p53/TP53 and decreases resistance to genotoxic stress. Does not change nuclear localization.|||Removed|||Required for interaction with the sumoylated form of CCAR2|||S-nitrosocysteine|||SirtT1 75 kDa fragment ^@ http://purl.uniprot.org/annotation/PRO_0000110257|||http://purl.uniprot.org/annotation/PRO_0000415290|||http://purl.uniprot.org/annotation/VSP_042190 http://togogenome.org/gene/10090:Pbrm1 ^@ http://purl.uniprot.org/uniprot/F8VQD1 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ BAH|||Basic and acidic residues|||Bromo|||Disordered|||HMG box|||Polar residues ^@ http://togogenome.org/gene/10090:Znhit6 ^@ http://purl.uniprot.org/uniprot/Q3UFB2 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Box C/D snoRNA protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HIT-type|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000280240|||http://purl.uniprot.org/annotation/VSP_023573 http://togogenome.org/gene/10090:H2ac13 ^@ http://purl.uniprot.org/uniprot/B2RVF0|||http://purl.uniprot.org/uniprot/C0HKE1|||http://purl.uniprot.org/uniprot/C0HKE2|||http://purl.uniprot.org/uniprot/C0HKE3|||http://purl.uniprot.org/uniprot/C0HKE4|||http://purl.uniprot.org/uniprot/C0HKE5|||http://purl.uniprot.org/uniprot/C0HKE6|||http://purl.uniprot.org/uniprot/C0HKE7|||http://purl.uniprot.org/uniprot/C0HKE8|||http://purl.uniprot.org/uniprot/C0HKE9 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Histone H2A type 1-C|||Histone H2A type 1-D|||Histone H2A type 1-E|||Histone H2A type 1-G|||Histone H2A type 1-I|||Histone H2A type 1-N|||Histone H2A type 1-O|||Histone H2A type 1-P|||Histone H2A/H2B/H3|||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_0000439715|||http://purl.uniprot.org/annotation/PRO_0000439716|||http://purl.uniprot.org/annotation/PRO_0000439717|||http://purl.uniprot.org/annotation/PRO_0000439718|||http://purl.uniprot.org/annotation/PRO_0000439719|||http://purl.uniprot.org/annotation/PRO_0000439720|||http://purl.uniprot.org/annotation/PRO_0000439721|||http://purl.uniprot.org/annotation/PRO_0000439722|||http://purl.uniprot.org/annotation/PRO_0000439723 http://togogenome.org/gene/10090:Fanca ^@ http://purl.uniprot.org/uniprot/Q9JL70 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Fanconi anemia group A protein homolog|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000087180 http://togogenome.org/gene/10090:Or10d1c ^@ http://purl.uniprot.org/uniprot/Q9EQ87 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Crk ^@ http://purl.uniprot.org/uniprot/Q3TQV3|||http://purl.uniprot.org/uniprot/Q5ND50|||http://purl.uniprot.org/uniprot/Q5ND51|||http://purl.uniprot.org/uniprot/Q64010|||http://purl.uniprot.org/uniprot/Q8JZR2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Site|||Splice Variant|||Strand ^@ Adapter molecule crk|||Disordered|||In isoform Crk-I.|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Pro residues|||Proline switch|||Removed|||SH2|||SH3|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000079352|||http://purl.uniprot.org/annotation/VSP_004174 http://togogenome.org/gene/10090:Stxbp4 ^@ http://purl.uniprot.org/uniprot/Q9WV89 ^@ 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 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand ^@ Abolishes phosphorylation by PKB/AKT2.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||No effect.|||PDZ|||Phosphoserine|||Phosphoserine; by PKB/AKT2|||Polar residues|||Syntaxin-binding protein 4|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000076331|||http://purl.uniprot.org/annotation/VSP_017179|||http://purl.uniprot.org/annotation/VSP_017180|||http://purl.uniprot.org/annotation/VSP_017181|||http://purl.uniprot.org/annotation/VSP_017182|||http://purl.uniprot.org/annotation/VSP_017183|||http://purl.uniprot.org/annotation/VSP_017184|||http://purl.uniprot.org/annotation/VSP_017185 http://togogenome.org/gene/10090:Zfp128 ^@ http://purl.uniprot.org/uniprot/Q8BGV5 ^@ 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 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_0000436533 http://togogenome.org/gene/10090:Adap1 ^@ http://purl.uniprot.org/uniprot/E9PY16|||http://purl.uniprot.org/uniprot/Q8BVR8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Arf-GAP|||PH ^@ http://togogenome.org/gene/10090:Dipk1c ^@ http://purl.uniprot.org/uniprot/Q8BQT2 ^@ 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_0000286708|||http://purl.uniprot.org/annotation/VSP_039089 http://togogenome.org/gene/10090:Ssbp4 ^@ http://purl.uniprot.org/uniprot/Q3U4B1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||LisH|||Polar residues ^@ http://togogenome.org/gene/10090:Magea4 ^@ http://purl.uniprot.org/uniprot/F2Z493 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Grin2b ^@ http://purl.uniprot.org/uniprot/G3X9V4|||http://purl.uniprot.org/uniprot/Q01097 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Functional determinant of NMDA receptors|||Glutamate receptor|||Glutamate receptor ionotropic, NMDA 2B|||Helical|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000011578|||http://purl.uniprot.org/annotation/PRO_5015091866 http://togogenome.org/gene/10090:Dpcd ^@ http://purl.uniprot.org/uniprot/Q8BPA8 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||Protein DPCD ^@ http://purl.uniprot.org/annotation/PRO_0000323724|||http://purl.uniprot.org/annotation/VSP_032081|||http://purl.uniprot.org/annotation/VSP_032082 http://togogenome.org/gene/10090:F830016B08Rik ^@ http://purl.uniprot.org/uniprot/G3UWE2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||IRG-type G ^@ http://togogenome.org/gene/10090:Pold3 ^@ http://purl.uniprot.org/uniprot/Q8BH76 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Mitd1 ^@ http://purl.uniprot.org/uniprot/Q8VDV8 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict ^@ Important for association with membranes|||MIT|||MIT domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000260496 http://togogenome.org/gene/10090:Try5 ^@ http://purl.uniprot.org/uniprot/Q9QUK9 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Signal Peptide|||Site ^@ Activation peptide|||Charge relay system|||Cleavage; by CTRC|||Cleavage; by autolysis|||Peptidase S1|||Trypsin-5 ^@ http://purl.uniprot.org/annotation/PRO_0000457720|||http://purl.uniprot.org/annotation/PRO_5015099940 http://togogenome.org/gene/10090:Or5as1 ^@ http://purl.uniprot.org/uniprot/Q7TR55 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or5k16 ^@ http://purl.uniprot.org/uniprot/F8VQ90 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Grn ^@ http://purl.uniprot.org/uniprot/P28798|||http://purl.uniprot.org/uniprot/Q3U9N4|||http://purl.uniprot.org/uniprot/Q544Y8|||http://purl.uniprot.org/uniprot/Q9D2V3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Peptide|||Sequence Conflict|||Signal Peptide ^@ Granulin-1|||Granulin-2|||Granulin-3|||Granulin-4|||Granulin-5|||Granulin-6|||Granulin-7|||Granulins|||Granulins domain-containing protein|||N-linked (GlcNAc...) asparagine|||Paragranulin ^@ http://purl.uniprot.org/annotation/PRO_0000012702|||http://purl.uniprot.org/annotation/PRO_0000012703|||http://purl.uniprot.org/annotation/PRO_0000012704|||http://purl.uniprot.org/annotation/PRO_0000012705|||http://purl.uniprot.org/annotation/PRO_0000012706|||http://purl.uniprot.org/annotation/PRO_0000012707|||http://purl.uniprot.org/annotation/PRO_0000012708|||http://purl.uniprot.org/annotation/PRO_0000012709|||http://purl.uniprot.org/annotation/PRO_0000446331|||http://purl.uniprot.org/annotation/PRO_5004324654|||http://purl.uniprot.org/annotation/PRO_5014309562|||http://purl.uniprot.org/annotation/PRO_5015097469 http://togogenome.org/gene/10090:H2-M10.3 ^@ http://purl.uniprot.org/uniprot/Q85ZW6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015098989 http://togogenome.org/gene/10090:Mixl1 ^@ http://purl.uniprot.org/uniprot/Q9WUI0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Disordered|||Homeobox|||Homeobox protein MIXL1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000311334 http://togogenome.org/gene/10090:Guca1b ^@ http://purl.uniprot.org/uniprot/Q8VBV8 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||Guanylyl cyclase-activating protein 2|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073809 http://togogenome.org/gene/10090:Cbs ^@ http://purl.uniprot.org/uniprot/Q91WT9 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Splice Variant ^@ CBS|||Cystathionine beta-synthase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||N6-(pyridoxal phosphate)lysine|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000262592|||http://purl.uniprot.org/annotation/VSP_021790 http://togogenome.org/gene/10090:Vps33a ^@ http://purl.uniprot.org/uniprot/Q9D2N9 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant ^@ Chain|||Sequence Conflict|||Sequence Variant ^@ Detected in mice with the buff mutation; leads to melanocytes with a reduced number of undermelanized melanosomes.|||Vacuolar protein sorting-associated protein 33A ^@ http://purl.uniprot.org/annotation/PRO_0000206303 http://togogenome.org/gene/10090:C1qtnf4 ^@ http://purl.uniprot.org/uniprot/A0A3B0IP17|||http://purl.uniprot.org/uniprot/Q8R066 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide ^@ C1q|||C1q 1|||C1q 2|||Complement C1q tumor necrosis factor-related protein 4|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000003534|||http://purl.uniprot.org/annotation/PRO_5030075160 http://togogenome.org/gene/10090:Upk1a ^@ http://purl.uniprot.org/uniprot/A2RSB9|||http://purl.uniprot.org/uniprot/Q9D132 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Uroplakin-1a ^@ http://purl.uniprot.org/annotation/PRO_0000219287 http://togogenome.org/gene/10090:Nos3 ^@ http://purl.uniprot.org/uniprot/P70313|||http://purl.uniprot.org/uniprot/Q8C5P3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Calmodulin-binding|||Disordered|||FAD-binding FR-type|||Flavodoxin-like|||Interaction with NOSIP|||N-myristoyl glycine|||Nitric oxide synthase 3|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine|||Phosphothreonine; by AMPK|||Pro residues|||Removed|||S-palmitoyl cysteine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000170944 http://togogenome.org/gene/10090:Ccnjl ^@ http://purl.uniprot.org/uniprot/Q5SRT8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Cyclin N-terminal|||Cyclin-J-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000309320 http://togogenome.org/gene/10090:Cnih2 ^@ http://purl.uniprot.org/uniprot/O35089|||http://purl.uniprot.org/uniprot/Q3SYI8 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Topological Domain|||Transmembrane ^@ Chain|||Helix|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Protein cornichon homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000122226 http://togogenome.org/gene/10090:Ncr1 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZY7|||http://purl.uniprot.org/uniprot/Q8C567 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like 1|||Ig-like 2|||Immunoglobulin subtype|||N-linked (GlcNAc...) asparagine|||Natural cytotoxicity triggering receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000015029|||http://purl.uniprot.org/annotation/PRO_5006451915 http://togogenome.org/gene/10090:Cntrob ^@ http://purl.uniprot.org/uniprot/Q8CB62 ^@ 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|||Centrobin|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Required for centrosome localization ^@ http://purl.uniprot.org/annotation/PRO_0000076241|||http://purl.uniprot.org/annotation/VSP_016842 http://togogenome.org/gene/10090:Hes2 ^@ http://purl.uniprot.org/uniprot/O54792 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Orange|||Pro residues|||Transcription factor HES-2|||WRPW motif|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127207 http://togogenome.org/gene/10090:Mark3 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VNZ6|||http://purl.uniprot.org/uniprot/Q03141 ^@ 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 ^@ Active Site|||Binding Site|||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.|||KA1|||MAP/microtubule affinity-regulating kinase 3|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LKB1|||Phosphothreonine; by PKC/PRKCZ|||Polar residues|||Protein kinase|||Proton acceptor|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000086305|||http://purl.uniprot.org/annotation/VSP_016140|||http://purl.uniprot.org/annotation/VSP_016141 http://togogenome.org/gene/10090:Anpep ^@ http://purl.uniprot.org/uniprot/P97449 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Aminopeptidase N|||Cytoplasmic|||Cytosolic Ser/Thr-rich junction|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Metalloprotease|||N-linked (GlcNAc...) asparagine|||No impact on substrate affinity of SLC6A19-mediated amino acid transport.|||Phosphotyrosine|||Proton acceptor|||Reduces substrate affinity of SLC6A19-mediated amino acid transport.|||Sulfotyrosine|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000095082 http://togogenome.org/gene/10090:Spaca9 ^@ http://purl.uniprot.org/uniprot/Q7TPM5 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Sequence Conflict|||Site|||Splice Variant ^@ Essential for interaction with INCA1|||In isoform 2.|||Sperm acrosome-associated protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000089674|||http://purl.uniprot.org/annotation/VSP_046487|||http://purl.uniprot.org/annotation/VSP_046488 http://togogenome.org/gene/10090:Elf4 ^@ http://purl.uniprot.org/uniprot/Q9Z2U4 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||ETS|||ETS-related transcription factor Elf-4|||Higher IL17A, IL1B, IL6, CXCL1 and TREM1 expression in bone marrow-derived macrophages from mutant mice compared to wild-type, after LPS stimulation. CD8+ T cells from mutant mice have reduced PRF1 expression when activated with IL-2 compared to cells from wild-type littermates.|||Higher TNFA, IL1B and IL6 expression in bone marrow-derived and peritoneal macrophages from mutant mice compared to wild-type, after VSV infection. Decreased viral clearance in mutant mice compared to wild-type. Loss of transcriptional activity shown in IFNB1 promoter-driven luciferase assay.|||Phosphoserine|||Polar residues|||RUNX1-binding ^@ http://purl.uniprot.org/annotation/PRO_0000204090 http://togogenome.org/gene/10090:Lim2 ^@ http://purl.uniprot.org/uniprot/P56563 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane ^@ C-linked (Man) tryptophan|||Cytoplasmic|||Extracellular|||Helical|||In To3.|||Lens fiber membrane intrinsic protein|||N-linked (GlcNAc...) asparagine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000164665 http://togogenome.org/gene/10090:Vipr2 ^@ http://purl.uniprot.org/uniprot/P41588|||http://purl.uniprot.org/uniprot/Q546Q8 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Vasoactive intestinal polypeptide receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000012861|||http://purl.uniprot.org/annotation/PRO_5014309643 http://togogenome.org/gene/10090:C2 ^@ http://purl.uniprot.org/uniprot/P21180 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Charge relay system|||Complement C2|||Complement C2a fragment|||Complement C2b fragment|||In isoform Short.|||MIDAS-like motif|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi 1|||Sushi 2|||Sushi 3|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000027613|||http://purl.uniprot.org/annotation/PRO_0000027614|||http://purl.uniprot.org/annotation/PRO_0000027615|||http://purl.uniprot.org/annotation/VSP_005385 http://togogenome.org/gene/10090:Pcmtd2 ^@ http://purl.uniprot.org/uniprot/Q8BHD8 ^@ Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict ^@ AdoMet binding motif|||BC-box|||CUL-box|||Disordered|||N-myristoyl glycine|||Protein-L-isoaspartate O-methyltransferase domain-containing protein 2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000111928 http://togogenome.org/gene/10090:Armc10 ^@ http://purl.uniprot.org/uniprot/Q9D0L7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ ARM|||Armadillo repeat-containing protein 10|||Helical|||In isoform 2.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000297708|||http://purl.uniprot.org/annotation/VSP_027363 http://togogenome.org/gene/10090:Kif9 ^@ http://purl.uniprot.org/uniprot/Q3V3Y6|||http://purl.uniprot.org/uniprot/Q8C0X6|||http://purl.uniprot.org/uniprot/Q9WV04 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Kinesin motor|||Kinesin-like protein KIF9|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000125443 http://togogenome.org/gene/10090:Fsd1 ^@ http://purl.uniprot.org/uniprot/Q7TPM6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ B30.2/SPRY|||COS|||Disordered|||Fibronectin type III and SPRY domain-containing protein 1|||Fibronectin type-III|||In isoform 2.|||Omega-N-methylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000316539|||http://purl.uniprot.org/annotation/VSP_030767 http://togogenome.org/gene/10090:Or11i1 ^@ http://purl.uniprot.org/uniprot/Q8VFC3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Prkcsh ^@ http://purl.uniprot.org/uniprot/O08795|||http://purl.uniprot.org/uniprot/Q3U518 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Signal Peptide|||Splice Variant|||Strand ^@ Acidic residues|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||Glucosidase 2 subunit beta|||In isoform 2.|||LDL-receptor class A 1|||LDL-receptor class A 2|||MRH|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Phosphoserine|||Phosphoserine; by PKC|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000004144|||http://purl.uniprot.org/annotation/VSP_010672 http://togogenome.org/gene/10090:Ppp1r3b ^@ http://purl.uniprot.org/uniprot/Q8C767 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Motif ^@ CBM21|||PP1-binding motif|||Phosphoserine|||Protein phosphatase 1 regulatory subunit 3B ^@ http://purl.uniprot.org/annotation/PRO_0000324544 http://togogenome.org/gene/10090:Prss2 ^@ http://purl.uniprot.org/uniprot/P07146|||http://purl.uniprot.org/uniprot/Q792Y6 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Signal Peptide|||Site ^@ Activation peptide|||Anionic trypsin-2|||Charge relay system|||Peptidase S1|||Required for specificity ^@ http://purl.uniprot.org/annotation/PRO_0000028203|||http://purl.uniprot.org/annotation/PRO_0000028204|||http://purl.uniprot.org/annotation/PRO_5011948595 http://togogenome.org/gene/10090:Slc35f6 ^@ http://purl.uniprot.org/uniprot/Q8VE96 ^@ 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|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ EamA|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Solute carrier family 35 member F6 ^@ http://purl.uniprot.org/annotation/PRO_0000232515 http://togogenome.org/gene/10090:Lgi1 ^@ http://purl.uniprot.org/uniprot/Q9JIA1 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide|||Splice Variant ^@ EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||EAR 7|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||LRRNT|||Leucine-rich glioma-inactivated protein 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017706|||http://purl.uniprot.org/annotation/VSP_061731|||http://purl.uniprot.org/annotation/VSP_061732 http://togogenome.org/gene/10090:Or8b53 ^@ http://purl.uniprot.org/uniprot/E9Q413 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Il13 ^@ http://purl.uniprot.org/uniprot/P20109 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Interleukin-13|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015550 http://togogenome.org/gene/10090:Maneal ^@ http://purl.uniprot.org/uniprot/Q6P1J0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Glycoprotein endo-alpha-1,2-mannosidase-like protein|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000282321 http://togogenome.org/gene/10090:Vps45 ^@ http://purl.uniprot.org/uniprot/P97390 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Vacuolar protein sorting-associated protein 45 ^@ http://purl.uniprot.org/annotation/PRO_0000206313 http://togogenome.org/gene/10090:Zbtb16 ^@ http://purl.uniprot.org/uniprot/Q3UQ17 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BTB|||C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Cypt1 ^@ http://purl.uniprot.org/uniprot/Q8CH20 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Splice Variant ^@ Cysteine-rich perinuclear theca protein 1|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000442286|||http://purl.uniprot.org/annotation/VSP_059219 http://togogenome.org/gene/10090:Pigk ^@ http://purl.uniprot.org/uniprot/Q8BL63|||http://purl.uniprot.org/uniprot/Q9CXY9 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Essential for GPI attachment|||GPI-anchor transamidase|||Helical|||Interchain (with C-186 in PIGT)|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000026530|||http://purl.uniprot.org/annotation/PRO_5015099013 http://togogenome.org/gene/10090:Asprv1 ^@ http://purl.uniprot.org/uniprot/Q09PK2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Transmembrane ^@ Abolishes production of active form of enzyme.|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase A2|||Polar residues|||Retroviral-like aspartic protease 1 ^@ http://purl.uniprot.org/annotation/PRO_0000271173|||http://purl.uniprot.org/annotation/PRO_0000271174|||http://purl.uniprot.org/annotation/PRO_0000271175 http://togogenome.org/gene/10090:Tas2r118 ^@ http://purl.uniprot.org/uniprot/P59529 ^@ 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 16 ^@ http://purl.uniprot.org/annotation/PRO_0000082267 http://togogenome.org/gene/10090:Npas3 ^@ http://purl.uniprot.org/uniprot/F8VQB2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Basic and acidic residues|||Basic residues|||Disordered|||PAS|||Polar residues ^@ http://togogenome.org/gene/10090:Cst3 ^@ http://purl.uniprot.org/uniprot/P21460 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Motif|||Sequence Conflict|||Signal Peptide|||Site ^@ Cystatin-C|||Reactive site|||Secondary area of contact ^@ http://purl.uniprot.org/annotation/PRO_0000006642 http://togogenome.org/gene/10090:Snapc1 ^@ http://purl.uniprot.org/uniprot/Q8K0S9 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||SNAPC3-binding|||SNAPC4-binding|||snRNA-activating protein complex subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072019 http://togogenome.org/gene/10090:Ifih1 ^@ http://purl.uniprot.org/uniprot/D2CGM4|||http://purl.uniprot.org/uniprot/Q3TGP5|||http://purl.uniprot.org/uniprot/Q8R5F7 ^@ 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 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ CARD 1|||CARD 2|||Cleavage|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Interferon-induced helicase C domain-containing protein 1|||Phosphoserine|||Phosphoserine; by RIOK3|||RLR CTR ^@ http://purl.uniprot.org/annotation/PRO_0000102013|||http://purl.uniprot.org/annotation/VSP_013339 http://togogenome.org/gene/10090:Aurkaip1 ^@ http://purl.uniprot.org/uniprot/Q9DCJ7 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Small ribosomal subunit protein mS38 ^@ http://purl.uniprot.org/annotation/PRO_0000064537 http://togogenome.org/gene/10090:Nudc ^@ http://purl.uniprot.org/uniprot/O35685 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Strand|||Turn ^@ Basic and acidic residues|||CS|||Disordered|||Interaction with EML4|||N6-acetyllysine|||Nuclear localization signal|||Nuclear migration protein nudC|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000057991 http://togogenome.org/gene/10090:Clec16a ^@ http://purl.uniprot.org/uniprot/Q80U30 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||FPL|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Protein CLEC16A ^@ http://purl.uniprot.org/annotation/PRO_0000274477|||http://purl.uniprot.org/annotation/VSP_022751|||http://purl.uniprot.org/annotation/VSP_022752|||http://purl.uniprot.org/annotation/VSP_022753|||http://purl.uniprot.org/annotation/VSP_022754|||http://purl.uniprot.org/annotation/VSP_022755|||http://purl.uniprot.org/annotation/VSP_022756|||http://purl.uniprot.org/annotation/VSP_022757|||http://purl.uniprot.org/annotation/VSP_022758|||http://purl.uniprot.org/annotation/VSP_022759 http://togogenome.org/gene/10090:6030458C11Rik ^@ http://purl.uniprot.org/uniprot/Q8BGC1 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Polar residues|||UPF0489 protein C5orf22 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000305003|||http://purl.uniprot.org/annotation/VSP_028185|||http://purl.uniprot.org/annotation/VSP_028186 http://togogenome.org/gene/10090:H2bc6 ^@ http://purl.uniprot.org/uniprot/Q6ZWY9 ^@ 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-C/E/G|||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-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_0000244831 http://togogenome.org/gene/10090:Tfcp2l1 ^@ http://purl.uniprot.org/uniprot/Q3UNW5 ^@ 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|||Grh/CP2 DB|||Mediate transcriptional repression|||Polar residues|||SAM2-like domain|||Transcription factor CP2-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000228007 http://togogenome.org/gene/10090:Efhc1 ^@ http://purl.uniprot.org/uniprot/B2CKC6|||http://purl.uniprot.org/uniprot/Q9D9T8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ DM10|||DM10 1|||DM10 2|||DM10 3|||EF-hand|||EF-hand domain-containing protein 1|||Required for its localization in the mitotic spindle and interaction with alpha-tubulin ^@ http://purl.uniprot.org/annotation/PRO_0000073878 http://togogenome.org/gene/10090:Il3 ^@ http://purl.uniprot.org/uniprot/P01586|||http://purl.uniprot.org/uniprot/Q5SX77 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Strand|||Turn ^@ Disordered|||Interleukin-3|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial ^@ http://purl.uniprot.org/annotation/PRO_0000015519|||http://purl.uniprot.org/annotation/PRO_5014310016 http://togogenome.org/gene/10090:C1galt1 ^@ http://purl.uniprot.org/uniprot/Q9JJ06 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1|||Helical; Signal-anchor for type II membrane protein|||In plt1; loss of function inducing thrombocytopenia and kidney disease.|||Lumenal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000285065 http://togogenome.org/gene/10090:Sh3bp1 ^@ http://purl.uniprot.org/uniprot/A2A5V2|||http://purl.uniprot.org/uniprot/A2A5V3|||http://purl.uniprot.org/uniprot/P55194 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ BAR|||Disordered|||Interaction with CD2AP|||Interaction with CGNL1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho-GAP|||SH3 domain-binding protein 1|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000056724 http://togogenome.org/gene/10090:Isg20l2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0R3|||http://purl.uniprot.org/uniprot/Q3U1G5 ^@ 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|||Exonuclease|||Interferon-stimulated 20 kDa exonuclease-like 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315280 http://togogenome.org/gene/10090:Casr ^@ http://purl.uniprot.org/uniprot/Q9QY96 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cysteine-rich (CR)|||Cytoplasmic|||Disordered|||Extracellular|||Extracellular calcium-sensing receptor|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform B.|||Interaction with RNF19A|||Interchain|||Ligand-binding 1 (LB1)|||Ligand-binding 2 (LB2)|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000012947|||http://purl.uniprot.org/annotation/VSP_002036 http://togogenome.org/gene/10090:Rps24 ^@ http://purl.uniprot.org/uniprot/P62849|||http://purl.uniprot.org/uniprot/Q5M9M7|||http://purl.uniprot.org/uniprot/Q9D7P1 ^@ 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 residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphothreonine|||Small ribosomal subunit protein eS24 ^@ http://purl.uniprot.org/annotation/PRO_0000137625|||http://purl.uniprot.org/annotation/VSP_011365|||http://purl.uniprot.org/annotation/VSP_011366 http://togogenome.org/gene/10090:Rbbp9 ^@ http://purl.uniprot.org/uniprot/O88851 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Region|||Sequence Conflict ^@ Charge relay system|||Involved in binding to RB1|||Putative hydrolase RBBP9|||Retinoblastoma protein binding ^@ http://purl.uniprot.org/annotation/PRO_0000097181 http://togogenome.org/gene/10090:Cep83 ^@ http://purl.uniprot.org/uniprot/Q9D5R3 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Centrosomal protein of 83 kDa|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000234496|||http://purl.uniprot.org/annotation/VSP_018333 http://togogenome.org/gene/10090:Spire1 ^@ http://purl.uniprot.org/uniprot/A0A286YDN9|||http://purl.uniprot.org/uniprot/A0A5H1ZRL1|||http://purl.uniprot.org/uniprot/D3YTL8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||KIND|||Polar residues ^@ http://togogenome.org/gene/10090:Flt3l ^@ http://purl.uniprot.org/uniprot/A9QW46|||http://purl.uniprot.org/uniprot/P49772 ^@ 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|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Fms-related tyrosine kinase 3 ligand|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000021282|||http://purl.uniprot.org/annotation/PRO_5010104502|||http://purl.uniprot.org/annotation/VSP_004253|||http://purl.uniprot.org/annotation/VSP_004254|||http://purl.uniprot.org/annotation/VSP_004255|||http://purl.uniprot.org/annotation/VSP_004256 http://togogenome.org/gene/10090:Rps6kc1 ^@ http://purl.uniprot.org/uniprot/E9QMX4|||http://purl.uniprot.org/uniprot/Q8BLK9 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||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_0000233128|||http://purl.uniprot.org/annotation/VSP_018043|||http://purl.uniprot.org/annotation/VSP_018044|||http://purl.uniprot.org/annotation/VSP_018045|||http://purl.uniprot.org/annotation/VSP_018046|||http://purl.uniprot.org/annotation/VSP_018047|||http://purl.uniprot.org/annotation/VSP_018048|||http://purl.uniprot.org/annotation/VSP_018049|||http://purl.uniprot.org/annotation/VSP_018050|||http://purl.uniprot.org/annotation/VSP_018051 http://togogenome.org/gene/10090:Mrpl20 ^@ http://purl.uniprot.org/uniprot/Q9CQL4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein bL20m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000248280 http://togogenome.org/gene/10090:Sema5b ^@ http://purl.uniprot.org/uniprot/Q60519 ^@ 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|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-5B|||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_0000032338|||http://purl.uniprot.org/annotation/VSP_029466|||http://purl.uniprot.org/annotation/VSP_029467|||http://purl.uniprot.org/annotation/VSP_029468 http://togogenome.org/gene/10090:Rps6kb2 ^@ http://purl.uniprot.org/uniprot/Q9Z1M4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ AGC-kinase C-terminal|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Ribosomal protein S6 kinase beta-2 ^@ http://purl.uniprot.org/annotation/PRO_0000086215 http://togogenome.org/gene/10090:Them4 ^@ http://purl.uniprot.org/uniprot/Q3UUI3 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Acyl-coenzyme A thioesterase THEM4|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000314180 http://togogenome.org/gene/10090:Pram1 ^@ http://purl.uniprot.org/uniprot/Q6BCL1 ^@ 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|||PML-RARA-regulated adapter molecule 1|||Phosphoserine|||Polar residues|||Pro residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000270172 http://togogenome.org/gene/10090:Gemin2 ^@ http://purl.uniprot.org/uniprot/Q9CQQ4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Gem-associated protein 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000087456 http://togogenome.org/gene/10090:Mettl4 ^@ http://purl.uniprot.org/uniprot/Q3U034 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Mutagenesis Site ^@ Abolished methyltransferase activity.|||N(6)-adenine-specific methyltransferase METTL4 ^@ http://purl.uniprot.org/annotation/PRO_0000251226 http://togogenome.org/gene/10090:Or6c88 ^@ http://purl.uniprot.org/uniprot/Q8VF26 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Adgrl1 ^@ http://purl.uniprot.org/uniprot/H7BX15|||http://purl.uniprot.org/uniprot/Q80TR1 ^@ 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|||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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ 100-fold decreased affinity for L-rhamnose.|||Abrogates L-rhamnose binding.|||Adhesion G protein-coupled receptor L1|||Cleavage; by autolysis|||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.|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||SUEL-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000070342|||http://purl.uniprot.org/annotation/PRO_5030172770|||http://purl.uniprot.org/annotation/VSP_022137 http://togogenome.org/gene/10090:Gmnn ^@ http://purl.uniprot.org/uniprot/O88513 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Turn ^@ Acidic residues|||Disordered|||Geminin|||Homeodomain binding|||N6-acetyllysine|||Necessary and sufficient for interaction with IDAS and CDT1|||Phosphoserine|||Phosphoserine; by CK2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000148730 http://togogenome.org/gene/10090:Rhbdf1 ^@ http://purl.uniprot.org/uniprot/Q6PIX5 ^@ 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|||Helical|||In isoform 2.|||Inactive rhomboid protein 1|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000340108|||http://purl.uniprot.org/annotation/VSP_034190|||http://purl.uniprot.org/annotation/VSP_034191 http://togogenome.org/gene/10090:Nfkbid ^@ http://purl.uniprot.org/uniprot/Q2TB02 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Disordered|||NF-kappa-B inhibitor delta|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000331115 http://togogenome.org/gene/10090:Vmn2r39 ^@ http://purl.uniprot.org/uniprot/L7N2E5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982293 http://togogenome.org/gene/10090:Cenpq ^@ http://purl.uniprot.org/uniprot/A0A1I7Q4A6|||http://purl.uniprot.org/uniprot/Q9CPQ5 ^@ 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|||Centromere protein Q|||Disordered|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000089535|||http://purl.uniprot.org/annotation/VSP_020451|||http://purl.uniprot.org/annotation/VSP_020452 http://togogenome.org/gene/10090:C130074G19Rik ^@ http://purl.uniprot.org/uniprot/Q8BGN9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Required for drug-induced death protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000265074 http://togogenome.org/gene/10090:Dph7 ^@ http://purl.uniprot.org/uniprot/Q3U5K4|||http://purl.uniprot.org/uniprot/Q9CYU6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ Diphthine methyltransferase|||In isoform 2.|||WD|||WD 1|||WD 2|||WD 3 ^@ http://purl.uniprot.org/annotation/PRO_0000050907|||http://purl.uniprot.org/annotation/VSP_014526|||http://purl.uniprot.org/annotation/VSP_014528 http://togogenome.org/gene/10090:Zgpat ^@ http://purl.uniprot.org/uniprot/Q8VDM1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C3H1-type|||Disordered|||G-patch|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger CCCH-type with G patch domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000213895 http://togogenome.org/gene/10090:Atp5h ^@ http://purl.uniprot.org/uniprot/Q9DCX2 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ ATP synthase subunit d, mitochondrial|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000071674 http://togogenome.org/gene/10090:Mrpl46 ^@ http://purl.uniprot.org/uniprot/Q9EQI8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ Large ribosomal subunit protein mL46|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000030577 http://togogenome.org/gene/10090:Nkain2 ^@ http://purl.uniprot.org/uniprot/Q4PNJ2 ^@ 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.|||Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000265089|||http://purl.uniprot.org/annotation/VSP_021903|||http://purl.uniprot.org/annotation/VSP_029299 http://togogenome.org/gene/10090:Hsd17b6 ^@ http://purl.uniprot.org/uniprot/Q9R092 ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Signal Peptide ^@ 17-beta-hydroxysteroid dehydrogenase type 6|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000303212 http://togogenome.org/gene/10090:Magel2 ^@ http://purl.uniprot.org/uniprot/Q9QZ04 ^@ 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_0000156739 http://togogenome.org/gene/10090:Susd6 ^@ http://purl.uniprot.org/uniprot/Q8BGE4|||http://purl.uniprot.org/uniprot/Q8C0M5 ^@ 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 ^@ Disordered|||Helical|||Polar residues|||Sushi|||Sushi domain-containing protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000432223 http://togogenome.org/gene/10090:Khdc1c ^@ http://purl.uniprot.org/uniprot/Q4KL78 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ KH homology domain-containing protein 1C|||KH; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000311432 http://togogenome.org/gene/10090:Tent5b ^@ http://purl.uniprot.org/uniprot/Q8C152 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Terminal nucleotidyltransferase 5B ^@ http://purl.uniprot.org/annotation/PRO_0000259932 http://togogenome.org/gene/10090:Slc26a8 ^@ http://purl.uniprot.org/uniprot/Q8R0C3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with RACGAP1|||N-linked (GlcNAc...) asparagine|||Polar residues|||STAS|||Testis anion transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000322588|||http://purl.uniprot.org/annotation/VSP_052702|||http://purl.uniprot.org/annotation/VSP_052703 http://togogenome.org/gene/10090:Pafah1b3 ^@ http://purl.uniprot.org/uniprot/Q3TJC2|||http://purl.uniprot.org/uniprot/Q61205 ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylserine|||Phosphoserine|||Platelet-activating factor acetylhydrolase IB subunit alpha1|||Removed|||SGNH hydrolase-type esterase ^@ http://purl.uniprot.org/annotation/PRO_0000058156 http://togogenome.org/gene/10090:Mysm1 ^@ http://purl.uniprot.org/uniprot/Q69Z66 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Deubiquitinase MYSM1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||JAMM motif|||LXXLL motif|||MPN|||Phosphoserine|||Phosphothreonine|||SANT|||SWIRM ^@ http://purl.uniprot.org/annotation/PRO_0000234074|||http://purl.uniprot.org/annotation/VSP_018212 http://togogenome.org/gene/10090:Tasor2 ^@ http://purl.uniprot.org/uniprot/Q5DTT3 ^@ 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 ^@ Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Protein TASOR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000299543 http://togogenome.org/gene/10090:Kpna7 ^@ http://purl.uniprot.org/uniprot/C0LLJ0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||IBB|||Importin subunit alpha-8|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000413537|||http://purl.uniprot.org/annotation/VSP_041924 http://togogenome.org/gene/10090:Mtrf1 ^@ http://purl.uniprot.org/uniprot/Q8K126 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Transit Peptide ^@ Chain|||Modified Residue|||Motif|||Region|||Transit Peptide ^@ GGQ|||GGQ domain|||Mitochondrion|||N5-methylglutamine|||Peptide chain release factor 1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000030334 http://togogenome.org/gene/10090:Sec24d ^@ http://purl.uniprot.org/uniprot/Q6NXL1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Gelsolin-like|||Polar residues|||Pro residues|||Sec23/Sec24 beta-sandwich|||Sec23/Sec24 helical|||Sec23/Sec24 trunk|||Zinc finger Sec23/Sec24-type ^@ http://togogenome.org/gene/10090:Cuta ^@ http://purl.uniprot.org/uniprot/D5MCW4|||http://purl.uniprot.org/uniprot/Q9CQ89 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Protein CutA ^@ http://purl.uniprot.org/annotation/PRO_0000006380|||http://purl.uniprot.org/annotation/PRO_5015088606|||http://purl.uniprot.org/annotation/VSP_013227|||http://purl.uniprot.org/annotation/VSP_013228 http://togogenome.org/gene/10090:Arhgap1 ^@ http://purl.uniprot.org/uniprot/A2AH25|||http://purl.uniprot.org/uniprot/Q5FWK3|||http://purl.uniprot.org/uniprot/Q8BQW4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ 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_0000323607 http://togogenome.org/gene/10090:Rsl1 ^@ http://purl.uniprot.org/uniprot/Q7M6Y1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Smarcal1 ^@ http://purl.uniprot.org/uniprot/Q8BJL0 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||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|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||DESH box|||Disordered|||HARP 1|||HARP 2|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||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_0000074349|||http://purl.uniprot.org/annotation/VSP_012919|||http://purl.uniprot.org/annotation/VSP_012920|||http://purl.uniprot.org/annotation/VSP_036216|||http://purl.uniprot.org/annotation/VSP_036217|||http://purl.uniprot.org/annotation/VSP_036218|||http://purl.uniprot.org/annotation/VSP_036219 http://togogenome.org/gene/10090:Nuf2 ^@ http://purl.uniprot.org/uniprot/Q99P69 ^@ 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 ^@ In isoform 2.|||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_0000249814|||http://purl.uniprot.org/annotation/VSP_020553|||http://purl.uniprot.org/annotation/VSP_020554 http://togogenome.org/gene/10090:Dynlt4 ^@ http://purl.uniprot.org/uniprot/Q8CDY7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Dynein light chain Tctex-type 4|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000316871 http://togogenome.org/gene/10090:Hsdl2 ^@ http://purl.uniprot.org/uniprot/B1AX78|||http://purl.uniprot.org/uniprot/Q2TPA8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Hydroxysteroid dehydrogenase-like protein 2|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||N6-succinyllysine|||Polar residues|||Proton acceptor|||SCP2 ^@ http://purl.uniprot.org/annotation/PRO_0000319889 http://togogenome.org/gene/10090:Tyms ^@ http://purl.uniprot.org/uniprot/P07607|||http://purl.uniprot.org/uniprot/Q544L2 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Strand|||Turn ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nucleophile|||Phosphoserine|||Thymidylate synthase|||Thymidylate synthase/dCMP hydroxymethylase|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000140902 http://togogenome.org/gene/10090:Psma8 ^@ http://purl.uniprot.org/uniprot/Q9CWH6 ^@ Chain|||Molecule Processing ^@ Chain ^@ Proteasome subunit alpha type-8 ^@ http://purl.uniprot.org/annotation/PRO_0000124150 http://togogenome.org/gene/10090:Afm ^@ http://purl.uniprot.org/uniprot/O89020 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Afamin|||Albumin 1|||Albumin 2|||Albumin 3|||Binding pocket for hydrophobic ligands|||Disordered|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000001107|||http://purl.uniprot.org/annotation/VSP_023387|||http://purl.uniprot.org/annotation/VSP_023388|||http://purl.uniprot.org/annotation/VSP_023389 http://togogenome.org/gene/10090:Scgb2b26 ^@ http://purl.uniprot.org/uniprot/Q8JZX1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099250 http://togogenome.org/gene/10090:Gm5592 ^@ http://purl.uniprot.org/uniprot/Q3V0A6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Uncharacterized protein C2orf78 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000319423 http://togogenome.org/gene/10090:Scai ^@ http://purl.uniprot.org/uniprot/Q8C4E7|||http://purl.uniprot.org/uniprot/Q8C8N2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Necessary to inhibit MRTFA-induced SRF transcriptional activity|||Phosphotyrosine|||Polar residues|||Protein SCAI|||Required for interaction with MRTFA ^@ http://purl.uniprot.org/annotation/PRO_0000089736|||http://purl.uniprot.org/annotation/VSP_015121|||http://purl.uniprot.org/annotation/VSP_015122 http://togogenome.org/gene/10090:Pkhd1l1 ^@ http://purl.uniprot.org/uniprot/Q80ZA4 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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|||In isoform 2.|||O-linked (GalNAc...) threonine|||PA14|||PbH1 1|||PbH1 10|||PbH1 2|||PbH1 3|||PbH1 4|||PbH1 5|||PbH1 6|||PbH1 7|||PbH1 8|||PbH1 9 ^@ http://purl.uniprot.org/annotation/PRO_0000318573|||http://purl.uniprot.org/annotation/VSP_031226|||http://purl.uniprot.org/annotation/VSP_031227 http://togogenome.org/gene/10090:Slc2a3 ^@ http://purl.uniprot.org/uniprot/P32037|||http://purl.uniprot.org/uniprot/Q3TPL8|||http://purl.uniprot.org/uniprot/Q8BLF7 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||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|||Important for selectivity against fructose|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Solute carrier family 2, facilitated glucose transporter member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000050354 http://togogenome.org/gene/10090:Pex5 ^@ http://purl.uniprot.org/uniprot/O09012 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Crosslink|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Amphipathic helix 1 (AH1)|||Amphipathic helix 2 (AH2)|||Amphipathic helix 3 (AH3)|||Amphipathic helix 4 (AH4)|||Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||LVxEF motif|||Peroxisomal targeting signal 1 receptor|||Phosphoserine|||Sensor of redox state|||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_0000106306|||http://purl.uniprot.org/annotation/VSP_024107 http://togogenome.org/gene/10090:Ino80 ^@ http://purl.uniprot.org/uniprot/Q6ZPV2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ 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|||Basic residues|||Chromatin-remodeling ATPase INO80|||DBINO|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000248830|||http://purl.uniprot.org/annotation/VSP_020334 http://togogenome.org/gene/10090:Naa25 ^@ http://purl.uniprot.org/uniprot/Q8BWZ3 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||N-alpha-acetyltransferase 25, NatB auxiliary subunit|||TPR 1|||TPR 2|||TPR 3|||TPR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000294338|||http://purl.uniprot.org/annotation/VSP_026631 http://togogenome.org/gene/10090:Or2ad1 ^@ http://purl.uniprot.org/uniprot/Q8VFG3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wscd1 ^@ http://purl.uniprot.org/uniprot/Q80XH4 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||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 1|||WSC 1|||WSC 2 ^@ http://purl.uniprot.org/annotation/PRO_0000305062|||http://purl.uniprot.org/annotation/VSP_028209|||http://purl.uniprot.org/annotation/VSP_028210 http://togogenome.org/gene/10090:Cxcl12 ^@ http://purl.uniprot.org/uniprot/H7BX38|||http://purl.uniprot.org/uniprot/P40224 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Basic residues|||Chemokine interleukin-8-like|||Disordered|||Important for dimer formation|||Important for integrin interaction and activation|||In isoform Alpha.|||Receptor activation motif|||Receptor and heparin binding|||Receptor binding|||Stromal cell-derived factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000005112|||http://purl.uniprot.org/annotation/PRO_5005683517|||http://purl.uniprot.org/annotation/VSP_037607 http://togogenome.org/gene/10090:Eif2ak4 ^@ http://purl.uniprot.org/uniprot/A2AUM0|||http://purl.uniprot.org/uniprot/Q9QZ05 ^@ 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|||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|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||Decreases autophosphorylation, binding to tRNA and Sindbis virus genomic RNA and eIF-2-alpha phosphorylation in amino acid-starved cells; when associated with I-1143.|||Decreases autophosphorylation, binding to tRNA and Sindbis virus genomic RNA and eIF-2-alpha phosphorylation in amino acid-starved cells; when associated with L-1142.|||Disordered|||Histidyl-tRNA synthetase-like|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Inhibits autophosphorylation, eIF-2-alpha phosphorylation and antiviral activity against Sindbis virus.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||RWD|||eIF-2-alpha kinase GCN2 ^@ http://purl.uniprot.org/annotation/PRO_0000085948|||http://purl.uniprot.org/annotation/VSP_013039|||http://purl.uniprot.org/annotation/VSP_013040|||http://purl.uniprot.org/annotation/VSP_013041|||http://purl.uniprot.org/annotation/VSP_013042|||http://purl.uniprot.org/annotation/VSP_013043|||http://purl.uniprot.org/annotation/VSP_013044|||http://purl.uniprot.org/annotation/VSP_013045|||http://purl.uniprot.org/annotation/VSP_013046|||http://purl.uniprot.org/annotation/VSP_013047|||http://purl.uniprot.org/annotation/VSP_013048|||http://purl.uniprot.org/annotation/VSP_013049|||http://purl.uniprot.org/annotation/VSP_013050 http://togogenome.org/gene/10090:Phactr3 ^@ http://purl.uniprot.org/uniprot/A2AHM4|||http://purl.uniprot.org/uniprot/Q6KCA9|||http://purl.uniprot.org/uniprot/Q8BYK5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphatase and actin regulator 3|||Phosphoserine|||Phosphothreonine|||Polar residues|||RPEL|||RPEL 1|||RPEL 2|||RPEL 3|||RPEL 4 ^@ http://purl.uniprot.org/annotation/PRO_0000126639|||http://purl.uniprot.org/annotation/VSP_009093|||http://purl.uniprot.org/annotation/VSP_009094|||http://purl.uniprot.org/annotation/VSP_009095 http://togogenome.org/gene/10090:Lrba ^@ http://purl.uniprot.org/uniprot/A0A0A6YXL6|||http://purl.uniprot.org/uniprot/A0A0A6YXX3|||http://purl.uniprot.org/uniprot/E9Q3Y4|||http://purl.uniprot.org/uniprot/Q8BSM6|||http://purl.uniprot.org/uniprot/Q8C7C2|||http://purl.uniprot.org/uniprot/Q8CBR4|||http://purl.uniprot.org/uniprot/Q9ESE1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Splice Variant|||Transmembrane ^@ BEACH|||BEACH-type PH|||Basic and acidic residues|||DUF4704|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Lipopolysaccharide-responsive and beige-like anchor protein|||N-acetylalanine|||Neurobeachin alpha-solenoid region|||Phosphoserine|||Polar residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000386545|||http://purl.uniprot.org/annotation/VSP_038227|||http://purl.uniprot.org/annotation/VSP_038228|||http://purl.uniprot.org/annotation/VSP_038229|||http://purl.uniprot.org/annotation/VSP_038230 http://togogenome.org/gene/10090:Or2n1e ^@ http://purl.uniprot.org/uniprot/Q7TRI7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nts ^@ http://purl.uniprot.org/uniprot/Q9D3P9 ^@ Chain|||Molecule Processing|||Peptide|||Signal Peptide|||Site ^@ Chain|||Peptide|||Signal Peptide|||Site ^@ Cleavage; by ACE and MME|||Cleavage; by MME|||Large neuromedin N|||Neuromedin N|||Neurotensin|||Tail peptide ^@ http://purl.uniprot.org/annotation/PRO_0000019526|||http://purl.uniprot.org/annotation/PRO_0000019527|||http://purl.uniprot.org/annotation/PRO_0000019528|||http://purl.uniprot.org/annotation/PRO_0000019529 http://togogenome.org/gene/10090:Ccdc187 ^@ http://purl.uniprot.org/uniprot/Q8C5V8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-coil domain-containing protein 187|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000435397 http://togogenome.org/gene/10090:Atxn7l1 ^@ http://purl.uniprot.org/uniprot/B2RW07|||http://purl.uniprot.org/uniprot/Q9CZ05 ^@ 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.|||Polar residues|||SCA7 ^@ http://purl.uniprot.org/annotation/PRO_0000254144|||http://purl.uniprot.org/annotation/VSP_021186 http://togogenome.org/gene/10090:Tcl1 ^@ http://purl.uniprot.org/uniprot/P56280 ^@ Chain|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Strand|||Turn ^@ T-cell leukemia/lymphoma protein 1A ^@ http://purl.uniprot.org/annotation/PRO_0000184489 http://togogenome.org/gene/10090:Acsf3 ^@ http://purl.uniprot.org/uniprot/Q3URE1 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Malonate--CoA ligase ACSF3, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000315801|||http://purl.uniprot.org/annotation/VSP_030705|||http://purl.uniprot.org/annotation/VSP_030706 http://togogenome.org/gene/10090:Psme3ip1 ^@ http://purl.uniprot.org/uniprot/Q91WE2 ^@ 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|||Interaction with PSME3|||N-acetylmethionine|||N6-acetyllysine|||PSME3-interacting protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000096848 http://togogenome.org/gene/10090:Wdr18 ^@ http://purl.uniprot.org/uniprot/Q4VBE8 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000233181 http://togogenome.org/gene/10090:Mrpl55 ^@ http://purl.uniprot.org/uniprot/Q9CZ83 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Large ribosomal subunit protein mL55|||Mitochondrion|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000273100|||http://purl.uniprot.org/annotation/VSP_022478 http://togogenome.org/gene/10090:Adamtsl4 ^@ http://purl.uniprot.org/uniprot/Q80T21 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ ADAMTS-like protein 4|||Disordered|||N-linked (GlcNAc...) asparagine|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000257967 http://togogenome.org/gene/10090:Pou4f2 ^@ http://purl.uniprot.org/uniprot/Q63934 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ 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|||Stimulates induction of neurite outgrowth and expression of synaptic genes. Abolishes the inhibitory effect on basal transcription and on gene activation by POU4F1. ^@ http://purl.uniprot.org/annotation/PRO_0000100741|||http://purl.uniprot.org/annotation/VSP_058838 http://togogenome.org/gene/10090:Hsd17b2 ^@ http://purl.uniprot.org/uniprot/P51658 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Estradiol 17-beta-dehydrogenase 2|||Helical; Signal-anchor for type II membrane protein|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054571 http://togogenome.org/gene/10090:Thnsl1 ^@ http://purl.uniprot.org/uniprot/Q149D1|||http://purl.uniprot.org/uniprot/Q8BH55 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ N6-(pyridoxal phosphate)lysine|||Threonine synthase N-terminal|||Threonine synthase-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000185648 http://togogenome.org/gene/10090:Bcs1l ^@ http://purl.uniprot.org/uniprot/Q9CZP5 ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Helical|||Mitochondrial chaperone BCS1|||Mitochondrial intermembrane|||Mitochondrial matrix|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000084773 http://togogenome.org/gene/10090:Prdx1 ^@ http://purl.uniprot.org/uniprot/P35700 ^@ Active Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Cysteine sulfenic acid (-SOH) intermediate|||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|||Removed|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000135077 http://togogenome.org/gene/10090:Trp53 ^@ http://purl.uniprot.org/uniprot/P02340|||http://purl.uniprot.org/uniprot/Q3UGQ1|||http://purl.uniprot.org/uniprot/Q549C9|||http://purl.uniprot.org/uniprot/Q80ZA1 ^@ 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|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn ^@ Basic (repression of DNA-binding)|||Basic and acidic residues|||Bipartite nuclear localization signal|||Can cooperate with an activated Ras to transform fibroblasts.|||Cellular tumor antigen p53|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In clone P53-M11.|||Interaction with AXIN1|||Interaction with CCAR2|||Interaction with DNA|||Interaction with E4F1|||Interaction with HIPK1|||Interaction with HIPK2|||Interaction with USP7|||Interaction with WWOX|||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|||Nuclear export signal|||Oligomerization|||Omega-N-methylarginine|||Phosphoserine; by AURKA, CDK1 and CDK2|||Phosphoserine; by AURKB|||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|||Required for interaction with FBXO42|||Required for interaction with ZNF385A|||Symmetric dimethylarginine|||Transcription activation (acidic)|||[KR]-[STA]-K motif|||p53 DNA-binding|||p53 tetramerisation|||p53 transactivation ^@ http://purl.uniprot.org/annotation/PRO_0000185709 http://togogenome.org/gene/10090:Ccr7 ^@ http://purl.uniprot.org/uniprot/P47774 ^@ 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 ^@ C-C chemokine receptor type 7|||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_0000012736 http://togogenome.org/gene/10090:Gpr83 ^@ http://purl.uniprot.org/uniprot/P30731 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||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.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000012804|||http://purl.uniprot.org/annotation/VSP_001988|||http://purl.uniprot.org/annotation/VSP_001989|||http://purl.uniprot.org/annotation/VSP_001990 http://togogenome.org/gene/10090:Rpl13 ^@ http://purl.uniprot.org/uniprot/P47963|||http://purl.uniprot.org/uniprot/Q5RKP3 ^@ 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 ^@ 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|||Large ribosomal subunit protein eL13|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000192920 http://togogenome.org/gene/10090:Scrt2 ^@ http://purl.uniprot.org/uniprot/Q8BTH6 ^@ 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_0000047039 http://togogenome.org/gene/10090:Or4p21 ^@ http://purl.uniprot.org/uniprot/Q7TR17 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp451 ^@ http://purl.uniprot.org/uniprot/Q8C0P7|||http://purl.uniprot.org/uniprot/Q8VCL4|||http://purl.uniprot.org/uniprot/Q9CUK0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8; atypical|||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|||Important for interaction with SMAD4|||Important for interaction with SUMO1 and SUMO2|||Important for ubiquitin binding|||Interaction with SUMO2 1|||Interaction with SUMO2 2|||Lamina-associated polypeptide 2 alpha C-terminal|||Omega-N-methylarginine|||PLRP|||Phosphoserine|||Polar residues|||Sufficient for E3 SUMO-protein ligase activity ^@ http://purl.uniprot.org/annotation/PRO_0000047599 http://togogenome.org/gene/10090:Gpc5 ^@ http://purl.uniprot.org/uniprot/H3BLN8|||http://purl.uniprot.org/uniprot/Q8CAL5 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide ^@ 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_0000012321|||http://purl.uniprot.org/annotation/PRO_0000012322|||http://purl.uniprot.org/annotation/PRO_0000333850 http://togogenome.org/gene/10090:Ints10 ^@ http://purl.uniprot.org/uniprot/Q8K2A7 ^@ 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_0000235689 http://togogenome.org/gene/10090:Evc2 ^@ http://purl.uniprot.org/uniprot/Q8K1G2 ^@ Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Inhibits interaction with EFCAB7.|||Limbin|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000084364 http://togogenome.org/gene/10090:Tcaf3 ^@ http://purl.uniprot.org/uniprot/Q6QR59 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Peptidase M60|||TRPM8 channel-associated factor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000320191 http://togogenome.org/gene/10090:Adcy3 ^@ http://purl.uniprot.org/uniprot/B8JK56|||http://purl.uniprot.org/uniprot/Q80TY9|||http://purl.uniprot.org/uniprot/Q8VHH7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Adenylate cyclase type 3|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)|||Guanylate cyclase|||Helical|||In Jll; dominant allele that increases enzyme activity, and decreases fasting insulin levels, fasting leptin levels, weight gain and fat accumulation when mice are kept on a high fat diet.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by CaMK2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000195688 http://togogenome.org/gene/10090:Pcdhgb1 ^@ http://purl.uniprot.org/uniprot/Q91XX8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099496 http://togogenome.org/gene/10090:Triap1 ^@ http://purl.uniprot.org/uniprot/Q9D8Z2 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Site ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||Important for interaction with PRELID3A|||N-acetylmethionine|||TP53-regulated inhibitor of apoptosis 1 ^@ http://purl.uniprot.org/annotation/PRO_0000220524 http://togogenome.org/gene/10090:Pdxk ^@ http://purl.uniprot.org/uniprot/Q8K183 ^@ 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|||Phosphoserine|||Proton acceptor|||Pyridoxal kinase ^@ http://purl.uniprot.org/annotation/PRO_0000213336 http://togogenome.org/gene/10090:Hebp2 ^@ http://purl.uniprot.org/uniprot/Q9WU63 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||Heme-binding protein 2|||Loss of heme binding.|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000116901 http://togogenome.org/gene/10090:Ddx19b ^@ http://purl.uniprot.org/uniprot/Q8BZY3|||http://purl.uniprot.org/uniprot/Q8R3C7 ^@ Domain Extent|||Motif|||Region ^@ Domain Extent|||Motif|||Region ^@ DEAD-box RNA helicase Q|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Q motif ^@ http://togogenome.org/gene/10090:Plpbp ^@ http://purl.uniprot.org/uniprot/Q544R1|||http://purl.uniprot.org/uniprot/Q6P8V7|||http://purl.uniprot.org/uniprot/Q9Z2Y8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Alanine racemase N-terminal|||N6-(pyridoxal phosphate)lysine|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine|||Pyridoxal phosphate homeostasis protein ^@ http://purl.uniprot.org/annotation/PRO_0000163211 http://togogenome.org/gene/10090:Or2t43 ^@ http://purl.uniprot.org/uniprot/M9MMJ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or52e5 ^@ http://purl.uniprot.org/uniprot/Q8VG26 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Eif1 ^@ http://purl.uniprot.org/uniprot/P48024|||http://purl.uniprot.org/uniprot/Q4V9T8 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Site ^@ Binds 40S ribosomal subunit|||Eukaryotic translation initiation factor 1|||N-acetylserine|||Phosphoserine|||Removed|||SUI1 ^@ http://purl.uniprot.org/annotation/PRO_0000130555 http://togogenome.org/gene/10090:Zfp935 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VP04|||http://purl.uniprot.org/uniprot/Q14DI0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Bpifb3 ^@ http://purl.uniprot.org/uniprot/Q80ZU7 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ BPI fold-containing family B member 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017171 http://togogenome.org/gene/10090:Rap1gap2 ^@ http://purl.uniprot.org/uniprot/A0A571BED8|||http://purl.uniprot.org/uniprot/Q5SVL6 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rap-GAP|||Rap1 GTPase-activating protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000312717|||http://purl.uniprot.org/annotation/VSP_029890|||http://purl.uniprot.org/annotation/VSP_029952 http://togogenome.org/gene/10090:Vgf ^@ http://purl.uniprot.org/uniprot/Q0VGU4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Complete loss of lipolytic function.|||Disordered|||Neuroendocrine regulatory peptide-1|||Neuroendocrine regulatory peptide-2|||Neurosecretory protein VGF|||Phosphoserine|||Polar residues|||Pro residues|||Pyrrolidone carboxylic acid|||VGF-derived peptide TLQP-21|||VGF-derived peptide TLQP-62 ^@ http://purl.uniprot.org/annotation/PRO_0000446628|||http://purl.uniprot.org/annotation/PRO_0000446629|||http://purl.uniprot.org/annotation/PRO_0000446630|||http://purl.uniprot.org/annotation/PRO_0000446631|||http://purl.uniprot.org/annotation/PRO_5015097006 http://togogenome.org/gene/10090:1700016C15Rik ^@ http://purl.uniprot.org/uniprot/Q9DAA7 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein SPMIP3 ^@ http://purl.uniprot.org/annotation/PRO_0000274316 http://togogenome.org/gene/10090:Tspan1 ^@ http://purl.uniprot.org/uniprot/Q99J59 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000382891 http://togogenome.org/gene/10090:Zdhhc11 ^@ http://purl.uniprot.org/uniprot/Q14AK4 ^@ 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 ^@ Cytoplasmic|||DHHC|||Disordered|||Helical|||Loss of protein-cysteine S-palmitoyltransferase activity.|||Lumenal|||Palmitoyltransferase ZDHHC11|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000413764 http://togogenome.org/gene/10090:Cep63 ^@ http://purl.uniprot.org/uniprot/F8VPJ7|||http://purl.uniprot.org/uniprot/U5KVR9 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Centrosomal protein Cep63/Deup1 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Morc4 ^@ http://purl.uniprot.org/uniprot/Q8BMD7 ^@ 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 ^@ Basic and acidic residues|||CW-type|||Disordered|||In isoform 2.|||MORC family CW-type zinc finger protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000096540|||http://purl.uniprot.org/annotation/VSP_015277|||http://purl.uniprot.org/annotation/VSP_015278 http://togogenome.org/gene/10090:Ms4a7 ^@ http://purl.uniprot.org/uniprot/E9Q9V5|||http://purl.uniprot.org/uniprot/Q3UAR5|||http://purl.uniprot.org/uniprot/Q8BV59|||http://purl.uniprot.org/uniprot/Q99N04|||http://purl.uniprot.org/uniprot/Q9D2W6 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Lhx1 ^@ http://purl.uniprot.org/uniprot/P63006|||http://purl.uniprot.org/uniprot/Q569N5 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Disrupts LDB1-binding; when associated with G-28.|||Disrupts LDB1-binding; when associated with G-88.|||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_0000075771 http://togogenome.org/gene/10090:Trim11 ^@ http://purl.uniprot.org/uniprot/Q99PQ2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ B box-type|||B30.2/SPRY|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase TRIM11|||In isoform 2.|||Phosphoserine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056216|||http://purl.uniprot.org/annotation/VSP_012059 http://togogenome.org/gene/10090:Sap30bp ^@ http://purl.uniprot.org/uniprot/Q02614 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||SAP30-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000083924 http://togogenome.org/gene/10090:Ccdc43 ^@ http://purl.uniprot.org/uniprot/Q9CR29 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000234501|||http://purl.uniprot.org/annotation/VSP_018336|||http://purl.uniprot.org/annotation/VSP_018337 http://togogenome.org/gene/10090:Stx3 ^@ http://purl.uniprot.org/uniprot/Q3UZI9|||http://purl.uniprot.org/uniprot/Q64704 ^@ 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|||Helical; Anchor for type IV membrane protein|||In isoform 3B and isoform 3C.|||In isoform 3C.|||In isoform 3D.|||Syntaxin-3|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000210200|||http://purl.uniprot.org/annotation/VSP_006341|||http://purl.uniprot.org/annotation/VSP_006342|||http://purl.uniprot.org/annotation/VSP_006344|||http://purl.uniprot.org/annotation/VSP_006346 http://togogenome.org/gene/10090:Rpa2 ^@ http://purl.uniprot.org/uniprot/Q62193 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with RAD52, TIPIN, UNG and XPA|||N-acetylmethionine|||OB|||Phosphoserine; by CDK1|||Phosphoserine; by CDK2|||Phosphoserine; by PRKDC|||Phosphothreonine; by PRKDC|||Polar residues|||Replication protein A 32 kDa subunit ^@ http://purl.uniprot.org/annotation/PRO_0000097271 http://togogenome.org/gene/10090:Pdxp ^@ http://purl.uniprot.org/uniprot/P60487|||http://purl.uniprot.org/uniprot/Q6IS27 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Strand|||Turn ^@ Abolishes homodimerization. Strongly decreases affinity for pyridoxal phosphate.|||Chronophin|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000068838 http://togogenome.org/gene/10090:Cox7c ^@ http://purl.uniprot.org/uniprot/P17665 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn ^@ Chain|||Helix|||Modified Residue|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn ^@ Cytochrome c oxidase subunit 7C, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000006166 http://togogenome.org/gene/10090:Amy2a4 ^@ http://purl.uniprot.org/uniprot/P00688 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ In A1 and B(C).|||In A1, B(A) and B(C).|||In A1, B(A) and B(C); requires 2 nucleotide substitutions.|||In A1, B(C) and AMY-2.2Y.|||In AMY-2.2Y.|||In B(A).|||In B(C).|||In B1.|||Nucleophile|||Pancreatic alpha-amylase 2a5|||Proton donor|||Pyrrolidone carboxylic acid|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000001398 http://togogenome.org/gene/10090:Fancd2 ^@ http://purl.uniprot.org/uniprot/A0A0N4SV29|||http://purl.uniprot.org/uniprot/B2RSU4|||http://purl.uniprot.org/uniprot/Q3U202|||http://purl.uniprot.org/uniprot/Q3UQJ0|||http://purl.uniprot.org/uniprot/Q80V62 ^@ Chain|||Compositionally Biased Region|||Crosslink|||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|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Fanconi anemia group D2 protein homolog|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Interaction with BRCA2|||Interaction with FANCE|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087169|||http://purl.uniprot.org/annotation/VSP_013889|||http://purl.uniprot.org/annotation/VSP_013890 http://togogenome.org/gene/10090:Smarca5 ^@ http://purl.uniprot.org/uniprot/Q91ZW3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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|||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_0000074355 http://togogenome.org/gene/10090:Slco3a1 ^@ http://purl.uniprot.org/uniprot/Q8R3L5 ^@ 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|||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.|||Kazal-like|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Solute carrier organic anion transporter family member 3A1 ^@ http://purl.uniprot.org/annotation/PRO_0000191065|||http://purl.uniprot.org/annotation/VSP_036839|||http://purl.uniprot.org/annotation/VSP_036840 http://togogenome.org/gene/10090:Pip5k1c ^@ http://purl.uniprot.org/uniprot/F8WHW6|||http://purl.uniprot.org/uniprot/O70161 ^@ 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 interaction with AP-2 complex.|||Abolishes interaction with AP2B1.|||Abolishes lipid kinase activity. Does not affect targeting of TLN1 to plasma membrane. Affects assembly of TLN1 into focal adhesions. Affects uropodium formation and retraction of the cell rear.|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Cannot rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Decreased tailin assembly into focal adhesions.|||Cannot rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Does not affect lipid kinase activity. Does not alter binding to tailin. Decreased tailin assembly into focal adhesions. Increased interaction with PLCG1.|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of phosphorylation by CSK. Abolishes interaction with AP-2 complex. Cannot rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration.|||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_0000185463|||http://purl.uniprot.org/annotation/VSP_016013|||http://purl.uniprot.org/annotation/VSP_016014|||http://purl.uniprot.org/annotation/VSP_016015 http://togogenome.org/gene/10090:Nktr ^@ http://purl.uniprot.org/uniprot/P30415 ^@ 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 ^@ Arg/Ser tandem repeat-rich|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||NK-tumor recognition protein|||PPIase cyclophilin-type|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064218 http://togogenome.org/gene/10090:Hsd17b12 ^@ http://purl.uniprot.org/uniprot/O70503|||http://purl.uniprot.org/uniprot/Q0VGQ1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Motif|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Di-lysine motif|||Helical|||In isoform 2.|||Proton acceptor|||Very-long-chain 3-oxoacyl-CoA reductase ^@ http://purl.uniprot.org/annotation/PRO_0000054576|||http://purl.uniprot.org/annotation/VSP_020255 http://togogenome.org/gene/10090:Or4d2b ^@ http://purl.uniprot.org/uniprot/Q5SW50 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lpo ^@ http://purl.uniprot.org/uniprot/Q5SW46 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Propeptide|||Signal Peptide|||Site ^@ 3'-nitrotyrosine|||Lactoperoxidase|||Phosphoserine|||Proton acceptor|||Transition state stabilizer|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000456225|||http://purl.uniprot.org/annotation/PRO_0000456226 http://togogenome.org/gene/10090:Echdc1 ^@ http://purl.uniprot.org/uniprot/Q9D9V3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Ethylmalonyl-CoA decarboxylase|||In isoform 2.|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000273247|||http://purl.uniprot.org/annotation/VSP_022499 http://togogenome.org/gene/10090:Dsg3 ^@ http://purl.uniprot.org/uniprot/O35902|||http://purl.uniprot.org/uniprot/Q3UFC6 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cytoplasmic|||Desmoglein repeat 1|||Desmoglein repeat 2|||Desmoglein-3|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000003853|||http://purl.uniprot.org/annotation/PRO_0000003854|||http://purl.uniprot.org/annotation/PRO_5015097478|||http://purl.uniprot.org/annotation/VSP_012905|||http://purl.uniprot.org/annotation/VSP_012906 http://togogenome.org/gene/10090:Taf5l ^@ http://purl.uniprot.org/uniprot/Q91WQ5 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ 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_0000051262 http://togogenome.org/gene/10090:Bbs9 ^@ http://purl.uniprot.org/uniprot/Q811G0 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Critical for protein stability|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Interaction with LZTL1|||Protein PTHB1|||Seven-bladed beta-propeller ^@ http://purl.uniprot.org/annotation/PRO_0000235270|||http://purl.uniprot.org/annotation/VSP_018429|||http://purl.uniprot.org/annotation/VSP_018430|||http://purl.uniprot.org/annotation/VSP_018431|||http://purl.uniprot.org/annotation/VSP_018432 http://togogenome.org/gene/10090:Sprr1a ^@ http://purl.uniprot.org/uniprot/Q62266 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ 1|||10|||11|||12|||13|||13 X 8 AA approximate tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Cornifin-A|||Disordered|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000149998 http://togogenome.org/gene/10090:Nectin1 ^@ http://purl.uniprot.org/uniprot/Q9JKF6 ^@ Chain|||Compositionally Biased Region|||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|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||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|||Interaction with FGFR|||N-linked (GlcNAc...) asparagine|||Nectin-1|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000015134 http://togogenome.org/gene/10090:Or14a257 ^@ http://purl.uniprot.org/uniprot/Q7TS06 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Prpsap2 ^@ http://purl.uniprot.org/uniprot/Q05BD4|||http://purl.uniprot.org/uniprot/Q5SWZ0|||http://purl.uniprot.org/uniprot/Q8R574 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ N-acetylmethionine|||Phosphoribosyl pyrophosphate synthase-associated protein 2|||Phosphoserine|||Ribose-phosphate pyrophosphokinase N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000141083 http://togogenome.org/gene/10090:Kprp ^@ http://purl.uniprot.org/uniprot/B2RUR4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Keratinocyte proline-rich protein|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000364006 http://togogenome.org/gene/10090:Usf1 ^@ http://purl.uniprot.org/uniprot/Q3UQH7|||http://purl.uniprot.org/uniprot/Q61069|||http://purl.uniprot.org/uniprot/Q8R4E5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region ^@ BHLH|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Leucine-zipper|||Upstream stimulatory factor 1|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127497 http://togogenome.org/gene/10090:Mup20 ^@ http://purl.uniprot.org/uniprot/Q5FW60 ^@ Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Helix|||Mass|||Signal Peptide|||Strand|||Turn ^@ Major urinary protein 20 ^@ http://purl.uniprot.org/annotation/PRO_0000398791 http://togogenome.org/gene/10090:Bpifa2 ^@ http://purl.uniprot.org/uniprot/P07743 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ BPI fold-containing family A member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000017185 http://togogenome.org/gene/10090:2310033P09Rik ^@ http://purl.uniprot.org/uniprot/Q99LX5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Multiple myeloma tumor-associated protein 2 homolog|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000096519 http://togogenome.org/gene/10090:Xirp2 ^@ http://purl.uniprot.org/uniprot/Q4U4S6 ^@ 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|||In isoform 2.|||LIM zinc-binding|||Phosphoserine|||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_0000316988|||http://purl.uniprot.org/annotation/VSP_030849|||http://purl.uniprot.org/annotation/VSP_030850 http://togogenome.org/gene/10090:Spats2 ^@ http://purl.uniprot.org/uniprot/Q8K1N4 ^@ 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|||Spermatogenesis-associated serine-rich protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000307698|||http://purl.uniprot.org/annotation/VSP_028790|||http://purl.uniprot.org/annotation/VSP_028791 http://togogenome.org/gene/10090:Cdkl3 ^@ http://purl.uniprot.org/uniprot/B1AU43|||http://purl.uniprot.org/uniprot/Q8BLF2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Cyclin-dependent kinase-like 3|||Disordered|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||[NKR]KIAxRE ^@ http://purl.uniprot.org/annotation/PRO_0000085822|||http://purl.uniprot.org/annotation/VSP_016149|||http://purl.uniprot.org/annotation/VSP_016150|||http://purl.uniprot.org/annotation/VSP_016151|||http://purl.uniprot.org/annotation/VSP_016152|||http://purl.uniprot.org/annotation/VSP_016154|||http://purl.uniprot.org/annotation/VSP_016155|||http://purl.uniprot.org/annotation/VSP_016156|||http://purl.uniprot.org/annotation/VSP_016157|||http://purl.uniprot.org/annotation/VSP_030154 http://togogenome.org/gene/10090:Gns ^@ http://purl.uniprot.org/uniprot/Q8BFR4 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ 3-oxoalanine (Cys)|||N-acetylglucosamine-6-sulfatase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphoserine|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000273189 http://togogenome.org/gene/10090:Zdhhc4 ^@ http://purl.uniprot.org/uniprot/Q9D6H5 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Motif|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Di-lysine motif|||Helical|||Lumenal|||Palmitoyltransferase ZDHHC4|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212866 http://togogenome.org/gene/10090:Glrp1 ^@ http://purl.uniprot.org/uniprot/E9Q9S8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Commd4 ^@ http://purl.uniprot.org/uniprot/Q9CQ02 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ COMM|||COMM domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000077394 http://togogenome.org/gene/10090:Ctsa ^@ http://purl.uniprot.org/uniprot/G3X8T3|||http://purl.uniprot.org/uniprot/P16675|||http://purl.uniprot.org/uniprot/Q544R6|||http://purl.uniprot.org/uniprot/Q9D2D1 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Carboxypeptidase|||Lysosomal protective protein|||Lysosomal protective protein 20 kDa chain|||Lysosomal protective protein 32 kDa chain|||N-linked (GlcNAc...) (high mannose) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000004277|||http://purl.uniprot.org/annotation/PRO_0000004278|||http://purl.uniprot.org/annotation/PRO_0000004279|||http://purl.uniprot.org/annotation/PRO_5005144768|||http://purl.uniprot.org/annotation/PRO_5015020033|||http://purl.uniprot.org/annotation/PRO_5015091840 http://togogenome.org/gene/10090:Nrp ^@ http://purl.uniprot.org/uniprot/Q5XLJ1|||http://purl.uniprot.org/uniprot/Q8BQJ0 ^@ Experimental Information|||Non-terminal Residue|||Region ^@ Non-terminal Residue|||Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Foxn3 ^@ http://purl.uniprot.org/uniprot/Q499D0 ^@ 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|||Fork-head|||Forkhead box protein N3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000245102 http://togogenome.org/gene/10090:Il15ra ^@ http://purl.uniprot.org/uniprot/Q501M1|||http://purl.uniprot.org/uniprot/Q60819|||http://purl.uniprot.org/uniprot/Q810T6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2, isoform 3, isoform 4 and isoform 6.|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interleukin-15 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Polar residues|||Soluble interleukin-15 receptor subunit alpha|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_0000011045|||http://purl.uniprot.org/annotation/PRO_0000333856|||http://purl.uniprot.org/annotation/VSP_012627|||http://purl.uniprot.org/annotation/VSP_012628|||http://purl.uniprot.org/annotation/VSP_012629|||http://purl.uniprot.org/annotation/VSP_012630|||http://purl.uniprot.org/annotation/VSP_012631|||http://purl.uniprot.org/annotation/VSP_012632|||http://purl.uniprot.org/annotation/VSP_012633 http://togogenome.org/gene/10090:Thra ^@ http://purl.uniprot.org/uniprot/P63058 ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||In isoform Alpha-1 and isoform Alpha-deltaE6.|||In isoform Alpha-3.|||In isoform Alpha-deltaE6.|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Polar residues|||Thyroid hormone receptor alpha ^@ http://purl.uniprot.org/annotation/PRO_0000053425|||http://purl.uniprot.org/annotation/VSP_003624|||http://purl.uniprot.org/annotation/VSP_003625|||http://purl.uniprot.org/annotation/VSP_038640 http://togogenome.org/gene/10090:Rev1 ^@ http://purl.uniprot.org/uniprot/Q920Q2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ BRCT|||Basic and acidic residues|||DNA repair protein REV1|||Disordered|||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_0000173993 http://togogenome.org/gene/10090:Pgrmc2 ^@ http://purl.uniprot.org/uniprot/Q80UU9 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Transmembrane ^@ Cytochrome b5 heme-binding|||Disordered|||Helical|||Membrane-associated progesterone receptor component 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000121744 http://togogenome.org/gene/10090:Acr ^@ http://purl.uniprot.org/uniprot/P23578|||http://purl.uniprot.org/uniprot/Q3ZB05 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Acrosin|||Acrosin heavy chain|||Acrosin light chain|||Charge relay system|||Interchain (between light and heavy chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Pro-rich ^@ http://purl.uniprot.org/annotation/PRO_0000027522|||http://purl.uniprot.org/annotation/PRO_0000027523|||http://purl.uniprot.org/annotation/PRO_0000027524|||http://purl.uniprot.org/annotation/PRO_0000027525 http://togogenome.org/gene/10090:Zdhhc7 ^@ http://purl.uniprot.org/uniprot/Q91WU6 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Fails to enhance DLG4 palmitoylation.|||Helical|||Loss of protein-cysteine S-palmitoyltransferase activity.|||Lumenal|||Palmitoyltransferase ZDHHC7|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212875 http://togogenome.org/gene/10090:Fam161b ^@ http://purl.uniprot.org/uniprot/Q8CB59 ^@ 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|||In isoform 2.|||Polar residues|||Protein FAM161B ^@ http://purl.uniprot.org/annotation/PRO_0000089891|||http://purl.uniprot.org/annotation/VSP_007818|||http://purl.uniprot.org/annotation/VSP_007819 http://togogenome.org/gene/10090:Or5an9 ^@ http://purl.uniprot.org/uniprot/Q8VF59 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gdf7 ^@ http://purl.uniprot.org/uniprot/P43029 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||Growth/differentiation factor 7|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033924|||http://purl.uniprot.org/annotation/PRO_0000033925|||http://purl.uniprot.org/annotation/VSP_010764 http://togogenome.org/gene/10090:Ppp3r1 ^@ http://purl.uniprot.org/uniprot/Q63810 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand ^@ Calcineurin A binding|||Calcineurin subunit B type 1|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||Interaction with PxVP motif in substrates of the catalytic subunit|||N-myristoyl glycine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073485|||http://purl.uniprot.org/annotation/VSP_024842 http://togogenome.org/gene/10090:Cish ^@ http://purl.uniprot.org/uniprot/Q62225|||http://purl.uniprot.org/uniprot/Q8C3F4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Cytokine-inducible SH2-containing protein|||Disordered|||SH2|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000181232 http://togogenome.org/gene/10090:Serpina3i ^@ http://purl.uniprot.org/uniprot/D3Z450 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Smim12 ^@ http://purl.uniprot.org/uniprot/Q78RX3 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Small integral membrane protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000414320 http://togogenome.org/gene/10090:Pkp1 ^@ http://purl.uniprot.org/uniprot/P97350 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Region|||Repeat ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Disordered|||Phosphoserine|||Plakophilin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000064285 http://togogenome.org/gene/10090:Or9i16 ^@ http://purl.uniprot.org/uniprot/Q8VFQ4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Limk2 ^@ http://purl.uniprot.org/uniprot/O54785|||http://purl.uniprot.org/uniprot/Q8BS94 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn ^@ Disordered|||In isoform 3.|||In isoform LIMK2b.|||LIM domain kinase 2|||LIM zinc-binding 1|||LIM zinc-binding 2|||PDZ|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by ROCK1 and CDC42BP|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000075810|||http://purl.uniprot.org/annotation/VSP_010350|||http://purl.uniprot.org/annotation/VSP_010351 http://togogenome.org/gene/10090:Gm10487 ^@ http://purl.uniprot.org/uniprot/Q62478 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Txn1 ^@ http://purl.uniprot.org/uniprot/P10639 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site ^@ Contributes to redox potential value|||Deprotonates C-terminal active site Cys|||Interchain; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Redox-active|||S-nitrosocysteine|||S-nitrosocysteine; alternate|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000120007 http://togogenome.org/gene/10090:Or4k52 ^@ http://purl.uniprot.org/uniprot/Q8VGE9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Otud5 ^@ http://purl.uniprot.org/uniprot/A2AES5|||http://purl.uniprot.org/uniprot/Q3U2S4 ^@ 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 ^@ Cys-loop|||Disordered|||His-loop|||In isoform 2.|||Nucleophile|||OTU|||OTU domain-containing protein 5|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Variable-loop ^@ http://purl.uniprot.org/annotation/PRO_0000278224|||http://purl.uniprot.org/annotation/VSP_023196 http://togogenome.org/gene/10090:Ecrg4 ^@ http://purl.uniprot.org/uniprot/Q99LS0 ^@ Experimental Information|||Molecule Processing|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Augurin ^@ http://purl.uniprot.org/annotation/PRO_0000250515|||http://purl.uniprot.org/annotation/PRO_0000363239|||http://purl.uniprot.org/annotation/PRO_0000363240 http://togogenome.org/gene/10090:Rab27b ^@ http://purl.uniprot.org/uniprot/Q05D38|||http://purl.uniprot.org/uniprot/Q549X4|||http://purl.uniprot.org/uniprot/Q99P58 ^@ Binding Site|||Chain|||Disulfide Bond|||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|||Disulfide Bond|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolishes the interaction with MLPH.|||Cysteine methyl ester|||Disordered|||Effector region|||Loss of GTPase activity.|||N-acetylthreonine|||Ras-related protein Rab-27B|||Removed|||S-geranylgeranyl cysteine|||Strongly reduces the interaction with MLPH. ^@ http://purl.uniprot.org/annotation/PRO_0000121225 http://togogenome.org/gene/10090:Slc20a2 ^@ http://purl.uniprot.org/uniprot/Q80UP8 ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium-dependent phosphate transporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000341269 http://togogenome.org/gene/10090:Txnl4b ^@ http://purl.uniprot.org/uniprot/Q8BUH1 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Thioredoxin-like protein 4B ^@ http://purl.uniprot.org/annotation/PRO_0000218290 http://togogenome.org/gene/10090:Lrrc3b ^@ http://purl.uniprot.org/uniprot/Q543Z7|||http://purl.uniprot.org/uniprot/Q8VCH9 ^@ 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|||LRRNT domain-containing protein|||Leucine-rich repeat-containing protein 3B|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000021617|||http://purl.uniprot.org/annotation/PRO_5014309623 http://togogenome.org/gene/10090:Spag4 ^@ http://purl.uniprot.org/uniprot/Q8BLQ4|||http://purl.uniprot.org/uniprot/Q9JJF2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Polar residues|||SUN|||Sperm-associated antigen 4 protein ^@ http://purl.uniprot.org/annotation/PRO_0000218917|||http://purl.uniprot.org/annotation/VSP_005958|||http://purl.uniprot.org/annotation/VSP_005959 http://togogenome.org/gene/10090:Zfp362 ^@ http://purl.uniprot.org/uniprot/B1ASA5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ddx46 ^@ http://purl.uniprot.org/uniprot/Q569Z5 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Splice Variant ^@ 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 isoform 2.|||N-myristoyl glycine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Probable ATP-dependent RNA helicase DDX46|||Q motif|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000055122|||http://purl.uniprot.org/annotation/VSP_016859 http://togogenome.org/gene/10090:Fbp1 ^@ http://purl.uniprot.org/uniprot/Q9QXD6 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Fructose-1,6-bisphosphatase 1|||N-acetylalanine|||N6-succinyllysine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000200499 http://togogenome.org/gene/10090:Apobec1 ^@ http://purl.uniprot.org/uniprot/P51908|||http://purl.uniprot.org/uniprot/Q3U9G8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ C->U-editing enzyme APOBEC-1|||CMP/dCMP-type deaminase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000171745 http://togogenome.org/gene/10090:Dnaaf10 ^@ http://purl.uniprot.org/uniprot/Q8BGF3 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ Dynein axonemal assembly factor 10|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000301672 http://togogenome.org/gene/10090:Pou2f2 ^@ http://purl.uniprot.org/uniprot/Q00196 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Homeobox|||In isoform OCT2.2.|||In isoform OCT2.3 and isoform OCT2.7.|||In isoform OCT2.4.|||In isoform OCT2.5.|||In isoform OCT2.6.|||In isoform OCT2.7.|||Leucine-zipper|||POU domain, class 2, transcription factor 2|||POU-specific|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000100715|||http://purl.uniprot.org/annotation/VSP_002326|||http://purl.uniprot.org/annotation/VSP_002327|||http://purl.uniprot.org/annotation/VSP_002328|||http://purl.uniprot.org/annotation/VSP_002329|||http://purl.uniprot.org/annotation/VSP_002330|||http://purl.uniprot.org/annotation/VSP_002331|||http://purl.uniprot.org/annotation/VSP_032188 http://togogenome.org/gene/10090:Myh7 ^@ http://purl.uniprot.org/uniprot/B2RXX9|||http://purl.uniprot.org/uniprot/Q91Z83 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region ^@ Actin-binding|||Disordered|||IQ|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-7|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000274177 http://togogenome.org/gene/10090:Guk1 ^@ http://purl.uniprot.org/uniprot/E9Q7K1|||http://purl.uniprot.org/uniprot/Q64520 ^@ 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 ^@ Guanylate kinase|||Guanylate kinase-like|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000170652|||http://purl.uniprot.org/annotation/VSP_060370 http://togogenome.org/gene/10090:Or5p53 ^@ http://purl.uniprot.org/uniprot/Q8VG44 ^@ 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 5P53 ^@ http://purl.uniprot.org/annotation/PRO_0000150833 http://togogenome.org/gene/10090:Zfp729a ^@ http://purl.uniprot.org/uniprot/Q4QQP3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Eps15l1 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLS1|||http://purl.uniprot.org/uniprot/Q60902 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EH|||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|||UIM 1|||UIM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000146119|||http://purl.uniprot.org/annotation/VSP_010681|||http://purl.uniprot.org/annotation/VSP_010682|||http://purl.uniprot.org/annotation/VSP_010683|||http://purl.uniprot.org/annotation/VSP_010684|||http://purl.uniprot.org/annotation/VSP_022638|||http://purl.uniprot.org/annotation/VSP_022639 http://togogenome.org/gene/10090:Rnf139 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0K8|||http://purl.uniprot.org/uniprot/Q7TMV1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF139|||Helical|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||RING-type|||RING-type; atypical|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056099 http://togogenome.org/gene/10090:Lzts3 ^@ http://purl.uniprot.org/uniprot/A2AHG0 ^@ 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.|||Leucine zipper putative tumor suppressor 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000394199|||http://purl.uniprot.org/annotation/VSP_039203|||http://purl.uniprot.org/annotation/VSP_039204|||http://purl.uniprot.org/annotation/VSP_039205 http://togogenome.org/gene/10090:C2cd4b ^@ http://purl.uniprot.org/uniprot/Q80XU5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Or11m3 ^@ http://purl.uniprot.org/uniprot/Q8VFD8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Jmjd7 ^@ http://purl.uniprot.org/uniprot/P0C872 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Strand|||Turn ^@ Bifunctional peptidase and (3S)-lysyl hydroxylase Jmjd7|||Interchain|||JmjC ^@ http://purl.uniprot.org/annotation/PRO_0000349375 http://togogenome.org/gene/10090:Stac ^@ http://purl.uniprot.org/uniprot/P97306|||http://purl.uniprot.org/uniprot/Q3UPL9|||http://purl.uniprot.org/uniprot/Q3UYD4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||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_0000072236 http://togogenome.org/gene/10090:Creld1 ^@ http://purl.uniprot.org/uniprot/A8C1T7|||http://purl.uniprot.org/uniprot/Q91XD7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ CXXC|||Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||Extracellular|||FU 1|||FU 2|||Helical|||N-linked (GlcNAc...) asparagine|||Protein disulfide isomerase Creld1|||Redox-active|||protein disulfide-isomerase ^@ http://purl.uniprot.org/annotation/PRO_0000042782|||http://purl.uniprot.org/annotation/PRO_5014297358 http://togogenome.org/gene/10090:Art4 ^@ http://purl.uniprot.org/uniprot/Q9CRA0 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Ecto-ADP-ribosyltransferase 4|||Extracellular|||GPI-anchor amidated alanine|||Helical|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||TR mART core ^@ http://purl.uniprot.org/annotation/PRO_0000416110|||http://purl.uniprot.org/annotation/PRO_0000416111 http://togogenome.org/gene/10090:Akirin2 ^@ http://purl.uniprot.org/uniprot/B1AXD8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Motif|||Sequence Conflict ^@ Akirin-2|||Nuclear localization signal|||Phosphoserine|||SYVS motif ^@ http://purl.uniprot.org/annotation/PRO_0000355121 http://togogenome.org/gene/10090:Gm13275 ^@ http://purl.uniprot.org/uniprot/B1AYI8 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5040053582 http://togogenome.org/gene/10090:Rgs19 ^@ http://purl.uniprot.org/uniprot/B7ZCT1|||http://purl.uniprot.org/uniprot/Q78NN4|||http://purl.uniprot.org/uniprot/Q8BFU4|||http://purl.uniprot.org/uniprot/Q9CX84 ^@ 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|||Interaction with GIPC|||Phosphoserine|||Phosphoserine; by MAPK1 and MAPK3|||RGS|||Regulator of G-protein signaling 19 ^@ http://purl.uniprot.org/annotation/PRO_0000204230 http://togogenome.org/gene/10090:Bnip5 ^@ http://purl.uniprot.org/uniprot/Q8CC96 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Protein BNIP5 ^@ http://purl.uniprot.org/annotation/PRO_0000317188 http://togogenome.org/gene/10090:Gzf1 ^@ http://purl.uniprot.org/uniprot/Q4VBD9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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|||Disordered|||GDNF-inducible zinc finger protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000409660 http://togogenome.org/gene/10090:4921507P07Rik ^@ http://purl.uniprot.org/uniprot/Q9D5Y0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Sperm-associated microtubule inner protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000089588 http://togogenome.org/gene/10090:Tbx18 ^@ http://purl.uniprot.org/uniprot/G3X919|||http://purl.uniprot.org/uniprot/Q8C003|||http://purl.uniprot.org/uniprot/Q9EPZ6 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Motif|||Region ^@ Disordered|||Engrailed homology 1 repressor|||Nuclear localization signal|||T-box|||T-box transcription factor TBX18 ^@ http://purl.uniprot.org/annotation/PRO_0000184447 http://togogenome.org/gene/10090:Lyset ^@ http://purl.uniprot.org/uniprot/Q8BH26 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Lysosomal enzyme trafficking factor ^@ http://purl.uniprot.org/annotation/PRO_0000089917 http://togogenome.org/gene/10090:Rnf180 ^@ http://purl.uniprot.org/uniprot/Q3U827 ^@ 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 4.|||In isoform 3.|||In isoform 4.|||Interaction with ZIC2|||Phosphoserine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000261618|||http://purl.uniprot.org/annotation/VSP_021741|||http://purl.uniprot.org/annotation/VSP_021742|||http://purl.uniprot.org/annotation/VSP_021743 http://togogenome.org/gene/10090:Setd4 ^@ http://purl.uniprot.org/uniprot/P58467 ^@ 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 ^@ Basic residues|||Disordered|||SET|||SET domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000079510 http://togogenome.org/gene/10090:Slc15a3 ^@ http://purl.uniprot.org/uniprot/Q8BPX9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Solute carrier family 15 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000295913 http://togogenome.org/gene/10090:Hyal3 ^@ http://purl.uniprot.org/uniprot/Q8VEI3 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ EGF-like|||Hyaluronidase-3|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000248201 http://togogenome.org/gene/10090:Ddx3x ^@ http://purl.uniprot.org/uniprot/Q3TQX5|||http://purl.uniprot.org/uniprot/Q62167 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ ATP-dependent RNA helicase DDX3X|||Basic and acidic 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|||Interaction with CHUK|||Interaction with EIF4E|||Interaction with GSK3B|||Interaction with IKBKE|||Interaction with NXF1|||Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwinding|||N-acetylserine|||N6-acetyllysine|||Nuclear export signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Q motif|||Removed|||Required for TBK1 and IKBKE-dependent IFNB1 activation ^@ http://purl.uniprot.org/annotation/PRO_0000055010 http://togogenome.org/gene/10090:Cobll1 ^@ http://purl.uniprot.org/uniprot/B1AZ15|||http://purl.uniprot.org/uniprot/Q3UMF0 ^@ 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|||Cordon-bleu protein-like 1|||Cordon-bleu ubiquitin-like|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 3.|||KKRRAP 1|||KKRRAP 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000260494|||http://purl.uniprot.org/annotation/VSP_021626|||http://purl.uniprot.org/annotation/VSP_021627|||http://purl.uniprot.org/annotation/VSP_022324 http://togogenome.org/gene/10090:Timp3 ^@ http://purl.uniprot.org/uniprot/P39876|||http://purl.uniprot.org/uniprot/Q54AE5 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Involved in metalloproteinase-binding|||Mediates interaction with EFEMP1|||Metalloproteinase inhibitor 3|||NTR ^@ http://purl.uniprot.org/annotation/PRO_0000034344|||http://purl.uniprot.org/annotation/PRO_5014309626 http://togogenome.org/gene/10090:Dnajc2 ^@ http://purl.uniprot.org/uniprot/P54103 ^@ 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|||DnaJ homolog subfamily C member 2|||J|||N-acetylmethionine|||Phosphoserine|||Polar residues|||SANT 1|||SANT 2|||ZRF1-UBD ^@ http://purl.uniprot.org/annotation/PRO_0000071124 http://togogenome.org/gene/10090:Pabir2 ^@ http://purl.uniprot.org/uniprot/G1UD78|||http://purl.uniprot.org/uniprot/Q6NZE7 ^@ 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.|||In isoform 4.|||N-acetylalanine|||Omega-N-methylarginine|||PABIR family member 2|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000254546|||http://purl.uniprot.org/annotation/VSP_021219|||http://purl.uniprot.org/annotation/VSP_021220|||http://purl.uniprot.org/annotation/VSP_021221 http://togogenome.org/gene/10090:Mgl2 ^@ http://purl.uniprot.org/uniprot/A9XX86|||http://purl.uniprot.org/uniprot/Q8JZN1 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||C-type lectin|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Miox ^@ http://purl.uniprot.org/uniprot/Q9QXN5 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ Inositol oxygenase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000079149 http://togogenome.org/gene/10090:1190005I06Rik ^@ http://purl.uniprot.org/uniprot/Q8K1L6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Phosphothreonine|||Required for interaction with PPP3CA|||Uncharacterized protein C16orf74 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000264622 http://togogenome.org/gene/10090:Arap3 ^@ http://purl.uniprot.org/uniprot/Q8R5G7 ^@ 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 ^@ Arf-GAP|||Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of Rho GAP activity. Enhances cell spreading.|||PH 1|||PH 2|||PH 3|||PH 4|||PH 5|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Ras-associating|||Rho-GAP|||SAM|||Strongly reduces phosphorylation by CSK; when associated with F-1399.|||Strongly reduces phosphorylation by CSK; when associated with F-1404. ^@ http://purl.uniprot.org/annotation/PRO_0000074216|||http://purl.uniprot.org/annotation/VSP_015002|||http://purl.uniprot.org/annotation/VSP_015003|||http://purl.uniprot.org/annotation/VSP_015004 http://togogenome.org/gene/10090:Ppp1r12b ^@ http://purl.uniprot.org/uniprot/A0A571BGD8|||http://purl.uniprot.org/uniprot/A6H644 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ ANK|||Basic and acidic residues|||Disordered|||Polar residues|||cGMP-dependent protein kinase interacting ^@ http://togogenome.org/gene/10090:Kcnk5 ^@ http://purl.uniprot.org/uniprot/Q9JK62 ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Interchain|||Polar residues|||Potassium channel ^@ http://togogenome.org/gene/10090:Med17 ^@ http://purl.uniprot.org/uniprot/Q8VCD5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Mediator of RNA polymerase II transcription subunit 17 ^@ http://purl.uniprot.org/annotation/PRO_0000304700 http://togogenome.org/gene/10090:Or12e7 ^@ http://purl.uniprot.org/uniprot/Q7TR49 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or5w16 ^@ http://purl.uniprot.org/uniprot/Q7TR39 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Frzb ^@ http://purl.uniprot.org/uniprot/P97401 ^@ 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 ^@ Disordered|||FZ|||N-linked (GlcNAc...) asparagine|||NTR|||Polar residues|||Secreted frizzled-related protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000032547 http://togogenome.org/gene/10090:Cacna1i ^@ http://purl.uniprot.org/uniprot/E9Q7P2 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site|||Transmembrane ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Ion transport|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Ndufa2 ^@ http://purl.uniprot.org/uniprot/Q9CQ75 ^@ Chain|||Disulfide Bond|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand ^@ N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2|||Redox-active|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118790 http://togogenome.org/gene/10090:Adam21 ^@ http://purl.uniprot.org/uniprot/Q9JI76 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||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_0000029110|||http://purl.uniprot.org/annotation/PRO_0000029111 http://togogenome.org/gene/10090:Tex10 ^@ http://purl.uniprot.org/uniprot/Q3URQ0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ HEAT|||Phosphothreonine|||Testis-expressed protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000391000 http://togogenome.org/gene/10090:Zfp369 ^@ http://purl.uniprot.org/uniprot/F8VQL6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB|||Polar residues|||SCAN box ^@ http://togogenome.org/gene/10090:Nfatc2 ^@ http://purl.uniprot.org/uniprot/A2AQC8|||http://purl.uniprot.org/uniprot/B5B2P6|||http://purl.uniprot.org/uniprot/B5B2P7|||http://purl.uniprot.org/uniprot/B5B2P8|||http://purl.uniprot.org/uniprot/B5B2Q2|||http://purl.uniprot.org/uniprot/B5B2Q4|||http://purl.uniprot.org/uniprot/B5B2Q6|||http://purl.uniprot.org/uniprot/B5B2R5|||http://purl.uniprot.org/uniprot/Q3TTU8|||http://purl.uniprot.org/uniprot/Q60591|||http://purl.uniprot.org/uniprot/Q8C443 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 1|||2|||3 X approximate SP repeats|||3; approximate|||Calcineurin-binding|||Decrease in binding to DNA.|||Disordered|||In isoform B.|||In isoform D.|||Induces aberrant nuclear localization of the phosphorylated form.|||Lowers dephosphorylation.|||No change in binding to DNA and confers DNA-binding sensitivity to sulfhydryl modifications.|||No change in binding to DNA.|||No dephosphorylation.|||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_0000205179|||http://purl.uniprot.org/annotation/VSP_005596|||http://purl.uniprot.org/annotation/VSP_005597 http://togogenome.org/gene/10090:Krt73 ^@ http://purl.uniprot.org/uniprot/Q6NXH9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Chain|||Domain Extent|||Region|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type II cytoskeletal 73|||Linker 1|||Linker 12|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000314882 http://togogenome.org/gene/10090:Hnrnpul1 ^@ http://purl.uniprot.org/uniprot/Q8VDM6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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.|||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_0000227556|||http://purl.uniprot.org/annotation/VSP_017553|||http://purl.uniprot.org/annotation/VSP_017554|||http://purl.uniprot.org/annotation/VSP_017555 http://togogenome.org/gene/10090:Manba ^@ http://purl.uniprot.org/uniprot/A0A0R4J092|||http://purl.uniprot.org/uniprot/Q8K2I4 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Beta-mannosidase|||Beta-mannosidase Ig-fold|||Glycoside hydrolase family 2 catalytic|||Mannosidase Ig/CBM-like|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000250613|||http://purl.uniprot.org/annotation/PRO_5006451946 http://togogenome.org/gene/10090:4932438H23Rik ^@ http://purl.uniprot.org/uniprot/Q9D4G1 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Uncharacterized protein C21orf62 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000079525 http://togogenome.org/gene/10090:Slc22a2 ^@ http://purl.uniprot.org/uniprot/O70577 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Involved in recognition of organic cations and participates in structural changes that occur during translocation of organic cations|||N-linked (GlcNAc...) asparagine|||Proline-rich sequence|||Solute carrier family 22 member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000320958|||http://purl.uniprot.org/annotation/VSP_031775|||http://purl.uniprot.org/annotation/VSP_031776 http://togogenome.org/gene/10090:Stpg4 ^@ http://purl.uniprot.org/uniprot/Q9DAG5 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein STPG4 ^@ http://purl.uniprot.org/annotation/PRO_0000311685 http://togogenome.org/gene/10090:Fam162b ^@ http://purl.uniprot.org/uniprot/B2RV81|||http://purl.uniprot.org/uniprot/Q9CX19 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Protein FAM162B ^@ http://purl.uniprot.org/annotation/PRO_0000254640 http://togogenome.org/gene/10090:Mill2 ^@ http://purl.uniprot.org/uniprot/Q8HWE5 ^@ Chain|||Disulfide Bond|||Domain Extent|||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|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Fails to bind to NIH-3T3 fibroblast cells; when associated with 273-A--A-276.|||Fails to bind to NIH-3T3 fibroblast cells; when associated with A-291.|||Fails to bind to heparan sulfate or to NIH-3T3 fibroblast cells; when associated with A-238 and A-244.|||Fails to bind to heparan sulfate or to NIH-3T3 fibroblast cells; when associated with A-238 and A-295.|||Fails to bind to heparan sulfate or to NIH-3T3 fibroblast cells; when associated with A-244 and A-295.|||GPI-anchor amidated aspartate|||Ig-like C1-type|||In isoform 2.|||MHC class I-like protein MILL2|||N-linked (GlcNAc...) asparagine|||No effect on binding to NIH-3T3 fibroblast cells.|||No effect on binding to NIH-3T3 fibroblast cells; when associated with A-109.|||No effect on binding to NIH-3T3 fibroblast cells; when associated with A-216.|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000452207|||http://purl.uniprot.org/annotation/PRO_5015099155|||http://purl.uniprot.org/annotation/VSP_060927 http://togogenome.org/gene/10090:Gml ^@ http://purl.uniprot.org/uniprot/E9PX31 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_5015090359 http://togogenome.org/gene/10090:Sema4g ^@ http://purl.uniprot.org/uniprot/Q9WUH7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Pro residues|||Sema|||Semaphorin-4G ^@ http://purl.uniprot.org/annotation/PRO_0000032334 http://togogenome.org/gene/10090:H2ac22 ^@ http://purl.uniprot.org/uniprot/B2RVF0|||http://purl.uniprot.org/uniprot/C0HKE1|||http://purl.uniprot.org/uniprot/C0HKE2|||http://purl.uniprot.org/uniprot/C0HKE3|||http://purl.uniprot.org/uniprot/C0HKE4|||http://purl.uniprot.org/uniprot/C0HKE5|||http://purl.uniprot.org/uniprot/C0HKE6|||http://purl.uniprot.org/uniprot/C0HKE7|||http://purl.uniprot.org/uniprot/C0HKE8|||http://purl.uniprot.org/uniprot/C0HKE9 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Histone H2A type 1-C|||Histone H2A type 1-D|||Histone H2A type 1-E|||Histone H2A type 1-G|||Histone H2A type 1-I|||Histone H2A type 1-N|||Histone H2A type 1-O|||Histone H2A type 1-P|||Histone H2A/H2B/H3|||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_0000439715|||http://purl.uniprot.org/annotation/PRO_0000439716|||http://purl.uniprot.org/annotation/PRO_0000439717|||http://purl.uniprot.org/annotation/PRO_0000439718|||http://purl.uniprot.org/annotation/PRO_0000439719|||http://purl.uniprot.org/annotation/PRO_0000439720|||http://purl.uniprot.org/annotation/PRO_0000439721|||http://purl.uniprot.org/annotation/PRO_0000439722|||http://purl.uniprot.org/annotation/PRO_0000439723 http://togogenome.org/gene/10090:Hibadh ^@ http://purl.uniprot.org/uniprot/Q99L13 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ 3-hydroxyisobutyrate dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000007159 http://togogenome.org/gene/10090:Dbt ^@ http://purl.uniprot.org/uniprot/P53395 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||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|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000020490 http://togogenome.org/gene/10090:Calm4 ^@ http://purl.uniprot.org/uniprot/Q9JM83 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Calmodulin-4|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4 ^@ http://purl.uniprot.org/annotation/PRO_0000073856 http://togogenome.org/gene/10090:Mageb1 ^@ http://purl.uniprot.org/uniprot/Q60761 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Or9g4 ^@ http://purl.uniprot.org/uniprot/A2ALD2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ G-protein coupled receptors family 1 profile ^@ http://togogenome.org/gene/10090:Vmn1r258 ^@ http://purl.uniprot.org/uniprot/D3YTW8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hexb ^@ http://purl.uniprot.org/uniprot/P20060|||http://purl.uniprot.org/uniprot/Q3TXR9 ^@ 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 ^@ Beta-hexosaminidase|||Beta-hexosaminidase eukaryotic type N-terminal|||Beta-hexosaminidase subunit beta|||Glycoside hydrolase family 20 catalytic|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000012006|||http://purl.uniprot.org/annotation/PRO_5010843323 http://togogenome.org/gene/10090:Poli ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Z5|||http://purl.uniprot.org/uniprot/E9Q3H9|||http://purl.uniprot.org/uniprot/E9QJU6|||http://purl.uniprot.org/uniprot/Q6R3M4 ^@ 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 binding and localization to nuclear foci after UV-induced DNA damage.|||Basic and acidic residues|||DNA polymerase iota|||DNA-binding|||Disordered|||Impairs ubiquitin binding and post-translation modification via ubiquitination; when associated with A-508. Abolishes ubiquitin binding and localization to nuclear foci after UV-induced DNA damage but does not affect catalytic activity; when associated with A-509, A-693 and A-694.|||Impairs ubiquitin binding and post-translation modification via ubiquitination; when associated with A-509. Abolishes ubiquitin binding and localization to nuclear foci after UV-induced DNA damage but does not affect catalytic activity; when associated with A-508, A-693 and A-694.|||Impairs ubiquitin binding and post-translation modification via ubiquitination; when associated with A-693. Abolishes ubiquitin binding and localization to nuclear foci after UV-induced DNA damage but does not affect catalytic activity; when associated with A-508, A-509 and A-693.|||Impairs ubiquitin binding and post-translation modification via ubiquitination; when associated with A-694. Abolishes ubiquitin binding and localization to nuclear foci after UV-induced DNA damage but does not affect catalytic activity; when associated with A-508, A-509 and A-694.|||In isoform 2.|||In strain: BALB/c.|||Polar residues|||Proton acceptor|||Ubiquitin-binding 1 (UBM1)|||Ubiquitin-binding 2 (UBM2)|||UmuC ^@ http://purl.uniprot.org/annotation/PRO_0000173989|||http://purl.uniprot.org/annotation/VSP_012800 http://togogenome.org/gene/10090:Ccdc77 ^@ http://purl.uniprot.org/uniprot/Q9CZH8 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Coiled-coil domain-containing protein 77|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000271004|||http://purl.uniprot.org/annotation/VSP_022264 http://togogenome.org/gene/10090:Matn4 ^@ http://purl.uniprot.org/uniprot/F2Z3U4|||http://purl.uniprot.org/uniprot/O89029 ^@ 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|||EGF-like 2|||EGF-like 3|||EGF-like 4|||In isoform Short.|||In strain: C57BL/6J.|||Matrilin-4|||N-linked (GlcNAc...) asparagine|||VWFA|||VWFA 1|||VWFA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000007661|||http://purl.uniprot.org/annotation/PRO_5015090999|||http://purl.uniprot.org/annotation/VSP_001401 http://togogenome.org/gene/10090:Or5d36 ^@ http://purl.uniprot.org/uniprot/Q8VFR4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pop7 ^@ http://purl.uniprot.org/uniprot/Q9DCH2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Ribonuclease P protein subunit p20 ^@ http://purl.uniprot.org/annotation/PRO_0000237701 http://togogenome.org/gene/10090:Btbd35f3 ^@ http://purl.uniprot.org/uniprot/A2CGC2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Tmem164 ^@ http://purl.uniprot.org/uniprot/A2AH99|||http://purl.uniprot.org/uniprot/Q3TLI7|||http://purl.uniprot.org/uniprot/Q6PHN7 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 164 ^@ http://purl.uniprot.org/annotation/PRO_0000259641|||http://purl.uniprot.org/annotation/PRO_5015086014 http://togogenome.org/gene/10090:Rbm34 ^@ http://purl.uniprot.org/uniprot/Q8C5L7 ^@ 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|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||RNA-binding protein 34|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081791 http://togogenome.org/gene/10090:Nbas ^@ http://purl.uniprot.org/uniprot/E9Q411|||http://purl.uniprot.org/uniprot/Q6GQV6|||http://purl.uniprot.org/uniprot/Q8BUH3 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Neuroblastoma-amplified sequence N-terminal|||Sec39 ^@ http://togogenome.org/gene/10090:Aldh1a7 ^@ http://purl.uniprot.org/uniprot/B2RTL5|||http://purl.uniprot.org/uniprot/O35945 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Site ^@ Aldehyde dehydrogenase|||Aldehyde dehydrogenase, cytosolic 1|||N-acetylserine|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Proton acceptor|||Removed|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000291264 http://togogenome.org/gene/10090:Uqcrc2 ^@ http://purl.uniprot.org/uniprot/Q9DB77 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Cytochrome b-c1 complex subunit 2, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000026792 http://togogenome.org/gene/10090:Pdcd1 ^@ http://purl.uniprot.org/uniprot/Q02242|||http://purl.uniprot.org/uniprot/Q544F3 ^@ Chain|||Crosslink|||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 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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|||Phosphotyrosine|||Programmed cell death protein 1|||Reduced tyrosine phosphorylation. Abolished ability to mediate recruitment of PTPN11/SHP-2.|||Reduced tyrosine phosphorylation. Decreased ability to mediate recruitment of PTPN11/SHP-2. ^@ http://purl.uniprot.org/annotation/PRO_0000014893|||http://purl.uniprot.org/annotation/PRO_5014309575 http://togogenome.org/gene/10090:Syt16 ^@ http://purl.uniprot.org/uniprot/Q7TN83 ^@ 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|||C2 1|||C2 2|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Synaptotagmin-16 ^@ http://purl.uniprot.org/annotation/PRO_0000258585|||http://purl.uniprot.org/annotation/VSP_021381|||http://purl.uniprot.org/annotation/VSP_021382|||http://purl.uniprot.org/annotation/VSP_021383|||http://purl.uniprot.org/annotation/VSP_021384|||http://purl.uniprot.org/annotation/VSP_021385 http://togogenome.org/gene/10090:Nampt ^@ http://purl.uniprot.org/uniprot/Q99KQ4 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ N-acetylmethionine|||Nicotinamide phosphoribosyltransferase|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000205864 http://togogenome.org/gene/10090:Unc5b ^@ http://purl.uniprot.org/uniprot/Q8K1S3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||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|||Lipid Binding|||Modified Residue|||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.|||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_0000036072|||http://purl.uniprot.org/annotation/VSP_011699 http://togogenome.org/gene/10090:Cgrrf1 ^@ http://purl.uniprot.org/uniprot/Q8BMJ7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Sequence Conflict|||Zinc Finger ^@ Cell growth regulator with RING finger domain protein 1|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055870 http://togogenome.org/gene/10090:Or10h1 ^@ http://purl.uniprot.org/uniprot/A0PK55 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bcl2 ^@ http://purl.uniprot.org/uniprot/P10417|||http://purl.uniprot.org/uniprot/Q6NTH7|||http://purl.uniprot.org/uniprot/Q8BQK4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Apoptosis regulator Bcl-2|||Apoptosis regulator Bcl-2 family BH4|||BH1|||BH2|||BH3|||BH4|||Cleavage; by caspases|||Helical|||In isoform Beta.|||Loss of phosphorylation. Unable to suppress apoptosis.|||Phosphoserine; by MAPK8|||Phosphoserine; by MAPK8 and PKC|||Phosphothreonine; by MAPK8 ^@ http://purl.uniprot.org/annotation/PRO_0000143049|||http://purl.uniprot.org/annotation/VSP_000513 http://togogenome.org/gene/10090:0610010K14Rik ^@ http://purl.uniprot.org/uniprot/A2CF83|||http://purl.uniprot.org/uniprot/D3Z687|||http://purl.uniprot.org/uniprot/Q9DCT6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Chromatin complexes subunit BAP18|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Phosphoserine|||SANT ^@ http://purl.uniprot.org/annotation/PRO_0000264252|||http://purl.uniprot.org/annotation/VSP_021892|||http://purl.uniprot.org/annotation/VSP_021893 http://togogenome.org/gene/10090:Kansl1l ^@ http://purl.uniprot.org/uniprot/Q5DTI6 ^@ 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.|||In isoform 4.|||In isoform 5.|||KAT8 regulatory NSL complex subunit 1-like protein|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000319583|||http://purl.uniprot.org/annotation/VSP_031502|||http://purl.uniprot.org/annotation/VSP_031503|||http://purl.uniprot.org/annotation/VSP_031504|||http://purl.uniprot.org/annotation/VSP_031505|||http://purl.uniprot.org/annotation/VSP_031506|||http://purl.uniprot.org/annotation/VSP_031507 http://togogenome.org/gene/10090:Fdx2 ^@ http://purl.uniprot.org/uniprot/Q9CPW2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ 2Fe-2S ferredoxin-type|||Disordered|||Ferredoxin-2, mitochondrial|||In isoform 2.|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000325953|||http://purl.uniprot.org/annotation/VSP_032498 http://togogenome.org/gene/10090:Prl3d3 ^@ http://purl.uniprot.org/uniprot/Q8CGZ7 ^@ Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099038 http://togogenome.org/gene/10090:1700029J07Rik ^@ http://purl.uniprot.org/uniprot/Q3U1D9 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Cilia-and flagella-associated protein 96|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000341951 http://togogenome.org/gene/10090:Sirt7 ^@ http://purl.uniprot.org/uniprot/Q8BKJ9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes deacylase and deacetylase activities. Reduced interaction with SIRT1, without abolishing it.|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Deacetylase sirtuin-type|||Disordered|||NAD-dependent protein deacetylase sirtuin-7|||Omega-N-methylarginine; alternate|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000110272 http://togogenome.org/gene/10090:Or8d1 ^@ http://purl.uniprot.org/uniprot/Q7TRB7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zpbp2 ^@ http://purl.uniprot.org/uniprot/Q5FWC7|||http://purl.uniprot.org/uniprot/Q6X786 ^@ 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.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Zona pellucida-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000041602|||http://purl.uniprot.org/annotation/PRO_5004256457|||http://purl.uniprot.org/annotation/VSP_011684|||http://purl.uniprot.org/annotation/VSP_011685 http://togogenome.org/gene/10090:Pcbp2 ^@ http://purl.uniprot.org/uniprot/A0A2R8VHP9|||http://purl.uniprot.org/uniprot/Q3TT81|||http://purl.uniprot.org/uniprot/Q61990 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Splice Variant ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||K Homology|||KH 1|||KH 2|||KH 3|||Phosphoserine|||Poly(rC)-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000050091|||http://purl.uniprot.org/annotation/VSP_002820|||http://purl.uniprot.org/annotation/VSP_002821 http://togogenome.org/gene/10090:Rhox6 ^@ http://purl.uniprot.org/uniprot/O70238 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Lpar6 ^@ http://purl.uniprot.org/uniprot/Q8BMC0 ^@ 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|||Lysophosphatidic acid receptor 6|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000070026 http://togogenome.org/gene/10090:Rbmx2 ^@ http://purl.uniprot.org/uniprot/Q8R0F5 ^@ 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|||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_0000081898 http://togogenome.org/gene/10090:Or10g1 ^@ http://purl.uniprot.org/uniprot/E9PZZ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rnf168 ^@ http://purl.uniprot.org/uniprot/E9PYW4|||http://purl.uniprot.org/uniprot/Q80XJ2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF168|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||LR motif 1|||LR motif 2|||MIU motif 1|||MIU motif 2|||Phosphoserine|||Polar residues|||RING-type|||UMI motif ^@ http://purl.uniprot.org/annotation/PRO_0000245597 http://togogenome.org/gene/10090:Dis3l2 ^@ http://purl.uniprot.org/uniprot/Q8CI75 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ 40% decreased enzyme activity.|||40% increased enzyme activity.|||Basic and acidic residues|||DIS3-like exonuclease 2|||Disordered|||Does not affect enzyme activity.|||Impaired enzyme activity and polyuridylated RNA-binding.|||Important for catalytic activity|||In isoform 2.|||Loss of enzyme activity and polyuridylated RNA-binding; when associated with A-612.|||Loss of enzyme activity and polyuridylated RNA-binding; when associated with A-74.|||Loss of exoribonuclease activity.|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314818|||http://purl.uniprot.org/annotation/VSP_030379 http://togogenome.org/gene/10090:Ankrd61 ^@ http://purl.uniprot.org/uniprot/Q9CQM6 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Repeat|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||Ankyrin repeat domain-containing protein 61|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000328763|||http://purl.uniprot.org/annotation/VSP_032775 http://togogenome.org/gene/10090:Sspn ^@ http://purl.uniprot.org/uniprot/E9Q8Y7|||http://purl.uniprot.org/uniprot/Q3TPB3|||http://purl.uniprot.org/uniprot/Q3TRE0|||http://purl.uniprot.org/uniprot/Q62147 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Sarcospan ^@ http://purl.uniprot.org/annotation/PRO_0000072227 http://togogenome.org/gene/10090:Cldn22 ^@ http://purl.uniprot.org/uniprot/Q9D7U6 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Claudin-22|||Cytoplasmic|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000144786 http://togogenome.org/gene/10090:Rasgrp1 ^@ http://purl.uniprot.org/uniprot/Q9Z1S3 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||Loss of function and transforming activity.|||N-terminal Ras-GEF|||PT region; mediates the BCR-dependent translocation to plasma membrane|||Phorbol-ester/DAG-type|||Phosphoserine|||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_0000316979 http://togogenome.org/gene/10090:Slc17a7 ^@ http://purl.uniprot.org/uniprot/Q3TXX4|||http://purl.uniprot.org/uniprot/Q8JZR7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Vesicular glutamate transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000331612 http://togogenome.org/gene/10090:Cspg5 ^@ http://purl.uniprot.org/uniprot/Q71M36 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Chondroitin sulfate proteoglycan 5|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interaction with GOPC|||Interaction with TNC and TNR|||N-linked (GlcNAc...) asparagine|||No chondroitin sulfate attachment. no effect on transport to the cell surface.|||No effect on chondroitin sulfate attachment.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000042152|||http://purl.uniprot.org/annotation/VSP_015762|||http://purl.uniprot.org/annotation/VSP_015763|||http://purl.uniprot.org/annotation/VSP_015764 http://togogenome.org/gene/10090:Npr2 ^@ http://purl.uniprot.org/uniprot/Q6VVW5 ^@ 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 ^@ Atrial natriuretic peptide receptor 2|||Cytoplasmic|||Extracellular|||Guanylate cyclase|||Helical|||In isoform 2.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000012365|||http://purl.uniprot.org/annotation/VSP_013583|||http://purl.uniprot.org/annotation/VSP_013584|||http://purl.uniprot.org/annotation/VSP_013585 http://togogenome.org/gene/10090:Tmem68 ^@ http://purl.uniprot.org/uniprot/Q9D850 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Monoacylglycerol/Diacylglycerol O-acyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000254593|||http://purl.uniprot.org/annotation/VSP_021247|||http://purl.uniprot.org/annotation/VSP_021248 http://togogenome.org/gene/10090:Prkg1 ^@ http://purl.uniprot.org/uniprot/P0C605|||http://purl.uniprot.org/uniprot/Q8BND1 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant ^@ AGC-kinase C-terminal|||Acidic residues|||Autoinhibitory domain|||Cyclic nucleotide-binding|||Disordered|||In isoform Beta.|||Interchain|||Leucine-zipper|||N-acetylserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||Required for dimerization|||cGMP-binding, high affinity|||cGMP-binding, low affinity|||cGMP-dependent protein kinase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000314022|||http://purl.uniprot.org/annotation/VSP_038715 http://togogenome.org/gene/10090:Fabp4 ^@ http://purl.uniprot.org/uniprot/P04117|||http://purl.uniprot.org/uniprot/Q542H7 ^@ 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 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand ^@ Abolishes export from nucleus; when associated with A-67 and A-87.|||Abolishes export from nucleus; when associated with A-67 and A-92.|||Abolishes export from nucleus; when associated with A-87 and A-92.|||Abolishes ligand-induced translocation to the nucleus.|||Abolishes ligand-induced translocation to the nucleus; when associated with A-22 and A-31.|||Abolishes ligand-induced translocation to the nucleus; when associated with A-22 and A-32.|||Abolishes ligand-induced translocation to the nucleus; when associated with A-31 and A-32.|||Cytosolic fatty-acid binding proteins|||Fatty acid-binding protein, adipocyte|||N-acetylcysteine|||Nuclear localization signal|||Phosphoserine|||Phosphotyrosine; by Tyr-kinases|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067367 http://togogenome.org/gene/10090:Gsdmc ^@ http://purl.uniprot.org/uniprot/Q99NB5 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Gasdermin-C|||Gasdermin-C, C-terminal|||Gasdermin-C, N-terminal|||Triggers pyroptosis ^@ http://purl.uniprot.org/annotation/PRO_0000349129|||http://purl.uniprot.org/annotation/PRO_0000451676|||http://purl.uniprot.org/annotation/PRO_0000451677 http://togogenome.org/gene/10090:Tsc22d1 ^@ http://purl.uniprot.org/uniprot/D3YW86|||http://purl.uniprot.org/uniprot/D3Z0V7|||http://purl.uniprot.org/uniprot/E9QLZ1|||http://purl.uniprot.org/uniprot/H3BLI9|||http://purl.uniprot.org/uniprot/P62500|||http://purl.uniprot.org/uniprot/Q3UXU0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes homodimerization; when associated with A-1024.|||Abolishes homodimerization; when associated with A-1030.|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||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_0000219366|||http://purl.uniprot.org/annotation/VSP_035327|||http://purl.uniprot.org/annotation/VSP_035328|||http://purl.uniprot.org/annotation/VSP_035329 http://togogenome.org/gene/10090:Mknk1 ^@ http://purl.uniprot.org/uniprot/A2A8W8|||http://purl.uniprot.org/uniprot/O08605|||http://purl.uniprot.org/uniprot/Q3U1I8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||Loss of kinase activity; when associated with T-209.|||Loss of kinase activity; when associated with T-214.|||MAP kinase-interacting serine/threonine-protein kinase 1|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphothreonine; by PAK2|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086335 http://togogenome.org/gene/10090:Or8b8 ^@ http://purl.uniprot.org/uniprot/B2RQ58|||http://purl.uniprot.org/uniprot/Q60882 ^@ 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 8B8 ^@ http://purl.uniprot.org/annotation/PRO_0000150822 http://togogenome.org/gene/10090:Vmn2r108 ^@ http://purl.uniprot.org/uniprot/E9PYS0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003243033 http://togogenome.org/gene/10090:Ablim2 ^@ http://purl.uniprot.org/uniprot/E9Q0W6|||http://purl.uniprot.org/uniprot/E9Q4K0|||http://purl.uniprot.org/uniprot/Q8BL65 ^@ 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 ^@ Actin-binding LIM protein 2|||Disordered|||HP|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||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_0000075700|||http://purl.uniprot.org/annotation/VSP_012120|||http://purl.uniprot.org/annotation/VSP_012121|||http://purl.uniprot.org/annotation/VSP_012122|||http://purl.uniprot.org/annotation/VSP_012123|||http://purl.uniprot.org/annotation/VSP_012124 http://togogenome.org/gene/10090:Skic8 ^@ http://purl.uniprot.org/uniprot/A0MNP4|||http://purl.uniprot.org/uniprot/D6RDC7|||http://purl.uniprot.org/uniprot/Q9ERF3 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ 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|||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_0000245852|||http://purl.uniprot.org/annotation/PRO_0000425749 http://togogenome.org/gene/10090:Atmin ^@ http://purl.uniprot.org/uniprot/Q6P9S1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger ^@ ATM interactor|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2; degenerate|||Disordered|||Polar residues|||Required for formation of RAD51 foci ^@ http://purl.uniprot.org/annotation/PRO_0000355036 http://togogenome.org/gene/10090:Pcdh19 ^@ http://purl.uniprot.org/uniprot/E9Q5E1|||http://purl.uniprot.org/uniprot/Q147Z9|||http://purl.uniprot.org/uniprot/Q80TF3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin-19 ^@ http://purl.uniprot.org/annotation/PRO_0000004004|||http://purl.uniprot.org/annotation/PRO_5003245744 http://togogenome.org/gene/10090:Cby2 ^@ http://purl.uniprot.org/uniprot/E9Q4B1|||http://purl.uniprot.org/uniprot/Q32MG2 ^@ 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.|||In isoform 3.|||Phosphoserine|||Polar residues|||Protein chibby homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000307293|||http://purl.uniprot.org/annotation/VSP_028675|||http://purl.uniprot.org/annotation/VSP_028676|||http://purl.uniprot.org/annotation/VSP_028677 http://togogenome.org/gene/10090:Mmp14 ^@ http://purl.uniprot.org/uniprot/P53690 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cysteine switch|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Matrix metalloproteinase-14|||Phosphotyrosine; by PKDCC|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028800|||http://purl.uniprot.org/annotation/PRO_0000028801 http://togogenome.org/gene/10090:Rnase13 ^@ http://purl.uniprot.org/uniprot/Q5GAM7 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Probable inactive ribonuclease-like protein 13 ^@ http://purl.uniprot.org/annotation/PRO_0000308706 http://togogenome.org/gene/10090:Vps50 ^@ http://purl.uniprot.org/uniprot/Q8CI71 ^@ 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 SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Syndetin ^@ http://purl.uniprot.org/annotation/PRO_0000307266|||http://purl.uniprot.org/annotation/VSP_028660|||http://purl.uniprot.org/annotation/VSP_028661|||http://purl.uniprot.org/annotation/VSP_028662|||http://purl.uniprot.org/annotation/VSP_028663 http://togogenome.org/gene/10090:Cabcoco1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J010|||http://purl.uniprot.org/uniprot/Q8CDT7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Ciliary-associated calcium-binding coiled-coil protein 1|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089820 http://togogenome.org/gene/10090:Dlx3 ^@ http://purl.uniprot.org/uniprot/Q64205|||http://purl.uniprot.org/uniprot/Q78ZZ8 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Homeobox protein DLX-3|||Interaction with DNA|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000049027 http://togogenome.org/gene/10090:Zfp764 ^@ http://purl.uniprot.org/uniprot/E9QAP1|||http://purl.uniprot.org/uniprot/Q8C964 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Cnnm1 ^@ http://purl.uniprot.org/uniprot/Q0GA42 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||CBS 1|||CBS 2|||CNNM transmembrane|||Disordered|||Helical|||Metal transporter CNNM1|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000295759 http://togogenome.org/gene/10090:Ndor1 ^@ http://purl.uniprot.org/uniprot/A0A2I3BQN1|||http://purl.uniprot.org/uniprot/A2AI05 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant|||Transmembrane ^@ FAD-binding FR-type|||Flavodoxin-like|||Helical|||In isoform 2.|||In isoform 3.|||NADPH-dependent diflavin oxidoreductase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000319540|||http://purl.uniprot.org/annotation/VSP_031488|||http://purl.uniprot.org/annotation/VSP_031489|||http://purl.uniprot.org/annotation/VSP_031490|||http://purl.uniprot.org/annotation/VSP_031491 http://togogenome.org/gene/10090:Hexa ^@ http://purl.uniprot.org/uniprot/P29416 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Beta-hexosaminidase subunit alpha|||Critical for hydrolysis GM2 gangliosides|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000011995|||http://purl.uniprot.org/annotation/PRO_0000011996 http://togogenome.org/gene/10090:Tac2 ^@ http://purl.uniprot.org/uniprot/P55099 ^@ Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Methionine amide|||Neurokinin-B ^@ http://purl.uniprot.org/annotation/PRO_0000033568|||http://purl.uniprot.org/annotation/PRO_0000033569|||http://purl.uniprot.org/annotation/PRO_0000033570 http://togogenome.org/gene/10090:Pusl1 ^@ http://purl.uniprot.org/uniprot/A2ADA5 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||Nucleophile|||tRNA pseudouridine synthase-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000358316|||http://purl.uniprot.org/annotation/VSP_036049|||http://purl.uniprot.org/annotation/VSP_036050|||http://purl.uniprot.org/annotation/VSP_036051|||http://purl.uniprot.org/annotation/VSP_036052|||http://purl.uniprot.org/annotation/VSP_036053|||http://purl.uniprot.org/annotation/VSP_036054 http://togogenome.org/gene/10090:Topbp1 ^@ http://purl.uniprot.org/uniprot/Q6ZQF0 ^@ 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|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn ^@ BRCT 1|||BRCT 2|||BRCT 3|||BRCT 4|||BRCT 5|||BRCT 6|||BRCT 7|||DNA topoisomerase 2-binding protein 1|||Disordered|||In strain: FVB/N.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000072632 http://togogenome.org/gene/10090:Aox1 ^@ http://purl.uniprot.org/uniprot/G3X8P9|||http://purl.uniprot.org/uniprot/O54754 ^@ 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 ^@ 2Fe-2S ferredoxin-type|||Abolishes catalytic activity on phthalazine and acetaldehyde. Decreases catalytic efficiency on benzaldehyde and retinal. Abolishes catalytic activity; when associated with E-806.|||Abolishes catalytic activity.|||Aldehyde oxidase 1|||Decreases substrate affinity and activity on benzaldehyde, phthalazine and acetaldehyde, while increases affinity for more hydrophobic aldehydes like retinal. Abolishes catalytic activity; when associated with R-884.|||FAD-binding PCMH-type|||In strain: 129/Sv.|||In strain: C57BL/6 XCBA and 129/Sv.|||In strain: C57BL/6 XCBA, requires 2 nucleotide substitutions.|||In strain: C57BL/6 XCBA.|||Phosphoserine|||Proton acceptor|||Proton acceptor; for azaheterocycle hydroxylase activity ^@ http://purl.uniprot.org/annotation/PRO_0000166106 http://togogenome.org/gene/10090:Abhd6 ^@ http://purl.uniprot.org/uniprot/Q8R2Y0|||http://purl.uniprot.org/uniprot/Q9D375 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ AB hydrolase-1|||Charge relay system|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Loss of the lipid hydrolase activity.|||Monoacylglycerol lipase ABHD6|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000281576|||http://purl.uniprot.org/annotation/VSP_024012 http://togogenome.org/gene/10090:Sds ^@ http://purl.uniprot.org/uniprot/Q3UEN6|||http://purl.uniprot.org/uniprot/Q8VBT2 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ L-serine dehydratase/L-threonine deaminase|||N-acetylalanine|||N6-(pyridoxal phosphate)lysine|||Removed|||Tryptophan synthase beta chain-like PALP ^@ http://purl.uniprot.org/annotation/PRO_0000185595 http://togogenome.org/gene/10090:Elk4 ^@ http://purl.uniprot.org/uniprot/P41158 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||ETS|||ETS domain-containing protein Elk-4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000204100 http://togogenome.org/gene/10090:Tcp1 ^@ http://purl.uniprot.org/uniprot/P11983 ^@ 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|||Phosphoserine|||Phosphotyrosine|||T-complex protein 1 subunit alpha ^@ http://purl.uniprot.org/annotation/PRO_0000128305|||http://purl.uniprot.org/annotation/VSP_024734|||http://purl.uniprot.org/annotation/VSP_024735 http://togogenome.org/gene/10090:Fggy ^@ http://purl.uniprot.org/uniprot/A2AJL3 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ FGGY carbohydrate kinase domain-containing protein|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000326453|||http://purl.uniprot.org/annotation/VSP_032660|||http://purl.uniprot.org/annotation/VSP_032661 http://togogenome.org/gene/10090:Ccdc112 ^@ http://purl.uniprot.org/uniprot/D3Z1J2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015088511 http://togogenome.org/gene/10090:Tpm4 ^@ http://purl.uniprot.org/uniprot/Q6IRU2 ^@ 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|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Tropomyosin alpha-4 chain ^@ http://purl.uniprot.org/annotation/PRO_0000205636 http://togogenome.org/gene/10090:Ryk ^@ http://purl.uniprot.org/uniprot/H9H9R6|||http://purl.uniprot.org/uniprot/Q01887|||http://purl.uniprot.org/uniprot/Q8K272 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase RYK|||WIF ^@ http://purl.uniprot.org/annotation/PRO_0000024465|||http://purl.uniprot.org/annotation/PRO_5003620519 http://togogenome.org/gene/10090:Fkbp9 ^@ http://purl.uniprot.org/uniprot/Q9Z247 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide ^@ EF-hand 1|||EF-hand 2|||N-linked (GlcNAc...) asparagine|||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_0000025516 http://togogenome.org/gene/10090:Kir3dl1 ^@ http://purl.uniprot.org/uniprot/D3Z751|||http://purl.uniprot.org/uniprot/Q673W4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Immunoglobulin|||Immunoglobulin subtype ^@ http://purl.uniprot.org/annotation/PRO_5003052447|||http://purl.uniprot.org/annotation/PRO_5015098137 http://togogenome.org/gene/10090:Armc9 ^@ http://purl.uniprot.org/uniprot/Q9D2I5 ^@ 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.|||In isoform 3.|||In isoform 4, isoform 6 and isoform 7.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||LisH|||LisH domain-containing protein ARMC9|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000280596|||http://purl.uniprot.org/annotation/VSP_023805|||http://purl.uniprot.org/annotation/VSP_023806|||http://purl.uniprot.org/annotation/VSP_023807|||http://purl.uniprot.org/annotation/VSP_023808|||http://purl.uniprot.org/annotation/VSP_023809|||http://purl.uniprot.org/annotation/VSP_023810|||http://purl.uniprot.org/annotation/VSP_023811|||http://purl.uniprot.org/annotation/VSP_023812|||http://purl.uniprot.org/annotation/VSP_023813|||http://purl.uniprot.org/annotation/VSP_023814|||http://purl.uniprot.org/annotation/VSP_023815|||http://purl.uniprot.org/annotation/VSP_023816 http://togogenome.org/gene/10090:Fst ^@ http://purl.uniprot.org/uniprot/P47931|||http://purl.uniprot.org/uniprot/Q8BNY0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ Acidic residues|||Disordered|||Follistatin|||Follistatin-like 1|||Follistatin-like 2|||Follistatin-like 3|||In isoform 2.|||Kazal-like|||Kazal-like 1|||Kazal-like 2|||Kazal-like 3|||N-linked (GlcNAc...) asparagine|||TB ^@ http://purl.uniprot.org/annotation/PRO_0000010104|||http://purl.uniprot.org/annotation/PRO_5015099045|||http://purl.uniprot.org/annotation/VSP_060082 http://togogenome.org/gene/10090:Samd15 ^@ http://purl.uniprot.org/uniprot/F6XZJ7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||SAM|||Sterile alpha motif domain-containing protein 15 ^@ http://purl.uniprot.org/annotation/PRO_0000416123 http://togogenome.org/gene/10090:Olfm3 ^@ http://purl.uniprot.org/uniprot/P63056|||http://purl.uniprot.org/uniprot/Q3UVC5 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Noelin-3|||Olfactomedin-like ^@ http://purl.uniprot.org/annotation/PRO_0000020081|||http://purl.uniprot.org/annotation/PRO_5014309193|||http://purl.uniprot.org/annotation/VSP_007747 http://togogenome.org/gene/10090:Cd209c ^@ http://purl.uniprot.org/uniprot/Q91ZW9 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site ^@ C-type lectin|||CD209 antigen-like protein C|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046606 http://togogenome.org/gene/10090:Psg17 ^@ http://purl.uniprot.org/uniprot/Q62056 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Slc38a5 ^@ http://purl.uniprot.org/uniprot/Q3U1J0 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Involved in pH-sensing to the transport activity regulation|||N-linked (GlcNAc...) asparagine|||Sodium-coupled neutral amino acid transporter 5 ^@ http://purl.uniprot.org/annotation/PRO_0000312116|||http://purl.uniprot.org/annotation/VSP_029703 http://togogenome.org/gene/10090:Tnfaip2 ^@ http://purl.uniprot.org/uniprot/Q61333 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Polar residues|||Tumor necrosis factor alpha-induced protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000118933 http://togogenome.org/gene/10090:Wdr7 ^@ http://purl.uniprot.org/uniprot/Q920I9 ^@ 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.|||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_0000051354|||http://purl.uniprot.org/annotation/VSP_015275 http://togogenome.org/gene/10090:Ctif ^@ http://purl.uniprot.org/uniprot/E9Q1U6|||http://purl.uniprot.org/uniprot/Q6PEE2 ^@ 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|||CBP80/20-dependent translation initiation factor|||Disordered|||In isoform 2.|||Interaction with NCBP1/CBP80|||MIF4G|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000050755|||http://purl.uniprot.org/annotation/VSP_038120 http://togogenome.org/gene/10090:Agtpbp1 ^@ http://purl.uniprot.org/uniprot/Q641K1 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Abolishes ability to rescue Purkinje cell degeneration in pcd mice when expressed in a transgene.|||Abolishes deglutamylase activity; when associated with Q-915.|||Abolishes deglutamylase activity; when associated with S-912.|||Basic and acidic residues|||Cytosolic carboxypeptidase 1|||Decreased tubulin deglutamylation.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In pcd; pcd(5J) mutant.|||Nucleophile|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000308691|||http://purl.uniprot.org/annotation/VSP_029045|||http://purl.uniprot.org/annotation/VSP_029046|||http://purl.uniprot.org/annotation/VSP_029047|||http://purl.uniprot.org/annotation/VSP_029048|||http://purl.uniprot.org/annotation/VSP_038803|||http://purl.uniprot.org/annotation/VSP_038804|||http://purl.uniprot.org/annotation/VSP_038805 http://togogenome.org/gene/10090:Slc52a3 ^@ http://purl.uniprot.org/uniprot/Q9D6X5 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier family 52, riboflavin transporter, member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000042637|||http://purl.uniprot.org/annotation/VSP_003816|||http://purl.uniprot.org/annotation/VSP_003817 http://togogenome.org/gene/10090:Pick1 ^@ http://purl.uniprot.org/uniprot/E9PUZ5|||http://purl.uniprot.org/uniprot/Q8C1W2 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ AH|||Disordered|||Galectin|||PDZ ^@ http://togogenome.org/gene/10090:H2bw2 ^@ http://purl.uniprot.org/uniprot/Q9DAB5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Histone H2A/H2B/H3 ^@ http://togogenome.org/gene/10090:Or4a75 ^@ http://purl.uniprot.org/uniprot/A0A1L1SSZ5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cys1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J216|||http://purl.uniprot.org/uniprot/Q8R4T1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Ciliary targeting motif|||Cystin-1|||Disordered|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000261178 http://togogenome.org/gene/10090:Wap ^@ http://purl.uniprot.org/uniprot/Q7M748 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ WAP ^@ http://purl.uniprot.org/annotation/PRO_5015098831 http://togogenome.org/gene/10090:Dync1i2 ^@ http://purl.uniprot.org/uniprot/A2BFF5|||http://purl.uniprot.org/uniprot/A2BFF7|||http://purl.uniprot.org/uniprot/A2BFF8|||http://purl.uniprot.org/uniprot/A2BFF9|||http://purl.uniprot.org/uniprot/D6Q0F5|||http://purl.uniprot.org/uniprot/D6Q0F6|||http://purl.uniprot.org/uniprot/D6Q0F7|||http://purl.uniprot.org/uniprot/O88487|||http://purl.uniprot.org/uniprot/Q3TPJ8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat ^@ Abolished both phosphorylation and pyrophosphorylation.|||Basic and acidic residues|||Cytoplasmic dynein 1 intermediate chain 2|||Diphosphoserine|||Disordered|||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_0000114656 http://togogenome.org/gene/10090:B9d2 ^@ http://purl.uniprot.org/uniprot/Q3UK10 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ B9 domain-containing protein 2|||C2 B9-type ^@ http://purl.uniprot.org/annotation/PRO_0000307675 http://togogenome.org/gene/10090:Ldlrad3 ^@ http://purl.uniprot.org/uniprot/A2AR95|||http://purl.uniprot.org/uniprot/B2RR20|||http://purl.uniprot.org/uniprot/B7ZND2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Involved in ITCH interaction|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||Low-density lipoprotein receptor class A domain-containing protein 3|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000299379|||http://purl.uniprot.org/annotation/PRO_5002867203|||http://purl.uniprot.org/annotation/PRO_5015087143|||http://purl.uniprot.org/annotation/VSP_027619|||http://purl.uniprot.org/annotation/VSP_027620 http://togogenome.org/gene/10090:Tas2r125 ^@ http://purl.uniprot.org/uniprot/Q7M710 ^@ 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 125 ^@ http://purl.uniprot.org/annotation/PRO_0000248483 http://togogenome.org/gene/10090:Npffr1 ^@ http://purl.uniprot.org/uniprot/E9Q468 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Col8a2 ^@ http://purl.uniprot.org/uniprot/P25318 ^@ 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 ^@ C1q|||Collagen alpha-2(VIII) chain|||Disordered|||In isoform 2.|||Nonhelical region (NC1)|||Nonhelical region (NC2)|||Pro residues|||Triple-helical region (COL1) ^@ http://purl.uniprot.org/annotation/PRO_0000005836|||http://purl.uniprot.org/annotation/VSP_014975 http://togogenome.org/gene/10090:Ifitm1 ^@ http://purl.uniprot.org/uniprot/Q9D103 ^@ Chain|||Experimental Information|||INTRAMEM|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Lipid Binding|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Interferon-induced transmembrane protein 1|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000398565 http://togogenome.org/gene/10090:Ctnna1 ^@ http://purl.uniprot.org/uniprot/P26231|||http://purl.uniprot.org/uniprot/Q545R0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Catenin alpha-1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with JUP and CTNNB1|||Interaction with alpha-actinin|||Involved in homodimerization|||Mice bearing this mutation exhibit several retinal pigment epithelium (RPE) anomalies, including pigmentary abnormalities, focal thickening, elevated lesions, and decreased light-activated responses. Mutant animals show dysmorphology in the form of RPE cell shedding and accumulation of large multinucleated RPE cells.|||N-acetylthreonine|||No effect on cell aggregation or E-cadherin/catenin complex assembly. Decreases strength of cell-cell adhesion.|||No effect on cell aggregation or E-cadherin/catenin complex assembly. Increases strength of cell-cell adhesion.|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000064262 http://togogenome.org/gene/10090:Hk2 ^@ http://purl.uniprot.org/uniprot/O08528 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Hexokinase 1|||Hexokinase 2|||Hexokinase large subdomain 1|||Hexokinase large subdomain 2|||Hexokinase small subdomain 1|||Hexokinase small subdomain 2|||Hexokinase-2|||Mitochondrial-binding peptide (MBP)|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000197588 http://togogenome.org/gene/10090:Bank1 ^@ http://purl.uniprot.org/uniprot/B0F3S4|||http://purl.uniprot.org/uniprot/Q80VH0 ^@ 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|||Acidic residues|||B-cell scaffold protein with ankyrin repeats|||Basic and acidic residues|||DBB|||Disordered|||Interaction with ITPR2|||Phosphotyrosine|||TIR ^@ http://purl.uniprot.org/annotation/PRO_0000251928 http://togogenome.org/gene/10090:Uimc1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J073|||http://purl.uniprot.org/uniprot/A0A0R4J183|||http://purl.uniprot.org/uniprot/Q5U5Q9 ^@ 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|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ AIR|||BRCA1-A complex subunit RAP80|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||LR motif|||Necessary for interaction with NR6A1 C-terminus|||Necessary for interaction with NR6A1 N-terminus|||Necessary for transcriptional repression|||Phosphoserine|||Phosphothreonine|||Polar residues|||UBZ4-type|||UIM 1|||UIM 2|||UIM-linker|||Zinc-finger-like region ^@ http://purl.uniprot.org/annotation/PRO_0000097548|||http://purl.uniprot.org/annotation/VSP_037266|||http://purl.uniprot.org/annotation/VSP_037267|||http://purl.uniprot.org/annotation/VSP_037268 http://togogenome.org/gene/10090:0610030E20Rik ^@ http://purl.uniprot.org/uniprot/Q149G0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||UPF0561 protein C2orf68 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000328786 http://togogenome.org/gene/10090:Il9 ^@ http://purl.uniprot.org/uniprot/P15247 ^@ Chain|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand ^@ Chain|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Strand ^@ Interleukin-9|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000015628 http://togogenome.org/gene/10090:Galnt18 ^@ http://purl.uniprot.org/uniprot/Q8K1B9 ^@ 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 ^@ Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 18|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059142 http://togogenome.org/gene/10090:Cdc42ep4 ^@ http://purl.uniprot.org/uniprot/Q9JM96 ^@ 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 4|||Disordered|||N6-methyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000212656 http://togogenome.org/gene/10090:Cldn16 ^@ http://purl.uniprot.org/uniprot/Q14BW2|||http://purl.uniprot.org/uniprot/Q925N4 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Claudin-16|||Cytoplasmic|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000144775 http://togogenome.org/gene/10090:Tmub2 ^@ http://purl.uniprot.org/uniprot/Q3V209 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Transmembrane and ubiquitin-like domain-containing protein 2|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000245313|||http://purl.uniprot.org/annotation/VSP_019705 http://togogenome.org/gene/10090:Rps5 ^@ http://purl.uniprot.org/uniprot/P97461 ^@ 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); alternate|||N-acetylmethionine|||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_0000124527|||http://purl.uniprot.org/annotation/PRO_0000370370 http://togogenome.org/gene/10090:Rbm22 ^@ http://purl.uniprot.org/uniprot/Q8BHS3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C3H1-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Pre-mRNA-splicing factor RBM22|||Pro residues|||RRM|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000250548 http://togogenome.org/gene/10090:Cetn2 ^@ http://purl.uniprot.org/uniprot/Q9R1K9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 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_0000073562 http://togogenome.org/gene/10090:Fastkd2 ^@ http://purl.uniprot.org/uniprot/Q922E6 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ FAST kinase domain-containing protein 2, mitochondrial|||Mitochondrion|||Phosphoserine|||RAP ^@ http://purl.uniprot.org/annotation/PRO_0000050784 http://togogenome.org/gene/10090:Serpina1b ^@ http://purl.uniprot.org/uniprot/P22599 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Alpha-1-antitrypsin 1-2|||N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000032389 http://togogenome.org/gene/10090:Cramp1 ^@ http://purl.uniprot.org/uniprot/Q6PG95 ^@ 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_0000264472 http://togogenome.org/gene/10090:Cd3g ^@ http://purl.uniprot.org/uniprot/P11942|||http://purl.uniprot.org/uniprot/Q3U4Y3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||ITAM|||Ig-like|||Immunoglobulin subtype 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||T-cell surface glycoprotein CD3 gamma chain ^@ http://purl.uniprot.org/annotation/PRO_0000014617|||http://purl.uniprot.org/annotation/PRO_5014309138 http://togogenome.org/gene/10090:Thumpd2 ^@ http://purl.uniprot.org/uniprot/Q9CZB3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||THUMP|||THUMP domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000072533 http://togogenome.org/gene/10090:Eya3 ^@ http://purl.uniprot.org/uniprot/P97480|||http://purl.uniprot.org/uniprot/Q3TP96|||http://purl.uniprot.org/uniprot/Q6P4T3 ^@ 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 ^@ Abolishes phosphatase activity and abolishes coactivation of the SIX1-DACH1 complex.|||Abolishes phosphatase activity.|||Basic and acidic residues|||Diminishes phosphatase activity by 24-fold.|||Diminishes phosphatase activity by 70%.|||Diminishes phosphatase activity.|||Disordered|||Eyes absent homolog 3|||In isoform 2.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000218649|||http://purl.uniprot.org/annotation/VSP_001494 http://togogenome.org/gene/10090:Gimap3 ^@ http://purl.uniprot.org/uniprot/Q99MI6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ AIG1-type G|||Cytoplasmic|||GTPase IMAP family member 3|||Helical; Anchor for type IV membrane protein|||Lumenal|||Required for targeting to the endoplasmic reticulum ^@ http://purl.uniprot.org/annotation/PRO_0000190994 http://togogenome.org/gene/10090:Ago2 ^@ http://purl.uniprot.org/uniprot/Q8CJG0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 3'-nitrotyrosine|||4-hydroxyproline|||Interaction with GW182 family members|||Interaction with guide RNA|||PAZ|||Phosphoserine|||Piwi|||Protein argonaute-2 ^@ http://purl.uniprot.org/annotation/PRO_0000194058 http://togogenome.org/gene/10090:Pik3r6 ^@ http://purl.uniprot.org/uniprot/Q3U6Q4 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||Phosphoinositide 3-kinase regulatory subunit 6 ^@ http://purl.uniprot.org/annotation/PRO_0000234339|||http://purl.uniprot.org/annotation/VSP_018255|||http://purl.uniprot.org/annotation/VSP_018256|||http://purl.uniprot.org/annotation/VSP_018257 http://togogenome.org/gene/10090:Gng11 ^@ http://purl.uniprot.org/uniprot/P61953 ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Propeptide|||Region ^@ Basic and acidic residues|||Cysteine methyl ester|||Disordered|||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_0000012661|||http://purl.uniprot.org/annotation/PRO_0000012662 http://togogenome.org/gene/10090:Lsm7 ^@ http://purl.uniprot.org/uniprot/Q9CQQ8 ^@ 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_0000125580 http://togogenome.org/gene/10090:Or2n1d ^@ http://purl.uniprot.org/uniprot/Q8VG72 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or4c121 ^@ http://purl.uniprot.org/uniprot/Q8VGM5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dpp6 ^@ http://purl.uniprot.org/uniprot/E9PWX1|||http://purl.uniprot.org/uniprot/Q3TY19|||http://purl.uniprot.org/uniprot/Q5U4C2|||http://purl.uniprot.org/uniprot/Q80VM5|||http://purl.uniprot.org/uniprot/Q9Z218 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dipeptidyl aminopeptidase-like protein 6|||Dipeptidylpeptidase IV N-terminal|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Peptidase S9 prolyl oligopeptidase catalytic|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000122410 http://togogenome.org/gene/10090:Zkscan17 ^@ http://purl.uniprot.org/uniprot/Q5SXI5 ^@ Chain|||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|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||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.|||In isoform 3.|||KRAB|||Nuclear localization signal|||Phosphoserine|||SCAN box|||Zinc finger protein 496 ^@ http://purl.uniprot.org/annotation/PRO_0000391906|||http://purl.uniprot.org/annotation/VSP_038768|||http://purl.uniprot.org/annotation/VSP_038769 http://togogenome.org/gene/10090:Klk1b11 ^@ http://purl.uniprot.org/uniprot/A0A1R3UDS6|||http://purl.uniprot.org/uniprot/P15946 ^@ 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|||Kallikrein 1-related peptidase b11|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027981|||http://purl.uniprot.org/annotation/PRO_0000027982|||http://purl.uniprot.org/annotation/PRO_5010196199 http://togogenome.org/gene/10090:Atp6ap1l ^@ http://purl.uniprot.org/uniprot/D3Z5W0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||V-type proton ATPase subunit S1 luminal|||V-type proton ATPase subunit S1/VOA1 transmembrane ^@ http://purl.uniprot.org/annotation/PRO_5003052434 http://togogenome.org/gene/10090:Serpinb6b ^@ http://purl.uniprot.org/uniprot/O08804 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Mrpl53 ^@ http://purl.uniprot.org/uniprot/Q9D1H8 ^@ Chain|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Region|||Transit Peptide ^@ Disordered|||Large ribosomal subunit protein mL53|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000261665 http://togogenome.org/gene/10090:Man2b2 ^@ http://purl.uniprot.org/uniprot/O54782 ^@ 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 ^@ Epididymis-specific alpha-mannosidase|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000012078 http://togogenome.org/gene/10090:Kidins220 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VME9|||http://purl.uniprot.org/uniprot/E9Q9B7 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Transmembrane ^@ ANK|||Basic and acidic residues|||Disordered|||Helical|||KAP NTPase|||Polar residues ^@ http://togogenome.org/gene/10090:Tfap2e ^@ http://purl.uniprot.org/uniprot/Q6VUP9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ H-S-H (helix-span-helix), dimerization|||PPxY motif|||Phosphoserine; by PKA|||Transcription factor AP-2-epsilon ^@ http://purl.uniprot.org/annotation/PRO_0000309517 http://togogenome.org/gene/10090:Vrk3 ^@ http://purl.uniprot.org/uniprot/Q3TAR6|||http://purl.uniprot.org/uniprot/Q8K3G5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Inactive serine/threonine-protein kinase VRK3|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000086809 http://togogenome.org/gene/10090:Smok3c ^@ http://purl.uniprot.org/uniprot/A0A087WSF2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Protein kinase ^@ http://togogenome.org/gene/10090:Irak4 ^@ http://purl.uniprot.org/uniprot/Q8R4K2 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ Death|||Disordered|||Interleukin-1 receptor-associated kinase 4|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086036 http://togogenome.org/gene/10090:Trp53inp2 ^@ http://purl.uniprot.org/uniprot/Q8CFU8 ^@ 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|||In isoform 2.|||LIR|||Phosphoserine|||Pro residues|||Tumor protein p53-inducible nuclear protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000072410|||http://purl.uniprot.org/annotation/VSP_007752 http://togogenome.org/gene/10090:Selenok ^@ http://purl.uniprot.org/uniprot/Q9JLJ1 ^@ Chain|||Modification|||Molecule Processing|||Non standard residue|||Region|||Site|||Transmembrane ^@ Chain|||Non standard residue|||Region|||Site|||Transmembrane ^@ Cleavage; by CAPN2|||Disordered|||Helical|||Selenocysteine|||Selenoprotein K ^@ http://purl.uniprot.org/annotation/PRO_0000097670 http://togogenome.org/gene/10090:Cxcl13 ^@ http://purl.uniprot.org/uniprot/O55038|||http://purl.uniprot.org/uniprot/Q3U1E8 ^@ 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 ^@ C-X-C motif chemokine|||C-X-C motif chemokine 13|||Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_0000005114|||http://purl.uniprot.org/annotation/PRO_5014205828 http://togogenome.org/gene/10090:Gm3500 ^@ http://purl.uniprot.org/uniprot/A6NAS7 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rsph4a ^@ http://purl.uniprot.org/uniprot/Q8BYM7 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Radial spoke head protein 4 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000313739 http://togogenome.org/gene/10090:Nup210l ^@ http://purl.uniprot.org/uniprot/Q9D2F7 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ BIG2|||Helical|||N-linked (GlcNAc...) asparagine|||Nuclear pore membrane glycoprotein 210-like ^@ http://purl.uniprot.org/annotation/PRO_0000236049 http://togogenome.org/gene/10090:Numbl ^@ http://purl.uniprot.org/uniprot/O08919|||http://purl.uniprot.org/uniprot/Q3UH86 ^@ 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|||Numb-like protein|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000058000 http://togogenome.org/gene/10090:Eef1ece2 ^@ http://purl.uniprot.org/uniprot/P0DPD9|||http://purl.uniprot.org/uniprot/P0DPE0|||http://purl.uniprot.org/uniprot/Q80Z57 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EEF1A lysine methyltransferase 4|||EEF1AKMT4-ECE2 readthrough transcript protein|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform Eef1akmt4-Ece2-2.|||Lumenal|||Methyltransferase-like region|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Peptidase M13 C-terminal|||Peptidase M13 N-terminal|||Phosphoserine|||Phosphotyrosine|||Proton donor|||Required for methyltransferase activity ^@ http://purl.uniprot.org/annotation/PRO_0000310760|||http://purl.uniprot.org/annotation/PRO_0000443291|||http://purl.uniprot.org/annotation/VSP_029335 http://togogenome.org/gene/10090:Hspa12a ^@ http://purl.uniprot.org/uniprot/Q8K0U4 ^@ 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 ^@ Disordered|||Heat shock 70 kDa protein 12A|||N-acetylalanine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000078293 http://togogenome.org/gene/10090:Adam5 ^@ http://purl.uniprot.org/uniprot/Q3TTE0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 5|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Peptidase M12B|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000349300|||http://purl.uniprot.org/annotation/PRO_0000349301|||http://purl.uniprot.org/annotation/VSP_035334|||http://purl.uniprot.org/annotation/VSP_035335|||http://purl.uniprot.org/annotation/VSP_035336|||http://purl.uniprot.org/annotation/VSP_035337|||http://purl.uniprot.org/annotation/VSP_035338 http://togogenome.org/gene/10090:Ubd ^@ http://purl.uniprot.org/uniprot/P63072 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Chain|||Domain Extent|||Mutagenesis Site|||Site ^@ Activation by thioester intermediate formation with UBA6|||Impaired conjugation of target proteins.|||Ubiquitin D|||Ubiquitin-like 1|||Ubiquitin-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000114894 http://togogenome.org/gene/10090:Lrrc47 ^@ http://purl.uniprot.org/uniprot/B1AX98|||http://purl.uniprot.org/uniprot/Q505F5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ B3/B4 tRNA-binding|||Basic and acidic residues|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Leucine-rich repeat-containing protein 47|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000223927 http://togogenome.org/gene/10090:Akr1d1 ^@ http://purl.uniprot.org/uniprot/Q8VCX1 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ Aldo-keto reductase family 1 member D1|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000124670 http://togogenome.org/gene/10090:Acta2 ^@ http://purl.uniprot.org/uniprot/P62737 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Actin, aortic smooth muscle|||Actin, aortic smooth muscle, intermediate form|||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_0000442605|||http://purl.uniprot.org/annotation/PRO_0000442606 http://togogenome.org/gene/10090:Slc2a9 ^@ http://purl.uniprot.org/uniprot/Q3T9X0 ^@ 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 ^@ Cytoplasmic|||Decreased N-glycosylation.|||Disordered|||Extracellular|||Helical; Name=1|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Solute carrier family 2, facilitated glucose transporter member 9 ^@ http://purl.uniprot.org/annotation/PRO_0000447626|||http://purl.uniprot.org/annotation/VSP_060215|||http://purl.uniprot.org/annotation/VSP_060216 http://togogenome.org/gene/10090:Pfdn4 ^@ http://purl.uniprot.org/uniprot/E9Q6U4|||http://purl.uniprot.org/uniprot/Q3UWL8|||http://purl.uniprot.org/uniprot/Q6P0X1 ^@ Coiled-Coil|||Region ^@ Coiled-Coil ^@ ^@ http://togogenome.org/gene/10090:Naprt ^@ http://purl.uniprot.org/uniprot/Q8CC86 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Nicotinate phosphoribosyltransferase|||Phosphohistidine ^@ http://purl.uniprot.org/annotation/PRO_0000315682 http://togogenome.org/gene/10090:Insm2 ^@ http://purl.uniprot.org/uniprot/Q9JMC2 ^@ 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; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Insulinoma-associated protein 2|||Pro residues|||SNAG domain ^@ http://purl.uniprot.org/annotation/PRO_0000331577 http://togogenome.org/gene/10090:Fubp1 ^@ http://purl.uniprot.org/uniprot/Q3TUE1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||K Homology|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Or2ag16 ^@ http://purl.uniprot.org/uniprot/Q7TRN4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ubr2 ^@ http://purl.uniprot.org/uniprot/Q3UPU3|||http://purl.uniprot.org/uniprot/Q6WKZ8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase UBR2|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylalanine|||RING-type; atypical|||Removed|||UBR-type ^@ http://purl.uniprot.org/annotation/PRO_0000056141|||http://purl.uniprot.org/annotation/VSP_015172|||http://purl.uniprot.org/annotation/VSP_015173 http://togogenome.org/gene/10090:Serp1 ^@ http://purl.uniprot.org/uniprot/Q9Z1W5 ^@ 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_0000274795 http://togogenome.org/gene/10090:Phc2 ^@ http://purl.uniprot.org/uniprot/Q9QWH1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||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|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||FCS-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HD1|||In isoform 2.|||Interaction with BMI1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Polyhomeotic-like protein 2|||Pro residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000076287|||http://purl.uniprot.org/annotation/VSP_016919 http://togogenome.org/gene/10090:Eif2s3y ^@ http://purl.uniprot.org/uniprot/Q9Z0N2 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Eukaryotic translation initiation factor 2 subunit 3, Y-linked|||G1|||G2|||G3|||G4|||G5|||N-acetylalanine|||Phosphoserine|||Removed|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000137440 http://togogenome.org/gene/10090:Cyc1 ^@ http://purl.uniprot.org/uniprot/Q9D0M3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn ^@ Cytochrome c|||Cytochrome c1, heme protein, mitochondrial|||Helical|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000006555|||http://purl.uniprot.org/annotation/VSP_025056 http://togogenome.org/gene/10090:Lrcol1 ^@ http://purl.uniprot.org/uniprot/Q3URS3 ^@ Chain|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Leucine-rich colipase-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000346759|||http://purl.uniprot.org/annotation/VSP_044127 http://togogenome.org/gene/10090:Or2r3 ^@ http://purl.uniprot.org/uniprot/Q8VGP5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mlip ^@ http://purl.uniprot.org/uniprot/Q5FW52 ^@ 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 1 and isoform 2.|||In isoform 1, isoform 2 and isoform 4.|||In isoform 1.|||In isoform 2 and isoform 4.|||In isoform 4.|||Muscular LMNA-interacting protein|||Phosphoserine|||Polar residues|||Required for interaction with ISL1 ^@ http://purl.uniprot.org/annotation/PRO_0000089539|||http://purl.uniprot.org/annotation/VSP_061858|||http://purl.uniprot.org/annotation/VSP_061859|||http://purl.uniprot.org/annotation/VSP_061860|||http://purl.uniprot.org/annotation/VSP_061861|||http://purl.uniprot.org/annotation/VSP_061862|||http://purl.uniprot.org/annotation/VSP_061863 http://togogenome.org/gene/10090:Tbx4 ^@ http://purl.uniprot.org/uniprot/P70325|||http://purl.uniprot.org/uniprot/Q8BSY3 ^@ 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|||Phosphoserine|||Polar residues|||T-box|||T-box transcription factor TBX4 ^@ http://purl.uniprot.org/annotation/PRO_0000184434 http://togogenome.org/gene/10090:Nudt16l2 ^@ http://purl.uniprot.org/uniprot/E9Q9G1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Nudix hydrolase ^@ http://togogenome.org/gene/10090:Aup1 ^@ http://purl.uniprot.org/uniprot/I6L970|||http://purl.uniprot.org/uniprot/P70295|||http://purl.uniprot.org/uniprot/Q3TBX5|||http://purl.uniprot.org/uniprot/Q3U3K9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ CUE|||Cytoplasmic|||Disordered|||Helical|||Lipid droplet-regulating VLDL assembly factor AUP1|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000020766 http://togogenome.org/gene/10090:Pspc1 ^@ http://purl.uniprot.org/uniprot/Q8R326 ^@ 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 ^@ Abolishes RNA-binding activity but not AR-mediated transcription coactivation; when associated with A-118; A-120 and A-197.|||Abolishes RNA-binding activity but not AR-mediated transcription coactivation; when associated with A-118; A-120 and A-199.|||Abolishes RNA-binding activity but not AR-mediated transcription coactivation; when associated with A-118; A-197 and A-199.|||Abolishes RNA-binding activity but not AR-mediated transcription coactivation; when associated with A-120; A-197 and A-199.|||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_0000297541|||http://purl.uniprot.org/annotation/VSP_027276|||http://purl.uniprot.org/annotation/VSP_027277 http://togogenome.org/gene/10090:Wdr43 ^@ http://purl.uniprot.org/uniprot/Q6ZQL4 ^@ 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_0000051393 http://togogenome.org/gene/10090:Mrps12 ^@ http://purl.uniprot.org/uniprot/O35680 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||Small ribosomal subunit protein uS12m ^@ http://purl.uniprot.org/annotation/PRO_0000030607 http://togogenome.org/gene/10090:Ppp1r15b ^@ http://purl.uniprot.org/uniprot/Q8BFW3 ^@ 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|||Disordered|||In isoform 2.|||Phosphoserine|||Protein phosphatase 1 regulatory subunit 15B ^@ http://purl.uniprot.org/annotation/PRO_0000320521|||http://purl.uniprot.org/annotation/VSP_031652 http://togogenome.org/gene/10090:Zbtb41 ^@ http://purl.uniprot.org/uniprot/Q811F1 ^@ 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 ^@ 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|||Zinc finger and BTB domain-containing protein 41 ^@ http://purl.uniprot.org/annotation/PRO_0000277815 http://togogenome.org/gene/10090:Angptl8 ^@ http://purl.uniprot.org/uniprot/A0A0A0R784|||http://purl.uniprot.org/uniprot/Q80WX2|||http://purl.uniprot.org/uniprot/Q8R1L8 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide ^@ Chain|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide ^@ Angiopoietin-like protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000319618|||http://purl.uniprot.org/annotation/PRO_5013175618 http://togogenome.org/gene/10090:Sqstm1 ^@ http://purl.uniprot.org/uniprot/Q64337 ^@ 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|||Site|||Splice Variant|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Turn|||Zinc Finger ^@ Abolished oligomerization without affecting interaction with KEAP1; when associated with A-69.|||Abolished oligomerization without affecting interaction with KEAP1; when associated with A-7.|||Abolishes interaction with KEAP1.|||Disordered|||Does not affect interaction with KEAP1. Decreased phosphorylation by MTOR.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Greatly decreases interaction with MAP1LC3B.|||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|||LIR|||MAP1LC3B-binding|||N-acetylalanine|||PB1|||Phosphomimetic mutant; promotes interaction with KEAP1 and nuclear accumulation of NFE2L2/NRF2.|||Phosphoserine|||Phosphoserine; by MTOR|||Phosphoserine; by ULK1 and TBK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Sequestosome-1|||Strongly decreased interaction with KEAP1.|||TRAF6-binding|||UBA|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000072177|||http://purl.uniprot.org/annotation/VSP_015842 http://togogenome.org/gene/10090:Ccser2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J2A7|||http://purl.uniprot.org/uniprot/Q3UHI0|||http://purl.uniprot.org/uniprot/S4R211 ^@ 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.|||Phosphoserine|||Polar residues|||Serine-rich coiled-coil domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000309462|||http://purl.uniprot.org/annotation/VSP_029183 http://togogenome.org/gene/10090:Prh1 ^@ http://purl.uniprot.org/uniprot/D3Z1V5 ^@ 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_5015088515 http://togogenome.org/gene/10090:Lrrc34 ^@ http://purl.uniprot.org/uniprot/Q9DAM1 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ LRR 1|||LRR 2|||Leucine-rich repeat-containing protein 34 ^@ http://purl.uniprot.org/annotation/PRO_0000228670 http://togogenome.org/gene/10090:Gpr89 ^@ http://purl.uniprot.org/uniprot/Q8BS95 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Transmembrane ^@ Golgi pH regulator|||Helical|||In explorer; no obvious external deformities but mutants are 40% smaller than wild-type litter mates and show reduced frequency of CD3+ T cells, CD4+ T cells and CD8+ T cells which all display elevated CD44 expression.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000223261 http://togogenome.org/gene/10090:Ift43 ^@ http://purl.uniprot.org/uniprot/Q9DA69 ^@ 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.|||Intraflagellar transport protein 43 homolog|||N-acetylmethionine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000254042|||http://purl.uniprot.org/annotation/VSP_021170|||http://purl.uniprot.org/annotation/VSP_021171 http://togogenome.org/gene/10090:Etv5 ^@ http://purl.uniprot.org/uniprot/Q9CXC9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||ETS|||ETS translocation variant 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204119 http://togogenome.org/gene/10090:Plscr5 ^@ http://purl.uniprot.org/uniprot/J3QM92 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Scyl1 ^@ http://purl.uniprot.org/uniprot/Q9EQC5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Decreased interaction with COPB1.|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||Interaction with COPB1|||N-terminal kinase-like protein|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000249542 http://togogenome.org/gene/10090:Pip4k2b ^@ http://purl.uniprot.org/uniprot/Q3UJ95|||http://purl.uniprot.org/uniprot/Q80XI4 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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_0000185471 http://togogenome.org/gene/10090:Or51a7 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFH3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Plp2 ^@ http://purl.uniprot.org/uniprot/Q0VEW4|||http://purl.uniprot.org/uniprot/Q9R1Q7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Transmembrane ^@ Helical|||MARVEL|||Proteolipid protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000156820 http://togogenome.org/gene/10090:Or52n4 ^@ http://purl.uniprot.org/uniprot/Q8VGV5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gpr119 ^@ http://purl.uniprot.org/uniprot/Q7TQP3 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ 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_0000069608 http://togogenome.org/gene/10090:Ints6l ^@ http://purl.uniprot.org/uniprot/Q8BND4 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Integrator complex subunit 6-like|||Phosphoserine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000076216 http://togogenome.org/gene/10090:Fam131a ^@ http://purl.uniprot.org/uniprot/D3Z4E4|||http://purl.uniprot.org/uniprot/Q8BWU3 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Protein FAM131A ^@ http://purl.uniprot.org/annotation/PRO_0000243933 http://togogenome.org/gene/10090:Tdpoz7 ^@ http://purl.uniprot.org/uniprot/E0CYU8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB|||MATH ^@ http://togogenome.org/gene/10090:Lca5l ^@ http://purl.uniprot.org/uniprot/A0A5H1ZRL0|||http://purl.uniprot.org/uniprot/Q8C0X0 ^@ 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.|||Lebercilin|||Lebercilin-like protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000331229|||http://purl.uniprot.org/annotation/VSP_059567 http://togogenome.org/gene/10090:Or10q1 ^@ http://purl.uniprot.org/uniprot/Q8VGP8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rarres1 ^@ http://purl.uniprot.org/uniprot/F6ZIS7|||http://purl.uniprot.org/uniprot/Q8BVL6 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Non-terminal Residue|||Region|||Signal Peptide ^@ Disordered ^@ http://purl.uniprot.org/annotation/PRO_5003352400 http://togogenome.org/gene/10090:Xkr6 ^@ http://purl.uniprot.org/uniprot/E9Q6C8 ^@ 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.|||In isoform 3.|||Pro residues|||XK-related protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000415853|||http://purl.uniprot.org/annotation/VSP_042406|||http://purl.uniprot.org/annotation/VSP_042407 http://togogenome.org/gene/10090:Polr2e ^@ http://purl.uniprot.org/uniprot/Q3V214|||http://purl.uniprot.org/uniprot/Q80UW8 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue ^@ 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_0000146076 http://togogenome.org/gene/10090:Best1 ^@ http://purl.uniprot.org/uniprot/O88870 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Bestrophin-1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000143116 http://togogenome.org/gene/10090:Smim8 ^@ http://purl.uniprot.org/uniprot/Q9CQQ0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Small integral membrane protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000089551 http://togogenome.org/gene/10090:Pcdhgb7 ^@ http://purl.uniprot.org/uniprot/Q91XX3 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (Man...) threonine ^@ http://purl.uniprot.org/annotation/PRO_5015099492 http://togogenome.org/gene/10090:Adcy8 ^@ http://purl.uniprot.org/uniprot/A0A2I3BQ46|||http://purl.uniprot.org/uniprot/P97490|||http://purl.uniprot.org/uniprot/Q3UUN2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||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|||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_0000195706 http://togogenome.org/gene/10090:Ubxn2a ^@ http://purl.uniprot.org/uniprot/Q99KJ0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||SEP|||UBX|||UBX domain-containing protein 2A ^@ http://purl.uniprot.org/annotation/PRO_0000211032 http://togogenome.org/gene/10090:Pgm5 ^@ http://purl.uniprot.org/uniprot/Q8BZF8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Phosphoglucomutase-like protein 5|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000294064 http://togogenome.org/gene/10090:Glra1 ^@ http://purl.uniprot.org/uniprot/Q5NCT9|||http://purl.uniprot.org/uniprot/Q64018 ^@ 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|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Eliminates potentiation of glycine-mediated currents by Zn(2+) and causes neuromotor defects similar to human startle disease.|||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 isoform b.|||In spd.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Reduces the increase of channel activity in response to ethanol and improves tolerance of intoxicating levels of alcohol. ^@ http://purl.uniprot.org/annotation/PRO_0000000413|||http://purl.uniprot.org/annotation/PRO_5015097964|||http://purl.uniprot.org/annotation/VSP_000080 http://togogenome.org/gene/10090:Cln3 ^@ http://purl.uniprot.org/uniprot/Q61124|||http://purl.uniprot.org/uniprot/Q6PAH4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Battenin|||Cysteine methyl ester|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Lysosomal targeting motif|||Lysosomal targeting motif. Required for AP1G1, AP2A2 and AP3D1 interaction|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000089859|||http://purl.uniprot.org/annotation/PRO_0000422292 http://togogenome.org/gene/10090:Nasp ^@ http://purl.uniprot.org/uniprot/B1AU75|||http://purl.uniprot.org/uniprot/B1AU76|||http://purl.uniprot.org/uniprot/Q99MD9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||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.|||N-acetylalanine|||N6-acetyllysine|||Nuclear autoantigenic sperm protein|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||Tetratricopeptide SHNi-TPR ^@ http://purl.uniprot.org/annotation/PRO_0000261597|||http://purl.uniprot.org/annotation/VSP_052237|||http://purl.uniprot.org/annotation/VSP_052238 http://togogenome.org/gene/10090:Taar1 ^@ http://purl.uniprot.org/uniprot/Q923Y8 ^@ 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|||Trace amine-associated receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000070143 http://togogenome.org/gene/10090:Sppl2a ^@ http://purl.uniprot.org/uniprot/Q9JJF9 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Does not inhibit lysosomal/late endosomal targeting.|||Helical|||Inhibits lysosomal/late endosomal targeting.|||Lumenal|||N-linked (GlcNAc...) asparagine|||PA|||PAL|||Signal peptide peptidase-like 2A|||YXXo lysosomal targeting motif ^@ http://purl.uniprot.org/annotation/PRO_0000073911 http://togogenome.org/gene/10090:Enho ^@ http://purl.uniprot.org/uniprot/Q8C7D8|||http://purl.uniprot.org/uniprot/Q8K1D8 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Non-terminal Residue|||Region|||Signal Peptide ^@ Adropin|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000292880 http://togogenome.org/gene/10090:Or52h9 ^@ http://purl.uniprot.org/uniprot/Q8VG78 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sdhb ^@ http://purl.uniprot.org/uniprot/Q9CQA3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ 2Fe-2S ferredoxin-type|||4Fe-4S ferredoxin-type|||Interaction with SDHAF1|||Mitochondrion|||N6-acetyllysine|||Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000010356 http://togogenome.org/gene/10090:Cox6b1 ^@ http://purl.uniprot.org/uniprot/P56391 ^@ 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 ^@ CHCH|||Cx10C motif|||Cx9C motif|||Cytochrome c oxidase subunit 6B1|||N-acetylalanine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194915 http://togogenome.org/gene/10090:Rapgef3 ^@ http://purl.uniprot.org/uniprot/E9Q2E5|||http://purl.uniprot.org/uniprot/Q3TES7|||http://purl.uniprot.org/uniprot/Q3UQC2|||http://purl.uniprot.org/uniprot/Q8VCC8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Cyclic nucleotide-binding|||DEP|||Disordered|||In isoform 2.|||Interaction with PDE3B|||N-terminal Ras-GEF|||Phosphoserine|||Polar residues|||Rap guanine nucleotide exchange factor 3|||Ras-GEF ^@ http://purl.uniprot.org/annotation/PRO_0000068868|||http://purl.uniprot.org/annotation/VSP_007610 http://togogenome.org/gene/10090:Fbxl14 ^@ http://purl.uniprot.org/uniprot/Q8BID8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ 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_0000119862 http://togogenome.org/gene/10090:Vill ^@ http://purl.uniprot.org/uniprot/G5E8C6|||http://purl.uniprot.org/uniprot/G5E8H0|||http://purl.uniprot.org/uniprot/Q91YD6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant ^@ Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||Gelsolin-like 6|||HP|||In isoform 2.|||In isoform 3.|||Villin-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000218739|||http://purl.uniprot.org/annotation/VSP_051690|||http://purl.uniprot.org/annotation/VSP_051691|||http://purl.uniprot.org/annotation/VSP_051692 http://togogenome.org/gene/10090:Tubg1 ^@ http://purl.uniprot.org/uniprot/P83887|||http://purl.uniprot.org/uniprot/Q6F4J1 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site ^@ Phosphomimetic mutant that lead to increased centrosome number.|||Phosphoserine; by BRSK1|||Tubulin gamma-1 chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase|||Weak effect possibly due to low expression of this mutant. ^@ http://purl.uniprot.org/annotation/PRO_0000048466 http://togogenome.org/gene/10090:D030056L22Rik ^@ http://purl.uniprot.org/uniprot/Q3U2A5|||http://purl.uniprot.org/uniprot/Q8VCE4 ^@ 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|||Putative WW-binding|||Uncharacterized protein C9orf40 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089683 http://togogenome.org/gene/10090:F7 ^@ http://purl.uniprot.org/uniprot/P70375|||http://purl.uniprot.org/uniprot/Q542C2 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site|||Strand ^@ (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||Charge relay system|||Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin|||EGF-like|||EGF-like 1; calcium-binding|||EGF-like 2|||Factor VII heavy chain|||Factor VII light chain|||Gla|||N-linked (GlcNAc...) asparagine|||O-linked (Glc...) serine; alternate|||O-linked (Xyl...) serine; alternate|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027732|||http://purl.uniprot.org/annotation/PRO_0000027733|||http://purl.uniprot.org/annotation/PRO_0000027734|||http://purl.uniprot.org/annotation/PRO_5014309590 http://togogenome.org/gene/10090:Kdm4d ^@ http://purl.uniprot.org/uniprot/Q3U2K5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||JmjC|||JmjN|||Lysine-specific demethylase 4D|||Polar residues|||PolyADP-ribosyl glutamic acid ^@ http://purl.uniprot.org/annotation/PRO_0000234377 http://togogenome.org/gene/10090:Arhgef10l ^@ http://purl.uniprot.org/uniprot/A2AWP8 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||DH|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||Phosphoserine|||Phosphotyrosine|||Pro residues|||Rho guanine nucleotide exchange factor 10-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000342362|||http://purl.uniprot.org/annotation/VSP_034427|||http://purl.uniprot.org/annotation/VSP_034428|||http://purl.uniprot.org/annotation/VSP_034429|||http://purl.uniprot.org/annotation/VSP_034430|||http://purl.uniprot.org/annotation/VSP_034431 http://togogenome.org/gene/10090:Zfp108 ^@ http://purl.uniprot.org/uniprot/Q8CCP6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Cept1 ^@ http://purl.uniprot.org/uniprot/Q8BGS7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Site|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Choline/ethanolaminephosphotransferase 1|||Disordered|||Helical|||In isoform 2.|||Increases basicity of active site His|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000289246|||http://purl.uniprot.org/annotation/VSP_025988 http://togogenome.org/gene/10090:Msc ^@ http://purl.uniprot.org/uniprot/O88940 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region ^@ Disordered|||Loss of DNA-binding.|||Musculin|||Nuclear localization signal|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127284 http://togogenome.org/gene/10090:Srsf4 ^@ http://purl.uniprot.org/uniprot/Q542V3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||RRM ^@ http://togogenome.org/gene/10090:Shc4 ^@ http://purl.uniprot.org/uniprot/Q6S5L9|||http://purl.uniprot.org/uniprot/Q8CB26 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ CH1|||CH2|||Disordered|||PID|||Phosphotyrosine|||Polar residues|||Pro residues|||SH2|||SHC-transforming protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000337201 http://togogenome.org/gene/10090:Mapk12 ^@ http://purl.uniprot.org/uniprot/O08911 ^@ 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 ^@ Mitogen-activated protein kinase 12|||Phosphothreonine|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||TXY ^@ http://purl.uniprot.org/annotation/PRO_0000186283 http://togogenome.org/gene/10090:Or7e176 ^@ http://purl.uniprot.org/uniprot/E9PVW2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Brd7 ^@ http://purl.uniprot.org/uniprot/O88665 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Bromo|||Bromodomain-containing protein 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000227665 http://togogenome.org/gene/10090:Tmcc2 ^@ http://purl.uniprot.org/uniprot/Q3T9T1|||http://purl.uniprot.org/uniprot/Q3TZY4|||http://purl.uniprot.org/uniprot/Q80W04 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ Basic residues|||Disordered|||Helical|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Transmembrane and coiled-coil domains protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000184598 http://togogenome.org/gene/10090:Rhox4d ^@ http://purl.uniprot.org/uniprot/Q2MDG0 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Pef1 ^@ http://purl.uniprot.org/uniprot/Q8BFY6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||4|||5|||6|||7|||8|||8 X 9 AA approximate tandem repeat of [AP]-P-G-G-P-Y-G-G-P-P|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||Peflin|||Pro residues|||Required for interaction with PDCD6 ^@ http://purl.uniprot.org/annotation/PRO_0000247046 http://togogenome.org/gene/10090:Cplx1 ^@ http://purl.uniprot.org/uniprot/P63040 ^@ 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|||Complexin-1|||Disordered|||Interaction with the SNARE complex ^@ http://purl.uniprot.org/annotation/PRO_0000144871 http://togogenome.org/gene/10090:Iqsec2 ^@ http://purl.uniprot.org/uniprot/A4GZ26|||http://purl.uniprot.org/uniprot/D3Z6V7|||http://purl.uniprot.org/uniprot/E9QAD8|||http://purl.uniprot.org/uniprot/Q5DU25 ^@ 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|||Basic residues|||Disordered|||IQ|||IQ motif and SEC7 domain-containing protein 2|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000245609 http://togogenome.org/gene/10090:Anapc11 ^@ http://purl.uniprot.org/uniprot/Q9CPX9 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Zinc Finger ^@ Anaphase-promoting complex subunit 11|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055748 http://togogenome.org/gene/10090:Slc5a3 ^@ http://purl.uniprot.org/uniprot/Q3UMR9|||http://purl.uniprot.org/uniprot/Q9JKZ2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Implicated in sodium coupling|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium/myo-inositol cotransporter ^@ http://purl.uniprot.org/annotation/PRO_0000105382 http://togogenome.org/gene/10090:Nkx3-1 ^@ http://purl.uniprot.org/uniprot/P97436|||http://purl.uniprot.org/uniprot/Q3UVH8 ^@ 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|||Homeobox protein Nkx-3.1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048946 http://togogenome.org/gene/10090:Necab2 ^@ http://purl.uniprot.org/uniprot/Q91ZP9 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||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_0000282614|||http://purl.uniprot.org/annotation/VSP_024215 http://togogenome.org/gene/10090:Cnbd2 ^@ http://purl.uniprot.org/uniprot/Q3TRZ7|||http://purl.uniprot.org/uniprot/Q9D5U8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Cyclic nucleotide-binding|||Cyclic nucleotide-binding domain-containing protein 2|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079473|||http://purl.uniprot.org/annotation/VSP_003825 http://togogenome.org/gene/10090:Shisal1 ^@ http://purl.uniprot.org/uniprot/A0A087WSN1|||http://purl.uniprot.org/uniprot/H7BX53|||http://purl.uniprot.org/uniprot/Q0VBP7 ^@ 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|||Pro residues|||Protein shisa-like-1 ^@ http://purl.uniprot.org/annotation/PRO_0000318952|||http://purl.uniprot.org/annotation/PRO_5040056378 http://togogenome.org/gene/10090:Paqr6 ^@ http://purl.uniprot.org/uniprot/D3Z1S5|||http://purl.uniprot.org/uniprot/Q0VBT6|||http://purl.uniprot.org/uniprot/Q6TCG5 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Membrane progestin receptor delta ^@ http://purl.uniprot.org/annotation/PRO_0000218851 http://togogenome.org/gene/10090:Zfx ^@ http://purl.uniprot.org/uniprot/B1ASD1|||http://purl.uniprot.org/uniprot/B7ZN32|||http://purl.uniprot.org/uniprot/P17012 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||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|||Phosphoserine|||Zinc finger X-chromosomal protein ^@ http://purl.uniprot.org/annotation/PRO_0000047259 http://togogenome.org/gene/10090:Dtnbp1 ^@ http://purl.uniprot.org/uniprot/Q91WZ8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Dysbindin|||In isoform 2.|||In isoform 3.|||Nuclear export signal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000191002|||http://purl.uniprot.org/annotation/VSP_009024|||http://purl.uniprot.org/annotation/VSP_021939 http://togogenome.org/gene/10090:Sprr2e ^@ http://purl.uniprot.org/uniprot/O70556 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1|||2|||3|||3 X 9 AA approximate tandem repeats|||Disordered|||Small proline-rich protein 2E ^@ http://purl.uniprot.org/annotation/PRO_0000150017 http://togogenome.org/gene/10090:Nrm ^@ http://purl.uniprot.org/uniprot/Q8VC65 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Helical|||Nuclear|||Nurim|||Perinuclear space ^@ http://purl.uniprot.org/annotation/PRO_0000299397 http://togogenome.org/gene/10090:Dda1 ^@ http://purl.uniprot.org/uniprot/D3YXY5|||http://purl.uniprot.org/uniprot/Q9D9Z5 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ DET1- and DDB1-associated protein 1|||DET1- and DDB1-associated protein 1 N-terminal|||Disordered|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000310271 http://togogenome.org/gene/10090:Or14j4 ^@ http://purl.uniprot.org/uniprot/B2RTB9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dars ^@ http://purl.uniprot.org/uniprot/Q922B2 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Aspartate|||Aspartate--tRNA ligase, cytoplasmic|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000111011 http://togogenome.org/gene/10090:Krt28 ^@ http://purl.uniprot.org/uniprot/A6BLY7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ 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_0000312706 http://togogenome.org/gene/10090:Xkrx ^@ http://purl.uniprot.org/uniprot/Q5GH68 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||XK-related protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000190773 http://togogenome.org/gene/10090:Fgf4 ^@ http://purl.uniprot.org/uniprot/A0A7U3JW80|||http://purl.uniprot.org/uniprot/P11403 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Sequence Conflict|||Signal Peptide ^@ Fibroblast growth factor|||Fibroblast growth factor 4 ^@ http://purl.uniprot.org/annotation/PRO_0000008954|||http://purl.uniprot.org/annotation/PRO_5031603811 http://togogenome.org/gene/10090:Spdef ^@ http://purl.uniprot.org/uniprot/Q9WTP3 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||ETS|||PNT|||SAM pointed domain-containing Ets transcription factor ^@ http://purl.uniprot.org/annotation/PRO_0000223959 http://togogenome.org/gene/10090:Albfm1 ^@ http://purl.uniprot.org/uniprot/F8VQ07 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Albumin ^@ http://togogenome.org/gene/10090:Mgat4a ^@ http://purl.uniprot.org/uniprot/Q812G0 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000288585|||http://purl.uniprot.org/annotation/PRO_0000288586|||http://purl.uniprot.org/annotation/VSP_025715 http://togogenome.org/gene/10090:Abca14 ^@ http://purl.uniprot.org/uniprot/E9Q8F8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ ABC transporter|||Helical ^@ http://togogenome.org/gene/10090:Gml2 ^@ http://purl.uniprot.org/uniprot/G5E8L7|||http://purl.uniprot.org/uniprot/Q9DAP4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ UPAR/Ly6|||UPAR/Ly6 domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5004325911|||http://purl.uniprot.org/annotation/PRO_5015091944 http://togogenome.org/gene/10090:Tdp2 ^@ http://purl.uniprot.org/uniprot/Q9JJX7 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with 5' end of substrate DNA|||Loss of magnesium binding.|||N-acetylmethionine|||Phosphothreonine; by ACVR1B|||Proton donor/acceptor|||Tyrosyl-DNA phosphodiesterase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000065679 http://togogenome.org/gene/10090:Gm35315 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSM0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type ^@ http://togogenome.org/gene/10090:Map3k8 ^@ http://purl.uniprot.org/uniprot/Q07174|||http://purl.uniprot.org/uniprot/Q3UEB8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Mitogen-activated protein kinase kinase kinase 8|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086256 http://togogenome.org/gene/10090:Carmil1 ^@ http://purl.uniprot.org/uniprot/D3Z030|||http://purl.uniprot.org/uniprot/Q6EDY6|||http://purl.uniprot.org/uniprot/Q9CTA1 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||CARMIL C-terminal|||CARMIL pleckstrin homology|||Decreased ability to bind heterodimeric capping protein (CP) and to inhibit the actin-capping activity of CP.|||Disordered|||F-actin-uncapping protein LRRC16A|||In isoform 2.|||In isoform 3.|||Inhibits capping activity of CP|||LRR 1|||LRR 10|||LRR 11|||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) and to inhibit the actin-capping activity of CP.|||N-acetylmethionine|||Necessary for localization at the cell membrane|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000325816|||http://purl.uniprot.org/annotation/VSP_032421|||http://purl.uniprot.org/annotation/VSP_032422|||http://purl.uniprot.org/annotation/VSP_032423|||http://purl.uniprot.org/annotation/VSP_032424 http://togogenome.org/gene/10090:Thsd7a ^@ http://purl.uniprot.org/uniprot/E9QNR5|||http://purl.uniprot.org/uniprot/Q69ZU6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Spondin-like TSP1|||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_0000256127|||http://purl.uniprot.org/annotation/PRO_0000444431|||http://purl.uniprot.org/annotation/PRO_5005911178 http://togogenome.org/gene/10090:Rexo5 ^@ http://purl.uniprot.org/uniprot/D3Z3J7|||http://purl.uniprot.org/uniprot/Q7TSF9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Exonuclease|||RRM ^@ http://togogenome.org/gene/10090:Phospho2 ^@ http://purl.uniprot.org/uniprot/Q9D9M5 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Nucleophile|||Proton donor|||Pyridoxal phosphate phosphatase PHOSPHO2 ^@ http://purl.uniprot.org/annotation/PRO_0000068834 http://togogenome.org/gene/10090:Zfp617 ^@ http://purl.uniprot.org/uniprot/Q91WM0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Gemin6 ^@ http://purl.uniprot.org/uniprot/Q9CX53 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ AD|||Gem-associated protein 6|||Phosphoserine|||Sm ^@ http://purl.uniprot.org/annotation/PRO_0000087461 http://togogenome.org/gene/10090:Mocos ^@ http://purl.uniprot.org/uniprot/Q14CH1 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue ^@ MOSC|||Molybdenum cofactor sulfurase|||N6-(pyridoxal phosphate)lysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000249953 http://togogenome.org/gene/10090:Txndc9 ^@ http://purl.uniprot.org/uniprot/Q9CQ79 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Phosphoserine|||Thioredoxin|||Thioredoxin domain-containing protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000120167 http://togogenome.org/gene/10090:Adssl1 ^@ http://purl.uniprot.org/uniprot/P28650|||http://purl.uniprot.org/uniprot/Q3UBP0 ^@ Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Region|||Splice Variant|||Strand|||Turn ^@ Adenylosuccinate synthetase isozyme 1|||Disordered|||In isoform 2.|||Proton acceptor|||Proton donor|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000095133|||http://purl.uniprot.org/annotation/VSP_008422 http://togogenome.org/gene/10090:Aadacl3 ^@ http://purl.uniprot.org/uniprot/A2A7Z8 ^@ Active Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Motif|||Transmembrane ^@ Arylacetamide deacetylase-like 3|||Helical|||Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000389253 http://togogenome.org/gene/10090:Smtnl1 ^@ http://purl.uniprot.org/uniprot/Q99LM3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand ^@ Basic and acidic residues|||Calmodulin-binding|||Calponin-homology (CH)|||Disordered|||Loss of phosphorylation. Loss of nuclear localization.|||Phosphoserine; by PKA and PKG|||Polar residues|||Smoothelin-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000317276 http://togogenome.org/gene/10090:Ptcd2 ^@ http://purl.uniprot.org/uniprot/Q8R3K3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ PPR|||Pentatricopeptide repeat-containing protein 2, mitochondrial|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000344051 http://togogenome.org/gene/10090:Otulinl ^@ http://purl.uniprot.org/uniprot/Q3TVP5 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Inactive ubiquitin thioesterase OTULINL|||OTU|||Required for membrane binding ^@ http://purl.uniprot.org/annotation/PRO_0000274405|||http://purl.uniprot.org/annotation/VSP_022738 http://togogenome.org/gene/10090:Eef1b2 ^@ http://purl.uniprot.org/uniprot/O70251 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 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_0000155022 http://togogenome.org/gene/10090:Plekhh2 ^@ http://purl.uniprot.org/uniprot/Q8C115 ^@ 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|||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_0000307122|||http://purl.uniprot.org/annotation/VSP_028576|||http://purl.uniprot.org/annotation/VSP_028577|||http://purl.uniprot.org/annotation/VSP_028578 http://togogenome.org/gene/10090:Lsm8 ^@ http://purl.uniprot.org/uniprot/Q6ZWM4 ^@ 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_0000125583 http://togogenome.org/gene/10090:Tmem50b ^@ http://purl.uniprot.org/uniprot/Q9D1X9 ^@ 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_0000174184 http://togogenome.org/gene/10090:Ddx56 ^@ http://purl.uniprot.org/uniprot/Q5SVX3|||http://purl.uniprot.org/uniprot/Q9D0R4 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region ^@ DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Phosphothreonine|||Probable ATP-dependent RNA helicase DDX56|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000055059 http://togogenome.org/gene/10090:Zfp37 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VJF3|||http://purl.uniprot.org/uniprot/A0A1Y7VLM5|||http://purl.uniprot.org/uniprot/P17141|||http://purl.uniprot.org/uniprot/Q6P3Z4|||http://purl.uniprot.org/uniprot/Q8R1B1 ^@ 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 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|||Phosphothreonine|||Polar residues|||Zinc finger protein 37 ^@ http://purl.uniprot.org/annotation/PRO_0000047294 http://togogenome.org/gene/10090:Dnajb13 ^@ http://purl.uniprot.org/uniprot/Q80Y75 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ DnaJ homolog subfamily B member 13|||J ^@ http://purl.uniprot.org/annotation/PRO_0000071040 http://togogenome.org/gene/10090:Apoc2l ^@ http://purl.uniprot.org/uniprot/Q05020|||http://purl.uniprot.org/uniprot/Q3UJG0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Region|||Sequence Conflict|||Signal Peptide ^@ Apolipoprotein C-II|||Lipid binding|||Lipoprotein lipase cofactor ^@ http://purl.uniprot.org/annotation/PRO_0000002026|||http://purl.uniprot.org/annotation/PRO_5014309204 http://togogenome.org/gene/10090:H2-DMb2 ^@ http://purl.uniprot.org/uniprot/Q31099 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097373 http://togogenome.org/gene/10090:Ppard ^@ http://purl.uniprot.org/uniprot/P35396|||http://purl.uniprot.org/uniprot/Q546I3 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||NR C4-type|||NR LBD|||Nuclear receptor|||Peroxisome proliferator-activated receptor delta|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053487 http://togogenome.org/gene/10090:Kti12 ^@ http://purl.uniprot.org/uniprot/Q9D1R2 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region ^@ Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Protein KTI12 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000285687 http://togogenome.org/gene/10090:Ppox ^@ http://purl.uniprot.org/uniprot/P51175|||http://purl.uniprot.org/uniprot/Q3UQA3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Amine oxidase|||Protoporphyrinogen oxidase ^@ http://purl.uniprot.org/annotation/PRO_0000135272 http://togogenome.org/gene/10090:Or5p59 ^@ http://purl.uniprot.org/uniprot/Q14AB1|||http://purl.uniprot.org/uniprot/Q8VG05 ^@ 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 5P59 ^@ http://purl.uniprot.org/annotation/PRO_0000150841 http://togogenome.org/gene/10090:Tsnax ^@ http://purl.uniprot.org/uniprot/Q9QZE7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Region ^@ 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_0000191687 http://togogenome.org/gene/10090:Erbb2 ^@ http://purl.uniprot.org/uniprot/P70424 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with PIK3C2B|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Receptor tyrosine-protein kinase erbB-2|||Required for interaction with KPNB1 and EEA1 ^@ http://purl.uniprot.org/annotation/PRO_0000042181 http://togogenome.org/gene/10090:Rnf222 ^@ http://purl.uniprot.org/uniprot/Q8CEF8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Chain|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Helical|||RING finger protein 222|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000329086 http://togogenome.org/gene/10090:Maco1 ^@ http://purl.uniprot.org/uniprot/Q7TQE6 ^@ 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|||Macoilin|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000070268 http://togogenome.org/gene/10090:C5ar2 ^@ http://purl.uniprot.org/uniprot/E9PVQ2|||http://purl.uniprot.org/uniprot/E9QQ21|||http://purl.uniprot.org/uniprot/Q8BW93 ^@ 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 ^@ C5a anaphylatoxin chemotactic 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|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000303083 http://togogenome.org/gene/10090:Naa20 ^@ http://purl.uniprot.org/uniprot/P61600|||http://purl.uniprot.org/uniprot/Q9DB82 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ N-acetyltransferase|||N-alpha-acetyltransferase 20 ^@ http://purl.uniprot.org/annotation/PRO_0000074535 http://togogenome.org/gene/10090:Vmac ^@ http://purl.uniprot.org/uniprot/G3XA49|||http://purl.uniprot.org/uniprot/Q8BP01 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Disordered|||Vimentin-type intermediate filament-associated coiled-coil protein ^@ http://purl.uniprot.org/annotation/PRO_0000319067 http://togogenome.org/gene/10090:Slc24a2 ^@ http://purl.uniprot.org/uniprot/Q8BUN9 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Alpha-1|||Alpha-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4 and isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Sodium/potassium/calcium exchanger 2 ^@ http://purl.uniprot.org/annotation/PRO_0000455294|||http://purl.uniprot.org/annotation/VSP_061480|||http://purl.uniprot.org/annotation/VSP_061481|||http://purl.uniprot.org/annotation/VSP_061482 http://togogenome.org/gene/10090:Lat ^@ http://purl.uniprot.org/uniprot/A0A0U1RP03|||http://purl.uniprot.org/uniprot/O54957|||http://purl.uniprot.org/uniprot/Q546H1 ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||Interaction with GRB2, GRAP2 and PIK3R1|||Interaction with PLCG1|||Linker for activation of T-cells family member 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000083326|||http://purl.uniprot.org/annotation/PRO_5006714320|||http://purl.uniprot.org/annotation/PRO_5014309648 http://togogenome.org/gene/10090:Tmem35b ^@ http://purl.uniprot.org/uniprot/Q3U0Y2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Helical|||Transmembrane protein 35B ^@ http://purl.uniprot.org/annotation/PRO_0000411097 http://togogenome.org/gene/10090:Cacnb1 ^@ http://purl.uniprot.org/uniprot/A2A542|||http://purl.uniprot.org/uniprot/A2A543|||http://purl.uniprot.org/uniprot/A2A545|||http://purl.uniprot.org/uniprot/Q8R3Z5 ^@ 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 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3|||Voltage-dependent L-type calcium channel subunit beta-1 ^@ http://purl.uniprot.org/annotation/PRO_0000144047|||http://purl.uniprot.org/annotation/VSP_010726|||http://purl.uniprot.org/annotation/VSP_010727|||http://purl.uniprot.org/annotation/VSP_010728|||http://purl.uniprot.org/annotation/VSP_010729 http://togogenome.org/gene/10090:Or5w22 ^@ http://purl.uniprot.org/uniprot/Q7TR48 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Copa ^@ http://purl.uniprot.org/uniprot/Q8BTF0|||http://purl.uniprot.org/uniprot/Q8CIE6 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Peptide|||Repeat|||Sequence Conflict ^@ Anaphase-promoting complex subunit 4-like WD40|||Coatomer WD associated region|||Coatomer alpha subunit C-terminal|||Coatomer subunit alpha|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Proxenin|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||Xenin ^@ http://purl.uniprot.org/annotation/PRO_0000327496|||http://purl.uniprot.org/annotation/PRO_0000327497|||http://purl.uniprot.org/annotation/PRO_0000327498 http://togogenome.org/gene/10090:Gpsm1 ^@ http://purl.uniprot.org/uniprot/Q6IR34 ^@ 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|||Disordered|||G-protein-signaling modulator 1|||GoLoco 1|||GoLoco 2|||GoLoco 3|||GoLoco 4|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||Interaction with STK11/LKB1|||Mediates association with membranes|||Omega-N-methylarginine|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9 ^@ http://purl.uniprot.org/annotation/PRO_0000252403|||http://purl.uniprot.org/annotation/VSP_039029|||http://purl.uniprot.org/annotation/VSP_039030|||http://purl.uniprot.org/annotation/VSP_039031|||http://purl.uniprot.org/annotation/VSP_039032|||http://purl.uniprot.org/annotation/VSP_039033 http://togogenome.org/gene/10090:Asah2 ^@ http://purl.uniprot.org/uniprot/B9EHG7|||http://purl.uniprot.org/uniprot/Q9JHE3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cleavage|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Neutral ceramidase|||Neutral ceramidase soluble form|||Neutral/alkaline non-lysosomal ceramidase C-terminal|||Neutral/alkaline non-lysosomal ceramidase N-terminal|||Nucleophile|||O-linked (GalNAc...) threonine|||Required for correct folding and localization ^@ http://purl.uniprot.org/annotation/PRO_0000247101|||http://purl.uniprot.org/annotation/PRO_0000247102 http://togogenome.org/gene/10090:Zfp407 ^@ http://purl.uniprot.org/uniprot/G3UVV3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Stpg3 ^@ http://purl.uniprot.org/uniprot/A2RSX4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Protein STPG3 ^@ http://purl.uniprot.org/annotation/PRO_0000437649 http://togogenome.org/gene/10090:Gm13283 ^@ http://purl.uniprot.org/uniprot/A0A087WPG5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5040059688 http://togogenome.org/gene/10090:Rgs5 ^@ http://purl.uniprot.org/uniprot/O08850 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ RGS|||Regulator of G-protein signaling 5 ^@ http://purl.uniprot.org/annotation/PRO_0000204189 http://togogenome.org/gene/10090:Nme3 ^@ http://purl.uniprot.org/uniprot/Q9WV85 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Nucleoside diphosphate kinase 3|||Pros-phosphohistidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000137124 http://togogenome.org/gene/10090:Cklf ^@ http://purl.uniprot.org/uniprot/Q9DAS1 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Splice Variant|||Transmembrane ^@ Chemokine-like factor|||Helical|||In isoform CKLF3.|||In isoform CKLF4.|||In isoform CKLF5.|||MARVEL ^@ http://purl.uniprot.org/annotation/PRO_0000186095|||http://purl.uniprot.org/annotation/VSP_050599|||http://purl.uniprot.org/annotation/VSP_050600|||http://purl.uniprot.org/annotation/VSP_050602|||http://purl.uniprot.org/annotation/VSP_050603 http://togogenome.org/gene/10090:Scgb2b2 ^@ http://purl.uniprot.org/uniprot/G5E8B4 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015091929 http://togogenome.org/gene/10090:4930402K13Rik ^@ http://purl.uniprot.org/uniprot/B1AW18|||http://purl.uniprot.org/uniprot/Q9D5P7 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:H2-DMa ^@ http://purl.uniprot.org/uniprot/Q31621 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097372 http://togogenome.org/gene/10090:Bpifb9a ^@ http://purl.uniprot.org/uniprot/Q80XI7 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Vomeromodulin ^@ http://purl.uniprot.org/annotation/PRO_0000045171|||http://purl.uniprot.org/annotation/VSP_016661 http://togogenome.org/gene/10090:Tceanc2 ^@ http://purl.uniprot.org/uniprot/Q8R2M0 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ 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_0000286575 http://togogenome.org/gene/10090:Gpr176 ^@ http://purl.uniprot.org/uniprot/Q80WT4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreases expression; No reduction of cAMP upon induction.|||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|||N-linked (GlcNAc...) asparagine|||No reduction of cAMP upon induction.|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000069657 http://togogenome.org/gene/10090:Prss39 ^@ http://purl.uniprot.org/uniprot/O70169 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Inactive serine protease 39|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000344981 http://togogenome.org/gene/10090:Sez6 ^@ http://purl.uniprot.org/uniprot/Q7TSK2 ^@ 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 ^@ CUB 1|||CUB 2|||CUB 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Seizure protein 6|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5 ^@ http://purl.uniprot.org/annotation/PRO_0000341348|||http://purl.uniprot.org/annotation/VSP_034254|||http://purl.uniprot.org/annotation/VSP_034255|||http://purl.uniprot.org/annotation/VSP_034256|||http://purl.uniprot.org/annotation/VSP_034257 http://togogenome.org/gene/10090:Or9s23 ^@ http://purl.uniprot.org/uniprot/Q8VGU3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Idh2 ^@ http://purl.uniprot.org/uniprot/P54071 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Critical for catalysis|||Isocitrate dehydrogenase [NADP], mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000014421 http://togogenome.org/gene/10090:Fastkd5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J291|||http://purl.uniprot.org/uniprot/Q7TMV3 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ FAST kinase domain-containing protein 5, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||RAP ^@ http://purl.uniprot.org/annotation/PRO_0000284981 http://togogenome.org/gene/10090:Pigz ^@ http://purl.uniprot.org/uniprot/Q8BTP0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ GPI mannosyltransferase 4|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000246269 http://togogenome.org/gene/10090:Trim55 ^@ http://purl.uniprot.org/uniprot/G3X8Y1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||B box-type|||COS|||Disordered|||Polar residues|||RING-type ^@ http://togogenome.org/gene/10090:Ccdc91 ^@ http://purl.uniprot.org/uniprot/Q9D8L5 ^@ 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 ^@ Coiled-coil domain-containing protein 91|||Disordered|||GGA1-binding motif|||Homodimerization|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000087479|||http://purl.uniprot.org/annotation/VSP_013245|||http://purl.uniprot.org/annotation/VSP_013246|||http://purl.uniprot.org/annotation/VSP_013247 http://togogenome.org/gene/10090:Rpap2 ^@ http://purl.uniprot.org/uniprot/Q8VC34 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Putative RNA polymerase II subunit B1 CTD phosphatase Rpap2|||RTR1-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000250649|||http://purl.uniprot.org/annotation/VSP_020682|||http://purl.uniprot.org/annotation/VSP_020683|||http://purl.uniprot.org/annotation/VSP_020684|||http://purl.uniprot.org/annotation/VSP_020685|||http://purl.uniprot.org/annotation/VSP_020686|||http://purl.uniprot.org/annotation/VSP_020687 http://togogenome.org/gene/10090:Rab11a ^@ http://purl.uniprot.org/uniprot/P62492|||http://purl.uniprot.org/uniprot/Q0PD45 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict ^@ Cysteine methyl ester|||Disordered|||Effector region|||N-acetylglycine|||Ras-related protein Rab-11A|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121152|||http://purl.uniprot.org/annotation/PRO_0000370808 http://togogenome.org/gene/10090:Pabpc4l ^@ http://purl.uniprot.org/uniprot/G5E8X2 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ RRM ^@ http://togogenome.org/gene/10090:Dnajc5 ^@ http://purl.uniprot.org/uniprot/P60904 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Turn ^@ DnaJ homolog subfamily C member 5|||J|||N6-acetyllysine|||No effect on palmitoylation. No change in subcellular location; when associated with C-129.|||No effect on palmitoylation. No change in subcellular location; when associated with G-118 and F-121.|||No effect on palmitoylation. No change in subcellular location; when associated with H-135.|||No effect on palmitoylation. No change in subcellular location; when associated with V-113 and F-121.|||No effect on palmitoylation. No change in subcellular location; when associated with V-113 and G-118.|||Phosphoserine|||Phosphotyrosine|||Reduced interaction with SYT9, but no effect on the interaction with HSC70.|||Reduced interaction with SYT9. ^@ http://purl.uniprot.org/annotation/PRO_0000071053 http://togogenome.org/gene/10090:Cd96 ^@ http://purl.uniprot.org/uniprot/Q3U0X8 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type 1|||Ig-like V-type 2|||N-linked (GlcNAc...) asparagine|||Polar residues|||T-cell surface protein tactile ^@ http://purl.uniprot.org/annotation/PRO_0000313891 http://togogenome.org/gene/10090:Kmt5b ^@ http://purl.uniprot.org/uniprot/Q3U8K7 ^@ Binding 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||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 SUMO2)|||Histone-lysine N-methyltransferase KMT5B|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||Loss of methyltransferase activity for H4K20me1 peptide.|||Polar residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000281788|||http://purl.uniprot.org/annotation/VSP_024053|||http://purl.uniprot.org/annotation/VSP_024054|||http://purl.uniprot.org/annotation/VSP_024055|||http://purl.uniprot.org/annotation/VSP_024056|||http://purl.uniprot.org/annotation/VSP_024057 http://togogenome.org/gene/10090:Fhl2 ^@ http://purl.uniprot.org/uniprot/O70433|||http://purl.uniprot.org/uniprot/Q543D7 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Zinc Finger ^@ C4-type|||Four and a half LIM domains protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000075738 http://togogenome.org/gene/10090:Moxd2 ^@ http://purl.uniprot.org/uniprot/Q7TT41 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DBH-like monooxygenase protein 2|||DOMON|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000305224 http://togogenome.org/gene/10090:Gm13306 ^@ http://purl.uniprot.org/uniprot/Q9Z1X0 ^@ 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 27|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000005240|||http://purl.uniprot.org/annotation/VSP_001065 http://togogenome.org/gene/10090:Coro2a ^@ http://purl.uniprot.org/uniprot/B1AVH4|||http://purl.uniprot.org/uniprot/B1AVH5|||http://purl.uniprot.org/uniprot/Q8C0P5 ^@ 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 ^@ Coronin-2A|||DUF1899|||Disordered|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000050929 http://togogenome.org/gene/10090:Ppp1r16a ^@ http://purl.uniprot.org/uniprot/Q923M0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Repeat ^@ 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_0000067041|||http://purl.uniprot.org/annotation/PRO_0000396708 http://togogenome.org/gene/10090:Med25 ^@ http://purl.uniprot.org/uniprot/A0A140LHG7|||http://purl.uniprot.org/uniprot/Q8VCB2 ^@ 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 ^@ Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with CREBBP|||Interaction with RARA|||Interaction with VP16|||Interaction with the Mediator complex|||LXXLL motif|||Mediator complex subunit Med25 NR box|||Mediator complex subunit Med25 PTOV|||Mediator complex subunit Med25 synapsin 1|||Mediator of RNA polymerase II transcription subunit 25|||Mediator of RNA polymerase II transcription subunit 25 von Willebrand factor type A|||Polar residues|||Pro residues|||SPIN-DOC-like zinc-finger ^@ http://purl.uniprot.org/annotation/PRO_0000304953|||http://purl.uniprot.org/annotation/VSP_028147|||http://purl.uniprot.org/annotation/VSP_028148|||http://purl.uniprot.org/annotation/VSP_028149|||http://purl.uniprot.org/annotation/VSP_028150 http://togogenome.org/gene/10090:Or6aa1 ^@ http://purl.uniprot.org/uniprot/Q8VFP0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cpsf4l ^@ http://purl.uniprot.org/uniprot/E9Q2N0|||http://purl.uniprot.org/uniprot/G3UWW6|||http://purl.uniprot.org/uniprot/Q3TTY7|||http://purl.uniprot.org/uniprot/Q9DBA5 ^@ Domain Extent|||Region|||Zinc Finger ^@ Domain Extent|||Region|||Zinc Finger ^@ C3H1-type|||Disordered ^@ http://togogenome.org/gene/10090:Abca9 ^@ http://purl.uniprot.org/uniprot/Q8K449 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family A member 9|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000250681 http://togogenome.org/gene/10090:Smarcb1 ^@ http://purl.uniprot.org/uniprot/Q9Z0H3 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Crosslink|||Modified Residue|||Region|||Repeat|||Splice Variant ^@ 1|||2|||2 X approximate tandem repeats|||DNA-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000205949|||http://purl.uniprot.org/annotation/VSP_004400 http://togogenome.org/gene/10090:Adal ^@ http://purl.uniprot.org/uniprot/Q80SY6|||http://purl.uniprot.org/uniprot/Z4YL50 ^@ 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|||Site|||Splice Variant ^@ Adenosine deaminase|||Adenosine deaminase-like protein|||Important for catalytic activity|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000285091|||http://purl.uniprot.org/annotation/VSP_024822|||http://purl.uniprot.org/annotation/VSP_024823|||http://purl.uniprot.org/annotation/VSP_024824|||http://purl.uniprot.org/annotation/VSP_024825 http://togogenome.org/gene/10090:Nedd1 ^@ http://purl.uniprot.org/uniprot/P33215 ^@ 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|||Phosphoserine; by PLK1|||Phosphothreonine; by CDK1|||Protein NEDD1|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8 ^@ http://purl.uniprot.org/annotation/PRO_0000051096|||http://purl.uniprot.org/annotation/VSP_016263|||http://purl.uniprot.org/annotation/VSP_016264 http://togogenome.org/gene/10090:Gcnt2 ^@ http://purl.uniprot.org/uniprot/P97402|||http://purl.uniprot.org/uniprot/Q6T5E4|||http://purl.uniprot.org/uniprot/Q7TPQ8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000191398 http://togogenome.org/gene/10090:Tnfrsf1a ^@ http://purl.uniprot.org/uniprot/P25118|||http://purl.uniprot.org/uniprot/Q3U479 ^@ 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|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ (Microbial infection) N-beta-linked (GlcNAc) arginine|||Cytoplasmic|||Death|||Extracellular|||Helical|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000034545|||http://purl.uniprot.org/annotation/PRO_5014309206 http://togogenome.org/gene/10090:Hcfc1 ^@ http://purl.uniprot.org/uniprot/B1AUX2|||http://purl.uniprot.org/uniprot/Q61191 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Strand ^@ Asymmetric dimethylarginine|||Cleavage; by autolysis|||Disordered|||Fibronectin type-III|||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|||Interaction with GABP2|||Interaction with SIN3A|||Interaction with ZBTB17|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Required for interaction with OGT ^@ http://purl.uniprot.org/annotation/PRO_0000016635|||http://purl.uniprot.org/annotation/PRO_0000016636|||http://purl.uniprot.org/annotation/PRO_0000016637|||http://purl.uniprot.org/annotation/PRO_0000016638|||http://purl.uniprot.org/annotation/PRO_0000016639|||http://purl.uniprot.org/annotation/PRO_0000016640|||http://purl.uniprot.org/annotation/PRO_0000016641|||http://purl.uniprot.org/annotation/PRO_0000016642|||http://purl.uniprot.org/annotation/PRO_0000016643|||http://purl.uniprot.org/annotation/PRO_0000016644|||http://purl.uniprot.org/annotation/PRO_0000016645|||http://purl.uniprot.org/annotation/PRO_0000016646 http://togogenome.org/gene/10090:Dnase2a ^@ http://purl.uniprot.org/uniprot/P56542|||http://purl.uniprot.org/uniprot/Q3UM14 ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Deoxyribonuclease-2-alpha|||N-linked (GlcNAc...) asparagine|||deoxyribonuclease II ^@ http://purl.uniprot.org/annotation/PRO_0000007292|||http://purl.uniprot.org/annotation/PRO_5014309169 http://togogenome.org/gene/10090:Atg13 ^@ http://purl.uniprot.org/uniprot/Q91YI1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Autophagy-related protein 13|||Disordered|||Important for interaction with ATG101|||In isoform 2.|||LIR|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by ULK1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000345151|||http://purl.uniprot.org/annotation/VSP_034922 http://togogenome.org/gene/10090:Man1c1 ^@ http://purl.uniprot.org/uniprot/Q6NXK9 ^@ Active Site|||Binding Site|||Disulfide Bond|||Modification|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Disulfide Bond|||Region|||Transmembrane ^@ Disordered|||Helical|||Proton donor ^@ http://togogenome.org/gene/10090:Nfe2l1 ^@ http://purl.uniprot.org/uniprot/Q3U5L0|||http://purl.uniprot.org/uniprot/Q3UFI8|||http://purl.uniprot.org/uniprot/Q3V3M1|||http://purl.uniprot.org/uniprot/Q61985|||http://purl.uniprot.org/uniprot/Q6GTN8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Abolishes interaction with FBXW7.|||Abolishes phosphorylation by CK2.|||Abolishes ubiquitination and degradation by the SCF(BTRC) complex.|||BZIP|||Basic and acidic residues|||Basic motif|||CPD|||Cholesterol recognition/amino acid consensus (CRAC) region|||Cleavage; by DDI2|||Destruction motif|||Disordered|||Does not affect phosphorylation by CK2.|||Endoplasmic reticulum membrane sensor NFE2L1|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Leucine-zipper|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CK2|||Polar residues|||Transcription factor NRF1|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076448|||http://purl.uniprot.org/annotation/PRO_0000443104|||http://purl.uniprot.org/annotation/VSP_000580|||http://purl.uniprot.org/annotation/VSP_000581|||http://purl.uniprot.org/annotation/VSP_046523|||http://purl.uniprot.org/annotation/VSP_046524 http://togogenome.org/gene/10090:Homez ^@ http://purl.uniprot.org/uniprot/A0A0R4J108|||http://purl.uniprot.org/uniprot/Q80W88 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox|||Homeobox 1|||Homeobox 2|||Homeobox 3|||Homeobox and leucine zipper protein Homez|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049136|||http://purl.uniprot.org/annotation/VSP_009133 http://togogenome.org/gene/10090:Gnb2 ^@ http://purl.uniprot.org/uniprot/P62880|||http://purl.uniprot.org/uniprot/Q3U9V4 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-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_0000127696 http://togogenome.org/gene/10090:Sucla2 ^@ http://purl.uniprot.org/uniprot/Q9Z2I9 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Site|||Transit Peptide ^@ ATP-grasp|||Important for substrate specificity|||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_0000033353 http://togogenome.org/gene/10090:Kcnq4 ^@ http://purl.uniprot.org/uniprot/Q9JK97 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ A-domain (Tetramerization)|||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|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily KQT member 4|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054038 http://togogenome.org/gene/10090:Kir3dl2 ^@ http://purl.uniprot.org/uniprot/Q673W2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Immunoglobulin subtype ^@ http://purl.uniprot.org/annotation/PRO_5015098138 http://togogenome.org/gene/10090:Racgap1 ^@ http://purl.uniprot.org/uniprot/Q9WVM1 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with SLC26A8|||N-acetylmethionine|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by AURKB|||Phosphoserine; by PLK1|||Phosphothreonine|||Rac GTPase-activating protein 1|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000228809 http://togogenome.org/gene/10090:Map1lc3a ^@ http://purl.uniprot.org/uniprot/Q91VR7 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Chain|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Cleavage; by ATG4B|||Important for interaction with ATG13 and for autophagosome formation|||Microtubule-associated proteins 1A/1B light chain 3A|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Phosphoserine; by PKA|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000017194|||http://purl.uniprot.org/annotation/PRO_0000017195 http://togogenome.org/gene/10090:Sycp2 ^@ http://purl.uniprot.org/uniprot/Q9CUU3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Synaptonemal complex protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000072367 http://togogenome.org/gene/10090:4933427D14Rik ^@ http://purl.uniprot.org/uniprot/A0A0R4J1C3|||http://purl.uniprot.org/uniprot/Q6A000 ^@ 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|||Necessary and sufficient for CEP20-binding|||Phosphoserine|||Polar residues|||Protein moonraker ^@ http://purl.uniprot.org/annotation/PRO_0000280110 http://togogenome.org/gene/10090:Slc22a28 ^@ http://purl.uniprot.org/uniprot/B2RT89|||http://purl.uniprot.org/uniprot/Q8BWE8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:Bcl2l10 ^@ http://purl.uniprot.org/uniprot/Q9Z0F3 ^@ Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ Chain|||Crosslink|||Helix|||Motif|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ BH1|||BH2|||Bcl-2-like protein 10|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000143069 http://togogenome.org/gene/10090:Tm9sf3 ^@ http://purl.uniprot.org/uniprot/Q9ET30 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Signal Peptide|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane 9 superfamily member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000034370 http://togogenome.org/gene/10090:Folr2 ^@ http://purl.uniprot.org/uniprot/Q05685 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide ^@ Folate receptor beta|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000008808|||http://purl.uniprot.org/annotation/PRO_0000008809 http://togogenome.org/gene/10090:Celf1 ^@ http://purl.uniprot.org/uniprot/P28659 ^@ 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 ^@ CUGBP Elav-like family member 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2|||RRM 3|||Reduces CDK4-mediated phosphorylation. ^@ http://purl.uniprot.org/annotation/PRO_0000081539|||http://purl.uniprot.org/annotation/VSP_005786|||http://purl.uniprot.org/annotation/VSP_005787|||http://purl.uniprot.org/annotation/VSP_026789 http://togogenome.org/gene/10090:Mrpl22 ^@ http://purl.uniprot.org/uniprot/Q8BU88 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein uL22m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000261645 http://togogenome.org/gene/10090:Rybp ^@ http://purl.uniprot.org/uniprot/Q8CCI5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with GABPB1 and FANK1|||Loss of ubiquitin binding.|||Phosphoserine|||Polar residues|||RING1 and YY1-binding protein|||RanBP2-type ^@ http://purl.uniprot.org/annotation/PRO_0000097551 http://togogenome.org/gene/10090:Crbn ^@ http://purl.uniprot.org/uniprot/Q8C7D2 ^@ 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 ^@ CULT|||Disordered|||In isoform 2.|||In isoform 3.|||Lon N-terminal|||Phosphoserine|||Protein cereblon ^@ http://purl.uniprot.org/annotation/PRO_0000076161|||http://purl.uniprot.org/annotation/VSP_015210|||http://purl.uniprot.org/annotation/VSP_039063 http://togogenome.org/gene/10090:Gm2897 ^@ http://purl.uniprot.org/uniprot/K7N6T7 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rprd1b ^@ http://purl.uniprot.org/uniprot/A0A0R4J195|||http://purl.uniprot.org/uniprot/Q9CSU0 ^@ 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 ^@ Basic and acidic residues|||CID|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Phosphotyrosine|||Regulation of nuclear pre-mRNA domain-containing protein 1B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000079442|||http://purl.uniprot.org/annotation/VSP_018618|||http://purl.uniprot.org/annotation/VSP_018619|||http://purl.uniprot.org/annotation/VSP_035576|||http://purl.uniprot.org/annotation/VSP_035577 http://togogenome.org/gene/10090:Nt5dc2 ^@ http://purl.uniprot.org/uniprot/Q91X76 ^@ Binding Site|||Site ^@ Binding Site ^@ ^@ http://togogenome.org/gene/10090:Disp2 ^@ http://purl.uniprot.org/uniprot/Q8CIP5 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Protein dispatched homolog 2|||SSD ^@ http://purl.uniprot.org/annotation/PRO_0000310697|||http://purl.uniprot.org/annotation/VSP_029324|||http://purl.uniprot.org/annotation/VSP_029325 http://togogenome.org/gene/10090:Camk2n2 ^@ http://purl.uniprot.org/uniprot/B2RXL5|||http://purl.uniprot.org/uniprot/Q78WH7 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Calcium/calmodulin-dependent protein kinase II inhibitor 2|||Disordered|||Inhibitory domain ^@ http://purl.uniprot.org/annotation/PRO_0000327267 http://togogenome.org/gene/10090:Rbbp4 ^@ http://purl.uniprot.org/uniprot/Q60972 ^@ Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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|||Interaction with ARMC12|||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_0000051187 http://togogenome.org/gene/10090:Or9k7 ^@ http://purl.uniprot.org/uniprot/Q8VEV5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r34 ^@ http://purl.uniprot.org/uniprot/G3XA52 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cyp26c1 ^@ http://purl.uniprot.org/uniprot/B2RXA7 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Cytochrome P450 26C1|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000458227 http://togogenome.org/gene/10090:Uncx ^@ http://purl.uniprot.org/uniprot/O08934 ^@ 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 unc-4 homolog|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000334625 http://togogenome.org/gene/10090:Cldn5 ^@ http://purl.uniprot.org/uniprot/O54942 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Claudin-5|||Cytoplasmic|||Extracellular|||Helical|||Interactions with TJP1, TJP2 and TJP3 ^@ http://purl.uniprot.org/annotation/PRO_0000144746 http://togogenome.org/gene/10090:Alg12 ^@ http://purl.uniprot.org/uniprot/Q8VCA2|||http://purl.uniprot.org/uniprot/Q8VDB2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000215782 http://togogenome.org/gene/10090:Sult1d1 ^@ http://purl.uniprot.org/uniprot/Q3UZZ6 ^@ 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 ^@ No effect on enzyme activity against dopamine.|||Proton acceptor|||Reduces enzyme activity against dopamine.|||Sulfotransferase 1 family member D1 ^@ http://purl.uniprot.org/annotation/PRO_0000416459 http://togogenome.org/gene/10090:Fam227a ^@ http://purl.uniprot.org/uniprot/A0A2R8VHN9|||http://purl.uniprot.org/uniprot/Q8CA61|||http://purl.uniprot.org/uniprot/Q9D3V8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Myadm ^@ http://purl.uniprot.org/uniprot/O35682|||http://purl.uniprot.org/uniprot/Q0VE46 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ Helical|||MARVEL|||MARVEL 1|||MARVEL 2|||Myeloid-associated differentiation marker ^@ http://purl.uniprot.org/annotation/PRO_0000156817 http://togogenome.org/gene/10090:Pcdhga12 ^@ http://purl.uniprot.org/uniprot/Q91XY7 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Efcab6 ^@ http://purl.uniprot.org/uniprot/Q6P1E8 ^@ 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 ^@ Disordered|||EF-hand 1|||EF-hand 10|||EF-hand 11|||EF-hand 12|||EF-hand 13|||EF-hand 14|||EF-hand 15|||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.|||Interaction with AR|||Interaction with PARK7|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000246026|||http://purl.uniprot.org/annotation/VSP_019814|||http://purl.uniprot.org/annotation/VSP_029427|||http://purl.uniprot.org/annotation/VSP_029428 http://togogenome.org/gene/10090:Pex1 ^@ http://purl.uniprot.org/uniprot/Q5BL07 ^@ 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of phospholipid-binding.|||No effect on phospholipid-binding.|||Peroxisomal ATPase PEX1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000304931|||http://purl.uniprot.org/annotation/VSP_028131 http://togogenome.org/gene/10090:Llph ^@ http://purl.uniprot.org/uniprot/Q9D945 ^@ 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 ^@ Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Protein LLP homolog ^@ http://purl.uniprot.org/annotation/PRO_0000274347|||http://purl.uniprot.org/annotation/VSP_022719 http://togogenome.org/gene/10090:Afg3l1 ^@ http://purl.uniprot.org/uniprot/Q920A7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant|||Transit Peptide|||Transmembrane ^@ AFG3-like protein 1|||Absence of proteolytic activity. Loss of its processing into the mature form.|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000084672|||http://purl.uniprot.org/annotation/VSP_031809|||http://purl.uniprot.org/annotation/VSP_031810 http://togogenome.org/gene/10090:Or2a25 ^@ http://purl.uniprot.org/uniprot/Q8VGP6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Atp2b2 ^@ http://purl.uniprot.org/uniprot/F8WHB1|||http://purl.uniprot.org/uniprot/Q3UHH0|||http://purl.uniprot.org/uniprot/Q3UHJ3|||http://purl.uniprot.org/uniprot/Q9R0K7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence 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 dfw; results in impaired long-term Ca2+ export at stereocilia.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKC|||Plasma membrane calcium-transporting ATPase 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000046215 http://togogenome.org/gene/10090:Tbcel ^@ http://purl.uniprot.org/uniprot/Q8C5W3 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||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_0000239669|||http://purl.uniprot.org/annotation/VSP_019253 http://togogenome.org/gene/10090:Syt6 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPS8|||http://purl.uniprot.org/uniprot/Q05BE2|||http://purl.uniprot.org/uniprot/Q3UY13|||http://purl.uniprot.org/uniprot/Q6P1H9|||http://purl.uniprot.org/uniprot/Q9R0N8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ C2|||C2 1|||C2 2|||Cysteine motif|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Necessary for cell membrane association (isoform 2)|||Phosphoserine|||Polar residues|||Synaptotagmin-6|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000183955|||http://purl.uniprot.org/annotation/VSP_041729 http://togogenome.org/gene/10090:Id3 ^@ http://purl.uniprot.org/uniprot/P41133|||http://purl.uniprot.org/uniprot/Q545W1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ BHLH|||DNA-binding protein inhibitor ID-3|||Interaction with IFI204|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127248 http://togogenome.org/gene/10090:Ushbp1 ^@ http://purl.uniprot.org/uniprot/Q8R370 ^@ 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|||Harmonin-binding protein USHBP1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000252110 http://togogenome.org/gene/10090:Napb ^@ http://purl.uniprot.org/uniprot/P28663 ^@ Chain|||Molecule Processing ^@ Chain ^@ Beta-soluble NSF attachment protein ^@ http://purl.uniprot.org/annotation/PRO_0000219061 http://togogenome.org/gene/10090:Or12k5 ^@ http://purl.uniprot.org/uniprot/Q7TRY5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kat2a ^@ http://purl.uniprot.org/uniprot/Q6P3Z8|||http://purl.uniprot.org/uniprot/Q9JHD2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Bromo|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone acetyltransferase KAT2A|||N-acetylalanine|||N-acetyltransferase|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proton donor/acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000211203 http://togogenome.org/gene/10090:Fer1l5 ^@ http://purl.uniprot.org/uniprot/M1INE8|||http://purl.uniprot.org/uniprot/M1JB08|||http://purl.uniprot.org/uniprot/M1JB80|||http://purl.uniprot.org/uniprot/P0DM40 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Transmembrane ^@ C2|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||C2 6|||C2 7|||Fer-1-like protein 5|||Ferlin B-domain|||Helical|||Peroxin/Ferlin|||Reduces interaction with EHD2. ^@ http://purl.uniprot.org/annotation/PRO_0000422647 http://togogenome.org/gene/10090:Prl8a2 ^@ http://purl.uniprot.org/uniprot/O35258|||http://purl.uniprot.org/uniprot/O54832 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015096770|||http://purl.uniprot.org/annotation/PRO_5015096793 http://togogenome.org/gene/10090:Plxna2 ^@ http://purl.uniprot.org/uniprot/P70207 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes interaction with SEMA6A.|||Cytoplasmic|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Plexin-A2|||Sema ^@ http://purl.uniprot.org/annotation/PRO_0000232748 http://togogenome.org/gene/10090:Gpbp1l1 ^@ http://purl.uniprot.org/uniprot/Q6NZP2 ^@ 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|||Phosphothreonine|||Polar residues|||Vasculin-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000324116 http://togogenome.org/gene/10090:Or8d6 ^@ http://purl.uniprot.org/uniprot/Q8VH09 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rictor ^@ http://purl.uniprot.org/uniprot/Q6QI06 ^@ 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 ubiquitin)|||In isoform 2.|||Interaction with NBN|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by RPS6KB1|||Polar residues|||Rapamycin-insensitive companion of mTOR ^@ http://purl.uniprot.org/annotation/PRO_0000308180|||http://purl.uniprot.org/annotation/VSP_052583 http://togogenome.org/gene/10090:Rdh9 ^@ http://purl.uniprot.org/uniprot/Q8K5C8 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099254 http://togogenome.org/gene/10090:Rnf8 ^@ http://purl.uniprot.org/uniprot/Q8VC56 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Zinc Finger ^@ Abolishes interaction with PIWIL1.|||Disordered|||E3 ubiquitin-protein ligase RNF8|||FHA|||Phosphoserine|||RING-type|||Required for interaction with PIWIL1 ^@ http://purl.uniprot.org/annotation/PRO_0000056049 http://togogenome.org/gene/10090:Clec4e ^@ http://purl.uniprot.org/uniprot/Q4FK29|||http://purl.uniprot.org/uniprot/Q9R0Q8 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Abolishes the association with FCER1G.|||Abrogates Malassezia recognition; when associated with D-171.|||Abrogates Malassezia recognition; when associated with Q-169.|||C-type lectin|||C-type lectin domain family 4 member E|||Confers specificity for glucose/mannose-type carbohydrates|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046620 http://togogenome.org/gene/10090:Gm21638 ^@ http://purl.uniprot.org/uniprot/J3QNI1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Dlgap5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0G7|||http://purl.uniprot.org/uniprot/Q8K4R9 ^@ 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|||Disks large-associated protein 5|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by AURKA|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000174300|||http://purl.uniprot.org/annotation/VSP_051825|||http://purl.uniprot.org/annotation/VSP_051826|||http://purl.uniprot.org/annotation/VSP_051827|||http://purl.uniprot.org/annotation/VSP_051828 http://togogenome.org/gene/10090:Fxyd6 ^@ http://purl.uniprot.org/uniprot/Q9D164 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||FXYD domain-containing ion transport regulator 6|||Helical|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000010374|||http://purl.uniprot.org/annotation/VSP_001585 http://togogenome.org/gene/10090:Csrp3 ^@ http://purl.uniprot.org/uniprot/P50462|||http://purl.uniprot.org/uniprot/Q545C7 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Cysteine and glycine-rich protein 3|||Interaction with CLF2|||Interaction with TCAP|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||Mice develop an age- and gene dosage-dependent hypertrophic cardiomyopathy and heart failure phenotype, characterized by almost complete loss of contractile reserve under catecholamine induced stress. They display increased in septum wall thickness, fractional shortening, and wall thickness per diameter (h/r). There is also evidence for skeletal muscle pathology. In addition, homozygous mutants show increased left ventricle (LC) mass per body weight (BW) and significantly reduced body weight. An increased nuclear localization of Csrp3 is also observed. Decreases interaction with TCAP.|||Nuclear localization signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000075728 http://togogenome.org/gene/10090:Npw ^@ http://purl.uniprot.org/uniprot/F7B5D6|||http://purl.uniprot.org/uniprot/Q3V2F0 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Signal Peptide ^@ Chain|||Non-terminal Residue|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5030169847 http://togogenome.org/gene/10090:Tmem88 ^@ http://purl.uniprot.org/uniprot/Q9D0N8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 88 ^@ http://purl.uniprot.org/annotation/PRO_0000251708 http://togogenome.org/gene/10090:Gstk1 ^@ http://purl.uniprot.org/uniprot/Q9DCM2 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Glutathione S-transferase kappa 1|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000185892 http://togogenome.org/gene/10090:Vmn2r112 ^@ http://purl.uniprot.org/uniprot/L7N221 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982389 http://togogenome.org/gene/10090:Abtb1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0A1|||http://purl.uniprot.org/uniprot/Q99LJ2 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||Ankyrin repeat and BTB/POZ domain-containing protein 1|||BTB|||BTB 1|||BTB 2 ^@ http://purl.uniprot.org/annotation/PRO_0000248268 http://togogenome.org/gene/10090:Skint3 ^@ http://purl.uniprot.org/uniprot/A7TZF0 ^@ 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 C1-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Selection and upkeep of intraepithelial T-cells protein 3 ^@ http://purl.uniprot.org/annotation/PRO_5000270105|||http://purl.uniprot.org/annotation/VSP_034880|||http://purl.uniprot.org/annotation/VSP_034881 http://togogenome.org/gene/10090:Gtf3c5 ^@ http://purl.uniprot.org/uniprot/Q3UI98|||http://purl.uniprot.org/uniprot/Q8R2T8 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||General transcription factor 3C polypeptide 5|||In isoform 2.|||N-acetylalanine|||Removed|||Transcription factor IIIC subunit 5 HTH|||Transcription factor IIIC subunit Tfc1/Sfc1 triple barrel ^@ http://purl.uniprot.org/annotation/PRO_0000209716|||http://purl.uniprot.org/annotation/VSP_010356 http://togogenome.org/gene/10090:Atp6v1g3 ^@ http://purl.uniprot.org/uniprot/Q8BMC1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||V-type proton ATPase subunit G 3 ^@ http://purl.uniprot.org/annotation/PRO_0000285921 http://togogenome.org/gene/10090:Pcdhac2 ^@ http://purl.uniprot.org/uniprot/Q91Y09 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Cadherin|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (Man...) threonine ^@ http://purl.uniprot.org/annotation/PRO_5015099532 http://togogenome.org/gene/10090:Or10p21 ^@ http://purl.uniprot.org/uniprot/Q8VGC1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tti2 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSJ1|||http://purl.uniprot.org/uniprot/Q8BGV4|||http://purl.uniprot.org/uniprot/Q8BNA7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||TELO2-interacting protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000279415 http://togogenome.org/gene/10090:Slc35f2 ^@ http://purl.uniprot.org/uniprot/Q7TML3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||N-acetylmethionine|||Phosphoserine|||Solute carrier family 35 member F2 ^@ http://purl.uniprot.org/annotation/PRO_0000307310 http://togogenome.org/gene/10090:Zfp781 ^@ http://purl.uniprot.org/uniprot/Q0P5U5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB ^@ http://togogenome.org/gene/10090:Dlgap2 ^@ http://purl.uniprot.org/uniprot/Q0VF59|||http://purl.uniprot.org/uniprot/Q3V2X4|||http://purl.uniprot.org/uniprot/Q8BJ42 ^@ 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|||Disks large-associated protein 2|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000174292|||http://purl.uniprot.org/annotation/VSP_014817 http://togogenome.org/gene/10090:Cmc1 ^@ http://purl.uniprot.org/uniprot/Q9CPZ8 ^@ 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_0000317186 http://togogenome.org/gene/10090:Lemd1 ^@ http://purl.uniprot.org/uniprot/A0A087WQH1|||http://purl.uniprot.org/uniprot/A0A087WR92|||http://purl.uniprot.org/uniprot/Q14C37 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||LEM|||LEM domain-containing protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000285248 http://togogenome.org/gene/10090:Arpc5l ^@ http://purl.uniprot.org/uniprot/Q9D898 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Actin-related protein 2/3 complex subunit 5-like protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000279481 http://togogenome.org/gene/10090:Mef2c ^@ http://purl.uniprot.org/uniprot/A0A0G2JEC2|||http://purl.uniprot.org/uniprot/A0A0H2UH28|||http://purl.uniprot.org/uniprot/A0A0H2UKB6|||http://purl.uniprot.org/uniprot/Q3V1B5|||http://purl.uniprot.org/uniprot/Q8CFN5 ^@ 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|||Strand ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand ^@ 7-fold increase in DNA binding.|||Basic and acidic residues|||Beta domain|||Cleavage|||Disordered|||Enhanced DNA binding activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 4 and isoform 5.|||Increased mobility in differentiating cells. Greatly reduced DNA binding.|||MADS-box|||Mef2-type|||Myocyte-specific enhancer factor 2C|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphoserine; by CK2|||Phosphoserine; by MAPK7|||Phosphothreonine|||Phosphothreonine; by MAPK14|||Polar residues|||Reduced DNA binding activity.|||Reduced acetylation by 30%. Some loss of DNA binding and transactivation activity.|||Transcription repressor ^@ http://purl.uniprot.org/annotation/PRO_0000199434|||http://purl.uniprot.org/annotation/VSP_012501|||http://purl.uniprot.org/annotation/VSP_012502|||http://purl.uniprot.org/annotation/VSP_012503|||http://purl.uniprot.org/annotation/VSP_012504|||http://purl.uniprot.org/annotation/VSP_012505 http://togogenome.org/gene/10090:Tada3 ^@ http://purl.uniprot.org/uniprot/Q8R0L9 ^@ 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.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Transcriptional adapter 3 ^@ http://purl.uniprot.org/annotation/PRO_0000072417|||http://purl.uniprot.org/annotation/VSP_009740|||http://purl.uniprot.org/annotation/VSP_009741 http://togogenome.org/gene/10090:Wdr83 ^@ http://purl.uniprot.org/uniprot/Q9DAJ4 ^@ 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.|||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_0000235264|||http://purl.uniprot.org/annotation/VSP_018417|||http://purl.uniprot.org/annotation/VSP_018418|||http://purl.uniprot.org/annotation/VSP_018419|||http://purl.uniprot.org/annotation/VSP_018420 http://togogenome.org/gene/10090:Pwwp3b ^@ http://purl.uniprot.org/uniprot/Q4VA55 ^@ 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|||PWWP|||PWWP domain-containing DNA repair factor 3B|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000257833 http://togogenome.org/gene/10090:Tprg ^@ http://purl.uniprot.org/uniprot/Q8CB49 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Tumor protein p63-regulated gene 1 protein|||hSac2 ^@ http://purl.uniprot.org/annotation/PRO_0000268826 http://togogenome.org/gene/10090:Mllt3 ^@ http://purl.uniprot.org/uniprot/A2AM29|||http://purl.uniprot.org/uniprot/Q3UIA3|||http://purl.uniprot.org/uniprot/Q9D2P1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ AF-9 ANC1 homology|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein AF-9|||YEATS ^@ http://purl.uniprot.org/annotation/PRO_0000305124 http://togogenome.org/gene/10090:Sesn2 ^@ http://purl.uniprot.org/uniprot/P58043 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region ^@ Basic and acidic residues|||C-terminal domain; mediates TORC1 regulation|||Cysteine sulfenic acid (-SOH) intermediate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-acetylmethionine|||N-terminal domain; mediates the alkylhydroperoxide reductase activity|||Phosphoserine|||Sestrin-2|||Unable to inhibit TORC1 signaling; when associated with A-419 and A-422.|||Unable to inhibit TORC1 signaling; when associated with A-419 and A-426.|||Unable to inhibit TORC1 signaling; when associated with A-422 and A-426. ^@ http://purl.uniprot.org/annotation/PRO_0000221182 http://togogenome.org/gene/10090:Dcaf10 ^@ http://purl.uniprot.org/uniprot/A2AKB9 ^@ 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.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000306834|||http://purl.uniprot.org/annotation/VSP_028514|||http://purl.uniprot.org/annotation/VSP_028515|||http://purl.uniprot.org/annotation/VSP_028516 http://togogenome.org/gene/10090:Zbtb46 ^@ http://purl.uniprot.org/uniprot/Q8BID6 ^@ 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 ^@ Acidic residues|||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 46 ^@ http://purl.uniprot.org/annotation/PRO_0000047747|||http://purl.uniprot.org/annotation/VSP_009387|||http://purl.uniprot.org/annotation/VSP_009388 http://togogenome.org/gene/10090:Klk4 ^@ http://purl.uniprot.org/uniprot/A0A1R3UDT0|||http://purl.uniprot.org/uniprot/Q9Z0M1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Kallikrein-4|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000436024|||http://purl.uniprot.org/annotation/PRO_5006493980|||http://purl.uniprot.org/annotation/PRO_5010330812 http://togogenome.org/gene/10090:Tpsg1 ^@ http://purl.uniprot.org/uniprot/E9QLD4|||http://purl.uniprot.org/uniprot/G3XA07 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5003244798 http://togogenome.org/gene/10090:Ccdc125 ^@ http://purl.uniprot.org/uniprot/G3UWA1|||http://purl.uniprot.org/uniprot/Q5U465 ^@ 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 ^@ Coiled-coil domain-containing protein 125|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288813|||http://purl.uniprot.org/annotation/VSP_025782|||http://purl.uniprot.org/annotation/VSP_025783|||http://purl.uniprot.org/annotation/VSP_025784|||http://purl.uniprot.org/annotation/VSP_026155 http://togogenome.org/gene/10090:S100a2 ^@ http://purl.uniprot.org/uniprot/J3QMC7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ S100/CaBP-9k-type calcium binding subdomain ^@ http://togogenome.org/gene/10090:Hoxa9 ^@ http://purl.uniprot.org/uniprot/P09631 ^@ Chain|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn ^@ Chain|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Turn ^@ Disordered|||Homeobox|||Homeobox protein Hox-A9|||In isoform HoxA-9T.|||Significant reduction in interaction with EIF4E.|||Symmetric dimethylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000200082|||http://purl.uniprot.org/annotation/VSP_002382|||http://purl.uniprot.org/annotation/VSP_002383 http://togogenome.org/gene/10090:Samt1b ^@ http://purl.uniprot.org/uniprot/A2BED8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Parpbp ^@ http://purl.uniprot.org/uniprot/A0A0R4J0G5|||http://purl.uniprot.org/uniprot/Q6IRT3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||PCNA-interacting partner ^@ http://purl.uniprot.org/annotation/PRO_0000280270 http://togogenome.org/gene/10090:Olfr765 ^@ http://purl.uniprot.org/uniprot/Q7TRI6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pdrg1 ^@ http://purl.uniprot.org/uniprot/P59048|||http://purl.uniprot.org/uniprot/Q3UKN2 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ p53 and DNA damage-regulated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000058278 http://togogenome.org/gene/10090:Mrgpra1 ^@ http://purl.uniprot.org/uniprot/G3UW97|||http://purl.uniprot.org/uniprot/Q91WW5 ^@ 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|||Mas-related G-protein coupled receptor member A1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069747 http://togogenome.org/gene/10090:Cd300ld ^@ http://purl.uniprot.org/uniprot/Q8VCH2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ CMRF35-like molecule 5|||Cytoplasmic|||Decreases surface expression in transfected pro-B cells and impairs interaction with FCER1G.|||Extracellular|||Helical|||Ig-like V-type|||Important for maintaining surface expression and for interaction with FCER1G|||Increases surface expression in transfected pro-B cells and impairs interaction with FCER1G.|||May play an important role in murine norovirus (MNV) binding ^@ http://purl.uniprot.org/annotation/PRO_0000320128 http://togogenome.org/gene/10090:Pxn ^@ http://purl.uniprot.org/uniprot/F8VQ28|||http://purl.uniprot.org/uniprot/Q8VI36 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform Alpha.|||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|||N-acetylmethionine|||Paxillin|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by PTK6|||Polar residues|||Required for binding to PARVA and ILK ^@ http://purl.uniprot.org/annotation/PRO_0000075854|||http://purl.uniprot.org/annotation/VSP_016357 http://togogenome.org/gene/10090:Or1e32 ^@ http://purl.uniprot.org/uniprot/Q7TRX6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wdr86 ^@ http://purl.uniprot.org/uniprot/D3Z757 ^@ Region|||Repeat ^@ Repeat ^@ WD ^@ http://togogenome.org/gene/10090:Ctnna3 ^@ http://purl.uniprot.org/uniprot/Q65CL1 ^@ 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|||Catenin alpha-3|||Disordered|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000064267 http://togogenome.org/gene/10090:Aox4 ^@ http://purl.uniprot.org/uniprot/Q3TYQ9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ 2Fe-2S ferredoxin-type|||Aldehyde oxidase 4|||FAD-binding PCMH-type|||Proton acceptor; for azaheterocycle hydroxylase activity ^@ http://purl.uniprot.org/annotation/PRO_0000425250 http://togogenome.org/gene/10090:Slc6a12 ^@ http://purl.uniprot.org/uniprot/G5E8Z4|||http://purl.uniprot.org/uniprot/Q8VCS9 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Ahcyl1 ^@ http://purl.uniprot.org/uniprot/Q80SW1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||Does not inhibit interaction with ITPR1.|||Inhibits SLC4A4 dephosphorylation by PP1 phosphatase and activity.|||Inhibits interaction with ITPR1.|||Interaction with BCL2L10|||N-acetylserine|||N6-acetyllysine|||NAD binding|||PDZ-binding|||PEST|||Phosphoserine|||Phosphoserine; by PKD|||Polar residues|||Removed|||S-adenosylhomocysteine hydrolase-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000230300 http://togogenome.org/gene/10090:Piezo2 ^@ http://purl.uniprot.org/uniprot/E9QNW4|||http://purl.uniprot.org/uniprot/Q8CD54|||http://purl.uniprot.org/uniprot/S4R2S0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Piezo|||Piezo non-specific cation channel R-Ras-binding|||Piezo-type mechanosensitive ion channel component 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000186819|||http://purl.uniprot.org/annotation/VSP_040473|||http://purl.uniprot.org/annotation/VSP_040474|||http://purl.uniprot.org/annotation/VSP_040631|||http://purl.uniprot.org/annotation/VSP_040632 http://togogenome.org/gene/10090:Nbl1 ^@ http://purl.uniprot.org/uniprot/Q61477 ^@ 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 ^@ CTCK|||Disordered|||Neuroblastoma suppressor of tumorigenicity 1 ^@ http://purl.uniprot.org/annotation/PRO_0000006723 http://togogenome.org/gene/10090:Hacl1 ^@ http://purl.uniprot.org/uniprot/Q9QXE0 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 2-hydroxyacyl-CoA lyase 1|||Microbody targeting signal|||N6-succinyllysine|||Phosphoserine|||Thiamine pyrophosphate binding ^@ http://purl.uniprot.org/annotation/PRO_0000090817 http://togogenome.org/gene/10090:Cdh18 ^@ http://purl.uniprot.org/uniprot/E9Q9Q6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245869 http://togogenome.org/gene/10090:Or4b12 ^@ http://purl.uniprot.org/uniprot/Q8VG62 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Spink10 ^@ http://purl.uniprot.org/uniprot/Q8CAC8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Site|||Transmembrane ^@ Helical|||Kazal-like 1|||Kazal-like 2|||Reactive bond|||Serine protease inhibitor Kazal-type 10 ^@ http://purl.uniprot.org/annotation/PRO_0000302141 http://togogenome.org/gene/10090:Sync ^@ http://purl.uniprot.org/uniprot/C0LQ87|||http://purl.uniprot.org/uniprot/C0LQ88|||http://purl.uniprot.org/uniprot/C0LQ89|||http://purl.uniprot.org/uniprot/Q9EPM5 ^@ 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 ^@ Coil 1A|||Coil 1b|||Coil 2|||Disordered|||Head|||IF rod|||In isoform 2.|||In isoform 3.|||Linker 1|||Linker 2|||Phosphoserine|||Polar residues|||Syncoilin|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000306181|||http://purl.uniprot.org/annotation/VSP_052550|||http://purl.uniprot.org/annotation/VSP_052551|||http://purl.uniprot.org/annotation/VSP_052552 http://togogenome.org/gene/10090:Dynlrb1 ^@ http://purl.uniprot.org/uniprot/A2AVR9|||http://purl.uniprot.org/uniprot/P62627 ^@ 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 ^@ Dynein light chain roadblock-type 1|||N-acetylalanine|||Removed|||Roadblock/LAMTOR2 ^@ http://purl.uniprot.org/annotation/PRO_0000220956 http://togogenome.org/gene/10090:Dipk1b ^@ http://purl.uniprot.org/uniprot/Q99ML4 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Divergent protein kinase domain 1B|||Helical|||Lumenal|||May mediate ER retention ^@ http://purl.uniprot.org/annotation/PRO_0000287232 http://togogenome.org/gene/10090:Mpv17 ^@ http://purl.uniprot.org/uniprot/E9Q1I6|||http://purl.uniprot.org/uniprot/G3UVW1|||http://purl.uniprot.org/uniprot/P19258 ^@ Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Chain|||Site|||Transmembrane ^@ Determines ion selectivity|||Helical|||Protein Mpv17 ^@ http://purl.uniprot.org/annotation/PRO_0000218928 http://togogenome.org/gene/10090:Tusc3 ^@ http://purl.uniprot.org/uniprot/Q8BTV1 ^@ 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|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Redox-active|||Thioredoxin|||Tumor suppressor candidate 3 ^@ http://purl.uniprot.org/annotation/PRO_0000414923 http://togogenome.org/gene/10090:Serp2 ^@ http://purl.uniprot.org/uniprot/Q6TAW2 ^@ 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; Anchor for type IV membrane protein|||In isoform 2.|||Lumenal|||Stress-associated endoplasmic reticulum protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000274800|||http://purl.uniprot.org/annotation/VSP_022876|||http://purl.uniprot.org/annotation/VSP_022877 http://togogenome.org/gene/10090:Ophn1 ^@ http://purl.uniprot.org/uniprot/Q8CA59|||http://purl.uniprot.org/uniprot/Q99J31 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ BAR|||Basic and acidic residues|||Disordered|||Oligophrenin-1|||PH|||Polar residues|||Pro residues|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000056761 http://togogenome.org/gene/10090:Hmox1 ^@ http://purl.uniprot.org/uniprot/P14901|||http://purl.uniprot.org/uniprot/Q3U5U6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||Heme oxygenase 1|||Heme oxygenase 1 soluble form|||Important for catalytic activity|||Phosphoserine|||Polar residues|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000209688|||http://purl.uniprot.org/annotation/PRO_0000455622 http://togogenome.org/gene/10090:Bax ^@ http://purl.uniprot.org/uniprot/Q07813|||http://purl.uniprot.org/uniprot/Q544Z6 ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Transmembrane|||Turn ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Transmembrane|||Turn ^@ Apoptosis regulator BAX|||BH1|||BH2|||BH3|||Bcl-2 Bcl-2 homology region 1-3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000143057 http://togogenome.org/gene/10090:Cers1 ^@ http://purl.uniprot.org/uniprot/A2RT05|||http://purl.uniprot.org/uniprot/P27545 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Transmembrane ^@ Ceramide synthase 1|||Decreased ceramide synthase activity.|||Does not affect ceramide synthase activity.|||Helical|||In toppler (to) mice; impairs ceramide synthase activity.|||N-acetylalanine|||Removed|||TLC ^@ http://purl.uniprot.org/annotation/PRO_0000185508 http://togogenome.org/gene/10090:Umps ^@ http://purl.uniprot.org/uniprot/P13439|||http://purl.uniprot.org/uniprot/Q544K9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Domain linker|||For OMPdecase activity|||OMPdecase|||OPRTase|||Orotidine 5'-phosphate decarboxylase|||Phosphotyrosine|||Uridine 5'-monophosphate synthase ^@ http://purl.uniprot.org/annotation/PRO_0000139650 http://togogenome.org/gene/10090:Mtm1 ^@ http://purl.uniprot.org/uniprot/B1AW21|||http://purl.uniprot.org/uniprot/Q3UDN6|||http://purl.uniprot.org/uniprot/Q9D4L1|||http://purl.uniprot.org/uniprot/Q9Z2C5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||GRAM|||Myotubularin|||Myotubularin phosphatase|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tyrosine specific protein phosphatases ^@ http://purl.uniprot.org/annotation/PRO_0000094931 http://togogenome.org/gene/10090:Wfdc11 ^@ http://purl.uniprot.org/uniprot/A2A5H7 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Protein WFDC11 ^@ http://purl.uniprot.org/annotation/PRO_0000415847 http://togogenome.org/gene/10090:Ahsg ^@ http://purl.uniprot.org/uniprot/P29699|||http://purl.uniprot.org/uniprot/Q3UEK9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Alpha-2-HS-glycoprotein|||Cystatin fetuin-A-type|||Cystatin fetuin-A-type 1|||Cystatin fetuin-A-type 2|||Disordered|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000008891|||http://purl.uniprot.org/annotation/PRO_5014309192 http://togogenome.org/gene/10090:Sp8 ^@ http://purl.uniprot.org/uniprot/Q5QR90|||http://purl.uniprot.org/uniprot/Q8BMJ8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Zinc Finger ^@ 9aaTAD|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Polar residues|||Transcription factor Sp8 ^@ http://purl.uniprot.org/annotation/PRO_0000047153 http://togogenome.org/gene/10090:Ubr7 ^@ http://purl.uniprot.org/uniprot/Q52KC0|||http://purl.uniprot.org/uniprot/Q8BU04 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||PHD-type; atypical|||Phosphoserine|||Polar residues|||Putative E3 ubiquitin-protein ligase UBR7|||UBR-type ^@ http://purl.uniprot.org/annotation/PRO_0000089933 http://togogenome.org/gene/10090:Pax7 ^@ http://purl.uniprot.org/uniprot/G3UX36|||http://purl.uniprot.org/uniprot/P47239 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Homeobox|||OAR|||PAI subdomain|||Paired|||Paired box protein Pax-7|||RED subdomain|||Sufficient to mediate interaction with PAXBP1 ^@ http://purl.uniprot.org/annotation/PRO_0000050195 http://togogenome.org/gene/10090:Cdca2 ^@ http://purl.uniprot.org/uniprot/Q14B71 ^@ 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|||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_0000287696|||http://purl.uniprot.org/annotation/VSP_025600|||http://purl.uniprot.org/annotation/VSP_025601 http://togogenome.org/gene/10090:Gm973 ^@ http://purl.uniprot.org/uniprot/E9Q295|||http://purl.uniprot.org/uniprot/Q6GQX7 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ildr1 ^@ http://purl.uniprot.org/uniprot/Q8CBR1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||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|||Modified Residue|||Region|||Sequence Conflict|||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 isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000245305|||http://purl.uniprot.org/annotation/VSP_019688|||http://purl.uniprot.org/annotation/VSP_019689|||http://purl.uniprot.org/annotation/VSP_019690 http://togogenome.org/gene/10090:Spata46 ^@ http://purl.uniprot.org/uniprot/Q4FZF2 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Spermatogenesis-associated protein 46 ^@ http://purl.uniprot.org/annotation/PRO_0000279460 http://togogenome.org/gene/10090:Or5m13b ^@ http://purl.uniprot.org/uniprot/Q7TR90 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fbxl4 ^@ http://purl.uniprot.org/uniprot/Q8BH70|||http://purl.uniprot.org/uniprot/V9GXH8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Modified Residue|||Repeat ^@ Asymmetric dimethylarginine|||F-box|||F-box/LRR-repeat protein 4|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9 ^@ http://purl.uniprot.org/annotation/PRO_0000307719 http://togogenome.org/gene/10090:Nat8f2 ^@ http://purl.uniprot.org/uniprot/Q8CHQ9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||N-acetyltransferase|||N-acetyltransferase family 8 member 2|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000284688 http://togogenome.org/gene/10090:Ephx3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J127|||http://purl.uniprot.org/uniprot/G3XA19|||http://purl.uniprot.org/uniprot/Q3V1F8 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ AB hydrolase-1|||Disordered|||Epoxide hydrolase 3|||Helical|||Nucleophile|||Polar residues|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000264233 http://togogenome.org/gene/10090:C1qtnf3 ^@ http://purl.uniprot.org/uniprot/D3YZ61|||http://purl.uniprot.org/uniprot/Q4ZJN6|||http://purl.uniprot.org/uniprot/Q9ES30 ^@ 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 3|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000003532|||http://purl.uniprot.org/annotation/PRO_5003052753|||http://purl.uniprot.org/annotation/PRO_5014309460 http://togogenome.org/gene/10090:Tfe3 ^@ http://purl.uniprot.org/uniprot/A2AEW0|||http://purl.uniprot.org/uniprot/A2AEW1|||http://purl.uniprot.org/uniprot/Q3U1L5|||http://purl.uniprot.org/uniprot/Q64092|||http://purl.uniprot.org/uniprot/Q8K420 ^@ 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|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Asymmetric dimethylarginine|||BHLH|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired phosphorylation by MTOR, leading to constitutive nuclear localization.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Leucine-zipper|||MiT/TFE transcription factors N-terminal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by MTOR|||Polar residues|||Strong transcription activation domain|||Transcription factor E3|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127472|||http://purl.uniprot.org/annotation/VSP_022143|||http://purl.uniprot.org/annotation/VSP_022144 http://togogenome.org/gene/10090:Rcn2 ^@ http://purl.uniprot.org/uniprot/Q8BP39|||http://purl.uniprot.org/uniprot/Q8BP92 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||Phosphothreonine|||Prevents secretion from ER|||Reticulocalbin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000004149 http://togogenome.org/gene/10090:Pdf ^@ http://purl.uniprot.org/uniprot/S4R2K0 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Region|||Transit Peptide ^@ Hydrophobic dimerization interface|||Mitochondrion|||Peptide deformylase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000455155 http://togogenome.org/gene/10090:Nvl ^@ http://purl.uniprot.org/uniprot/Q9DBY8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with RPL5|||Interaction with WDR74|||N6-acetyllysine|||Nuclear localization signal|||Nuclear valosin-containing protein-like|||Nucleolar localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084589 http://togogenome.org/gene/10090:Cd53 ^@ http://purl.uniprot.org/uniprot/Q3TV80|||http://purl.uniprot.org/uniprot/Q3U0W1|||http://purl.uniprot.org/uniprot/Q61451 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Leukocyte surface antigen CD53|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219213 http://togogenome.org/gene/10090:Vmn1r5 ^@ http://purl.uniprot.org/uniprot/B2RQT2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:F10 ^@ http://purl.uniprot.org/uniprot/O88947|||http://purl.uniprot.org/uniprot/Q3TBR2|||http://purl.uniprot.org/uniprot/Q3U3V1|||http://purl.uniprot.org/uniprot/Q80Y26 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||Activated factor Xa heavy chain|||Activation peptide|||Charge relay system|||Coagulation factor X|||EGF-like|||EGF-like 1; calcium-binding|||EGF-like 2|||Factor X heavy chain|||Factor X light chain|||Gla|||Interchain (between light and heavy chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027792|||http://purl.uniprot.org/annotation/PRO_0000027793|||http://purl.uniprot.org/annotation/PRO_0000027794|||http://purl.uniprot.org/annotation/PRO_0000027795|||http://purl.uniprot.org/annotation/PRO_0000027796|||http://purl.uniprot.org/annotation/PRO_0000027797|||http://purl.uniprot.org/annotation/PRO_5014309137 http://togogenome.org/gene/10090:Garin1b ^@ http://purl.uniprot.org/uniprot/B7XG46|||http://purl.uniprot.org/uniprot/B7ZWJ6|||http://purl.uniprot.org/uniprot/Q3UZD7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Golgi associated RAB2 interactor protein-like Rab2B-binding|||Golgi-associated RAB2 interactor protein 1B ^@ http://purl.uniprot.org/annotation/PRO_0000311687 http://togogenome.org/gene/10090:Chpf ^@ http://purl.uniprot.org/uniprot/Q6IQX7 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Region|||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_0000189561|||http://purl.uniprot.org/annotation/VSP_053435|||http://purl.uniprot.org/annotation/VSP_053436 http://togogenome.org/gene/10090:Nectin4 ^@ http://purl.uniprot.org/uniprot/Q8R007 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nectin-4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000297674|||http://purl.uniprot.org/annotation/VSP_027336 http://togogenome.org/gene/10090:Pin1 ^@ http://purl.uniprot.org/uniprot/Q9QUR7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N6-acetyllysine|||Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1|||Phosphoserine|||Polar residues|||PpiC|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000193436 http://togogenome.org/gene/10090:Reg1 ^@ http://purl.uniprot.org/uniprot/P43137|||http://purl.uniprot.org/uniprot/Q3TV26 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide ^@ C-type lectin|||C-type lectin domain-containing protein|||Lithostathine-1|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000017426|||http://purl.uniprot.org/annotation/PRO_5014309146 http://togogenome.org/gene/10090:Cic ^@ http://purl.uniprot.org/uniprot/Q924A2 ^@ 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 ^@ Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||HMG box|||In isoform 2.|||Interaction with ATXN1|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein capicua homolog ^@ http://purl.uniprot.org/annotation/PRO_0000048599|||http://purl.uniprot.org/annotation/VSP_026140|||http://purl.uniprot.org/annotation/VSP_026141|||http://purl.uniprot.org/annotation/VSP_039804 http://togogenome.org/gene/10090:Or4c126 ^@ http://purl.uniprot.org/uniprot/Q8VFB0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:2810459M11Rik ^@ http://purl.uniprot.org/uniprot/B7ZMV2|||http://purl.uniprot.org/uniprot/Q9CYS6 ^@ 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 C2orf72 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000339301|||http://purl.uniprot.org/annotation/VSP_040798 http://togogenome.org/gene/10090:Or8k53 ^@ http://purl.uniprot.org/uniprot/A2AVX9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dpm3 ^@ http://purl.uniprot.org/uniprot/Q9D1Q4 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Dolichol-phosphate mannosyltransferase subunit 3|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000195001 http://togogenome.org/gene/10090:Klk1b26 ^@ http://purl.uniprot.org/uniprot/A0A1R3UDC2|||http://purl.uniprot.org/uniprot/P36369 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Kallikrein 1-related peptidase b26|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027993|||http://purl.uniprot.org/annotation/PRO_0000027994|||http://purl.uniprot.org/annotation/PRO_5010276282 http://togogenome.org/gene/10090:Kank2 ^@ http://purl.uniprot.org/uniprot/Q8BX02 ^@ 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 ^@ ANK 0; degenerate|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with AIFM1|||Interaction with NCOA1|||KN motif and ankyrin repeat domain-containing protein 2|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000240841|||http://purl.uniprot.org/annotation/VSP_019430|||http://purl.uniprot.org/annotation/VSP_019431 http://togogenome.org/gene/10090:Serpinb9g ^@ http://purl.uniprot.org/uniprot/Q8VHQ1|||http://purl.uniprot.org/uniprot/Q9DAZ7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Dcstamp ^@ http://purl.uniprot.org/uniprot/A0A2I3BPX1|||http://purl.uniprot.org/uniprot/Q7TNJ0 ^@ 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|||Dendritic cell-specific transmembrane protein|||Dendritic cell-specific transmembrane protein-like|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4. ^@ http://purl.uniprot.org/annotation/PRO_0000072585|||http://purl.uniprot.org/annotation/VSP_051763|||http://purl.uniprot.org/annotation/VSP_051764|||http://purl.uniprot.org/annotation/VSP_051765 http://togogenome.org/gene/10090:Zfp169 ^@ http://purl.uniprot.org/uniprot/E9Q3R6|||http://purl.uniprot.org/uniprot/G5E912|||http://purl.uniprot.org/uniprot/Q6PAM4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Defa29 ^@ http://purl.uniprot.org/uniprot/Q9D815 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Alpha-defensin N-terminal|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015099691 http://togogenome.org/gene/10090:Aoah ^@ http://purl.uniprot.org/uniprot/O35298|||http://purl.uniprot.org/uniprot/Q5FW74 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Site|||Strand|||Turn ^@ Acyloxyacyl hydrolase large subunit|||Acyloxyacyl hydrolase small subunit|||Important for enzyme activity, localization to cytoplasmic vesicles, and protein stability|||Interacts with lipopolysaccharide|||Interchain (between small and large subunit)|||Lipopolysaccharide binding|||Loss of catalytic activity.|||N-linked (GlcNAc...) asparagine|||Saposin B-type ^@ http://purl.uniprot.org/annotation/PRO_0000041812|||http://purl.uniprot.org/annotation/PRO_0000041813|||http://purl.uniprot.org/annotation/PRO_0000041814|||http://purl.uniprot.org/annotation/PRO_5015097881 http://togogenome.org/gene/10090:Nono ^@ http://purl.uniprot.org/uniprot/Q4FK11|||http://purl.uniprot.org/uniprot/Q99K48 ^@ Chain|||Coiled-Coil|||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|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ 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_0000081684|||http://purl.uniprot.org/annotation/VSP_013981 http://togogenome.org/gene/10090:Drd3 ^@ http://purl.uniprot.org/uniprot/A0A2R8VHF0|||http://purl.uniprot.org/uniprot/P30728|||http://purl.uniprot.org/uniprot/Q0VEC4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 D3Short.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069398|||http://purl.uniprot.org/annotation/VSP_001873 http://togogenome.org/gene/10090:Smr2 ^@ http://purl.uniprot.org/uniprot/O35979|||http://purl.uniprot.org/uniprot/O35985 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Disordered|||Polar residues|||Submaxillary gland androgen-regulated protein 2, isoform delta|||Submaxillary gland androgen-regulated protein 2, isoform gamma ^@ http://purl.uniprot.org/annotation/PRO_0000022376|||http://purl.uniprot.org/annotation/PRO_0000022377 http://togogenome.org/gene/10090:Ranbp6 ^@ http://purl.uniprot.org/uniprot/Q8BIV3 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||N-acetylalanine|||Ran-binding protein 6|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000120780 http://togogenome.org/gene/10090:Hif3a ^@ http://purl.uniprot.org/uniprot/Q0VBL6 ^@ Chain|||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|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ 4-hydroxyproline|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hypoxia-inducible factor 3-alpha|||In isoform 2 and isoform 3.|||In isoform 2.|||LAPYISMD|||LRRLL|||NTAD|||Nuclear export signal (isoform 2)|||Nuclear localization signal (isoform 2)|||ODD|||PAS 1|||PAS 2|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000284415|||http://purl.uniprot.org/annotation/VSP_024528|||http://purl.uniprot.org/annotation/VSP_024529|||http://purl.uniprot.org/annotation/VSP_024530|||http://purl.uniprot.org/annotation/VSP_024531 http://togogenome.org/gene/10090:Srpr ^@ http://purl.uniprot.org/uniprot/Q9DBG7 ^@ 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|||NG domain|||Phosphoserine|||Phosphothreonine|||Polar residues|||Signal recognition particle receptor subunit alpha ^@ http://purl.uniprot.org/annotation/PRO_0000101214 http://togogenome.org/gene/10090:Eif4g3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J112|||http://purl.uniprot.org/uniprot/A2AMI2|||http://purl.uniprot.org/uniprot/Q80XI3 ^@ 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|||EIF4A-binding|||EIF4E-binding|||Eukaryotic translation initiation factor 4 gamma 3|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||In isoform 2 and isoform 4.|||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|||W2|||eIF3/EIF4A-binding ^@ http://purl.uniprot.org/annotation/PRO_0000213330|||http://purl.uniprot.org/annotation/VSP_010490|||http://purl.uniprot.org/annotation/VSP_010491|||http://purl.uniprot.org/annotation/VSP_026029 http://togogenome.org/gene/10090:Klra5 ^@ http://purl.uniprot.org/uniprot/Q548A2|||http://purl.uniprot.org/uniprot/Q60652 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Killer cell lectin-like receptor 5|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046683 http://togogenome.org/gene/10090:Tmem216 ^@ http://purl.uniprot.org/uniprot/Q9CQC4 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Transmembrane protein 216 ^@ http://purl.uniprot.org/annotation/PRO_0000318956|||http://purl.uniprot.org/annotation/VSP_040297 http://togogenome.org/gene/10090:Plxnb3 ^@ http://purl.uniprot.org/uniprot/Q9QY40 ^@ 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|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||N-linked (GlcNAc...) asparagine|||PSI 1|||PSI 2|||PSI 3|||Plexin-B3|||Sema ^@ http://purl.uniprot.org/annotation/PRO_0000024675 http://togogenome.org/gene/10090:Lrrc8a ^@ http://purl.uniprot.org/uniprot/Q80WG5 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Di-leucine motif|||Extracellular|||Helical|||In ebo; causes male sterility.|||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-acetylmethionine|||N-linked (GlcNAc...) asparagine|||No effect on anion channel activity. Impairs channel selectivity, so that the channel is also permeable to Na(+) ions.|||Phosphoserine|||Phosphothreonine|||Required for anion selectivity|||Volume-regulated anion channel subunit LRRC8A ^@ http://purl.uniprot.org/annotation/PRO_0000084500 http://togogenome.org/gene/10090:Rere ^@ http://purl.uniprot.org/uniprot/Q80TZ9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SANT ^@ http://purl.uniprot.org/annotation/PRO_0000083505 http://togogenome.org/gene/10090:Rasal3 ^@ http://purl.uniprot.org/uniprot/Q8C2K5|||http://purl.uniprot.org/uniprot/Q8CAS7 ^@ 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 ^@ C2|||Disordered|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||RAS protein activator like-3|||Ras-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000322567|||http://purl.uniprot.org/annotation/VSP_031931|||http://purl.uniprot.org/annotation/VSP_031932 http://togogenome.org/gene/10090:Actn2 ^@ http://purl.uniprot.org/uniprot/Q5FW75|||http://purl.uniprot.org/uniprot/Q9JI91 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Actin-binding|||Alpha-actinin-2|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||EF-hand|||EF-hand 1|||EF-hand 2|||Phosphothreonine|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4 ^@ http://purl.uniprot.org/annotation/PRO_0000073436 http://togogenome.org/gene/10090:Arsj ^@ http://purl.uniprot.org/uniprot/Q32KI8|||http://purl.uniprot.org/uniprot/Q8BM89 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide ^@ 3-oxoalanine (Cys)|||Arylsulfatase J|||Basic residues|||Disordered|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Sulfatase N-terminal|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000042218 http://togogenome.org/gene/10090:Xylt2 ^@ http://purl.uniprot.org/uniprot/Q3TZ69|||http://purl.uniprot.org/uniprot/Q3UCI0|||http://purl.uniprot.org/uniprot/Q9EPL0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Xylosyltransferase 2|||Xylosyltransferase C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000191407 http://togogenome.org/gene/10090:Unc45a ^@ http://purl.uniprot.org/uniprot/Q99KD5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||N6-acetyllysine|||Protein unc-45 homolog A|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000249889 http://togogenome.org/gene/10090:Furin ^@ http://purl.uniprot.org/uniprot/P23188 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||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|||Propeptide|||Region|||Repeat|||Sequence Conflict|||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|||Inhibition peptide|||Lumenal|||N-linked (GlcNAc...) asparagine|||P/Homo B|||Peptidase S8|||Phosphoserine|||Polar residues|||Trans Golgi network signal ^@ http://purl.uniprot.org/annotation/PRO_0000027030|||http://purl.uniprot.org/annotation/PRO_0000027031 http://togogenome.org/gene/10090:Smad6 ^@ http://purl.uniprot.org/uniprot/O35182 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Dimethylated arginine; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||MH1|||MH2|||Mothers against decapentaplegic homolog 6|||Omega-N-methylarginine; alternate|||Phosphoserine; by PRKX; in vitro|||Strongly decreased methylation. ^@ http://purl.uniprot.org/annotation/PRO_0000090870 http://togogenome.org/gene/10090:Ubtf ^@ http://purl.uniprot.org/uniprot/A2AWT5|||http://purl.uniprot.org/uniprot/A2AWT6|||http://purl.uniprot.org/uniprot/A2AWT7|||http://purl.uniprot.org/uniprot/Q9DBH1 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||HMG box|||Polar residues ^@ http://togogenome.org/gene/10090:Ces3a ^@ http://purl.uniprot.org/uniprot/Q63880 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Acyl-ester intermediate|||Carboxylesterase 3A|||Charge relay system|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000008575|||http://purl.uniprot.org/annotation/VSP_028268 http://togogenome.org/gene/10090:Aspm ^@ http://purl.uniprot.org/uniprot/Q8CJ27 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abnormal spindle-like microcephaly-associated protein homolog|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Disrupts interaction with KATNA1:KATNB1.|||Disrupts interaction with KATNA1:KATNB1; when associated with A-302.|||Disrupts interaction with KATNA1:KATNB1; when associated with A-377.|||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 4|||IQ 5|||IQ 6|||IQ 7|||IQ 8|||IQ 9|||In isoform 2.|||Phosphoserine|||Sufficient for interaction with KATNA1:KATNB1 ^@ http://purl.uniprot.org/annotation/PRO_0000191336|||http://purl.uniprot.org/annotation/VSP_059014 http://togogenome.org/gene/10090:Scn4b ^@ http://purl.uniprot.org/uniprot/Q1MXF9|||http://purl.uniprot.org/uniprot/Q7M729 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Interchain; with alpha subunit|||N-linked (GlcNAc...) asparagine|||Sodium channel subunit beta-4 ^@ http://purl.uniprot.org/annotation/PRO_0000014938 http://togogenome.org/gene/10090:Serpini2 ^@ http://purl.uniprot.org/uniprot/Q4G0D3|||http://purl.uniprot.org/uniprot/Q9JK88 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site ^@ N-linked (GlcNAc...) asparagine|||Reactive bond|||Serpin|||Serpin I2 ^@ http://purl.uniprot.org/annotation/PRO_0000032526|||http://purl.uniprot.org/annotation/PRO_5014309356 http://togogenome.org/gene/10090:Cyp2c37 ^@ http://purl.uniprot.org/uniprot/P56654|||http://purl.uniprot.org/uniprot/Q9DBD9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Cytochrome P450 2C37|||N6-acetyllysine|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051720|||http://purl.uniprot.org/annotation/PRO_5004324701 http://togogenome.org/gene/10090:Gm8271 ^@ http://purl.uniprot.org/uniprot/L7N2E2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tcf15 ^@ http://purl.uniprot.org/uniprot/Q60756 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disordered|||Does not affect formation of a heterodimer with TCF3 and ability to bind DNA.|||Impaired formation of a heterodimer with TCF3 and decreased ability to bind DNA.|||Phosphoserine|||Transcription factor 15|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127462 http://togogenome.org/gene/10090:Dmrtc1a ^@ http://purl.uniprot.org/uniprot/B1AX34|||http://purl.uniprot.org/uniprot/Q9D9R7 ^@ 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|||Doublesex- and mab-3-related transcription factor C1|||Doublesex- and mab-3-related transcription factor C1/C2 C-terminal|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000244103|||http://purl.uniprot.org/annotation/VSP_019522|||http://purl.uniprot.org/annotation/VSP_019523|||http://purl.uniprot.org/annotation/VSP_019524 http://togogenome.org/gene/10090:Ldlrap1 ^@ http://purl.uniprot.org/uniprot/Q8C142 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ AP-2 complex binding|||Clathrin box|||Disordered|||Low density lipoprotein receptor adapter protein 1|||N-acetylmethionine|||PID|||Phosphoserine|||[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif ^@ http://purl.uniprot.org/annotation/PRO_0000064676 http://togogenome.org/gene/10090:Tmem106a ^@ http://purl.uniprot.org/uniprot/Q8VC04 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 106A ^@ http://purl.uniprot.org/annotation/PRO_0000242138 http://togogenome.org/gene/10090:Zbtb48 ^@ http://purl.uniprot.org/uniprot/Q1H9T6 ^@ 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 ^@ BTB|||Basic and acidic residues|||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)|||In isoform 2.|||Polar residues|||Telomere zinc finger-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000292136|||http://purl.uniprot.org/annotation/VSP_026381 http://togogenome.org/gene/10090:Gas1 ^@ http://purl.uniprot.org/uniprot/A0A286YD87|||http://purl.uniprot.org/uniprot/Q01721 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||GDNF/GAS1|||GPI-anchor amidated serine|||Growth arrest-specific protein 1|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000021320|||http://purl.uniprot.org/annotation/PRO_0000021321 http://togogenome.org/gene/10090:Srebf1 ^@ http://purl.uniprot.org/uniprot/Q9WTN3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ 9aaTAD|||Abolishes AMPK-mediated phosphorylation.|||Cleavage; by MBTPS1|||Cleavage; by MBTPS2|||Cleavage; by caspase-3 and caspase-7|||Cytoplasmic|||Disordered|||Does not affect AMPK-mediated phosphorylation.|||Helical|||In isoform SREBP-1A-W42 and isoform SREBP-1C-W42.|||In isoform SREBP-1C and isoform SREBP-1C-W42.|||Interaction with LMNA|||Leucine-zipper|||Lumenal|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by SIK1|||Polar residues|||Processed sterol regulatory element-binding protein 1|||Sterol regulatory element-binding protein 1|||Strongly impairs affects phosphorylation by SIK1.|||Transcriptional activation (acidic)|||Weakly affects phosphorylation by SIK1.|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127448|||http://purl.uniprot.org/annotation/PRO_0000314030|||http://purl.uniprot.org/annotation/VSP_002151|||http://purl.uniprot.org/annotation/VSP_002152 http://togogenome.org/gene/10090:Clic6 ^@ http://purl.uniprot.org/uniprot/Q8BHB9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Transmembrane|||Turn ^@ Basic and acidic residues|||Chloride intracellular channel protein 6|||Disordered|||GST C-terminal|||Helical; Note=After insertion into the membrane|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000144218 http://togogenome.org/gene/10090:Apela ^@ http://purl.uniprot.org/uniprot/P0DMC4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Sequence Conflict|||Signal Peptide ^@ Apelin receptor early endogenous ligand ^@ http://purl.uniprot.org/annotation/PRO_0000425558 http://togogenome.org/gene/10090:Ankdd1b ^@ http://purl.uniprot.org/uniprot/Q14DN9 ^@ 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 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and death domain-containing protein 1B|||Death|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000332161|||http://purl.uniprot.org/annotation/VSP_046263 http://togogenome.org/gene/10090:Irs4 ^@ http://purl.uniprot.org/uniprot/Q9Z0Y7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||CRK-binding|||Disordered|||GRB2-binding|||IRS-type PTB|||Insulin receptor substrate 4|||PH|||Phosphotyrosine|||Polar 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_0000314679 http://togogenome.org/gene/10090:Ift88 ^@ http://purl.uniprot.org/uniprot/G3X9Z7|||http://purl.uniprot.org/uniprot/Q3TUP2|||http://purl.uniprot.org/uniprot/Q61371 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Intraflagellar transport protein 88 homolog|||Polar residues|||TPR|||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_0000106392 http://togogenome.org/gene/10090:Tmed9 ^@ http://purl.uniprot.org/uniprot/Q6PDC2|||http://purl.uniprot.org/uniprot/Q99KF1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||GOLD|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Required for interaction with STX17|||Transmembrane emp24 domain-containing protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000010397 http://togogenome.org/gene/10090:Evi2b ^@ http://purl.uniprot.org/uniprot/Q8VD58 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein EVI2B ^@ http://purl.uniprot.org/annotation/PRO_0000021214 http://togogenome.org/gene/10090:Mthfd2 ^@ http://purl.uniprot.org/uniprot/P18155 ^@ Binding Site|||Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Transit Peptide ^@ Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Mitochondrion|||N6-acetyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000034050 http://togogenome.org/gene/10090:Bod1 ^@ http://purl.uniprot.org/uniprot/Q5SQY2 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Biorientation of chromosomes in cell division protein 1|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000187029 http://togogenome.org/gene/10090:Prelp ^@ http://purl.uniprot.org/uniprot/Q543S0|||http://purl.uniprot.org/uniprot/Q8CAZ9|||http://purl.uniprot.org/uniprot/Q9JK53 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||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|||LRRNT|||LRRNT domain-containing protein|||N-linked (GlcNAc...) asparagine|||Pro residues|||Prolargin ^@ http://purl.uniprot.org/annotation/PRO_0000032745|||http://purl.uniprot.org/annotation/PRO_5004304037|||http://purl.uniprot.org/annotation/PRO_5014309599 http://togogenome.org/gene/10090:Trat1 ^@ http://purl.uniprot.org/uniprot/A0A338P6G9|||http://purl.uniprot.org/uniprot/Q3UU67 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||In isoform 3.|||Interaction with PIK3R1|||Interchain|||Phosphoserine|||Phosphotyrosine|||T-cell receptor-associated transmembrane adapter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000083345|||http://purl.uniprot.org/annotation/VSP_016638|||http://purl.uniprot.org/annotation/VSP_016639|||http://purl.uniprot.org/annotation/VSP_016640 http://togogenome.org/gene/10090:Shtn1 ^@ http://purl.uniprot.org/uniprot/Q8K2Q9 ^@ 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.|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by PAK1|||Phosphothreonine|||Polar residues|||Pro residues|||Shootin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000295741|||http://purl.uniprot.org/annotation/VSP_027054|||http://purl.uniprot.org/annotation/VSP_027055 http://togogenome.org/gene/10090:Or11a4 ^@ http://purl.uniprot.org/uniprot/Q8VFE3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tdrd3 ^@ http://purl.uniprot.org/uniprot/Q91W18 ^@ 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|||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.|||Phosphoserine|||Polar residues|||Tudor|||Tudor domain-containing protein 3|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000183164|||http://purl.uniprot.org/annotation/VSP_034485|||http://purl.uniprot.org/annotation/VSP_037054 http://togogenome.org/gene/10090:Lce3d ^@ http://purl.uniprot.org/uniprot/E9Q8V1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rhpn1 ^@ http://purl.uniprot.org/uniprot/E9Q7Q7|||http://purl.uniprot.org/uniprot/Q61085|||http://purl.uniprot.org/uniprot/Q80WU2 ^@ 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 ^@ BRO1|||Disordered|||PDZ|||Phosphoserine|||Polar residues|||REM-1|||Rhophilin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000218896 http://togogenome.org/gene/10090:Ankrd34c ^@ http://purl.uniprot.org/uniprot/B2RPW9|||http://purl.uniprot.org/uniprot/Q8BLB8 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 34C|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000319105 http://togogenome.org/gene/10090:Yars2 ^@ http://purl.uniprot.org/uniprot/Q8BYL4 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Transit Peptide ^@ 'HIGH' region|||'KMSKS' region|||Mitochondrion|||N6-acetyllysine|||Tyrosine--tRNA ligase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000035831 http://togogenome.org/gene/10090:Dgkq ^@ http://purl.uniprot.org/uniprot/Q6P5E8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant|||Zinc Finger ^@ DAGKc|||Diacylglycerol kinase theta|||Disordered|||In isoform 2.|||LXXLL motif 1|||LXXLL motif 2|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phorbol-ester/DAG-type 3|||Phosphoserine|||Ras-associating ^@ http://purl.uniprot.org/annotation/PRO_0000381763|||http://purl.uniprot.org/annotation/VSP_037832 http://togogenome.org/gene/10090:Zfp647 ^@ http://purl.uniprot.org/uniprot/Q7TNU6 ^@ 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|||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|||Zinc finger protein 250 ^@ http://purl.uniprot.org/annotation/PRO_0000047484 http://togogenome.org/gene/10090:Glrx2 ^@ http://purl.uniprot.org/uniprot/A2A5W4|||http://purl.uniprot.org/uniprot/Q3UQ95|||http://purl.uniprot.org/uniprot/Q923X4 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Splice Variant|||Transit Peptide ^@ Glutaredoxin|||Glutaredoxin-2, mitochondrial|||In isoform 2.|||Mitochondrion|||Redox-active; alternate|||S-glutathionyl cysteine; alternate|||in inactive form ^@ http://purl.uniprot.org/annotation/PRO_0000011629|||http://purl.uniprot.org/annotation/VSP_015222 http://togogenome.org/gene/10090:Ltbp3 ^@ http://purl.uniprot.org/uniprot/Q61810 ^@ 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 ^@ Basic and acidic residues|||Disordered|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11; calcium-binding|||EGF-like 12; 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 isoform 2.|||Interchain (with C-33 in TGFB1); in linked form|||Latent-transforming growth factor beta-binding protein 3|||N-linked (GlcNAc...) asparagine|||TB 1|||TB 2|||TB 3|||TB 4 ^@ http://purl.uniprot.org/annotation/PRO_0000007647|||http://purl.uniprot.org/annotation/VSP_009242|||http://purl.uniprot.org/annotation/VSP_009243 http://togogenome.org/gene/10090:Nat8f4 ^@ http://purl.uniprot.org/uniprot/E0CYM0|||http://purl.uniprot.org/uniprot/G5E8L3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||N-acetyltransferase ^@ http://togogenome.org/gene/10090:Clps ^@ http://purl.uniprot.org/uniprot/B2KF29|||http://purl.uniprot.org/uniprot/Q9CQC2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Signal Peptide ^@ Colipase|||Colipase C-terminal|||Enterostatin, activation peptide ^@ http://purl.uniprot.org/annotation/PRO_0000005698|||http://purl.uniprot.org/annotation/PRO_0000005699|||http://purl.uniprot.org/annotation/PRO_5002780134 http://togogenome.org/gene/10090:Sdc4 ^@ http://purl.uniprot.org/uniprot/O35988|||http://purl.uniprot.org/uniprot/Q3U5S6 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Neurexin/syndecan/glycophorin C|||O-linked (Xyl...) (glycosaminoglycan) serine|||Syndecan|||Syndecan-4 ^@ http://purl.uniprot.org/annotation/PRO_0000033512|||http://purl.uniprot.org/annotation/PRO_5014309195 http://togogenome.org/gene/10090:Srbd1 ^@ http://purl.uniprot.org/uniprot/F8WGW3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||S1 motif ^@ http://togogenome.org/gene/10090:Fbxw17 ^@ http://purl.uniprot.org/uniprot/Q8CFE8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Epha1 ^@ http://purl.uniprot.org/uniprot/Q60750 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 1|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000016799 http://togogenome.org/gene/10090:Sec1 ^@ http://purl.uniprot.org/uniprot/Q8CDC9 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Or52n4b ^@ http://purl.uniprot.org/uniprot/Q7TRU8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gpr22 ^@ http://purl.uniprot.org/uniprot/G3X9C3|||http://purl.uniprot.org/uniprot/Q8BZL4 ^@ 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 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_0000303235 http://togogenome.org/gene/10090:Casp8 ^@ http://purl.uniprot.org/uniprot/A0A087WQT6|||http://purl.uniprot.org/uniprot/O89110|||http://purl.uniprot.org/uniprot/Q3U607 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Site ^@ Caspase family p10|||Caspase family p20|||Caspase-8 subunit p10|||Caspase-8 subunit p18|||Cleavage; by CASP6|||Cleavage; by autocatalytic cleavage|||DED|||DED 1|||DED 2|||Loss of autocatalytic cleavage; when associated with A-212; A-218 and A-225.|||Loss of autocatalytic cleavage; when associated with A-212; A-218 and A-387.|||Loss of autocatalytic cleavage; when associated with A-212; A-225 and A-387.|||Loss of autocatalytic cleavage; when associated with A-218; A-225 and A-387.|||Loss of kinase ativity. Knockin mice show embryonic lethality caused by endothelial cell necroptosis leading to cardiovascular defects. Mlkl deficiency rescues the cardiovascular phenotype of knockin mice, but causes perinatal lethality caused by induction of pyroptosis.|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000004632|||http://purl.uniprot.org/annotation/PRO_0000004633|||http://purl.uniprot.org/annotation/PRO_0000004634|||http://purl.uniprot.org/annotation/PRO_0000004635 http://togogenome.org/gene/10090:Tnpo3 ^@ http://purl.uniprot.org/uniprot/Q6P2B1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Transportin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000120782|||http://purl.uniprot.org/annotation/VSP_011179|||http://purl.uniprot.org/annotation/VSP_019595|||http://purl.uniprot.org/annotation/VSP_019596 http://togogenome.org/gene/10090:Flvcr2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0E9|||http://purl.uniprot.org/uniprot/Q3UL56|||http://purl.uniprot.org/uniprot/Q91X85 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ 1|||2|||3|||4|||5|||6|||7|||8|||8 X 6 AA tandem repeats of P-S-[VSG]-S-[VIAG]-[HDRL]|||Disordered|||Helical|||Heme transporter FLVCR2|||Major facilitator superfamily (MFS) profile|||Phosphoserine|||Polar residues|||Present at mitochondrial membrane. Impairs interaction with HMOX1. Abolishes the response to heme. ^@ http://purl.uniprot.org/annotation/PRO_0000084847 http://togogenome.org/gene/10090:D2hgdh ^@ http://purl.uniprot.org/uniprot/E9QN44|||http://purl.uniprot.org/uniprot/Q8CIM3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Transit Peptide ^@ D-2-hydroxyglutarate dehydrogenase, mitochondrial|||FAD-binding PCMH-type|||Mitochondrion|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000231675|||http://purl.uniprot.org/annotation/PRO_5003244817 http://togogenome.org/gene/10090:Fabp9 ^@ http://purl.uniprot.org/uniprot/O08716 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Fatty acid-binding protein 9|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000067385 http://togogenome.org/gene/10090:Kdr ^@ http://purl.uniprot.org/uniprot/P35918 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||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|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||In isoform 2.|||Interaction with SHB|||Interchain (with C-189 in SLC31A1)|||Loss of enzyme activity. Abolishes ubiquitination in response to VEGFA binding.|||Loss of interaction with SHB.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Redox-active|||Strongly reduced autophosphorylation.|||Strongly reduces internalization and down-regulation of the activated receptor; when associated with A-1188.|||Strongly reduces internalization and down-regulation of the activated receptor; when associated with A-1191.|||Vascular endothelial growth factor receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000016772|||http://purl.uniprot.org/annotation/VSP_041986|||http://purl.uniprot.org/annotation/VSP_041987 http://togogenome.org/gene/10090:Bmx ^@ http://purl.uniprot.org/uniprot/B1AUL6|||http://purl.uniprot.org/uniprot/P97504 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Zinc Finger ^@ Btk-type|||Cytoplasmic tyrosine-protein kinase BMX|||PH|||Phosphotyrosine; by SRC and autocatalysis|||Protein kinase|||Proton acceptor|||SH2 ^@ http://purl.uniprot.org/annotation/PRO_0000088064 http://togogenome.org/gene/10090:Arhgef17 ^@ http://purl.uniprot.org/uniprot/Q80U35 ^@ 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|||DH|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho guanine nucleotide exchange factor 17 ^@ http://purl.uniprot.org/annotation/PRO_0000286590|||http://purl.uniprot.org/annotation/VSP_025104|||http://purl.uniprot.org/annotation/VSP_025105 http://togogenome.org/gene/10090:Lrrc8e ^@ http://purl.uniprot.org/uniprot/Q66JT1 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||LRR 1|||LRR 10|||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_0000076251 http://togogenome.org/gene/10090:Luzp4 ^@ http://purl.uniprot.org/uniprot/B1AV09|||http://purl.uniprot.org/uniprot/L7N278 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gm17455 ^@ http://purl.uniprot.org/uniprot/G3UW87 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Cltb ^@ http://purl.uniprot.org/uniprot/Q3TJ95|||http://purl.uniprot.org/uniprot/Q3TWZ9|||http://purl.uniprot.org/uniprot/Q6IRU5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region|||Splice Variant ^@ Clathrin light chain B|||Disordered|||In isoform 2.|||In isoform 3.|||Involved in binding clathrin heavy chain|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000205772|||http://purl.uniprot.org/annotation/VSP_013382|||http://purl.uniprot.org/annotation/VSP_013383 http://togogenome.org/gene/10090:Vmn1r165 ^@ http://purl.uniprot.org/uniprot/D3YTY1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ssb ^@ http://purl.uniprot.org/uniprot/P32067|||http://purl.uniprot.org/uniprot/Q564E6 ^@ 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|||Lupus La protein homolog|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||RRM|||XRRM|||xRRM ^@ http://purl.uniprot.org/annotation/PRO_0000207600 http://togogenome.org/gene/10090:Pm20d2 ^@ http://purl.uniprot.org/uniprot/A3KG59 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Xaa-Arg dipeptidase ^@ http://purl.uniprot.org/annotation/PRO_0000286341|||http://purl.uniprot.org/annotation/VSP_025030|||http://purl.uniprot.org/annotation/VSP_025031 http://togogenome.org/gene/10090:Mapk4 ^@ http://purl.uniprot.org/uniprot/Q6P5G0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ ATP-binding site mutant; unable to activate MAPKAPK5.|||Abolishes binding to MAPKAPK5.|||Basic and acidic residues|||Disordered|||FRIEDE motif|||Impairs binding to MAPKAPK5.|||Kinase defective mutant, abolishes activity.|||Mitogen-activated protein kinase 4|||Phosphoserine|||Phosphoserine; by PAK1, PAK2 and PAK3|||Pro residues|||Protein kinase|||Proton acceptor|||SEG motif|||Unable to activate MAPKAPK5 promote MAPKAPK5 localization to the cytoplasm. ^@ http://purl.uniprot.org/annotation/PRO_0000186255 http://togogenome.org/gene/10090:Or52r1b ^@ http://purl.uniprot.org/uniprot/Q8VGV9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mtpap ^@ http://purl.uniprot.org/uniprot/Q9D0D3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||N6-acetyllysine|||PAP-associated|||Polar residues|||Poly(A) RNA polymerase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000250690 http://togogenome.org/gene/10090:Zfyve16 ^@ http://purl.uniprot.org/uniprot/Q80U44 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||FYVE-type|||Phosphoserine|||Polar residues|||Zinc finger FYVE domain-containing protein 16 ^@ http://purl.uniprot.org/annotation/PRO_0000098717 http://togogenome.org/gene/10090:Grm7 ^@ http://purl.uniprot.org/uniprot/G5E8D5|||http://purl.uniprot.org/uniprot/Q68ED2 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Metabotropic glutamate receptor 7|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000012939|||http://purl.uniprot.org/annotation/PRO_5003475858 http://togogenome.org/gene/10090:Slc38a2 ^@ http://purl.uniprot.org/uniprot/Q8CFE6 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||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_0000311370 http://togogenome.org/gene/10090:Tmem270 ^@ http://purl.uniprot.org/uniprot/Q6UJB9 ^@ 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 270 ^@ http://purl.uniprot.org/annotation/PRO_0000308416|||http://purl.uniprot.org/annotation/VSP_028980 http://togogenome.org/gene/10090:Bri3 ^@ http://purl.uniprot.org/uniprot/E9PUB2|||http://purl.uniprot.org/uniprot/P28662|||http://purl.uniprot.org/uniprot/Q8C4X5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Membrane protein BRI3 ^@ http://purl.uniprot.org/annotation/PRO_0000064924 http://togogenome.org/gene/10090:Tmco4 ^@ http://purl.uniprot.org/uniprot/Q91WU4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Polar residues|||Transmembrane and coiled-coil domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000305150|||http://purl.uniprot.org/annotation/VSP_028243|||http://purl.uniprot.org/annotation/VSP_028244|||http://purl.uniprot.org/annotation/VSP_028245 http://togogenome.org/gene/10090:Grhl2 ^@ http://purl.uniprot.org/uniprot/Q8K5C0|||http://purl.uniprot.org/uniprot/Q9DCN4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Disordered|||Grainyhead-like protein 2 homolog|||Grh/CP2 DB|||Important for activation of transcription|||Polar residues|||Transcription activation ^@ http://purl.uniprot.org/annotation/PRO_0000227995 http://togogenome.org/gene/10090:Gtf2a2 ^@ http://purl.uniprot.org/uniprot/D3Z7C2|||http://purl.uniprot.org/uniprot/Q3TE88|||http://purl.uniprot.org/uniprot/Q3TN86|||http://purl.uniprot.org/uniprot/Q80ZM7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ 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_0000194043 http://togogenome.org/gene/10090:Dst ^@ http://purl.uniprot.org/uniprot/Q91ZU6|||http://purl.uniprot.org/uniprot/S4R1P5 ^@ 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|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ 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 1.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Microtubule tip localization signal|||Nuclear localization signal; in isoform 6|||Phosphoserine|||Plectin 1|||Plectin 2|||Plectin 3|||Plectin 4|||Plectin 5|||Polar residues|||Prevents isoform 6 from localizing to the nucleus; when associated with A-1385.|||Prevents isoform 6 from localizing to the nucleus; when associated with A-1386.|||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_0000078141|||http://purl.uniprot.org/annotation/VSP_041542|||http://purl.uniprot.org/annotation/VSP_041543|||http://purl.uniprot.org/annotation/VSP_041544|||http://purl.uniprot.org/annotation/VSP_041545|||http://purl.uniprot.org/annotation/VSP_041546|||http://purl.uniprot.org/annotation/VSP_041549|||http://purl.uniprot.org/annotation/VSP_041550|||http://purl.uniprot.org/annotation/VSP_041551|||http://purl.uniprot.org/annotation/VSP_041552|||http://purl.uniprot.org/annotation/VSP_055459|||http://purl.uniprot.org/annotation/VSP_055460|||http://purl.uniprot.org/annotation/VSP_055461 http://togogenome.org/gene/10090:Svbp ^@ http://purl.uniprot.org/uniprot/A2A7P9|||http://purl.uniprot.org/uniprot/Q99LQ4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Small vasohibin-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000233664 http://togogenome.org/gene/10090:Ifna14 ^@ http://purl.uniprot.org/uniprot/Q810G3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015098939 http://togogenome.org/gene/10090:Mtap ^@ http://purl.uniprot.org/uniprot/Q9CQ65 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue|||Site ^@ Important for substrate specificity|||N6-acetyllysine|||S-methyl-5'-thioadenosine phosphorylase ^@ http://purl.uniprot.org/annotation/PRO_0000184546 http://togogenome.org/gene/10090:H4c16 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Itpa ^@ http://purl.uniprot.org/uniprot/Q60I30|||http://purl.uniprot.org/uniprot/Q9D892 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Inosine triphosphate pyrophosphatase|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000178281 http://togogenome.org/gene/10090:Fbxo47 ^@ http://purl.uniprot.org/uniprot/A2A6H3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ F-box|||F-box only protein 47 ^@ http://purl.uniprot.org/annotation/PRO_0000307726 http://togogenome.org/gene/10090:Prdx5 ^@ http://purl.uniprot.org/uniprot/P99029 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Cysteine sulfenic acid (-SOH) intermediate|||In isoform Cytoplasmic+peroxisomal.|||Microbody targeting signal|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Peroxiredoxin-5, mitochondrial|||Phosphoserine|||Redox-active|||S-palmitoyl cysteine|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000023795|||http://purl.uniprot.org/annotation/VSP_018830 http://togogenome.org/gene/10090:Shmt2 ^@ http://purl.uniprot.org/uniprot/Q9CZN7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine; alternate|||N6-acetyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Serine hydroxymethyltransferase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000443804|||http://purl.uniprot.org/annotation/VSP_059519 http://togogenome.org/gene/10090:Or7g34 ^@ http://purl.uniprot.org/uniprot/Q8VFF1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfyve27 ^@ http://purl.uniprot.org/uniprot/Q3TXX3 ^@ Binding Site|||Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||INTRAMEM|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||Disordered|||FYVE-type|||Helical|||In isoform 2.|||Lumenal|||Necessary for interaction with KIF5A|||Necessary for interaction with RAB11A and function in neurite outgrowth|||Necessary for interaction with VAPA|||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_0000245602|||http://purl.uniprot.org/annotation/VSP_019757 http://togogenome.org/gene/10090:Pard6a ^@ http://purl.uniprot.org/uniprot/D3Z2R1|||http://purl.uniprot.org/uniprot/Q3TY70|||http://purl.uniprot.org/uniprot/Q9Z101 ^@ 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.|||In isoform 3.|||Interaction with PARD3 and CDC42|||Interaction with PRKCI and PRKCZ|||PB1|||PDZ|||Partitioning defective 6 homolog alpha|||Phosphoserine|||Pseudo-CRIB ^@ http://purl.uniprot.org/annotation/PRO_0000112514|||http://purl.uniprot.org/annotation/VSP_015462|||http://purl.uniprot.org/annotation/VSP_015463 http://togogenome.org/gene/10090:Klhl17 ^@ http://purl.uniprot.org/uniprot/B2RTE7|||http://purl.uniprot.org/uniprot/Q6TDP3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ 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_0000119120 http://togogenome.org/gene/10090:Prss46 ^@ http://purl.uniprot.org/uniprot/Q5M8S2 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Splice Variant|||Transmembrane ^@ Charge relay system|||Helical|||In isoform 2.|||Peptidase S1|||Serine protease 46 ^@ http://purl.uniprot.org/annotation/PRO_0000418333|||http://purl.uniprot.org/annotation/VSP_044025 http://togogenome.org/gene/10090:Cd33 ^@ http://purl.uniprot.org/uniprot/Q63994 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 33-A.|||Myeloid cell surface antigen CD33|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014879|||http://purl.uniprot.org/annotation/VSP_002534 http://togogenome.org/gene/10090:Il27ra ^@ http://purl.uniprot.org/uniprot/O70394|||http://purl.uniprot.org/uniprot/Q3UZN3 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III domain-containing protein|||Helical|||Interleukin-27 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010877|||http://purl.uniprot.org/annotation/PRO_5004230312 http://togogenome.org/gene/10090:Nxph3 ^@ http://purl.uniprot.org/uniprot/Q544G3|||http://purl.uniprot.org/uniprot/Q91VX5 ^@ 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|||II|||III|||IV (linker domain)|||N-linked (GlcNAc...) asparagine|||Neurexophilin|||Neurexophilin-3|||V (Cys-rich) ^@ http://purl.uniprot.org/annotation/PRO_0000020066|||http://purl.uniprot.org/annotation/PRO_5014309563 http://togogenome.org/gene/10090:Or10h1b ^@ http://purl.uniprot.org/uniprot/K7N6Q1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rgs1 ^@ http://purl.uniprot.org/uniprot/Q9JL25 ^@ 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.|||RGS|||Regulator of G-protein signaling 1 ^@ http://purl.uniprot.org/annotation/PRO_0000204176|||http://purl.uniprot.org/annotation/VSP_036732 http://togogenome.org/gene/10090:Dgat2l6 ^@ http://purl.uniprot.org/uniprot/A2ADU8 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Diacylglycerol O-acyltransferase 2-like protein 6|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000320297 http://togogenome.org/gene/10090:Chml ^@ http://purl.uniprot.org/uniprot/A0A0R4J1A1|||http://purl.uniprot.org/uniprot/Q9QZD5 ^@ 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|||Rab proteins geranylgeranyltransferase component A 2 ^@ http://purl.uniprot.org/annotation/PRO_0000056690 http://togogenome.org/gene/10090:Mcf2l ^@ http://purl.uniprot.org/uniprot/E9PXE2|||http://purl.uniprot.org/uniprot/E9PY12|||http://purl.uniprot.org/uniprot/E9PY13|||http://purl.uniprot.org/uniprot/Q6PDM6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||CRAL-TRIO|||DH|||Disordered|||PH|||Polar residues|||SH3 ^@ http://togogenome.org/gene/10090:Tpd52 ^@ http://purl.uniprot.org/uniprot/E9PUA7|||http://purl.uniprot.org/uniprot/F8WHQ1|||http://purl.uniprot.org/uniprot/Q62393 ^@ 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 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tumor protein D52 ^@ http://purl.uniprot.org/annotation/PRO_0000185739|||http://purl.uniprot.org/annotation/VSP_037379|||http://purl.uniprot.org/annotation/VSP_037380 http://togogenome.org/gene/10090:Crtc1 ^@ http://purl.uniprot.org/uniprot/Q68ED7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site ^@ Basic and acidic residues|||CREB-regulated transcription coactivator 1|||Disordered|||No effect on interaction with 14-3-3 proteins.|||Nuclear export signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for ubiquitination and degradation|||Up-regulates CREB transcription factor activity.|||Up-regulates CREB transcription factor activity. Reduces interaction with 14-3-3 proteins. ^@ http://purl.uniprot.org/annotation/PRO_0000096355 http://togogenome.org/gene/10090:Nnat ^@ http://purl.uniprot.org/uniprot/G3UWR4|||http://purl.uniprot.org/uniprot/G3UWR7|||http://purl.uniprot.org/uniprot/G3X9K1|||http://purl.uniprot.org/uniprot/Q548P9|||http://purl.uniprot.org/uniprot/Q61979 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Neuronatin ^@ http://purl.uniprot.org/annotation/PRO_0000096883|||http://purl.uniprot.org/annotation/VSP_004333 http://togogenome.org/gene/10090:Fgl2 ^@ http://purl.uniprot.org/uniprot/P12804|||http://purl.uniprot.org/uniprot/Q544K3 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Fibrinogen C-terminal|||Fibroleukin|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009107|||http://purl.uniprot.org/annotation/PRO_5014309630 http://togogenome.org/gene/10090:Or7g18 ^@ http://purl.uniprot.org/uniprot/Q8VFJ5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r249 ^@ http://purl.uniprot.org/uniprot/K9J7F4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Abcb8 ^@ http://purl.uniprot.org/uniprot/Q9CXJ4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Transit Peptide|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||Disordered|||Helical|||Mitochondrial potassium channel ATP-binding subunit|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000356233 http://togogenome.org/gene/10090:Ccl2 ^@ http://purl.uniprot.org/uniprot/P10148|||http://purl.uniprot.org/uniprot/Q5SVU3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Signal Peptide ^@ C-C motif chemokine|||C-C motif chemokine 2|||Chemokine interleukin-8-like|||In strain: SJL/J.|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000005149|||http://purl.uniprot.org/annotation/PRO_5014205902 http://togogenome.org/gene/10090:Antxrl ^@ http://purl.uniprot.org/uniprot/A0A2U7XVH6|||http://purl.uniprot.org/uniprot/Q8BVM2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Anthrax toxin receptor-like|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Pro residues|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000332168|||http://purl.uniprot.org/annotation/PRO_5016151484 http://togogenome.org/gene/10090:Abat ^@ http://purl.uniprot.org/uniprot/P61922 ^@ Binding Site|||Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Splice Variant|||Transit Peptide ^@ 4-aminobutyrate aminotransferase, mitochondrial|||In isoform 2.|||Interchain|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000001250|||http://purl.uniprot.org/annotation/VSP_012005 http://togogenome.org/gene/10090:Teddm3 ^@ http://purl.uniprot.org/uniprot/Q9CQH1 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Mapkapk5 ^@ http://purl.uniprot.org/uniprot/O54992 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Splice Variant ^@ Constitutive active mutant. In a knockin model, mouse display increased amounts of head dips and open arm time on the maze, compared to littermate controls. In addition, they also explore further into the open arm on the elevated plus maze and are less active in the closed arm compared to littermate controls. Male knockin mice display no differences in anxiety, but their locomotor activity increases compared to non-transgenic littermates.|||Impairs protein kinase activity and shuttling to the cytoplasm.|||Impairs shuttling to the cytoplasm.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4 and isoform 5.|||Kinase defective mutant, abolishes activity.|||MAP kinase-activated protein kinase 5|||Mimicks phosphorylation state, leading to localization to the cytoplasm.|||No p38-alpha/MAPK14-, p38-beta/MAPK11-, ERK3/MAPK6-, ERK4/MAPK4-induced activation.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine; by MAPK11, MAPK14, MAPK4, MAPK6 and PKA|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086297|||http://purl.uniprot.org/annotation/VSP_011598|||http://purl.uniprot.org/annotation/VSP_011599|||http://purl.uniprot.org/annotation/VSP_011600 http://togogenome.org/gene/10090:Cars ^@ http://purl.uniprot.org/uniprot/Q3U716|||http://purl.uniprot.org/uniprot/Q3UXN3|||http://purl.uniprot.org/uniprot/Q9ER72 ^@ 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 ^@ 'HIGH' region|||'KMSKS' region|||Basic and acidic residues|||Cysteine--tRNA ligase, cytoplasmic|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||tRNA synthetases class I catalytic ^@ http://purl.uniprot.org/annotation/PRO_0000159551|||http://purl.uniprot.org/annotation/VSP_010258 http://togogenome.org/gene/10090:Hltf ^@ http://purl.uniprot.org/uniprot/Q6PCN7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||DEGH box|||DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||Helicase-like transcription factor|||Interaction with SP1 and SP3|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by JAK2|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056185 http://togogenome.org/gene/10090:Guca2b ^@ http://purl.uniprot.org/uniprot/O09051|||http://purl.uniprot.org/uniprot/Q9QUQ3 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Uroguanylin ^@ http://purl.uniprot.org/annotation/PRO_0000013150|||http://purl.uniprot.org/annotation/PRO_0000013151|||http://purl.uniprot.org/annotation/PRO_5014313158 http://togogenome.org/gene/10090:Or4a47 ^@ http://purl.uniprot.org/uniprot/Q8VGP1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dusp5 ^@ http://purl.uniprot.org/uniprot/Q1HL35 ^@ Active Site|||Domain Extent|||Region|||Site ^@ Active Site|||Domain Extent ^@ Phosphocysteine intermediate|||Rhodanese|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://togogenome.org/gene/10090:Synj2 ^@ http://purl.uniprot.org/uniprot/D3YZB2|||http://purl.uniprot.org/uniprot/E9Q4P5|||http://purl.uniprot.org/uniprot/F8WHD8|||http://purl.uniprot.org/uniprot/Q3TTB3|||http://purl.uniprot.org/uniprot/Q9D2G5 ^@ 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 ^@ Catalytic|||Disordered|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6.|||Phosphoserine|||Polar residues|||Pro residues|||RRM|||SAC|||Synaptojanin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000209734|||http://purl.uniprot.org/annotation/VSP_009304|||http://purl.uniprot.org/annotation/VSP_009305|||http://purl.uniprot.org/annotation/VSP_009306|||http://purl.uniprot.org/annotation/VSP_009307|||http://purl.uniprot.org/annotation/VSP_009308|||http://purl.uniprot.org/annotation/VSP_009309|||http://purl.uniprot.org/annotation/VSP_009310|||http://purl.uniprot.org/annotation/VSP_010563 http://togogenome.org/gene/10090:Ptpn11 ^@ http://purl.uniprot.org/uniprot/P35235 ^@ 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 ^@ In isoform 2.|||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_0000094768|||http://purl.uniprot.org/annotation/VSP_060440 http://togogenome.org/gene/10090:Morn5 ^@ http://purl.uniprot.org/uniprot/Q9DAI9 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ MORN 1|||MORN 2|||MORN 3|||MORN repeat-containing protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000292841 http://togogenome.org/gene/10090:Tmem179 ^@ http://purl.uniprot.org/uniprot/Q8BHH9 ^@ 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 179 ^@ http://purl.uniprot.org/annotation/PRO_0000254553 http://togogenome.org/gene/10090:Ajuba ^@ http://purl.uniprot.org/uniprot/Q91XC0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||LIM domain-containing protein ajuba|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Nuclear localization signal|||Phosphoserine|||Polar residues|||PreLIM ^@ http://purl.uniprot.org/annotation/PRO_0000312626 http://togogenome.org/gene/10090:Rac3 ^@ http://purl.uniprot.org/uniprot/P60764 ^@ Binding Site|||Chain|||Crosslink|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Lipid Binding|||Modified Residue|||Motif|||Propeptide ^@ Cysteine methyl ester|||Effector region|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Ras-related C3 botulinum toxin substrate 3|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000198890|||http://purl.uniprot.org/annotation/PRO_0000281241 http://togogenome.org/gene/10090:Bag4 ^@ http://purl.uniprot.org/uniprot/A6H6S8|||http://purl.uniprot.org/uniprot/Q8CI61 ^@ 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 ^@ Abolishes interaction with HSP70 and TNFRSF1A.|||BAG|||BAG family molecular chaperone regulator 4|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000088871 http://togogenome.org/gene/10090:Fcrl1 ^@ http://purl.uniprot.org/uniprot/A0A0A6YY56|||http://purl.uniprot.org/uniprot/A0A0R4J0W8|||http://purl.uniprot.org/uniprot/E9Q5S9|||http://purl.uniprot.org/uniprot/E9Q958|||http://purl.uniprot.org/uniprot/Q8R4Y0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Fc receptor-like protein 1|||Helical|||ITIM motif 1|||ITIM motif 2|||ITIM motif 3|||ITIM motif 4|||ITIM motif 5|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000331639|||http://purl.uniprot.org/annotation/PRO_5002034135|||http://purl.uniprot.org/annotation/PRO_5003244451|||http://purl.uniprot.org/annotation/PRO_5006451985|||http://purl.uniprot.org/annotation/VSP_033296|||http://purl.uniprot.org/annotation/VSP_033297|||http://purl.uniprot.org/annotation/VSP_033298|||http://purl.uniprot.org/annotation/VSP_033299 http://togogenome.org/gene/10090:Fam83e ^@ http://purl.uniprot.org/uniprot/Q80XS7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Protein FAM83E ^@ http://purl.uniprot.org/annotation/PRO_0000314930 http://togogenome.org/gene/10090:Ptges ^@ http://purl.uniprot.org/uniprot/Q8BNP8|||http://purl.uniprot.org/uniprot/Q9JM51 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Essential for protaglandin-E synthase activity|||Helical|||Lumenal|||Prostaglandin E synthase ^@ http://purl.uniprot.org/annotation/PRO_0000217747 http://togogenome.org/gene/10090:Plekho1 ^@ http://purl.uniprot.org/uniprot/Q9JIY0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||Interaction with ATM, CKIP, IFP35 and NMI|||Interaction with capping proteins (CPs)|||Interacts with capping protein|||Negative regulator of AP-1 activity|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family O member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000310424 http://togogenome.org/gene/10090:P4hb ^@ http://purl.uniprot.org/uniprot/P09103 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site ^@ Contributes to redox potential value|||Homozygotes are born at Mendelian ratios and have no phenotypic abnormalities from birth to adulthood. Increased ERN1 activity.|||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|||Phosphoserine|||Prevents secretion from ER|||Protein disulfide-isomerase|||Redox-active|||Thioredoxin 1|||Thioredoxin 2 ^@ http://purl.uniprot.org/annotation/PRO_0000034196 http://togogenome.org/gene/10090:Pirt ^@ http://purl.uniprot.org/uniprot/Q3UFA4|||http://purl.uniprot.org/uniprot/Q8BFY0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Transmembrane ^@ Abolishes phosphoinositide-binding and ability to activate TRPV1 without affecting the interaction with TRPV1.|||Abolishes phosphoinositide-binding but does not affect the interaction with TRPV1.|||Basic and acidic residues|||Disordered|||Helical|||Phosphoinositide-interacting protein ^@ http://purl.uniprot.org/annotation/PRO_0000347061 http://togogenome.org/gene/10090:Rusc2 ^@ http://purl.uniprot.org/uniprot/Q3V1Z0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||RUN|||SH3 ^@ http://togogenome.org/gene/10090:Or52ad1 ^@ http://purl.uniprot.org/uniprot/E9PUN7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Oas1e ^@ http://purl.uniprot.org/uniprot/A0A0J9YV76|||http://purl.uniprot.org/uniprot/Q8C2W3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ 2'-5'-oligoadenylate synthetase 1 ^@ http://togogenome.org/gene/10090:Erlec1 ^@ http://purl.uniprot.org/uniprot/Q8VEH8 ^@ 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 ^@ Endoplasmic reticulum lectin 1|||MRH 1|||MRH 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000042183 http://togogenome.org/gene/10090:Atp6v1b1 ^@ http://purl.uniprot.org/uniprot/Q91YH6 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Motif|||Region|||Sequence Conflict ^@ Disordered|||PDZ-binding|||V-type proton ATPase subunit B, kidney isoform ^@ http://purl.uniprot.org/annotation/PRO_0000453034 http://togogenome.org/gene/10090:Ppp2r5e ^@ http://purl.uniprot.org/uniprot/Q61151 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform ^@ http://purl.uniprot.org/annotation/PRO_0000071455 http://togogenome.org/gene/10090:Tep1 ^@ http://purl.uniprot.org/uniprot/P97499|||http://purl.uniprot.org/uniprot/Q5XKB2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||NACHT|||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_0000050983 http://togogenome.org/gene/10090:Csn2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JF04|||http://purl.uniprot.org/uniprot/P10598|||http://purl.uniprot.org/uniprot/Q8BGL0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Beta-casein|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000004477|||http://purl.uniprot.org/annotation/PRO_5012136035|||http://purl.uniprot.org/annotation/PRO_5015099021 http://togogenome.org/gene/10090:Adnp ^@ http://purl.uniprot.org/uniprot/Q3UYC8|||http://purl.uniprot.org/uniprot/Q5BL11|||http://purl.uniprot.org/uniprot/Q9Z103 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Zinc Finger ^@ Activity-dependent neuroprotector homeobox protein|||Asymmetric dimethylarginine|||Basic and acidic residues|||Binds to beta-catenin/CTNNB1|||C2H2-type|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5; atypical|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8; atypical|||C2H2-type 9; atypical|||Disordered|||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; contributes to CTNNB1-binding, but less effective than whole N-terminal region|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048808 http://togogenome.org/gene/10090:Tspan3 ^@ http://purl.uniprot.org/uniprot/Q545L1|||http://purl.uniprot.org/uniprot/Q80XR4|||http://purl.uniprot.org/uniprot/Q9QY33 ^@ 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-3 ^@ http://purl.uniprot.org/annotation/PRO_0000219240 http://togogenome.org/gene/10090:Naalad2 ^@ http://purl.uniprot.org/uniprot/Q3UZV6|||http://purl.uniprot.org/uniprot/Q9CZR2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Charge relay system|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||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_0000174122 http://togogenome.org/gene/10090:Vmn1r104 ^@ http://purl.uniprot.org/uniprot/L7N293 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cct7 ^@ http://purl.uniprot.org/uniprot/P80313|||http://purl.uniprot.org/uniprot/Q3TIJ7|||http://purl.uniprot.org/uniprot/Q3UDB1|||http://purl.uniprot.org/uniprot/Q3UIJ0 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Crosslink|||Modified Residue|||Non-terminal Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||T-complex protein 1 subunit eta ^@ http://purl.uniprot.org/annotation/PRO_0000128366 http://togogenome.org/gene/10090:Slc25a15 ^@ http://purl.uniprot.org/uniprot/Q543E2|||http://purl.uniprot.org/uniprot/Q9WVD5 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Repeat|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial ornithine transporter 1|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090651 http://togogenome.org/gene/10090:Vmn1r52 ^@ http://purl.uniprot.org/uniprot/Q9EP79 ^@ 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|||Vomeronasal type-1 receptor 52 ^@ http://purl.uniprot.org/annotation/PRO_0000239962 http://togogenome.org/gene/10090:Or6c70 ^@ http://purl.uniprot.org/uniprot/Q7TRH4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cox5b ^@ http://purl.uniprot.org/uniprot/Q9D881 ^@ Binding Site|||Modification|||Modified Residue|||Site ^@ Binding Site|||Modified Residue ^@ N6-acetyllysine ^@ http://togogenome.org/gene/10090:Gramd1a ^@ http://purl.uniprot.org/uniprot/Q8VEF1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Disordered|||GRAM|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Protein Aster-A|||VASt ^@ http://purl.uniprot.org/annotation/PRO_0000287447|||http://purl.uniprot.org/annotation/VSP_025467|||http://purl.uniprot.org/annotation/VSP_025468 http://togogenome.org/gene/10090:Sars2 ^@ http://purl.uniprot.org/uniprot/Q9JJL8 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Serine--tRNA ligase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000035823 http://togogenome.org/gene/10090:Zfp422 ^@ http://purl.uniprot.org/uniprot/Q3U7F6|||http://purl.uniprot.org/uniprot/Q9ERU3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||N6-acetyllysine|||Zinc finger protein 22 ^@ http://purl.uniprot.org/annotation/PRO_0000047349 http://togogenome.org/gene/10090:H3f3b ^@ http://purl.uniprot.org/uniprot/P84244 ^@ Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand ^@ 5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Abolished serotonylation by TGM2. Reduced neurite length.|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.3|||Interaction with ZMYND11|||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; 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_0000221251 http://togogenome.org/gene/10090:Strbp ^@ http://purl.uniprot.org/uniprot/Q91WM1 ^@ 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|||DRBM 1|||DRBM 2|||DZF|||Disordered|||In isoform 2.|||Polar residues|||Spermatid perinuclear RNA-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000274918|||http://purl.uniprot.org/annotation/VSP_022938 http://togogenome.org/gene/10090:Nob1 ^@ http://purl.uniprot.org/uniprot/Q148S3|||http://purl.uniprot.org/uniprot/Q8BW10 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Strand|||Zinc Finger ^@ Acidic residues|||Disordered|||NOB1|||PIN|||PINc|||Phosphoserine|||RNA-binding protein NOB1 ^@ http://purl.uniprot.org/annotation/PRO_0000233267 http://togogenome.org/gene/10090:Ipo8 ^@ http://purl.uniprot.org/uniprot/Q7TMY7 ^@ 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|||Importin N-terminal|||Importin-8|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000120753|||http://purl.uniprot.org/annotation/VSP_009656 http://togogenome.org/gene/10090:Sugp1 ^@ http://purl.uniprot.org/uniprot/Q8CH02 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||G-patch|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||SURP and G-patch domain-containing protein 1|||SURP motif 1|||SURP motif 2 ^@ http://purl.uniprot.org/annotation/PRO_0000097702 http://togogenome.org/gene/10090:Ttc19 ^@ http://purl.uniprot.org/uniprot/Q8CC21 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Chain|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Cleavage; by PARL|||In isoform 2.|||Mitochondrion|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||Tetratricopeptide repeat protein 19, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000106408|||http://purl.uniprot.org/annotation/VSP_041051 http://togogenome.org/gene/10090:Prss51 ^@ http://purl.uniprot.org/uniprot/E9PXD1|||http://purl.uniprot.org/uniprot/Q9DAL4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Peptidase S1 ^@ http://togogenome.org/gene/10090:Rimbp3 ^@ http://purl.uniprot.org/uniprot/Q3V0F0 ^@ 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|||Fibronectin type-III 1|||Fibronectin type-III 2|||Phosphoserine|||Polar residues|||RIMS-binding protein 3|||SH3 1|||SH3 2|||SH3 3 ^@ http://purl.uniprot.org/annotation/PRO_0000259598 http://togogenome.org/gene/10090:Otoa ^@ http://purl.uniprot.org/uniprot/Q8K561 ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Otoancorin|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000021973|||http://purl.uniprot.org/annotation/PRO_0000021974 http://togogenome.org/gene/10090:Nlrc4 ^@ http://purl.uniprot.org/uniprot/Q3UP24 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ Abolishes phosphorylation and prevents activation of caspase-1 and pyroptosis in response to S.typhimurium.|||CARD|||Constitutively active.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Mimics phosphorylation; causes rapid macrophage pyroptosis without infection.|||NACHT|||NLR family CARD domain-containing protein 4|||Nucleotide-binding domain (NBD)|||Phosphoserine|||Winged-helix domain (WHD) ^@ http://purl.uniprot.org/annotation/PRO_0000419975 http://togogenome.org/gene/10090:Cd300ld3 ^@ http://purl.uniprot.org/uniprot/Q6SJQ5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ CMRF35-like molecule 3|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||Important for maintaining surface expression and for interaction with FCER1G|||Increases surface expression in transfected pro-B cells and enhances interaction with FCER1G. Slightly increases surface expression and enhances interaction with FCER1G; when associated with 189-Y--L-198.|||Reduces surface expression in transfected pro-B cells and enhances interaction with FCER1G. Slightly increases surface expression in transfected pro-B cells and enhances interaction with FCER1G; when associated with 177-S--R-182. ^@ http://purl.uniprot.org/annotation/PRO_0000320125 http://togogenome.org/gene/10090:Ptger2 ^@ http://purl.uniprot.org/uniprot/Q543A9|||http://purl.uniprot.org/uniprot/Q62053 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||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|||N-linked (GlcNAc...) asparagine|||Prostaglandin E2 receptor EP2 subtype ^@ http://purl.uniprot.org/annotation/PRO_0000070055 http://togogenome.org/gene/10090:Tmem54 ^@ http://purl.uniprot.org/uniprot/A2A7R1|||http://purl.uniprot.org/uniprot/A2A7R2|||http://purl.uniprot.org/uniprot/Q9D6Y3|||http://purl.uniprot.org/uniprot/Q9D7S1 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 54 ^@ http://purl.uniprot.org/annotation/PRO_0000226990 http://togogenome.org/gene/10090:Ccdc9b ^@ http://purl.uniprot.org/uniprot/A3KGF9 ^@ 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|||Coiled-coil domain-containing protein 9B|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295734 http://togogenome.org/gene/10090:Rph3a ^@ http://purl.uniprot.org/uniprot/P47708 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||C2 1|||C2 2|||Disordered|||FYVE-type|||Omega-N-methylarginine|||Phosphoserine|||Pro residues|||RabBD|||Rabphilin-3A ^@ http://purl.uniprot.org/annotation/PRO_0000190228 http://togogenome.org/gene/10090:Rab22a ^@ http://purl.uniprot.org/uniprot/P35285|||http://purl.uniprot.org/uniprot/Q0PD34 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Lipid Binding|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Constitutively active. Disrupts general recycling of receptors in embryonic fibroblasts.|||Disordered|||Effector region|||Ras-related protein Rab-22A|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121210 http://togogenome.org/gene/10090:Cdc42ep1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0S1|||http://purl.uniprot.org/uniprot/Q91W92 ^@ 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|||2|||3|||3 X 7 AA tandem repeats of [PT]-[AT]-A-[ENT]-[PT]-[PTS]-[AG]|||Basic and acidic residues|||CRIB|||Cdc42 effector protein 1|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000212658 http://togogenome.org/gene/10090:Gm13889 ^@ http://purl.uniprot.org/uniprot/A0A087WSH6|||http://purl.uniprot.org/uniprot/Q3UPL5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Uncharacterized protein C11orf96 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000320642 http://togogenome.org/gene/10090:Zfp106 ^@ http://purl.uniprot.org/uniprot/R4GML0 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Acidic residues|||Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues|||WD ^@ http://togogenome.org/gene/10090:Cox4i1 ^@ http://purl.uniprot.org/uniprot/A2RSV8|||http://purl.uniprot.org/uniprot/P19783 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn ^@ Cytochrome c oxidase subunit 4 isoform 1, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000006085 http://togogenome.org/gene/10090:Parp6 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0T1|||http://purl.uniprot.org/uniprot/G5E856|||http://purl.uniprot.org/uniprot/Q6P6P7 ^@ 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.|||PARP catalytic|||Protein mono-ADP-ribosyltransferase PARP6 ^@ http://purl.uniprot.org/annotation/PRO_0000252431|||http://purl.uniprot.org/annotation/VSP_020967|||http://purl.uniprot.org/annotation/VSP_020968|||http://purl.uniprot.org/annotation/VSP_020969 http://togogenome.org/gene/10090:Kyat3 ^@ http://purl.uniprot.org/uniprot/Q71RI9 ^@ Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Splice Variant|||Strand|||Turn ^@ In isoform 2.|||Kynurenine--oxoglutarate transaminase 3|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000287705|||http://purl.uniprot.org/annotation/VSP_025605 http://togogenome.org/gene/10090:Tc2n ^@ http://purl.uniprot.org/uniprot/Q91XT6 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes nuclear localization.|||C2 1|||C2 2|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Tandem C2 domains nuclear protein ^@ http://purl.uniprot.org/annotation/PRO_0000072415 http://togogenome.org/gene/10090:Srms ^@ http://purl.uniprot.org/uniprot/Q0VBH4|||http://purl.uniprot.org/uniprot/Q8BQI4 ^@ Binding Site|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Domain Extent|||Non-terminal Residue ^@ Protein kinase|||SH2|||SH3 ^@ http://togogenome.org/gene/10090:Vmn2r77 ^@ http://purl.uniprot.org/uniprot/L7N2B7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://togogenome.org/gene/10090:Cpxcr1 ^@ http://purl.uniprot.org/uniprot/Q3V0P1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||CPX chromosomal region candidate gene 1 protein homolog|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000305345 http://togogenome.org/gene/10090:Odf4 ^@ http://purl.uniprot.org/uniprot/Q8VI88 ^@ 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 ^@ Disordered|||Helical|||In isoform 2.|||Outer dense fiber protein 4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000304723|||http://purl.uniprot.org/annotation/VSP_028117|||http://purl.uniprot.org/annotation/VSP_028118 http://togogenome.org/gene/10090:Abraxas1 ^@ http://purl.uniprot.org/uniprot/Q8BPZ8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ BRCA1-A complex subunit Abraxas 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||MPN|||Phosphoserine|||pSXXF motif ^@ http://purl.uniprot.org/annotation/PRO_0000278576|||http://purl.uniprot.org/annotation/VSP_023335|||http://purl.uniprot.org/annotation/VSP_023336 http://togogenome.org/gene/10090:Smbd1 ^@ http://purl.uniprot.org/uniprot/J3QPC1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ SMB ^@ http://purl.uniprot.org/annotation/PRO_5003776673 http://togogenome.org/gene/10090:Adam20 ^@ http://purl.uniprot.org/uniprot/Q7M763 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disintegrin|||Disordered|||EGF-like|||Helical|||Peptidase M12B ^@ http://togogenome.org/gene/10090:Bmp2 ^@ http://purl.uniprot.org/uniprot/P21274 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic residues|||Bone morphogenetic protein 2|||Cleaved by PCSK5|||Disordered|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000033826|||http://purl.uniprot.org/annotation/PRO_0000033827 http://togogenome.org/gene/10090:Gdf2 ^@ http://purl.uniprot.org/uniprot/Q9WV56 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Growth/differentiation factor 2|||Interaction with ENG|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033904|||http://purl.uniprot.org/annotation/PRO_0000033905 http://togogenome.org/gene/10090:Arhgef38 ^@ http://purl.uniprot.org/uniprot/Q80VK6 ^@ 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 ^@ BAR|||DH|||Disordered|||In isoform 1.|||In isoform 2.|||Phosphothreonine|||Polar residues|||Rho guanine nucleotide exchange factor 38|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000318988|||http://purl.uniprot.org/annotation/VSP_031334|||http://purl.uniprot.org/annotation/VSP_031335|||http://purl.uniprot.org/annotation/VSP_053831 http://togogenome.org/gene/10090:Trim9 ^@ http://purl.uniprot.org/uniprot/E9Q524|||http://purl.uniprot.org/uniprot/E9QLH4|||http://purl.uniprot.org/uniprot/Q3TR28|||http://purl.uniprot.org/uniprot/Q8C7M3 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ B box-type|||B box-type 1|||B box-type 2|||B30.2/SPRY|||COS|||Disordered|||E3 ubiquitin-protein ligase TRIM9|||Fibronectin type-III|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056209|||http://purl.uniprot.org/annotation/VSP_007930|||http://purl.uniprot.org/annotation/VSP_007931|||http://purl.uniprot.org/annotation/VSP_007932|||http://purl.uniprot.org/annotation/VSP_007933|||http://purl.uniprot.org/annotation/VSP_007934|||http://purl.uniprot.org/annotation/VSP_007935|||http://purl.uniprot.org/annotation/VSP_007936|||http://purl.uniprot.org/annotation/VSP_007937|||http://purl.uniprot.org/annotation/VSP_007938 http://togogenome.org/gene/10090:Hcn4 ^@ http://purl.uniprot.org/uniprot/B2RY58 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Cyclic nucleotide-binding|||Disordered|||Helical|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Sorcs2 ^@ http://purl.uniprot.org/uniprot/Q8BI61|||http://purl.uniprot.org/uniprot/Q8BI74|||http://purl.uniprot.org/uniprot/Q9EPR5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ BNR 1|||BNR 2|||BNR 3|||BNR 4|||BNR 5|||BNR 6|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Introduces an N-glycosylation site and disrupts interaction with NGF and BDNF.|||N-linked (GlcNAc...) asparagine|||PKD|||SorCS2 104 kDa chain|||SorCS2 122 kDa chain|||SorCS2 18 kDa chain|||VPS10|||VPS10 domain-containing receptor SorCS2 ^@ http://purl.uniprot.org/annotation/PRO_0000033173|||http://purl.uniprot.org/annotation/PRO_0000447472|||http://purl.uniprot.org/annotation/PRO_0000447473|||http://purl.uniprot.org/annotation/PRO_0000447474 http://togogenome.org/gene/10090:Zfp975 ^@ http://purl.uniprot.org/uniprot/Q6NVD6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dnm1l ^@ http://purl.uniprot.org/uniprot/A0A2U3TZ67|||http://purl.uniprot.org/uniprot/E9PUD2|||http://purl.uniprot.org/uniprot/Q8K1M6 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes GTP hydrolysis.|||B domain|||C-terminal dimerization domain|||Disordered|||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|||Important for homodimerization|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with GSK3B|||Loss of activity and phosphorylation. Unable to rescue aberrant mitochondrial fission in PINK1 null mutant neurons.|||Middle domain|||N-acetylmethionine|||N6-acetyllysine; alternate|||O-linked (GlcNAc) threonine|||Phosphoserine|||Phosphoserine; by CAMK1 and PKA|||Phosphoserine; by PINK1|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000206567|||http://purl.uniprot.org/annotation/VSP_013689|||http://purl.uniprot.org/annotation/VSP_013690|||http://purl.uniprot.org/annotation/VSP_013691|||http://purl.uniprot.org/annotation/VSP_013692|||http://purl.uniprot.org/annotation/VSP_013693|||http://purl.uniprot.org/annotation/VSP_013694|||http://purl.uniprot.org/annotation/VSP_013695 http://togogenome.org/gene/10090:Ivl ^@ http://purl.uniprot.org/uniprot/G3X9D9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Involucrin 2|||Involucrin N-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Atg3 ^@ http://purl.uniprot.org/uniprot/Q9CPX6 ^@ Active Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Chain|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Site ^@ Abolishes ATG12 conjugation, leading to an expansion in mitochondrial mass and fragmented mitochondrial morphology. Does not affect PE-conjugation to ATG8-like proteins.|||Abolishes E2-like activity.|||Cleavage; by CASP8|||Disordered|||Does not affect ATG12 conjugation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12)|||Glycyl thioester intermediate|||N-acetylmethionine|||Ubiquitin-like-conjugating enzyme ATG3 ^@ http://purl.uniprot.org/annotation/PRO_0000213570 http://togogenome.org/gene/10090:Gm6614 ^@ http://purl.uniprot.org/uniprot/L7N251 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Kazal-like|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:Scin ^@ http://purl.uniprot.org/uniprot/Q3UWV5|||http://purl.uniprot.org/uniprot/Q60604 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Actin-severing|||Ca(2+)-dependent actin binding|||Gelsolin-like|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||Gelsolin-like 6|||In isoform 2.|||Phosphotyrosine|||Scinderin ^@ http://purl.uniprot.org/annotation/PRO_0000218745|||http://purl.uniprot.org/annotation/VSP_006730 http://togogenome.org/gene/10090:Gnl1 ^@ http://purl.uniprot.org/uniprot/P36916|||http://purl.uniprot.org/uniprot/Q52KE3 ^@ 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 ^@ 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_0000122442|||http://purl.uniprot.org/annotation/VSP_026994|||http://purl.uniprot.org/annotation/VSP_026995 http://togogenome.org/gene/10090:Tbr1 ^@ http://purl.uniprot.org/uniprot/Q64336 ^@ 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 ^@ Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||T-box|||T-box brain protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000184458 http://togogenome.org/gene/10090:Kcnt1 ^@ http://purl.uniprot.org/uniprot/A0A0G2JER3|||http://purl.uniprot.org/uniprot/A2AHB7|||http://purl.uniprot.org/uniprot/A2AHB8|||http://purl.uniprot.org/uniprot/A2AHB9|||http://purl.uniprot.org/uniprot/C0KTP6|||http://purl.uniprot.org/uniprot/Q6ZPR4|||http://purl.uniprot.org/uniprot/Q8C853 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Non-terminal Residue|||Region|||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|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pore-forming|||Potassium channel|||Potassium channel subfamily T member 1|||RCK N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000054091 http://togogenome.org/gene/10090:Zfp955a ^@ http://purl.uniprot.org/uniprot/Q80XR7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Tada2a ^@ http://purl.uniprot.org/uniprot/Q8CHV6 ^@ Binding Site|||Chain|||Crosslink|||DNA Binding|||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|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Loss of nuclear localization. Reduces DNA binding.|||Phosphoserine|||Reduces DNA binding.|||SANT|||SWIRM|||Transcriptional adapter 2-alpha|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000240669 http://togogenome.org/gene/10090:Tmem109 ^@ http://purl.uniprot.org/uniprot/Q3UBX0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Voltage-gated monoatomic cation channel TMEM109 ^@ http://purl.uniprot.org/annotation/PRO_0000044619 http://togogenome.org/gene/10090:Vmn2r86 ^@ http://purl.uniprot.org/uniprot/G5E8Y4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015091916 http://togogenome.org/gene/10090:Cyp2d22 ^@ http://purl.uniprot.org/uniprot/Q9JKY7 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Smg6 ^@ http://purl.uniprot.org/uniprot/P61406 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||EJC-binding motif 1; mediates interaction with the EJC|||EJC-binding motif 2; mediates interaction with the EJC|||Omega-N-methylarginine|||PINc|||Phosphoserine|||Phosphothreonine|||Polar residues|||Telomerase-binding protein EST1A ^@ http://purl.uniprot.org/annotation/PRO_0000087070 http://togogenome.org/gene/10090:Foxj3 ^@ http://purl.uniprot.org/uniprot/Q8BUR3 ^@ 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 ^@ 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_0000091856|||http://purl.uniprot.org/annotation/VSP_010368 http://togogenome.org/gene/10090:Celf6 ^@ http://purl.uniprot.org/uniprot/D3YX51|||http://purl.uniprot.org/uniprot/Q7TN33 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ CUGBP Elav-like family member 6|||Disordered|||In isoform 2.|||Polar residues|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000295230|||http://purl.uniprot.org/annotation/VSP_026849 http://togogenome.org/gene/10090:Trim63 ^@ http://purl.uniprot.org/uniprot/F8VPZ1|||http://purl.uniprot.org/uniprot/Q8CFN7 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Acidic residues|||B box-type|||COS|||Disordered|||RING-type ^@ http://togogenome.org/gene/10090:Igbp1b ^@ http://purl.uniprot.org/uniprot/A0A0B4J1F7 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:AI837181 ^@ http://purl.uniprot.org/uniprot/Q8VD62 ^@ 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 1.|||UPF0696 protein C11orf68 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000228118|||http://purl.uniprot.org/annotation/VSP_059973|||http://purl.uniprot.org/annotation/VSP_059974 http://togogenome.org/gene/10090:Hddc2 ^@ http://purl.uniprot.org/uniprot/Q3SXD3 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ 5'-deoxynucleotidase HDDC2|||HD|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000311390 http://togogenome.org/gene/10090:Chil6 ^@ http://purl.uniprot.org/uniprot/Q80W26 ^@ Domain Extent|||Region ^@ Domain Extent ^@ GH18 ^@ http://togogenome.org/gene/10090:Egfl7 ^@ http://purl.uniprot.org/uniprot/Q3UTJ7|||http://purl.uniprot.org/uniprot/Q9QXT5 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Signal Peptide|||Splice Variant ^@ Cell attachment site|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EMI|||Epidermal growth factor-like protein 7|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000007529|||http://purl.uniprot.org/annotation/PRO_5015097512|||http://purl.uniprot.org/annotation/VSP_011765 http://togogenome.org/gene/10090:Rps15 ^@ http://purl.uniprot.org/uniprot/P62843 ^@ 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)|||N-acetylalanine|||Removed|||Small ribosomal subunit protein uS19 ^@ http://purl.uniprot.org/annotation/PRO_0000130029 http://togogenome.org/gene/10090:Nthl1 ^@ http://purl.uniprot.org/uniprot/O35980 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Site|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||Endonuclease III-like protein 1|||HhH|||Important for catalytic activity|||Mitochondrion|||Nucleophile; for N-glycosylase activity|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000102228 http://togogenome.org/gene/10090:Dmrta2 ^@ http://purl.uniprot.org/uniprot/A2A9A2 ^@ 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 ^@ DM|||DMA|||Disordered|||Doublesex- and mab-3-related transcription factor A2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000333773 http://togogenome.org/gene/10090:Kndc1 ^@ http://purl.uniprot.org/uniprot/Q0KK55 ^@ 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 ^@ Abolishes interaction with MAP2.|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||KIND 1|||KIND 2|||Kinase non-catalytic C-lobe domain-containing protein 1|||N-terminal Ras-GEF|||No effect on interaction with MAP2.|||Phosphoserine|||Polar residues|||Ras-GEF ^@ http://purl.uniprot.org/annotation/PRO_0000307142|||http://purl.uniprot.org/annotation/VSP_028599|||http://purl.uniprot.org/annotation/VSP_028600|||http://purl.uniprot.org/annotation/VSP_028601 http://togogenome.org/gene/10090:Tjp3 ^@ http://purl.uniprot.org/uniprot/Q3UZ47|||http://purl.uniprot.org/uniprot/Q921G9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Guanylate kinase-like|||PDZ|||SH3 ^@ http://togogenome.org/gene/10090:Blvrb ^@ http://purl.uniprot.org/uniprot/E9PZC4|||http://purl.uniprot.org/uniprot/Q3U6G1|||http://purl.uniprot.org/uniprot/Q923D2 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Flavin reductase (NADPH)|||NAD(P)-binding|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000064949 http://togogenome.org/gene/10090:Ifnar1 ^@ http://purl.uniprot.org/uniprot/P33896 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes interaction with FBXW11. Prevents interalization from the cell membrane and lysosomal degradation.|||Cytoplasmic|||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|||Important for interaction with TYK2|||Interferon alpha/beta receptor 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000011002 http://togogenome.org/gene/10090:Usp12 ^@ http://purl.uniprot.org/uniprot/Q9D9M2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 12 ^@ http://purl.uniprot.org/annotation/PRO_0000260312|||http://purl.uniprot.org/annotation/VSP_037617 http://togogenome.org/gene/10090:9130019O22Rik ^@ http://purl.uniprot.org/uniprot/G3X941 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Clnk ^@ http://purl.uniprot.org/uniprot/Q9QZE2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Basic and acidic residues|||Cytokine-dependent hematopoietic cell linker|||Disordered|||In isoform 2.|||Increases natural killer cell activation and interferon-gamma production. Loss of FGR binding.|||Interaction with FYB1|||Loss of binding to FYB1 and MAP4K1. Reduced tyrosine phosphorylation. No effect on the suppression of natural killer cell activation and suppression of interferon-gamma production.|||Loss of phosphorylation and loss of interaction with PLCG1, PLCG2 and VAV. No effect on the suppression of natural killer cell activation and suppression of interferon-gamma production; when associated with F-69, F-101, F-153, F-174 and F-188.|||Loss of phosphorylation and loss of interaction with PLCG1, PLCG2 and VAV. No effect on the suppression of natural killer cell activation and suppression of interferon-gamma production; when associated with F-69, F-96, F-101, F-153 and F-174.|||Loss of phosphorylation and loss of interaction with PLCG1, PLCG2 and VAV. No effect on the suppression of natural killer cell activation and suppression of interferon-gamma production; when associated with F-69, F-96, F-101, F-153 and F-188.|||Loss of phosphorylation and loss of interaction with PLCG1, PLCG2 and VAV. No effect on the suppression of natural killer cell activation and suppression of interferon-gamma production; when associated with F-69, F-96, F-101, F-174 and F-188.|||Loss of phosphorylation and loss of interaction with PLCG1, PLCG2 and VAV. No effect on the suppression of natural killer cell activation and suppression of interferon-gamma production; when associated with F-69, F-96, F-153, F-174 and F-188.|||Loss of phosphorylation and loss of interaction with PLCG1, PLCG2 and VAV. No effect on the suppression of natural killer cell activation and suppression of interferon-gamma production; when associated with F-96, F-101, F-153, F-174 and F-188.|||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|||Slightly increases natural killer cell activation and interferon-gamma production. ^@ http://purl.uniprot.org/annotation/PRO_0000314598|||http://purl.uniprot.org/annotation/VSP_030334 http://togogenome.org/gene/10090:Larp1b ^@ http://purl.uniprot.org/uniprot/A0A0A6YWC2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||HTH La-type RNA-binding|||Polar residues ^@ http://togogenome.org/gene/10090:Foxp4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J161|||http://purl.uniprot.org/uniprot/A0A0R4J1I5|||http://purl.uniprot.org/uniprot/Q9DBY0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||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|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C2H2-type|||Disordered|||Fork-head|||Forkhead box protein P4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||Leucine-zipper|||Loss of dimerization. Almost complete loss of DNA-binding. Reduced transcriptional repression activity.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247653|||http://purl.uniprot.org/annotation/VSP_052129|||http://purl.uniprot.org/annotation/VSP_052130|||http://purl.uniprot.org/annotation/VSP_052131 http://togogenome.org/gene/10090:Cenpi ^@ http://purl.uniprot.org/uniprot/Q3TTB0|||http://purl.uniprot.org/uniprot/Q8K1K4 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Centromere protein I|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000087355 http://togogenome.org/gene/10090:Ubash3b ^@ http://purl.uniprot.org/uniprot/Q8BGG7 ^@ 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 ^@ In isoform 2.|||Phosphoserine|||Phosphothreonine|||Protein tyrosine phosphatase|||SH3|||Tele-phosphohistidine intermediate|||UBA|||Ubiquitin-associated and SH3 domain-containing protein B ^@ http://purl.uniprot.org/annotation/PRO_0000245509|||http://purl.uniprot.org/annotation/VSP_019716 http://togogenome.org/gene/10090:Efna1 ^@ http://purl.uniprot.org/uniprot/D3YTT5|||http://purl.uniprot.org/uniprot/P52793|||http://purl.uniprot.org/uniprot/Q9D7K8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Ephrin RBD|||Ephrin RBD domain-containing protein|||Ephrin-A1|||Ephrin-A1, secreted form|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000008355|||http://purl.uniprot.org/annotation/PRO_0000008356|||http://purl.uniprot.org/annotation/PRO_0000389631|||http://purl.uniprot.org/annotation/PRO_5004325893 http://togogenome.org/gene/10090:Pex19 ^@ http://purl.uniprot.org/uniprot/Q8VCI5 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ Cysteine methyl ester|||Disordered|||Docking to the peroxisome membrane and binding to PEX3|||In isoform 2.|||N-acetylalanine|||Necessary for PEX19 function on peroxisome biogenesis|||Peroxisomal biogenesis factor 19|||Phosphoserine|||Phosphothreonine|||Removed|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000218760|||http://purl.uniprot.org/annotation/PRO_0000396701|||http://purl.uniprot.org/annotation/VSP_012652 http://togogenome.org/gene/10090:Lmbrd2 ^@ http://purl.uniprot.org/uniprot/Q8C561 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor-associated protein LMBRD2|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000299162|||http://purl.uniprot.org/annotation/VSP_027568|||http://purl.uniprot.org/annotation/VSP_027569 http://togogenome.org/gene/10090:Or2a56 ^@ http://purl.uniprot.org/uniprot/Q8VFS6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ubl3 ^@ http://purl.uniprot.org/uniprot/Q9Z2M6 ^@ Chain|||Domain Extent|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Strand|||Turn ^@ 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_0000114863|||http://purl.uniprot.org/annotation/PRO_0000248184 http://togogenome.org/gene/10090:Mical3 ^@ http://purl.uniprot.org/uniprot/Q5CZW8|||http://purl.uniprot.org/uniprot/Q8CJ19 ^@ 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|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LIM zinc-binding|||Monooxygenase domain|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||[F-actin]-monooxygenase MICAL3|||bMERB ^@ http://purl.uniprot.org/annotation/PRO_0000075847|||http://purl.uniprot.org/annotation/VSP_039490|||http://purl.uniprot.org/annotation/VSP_039491|||http://purl.uniprot.org/annotation/VSP_039492|||http://purl.uniprot.org/annotation/VSP_039493|||http://purl.uniprot.org/annotation/VSP_039494|||http://purl.uniprot.org/annotation/VSP_039495 http://togogenome.org/gene/10090:Sh2b2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JED4|||http://purl.uniprot.org/uniprot/Q9JID9 ^@ 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 ^@ Disordered|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SH2|||SH2B adapter protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000064648 http://togogenome.org/gene/10090:Ifi204 ^@ http://purl.uniprot.org/uniprot/P0DOV2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ 1|||2|||3|||3 X 7 AA tandem repeats of A-[GR]-T-S-T-A-Q|||Basic and acidic residues|||Disordered|||HIN-200 1|||HIN-200 2|||Interaction with ID2|||Interferon-activable protein 204|||Nuclear export signal|||Nuclear localization signal|||Polar residues|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000153721 http://togogenome.org/gene/10090:Atp5c1 ^@ http://purl.uniprot.org/uniprot/Q91VR2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ ATP synthase subunit gamma, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000002686 http://togogenome.org/gene/10090:Defb25 ^@ http://purl.uniprot.org/uniprot/Q30KN8 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 25 ^@ http://purl.uniprot.org/annotation/PRO_0000352707 http://togogenome.org/gene/10090:Yipf2 ^@ http://purl.uniprot.org/uniprot/Q99LP8 ^@ 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|||Protein YIPF2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000241455 http://togogenome.org/gene/10090:Alpi ^@ http://purl.uniprot.org/uniprot/F8VPQ6 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Signal Peptide ^@ Alkaline phosphatase|||Phosphoserine intermediate ^@ http://purl.uniprot.org/annotation/PRO_5003379231 http://togogenome.org/gene/10090:Spink14 ^@ http://purl.uniprot.org/uniprot/B9EJP9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Kazal-like ^@ http://purl.uniprot.org/annotation/PRO_5015087495 http://togogenome.org/gene/10090:Lcn8 ^@ http://purl.uniprot.org/uniprot/Q924P3 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Epididymal-specific lipocalin-8|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017917 http://togogenome.org/gene/10090:Pnp ^@ http://purl.uniprot.org/uniprot/P23492|||http://purl.uniprot.org/uniprot/Q543K9 ^@ 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|||Site ^@ Important for substrate specificity|||In haplotype NPB.|||In haplotype NPC.|||In haplotype NPD.|||N-acetylmethionine|||Nucleoside phosphorylase|||Purine nucleoside phosphorylase ^@ http://purl.uniprot.org/annotation/PRO_0000184537 http://togogenome.org/gene/10090:Eva1b ^@ http://purl.uniprot.org/uniprot/Q8K2Y3 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ Acidic residues|||Disordered|||Helical|||Phosphothreonine|||Polar residues|||Protein eva-1 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000271113 http://togogenome.org/gene/10090:Iba57 ^@ http://purl.uniprot.org/uniprot/Q8CAK1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Putative transferase CAF17 homolog, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000278634 http://togogenome.org/gene/10090:Erp44 ^@ http://purl.uniprot.org/uniprot/Q9D1Q6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Signal Peptide ^@ Disordered|||Endoplasmic reticulum resident protein 44|||Interaction with ITPR1|||No effect on interaction with ITPR1.|||Polar residues|||Prevents secretion from ER|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000034181 http://togogenome.org/gene/10090:Plekha8 ^@ http://purl.uniprot.org/uniprot/Q80W71 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||Glycolipid transfer protein homology domain|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology domain-containing family A member 8 ^@ http://purl.uniprot.org/annotation/PRO_0000306866|||http://purl.uniprot.org/annotation/VSP_028547 http://togogenome.org/gene/10090:Or51k1 ^@ http://purl.uniprot.org/uniprot/Q8VGY8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Caskin2 ^@ http://purl.uniprot.org/uniprot/Q8VHK1 ^@ 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|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Caskin-2|||Disordered|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SAM 1|||SAM 2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000066984 http://togogenome.org/gene/10090:Fzr1 ^@ http://purl.uniprot.org/uniprot/Q3U3D4|||http://purl.uniprot.org/uniprot/Q9R1K5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Anaphase-promoting complex subunit 4-like WD40|||Basic and acidic residues|||Disordered|||Fizzy-related protein homolog|||N6-acetyllysine|||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_0000051002 http://togogenome.org/gene/10090:Lrp6 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0A9|||http://purl.uniprot.org/uniprot/O88572 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Beta-propeller 1|||Beta-propeller 2|||Beta-propeller 3|||Beta-propeller 4|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In rs.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||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 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|||Low-density lipoprotein receptor-related protein 6|||N-linked (GlcNAc...) asparagine|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000017331|||http://purl.uniprot.org/annotation/PRO_5010897944 http://togogenome.org/gene/10090:Nostrin ^@ http://purl.uniprot.org/uniprot/Q6WKZ7 ^@ 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 ^@ Disordered|||F-BAR|||Nostrin|||Phosphoserine|||Polar residues|||REM-1|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000289090 http://togogenome.org/gene/10090:Ndc80 ^@ http://purl.uniprot.org/uniprot/Q9D0F1 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||N6-acetyllysine|||Nuclear localization|||Phosphoserine|||Phosphoserine; by NEK2 ^@ http://purl.uniprot.org/annotation/PRO_0000249552 http://togogenome.org/gene/10090:P2ry1 ^@ http://purl.uniprot.org/uniprot/P49650|||http://purl.uniprot.org/uniprot/Q544J5|||http://purl.uniprot.org/uniprot/Q8BMJ5 ^@ 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|||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|||P2Y purinoceptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000070007 http://togogenome.org/gene/10090:Igsf1 ^@ http://purl.uniprot.org/uniprot/Q7TQA1 ^@ 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 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 isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000318513|||http://purl.uniprot.org/annotation/VSP_031198|||http://purl.uniprot.org/annotation/VSP_031199|||http://purl.uniprot.org/annotation/VSP_031200|||http://purl.uniprot.org/annotation/VSP_031201|||http://purl.uniprot.org/annotation/VSP_031202|||http://purl.uniprot.org/annotation/VSP_031203 http://togogenome.org/gene/10090:Ghrhr ^@ http://purl.uniprot.org/uniprot/P32082 ^@ 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|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Growth hormone-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 lit.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000012829 http://togogenome.org/gene/10090:Rpl9 ^@ http://purl.uniprot.org/uniprot/P51410|||http://purl.uniprot.org/uniprot/Q5EBQ6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Variant ^@ In UV-induced tumor 6132A antigen.|||Large ribosomal subunit protein uL6|||Large ribosomal subunit protein uL6 alpha-beta|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000131099 http://togogenome.org/gene/10090:Mzf1 ^@ http://purl.uniprot.org/uniprot/A1L357|||http://purl.uniprot.org/uniprot/A1L358|||http://purl.uniprot.org/uniprot/S4R1L6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues|||SCAN box ^@ http://togogenome.org/gene/10090:Cldn34c2 ^@ http://purl.uniprot.org/uniprot/A0A571BG29 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Pcdhga6 ^@ http://purl.uniprot.org/uniprot/Q91XY2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099497 http://togogenome.org/gene/10090:Cdk2ap2 ^@ http://purl.uniprot.org/uniprot/Q9CPY4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Cyclin-dependent kinase 2-associated protein 2|||Disordered|||Interaction with CDK2|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000079964 http://togogenome.org/gene/10090:Sag ^@ http://purl.uniprot.org/uniprot/P20443|||http://purl.uniprot.org/uniprot/Q3UPX6 ^@ 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 ^@ Abrogates tetramerization, reduces dimerization, does not affect binding to microtubules and to phosphorylated light-activated rhodopsin; when associated with A-198, or with A-198 and V-349.|||Abrogates tetramerization, reduces dimerization, does not affect binding to microtubules and to phosphorylated light-activated rhodopsin; when associated with A-86 and A-198.|||Abrogates tetramerization, reduces dimerization, does not affect binding to microtubules and to phosphorylated light-activated rhodopsin; when associated with A-86, or with A-86 and V-349.|||Arrestin C-terminal-like|||Disordered|||Interaction with RHO|||Phosphothreonine|||S-arrestin|||Strongly increases affinity for RHO. ^@ http://purl.uniprot.org/annotation/PRO_0000205187 http://togogenome.org/gene/10090:Ttll2 ^@ http://purl.uniprot.org/uniprot/A4Q9E4 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Site ^@ Disordered|||Essential for specifying initiation versus elongation step of the polyglutamylase activity|||Probable tubulin polyglutamylase TTLL2|||TTL ^@ http://purl.uniprot.org/annotation/PRO_0000326158 http://togogenome.org/gene/10090:Cdh4 ^@ http://purl.uniprot.org/uniprot/P39038|||http://purl.uniprot.org/uniprot/Q80ZV4 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-4|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000003751|||http://purl.uniprot.org/annotation/PRO_0000003752|||http://purl.uniprot.org/annotation/PRO_5015098936 http://togogenome.org/gene/10090:Ackr1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0J4|||http://purl.uniprot.org/uniprot/Q9QUI6 ^@ 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 ^@ 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 strain: BLG2/Msf, C57BL/10SnJ, CAST/Ei, HMI/Msf, MSM/Msf, NJL/Msf and SWN/Msf.|||In strain: BLG2/Msf, C57BL/10SnJ, CAST/Ei, HMI/Msf, MSM/Msf, NJL/Msf, pgn2 and SWN/Msf.|||In strain: BLG2/Msf, C57BL/10SnJ, HMI/Msf, MSM/Msf, NJL/Msf and SWN/Msf.|||In strain: BLG2/Msf.|||In strain: C57BL/10SnJ, HMI/Msf, MSM/Msf and SWN/Msf.|||In strain: NJL/Msf.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000152587 http://togogenome.org/gene/10090:Slc40a1 ^@ http://purl.uniprot.org/uniprot/Q9JHI9 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Solute carrier family 40 member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000191311 http://togogenome.org/gene/10090:Cmtm2a ^@ http://purl.uniprot.org/uniprot/Q9DAR1 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Splice Variant|||Transmembrane ^@ CKLF-like MARVEL transmembrane domain-containing protein 2A|||Helical|||In isoform 2.|||In isoform 3.|||MARVEL ^@ http://purl.uniprot.org/annotation/PRO_0000186099|||http://purl.uniprot.org/annotation/VSP_008253|||http://purl.uniprot.org/annotation/VSP_008254|||http://purl.uniprot.org/annotation/VSP_008255 http://togogenome.org/gene/10090:Megf6 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ83 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ EGF-like|||EMI ^@ http://purl.uniprot.org/annotation/PRO_5001974140 http://togogenome.org/gene/10090:Gm5127 ^@ http://purl.uniprot.org/uniprot/Q3UQH6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wdr36 ^@ http://purl.uniprot.org/uniprot/Q3TA68|||http://purl.uniprot.org/uniprot/Q3TAQ9|||http://purl.uniprot.org/uniprot/Q8BHI6 ^@ Domain Extent|||Region|||Repeat ^@ Domain Extent|||Repeat ^@ Anaphase-promoting complex subunit 4-like WD40|||Small-subunit processome Utp21|||WD ^@ http://togogenome.org/gene/10090:Emc8 ^@ http://purl.uniprot.org/uniprot/O70378|||http://purl.uniprot.org/uniprot/Q3TPU5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ ER membrane protein complex subunit 8|||MPN ^@ http://purl.uniprot.org/annotation/PRO_0000221188 http://togogenome.org/gene/10090:Kcnk9 ^@ http://purl.uniprot.org/uniprot/Q3LS21 ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||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_0000101755 http://togogenome.org/gene/10090:Arf3 ^@ http://purl.uniprot.org/uniprot/P61205 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding ^@ ADP-ribosylation factor 3|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207387 http://togogenome.org/gene/10090:Wnt2 ^@ http://purl.uniprot.org/uniprot/P21552|||http://purl.uniprot.org/uniprot/Q8BRC7 ^@ 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|||Protein Wnt-2 ^@ http://purl.uniprot.org/annotation/PRO_0000041411|||http://purl.uniprot.org/annotation/PRO_5004305942 http://togogenome.org/gene/10090:Defa21 ^@ http://purl.uniprot.org/uniprot/Q8C1P2 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Alpha-defensin 21|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000300068|||http://purl.uniprot.org/annotation/PRO_0000300069 http://togogenome.org/gene/10090:Slc7a1 ^@ http://purl.uniprot.org/uniprot/Q09143|||http://purl.uniprot.org/uniprot/Q3TQZ8|||http://purl.uniprot.org/uniprot/Q3UGD6 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Topological Domain|||Transmembrane ^@ Cationic amino acid transporter C-terminal|||Cytoplasmic|||Extracellular|||Helical|||High affinity cationic amino acid transporter 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000054262 http://togogenome.org/gene/10090:Zc3h8 ^@ http://purl.uniprot.org/uniprot/Q9JJ48 ^@ 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 ^@ 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|||Polar residues|||Zinc finger CCCH domain-containing protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000213904 http://togogenome.org/gene/10090:Klrg1 ^@ http://purl.uniprot.org/uniprot/O88713 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes the formation of KLRG1/PTPN11 and KLRG1/INPP5D.|||Abrogates completely INPP5D recruitment.|||C-type lectin|||Cytoplasmic|||Decreases association with PTPN11.|||Enhances association with PTPN11.|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||ITIM motif|||Killer cell lectin-like receptor subfamily G member 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000331257 http://togogenome.org/gene/10090:Or6c66 ^@ http://purl.uniprot.org/uniprot/Q7TRH8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nopchap1 ^@ http://purl.uniprot.org/uniprot/Q9CX66 ^@ 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|||NOP protein chaperone 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000263624 http://togogenome.org/gene/10090:Hp1bp3 ^@ http://purl.uniprot.org/uniprot/Q3TEA8 ^@ 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 SUMO2)|||H15 1|||H15 2|||H15 3|||Heterochromatin protein 1-binding protein 3|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||PxVxL motif|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000339643|||http://purl.uniprot.org/annotation/VSP_034174|||http://purl.uniprot.org/annotation/VSP_034175 http://togogenome.org/gene/10090:Patl2 ^@ http://purl.uniprot.org/uniprot/A2ARM1 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Protein PAT1 homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000404578 http://togogenome.org/gene/10090:Rsph9 ^@ http://purl.uniprot.org/uniprot/Q9D9V4 ^@ Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Strand|||Turn ^@ Radial spoke head protein 9 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089562 http://togogenome.org/gene/10090:Pdxdc1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J034|||http://purl.uniprot.org/uniprot/Q99K01 ^@ 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.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pyridoxal-dependent decarboxylase domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000297678|||http://purl.uniprot.org/annotation/VSP_027344|||http://purl.uniprot.org/annotation/VSP_027345|||http://purl.uniprot.org/annotation/VSP_027346|||http://purl.uniprot.org/annotation/VSP_029421|||http://purl.uniprot.org/annotation/VSP_029422 http://togogenome.org/gene/10090:Mrgpre ^@ http://purl.uniprot.org/uniprot/Q4V9R2|||http://purl.uniprot.org/uniprot/Q91ZB7 ^@ 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|||Mas-related G-protein coupled receptor member E|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069762 http://togogenome.org/gene/10090:Klra8 ^@ http://purl.uniprot.org/uniprot/Q3UPS5|||http://purl.uniprot.org/uniprot/Q60682 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform H2.|||Killer cell lectin-like receptor 8|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046686|||http://purl.uniprot.org/annotation/VSP_003071 http://togogenome.org/gene/10090:Gal ^@ http://purl.uniprot.org/uniprot/A0A498WGR4|||http://purl.uniprot.org/uniprot/P47212|||http://purl.uniprot.org/uniprot/Q3V002 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide ^@ Galanin|||Galanin message-associated peptide|||Galanin peptides|||Phosphoserine|||Threonine amide ^@ http://purl.uniprot.org/annotation/PRO_0000010451|||http://purl.uniprot.org/annotation/PRO_0000010452|||http://purl.uniprot.org/annotation/PRO_0000010453|||http://purl.uniprot.org/annotation/PRO_5014309242|||http://purl.uniprot.org/annotation/PRO_5030095951 http://togogenome.org/gene/10090:Pyroxd1 ^@ http://purl.uniprot.org/uniprot/Q3TMV7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ N-acetylmethionine|||Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000327420 http://togogenome.org/gene/10090:Or1f19 ^@ http://purl.uniprot.org/uniprot/Q8VGB9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Apbb1ip ^@ http://purl.uniprot.org/uniprot/B1AYC9|||http://purl.uniprot.org/uniprot/Q8R5A3 ^@ 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 ^@ Amyloid beta A4 precursor protein-binding family B member 1-interacting protein|||Disordered|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Ras-associating ^@ http://purl.uniprot.org/annotation/PRO_0000181348 http://togogenome.org/gene/10090:Slc25a38 ^@ http://purl.uniprot.org/uniprot/Q91XD8 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Repeat|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial glycine transporter|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000291803 http://togogenome.org/gene/10090:Zfp229 ^@ http://purl.uniprot.org/uniprot/E9PWT2|||http://purl.uniprot.org/uniprot/Q80ZY7 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Csnk1d ^@ http://purl.uniprot.org/uniprot/Q3UBT6|||http://purl.uniprot.org/uniprot/Q3USK2|||http://purl.uniprot.org/uniprot/Q9DC28 ^@ 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 NEDD9 phosphorylation.|||Autoinhibitory|||Basic and acidic residues|||Casein kinase I isoform delta|||Centrosomal localization signal (CLS)|||Disordered|||In isoform 2.|||Increases pain sensitivity; reduces threshold for induction of cortical spreading depression; increases arterial dilation during cortical spreading depression and increases spontaneous and evoked calcium signaling in astrocytes.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000192834|||http://purl.uniprot.org/annotation/VSP_010254 http://togogenome.org/gene/10090:Spred3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0K0|||http://purl.uniprot.org/uniprot/Q6P6N5 ^@ 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 ^@ Asymmetric dimethylarginine|||Disordered|||KBD|||Omega-N-methylarginine|||Polar residues|||Pro residues|||SPR|||Sprouty-related, EVH1 domain-containing protein 3|||WH1 ^@ http://purl.uniprot.org/annotation/PRO_0000076914 http://togogenome.org/gene/10090:Chrm1 ^@ http://purl.uniprot.org/uniprot/P12657 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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|||Muscarinic acetylcholine receptor M1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069017 http://togogenome.org/gene/10090:Cyb5r4 ^@ http://purl.uniprot.org/uniprot/Q3TDX8 ^@ 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 ^@ CS|||Cytochrome b5 heme-binding|||Cytochrome b5 reductase 4|||Disordered|||FAD-binding FR-type|||In isoform 2.|||N-acetylmethionine|||Polar residues|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000410469|||http://purl.uniprot.org/annotation/VSP_041453 http://togogenome.org/gene/10090:Ntrk2 ^@ http://purl.uniprot.org/uniprot/A0A286YDA3|||http://purl.uniprot.org/uniprot/P15209|||http://purl.uniprot.org/uniprot/Q3UHE3 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ BDNF/NT-3 growth factors receptor|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like domain-containing protein|||In isoform GP95-TRKB.|||In isoform L1.|||In isoform L10.|||Interaction with MAPK8IP3/JIP3|||Interaction with PLCG1|||Interaction with SH2D1A|||Interaction with SHC1|||LRR 1|||LRR 2|||LRRCT|||LRRNT|||Loss of interaction with PLCG1.|||Loss of interaction with SHC1.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000016728|||http://purl.uniprot.org/annotation/PRO_5004230160|||http://purl.uniprot.org/annotation/PRO_5011488593|||http://purl.uniprot.org/annotation/VSP_002905|||http://purl.uniprot.org/annotation/VSP_002906|||http://purl.uniprot.org/annotation/VSP_002907|||http://purl.uniprot.org/annotation/VSP_002908|||http://purl.uniprot.org/annotation/VSP_002909 http://togogenome.org/gene/10090:Dlst ^@ http://purl.uniprot.org/uniprot/Q9D2G2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial|||Disordered|||In isoform 2.|||Lipoyl-binding|||Mitochondrion|||N6-acetyllysine|||N6-lipoyllysine|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000020473|||http://purl.uniprot.org/annotation/VSP_025015|||http://purl.uniprot.org/annotation/VSP_025016 http://togogenome.org/gene/10090:Inava ^@ http://purl.uniprot.org/uniprot/G3X9Z8|||http://purl.uniprot.org/uniprot/Q7TN12 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Cytohesin Ubiquitin Protein Inducing|||Disordered|||Innate immunity activator protein|||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_0000251730 http://togogenome.org/gene/10090:6330403K07Rik ^@ http://purl.uniprot.org/uniprot/Q6NSQ3|||http://purl.uniprot.org/uniprot/Q8VBZ2 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Twf1 ^@ http://purl.uniprot.org/uniprot/Q91YR1 ^@ 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|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Twinfilin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000214951 http://togogenome.org/gene/10090:Mpzl3 ^@ http://purl.uniprot.org/uniprot/Q3V3F6 ^@ 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 rc.|||Myelin protein zero-like protein 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000280283|||http://purl.uniprot.org/annotation/VSP_023606|||http://purl.uniprot.org/annotation/VSP_023607 http://togogenome.org/gene/10090:Huwe1 ^@ http://purl.uniprot.org/uniprot/A2AFQ0|||http://purl.uniprot.org/uniprot/Q3TNP1|||http://purl.uniprot.org/uniprot/Q4JG03|||http://purl.uniprot.org/uniprot/Q7TMY8 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||DUF908|||DUF913|||Disordered|||E3 ubiquitin-protein ligase HUWE1|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||UBA|||UIM|||WWE ^@ http://purl.uniprot.org/annotation/PRO_0000120341|||http://purl.uniprot.org/annotation/VSP_011147|||http://purl.uniprot.org/annotation/VSP_011148|||http://purl.uniprot.org/annotation/VSP_011149|||http://purl.uniprot.org/annotation/VSP_011150|||http://purl.uniprot.org/annotation/VSP_011151 http://togogenome.org/gene/10090:Serpina1f ^@ http://purl.uniprot.org/uniprot/E9PUC6|||http://purl.uniprot.org/uniprot/G3X9Z5|||http://purl.uniprot.org/uniprot/Q9DCQ7 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Alpha-1-antitrypsin 1-6|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_0000347280|||http://purl.uniprot.org/annotation/PRO_5003244241|||http://purl.uniprot.org/annotation/PRO_5015091851|||http://purl.uniprot.org/annotation/VSP_052895 http://togogenome.org/gene/10090:Dcaf13 ^@ http://purl.uniprot.org/uniprot/Q6PAC3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ DDB1- and CUL4-associated factor 13|||N6-acetyllysine|||Required for nucleolar location|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000310429 http://togogenome.org/gene/10090:Optc ^@ http://purl.uniprot.org/uniprot/E9PUR1|||http://purl.uniprot.org/uniprot/G3UVW2|||http://purl.uniprot.org/uniprot/Q14BF5|||http://purl.uniprot.org/uniprot/Q3U5A9|||http://purl.uniprot.org/uniprot/Q4KL49|||http://purl.uniprot.org/uniprot/Q920A0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage; by MMP13|||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_0000032766|||http://purl.uniprot.org/annotation/PRO_5004182989|||http://purl.uniprot.org/annotation/PRO_5004229823|||http://purl.uniprot.org/annotation/PRO_5004239854 http://togogenome.org/gene/10090:Chchd4 ^@ http://purl.uniprot.org/uniprot/Q8VEA4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Domain Extent|||Motif|||Region ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||Mitochondrial intermembrane space import and assembly protein 40|||Redox-active ^@ http://purl.uniprot.org/annotation/PRO_0000129166 http://togogenome.org/gene/10090:P2ry6 ^@ http://purl.uniprot.org/uniprot/Q3UQ86|||http://purl.uniprot.org/uniprot/Q9ERK9 ^@ 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|||P2Y purinoceptor 6 ^@ http://purl.uniprot.org/annotation/PRO_0000070029 http://togogenome.org/gene/10090:Psmd1 ^@ http://purl.uniprot.org/uniprot/Q3TXS7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ 26S proteasome non-ATPase regulatory subunit 1|||Acidic residues|||Basic and acidic residues|||Disordered|||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_0000231598 http://togogenome.org/gene/10090:Wfdc2 ^@ http://purl.uniprot.org/uniprot/Q4FZJ6|||http://purl.uniprot.org/uniprot/Q9DAU7 ^@ 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|||Polar residues|||WAP|||WAP 1|||WAP 2|||WAP four-disulfide core domain protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000041371|||http://purl.uniprot.org/annotation/PRO_5009970953 http://togogenome.org/gene/10090:Defb2 ^@ http://purl.uniprot.org/uniprot/P82020|||http://purl.uniprot.org/uniprot/Q32MH3 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Peptide|||Signal Peptide ^@ Beta-defensin 2 ^@ http://purl.uniprot.org/annotation/PRO_0000006927|||http://purl.uniprot.org/annotation/PRO_5014309011 http://togogenome.org/gene/10090:Spaca3 ^@ http://purl.uniprot.org/uniprot/A0A077S9M6|||http://purl.uniprot.org/uniprot/Q9D9X8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||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|||Helix|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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_0000256221|||http://purl.uniprot.org/annotation/PRO_0000256222|||http://purl.uniprot.org/annotation/PRO_5001723544|||http://purl.uniprot.org/annotation/VSP_021330 http://togogenome.org/gene/10090:Aig1 ^@ http://purl.uniprot.org/uniprot/Q3TS32|||http://purl.uniprot.org/uniprot/Q9D8B1 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Androgen-induced gene 1 protein|||Cytoplasmic|||Extracellular|||Helical|||Important for catalytic activity|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000190099|||http://purl.uniprot.org/annotation/VSP_060696 http://togogenome.org/gene/10090:Ext1 ^@ http://purl.uniprot.org/uniprot/P97464|||http://purl.uniprot.org/uniprot/Q3V1P4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Exostosin GT47|||Exostosin-1|||Glycosyl transferase 64|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149649 http://togogenome.org/gene/10090:Best3 ^@ http://purl.uniprot.org/uniprot/Q6H1V1 ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Bestrophin-3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000143122 http://togogenome.org/gene/10090:Lmo4 ^@ http://purl.uniprot.org/uniprot/P61969|||http://purl.uniprot.org/uniprot/Q542S1 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Strand|||Turn ^@ LIM domain transcription factor LMO4|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||Reduces binding to RBBP8. ^@ http://purl.uniprot.org/annotation/PRO_0000075821 http://togogenome.org/gene/10090:Ugt1a10 ^@ http://purl.uniprot.org/uniprot/E9PXN7|||http://purl.uniprot.org/uniprot/Q5FW80|||http://purl.uniprot.org/uniprot/Q6XL43 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||UDP-glucuronosyltransferase ^@ http://purl.uniprot.org/annotation/PRO_5005128624|||http://purl.uniprot.org/annotation/PRO_5005143649|||http://purl.uniprot.org/annotation/PRO_5005144136 http://togogenome.org/gene/10090:2900092C05Rik ^@ http://purl.uniprot.org/uniprot/Q5I0V9 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015097905 http://togogenome.org/gene/10090:Spata6l ^@ http://purl.uniprot.org/uniprot/B2RV46|||http://purl.uniprot.org/uniprot/Q8BI12 ^@ 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|||Spermatogenesis associated 6-like protein|||Spermatogenesis-associated protein 6 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000417503 http://togogenome.org/gene/10090:Ilrun ^@ http://purl.uniprot.org/uniprot/A0A3B2WCT9|||http://purl.uniprot.org/uniprot/B2KF54|||http://purl.uniprot.org/uniprot/Q3TT38 ^@ 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|||Next to BRCA1 central|||Phosphoserine|||Polar residues|||Protein ILRUN ^@ http://purl.uniprot.org/annotation/PRO_0000223319 http://togogenome.org/gene/10090:Taf12 ^@ http://purl.uniprot.org/uniprot/Q3UT56|||http://purl.uniprot.org/uniprot/Q8VE65 ^@ 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 ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-fold|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription initiation factor TFIID subunit 12 ^@ http://purl.uniprot.org/annotation/PRO_0000118908 http://togogenome.org/gene/10090:Pou1f1 ^@ http://purl.uniprot.org/uniprot/Q00286 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant ^@ Chain|||DNA Binding|||Domain Extent|||Motif|||Sequence Variant|||Splice Variant ^@ 9aaTAD|||Homeobox|||In dw.|||In isoform 2.|||In isoform 3.|||POU-specific|||Pituitary-specific positive transcription factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000100699|||http://purl.uniprot.org/annotation/VSP_012550|||http://purl.uniprot.org/annotation/VSP_012551 http://togogenome.org/gene/10090:Rad54l ^@ http://purl.uniprot.org/uniprot/P70270 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||DEGH box|||DNA repair and recombination protein RAD54-like|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by NEK1|||Required for chromatin remodeling, strand pairing activities and coupling of ATPase activity ^@ http://purl.uniprot.org/annotation/PRO_0000074338 http://togogenome.org/gene/10090:Or5p4 ^@ http://purl.uniprot.org/uniprot/Q8VGI5 ^@ 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 5P4 ^@ http://purl.uniprot.org/annotation/PRO_0000150839 http://togogenome.org/gene/10090:Vkorc1 ^@ http://purl.uniprot.org/uniprot/Q9CRC0 ^@ Binding Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Identified in warfarin-resistant animals.|||Lumenal|||Redox-active|||Vitamin K epoxide reductase complex subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000191669 http://togogenome.org/gene/10090:4930451I11Rik ^@ http://purl.uniprot.org/uniprot/E9Q9R3 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Chain|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Fertilization-influencing membrane protein|||Helical|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_5003244526|||http://purl.uniprot.org/annotation/VSP_060728|||http://purl.uniprot.org/annotation/VSP_060729 http://togogenome.org/gene/10090:Gon7 ^@ http://purl.uniprot.org/uniprot/P0C8B4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Acidic residues|||Disordered|||EKC/KEOPS complex subunit GON7|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000352801 http://togogenome.org/gene/10090:Pard6g ^@ http://purl.uniprot.org/uniprot/Q8CBL3|||http://purl.uniprot.org/uniprot/Q9JK84 ^@ 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|||Interaction with PRKCI and PRKCZ|||PB1|||PDZ|||Partitioning defective 6 homolog gamma|||Polar residues|||Pseudo-CRIB ^@ http://purl.uniprot.org/annotation/PRO_0000112519 http://togogenome.org/gene/10090:Tmem47 ^@ http://purl.uniprot.org/uniprot/Q9JJG6 ^@ 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-acetylalanine|||Removed|||Transmembrane protein 47 ^@ http://purl.uniprot.org/annotation/PRO_0000072574|||http://purl.uniprot.org/annotation/VSP_034861 http://togogenome.org/gene/10090:Epo ^@ http://purl.uniprot.org/uniprot/B7ZMY9|||http://purl.uniprot.org/uniprot/P07321|||http://purl.uniprot.org/uniprot/Q0VED9 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Erythropoietin|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000008405|||http://purl.uniprot.org/annotation/PRO_5014306852|||http://purl.uniprot.org/annotation/PRO_5015087435 http://togogenome.org/gene/10090:Fthl17e ^@ http://purl.uniprot.org/uniprot/Q3SXD1|||http://purl.uniprot.org/uniprot/Q99MX2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Ferritin heavy polypeptide-like 17E|||Ferritin-like diiron ^@ http://purl.uniprot.org/annotation/PRO_0000201069 http://togogenome.org/gene/10090:Tfpt ^@ http://purl.uniprot.org/uniprot/Q3U1J1 ^@ 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|||Polar residues|||TCF3 fusion partner homolog ^@ http://purl.uniprot.org/annotation/PRO_0000254582|||http://purl.uniprot.org/annotation/VSP_021243 http://togogenome.org/gene/10090:Rd3 ^@ http://purl.uniprot.org/uniprot/Q05D96|||http://purl.uniprot.org/uniprot/Q8BRE0 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Disordered|||Protein RD3 ^@ http://purl.uniprot.org/annotation/PRO_0000089249 http://togogenome.org/gene/10090:Pdia6 ^@ http://purl.uniprot.org/uniprot/Q3TML0|||http://purl.uniprot.org/uniprot/Q922R8 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Acidic residues|||Disordered|||Phosphoserine|||Prevents secretion from ER|||Protein disulfide-isomerase A6|||Redox-active|||Thioredoxin|||Thioredoxin 1|||Thioredoxin 2 ^@ http://purl.uniprot.org/annotation/PRO_0000034238|||http://purl.uniprot.org/annotation/PRO_5015097443 http://togogenome.org/gene/10090:Scg2 ^@ http://purl.uniprot.org/uniprot/Q03517|||http://purl.uniprot.org/uniprot/Q4W8U9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Manserin|||Phosphoserine|||Secretogranin-2|||Secretoneurin|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000005455|||http://purl.uniprot.org/annotation/PRO_0000005456|||http://purl.uniprot.org/annotation/PRO_0000432737|||http://purl.uniprot.org/annotation/PRO_5015097706 http://togogenome.org/gene/10090:Vmn1r70 ^@ http://purl.uniprot.org/uniprot/Q8R254 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp882 ^@ http://purl.uniprot.org/uniprot/E9Q4R4|||http://purl.uniprot.org/uniprot/Q8BYD7 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:G6pc3 ^@ http://purl.uniprot.org/uniprot/Q6NSQ9 ^@ 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|||Glucose-6-phosphatase 3|||Helical|||Lumenal|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000334513 http://togogenome.org/gene/10090:Garnl3 ^@ http://purl.uniprot.org/uniprot/Q3V0G7 ^@ 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|||CNH|||Disordered|||GTPase-activating Rap/Ran-GAP domain-like protein 3|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rap-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000312216|||http://purl.uniprot.org/annotation/VSP_029746|||http://purl.uniprot.org/annotation/VSP_029747 http://togogenome.org/gene/10090:Med4 ^@ http://purl.uniprot.org/uniprot/Q9CQA5 ^@ 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.|||Mediator of RNA polymerase II transcription subunit 4|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000096384|||http://purl.uniprot.org/annotation/VSP_027918|||http://purl.uniprot.org/annotation/VSP_027919 http://togogenome.org/gene/10090:Kcne3 ^@ http://purl.uniprot.org/uniprot/Q545H9|||http://purl.uniprot.org/uniprot/Q9WTW2 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Potassium voltage-gated channel subfamily E member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000144290 http://togogenome.org/gene/10090:Stkld1 ^@ http://purl.uniprot.org/uniprot/Q80YS9 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region ^@ Disordered|||Protein kinase|||Serine/threonine kinase-like domain-containing protein STKLD1 ^@ http://purl.uniprot.org/annotation/PRO_0000307899 http://togogenome.org/gene/10090:Fam181a ^@ http://purl.uniprot.org/uniprot/J3QNB7 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Edem2 ^@ http://purl.uniprot.org/uniprot/Q8BJT9 ^@ 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 ^@ Disordered|||ER degradation-enhancing alpha-mannosidase-like protein 2|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5014588821 http://togogenome.org/gene/10090:Cipc ^@ http://purl.uniprot.org/uniprot/Q8R0W1|||http://purl.uniprot.org/uniprot/Z4YJJ0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Basic and acidic residues|||CLOCK-interacting pacemaker|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000256134|||http://purl.uniprot.org/annotation/VSP_055396 http://togogenome.org/gene/10090:Rel ^@ http://purl.uniprot.org/uniprot/A4QPD3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ RHD ^@ http://togogenome.org/gene/10090:3425401B19Rik ^@ http://purl.uniprot.org/uniprot/D3Z1D3 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Cardiac-enriched FHL2-interacting protein|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000444578 http://togogenome.org/gene/10090:Or9q1 ^@ http://purl.uniprot.org/uniprot/Q7TQQ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pla2g5 ^@ http://purl.uniprot.org/uniprot/P97391|||http://purl.uniprot.org/uniprot/Q6GTW1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Impairs cysteinyl leukotrienes synthesis and phagocytosis of IgG immune complexes by synovial fluid monocyte/macrophage cells.|||Phospholipase A2|||Phospholipase A2 group V ^@ http://purl.uniprot.org/annotation/PRO_0000022762|||http://purl.uniprot.org/annotation/PRO_5015020072 http://togogenome.org/gene/10090:Kdelr3 ^@ http://purl.uniprot.org/uniprot/Q8R1L4 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Site|||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|||Interaction with the K-D-E-L motif on target proteins|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000194159 http://togogenome.org/gene/10090:Tmem236 ^@ http://purl.uniprot.org/uniprot/A2ARJ3 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 236 ^@ http://purl.uniprot.org/annotation/PRO_0000409538 http://togogenome.org/gene/10090:Mycn ^@ http://purl.uniprot.org/uniprot/P03966|||http://purl.uniprot.org/uniprot/Q3UII1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 9aaTAD|||Acidic residues|||BHLH|||Basic and acidic residues|||Disordered|||Interaction with AURKA|||Interaction with AURKA and FBXW7|||Leucine-zipper|||N-myc proto-oncogene protein|||Phosphoserine; by CK2|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127325 http://togogenome.org/gene/10090:Or4x6 ^@ http://purl.uniprot.org/uniprot/Q8VEZ2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp185 ^@ http://purl.uniprot.org/uniprot/A2BI37|||http://purl.uniprot.org/uniprot/G5E8W8|||http://purl.uniprot.org/uniprot/Q62394|||http://purl.uniprot.org/uniprot/Q8C875|||http://purl.uniprot.org/uniprot/Q9CRR9 ^@ 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 ^@ Basic and acidic residues|||Disordered|||LIM zinc-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 185 ^@ http://purl.uniprot.org/annotation/PRO_0000075912 http://togogenome.org/gene/10090:Dctn4 ^@ http://purl.uniprot.org/uniprot/Q8CBY8 ^@ Chain|||Coiled-Coil|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Crosslink|||Initiator Methionine|||Modified Residue|||Splice Variant ^@ Dynactin subunit 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000079824|||http://purl.uniprot.org/annotation/VSP_013573 http://togogenome.org/gene/10090:Aox2 ^@ http://purl.uniprot.org/uniprot/Q5SGK3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ 2Fe-2S ferredoxin-type|||Aldehyde oxidase 2|||FAD-binding PCMH-type|||Proton acceptor; for azaheterocycle hydroxylase activity ^@ http://purl.uniprot.org/annotation/PRO_0000425245 http://togogenome.org/gene/10090:Malrd1 ^@ http://purl.uniprot.org/uniprot/A2AJX4 ^@ 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|||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_5007184230 http://togogenome.org/gene/10090:Gm21671 ^@ http://purl.uniprot.org/uniprot/G3UY31 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ror1 ^@ http://purl.uniprot.org/uniprot/Q501P6|||http://purl.uniprot.org/uniprot/Q9Z139 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||FZ|||Helical|||Ig-like|||Ig-like C2-type|||Inactive tyrosine-protein kinase transmembrane receptor ROR1|||Kringle|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000024459|||http://purl.uniprot.org/annotation/PRO_5004247855 http://togogenome.org/gene/10090:Dspp ^@ http://purl.uniprot.org/uniprot/E9Q9Z9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003244532 http://togogenome.org/gene/10090:Tprgl ^@ http://purl.uniprot.org/uniprot/Q9DBS2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Important for homomultimer formation|||Important for homomultimer formation and localization to presynaptic regions|||Phosphoserine|||Phosphothreonine|||Tumor protein p63-regulated gene 1-like protein|||hSac2 ^@ http://purl.uniprot.org/annotation/PRO_0000269187 http://togogenome.org/gene/10090:Rbbp8nl ^@ http://purl.uniprot.org/uniprot/A2ABX0|||http://purl.uniprot.org/uniprot/Q8CEB4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DNA endonuclease Ctp1 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Mylpf ^@ http://purl.uniprot.org/uniprot/A0A0U1RP93|||http://purl.uniprot.org/uniprot/P97457|||http://purl.uniprot.org/uniprot/Q545G1 ^@ 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|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Myosin regulatory light chain 11|||N,N,N-trimethylalanine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000019310 http://togogenome.org/gene/10090:Utp11 ^@ http://purl.uniprot.org/uniprot/Q9CZJ1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Probable U3 small nucleolar RNA-associated protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000211043 http://togogenome.org/gene/10090:Slc14a1 ^@ http://purl.uniprot.org/uniprot/Q8VHL0 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Helical|||Important for channel permeability|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Urea transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000065738|||http://purl.uniprot.org/annotation/VSP_041574 http://togogenome.org/gene/10090:Ss18l2 ^@ http://purl.uniprot.org/uniprot/Q9D174 ^@ Chain|||Molecule Processing|||Motif|||Region ^@ Chain|||Motif ^@ SH2-binding|||SS18-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000181827 http://togogenome.org/gene/10090:Kpna3 ^@ http://purl.uniprot.org/uniprot/O35344|||http://purl.uniprot.org/uniprot/Q543M7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat ^@ ARM|||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|||N-acetylalanine|||NLS binding site (major)|||NLS binding site (minor)|||Nuclear localization signal|||Phosphoserine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000120725 http://togogenome.org/gene/10090:C1s1 ^@ http://purl.uniprot.org/uniprot/E9Q6C2|||http://purl.uniprot.org/uniprot/Q14DT6|||http://purl.uniprot.org/uniprot/Q8CG14 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ (3R)-3-hydroxyasparagine|||CUB|||CUB 1|||CUB 2|||Charge relay system|||Complement C1s-1 subcomponent|||Complement C1s-A subcomponent heavy chain|||Complement C1s-A subcomponent light chain|||EGF-like; calcium-binding|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi|||Sushi 1|||Sushi 2 ^@ http://purl.uniprot.org/annotation/PRO_0000042193|||http://purl.uniprot.org/annotation/PRO_0000042194|||http://purl.uniprot.org/annotation/PRO_0000042195|||http://purl.uniprot.org/annotation/PRO_5004182999|||http://purl.uniprot.org/annotation/PRO_5015090366 http://togogenome.org/gene/10090:AY358078 ^@ http://purl.uniprot.org/uniprot/Q6UY53 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Gpr142 ^@ http://purl.uniprot.org/uniprot/A2AD24|||http://purl.uniprot.org/uniprot/Q1XA02|||http://purl.uniprot.org/uniprot/Q7TQN9 ^@ 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 142 ^@ http://purl.uniprot.org/annotation/PRO_0000069621 http://togogenome.org/gene/10090:Eaf2 ^@ http://purl.uniprot.org/uniprot/K4DI60|||http://purl.uniprot.org/uniprot/Q91ZD6 ^@ 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_0000130338|||http://purl.uniprot.org/annotation/VSP_015311 http://togogenome.org/gene/10090:Pdk2 ^@ http://purl.uniprot.org/uniprot/Q9JK42 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Histidine kinase|||Mitochondrion|||N6-succinyllysine|||Phosphotyrosine|||[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000023441 http://togogenome.org/gene/10090:Or1e16 ^@ http://purl.uniprot.org/uniprot/Q8VGI1 ^@ 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 1E16 ^@ http://purl.uniprot.org/annotation/PRO_0000233898 http://togogenome.org/gene/10090:Zc3h7a ^@ http://purl.uniprot.org/uniprot/E9PWW6|||http://purl.uniprot.org/uniprot/Q3UBH9 ^@ Domain Extent|||Region|||Zinc Finger ^@ Domain Extent|||Zinc Finger ^@ C3H1-type ^@ http://togogenome.org/gene/10090:Zc3h7b ^@ http://purl.uniprot.org/uniprot/F8VPP8 ^@ Domain Extent|||Region|||Repeat|||Zinc Finger ^@ Domain Extent|||Region|||Repeat|||Zinc Finger ^@ C3H1-type|||Disordered|||TPR ^@ http://togogenome.org/gene/10090:Gipc3 ^@ http://purl.uniprot.org/uniprot/Q8R5M0 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant ^@ Chain|||Domain Extent|||Sequence Variant ^@ In ahl5.|||PDZ|||PDZ domain-containing protein GIPC3 ^@ http://purl.uniprot.org/annotation/PRO_0000247192 http://togogenome.org/gene/10090:Ate1 ^@ http://purl.uniprot.org/uniprot/J3QNU1|||http://purl.uniprot.org/uniprot/Q80YP1|||http://purl.uniprot.org/uniprot/Q8BP95|||http://purl.uniprot.org/uniprot/Q9Z2A5 ^@ 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 ^@ Arginyl-tRNA--protein transferase 1|||Basic and acidic residues|||Disordered|||In isoform ATE1-2 and isoform ATE1-4.|||In isoform ATE1-3 and isoform ATE1-4.|||N-end aminoacyl transferase N-terminal|||N-end rule aminoacyl transferase C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000195089|||http://purl.uniprot.org/annotation/VSP_000337|||http://purl.uniprot.org/annotation/VSP_061924 http://togogenome.org/gene/10090:Prpf38b ^@ http://purl.uniprot.org/uniprot/Q80SY5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pre-mRNA-splicing factor 38B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000287236 http://togogenome.org/gene/10090:Smr3a ^@ http://purl.uniprot.org/uniprot/Q61900 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Signal Peptide ^@ 1|||2|||3|||3 X 12 AA tandem repeats of G-P-G-I-G-R-P-[HP]-P-P-P-[PF]|||Disordered|||Polar residues|||Pro residues|||Submaxillary gland androgen-regulated protein 3A ^@ http://purl.uniprot.org/annotation/PRO_0000022368 http://togogenome.org/gene/10090:Or8k18 ^@ http://purl.uniprot.org/uniprot/A2ARZ0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fam43b ^@ http://purl.uniprot.org/uniprot/A2AM80 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||PID ^@ http://togogenome.org/gene/10090:Pgr ^@ http://purl.uniprot.org/uniprot/Q00175|||http://purl.uniprot.org/uniprot/Q8BW69 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ AF1; mediates transcriptional activation|||AF2; mediates transcriptional activation|||AF3; mediates transcriptional activation (in isoform B)|||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|||In isoform A.|||LXXL motif 1|||Mediates transcriptional transrepression (in isoform A)|||Modulating, Pro-Rich|||NR C4-type|||NR LBD|||Nuclear localization signal|||Nuclear receptor|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphoserine; by MAPK|||Phosphoserine; by MAPK1|||Polar residues|||Pro residues|||Progesterone receptor ^@ http://purl.uniprot.org/annotation/PRO_0000053695|||http://purl.uniprot.org/annotation/VSP_058743 http://togogenome.org/gene/10090:Trdn ^@ http://purl.uniprot.org/uniprot/E9Q9K5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interchain|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Triadin ^@ http://purl.uniprot.org/annotation/PRO_0000430562|||http://purl.uniprot.org/annotation/VSP_056795|||http://purl.uniprot.org/annotation/VSP_056796|||http://purl.uniprot.org/annotation/VSP_056797|||http://purl.uniprot.org/annotation/VSP_056798|||http://purl.uniprot.org/annotation/VSP_056799|||http://purl.uniprot.org/annotation/VSP_056800|||http://purl.uniprot.org/annotation/VSP_056801 http://togogenome.org/gene/10090:Pigu ^@ http://purl.uniprot.org/uniprot/Q3TAA8 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015097437 http://togogenome.org/gene/10090:Lrrtm1 ^@ http://purl.uniprot.org/uniprot/Q8K377 ^@ 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 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_0000018351 http://togogenome.org/gene/10090:Tmem120b ^@ http://purl.uniprot.org/uniprot/Q3TA38 ^@ 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 protein 120B ^@ http://purl.uniprot.org/annotation/PRO_0000309530|||http://purl.uniprot.org/annotation/VSP_029233 http://togogenome.org/gene/10090:Gbp2b ^@ http://purl.uniprot.org/uniprot/A4UUI2 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ GB1/RHD3-type G ^@ http://togogenome.org/gene/10090:Snta1 ^@ http://purl.uniprot.org/uniprot/A2AKD7|||http://purl.uniprot.org/uniprot/Q3UVD6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||PDZ|||PH ^@ http://togogenome.org/gene/10090:Copz1 ^@ http://purl.uniprot.org/uniprot/P61924|||http://purl.uniprot.org/uniprot/Q542M2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ AP complex mu/sigma subunit|||Coatomer subunit zeta-1|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000193826 http://togogenome.org/gene/10090:Atp5k ^@ http://purl.uniprot.org/uniprot/Q06185 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ ATP synthase subunit e, mitochondrial|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000071685 http://togogenome.org/gene/10090:Slc9a6 ^@ http://purl.uniprot.org/uniprot/A1L3P4 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Mutagenesis Site|||Sequence Conflict|||Transmembrane ^@ 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|||Mice have normal brain size at 6 months of age and do not show cerebellar degeneration or defective neuronal arborization. Neurons from male mice also do not demonstrate an abnormality in intraendosomal pH compared with controls.|||Sodium/hydrogen exchanger 6 ^@ http://purl.uniprot.org/annotation/PRO_0000457379 http://togogenome.org/gene/10090:Acot8 ^@ http://purl.uniprot.org/uniprot/P58137 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Motif|||Sequence Conflict ^@ Acyl-coenzyme A thioesterase 8|||Charge relay system|||Microbody targeting signal ^@ http://purl.uniprot.org/annotation/PRO_0000202153 http://togogenome.org/gene/10090:Tmem107 ^@ http://purl.uniprot.org/uniprot/Q9CPV0 ^@ 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 Schlei; decreases cilium assembly; loss of protein localization to cilium.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 107 ^@ http://purl.uniprot.org/annotation/PRO_0000254542|||http://purl.uniprot.org/annotation/VSP_021214 http://togogenome.org/gene/10090:Muc5ac ^@ http://purl.uniprot.org/uniprot/E9PWB6 ^@ 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 ^@ Basic and acidic residues|||CTCK|||Disordered|||VWFC|||VWFD ^@ http://purl.uniprot.org/annotation/PRO_5015090352 http://togogenome.org/gene/10090:Trim60 ^@ http://purl.uniprot.org/uniprot/Q8VI40 ^@ 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|||E3 SUMO-protein ligase TRIM60|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000249190 http://togogenome.org/gene/10090:Cldn34c3 ^@ http://purl.uniprot.org/uniprot/A0A991ENX4 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Grxcr2 ^@ http://purl.uniprot.org/uniprot/Q3TYR5 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Glutaredoxin domain-containing cysteine-rich protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000349192 http://togogenome.org/gene/10090:Sigirr ^@ http://purl.uniprot.org/uniprot/Q3UKS3|||http://purl.uniprot.org/uniprot/Q9JLZ8 ^@ 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 ^@ Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||Ig-like|||Ig-like C2-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Single Ig IL-1-related receptor|||TIR ^@ http://purl.uniprot.org/annotation/PRO_0000099066|||http://purl.uniprot.org/annotation/VSP_015718 http://togogenome.org/gene/10090:H2al1o ^@ http://purl.uniprot.org/uniprot/L7MU04 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Histone H2A/H2B/H3 ^@ http://togogenome.org/gene/10090:Ccdc121rt1 ^@ http://purl.uniprot.org/uniprot/E9Q6D3|||http://purl.uniprot.org/uniprot/Q8C5G9 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF4515|||Disordered ^@ http://togogenome.org/gene/10090:Dhdds ^@ http://purl.uniprot.org/uniprot/Q99KU1 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Sequence Conflict|||Splice Variant ^@ Dehydrodolichyl diphosphate synthase complex subunit Dhdds|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000123750|||http://purl.uniprot.org/annotation/VSP_010032 http://togogenome.org/gene/10090:Zfp654 ^@ http://purl.uniprot.org/uniprot/Q9DAU9 ^@ 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|||C2H2-type 4|||C2H2-type 5|||Disordered|||Phosphoserine|||Polar residues|||Zinc finger protein 654 ^@ http://purl.uniprot.org/annotation/PRO_0000311947 http://togogenome.org/gene/10090:Gcm2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J021|||http://purl.uniprot.org/uniprot/O09102 ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict ^@ Basic and acidic residues|||C-terminal conserved inhibitory domain (CCID)|||Chorion-specific transcription factor GCMb|||Disordered|||GCM ^@ http://purl.uniprot.org/annotation/PRO_0000126651 http://togogenome.org/gene/10090:Srpx2 ^@ http://purl.uniprot.org/uniprot/Q8R054 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ HYR|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi repeat-containing protein SRPX2 ^@ http://purl.uniprot.org/annotation/PRO_0000274526 http://togogenome.org/gene/10090:Lvrn ^@ http://purl.uniprot.org/uniprot/E9QJR0 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Site ^@ Aminopeptidase N-like N-terminal|||ERAP1-like C-terminal|||Peptidase M1 membrane alanine aminopeptidase|||Proton acceptor|||Transition state stabilizer ^@ http://togogenome.org/gene/10090:Atoh1 ^@ http://purl.uniprot.org/uniprot/P48985 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Transcription factor Atoh1|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127140 http://togogenome.org/gene/10090:Prl2a1 ^@ http://purl.uniprot.org/uniprot/A0A0M5HDY7|||http://purl.uniprot.org/uniprot/Q9JHK0 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ Prolactin-2A1 ^@ http://purl.uniprot.org/annotation/PRO_0000045161|||http://purl.uniprot.org/annotation/PRO_5015043300 http://togogenome.org/gene/10090:Fcsk ^@ http://purl.uniprot.org/uniprot/Q7TMC8 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Binding Site|||Chain|||Splice Variant ^@ In isoform 2.|||L-fucose kinase ^@ http://purl.uniprot.org/annotation/PRO_0000436383|||http://purl.uniprot.org/annotation/VSP_058365 http://togogenome.org/gene/10090:Ndufaf8 ^@ http://purl.uniprot.org/uniprot/A2AMZ4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Domain Extent|||Motif ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 8 ^@ http://purl.uniprot.org/annotation/PRO_0000299481 http://togogenome.org/gene/10090:Arhgap31 ^@ http://purl.uniprot.org/uniprot/A6X8Z5|||http://purl.uniprot.org/uniprot/B2RSI0 ^@ 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 ^@ 70% reduction of GAP activity; when associated with A-56.|||70% reduction of GAP activity; when associated with V-169.|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by GSK3|||Polar residues|||Pro residues|||Rho GTPase-activating protein 31|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000320115 http://togogenome.org/gene/10090:Or1s2 ^@ http://purl.uniprot.org/uniprot/B9EHG2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tns3 ^@ http://purl.uniprot.org/uniprot/A0A5F8MP98|||http://purl.uniprot.org/uniprot/Q5SSZ5|||http://purl.uniprot.org/uniprot/Q8BWF4 ^@ 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 ^@ C2 tensin-type|||Disordered|||In isoform 2.|||PTB|||Phorbol-ester/DAG-type|||Phosphatase tensin-type|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH2|||Tensin-3|||Tyrosine specific protein phosphatases ^@ http://purl.uniprot.org/annotation/PRO_0000295916|||http://purl.uniprot.org/annotation/VSP_027128 http://togogenome.org/gene/10090:Cast ^@ http://purl.uniprot.org/uniprot/A0A1Y7VJN8|||http://purl.uniprot.org/uniprot/P51125|||http://purl.uniprot.org/uniprot/Q3TTN2|||http://purl.uniprot.org/uniprot/Q8C281|||http://purl.uniprot.org/uniprot/Q8CB83|||http://purl.uniprot.org/uniprot/Q8CE04|||http://purl.uniprot.org/uniprot/Q8CE80|||http://purl.uniprot.org/uniprot/Q921U7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||Splice Variant ^@ Basic and acidic residues|||Calpastatin|||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.|||In isoform 6.|||In isoform 7.|||Inhibitory domain 1|||Inhibitory domain 2|||Inhibitory domain 3|||Inhibitory domain 4|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000147633|||http://purl.uniprot.org/annotation/VSP_000745|||http://purl.uniprot.org/annotation/VSP_000746|||http://purl.uniprot.org/annotation/VSP_000747|||http://purl.uniprot.org/annotation/VSP_000748|||http://purl.uniprot.org/annotation/VSP_000749|||http://purl.uniprot.org/annotation/VSP_000750|||http://purl.uniprot.org/annotation/VSP_000751|||http://purl.uniprot.org/annotation/VSP_000752 http://togogenome.org/gene/10090:Plcl2 ^@ http://purl.uniprot.org/uniprot/Q8K394 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||C2|||Disordered|||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_0000288852 http://togogenome.org/gene/10090:Usp2 ^@ http://purl.uniprot.org/uniprot/O88623 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 4.|||Necessary for interaction with MDM4|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000080617|||http://purl.uniprot.org/annotation/VSP_061745|||http://purl.uniprot.org/annotation/VSP_061746|||http://purl.uniprot.org/annotation/VSP_061747|||http://purl.uniprot.org/annotation/VSP_061748 http://togogenome.org/gene/10090:Borcs7 ^@ http://purl.uniprot.org/uniprot/Q9CRC6 ^@ Chain|||Molecule Processing ^@ Chain ^@ BLOC-1-related complex subunit 7 ^@ http://purl.uniprot.org/annotation/PRO_0000089788 http://togogenome.org/gene/10090:Dnaaf6 ^@ http://purl.uniprot.org/uniprot/Q3KNI6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Dynein axonemal assembly factor 6 ^@ http://purl.uniprot.org/annotation/PRO_0000431551 http://togogenome.org/gene/10090:Ly6e ^@ http://purl.uniprot.org/uniprot/Q64253 ^@ 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 ^@ GPI-anchor amidated alanine|||Lymphocyte antigen 6E|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036140|||http://purl.uniprot.org/annotation/PRO_0000036141 http://togogenome.org/gene/10090:Gm10096 ^@ http://purl.uniprot.org/uniprot/Q62478 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Trim10 ^@ http://purl.uniprot.org/uniprot/Q9WUH5 ^@ 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 10 ^@ http://purl.uniprot.org/annotation/PRO_0000056212 http://togogenome.org/gene/10090:Vmn1r170 ^@ http://purl.uniprot.org/uniprot/K7N6W9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clvs1 ^@ http://purl.uniprot.org/uniprot/Q9D4C9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ CRAL-TRIO|||Clavesin-1|||Disordered|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000297656|||http://purl.uniprot.org/annotation/VSP_027330|||http://purl.uniprot.org/annotation/VSP_027331 http://togogenome.org/gene/10090:Cebpg ^@ http://purl.uniprot.org/uniprot/P53568|||http://purl.uniprot.org/uniprot/Q54AJ1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region ^@ BZIP|||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|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076629 http://togogenome.org/gene/10090:Klf14 ^@ http://purl.uniprot.org/uniprot/Q19A41 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 14|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000294169 http://togogenome.org/gene/10090:Zmpste24 ^@ http://purl.uniprot.org/uniprot/B9EHY2|||http://purl.uniprot.org/uniprot/Q80W54 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CAAX prenyl protease 1 N-terminal|||CAAX prenyl protease 1 homolog|||Disordered|||Helical|||Lumenal|||Nuclear|||Peptidase M48|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000138845 http://togogenome.org/gene/10090:Mtss2 ^@ http://purl.uniprot.org/uniprot/D3YWC9|||http://purl.uniprot.org/uniprot/Q6P9S0 ^@ 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|||IMD|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein MTSS 2|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000319611 http://togogenome.org/gene/10090:Mcoln1 ^@ http://purl.uniprot.org/uniprot/Q99J21 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Constitutively active channel that is targeted to the cell membrane.|||Cytoplasmic|||Dileucine internalization motif; mediates AP2 complex-dependent internalization|||Dileucine motif; mediates targeting to lysosomes|||Disordered|||Extracellular|||Extracellular/lumenal pore loop|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||Interaction with phosphoinositides|||Mucolipin-1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PAK|||Polar residues|||Pore-forming|||Required for palmitoylation and association with membranes|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000215364|||http://purl.uniprot.org/annotation/VSP_010821 http://togogenome.org/gene/10090:Slc39a1 ^@ http://purl.uniprot.org/uniprot/Q9QZ03 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Zinc transporter ZIP1 ^@ http://purl.uniprot.org/annotation/PRO_0000068764 http://togogenome.org/gene/10090:Ap2b1 ^@ http://purl.uniprot.org/uniprot/Q5SWR1|||http://purl.uniprot.org/uniprot/Q9DBG3 ^@ 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 ^@ AP-2 complex subunit beta|||Beta-adaptin appendage C-terminal subdomain|||Clathrin adaptor alpha/beta/gamma-adaptin appendage Ig-like subdomain|||Disordered|||In isoform 2.|||N-acetylthreonine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000193743|||http://purl.uniprot.org/annotation/VSP_011491 http://togogenome.org/gene/10090:Stard6 ^@ http://purl.uniprot.org/uniprot/P59096|||http://purl.uniprot.org/uniprot/Q8C1R6|||http://purl.uniprot.org/uniprot/Q9CPT8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||START|||StAR-related lipid transfer protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000220673 http://togogenome.org/gene/10090:Slc9c1 ^@ http://purl.uniprot.org/uniprot/Q6UJY2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Ion transport-like|||N-linked (GlcNAc...) asparagine|||Sodium/hydrogen exchanger 10 ^@ http://purl.uniprot.org/annotation/PRO_0000295705 http://togogenome.org/gene/10090:Gtf2h1 ^@ http://purl.uniprot.org/uniprot/E9QKD9|||http://purl.uniprot.org/uniprot/G3X8R4|||http://purl.uniprot.org/uniprot/Q7TPY0|||http://purl.uniprot.org/uniprot/Q9DBA9 ^@ 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 ^@ BSD|||BSD 1|||BSD 2|||Disordered|||General transcription factor IIH subunit 1|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000119246 http://togogenome.org/gene/10090:Dtnb ^@ http://purl.uniprot.org/uniprot/O70585|||http://purl.uniprot.org/uniprot/Q8K0N0 ^@ 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|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Does not affect interaction with Kif5A.|||Dystrobrevin beta|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine; by PKA|||Phosphothreonine; by PKA and PKC|||Phosphothreonine; by PKC|||Polar residues|||Reduces interaction with Kif5A.|||Syntrophin-binding region|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000086879|||http://purl.uniprot.org/annotation/VSP_004227|||http://purl.uniprot.org/annotation/VSP_004228|||http://purl.uniprot.org/annotation/VSP_004229 http://togogenome.org/gene/10090:Hoxd4 ^@ http://purl.uniprot.org/uniprot/P10628 ^@ 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-D4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000200211 http://togogenome.org/gene/10090:Swap70 ^@ http://purl.uniprot.org/uniprot/Q6A028 ^@ 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 ^@ Basic and acidic residues|||Disordered|||PH|||Switch-associated protein 70 ^@ http://purl.uniprot.org/annotation/PRO_0000240281 http://togogenome.org/gene/10090:Kcnk18 ^@ http://purl.uniprot.org/uniprot/Q6VV64 ^@ Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Enhances basal channel activity and abolishes stimulation by calcineurin.|||Helical|||Insensitive to extracellular protons.|||Interaction with YWHAH|||Interaction with calcineurin|||Loss of interaction with YWHAH.|||Loss of interaction with calcineurin and activation by elevated intracellular calcium; when associated with A-214.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel subfamily K member 18|||Strongly reduced activation by elevated intracellular calcium. Loss of interaction with calcineurin and activation by elevated intracellular calcium; when associated with A-212.|||Strongly reduced current amplitude and localization to cell membrane. ^@ http://purl.uniprot.org/annotation/PRO_0000312501 http://togogenome.org/gene/10090:Mthfd2l ^@ http://purl.uniprot.org/uniprot/D3YZG8 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000413328 http://togogenome.org/gene/10090:H4c6 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Itpripl2 ^@ http://purl.uniprot.org/uniprot/Q3UV16 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||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_0000336094 http://togogenome.org/gene/10090:Fbxo9 ^@ http://purl.uniprot.org/uniprot/Q8BK06 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||F-box|||F-box only protein 9|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Removed|||TPR ^@ http://purl.uniprot.org/annotation/PRO_0000119887|||http://purl.uniprot.org/annotation/VSP_012929|||http://purl.uniprot.org/annotation/VSP_012930|||http://purl.uniprot.org/annotation/VSP_012931 http://togogenome.org/gene/10090:Prg4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J207|||http://purl.uniprot.org/uniprot/E0CZ58|||http://purl.uniprot.org/uniprot/Q9JM99 ^@ 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|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ 10|||11|||12; approximate|||13|||14|||15|||16; approximate|||17|||18|||19|||1; approximate|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||2; approximate|||30|||31|||32|||33|||34|||35|||36|||37|||37 X 8 AA repeats of K-X-P-X-P-T-T-X|||3; approximate|||4; approximate|||5|||6; approximate|||7|||8|||9|||Alternate|||Basic and acidic residues|||Basic residues|||Cleavage; by subtilisin-like proprotein convertase 4|||Cleaved by subtilisin-like proprotein convertase 4.|||Cleaved by subtilisin-like proprotein convertase.|||Disordered|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||In isoform B and isoform D.|||In isoform C, isoform D and isoform E.|||In isoform E.|||N-linked (GlcNAc...) asparagine|||Not cleaved by subtilisin-like proprotein convertase 4.|||Not cleaved by subtilisin-like proprotein convertase 4. Not cleaved by subtilisin-like proprotein convertase; when associated with A-795.|||Not cleaved by subtilisin-like proprotein convertase. Not cleaved by subtilisin-like proprotein convertase; when associated with A-1053.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Polar residues|||Pro residues|||Proteoglycan 4|||Proteoglycan 4 C-terminal part|||SMB|||SMB 1|||SMB 2 ^@ http://purl.uniprot.org/annotation/PRO_0000043234|||http://purl.uniprot.org/annotation/PRO_0000043235|||http://purl.uniprot.org/annotation/PRO_5015044319|||http://purl.uniprot.org/annotation/PRO_5015088656|||http://purl.uniprot.org/annotation/VSP_016471|||http://purl.uniprot.org/annotation/VSP_016472|||http://purl.uniprot.org/annotation/VSP_016473 http://togogenome.org/gene/10090:Rnf216 ^@ http://purl.uniprot.org/uniprot/P58283 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 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 isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain ^@ http://purl.uniprot.org/annotation/PRO_0000056294|||http://purl.uniprot.org/annotation/VSP_007408|||http://purl.uniprot.org/annotation/VSP_019293|||http://purl.uniprot.org/annotation/VSP_019294 http://togogenome.org/gene/10090:Or8b12 ^@ http://purl.uniprot.org/uniprot/Q7TRE6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wdfy1 ^@ http://purl.uniprot.org/uniprot/E9Q4P1|||http://purl.uniprot.org/uniprot/Q9DAD3 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Modified Residue|||Repeat|||Sequence Conflict|||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_0000434594 http://togogenome.org/gene/10090:Ccdc178 ^@ http://purl.uniprot.org/uniprot/Q8CDV0 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict ^@ Coiled-coil domain-containing protein 178|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000223317 http://togogenome.org/gene/10090:Arap2 ^@ http://purl.uniprot.org/uniprot/E9QP44 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Arf-GAP|||Basic and acidic residues|||Disordered|||PH|||Polar residues|||Ras-associating|||Rho-GAP|||SAM ^@ http://togogenome.org/gene/10090:Fcrlb ^@ http://purl.uniprot.org/uniprot/Q5DRQ8 ^@ 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 ^@ Disordered|||Fc receptor-like B|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000332993 http://togogenome.org/gene/10090:Psapl1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1A5|||http://purl.uniprot.org/uniprot/Q8C1C1 ^@ 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|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Proactivator polypeptide-like 1|||Saposin A-like|||Saposin A-type|||Saposin A-type 1|||Saposin A-type 2|||Saposin B-Val-like|||Saposin B-like|||Saposin B-type|||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_0000280315|||http://purl.uniprot.org/annotation/PRO_0000280316|||http://purl.uniprot.org/annotation/PRO_0000280317|||http://purl.uniprot.org/annotation/PRO_0000280318|||http://purl.uniprot.org/annotation/PRO_0000280319|||http://purl.uniprot.org/annotation/PRO_0000280320|||http://purl.uniprot.org/annotation/PRO_0000280321|||http://purl.uniprot.org/annotation/PRO_0000280322|||http://purl.uniprot.org/annotation/PRO_0000280323|||http://purl.uniprot.org/annotation/PRO_0000280324|||http://purl.uniprot.org/annotation/PRO_5015044316 http://togogenome.org/gene/10090:Cd47 ^@ http://purl.uniprot.org/uniprot/Q61735 ^@ 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|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||Leukocyte surface antigen CD47|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000042206|||http://purl.uniprot.org/annotation/VSP_015793 http://togogenome.org/gene/10090:Or2v1 ^@ http://purl.uniprot.org/uniprot/Q8VGD6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Olfactory receptor 2V1 ^@ http://purl.uniprot.org/annotation/PRO_0000422155|||http://purl.uniprot.org/annotation/VSP_046444 http://togogenome.org/gene/10090:Col25a1 ^@ http://purl.uniprot.org/uniprot/B2RQR7|||http://purl.uniprot.org/uniprot/E9Q5L6|||http://purl.uniprot.org/uniprot/Q99MQ5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ 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 8|||Collagen-like Alzheimer amyloid plaque component|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Interaction with amyloid-beta peptide|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000259613|||http://purl.uniprot.org/annotation/PRO_0000259614 http://togogenome.org/gene/10090:Nelfb ^@ http://purl.uniprot.org/uniprot/Q8C4Y3 ^@ 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.|||N6-acetyllysine|||Negative elongation factor B|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000219130|||http://purl.uniprot.org/annotation/VSP_059999 http://togogenome.org/gene/10090:Rhog ^@ http://purl.uniprot.org/uniprot/P84096 ^@ 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|||Phosphothreonine|||Removed in mature form|||Rho-related GTP-binding protein RhoG|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000042030|||http://purl.uniprot.org/annotation/PRO_0000042031 http://togogenome.org/gene/10090:Chmp4c ^@ http://purl.uniprot.org/uniprot/Q9D7F7 ^@ 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|||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_0000211496 http://togogenome.org/gene/10090:Duox1 ^@ http://purl.uniprot.org/uniprot/A2AQ92 ^@ 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 ^@ Disordered|||EF-hand|||FAD-binding FR-type|||Helical|||NAD(P)H oxidase (H2O2-forming)|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5002642730 http://togogenome.org/gene/10090:Zscan30 ^@ http://purl.uniprot.org/uniprot/Q149X8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ SCAN box ^@ http://togogenome.org/gene/10090:Fgd1 ^@ http://purl.uniprot.org/uniprot/A2ALP5|||http://purl.uniprot.org/uniprot/P52734|||http://purl.uniprot.org/uniprot/Q3UG32 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Abolishes binding to DBNL.|||Acidic residues|||DH|||Disordered|||FYVE, RhoGEF and PH domain-containing protein 1|||FYVE-type|||No effect on binding to DBNL.|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000080941 http://togogenome.org/gene/10090:Mcm7 ^@ http://purl.uniprot.org/uniprot/Q3U4T8|||http://purl.uniprot.org/uniprot/Q61881 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Almost abolishes MCM complex DNA helicase activity. Strongly decreases MCM complex ATPase activity. No effect on MCM complex formation. No effect on ATP and ssDNA binding.|||Arginine finger|||DNA replication licensing factor MCM7|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with ATRIP|||Interaction with RAD17|||MCM|||N-acetylalanine|||Phosphoserine|||Removed|||Strongly decreases MCM complex ATPase and DNA helicase activities. No effect on MCM complex formation. No effect on ATP and ssDNA binding. ^@ http://purl.uniprot.org/annotation/PRO_0000194120 http://togogenome.org/gene/10090:Cryab ^@ http://purl.uniprot.org/uniprot/P23927|||http://purl.uniprot.org/uniprot/Q52L78 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Alpha-crystallin B chain|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||SHSP|||sHSP ^@ http://purl.uniprot.org/annotation/PRO_0000125910 http://togogenome.org/gene/10090:Nol10 ^@ http://purl.uniprot.org/uniprot/Q3TUB5|||http://purl.uniprot.org/uniprot/Q5RJG1 ^@ 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|||Basic residues|||Disordered|||N-acetylmethionine|||NUC153|||Nucleolar protein 10|||Phosphoserine|||Phosphothreonine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000051102 http://togogenome.org/gene/10090:Osbp2 ^@ http://purl.uniprot.org/uniprot/Q5QNQ6|||http://purl.uniprot.org/uniprot/Q6PE09|||http://purl.uniprot.org/uniprot/Q8K0C7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Oxysterol-binding protein 2|||PH|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000223481 http://togogenome.org/gene/10090:Hbq1a ^@ http://purl.uniprot.org/uniprot/Q8BYM1 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Globin family profile|||distal binding residue|||proximal binding residue ^@ http://togogenome.org/gene/10090:Terf1 ^@ http://purl.uniprot.org/uniprot/P70371|||http://purl.uniprot.org/uniprot/Q3V252 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH myb-type|||Interaction with RLIM|||Myb-like|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine; by ATM|||Polar residues|||Removed|||TRFH mediates dimerization|||Telomeric repeat-binding factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000197130 http://togogenome.org/gene/10090:Tff1 ^@ http://purl.uniprot.org/uniprot/Q08423|||http://purl.uniprot.org/uniprot/Q149Y8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Signal Peptide ^@ Or 23|||P-type|||Pyrrolidone carboxylic acid|||Trefoil factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000023457|||http://purl.uniprot.org/annotation/PRO_5014306912 http://togogenome.org/gene/10090:Vmn1r254 ^@ http://purl.uniprot.org/uniprot/K7N6J2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Krt25 ^@ http://purl.uniprot.org/uniprot/Q8VCW2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||In Rex mutant M100573; mice exhibit curly hair and vibrissae. The diameter of the hair shaft is irregular due to morphological abnormalities in all three layers of the irs.|||In Rex mutant Re; mice exhibit curly hair and vibrissae. The diameter of the hair shaft is irregular due to morphological abnormalities in all three layers of the irs.|||Keratin, type I cytoskeletal 25|||Linker 1|||Linker 12|||Phosphoserine|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000312692 http://togogenome.org/gene/10090:Abca6 ^@ http://purl.uniprot.org/uniprot/Q8K441 ^@ 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 ^@ ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family A member 6|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000250673|||http://purl.uniprot.org/annotation/VSP_020699|||http://purl.uniprot.org/annotation/VSP_020700 http://togogenome.org/gene/10090:Ccl4 ^@ http://purl.uniprot.org/uniprot/P14097|||http://purl.uniprot.org/uniprot/Q5QNV9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ C-C motif chemokine|||C-C motif chemokine 4|||Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_0000005166|||http://purl.uniprot.org/annotation/PRO_5014205897 http://togogenome.org/gene/10090:Ap4e1 ^@ http://purl.uniprot.org/uniprot/Q80V94 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ AP-4 complex subunit epsilon-1|||Basic and acidic residues|||Disordered|||Interaction with TEPSIN|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000229749 http://togogenome.org/gene/10090:Ascc1 ^@ http://purl.uniprot.org/uniprot/Q9D8Z1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Activating signal cointegrator 1 complex subunit 1|||KH|||Required for interaction with ASCC3 ^@ http://purl.uniprot.org/annotation/PRO_0000050101 http://togogenome.org/gene/10090:Klhl6 ^@ http://purl.uniprot.org/uniprot/Q6V595 ^@ 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 6 ^@ http://purl.uniprot.org/annotation/PRO_0000119107 http://togogenome.org/gene/10090:Gabra3 ^@ http://purl.uniprot.org/uniprot/P26049|||http://purl.uniprot.org/uniprot/Q8CAB3 ^@ 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|||Disordered|||Extracellular|||Gamma-aminobutyric acid receptor subunit alpha-3|||Helical|||In RNA edited version.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000000438|||http://purl.uniprot.org/annotation/PRO_5014312035 http://togogenome.org/gene/10090:Tspan12 ^@ http://purl.uniprot.org/uniprot/Q8BKT6 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Lipid Binding|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||S-palmitoyl cysteine|||Tetraspanin-12 ^@ http://purl.uniprot.org/annotation/PRO_0000290009|||http://purl.uniprot.org/annotation/VSP_038526 http://togogenome.org/gene/10090:Ska2 ^@ http://purl.uniprot.org/uniprot/Q9CR46 ^@ Chain|||Molecule Processing ^@ Chain ^@ Spindle and kinetochore-associated protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000273161 http://togogenome.org/gene/10090:Gzmb ^@ http://purl.uniprot.org/uniprot/P04187|||http://purl.uniprot.org/uniprot/Q3TZH4 ^@ 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|||Site ^@ Activation peptide|||Charge relay system|||Granzyme B(G,H)|||Mediates preference for Asp-containing substrates|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Peptidase S1 domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000027401|||http://purl.uniprot.org/annotation/PRO_0000027402|||http://purl.uniprot.org/annotation/PRO_5014309191 http://togogenome.org/gene/10090:Lax1 ^@ http://purl.uniprot.org/uniprot/Q8BHB3 ^@ 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; Signal-anchor for type III membrane protein|||Lymphocyte transmembrane adapter 1|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000083330 http://togogenome.org/gene/10090:Sox30 ^@ http://purl.uniprot.org/uniprot/Q8CGW4 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Basic and acidic residues|||Disordered|||HMG box|||Polar residues|||Pro residues|||Transcription factor SOX-30 ^@ http://purl.uniprot.org/annotation/PRO_0000048775 http://togogenome.org/gene/10090:Mcu ^@ http://purl.uniprot.org/uniprot/Q3UMR5 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Coiled-Coil|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Calcium uniporter protein, mitochondrial|||DXXE|||Helical|||In isoform 2.|||Inner juxtamembrane helix (IJMH)|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N-terminal MCU domain|||N6-acetyllysine|||Outer juxtamembrane helix (OJMH)|||Phosphoserine; by CaMK2|||Strongly reduces calcium channel activity; when associated with V-256.|||Strongly reduces calcium channel activity; when associated with W-251. ^@ http://purl.uniprot.org/annotation/PRO_0000282977|||http://purl.uniprot.org/annotation/VSP_024264|||http://purl.uniprot.org/annotation/VSP_024265 http://togogenome.org/gene/10090:Synpr ^@ http://purl.uniprot.org/uniprot/Q8BGN8 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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_0000179158|||http://purl.uniprot.org/annotation/VSP_008550 http://togogenome.org/gene/10090:Ptpn23 ^@ http://purl.uniprot.org/uniprot/Q6PB44 ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||21 X 2 AA approximate tandem repeats of P-Q|||3|||4|||5|||6|||7|||8|||9|||BRO1|||Basic and acidic residues|||Disordered|||His|||In isoform 2.|||Omega-N-methylarginine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Pro residues|||TPR 1|||TPR 2|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 23 ^@ http://purl.uniprot.org/annotation/PRO_0000094778|||http://purl.uniprot.org/annotation/VSP_014195 http://togogenome.org/gene/10090:Tmem202 ^@ http://purl.uniprot.org/uniprot/B9EHM8|||http://purl.uniprot.org/uniprot/Q80W35 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 202 ^@ http://purl.uniprot.org/annotation/PRO_0000317202 http://togogenome.org/gene/10090:Gm4846 ^@ http://purl.uniprot.org/uniprot/B2RWH8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Pnrc2 ^@ http://purl.uniprot.org/uniprot/Q9CR73 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Proline-rich nuclear receptor coactivator 2|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000058486 http://togogenome.org/gene/10090:Zdhhc16 ^@ http://purl.uniprot.org/uniprot/Q9ESG8 ^@ 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 ZDHHC16|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212899 http://togogenome.org/gene/10090:Dazl ^@ http://purl.uniprot.org/uniprot/Q3TUC3|||http://purl.uniprot.org/uniprot/Q64368 ^@ 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|||Region|||Strand ^@ Abolishes RNA-binding but not homodimerization; when associated with D-43; D-82 and D-84.|||Abolishes RNA-binding but not homodimerization; when associated with D-43; D-82 and D-87.|||Abolishes RNA-binding but not homodimerization; when associated with D-43; D-84 and D-87.|||Abolishes RNA-binding but not homodimerization; when associated with D-82; D-84 and D-87.|||DAZ|||Deleted in azoospermia-like|||Disordered|||Homodimerization|||Phosphotyrosine|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081561 http://togogenome.org/gene/10090:Rassf9 ^@ http://purl.uniprot.org/uniprot/A0A1X7SB70|||http://purl.uniprot.org/uniprot/Q8K342 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Ras association domain-containing protein 9|||Ras-associating ^@ http://purl.uniprot.org/annotation/PRO_0000299453 http://togogenome.org/gene/10090:Zfp9 ^@ http://purl.uniprot.org/uniprot/Q8BIS1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Cpne1 ^@ http://purl.uniprot.org/uniprot/Q3U893|||http://purl.uniprot.org/uniprot/Q8C166 ^@ 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 ^@ C2|||C2 1|||C2 2|||Copine-1|||N6-acetyllysine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000144835 http://togogenome.org/gene/10090:Wdr46 ^@ http://purl.uniprot.org/uniprot/Q9Z0H1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat-containing protein 46 ^@ http://purl.uniprot.org/annotation/PRO_0000051396 http://togogenome.org/gene/10090:Katnbl1 ^@ http://purl.uniprot.org/uniprot/Q9CWJ3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Modified Residue|||Motif ^@ KATNB1-like protein 1|||Nuclear localization signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000089982 http://togogenome.org/gene/10090:Nrf1 ^@ http://purl.uniprot.org/uniprot/E9Q7X0|||http://purl.uniprot.org/uniprot/G3XA39|||http://purl.uniprot.org/uniprot/Q3UXF4|||http://purl.uniprot.org/uniprot/Q3UYQ3|||http://purl.uniprot.org/uniprot/Q8C4C0|||http://purl.uniprot.org/uniprot/Q8CAV3|||http://purl.uniprot.org/uniprot/Q99K73|||http://purl.uniprot.org/uniprot/Q9WU00 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Dimerization|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform Short.|||Nuclear localization signal|||Nuclear respiratory factor 1|||Nuclear respiratory factor 1 NLS/DNA-binding dimerisation|||Phosphoserine; by CK2|||Required for transcriptional activation|||TGS ^@ http://purl.uniprot.org/annotation/PRO_0000100209|||http://purl.uniprot.org/annotation/VSP_003599 http://togogenome.org/gene/10090:Cypt4 ^@ http://purl.uniprot.org/uniprot/Q6P925 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic residues|||Disordered ^@ http://togogenome.org/gene/10090:Hmgcll1 ^@ http://purl.uniprot.org/uniprot/Q8JZS7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding ^@ 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic|||N-myristoyl glycine|||Pyruvate carboxyltransferase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000334670 http://togogenome.org/gene/10090:Elp6 ^@ http://purl.uniprot.org/uniprot/Q8BK75 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Splice Variant ^@ Chain|||Mutagenesis Site|||Splice Variant ^@ Elongator complex protein 6|||In isoform 2.|||In wobbly mutant; destabilization of the elongator complex and reduced tRNA wobble base modification leading to protein misfolding and aggregation in Purkinje neurons (PN), PN degeneration, microgliosis triggered by the NLPR3 inflammasome and an ataxia-like phenotype. ^@ http://purl.uniprot.org/annotation/PRO_0000274361|||http://purl.uniprot.org/annotation/VSP_022723 http://togogenome.org/gene/10090:Pdcd6 ^@ http://purl.uniprot.org/uniprot/P12815 ^@ 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 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand ^@ Abolishes magnesium and calcium-binding to the EF-hand 5 domain (EF5).|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||In isoform 2.|||N-acetylalanine|||Programmed cell death protein 6|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073730|||http://purl.uniprot.org/annotation/VSP_047715 http://togogenome.org/gene/10090:Zfp992 ^@ http://purl.uniprot.org/uniprot/B1ASD8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Mast4 ^@ http://purl.uniprot.org/uniprot/E9PWX8|||http://purl.uniprot.org/uniprot/E9QPR4|||http://purl.uniprot.org/uniprot/Q811L6 ^@ 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 ^@ AGC-kinase C-terminal|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Microtubule-associated serine/threonine-protein kinase 4|||PDZ|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000293629|||http://purl.uniprot.org/annotation/VSP_041616|||http://purl.uniprot.org/annotation/VSP_052478|||http://purl.uniprot.org/annotation/VSP_052479|||http://purl.uniprot.org/annotation/VSP_052480 http://togogenome.org/gene/10090:Esam ^@ http://purl.uniprot.org/uniprot/Q3U102|||http://purl.uniprot.org/uniprot/Q925F2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Endothelial cell-selective adhesion molecule|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||Ig-like domain-containing protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014754|||http://purl.uniprot.org/annotation/PRO_5015097461 http://togogenome.org/gene/10090:Babam2 ^@ http://purl.uniprot.org/uniprot/Q8K3W0 ^@ 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.|||In isoform 5.|||N-acetylmethionine|||Phosphoserine|||UEV-like 1|||UEV-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000224190|||http://purl.uniprot.org/annotation/VSP_037262|||http://purl.uniprot.org/annotation/VSP_037263|||http://purl.uniprot.org/annotation/VSP_051952|||http://purl.uniprot.org/annotation/VSP_051953 http://togogenome.org/gene/10090:Kcnab3 ^@ http://purl.uniprot.org/uniprot/Q8C439|||http://purl.uniprot.org/uniprot/Q8C7S9|||http://purl.uniprot.org/uniprot/Q8VD73 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||NADP-dependent oxidoreductase ^@ http://togogenome.org/gene/10090:Zfp354c ^@ http://purl.uniprot.org/uniprot/Q571J5 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||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)|||KRAB|||Zinc finger protein 354C ^@ http://purl.uniprot.org/annotation/PRO_0000280409 http://togogenome.org/gene/10090:Csnk2a1 ^@ http://purl.uniprot.org/uniprot/Q60737 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Casein kinase II subunit alpha|||Interaction with beta subunit|||Phosphoserine; by CDK1|||Phosphothreonine; by CDK1|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085884 http://togogenome.org/gene/10090:Or13a25 ^@ http://purl.uniprot.org/uniprot/Q8VGL9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Adprhl1 ^@ http://purl.uniprot.org/uniprot/Q8BGK2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Inactive ADP-ribosyltransferase ARH2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000277607 http://togogenome.org/gene/10090:Psmc1 ^@ http://purl.uniprot.org/uniprot/P62192|||http://purl.uniprot.org/uniprot/Q542I9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region ^@ 26S proteasome regulatory subunit 4|||AAA+ ATPase|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-myristoyl glycine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000084678 http://togogenome.org/gene/10090:Cd28 ^@ http://purl.uniprot.org/uniprot/P31041|||http://purl.uniprot.org/uniprot/Q8CDB3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||Immunoglobulin V-set|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||T-cell-specific surface glycoprotein CD28 ^@ http://purl.uniprot.org/annotation/PRO_0000014653|||http://purl.uniprot.org/annotation/PRO_5004304058 http://togogenome.org/gene/10090:Sertm1 ^@ http://purl.uniprot.org/uniprot/Q8CD78 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Serine-rich and transmembrane domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000331522 http://togogenome.org/gene/10090:Ttc4 ^@ http://purl.uniprot.org/uniprot/Q3UZC4|||http://purl.uniprot.org/uniprot/Q8R3H9|||http://purl.uniprot.org/uniprot/Q9CSK1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Site ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Repeat|||Site ^@ Cns1/TTC4 wheel|||Essential for interaction with CDC6|||Essential for interaction with HSPA8|||N-acetylmethionine|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000106380 http://togogenome.org/gene/10090:Mobp ^@ http://purl.uniprot.org/uniprot/Q9D2P8 ^@ 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 X 9 AA approximate tandem repeats|||3; half-length|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Myelin-associated oligodendrocyte basic protein|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000281026|||http://purl.uniprot.org/annotation/VSP_023936|||http://purl.uniprot.org/annotation/VSP_023937|||http://purl.uniprot.org/annotation/VSP_023938|||http://purl.uniprot.org/annotation/VSP_023939|||http://purl.uniprot.org/annotation/VSP_023940|||http://purl.uniprot.org/annotation/VSP_023941|||http://purl.uniprot.org/annotation/VSP_023942 http://togogenome.org/gene/10090:Sema3a ^@ http://purl.uniprot.org/uniprot/A0A803Z7F8|||http://purl.uniprot.org/uniprot/O08665 ^@ 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|||Ig-like|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3A ^@ http://purl.uniprot.org/annotation/PRO_0000032304|||http://purl.uniprot.org/annotation/PRO_5040028599 http://togogenome.org/gene/10090:Scamp4 ^@ http://purl.uniprot.org/uniprot/Q3TGX0|||http://purl.uniprot.org/uniprot/Q9JKV5 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Phosphothreonine|||Secretory carrier-associated membrane protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000191260 http://togogenome.org/gene/10090:Hao1 ^@ http://purl.uniprot.org/uniprot/Q3UEE8|||http://purl.uniprot.org/uniprot/Q9WU19 ^@ 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 ^@ 2-Hydroxyacid oxidase 1|||FMN hydroxy acid dehydrogenase|||Microbody targeting signal|||N6-succinyllysine|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000206319 http://togogenome.org/gene/10090:Tmem167b ^@ http://purl.uniprot.org/uniprot/Q80X45 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Protein kish-B ^@ http://purl.uniprot.org/annotation/PRO_0000265082 http://togogenome.org/gene/10090:Marchf11 ^@ http://purl.uniprot.org/uniprot/D3YXE6|||http://purl.uniprot.org/uniprot/Q8CBH7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||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_0000339345|||http://purl.uniprot.org/annotation/VSP_034148|||http://purl.uniprot.org/annotation/VSP_034149 http://togogenome.org/gene/10090:Batf ^@ http://purl.uniprot.org/uniprot/O35284 ^@ 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 ^@ Basic and acidic residues|||Basic leucine zipper transcriptional factor ATF-like|||Basic motif|||Decreased phosphorylation; when associated with A-43.|||Decreased phosphorylation; when associated with A-48.|||Disordered|||Does not affect interaction with IRF4 and ability to mediate differentiation of Th17 cells. Retains 50% of activity; when associated with D63 and 69-Q-T-70. Loss of function; when associated with Q-55; A-56 and D-63.|||Impairs interaction with IRF4 and the recruitment of IRF4 to AICE motifs, leading to defects in mediate differentiation of Th17 cells. Loss of function; when associated with A-56; D-63 and K-77.|||Leucine-zipper|||Loss of function; when associated with Q-55; D-63 and K-77.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Retains 50% of activity; when associated with 69-Q-T-70 and K-77. Loss of function; when associated with Q-55; A-56 and K-77.|||Retains 50% of activity; when associated with D-63 and K-77.|||Retains the ability to dimerize with JUNB and localization in the nucleus but abolishes DNA-binding.|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076596 http://togogenome.org/gene/10090:Rin2 ^@ http://purl.uniprot.org/uniprot/F8WGD2|||http://purl.uniprot.org/uniprot/Q9D684 ^@ 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.|||Interaction with RAB5B|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Ras and Rab interactor 2|||Ras-associating|||SH2|||VPS9 ^@ http://purl.uniprot.org/annotation/PRO_0000191321|||http://purl.uniprot.org/annotation/VSP_007581 http://togogenome.org/gene/10090:Cdcp2 ^@ http://purl.uniprot.org/uniprot/Q8BQH6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ CUB 1|||CUB 2|||CUB 3|||CUB domain-containing protein 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000305072 http://togogenome.org/gene/10090:Sox5 ^@ http://purl.uniprot.org/uniprot/B2KFM4|||http://purl.uniprot.org/uniprot/B2KFM9|||http://purl.uniprot.org/uniprot/P35710|||http://purl.uniprot.org/uniprot/Q2TBA9|||http://purl.uniprot.org/uniprot/Q3TVF9|||http://purl.uniprot.org/uniprot/Q8C4K8 ^@ 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|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Disordered|||HMG box|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription factor SOX-5 ^@ http://purl.uniprot.org/annotation/PRO_0000048727|||http://purl.uniprot.org/annotation/VSP_007265|||http://purl.uniprot.org/annotation/VSP_007266|||http://purl.uniprot.org/annotation/VSP_007267 http://togogenome.org/gene/10090:Il10rb ^@ http://purl.uniprot.org/uniprot/Q8VHM7 ^@ 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|||Fibronectin type-III|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099432 http://togogenome.org/gene/10090:Poglut1 ^@ http://purl.uniprot.org/uniprot/Q8BLG5|||http://purl.uniprot.org/uniprot/Q8BV60|||http://purl.uniprot.org/uniprot/Q8BYB9 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Glycosyl transferase CAP10|||Glycosyl transferase CAP10 domain-containing protein|||Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Protein O-glucosyltransferase 1|||Proton donor/acceptor|||Significantly more secreted than wild-type. ^@ http://purl.uniprot.org/annotation/PRO_0000246686|||http://purl.uniprot.org/annotation/PRO_5004303800 http://togogenome.org/gene/10090:Igtp ^@ http://purl.uniprot.org/uniprot/Q9DCE9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict ^@ Abolished GTP-binding leading tand GTPase activity without affecting localizatiom to the endoplasmic reticulum.|||IRG-type G|||Immunity-related GTPase family M protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000457976 http://togogenome.org/gene/10090:Or5aq1b ^@ http://purl.uniprot.org/uniprot/A2AVB8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mus81 ^@ http://purl.uniprot.org/uniprot/Q91ZJ0 ^@ 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 ^@ Crossover junction endonuclease MUS81|||Disordered|||ERCC4|||Interaction with BLM|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000198859 http://togogenome.org/gene/10090:Ear10 ^@ http://purl.uniprot.org/uniprot/Q923L6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_5015020138 http://togogenome.org/gene/10090:Eno2 ^@ http://purl.uniprot.org/uniprot/D3Z6E4|||http://purl.uniprot.org/uniprot/P17183|||http://purl.uniprot.org/uniprot/Q545V3 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Enolase C-terminal TIM barrel|||Enolase N-terminal|||Gamma-enolase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||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_0000134113 http://togogenome.org/gene/10090:Btbd35f17 ^@ http://purl.uniprot.org/uniprot/L7MU81 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Mgat3 ^@ http://purl.uniprot.org/uniprot/Q5RKT9 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Nphs1 ^@ http://purl.uniprot.org/uniprot/Q9QZS7 ^@ 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|||Fibronectin type-III|||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 isoform 2.|||N-linked (GlcNAc...) asparagine|||Nephrin|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by FYN ^@ http://purl.uniprot.org/annotation/PRO_0000015053|||http://purl.uniprot.org/annotation/VSP_040676 http://togogenome.org/gene/10090:Pate1 ^@ http://purl.uniprot.org/uniprot/E9Q658 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5003244456 http://togogenome.org/gene/10090:L3mbtl2 ^@ http://purl.uniprot.org/uniprot/G3UY70|||http://purl.uniprot.org/uniprot/P59178|||http://purl.uniprot.org/uniprot/Q80XB1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ 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|||Lethal(3)malignant brain tumor-like protein 2|||MBT|||MBT 1|||MBT 2|||MBT 3|||MBT 4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084449 http://togogenome.org/gene/10090:Tcea2 ^@ http://purl.uniprot.org/uniprot/Q810R3|||http://purl.uniprot.org/uniprot/Q9QVN7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Polar residues|||TFIIS N-terminal|||TFIIS central|||TFIIS-type|||Transcription elongation factor A protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000121450 http://togogenome.org/gene/10090:Onecut3 ^@ http://purl.uniprot.org/uniprot/Q8K557 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict ^@ CUT|||Disordered|||Homeobox|||One cut domain family member 3|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000271219 http://togogenome.org/gene/10090:Ubl5c ^@ http://purl.uniprot.org/uniprot/A0A1Y7VKT9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ubiquitin-like ^@ http://togogenome.org/gene/10090:Chst11 ^@ http://purl.uniprot.org/uniprot/B7ZMT9|||http://purl.uniprot.org/uniprot/Q9JME2 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 11|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000189665 http://togogenome.org/gene/10090:Arhgef6 ^@ http://purl.uniprot.org/uniprot/F6WMJ3|||http://purl.uniprot.org/uniprot/Q8K4I3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Calponin-homology (CH)|||DH|||Disordered|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho guanine nucleotide exchange factor 6|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000080918 http://togogenome.org/gene/10090:Ptprn2 ^@ http://purl.uniprot.org/uniprot/A3KN68|||http://purl.uniprot.org/uniprot/P80560|||http://purl.uniprot.org/uniprot/Q3UU93 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||IA-2beta60|||IA-2beta64|||IA-2beta71|||Impairs localization to secretory granules, promotes location at the TGN, decreases interaction with alpha- and gamma-type adaptin subunits.|||Impairs localization to secretory granules, promotes location at the plasma membrane, defective ind gamma endocytosis, highly decreases interaction with alpha- and gamma-type adaptin subunits.|||Involved in localization to secretory granules; interaction with CPE|||Leucine-based sorting signal|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Receptor-type tyrosine-protein phosphatase N2|||Tyrosine specific protein phosphatases|||Tyrosine-based internalization motif|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000025456|||http://purl.uniprot.org/annotation/PRO_0000438071|||http://purl.uniprot.org/annotation/PRO_0000438072|||http://purl.uniprot.org/annotation/PRO_0000438090|||http://purl.uniprot.org/annotation/PRO_5002655525|||http://purl.uniprot.org/annotation/PRO_5015097516 http://togogenome.org/gene/10090:Trip13 ^@ http://purl.uniprot.org/uniprot/Q3UA06 ^@ 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 ^@ In isoform 2.|||N-acetylmethionine|||Pachytene checkpoint protein 2 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000084783|||http://purl.uniprot.org/annotation/VSP_041559 http://togogenome.org/gene/10090:Sp110 ^@ http://purl.uniprot.org/uniprot/Q8BVK9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||Basic residues|||Disordered|||HSR|||Nuclear localization signal|||Phosphoserine|||Polar residues|||SAND|||Sp110 nuclear body protein ^@ http://purl.uniprot.org/annotation/PRO_0000247960 http://togogenome.org/gene/10090:Jun ^@ http://purl.uniprot.org/uniprot/P05627|||http://purl.uniprot.org/uniprot/Q52L79 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ BZIP|||Basic motif|||Disordered|||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 PAGE4|||Leucine-zipper|||N6-acetyllysine|||N6-acetyllysine; alternate|||Necessary for synergistic transcriptional activity with SMAD3|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphoserine; by MAPK8 and PLK3|||Phosphothreonine|||Phosphothreonine; by PAK2|||Pro residues|||Transcription factor Jun|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076430 http://togogenome.org/gene/10090:Iffo2 ^@ http://purl.uniprot.org/uniprot/B1AZL1|||http://purl.uniprot.org/uniprot/Q8R2V2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||IF rod|||Intermediate filament family orphan 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000326186 http://togogenome.org/gene/10090:Utp23 ^@ http://purl.uniprot.org/uniprot/Q9CX11 ^@ 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)|||Phosphoserine|||rRNA-processing protein UTP23 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000285635 http://togogenome.org/gene/10090:Gpc1 ^@ http://purl.uniprot.org/uniprot/Q3U379|||http://purl.uniprot.org/uniprot/Q9QZF2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||GPI-anchor amidated serine|||Glypican-1|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (heparan sulfate) serine|||Polar residues|||Removed in mature form|||Secreted glypican-1 ^@ http://purl.uniprot.org/annotation/PRO_0000012297|||http://purl.uniprot.org/annotation/PRO_0000012298|||http://purl.uniprot.org/annotation/PRO_0000333838|||http://purl.uniprot.org/annotation/PRO_5014309203 http://togogenome.org/gene/10090:Mid1ip1 ^@ http://purl.uniprot.org/uniprot/Q4FK31|||http://purl.uniprot.org/uniprot/Q9CQ20 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Mid1-interacting protein 1|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000123778 http://togogenome.org/gene/10090:Gm6710 ^@ http://purl.uniprot.org/uniprot/A2ART0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Scml4 ^@ http://purl.uniprot.org/uniprot/Q3UR41|||http://purl.uniprot.org/uniprot/Q80VG1 ^@ 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.|||Phosphoserine|||Polar residues|||SAM|||Sex comb on midleg-like protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000337172|||http://purl.uniprot.org/annotation/VSP_033947 http://togogenome.org/gene/10090:Slc39a7 ^@ http://purl.uniprot.org/uniprot/A0A068BIT0|||http://purl.uniprot.org/uniprot/Q31125 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Abolished METTL9-mediated methylation.|||Basic and acidic residues|||Decreased METTL9-mediated methylation; when associated with A-204.|||Decreased METTL9-mediated methylation; when associated with A-216.|||Decreased METTL9-mediated methylation; when associated with A-254.|||Decreased METTL9-mediated methylation; when associated with A-262.|||Disordered|||Helical|||Homozygous mice have profound B cell immunodeficiency and impaired transition from late pre-B to immature B cell. B cells from mutant mice exhibit a diminished concentration of cytoplasmic free zinc and decreased phosphorylation of signaling molecules downstream of the pre-B cell and B cell receptors.|||Phosphoserine|||Pros-methylhistidine|||Zinc transporter SLC39A7 ^@ http://purl.uniprot.org/annotation/PRO_0000213689|||http://purl.uniprot.org/annotation/PRO_5010012414 http://togogenome.org/gene/10090:Zic5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0E2|||http://purl.uniprot.org/uniprot/Q7TQ40 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ C2H2-type|||C2H2-type 1; degenerate|||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_0000406213 http://togogenome.org/gene/10090:Nwd2 ^@ http://purl.uniprot.org/uniprot/Q6P5U7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||NACHT|||NACHT and WD repeat domain-containing protein 2|||Polar residues|||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_0000320921 http://togogenome.org/gene/10090:Cyp2j8 ^@ http://purl.uniprot.org/uniprot/G3UZ38 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Vmn2r90 ^@ http://purl.uniprot.org/uniprot/E9PXJ8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245484 http://togogenome.org/gene/10090:Nlrp1b ^@ http://purl.uniprot.org/uniprot/A1Z198 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Region|||Repeat|||Site|||Splice Variant ^@ CARD|||Cleavage; by autolysis|||Disordered|||FIIND|||In isoform 2 and isoform 3.|||In isoform 3.|||LRR 1|||LRR 2|||NACHT|||NACHT, LRR and PYD domains-containing protein 1b allele 2|||NACHT, LRR and PYD domains-containing protein 1b, C-terminus|||NACHT, LRR and PYD domains-containing protein 1b, N-terminus|||Trigger for autolytic processing|||UPA|||ZU5 ^@ http://purl.uniprot.org/annotation/PRO_0000435104|||http://purl.uniprot.org/annotation/PRO_0000452857|||http://purl.uniprot.org/annotation/PRO_0000452858|||http://purl.uniprot.org/annotation/VSP_058005|||http://purl.uniprot.org/annotation/VSP_058006|||http://purl.uniprot.org/annotation/VSP_058007 http://togogenome.org/gene/10090:Cyp8b1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0N7|||http://purl.uniprot.org/uniprot/O88962 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Sequence Variant|||Transmembrane ^@ 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase|||Helical|||In strain: 129/SvJ.|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051914 http://togogenome.org/gene/10090:Smim13 ^@ http://purl.uniprot.org/uniprot/E9Q942 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Polar residues|||Small integral membrane protein 13 ^@ http://purl.uniprot.org/annotation/PRO_0000414061 http://togogenome.org/gene/10090:Or4e2 ^@ http://purl.uniprot.org/uniprot/Q7TQQ0 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreased receptor activity in response to MTMT binding, even in the presence of copper.|||Decreased receptor activity in response to MTMT binding, even in the presence of copper. Complete loss of receptor activity in the absence of copper.|||Decreased receptor activity in response to MTMT binding, even in the presence of copper. Shows low constitutive activity in the presence of copper. MTMT binding in the absence of copper results in an inverse agonist effect.|||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 change in receptor activity in response to MTMT binding in the presence of copper. Complete loss of receptor activity in the absence of copper.|||No change in receptor activity in response to MTMT binding in the presence of copper. Decreased receptor activity in the absence of copper.|||No change in receptor activity in response to MTMT binding. No change in the copper-induced enhancement of receptor activity.|||No receptor activity in response to MTMT binding, even in the presence of copper.|||No receptor activity in response to MTMT binding, even in the presence of copper. Little to no expression detected on plasma membrane.|||Olfactory receptor 4E2 ^@ http://purl.uniprot.org/annotation/PRO_0000444894 http://togogenome.org/gene/10090:AU021092 ^@ http://purl.uniprot.org/uniprot/Q3UST5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Polar residues|||UPF0764 protein C16orf89 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000326203 http://togogenome.org/gene/10090:Hdlbp ^@ http://purl.uniprot.org/uniprot/Q3U4Z7|||http://purl.uniprot.org/uniprot/Q3V1M8|||http://purl.uniprot.org/uniprot/Q8VDJ3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||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_0000050132 http://togogenome.org/gene/10090:Ckap2l ^@ http://purl.uniprot.org/uniprot/Q7TS74 ^@ 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 ^@ Basic and acidic residues|||Cytoskeleton-associated protein 2-like|||Disordered|||Drastically enhances protein stability.|||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.|||KEN box|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000324336|||http://purl.uniprot.org/annotation/VSP_032221|||http://purl.uniprot.org/annotation/VSP_032222 http://togogenome.org/gene/10090:Spata16 ^@ http://purl.uniprot.org/uniprot/Q8C636 ^@ 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.|||No loss of male fertility.|||Polar residues|||Spermatogenesis-associated protein 16 ^@ http://purl.uniprot.org/annotation/PRO_0000315832|||http://purl.uniprot.org/annotation/VSP_030726 http://togogenome.org/gene/10090:Plekhg2 ^@ http://purl.uniprot.org/uniprot/D3Z5N8|||http://purl.uniprot.org/uniprot/E9QKB6|||http://purl.uniprot.org/uniprot/G5E8T4|||http://purl.uniprot.org/uniprot/Q6KAU7 ^@ 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 ^@ DH|||Disordered|||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_0000306862|||http://purl.uniprot.org/annotation/VSP_028531|||http://purl.uniprot.org/annotation/VSP_028532 http://togogenome.org/gene/10090:Egr2 ^@ http://purl.uniprot.org/uniprot/P08152|||http://purl.uniprot.org/uniprot/Q3U207 ^@ 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 acetylation.|||Abolishes interaction with WWP2; if associated with F-174.|||Abolishes interaction with WWP2; if associated with F-208.|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||E3 SUMO-protein ligase EGR2|||In isoform Short.|||Inhibits interaction with SFN.|||N6-acetyllysine; by EP300|||Polar residues|||Reduces transcriptional regulatory activity. ^@ http://purl.uniprot.org/annotation/PRO_0000047120|||http://purl.uniprot.org/annotation/VSP_006864 http://togogenome.org/gene/10090:Ptprg ^@ http://purl.uniprot.org/uniprot/A0A991ELE1|||http://purl.uniprot.org/uniprot/Q05909|||http://purl.uniprot.org/uniprot/Q3UND4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||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|||Region|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Alpha-carbonic anhydrase|||Ancestral active site|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Receptor-type tyrosine-protein phosphatase gamma|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000025442 http://togogenome.org/gene/10090:Or51q1c ^@ http://purl.uniprot.org/uniprot/Q8VH20 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Msrb1 ^@ http://purl.uniprot.org/uniprot/Q9JLC3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Non standard residue|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non standard residue|||Strand|||Turn ^@ Methionine-R-sulfoxide reductase B1|||MsrB|||Nucleophile|||Optimum pH 7.5.|||Selenocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000140322 http://togogenome.org/gene/10090:Pibf1 ^@ http://purl.uniprot.org/uniprot/E9Q6K3|||http://purl.uniprot.org/uniprot/Q8BIR5|||http://purl.uniprot.org/uniprot/Q9CVX7 ^@ Coiled-Coil|||Region ^@ Coiled-Coil ^@ ^@ http://togogenome.org/gene/10090:Rhbdl1 ^@ http://purl.uniprot.org/uniprot/Q3USF1|||http://purl.uniprot.org/uniprot/Q8VC82 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Transmembrane ^@ Helical|||Nucleophile|||Peptidase S54 rhomboid|||Rhomboid-related protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000206174 http://togogenome.org/gene/10090:Bmi1 ^@ http://purl.uniprot.org/uniprot/P25916|||http://purl.uniprot.org/uniprot/Q2LC58 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Strand|||Turn|||Zinc Finger ^@ Disordered|||Interaction with E4F1|||Interaction with PHC2|||Nuclear localization signal|||Polar residues|||Polycomb complex protein BMI-1|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055988 http://togogenome.org/gene/10090:Tlcd2 ^@ http://purl.uniprot.org/uniprot/Q8VC26 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||TLC|||TLC domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000328991|||http://purl.uniprot.org/annotation/VSP_032879|||http://purl.uniprot.org/annotation/VSP_032880 http://togogenome.org/gene/10090:Ifrd1 ^@ http://purl.uniprot.org/uniprot/P19182 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Interferon-related developmental regulator 1 ^@ http://purl.uniprot.org/annotation/PRO_0000153286 http://togogenome.org/gene/10090:Krtap16-3 ^@ http://purl.uniprot.org/uniprot/Q8C1I6 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ 25 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 16-3 ^@ http://purl.uniprot.org/annotation/PRO_0000356210 http://togogenome.org/gene/10090:Raf1 ^@ http://purl.uniprot.org/uniprot/Q99N57 ^@ 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|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform 2.|||Interaction with PEBP1/RKIP|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by MAPK1|||Phosphoserine; by PAK1, PAK2 and PAK3|||Phosphoserine; by PAK1, PAK2, PAK3 and PAK5|||Phosphoserine; by PKA|||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|||Symmetric dimethylarginine; by PRMT5 ^@ http://purl.uniprot.org/annotation/PRO_0000086597|||http://purl.uniprot.org/annotation/VSP_034629 http://togogenome.org/gene/10090:Cd69 ^@ http://purl.uniprot.org/uniprot/P37217|||http://purl.uniprot.org/uniprot/Q3U6A8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ 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_0000046584 http://togogenome.org/gene/10090:A930018P22Rik ^@ http://purl.uniprot.org/uniprot/Q9D1Z2 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Uncharacterized protein C11orf91 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000340698 http://togogenome.org/gene/10090:Tnip2 ^@ http://purl.uniprot.org/uniprot/Q99JG7 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ CCHC NOA-type|||Disordered|||Phosphoserine|||TNFAIP3-interacting protein 2|||Ubiquitin-binding domain (UBD) ^@ http://purl.uniprot.org/annotation/PRO_0000322584 http://togogenome.org/gene/10090:Ywhaz ^@ http://purl.uniprot.org/uniprot/P63101 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Site|||Turn ^@ 14-3-3 protein zeta/delta|||Interaction with phosphoserine on interacting protein|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine; by CK1 ^@ http://purl.uniprot.org/annotation/PRO_0000058628 http://togogenome.org/gene/10090:Nupr1l ^@ http://purl.uniprot.org/uniprot/Q497P3 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Nuclear protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000346769 http://togogenome.org/gene/10090:Enpp6 ^@ http://purl.uniprot.org/uniprot/Q8BGN3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Almost loss of glycerophosphocholine cholinephosphodiesterase activity. Loss of choline metabolism.|||Does not affect Glycerophosphocholine cholinephosphodiesterase activity; when associated withA-393. Does not affect choline metabolism; when associated with A-393.|||Does not affect glycerophosphocholine cholinephosphodiesterase activity; when associated with S-412. Does not affect choline metabolism; when associated with S-412.|||GPI-anchor amidated serine|||Glycerophosphocholine cholinephosphodiesterase ENPP6|||Highly decreases glycerophosphocholine cholinephosphodiesterase activity. Loss of choline metabolism.|||Interchain|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphoserine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000239363|||http://purl.uniprot.org/annotation/PRO_0000420891 http://togogenome.org/gene/10090:Ddi1 ^@ http://purl.uniprot.org/uniprot/Q9DAF3 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand|||Turn ^@ Basic residues|||Disordered|||Protein DDI1 homolog 1|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000287088 http://togogenome.org/gene/10090:Fra10ac1 ^@ http://purl.uniprot.org/uniprot/Q8BP78 ^@ 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|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Protein FRA10AC1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000087149 http://togogenome.org/gene/10090:Six5 ^@ http://purl.uniprot.org/uniprot/P70178 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein SIX5 ^@ http://purl.uniprot.org/annotation/PRO_0000049306 http://togogenome.org/gene/10090:Ube2d2b ^@ http://purl.uniprot.org/uniprot/Q6ZWY6 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ Glycyl thioester intermediate|||UBC core|||Ubiquitin-conjugating enzyme E2 D2B ^@ http://purl.uniprot.org/annotation/PRO_0000283816 http://togogenome.org/gene/10090:Cenpo ^@ http://purl.uniprot.org/uniprot/Q8K015 ^@ 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 ^@ Centromere protein O|||Disordered|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000249503|||http://purl.uniprot.org/annotation/VSP_020447|||http://purl.uniprot.org/annotation/VSP_020448 http://togogenome.org/gene/10090:Angptl2 ^@ http://purl.uniprot.org/uniprot/Q9R045 ^@ 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 ^@ Angiopoietin-related protein 2|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009121 http://togogenome.org/gene/10090:Ociad1 ^@ http://purl.uniprot.org/uniprot/Q9CRD0 ^@ 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.|||OCIA|||OCIA domain-containing protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000299384|||http://purl.uniprot.org/annotation/VSP_027623|||http://purl.uniprot.org/annotation/VSP_027624|||http://purl.uniprot.org/annotation/VSP_027625 http://togogenome.org/gene/10090:Irgc1 ^@ http://purl.uniprot.org/uniprot/D3Z720 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||IRG-type G ^@ http://togogenome.org/gene/10090:Btbd1 ^@ http://purl.uniprot.org/uniprot/P58544 ^@ 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 ^@ BACK|||BTB|||BTB/POZ domain-containing protein 1|||Disordered|||Fails to induce myogenic differentiation in C2C12 cells.|||Omega-N-methylarginine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000186209 http://togogenome.org/gene/10090:Aff1 ^@ http://purl.uniprot.org/uniprot/A3KMF4|||http://purl.uniprot.org/uniprot/E9Q921|||http://purl.uniprot.org/uniprot/Q3UP77|||http://purl.uniprot.org/uniprot/Q3UQD9 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ AF4/FMR2 C-terminal homology|||Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Snx10 ^@ http://purl.uniprot.org/uniprot/Q3UBN7|||http://purl.uniprot.org/uniprot/Q4FJX6|||http://purl.uniprot.org/uniprot/Q9CWT3 ^@ 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 ^@ Basic and acidic residues|||Disordered|||PX|||Polar residues|||Required for interaction with ATP6V1D|||Sorting nexin-10 ^@ http://purl.uniprot.org/annotation/PRO_0000213855 http://togogenome.org/gene/10090:Vangl2 ^@ http://purl.uniprot.org/uniprot/Q91ZD4 ^@ 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 residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In Lp.|||Polar residues|||Vang-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000186196 http://togogenome.org/gene/10090:Phf24 ^@ http://purl.uniprot.org/uniprot/Q80TL4 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||N-myristoyl glycine|||Omega-N-methylarginine|||PHD finger protein 24|||PHD-type|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000059332|||http://purl.uniprot.org/annotation/VSP_014952 http://togogenome.org/gene/10090:Ppat ^@ http://purl.uniprot.org/uniprot/Q3UGA8|||http://purl.uniprot.org/uniprot/Q8CIH9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Propeptide|||Sequence Conflict ^@ Amidophosphoribosyltransferase|||Glutamine amidotransferase type-2|||N-acetylmethionine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000455153|||http://purl.uniprot.org/annotation/PRO_0000455154 http://togogenome.org/gene/10090:Tle4 ^@ http://purl.uniprot.org/uniprot/Q3UY41|||http://purl.uniprot.org/uniprot/Q62441 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||CcN domain|||Disordered|||GP domain|||Groucho/TLE N-terminal Q-rich|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by CK2|||Phosphothreonine|||Polar residues|||Q domain|||SP domain|||Transducin-like enhancer protein 4|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051284 http://togogenome.org/gene/10090:Lrp8 ^@ http://purl.uniprot.org/uniprot/A0A571BE60|||http://purl.uniprot.org/uniprot/B1AXJ4|||http://purl.uniprot.org/uniprot/B1AXJ5|||http://purl.uniprot.org/uniprot/F6YZZ8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Disordered|||EGF-like|||Helical|||LDL-receptor class B ^@ http://purl.uniprot.org/annotation/PRO_5002761485|||http://purl.uniprot.org/annotation/PRO_5002761947|||http://purl.uniprot.org/annotation/PRO_5021715989|||http://purl.uniprot.org/annotation/PRO_5021852363 http://togogenome.org/gene/10090:Or2y16 ^@ http://purl.uniprot.org/uniprot/Q8VFA3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ypel1 ^@ http://purl.uniprot.org/uniprot/A0A338P6Z8|||http://purl.uniprot.org/uniprot/Q65Z96|||http://purl.uniprot.org/uniprot/Q9ESC7 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif ^@ Nuclear localization signal|||Protein yippee-like 1|||Yippee ^@ http://purl.uniprot.org/annotation/PRO_0000212382 http://togogenome.org/gene/10090:Defb33 ^@ http://purl.uniprot.org/uniprot/Q30KN3 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 33 ^@ http://purl.uniprot.org/annotation/PRO_0000352712 http://togogenome.org/gene/10090:Ambn ^@ http://purl.uniprot.org/uniprot/O55189|||http://purl.uniprot.org/uniprot/Q5M8P3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Modified Residue|||Region|||Signal Peptide ^@ Ameloblastin|||Disordered|||Hydroxyproline|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000001193|||http://purl.uniprot.org/annotation/PRO_5015097936 http://togogenome.org/gene/10090:Spint1 ^@ http://purl.uniprot.org/uniprot/Q9R097 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site ^@ BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||Kunitz-type protease inhibitor 1|||LDL-receptor class A|||MANSC|||N-linked (GlcNAc...) asparagine|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000016884 http://togogenome.org/gene/10090:Azin1 ^@ http://purl.uniprot.org/uniprot/O35484 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Chain|||Helix|||Sequence Conflict|||Site|||Strand|||Turn ^@ Antizyme inhibitor 1|||Not modified ^@ http://purl.uniprot.org/annotation/PRO_0000149993 http://togogenome.org/gene/10090:Git2 ^@ http://purl.uniprot.org/uniprot/D3Z1I2|||http://purl.uniprot.org/uniprot/E9PVA6|||http://purl.uniprot.org/uniprot/Q5DU47|||http://purl.uniprot.org/uniprot/Q80XR8|||http://purl.uniprot.org/uniprot/Q9JLQ2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ARF GTPase-activating protein GIT2|||Arf-GAP|||Basic and acidic residues|||C4-type|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000074204 http://togogenome.org/gene/10090:Or8k20 ^@ http://purl.uniprot.org/uniprot/Q7TR76 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Icam5 ^@ http://purl.uniprot.org/uniprot/Q60625 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Fails to form disulfide bonds and to induce filopodia-like protrusions.|||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|||Ig-like C2-type 9|||Intercellular adhesion molecule 5|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000014800 http://togogenome.org/gene/10090:Tha1 ^@ http://purl.uniprot.org/uniprot/Q6XPS7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Signal Peptide ^@ Aromatic amino acid beta-eliminating lyase/threonine aldolase|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_5015098600 http://togogenome.org/gene/10090:Esf1 ^@ http://purl.uniprot.org/uniprot/A2APY6|||http://purl.uniprot.org/uniprot/Q3V1V3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||ESF1 homolog|||N-acetylserine|||NUC153|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000233166 http://togogenome.org/gene/10090:Rbm15 ^@ http://purl.uniprot.org/uniprot/Q0VBL3 ^@ 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 ^@ Asymmetric dimethylarginine; alternate; by PRMT1|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||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_0000444611|||http://purl.uniprot.org/annotation/VSP_059625 http://togogenome.org/gene/10090:Cttnbp2 ^@ http://purl.uniprot.org/uniprot/B9EJA2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Almost complete loss of CTTN-binding and loss of regulation of spine density; when associated with A-540.|||Almost complete loss of CTTN-binding and loss of regulation of spine density; when associated with A-543.|||Asymmetric dimethylarginine|||Basic and acidic residues|||Cortactin-binding protein 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||Pro residues|||Reduced CTTN-binding; when associated with A-599.|||Reduced CTTN-binding; when associated with A-602. ^@ http://purl.uniprot.org/annotation/PRO_0000422172|||http://purl.uniprot.org/annotation/VSP_046473|||http://purl.uniprot.org/annotation/VSP_046474|||http://purl.uniprot.org/annotation/VSP_046475|||http://purl.uniprot.org/annotation/VSP_046476|||http://purl.uniprot.org/annotation/VSP_046477|||http://purl.uniprot.org/annotation/VSP_046478 http://togogenome.org/gene/10090:Vmn1r149 ^@ http://purl.uniprot.org/uniprot/E9PWL6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tmem64 ^@ http://purl.uniprot.org/uniprot/Q3U145 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 64|||VTT domain ^@ http://purl.uniprot.org/annotation/PRO_0000287343 http://togogenome.org/gene/10090:Adgra1 ^@ http://purl.uniprot.org/uniprot/Q6PHM3|||http://purl.uniprot.org/uniprot/Q8C4G9 ^@ 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 ^@ Adhesion G protein-coupled receptor A1|||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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000433253 http://togogenome.org/gene/10090:Sh3d21 ^@ http://purl.uniprot.org/uniprot/Q7TSG5|||http://purl.uniprot.org/uniprot/Q9CT24|||http://purl.uniprot.org/uniprot/Q9D9T7|||http://purl.uniprot.org/uniprot/Z4YK11 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||SH3|||SH3 domain-containing protein 21 ^@ http://purl.uniprot.org/annotation/PRO_0000337131|||http://purl.uniprot.org/annotation/VSP_033936 http://togogenome.org/gene/10090:Vmn1r21 ^@ http://purl.uniprot.org/uniprot/Q8R2C6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nr1h5 ^@ http://purl.uniprot.org/uniprot/A0A0G2JEJ9|||http://purl.uniprot.org/uniprot/A0A0G2JG67|||http://purl.uniprot.org/uniprot/E9Q5A6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||NR LBD|||Nuclear receptor ^@ http://togogenome.org/gene/10090:Lta ^@ http://purl.uniprot.org/uniprot/P09225|||http://purl.uniprot.org/uniprot/Q542S2 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Lymphotoxin-alpha|||N-linked (GlcNAc...) asparagine|||TNF family profile ^@ http://purl.uniprot.org/annotation/PRO_0000034467 http://togogenome.org/gene/10090:Rgsl1 ^@ http://purl.uniprot.org/uniprot/H3BL40|||http://purl.uniprot.org/uniprot/Q8CDT4 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||RGS ^@ http://togogenome.org/gene/10090:Cfhr2 ^@ http://purl.uniprot.org/uniprot/Q4LDF6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Sushi ^@ http://purl.uniprot.org/annotation/PRO_5015097629 http://togogenome.org/gene/10090:Rtf2 ^@ http://purl.uniprot.org/uniprot/Q99K95 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Replication termination factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000079428 http://togogenome.org/gene/10090:Zfp523 ^@ http://purl.uniprot.org/uniprot/Q8BMU0 ^@ Chain|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Zinc Finger ^@ Chain|||Crosslink|||Region|||Repeat|||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 2.|||Zinc finger protein 76 ^@ http://purl.uniprot.org/annotation/PRO_0000353096|||http://purl.uniprot.org/annotation/VSP_035628|||http://purl.uniprot.org/annotation/VSP_035629 http://togogenome.org/gene/10090:Degs1 ^@ http://purl.uniprot.org/uniprot/O09005 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict|||Transmembrane ^@ Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||N-myristoyl glycine|||Phosphoserine|||Removed|||Sphingolipid delta(4)-desaturase DES1 ^@ http://purl.uniprot.org/annotation/PRO_0000312729 http://togogenome.org/gene/10090:Gimap4 ^@ http://purl.uniprot.org/uniprot/D3YWB5|||http://purl.uniprot.org/uniprot/D3Z3F3|||http://purl.uniprot.org/uniprot/D3Z7Q4|||http://purl.uniprot.org/uniprot/Q99JY3 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant ^@ AIG1-type G|||Disordered|||G1|||G2|||G3|||G4|||G5|||GTPase IMAP family member 4|||IQ|||In isoform 2.|||Loss of interaction with CALM1. ^@ http://purl.uniprot.org/annotation/PRO_0000190988|||http://purl.uniprot.org/annotation/VSP_060167|||http://purl.uniprot.org/annotation/VSP_060168 http://togogenome.org/gene/10090:Rps18 ^@ http://purl.uniprot.org/uniprot/P62270 ^@ 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)|||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_0000132213 http://togogenome.org/gene/10090:N6amt1 ^@ http://purl.uniprot.org/uniprot/Q6SKR2 ^@ 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.|||Methyltransferase N6AMT1 ^@ http://purl.uniprot.org/annotation/PRO_0000445556|||http://purl.uniprot.org/annotation/VSP_059900|||http://purl.uniprot.org/annotation/VSP_059901|||http://purl.uniprot.org/annotation/VSP_059902|||http://purl.uniprot.org/annotation/VSP_059903 http://togogenome.org/gene/10090:Cldnd1 ^@ http://purl.uniprot.org/uniprot/A0A811BIT5|||http://purl.uniprot.org/uniprot/Q9CQX5 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Claudin domain-containing protein 1|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000164695 http://togogenome.org/gene/10090:Or5m9 ^@ http://purl.uniprot.org/uniprot/A0A1L1ST14 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp626 ^@ http://purl.uniprot.org/uniprot/A0A0U1RQ84|||http://purl.uniprot.org/uniprot/Q9CUC2 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Fam120c ^@ http://purl.uniprot.org/uniprot/Q3V3X9|||http://purl.uniprot.org/uniprot/Q8C3F2 ^@ 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|||Constitutive coactivator of PPAR-gamma-like protein 2|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000221629|||http://purl.uniprot.org/annotation/VSP_010521|||http://purl.uniprot.org/annotation/VSP_010522|||http://purl.uniprot.org/annotation/VSP_010523|||http://purl.uniprot.org/annotation/VSP_010524 http://togogenome.org/gene/10090:Susd2 ^@ http://purl.uniprot.org/uniprot/Q9DBX3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ AMOP|||Alternate|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||SMB|||Sushi|||Sushi domain-containing protein 2|||VWFD ^@ http://purl.uniprot.org/annotation/PRO_0000249440|||http://purl.uniprot.org/annotation/VSP_020425|||http://purl.uniprot.org/annotation/VSP_020426 http://togogenome.org/gene/10090:Cdt1 ^@ http://purl.uniprot.org/uniprot/Q8R4E9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ Cyclin-binding motif|||DNA replication factor Cdt1|||Disordered|||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_0000191620 http://togogenome.org/gene/10090:Gm20843 ^@ http://purl.uniprot.org/uniprot/J3QNI1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Havcr2 ^@ http://purl.uniprot.org/uniprot/Q8VIM0 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes phagocytic activity.|||Abolishes phosphorylation, disrupts interaction with PIK3R1 and PIK3R2, no LGALS9-mediated disruption of interaction with BAG6; when associated with F-256.|||Abolishes phosphorylation, disrupts interaction with PIK3R1 and PIK3R2, no LGALS9-mediated disruption of interaction with BAG6; when associated with F-263.|||Cytoplasmic|||Decreases phosphatidylserine binding, abolishes phagocytic activity.|||Decreases phosphatidylserine binding.|||Disordered|||Extracellular|||Greatly decreases phosphatidylserine binding.|||Helical|||Hepatitis A virus cellular receptor 2 homolog|||Ig-like V-type|||In isoform 2.|||Interaction with BAG6|||N-linked (GlcNAc...) asparagine|||No effect on phagocytic activity.|||O-linked (GalNAc...) threonine|||Phosphotyrosine; by ITK ^@ http://purl.uniprot.org/annotation/PRO_0000042102|||http://purl.uniprot.org/annotation/VSP_058116 http://togogenome.org/gene/10090:Scgb1b27 ^@ http://purl.uniprot.org/uniprot/Q91WB5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099530 http://togogenome.org/gene/10090:Actc1 ^@ http://purl.uniprot.org/uniprot/P68033 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Actin, alpha cardiac muscle 1|||Actin, alpha cardiac muscle 1, intermediate form|||Methionine (R)-sulfoxide|||N-acetylcysteine; in intermediate form|||N6-methyllysine|||Removed|||Tele-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000000815|||http://purl.uniprot.org/annotation/PRO_0000442999 http://togogenome.org/gene/10090:Cxcl2 ^@ http://purl.uniprot.org/uniprot/P10889|||http://purl.uniprot.org/uniprot/Q3U1J5 ^@ 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 ^@ C-X-C motif chemokine|||C-X-C motif chemokine 2|||Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_0000005061|||http://purl.uniprot.org/annotation/PRO_5014205827 http://togogenome.org/gene/10090:Itgb1bp1 ^@ http://purl.uniprot.org/uniprot/O35671 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Disordered|||Integrin beta-1-binding protein 1|||Interaction with ITGB1|||Interaction with KRIT1|||Nuclear localization signal|||PID|||Phosphoserine|||Phosphothreonine; by CaMK2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084265 http://togogenome.org/gene/10090:Ankrd44 ^@ http://purl.uniprot.org/uniprot/B2RXR6|||http://purl.uniprot.org/uniprot/E9QNQ2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||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|||Disordered|||Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B ^@ http://purl.uniprot.org/annotation/PRO_0000355975 http://togogenome.org/gene/10090:Fbxo31 ^@ http://purl.uniprot.org/uniprot/Q3TQF0 ^@ 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|||F-box|||F-box only protein 31|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000349260 http://togogenome.org/gene/10090:Capn11 ^@ http://purl.uniprot.org/uniprot/Q6J756 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region ^@ Calpain catalytic|||Calpain-11|||Domain III|||Domain IV|||EF-hand 1|||EF-hand 2|||Linker ^@ http://purl.uniprot.org/annotation/PRO_0000356219 http://togogenome.org/gene/10090:Tmprss5 ^@ http://purl.uniprot.org/uniprot/A2RSL0|||http://purl.uniprot.org/uniprot/Q9ER04 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Charge relay system|||Cleavage|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 1.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SRCR|||Transmembrane protease serine 5 ^@ http://purl.uniprot.org/annotation/PRO_0000088695|||http://purl.uniprot.org/annotation/VSP_005395|||http://purl.uniprot.org/annotation/VSP_005396|||http://purl.uniprot.org/annotation/VSP_005397|||http://purl.uniprot.org/annotation/VSP_005398 http://togogenome.org/gene/10090:Enc1 ^@ http://purl.uniprot.org/uniprot/O35709 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ BTB|||Ectoderm-neural cortex protein 1|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6 ^@ http://purl.uniprot.org/annotation/PRO_0000119069 http://togogenome.org/gene/10090:Arfgef2 ^@ http://purl.uniprot.org/uniprot/A2A5R2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Brefeldin A-inhibited guanine nucleotide-exchange protein 2|||DCB; DCB:DCB domain and DCB:HUS domain interaction|||Disordered|||HUS; DCB:HUS domain interaction|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000419332 http://togogenome.org/gene/10090:Lrrc73 ^@ http://purl.uniprot.org/uniprot/B2RWC4 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Gm14632 ^@ http://purl.uniprot.org/uniprot/Q62478 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Tbc1d30 ^@ http://purl.uniprot.org/uniprot/Q69ZT9 ^@ 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 ^@ Disordered|||Phosphoserine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 30 ^@ http://purl.uniprot.org/annotation/PRO_0000320653 http://togogenome.org/gene/10090:Zfp28 ^@ http://purl.uniprot.org/uniprot/P10078|||http://purl.uniprot.org/uniprot/Q69ZJ8 ^@ 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 ^@ C2H2-type|||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.|||In strain: 129/Sv; requires 2 nucleotide substitutions.|||KRAB|||Polar residues|||Zinc finger protein 28 ^@ http://purl.uniprot.org/annotation/PRO_0000047290|||http://purl.uniprot.org/annotation/VSP_006882 http://togogenome.org/gene/10090:Ugt2b1 ^@ http://purl.uniprot.org/uniprot/Q8R084 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||UDP-glucuronosyltransferase ^@ http://purl.uniprot.org/annotation/PRO_5015020128 http://togogenome.org/gene/10090:Surf2 ^@ http://purl.uniprot.org/uniprot/P09926|||http://purl.uniprot.org/uniprot/Q4VAF7 ^@ 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|||Phosphothreonine|||Surfeit locus protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000072320 http://togogenome.org/gene/10090:Dgcr8 ^@ http://purl.uniprot.org/uniprot/Q9EQM6 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ DRBM 1|||DRBM 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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|||WW|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000079879 http://togogenome.org/gene/10090:Slc28a2 ^@ http://purl.uniprot.org/uniprot/O88627 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Phosphoserine|||Sodium/nucleoside cotransporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000070451 http://togogenome.org/gene/10090:Adam2 ^@ http://purl.uniprot.org/uniprot/Q60718 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 2|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000029046|||http://purl.uniprot.org/annotation/PRO_0000029047 http://togogenome.org/gene/10090:Zscan12 ^@ http://purl.uniprot.org/uniprot/Q6ZQB8|||http://purl.uniprot.org/uniprot/Q8C6D3|||http://purl.uniprot.org/uniprot/Q9Z1D7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||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; degenerate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000047404 http://togogenome.org/gene/10090:Lbh ^@ http://purl.uniprot.org/uniprot/Q9CX60 ^@ 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|||LBH|||Phosphoserine|||Protein LBH ^@ http://purl.uniprot.org/annotation/PRO_0000324803 http://togogenome.org/gene/10090:Grk2 ^@ http://purl.uniprot.org/uniprot/Q3U1V3|||http://purl.uniprot.org/uniprot/Q7TS64|||http://purl.uniprot.org/uniprot/Q99MK8 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ AGC-kinase C-terminal|||Beta-adrenergic receptor kinase 1|||N-terminal|||PH|||Phosphoserine|||Protein kinase|||Proton acceptor|||RGS|||Required for receptor phosphorylation ^@ http://purl.uniprot.org/annotation/PRO_0000085629 http://togogenome.org/gene/10090:Dpf3 ^@ http://purl.uniprot.org/uniprot/B5TZD5|||http://purl.uniprot.org/uniprot/P58269 ^@ 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 ^@ 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 4.|||In isoform 3.|||In isoform 4.|||Interaction with HDGFL2|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Zinc finger protein DPF3 ^@ http://purl.uniprot.org/annotation/PRO_0000168155|||http://purl.uniprot.org/annotation/VSP_035885|||http://purl.uniprot.org/annotation/VSP_035886|||http://purl.uniprot.org/annotation/VSP_035887 http://togogenome.org/gene/10090:Scgb1b19 ^@ http://purl.uniprot.org/uniprot/F6WYW0 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015091124 http://togogenome.org/gene/10090:Zfp248 ^@ http://purl.uniprot.org/uniprot/Q640N4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:H2ac1 ^@ http://purl.uniprot.org/uniprot/Q8CGP4 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Histone H2A C-terminal|||Histone H2A/H2B/H3 ^@ http://togogenome.org/gene/10090:Gsta4 ^@ http://purl.uniprot.org/uniprot/P24472 ^@ 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 ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase A4|||N-acetylmethionine|||Requires 2 nucleotide substitutions. ^@ http://purl.uniprot.org/annotation/PRO_0000185791 http://togogenome.org/gene/10090:Cyfip2 ^@ http://purl.uniprot.org/uniprot/Q5SQX6|||http://purl.uniprot.org/uniprot/Q6PGK0 ^@ 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 ^@ CYRIA/CYRIB Rac1 binding|||Cytoplasmic FMR1-interacting protein 2|||In RNA edited version.|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000279710 http://togogenome.org/gene/10090:Nubp2 ^@ http://purl.uniprot.org/uniprot/Q9R061 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Cytosolic Fe-S cluster assembly factor NUBP2|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000184946 http://togogenome.org/gene/10090:Ing3 ^@ http://purl.uniprot.org/uniprot/D3YUP8|||http://purl.uniprot.org/uniprot/Q8VEK6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone H3K4me3 binding|||Inhibitor of growth protein 3|||N6-acetyllysine|||PHD-type ^@ http://purl.uniprot.org/annotation/PRO_0000212666 http://togogenome.org/gene/10090:Npas2 ^@ http://purl.uniprot.org/uniprot/G3X9B7|||http://purl.uniprot.org/uniprot/P97460|||http://purl.uniprot.org/uniprot/Q32ME6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region ^@ BHLH|||Basic and acidic residues|||Disordered|||Neuronal PAS domain-containing protein 2|||PAC|||PAS|||PAS 1|||PAS 2|||Polar residues|||Significant decrease in DNA binding affinity resulting in a loss of the transcriptional activity.|||Sufficient for heterodimer formation with BMAL1, E-box binding and for the effect of NADPH|||axial binding residue|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127407 http://togogenome.org/gene/10090:Iah1 ^@ http://purl.uniprot.org/uniprot/Q9DB29 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Chain|||Modified Residue|||Site ^@ Isoamyl acetate-hydrolyzing esterase 1 homolog|||N6-succinyllysine|||Nucleophile|||Proton acceptor|||Proton donor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000315724 http://togogenome.org/gene/10090:Aars ^@ http://purl.uniprot.org/uniprot/Q3UD67|||http://purl.uniprot.org/uniprot/Q8BGQ7 ^@ 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 ^@ Alanine--tRNA ligase, cytoplasmic|||Alanyl-transfer RNA synthetases family profile|||Decreases misincorporation of Cys instead of Ala.|||Homozygous embryos die at midgestation. Defects are caused by a dramatic increase in production of Ser-mischarged tRNA(Ala).|||In sti; homozygous mice display an unkempt sticky appearance of fur and show cerebellar Purkinje cell loss and ataxia; defects are caused by impaired ability to edit incorrectly charged tRNA, resulting in formation of ubiquitinated protein aggregates in cerebellar Purkinje cells and degeneration of these neurons.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000075282 http://togogenome.org/gene/10090:Ccnyl1 ^@ http://purl.uniprot.org/uniprot/E9Q226 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Cyclin-like ^@ http://togogenome.org/gene/10090:Tmem243 ^@ http://purl.uniprot.org/uniprot/B2RVB9 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Psmd9 ^@ http://purl.uniprot.org/uniprot/Q9CR00 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ 26S proteasome non-ATPase regulatory subunit 9|||PDZ|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000173853 http://togogenome.org/gene/10090:F2rl2 ^@ http://purl.uniprot.org/uniprot/O08675 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||Proteinase-activated receptor 3|||Removed for receptor activation ^@ http://purl.uniprot.org/annotation/PRO_0000012758|||http://purl.uniprot.org/annotation/PRO_0000012759 http://togogenome.org/gene/10090:Sgce ^@ http://purl.uniprot.org/uniprot/E9PX46|||http://purl.uniprot.org/uniprot/F6R6P2|||http://purl.uniprot.org/uniprot/F8WGM3|||http://purl.uniprot.org/uniprot/O70258|||http://purl.uniprot.org/uniprot/Q4H437|||http://purl.uniprot.org/uniprot/Q4H438|||http://purl.uniprot.org/uniprot/Q6L8N9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dystroglycan-type cadherin-like|||Epsilon-sarcoglycan|||Extracellular|||Helical|||In isoform 2.|||Misfolded, leading to the interaction with TOR1A, ubiquitination and a decrease of the half-life. Impairs intracellular transport. No effect on glycosylation.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000031678|||http://purl.uniprot.org/annotation/PRO_5004238817|||http://purl.uniprot.org/annotation/PRO_5004239253|||http://purl.uniprot.org/annotation/PRO_5004275824|||http://purl.uniprot.org/annotation/VSP_006019 http://togogenome.org/gene/10090:Bfsp1 ^@ http://purl.uniprot.org/uniprot/A2AMT1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ 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 isoform 2.|||Interaction with MIP|||Linker 1|||Linker 12|||N-acetylalanine|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000285854|||http://purl.uniprot.org/annotation/PRO_0000448672|||http://purl.uniprot.org/annotation/PRO_0000448673|||http://purl.uniprot.org/annotation/VSP_024920 http://togogenome.org/gene/10090:Lmx1a ^@ http://purl.uniprot.org/uniprot/Q543W2|||http://purl.uniprot.org/uniprot/Q9JKU8 ^@ 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 homeobox transcription factor 1-alpha|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000075827 http://togogenome.org/gene/10090:Gm12250 ^@ http://purl.uniprot.org/uniprot/Q0GUM3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Transmembrane ^@ Abolished GTPase activity, promoting localization to lipid droplets.|||Abolished localization to pathogen-containing vacuoles.|||Does not affect formation of a head-to-head homodimer in presence of GDP.|||Helical|||IRG-type G|||Impaired formation of a head-to-head homodimer in presence of GDP.|||Interferon-gamma-inducible GTPase 10|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000457891 http://togogenome.org/gene/10090:Vmn2r42 ^@ http://purl.uniprot.org/uniprot/D3Z1K8|||http://purl.uniprot.org/uniprot/O35192 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003052572|||http://purl.uniprot.org/annotation/PRO_5015096769 http://togogenome.org/gene/10090:Usp30 ^@ http://purl.uniprot.org/uniprot/Q3UN04 ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Does not affect binding to diterpenoid derivative 15-oxospiramilactone (S3) inhibitor.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Loss of deubiquitinase activity and binding to diterpenoid derivative 15-oxospiramilactone (S3) inhibitor.|||Mitochondrial intermembrane|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 30 ^@ http://purl.uniprot.org/annotation/PRO_0000377537 http://togogenome.org/gene/10090:Cacna1e ^@ http://purl.uniprot.org/uniprot/A0A087WS83 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site|||Transmembrane ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||EF-hand|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:4921524J17Rik ^@ http://purl.uniprot.org/uniprot/Q9CR55 ^@ 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|||Basic residues|||Disordered|||Phosphoserine|||UPF0547 protein C16orf87 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000326522 http://togogenome.org/gene/10090:Taf3 ^@ http://purl.uniprot.org/uniprot/A2ASY1|||http://purl.uniprot.org/uniprot/Q5HZG4 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Transcription initiation factor TFIID subunit 3 ^@ http://purl.uniprot.org/annotation/PRO_0000245529|||http://purl.uniprot.org/annotation/VSP_019736|||http://purl.uniprot.org/annotation/VSP_019737 http://togogenome.org/gene/10090:Vmn2r81 ^@ http://purl.uniprot.org/uniprot/Q80Z09 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015098928 http://togogenome.org/gene/10090:Mroh2b ^@ http://purl.uniprot.org/uniprot/Q7M6Y6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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.|||Maestro heat-like repeat-containing protein family member 2B ^@ http://purl.uniprot.org/annotation/PRO_0000395105|||http://purl.uniprot.org/annotation/VSP_058721|||http://purl.uniprot.org/annotation/VSP_058722 http://togogenome.org/gene/10090:4930595M18Rik ^@ http://purl.uniprot.org/uniprot/A2RRY9|||http://purl.uniprot.org/uniprot/Q8CDN0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||RING-type|||RRM ^@ http://togogenome.org/gene/10090:Gp1bb ^@ http://purl.uniprot.org/uniprot/B2RR03|||http://purl.uniprot.org/uniprot/P56400 ^@ 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|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Interchain (with C-608 or C-609 in GP1BA)|||LRR|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Platelet glycoprotein Ib beta chain ^@ http://purl.uniprot.org/annotation/PRO_0000021346|||http://purl.uniprot.org/annotation/PRO_5015087151 http://togogenome.org/gene/10090:Spock3 ^@ http://purl.uniprot.org/uniprot/Q571A9|||http://purl.uniprot.org/uniprot/Q8BKV0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant ^@ Acidic residues|||Disordered|||In isoform 2.|||Kazal-like|||O-linked (Xyl...) (glycosaminoglycan) serine|||Testican-3|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000026704|||http://purl.uniprot.org/annotation/VSP_013633 http://togogenome.org/gene/10090:Ppp1r9a ^@ http://purl.uniprot.org/uniprot/H3BJD6|||http://purl.uniprot.org/uniprot/Q7TN74 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||PDZ|||Polar residues|||SAM ^@ http://togogenome.org/gene/10090:Lipm ^@ http://purl.uniprot.org/uniprot/Q8K2A6 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ AB hydrolase-1|||Charge relay system|||Lipase member M|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000286830 http://togogenome.org/gene/10090:Or6c209 ^@ http://purl.uniprot.org/uniprot/Q8VGI7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp931 ^@ http://purl.uniprot.org/uniprot/A2AHM2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dnah7a ^@ http://purl.uniprot.org/uniprot/E9Q0T8 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disordered|||EF-hand ^@ http://togogenome.org/gene/10090:Galnt12 ^@ http://purl.uniprot.org/uniprot/Q60GT3|||http://purl.uniprot.org/uniprot/Q8BGT9 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Region|||Topological Domain|||Transmembrane ^@ Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Polypeptide N-acetylgalactosaminyltransferase 12|||Ricin B lectin|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059129 http://togogenome.org/gene/10090:Esp34 ^@ http://purl.uniprot.org/uniprot/A8R0W6 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015086681 http://togogenome.org/gene/10090:Mettl23 ^@ http://purl.uniprot.org/uniprot/A2AA28 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Histone-arginine methyltransferase METTL23 ^@ http://purl.uniprot.org/annotation/PRO_0000321521 http://togogenome.org/gene/10090:Map2k1 ^@ http://purl.uniprot.org/uniprot/P31938|||http://purl.uniprot.org/uniprot/Q3TMJ8 ^@ 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|||Region|||Sequence Conflict|||Site ^@ Cleavage; by anthrax lethal factor|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 1|||Impairs interaction with MAP2K2/MEK2.|||Phosphoserine; by PAK|||Phosphoserine; by RAF|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Protein kinase|||Proton acceptor|||RAF1-binding|||Results in hyperphosphorylation of the RAF-dependent sites and prolonged ERK phosphorylation.|||Results in hypophosphorylation of the RAF-dependent sites and faster ERK inactivation. ^@ http://purl.uniprot.org/annotation/PRO_0000086366 http://togogenome.org/gene/10090:Calcoco2 ^@ http://purl.uniprot.org/uniprot/A2A6M5 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Motif|||Region|||Splice Variant ^@ CLIR|||Calcium-binding and coiled-coil domain-containing protein 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with LGALS8|||LIR-like ^@ http://purl.uniprot.org/annotation/PRO_0000312339|||http://purl.uniprot.org/annotation/VSP_029830|||http://purl.uniprot.org/annotation/VSP_029831|||http://purl.uniprot.org/annotation/VSP_029832|||http://purl.uniprot.org/annotation/VSP_029833 http://togogenome.org/gene/10090:Pink1 ^@ http://purl.uniprot.org/uniprot/Q99MQ3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Abolishes ubiquitin phosphorylation; when associated with A-218 and A-361.|||Abolishes ubiquitin phosphorylation; when associated with A-218 and A-383.|||Abolishes ubiquitin phosphorylation; when associated with A-361 and A-383.|||Cytoplasmic|||Helical|||Mitochondrial intermembrane|||Mitochondrion|||Phosphoserine; by autocatalysis|||Protein kinase|||Proton acceptor|||Required for outer membrane localization|||Serine/threonine-protein kinase PINK1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000024370 http://togogenome.org/gene/10090:Or4a27 ^@ http://purl.uniprot.org/uniprot/Q7TR13 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Glp2r ^@ http://purl.uniprot.org/uniprot/A0A158RFU9|||http://purl.uniprot.org/uniprot/Q5IXF8 ^@ 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|||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_0000307111|||http://purl.uniprot.org/annotation/PRO_5007631767 http://togogenome.org/gene/10090:Kcnh2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1K0|||http://purl.uniprot.org/uniprot/O35219|||http://purl.uniprot.org/uniprot/Q53Z09 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||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|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||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.|||In strain: BALB/c.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||PAC|||PAS|||Phosphoserine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 2|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054000|||http://purl.uniprot.org/annotation/VSP_000969|||http://purl.uniprot.org/annotation/VSP_000970 http://togogenome.org/gene/10090:Atf5 ^@ http://purl.uniprot.org/uniprot/O70191|||http://purl.uniprot.org/uniprot/Q3UJF3 ^@ 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 ^@ BZIP|||Basic and acidic residues|||Basic motif|||Cyclic AMP-dependent transcription factor ATF-5|||Decreases acetylation levels and interaction with CEBPB.|||Disordered|||Enhances interaction with CEBPB.|||Interaction with PTP4A1|||Leucine-zipper|||N6-acetyllysine; by EP300|||Phosphoserine|||Pro residues|||Required for protein stabilization induced by IL1B|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076587 http://togogenome.org/gene/10090:Fam193a ^@ http://purl.uniprot.org/uniprot/Q8CGI1 ^@ 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|||Phosphoserine|||Polar residues|||Protein FAM193A ^@ http://purl.uniprot.org/annotation/PRO_0000089431 http://togogenome.org/gene/10090:Eif3b ^@ http://purl.uniprot.org/uniprot/Q8JZQ9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Disordered|||Eukaryotic translation initiation factor 3 subunit B|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||Sufficient for interaction with EIF3E|||Sufficient for interaction with EIF3J|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000223479 http://togogenome.org/gene/10090:Vmn2r45 ^@ http://purl.uniprot.org/uniprot/L7N2B5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982289 http://togogenome.org/gene/10090:B3galt4 ^@ http://purl.uniprot.org/uniprot/Q9Z0F0 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Beta-1,3-galactosyltransferase 4|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In strain: BLG2/Msf.|||In strain: pgn2.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219161 http://togogenome.org/gene/10090:Plac1 ^@ http://purl.uniprot.org/uniprot/Q9JI83 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Sequence Conflict|||Signal Peptide ^@ Placenta-specific protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000251145 http://togogenome.org/gene/10090:Oas1g ^@ http://purl.uniprot.org/uniprot/Q8K469 ^@ Domain Extent|||Region ^@ Domain Extent ^@ 2'-5'-oligoadenylate synthetase 1|||Polymerase nucleotidyl transferase ^@ http://togogenome.org/gene/10090:Treml2 ^@ http://purl.uniprot.org/uniprot/Q2LA85 ^@ 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|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Trem-like transcript 2 protein ^@ http://purl.uniprot.org/annotation/PRO_0000253858 http://togogenome.org/gene/10090:Myo5a ^@ http://purl.uniprot.org/uniprot/D3YZ62|||http://purl.uniprot.org/uniprot/D3Z4J3|||http://purl.uniprot.org/uniprot/Q99104 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||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|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Actin-binding|||Dilute|||Disordered|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||IQ 6|||Myosin N-terminal SH3-like|||Myosin motor|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Slightly reduces affinity for MLPH.|||Strongly reduces affinity for MLPH and SYTL4.|||Unconventional myosin-Va ^@ http://purl.uniprot.org/annotation/PRO_0000123457 http://togogenome.org/gene/10090:Pamr1 ^@ http://purl.uniprot.org/uniprot/Q8BU25 ^@ 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 ^@ CUB|||EGF-like|||Inactive serine protease PAMR1|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi 1|||Sushi 2 ^@ http://purl.uniprot.org/annotation/PRO_0000287603 http://togogenome.org/gene/10090:Clec2g ^@ http://purl.uniprot.org/uniprot/A0A0N4SUR3|||http://purl.uniprot.org/uniprot/F5CSM6|||http://purl.uniprot.org/uniprot/F5CSM7|||http://purl.uniprot.org/uniprot/Q9D676 ^@ 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 ^@ C-type lectin|||C-type lectin domain family 2 member G|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000315289|||http://purl.uniprot.org/annotation/VSP_030529 http://togogenome.org/gene/10090:Or51a43 ^@ http://purl.uniprot.org/uniprot/Q8VH21 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:7420426K07Rik ^@ http://purl.uniprot.org/uniprot/Q3UX66 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:H60b ^@ http://purl.uniprot.org/uniprot/B1B212 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Histocompatibility antigen 60b|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_5006716408 http://togogenome.org/gene/10090:Zfp94 ^@ http://purl.uniprot.org/uniprot/E9Q6Y4|||http://purl.uniprot.org/uniprot/Q3UUP5|||http://purl.uniprot.org/uniprot/Q61117 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Egfl6 ^@ http://purl.uniprot.org/uniprot/Q9JJZ5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide ^@ 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|||Loss of adhesive activity.|||MAM|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000295812 http://togogenome.org/gene/10090:Maml3 ^@ http://purl.uniprot.org/uniprot/D4QGC2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Neurogenic mastermind-like N-terminal|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Gm21704 ^@ http://purl.uniprot.org/uniprot/O35698 ^@ 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|||RNA-binding motif protein, Y chromosome, family 1 member A1|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000341540 http://togogenome.org/gene/10090:Rp2 ^@ http://purl.uniprot.org/uniprot/Q9EPK2 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Splice Variant ^@ C-CAP/cofactor C-like|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-myristoyl glycine|||Protein XRP2|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000235804|||http://purl.uniprot.org/annotation/VSP_018481|||http://purl.uniprot.org/annotation/VSP_018482|||http://purl.uniprot.org/annotation/VSP_018483|||http://purl.uniprot.org/annotation/VSP_018484 http://togogenome.org/gene/10090:Trappc2l ^@ http://purl.uniprot.org/uniprot/Q9JME7 ^@ Chain|||Molecule Processing ^@ Chain ^@ Trafficking protein particle complex subunit 2-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000294452 http://togogenome.org/gene/10090:Or4d10 ^@ http://purl.uniprot.org/uniprot/Q7TQS1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Itpkc ^@ http://purl.uniprot.org/uniprot/Q7TS72 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Calmodulin-binding|||Disordered|||Inositol-trisphosphate 3-kinase C|||Nuclear export signal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000234071 http://togogenome.org/gene/10090:Kcnj10 ^@ http://purl.uniprot.org/uniprot/Q56VN0|||http://purl.uniprot.org/uniprot/Q8C7Z5|||http://purl.uniprot.org/uniprot/Q9JM63 ^@ Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Motif|||Site|||Topological Domain|||Transmembrane ^@ ATP-sensitive inward rectifier potassium channel 10|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Inward rectifier potassium channel C-terminal|||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_0000154954 http://togogenome.org/gene/10090:Myo15a ^@ http://purl.uniprot.org/uniprot/Q9QZZ4 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn ^@ Actin-binding|||Basic and acidic residues|||Disordered|||FERM|||IQ 1|||IQ 2|||In isoform 2 and isoform 3.|||In isoform 3.|||In sh-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_0000123475|||http://purl.uniprot.org/annotation/VSP_029944|||http://purl.uniprot.org/annotation/VSP_029945 http://togogenome.org/gene/10090:Uty ^@ http://purl.uniprot.org/uniprot/E9PWW8|||http://purl.uniprot.org/uniprot/Q3UQE8|||http://purl.uniprot.org/uniprot/Q8C926 ^@ Domain Extent|||Region|||Repeat|||Transmembrane ^@ Domain Extent|||Region|||Repeat|||Transmembrane ^@ Disordered|||Helical|||JmjC|||TPR ^@ http://togogenome.org/gene/10090:Cbr2 ^@ http://purl.uniprot.org/uniprot/P08074 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Strand ^@ Carbonyl reductase [NADPH] 2|||Converts the coenzyme specificity from NADP to NAD.|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054547 http://togogenome.org/gene/10090:Slc16a14 ^@ http://purl.uniprot.org/uniprot/Q8K1C7 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Monocarboxylate transporter 14 ^@ http://purl.uniprot.org/annotation/PRO_0000288924 http://togogenome.org/gene/10090:Fmnl1 ^@ http://purl.uniprot.org/uniprot/A2AB60|||http://purl.uniprot.org/uniprot/Q3TY82|||http://purl.uniprot.org/uniprot/Q9JL26 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||DAD|||Disordered|||FH2|||Formin-like protein 1|||GBD/FH3|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194891|||http://purl.uniprot.org/annotation/VSP_013978|||http://purl.uniprot.org/annotation/VSP_013979|||http://purl.uniprot.org/annotation/VSP_013980 http://togogenome.org/gene/10090:Mrpl35 ^@ http://purl.uniprot.org/uniprot/Q9CQL6 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Large ribosomal subunit protein bL35m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000030526 http://togogenome.org/gene/10090:Rsl24d1 ^@ http://purl.uniprot.org/uniprot/Q5EBK7|||http://purl.uniprot.org/uniprot/Q99L28 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Probable ribosome biogenesis protein RLP24|||TRASH ^@ http://purl.uniprot.org/annotation/PRO_0000136897 http://togogenome.org/gene/10090:Gpr155 ^@ http://purl.uniprot.org/uniprot/A2AWR3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||DEP|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Lysosomal cholesterol signaling protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000458850|||http://purl.uniprot.org/annotation/VSP_061976|||http://purl.uniprot.org/annotation/VSP_061977|||http://purl.uniprot.org/annotation/VSP_061978|||http://purl.uniprot.org/annotation/VSP_061979|||http://purl.uniprot.org/annotation/VSP_061980|||http://purl.uniprot.org/annotation/VSP_061981|||http://purl.uniprot.org/annotation/VSP_061982 http://togogenome.org/gene/10090:Rrbp1 ^@ http://purl.uniprot.org/uniprot/A2AVJ7|||http://purl.uniprot.org/uniprot/Q8CAB9|||http://purl.uniprot.org/uniprot/Q99PL5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||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|||6|||60|||61|||61 X 10 AA tandem repeats of [NSQ]-[NKQVGA]-[GSAQKRT]-[ASGDTK]-[KGTQSAV]-[KGAED]-[EQVGIPTDMA]-[EGVAS]-[AGVPETNS]-[AQNGPTVS]|||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 RRp0.|||In isoform RRp1.8.|||In isoform RRp10.|||In isoform RRp15a.|||In isoform RRp15b.|||In isoform RRp16.8.|||In isoform RRp2.|||In isoform RRp41.|||In isoform RRp47.|||In isoform RRp5.4.|||In isoform RRp61, isoform RRp1.8, isoform RRp0, isoform RRp2, isoform RRp16.8, isoform RRp15b, isoform RRp10, isoform RRp5.4, isoform RRp15a, isoform RRp47 and isoform RRp41.|||Lumenal|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Ribosome receptor lysine/proline rich|||Ribosome-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000097442|||http://purl.uniprot.org/annotation/VSP_003951|||http://purl.uniprot.org/annotation/VSP_003952|||http://purl.uniprot.org/annotation/VSP_003953|||http://purl.uniprot.org/annotation/VSP_003954|||http://purl.uniprot.org/annotation/VSP_003955|||http://purl.uniprot.org/annotation/VSP_003956|||http://purl.uniprot.org/annotation/VSP_003957|||http://purl.uniprot.org/annotation/VSP_003958|||http://purl.uniprot.org/annotation/VSP_003959|||http://purl.uniprot.org/annotation/VSP_003961|||http://purl.uniprot.org/annotation/VSP_003962|||http://purl.uniprot.org/annotation/VSP_003963|||http://purl.uniprot.org/annotation/VSP_003964 http://togogenome.org/gene/10090:Ebf3 ^@ http://purl.uniprot.org/uniprot/O08791|||http://purl.uniprot.org/uniprot/Q5DTH8|||http://purl.uniprot.org/uniprot/Q6NXL3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Zinc Finger ^@ C5-type|||Disordered|||IPT/TIG|||In isoform Short.|||Interaction with DNA|||Transcription factor COE3 ^@ http://purl.uniprot.org/annotation/PRO_0000107833|||http://purl.uniprot.org/annotation/VSP_001115|||http://purl.uniprot.org/annotation/VSP_001116 http://togogenome.org/gene/10090:Sdr16c5 ^@ http://purl.uniprot.org/uniprot/Q7TQA3 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Transmembrane ^@ Epidermal retinol dehydrogenase 2|||Helical|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000305974 http://togogenome.org/gene/10090:Mex3a ^@ http://purl.uniprot.org/uniprot/G3UYU0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Pro residues|||RING-type ^@ http://togogenome.org/gene/10090:Or1e23 ^@ http://purl.uniprot.org/uniprot/Q8VF79 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or6k2 ^@ http://purl.uniprot.org/uniprot/A6H6I2|||http://purl.uniprot.org/uniprot/E9Q4G0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ston2 ^@ http://purl.uniprot.org/uniprot/Q8BZ60 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Disordered|||MHD|||NPF 1|||NPF 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||SHD|||Stonin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000185733 http://togogenome.org/gene/10090:Prpmp5 ^@ http://purl.uniprot.org/uniprot/E9PXN1 ^@ 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_5003244303 http://togogenome.org/gene/10090:Rhobtb1 ^@ http://purl.uniprot.org/uniprot/B7ZMU4|||http://purl.uniprot.org/uniprot/Q9DAK3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ BTB|||BTB 1|||BTB 2|||Disordered|||Rho-like|||Rho-related BTB domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000198961 http://togogenome.org/gene/10090:Tuba1a ^@ http://purl.uniprot.org/uniprot/P68369 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ 3'-nitrotyrosine|||5-glutamyl polyglutamate|||Detyrosinated tubulin alpha-1A chain|||Disordered|||Involved in polymerization|||N6-acetyllysine|||Phosphoserine|||Tubulin alpha-1A chain ^@ http://purl.uniprot.org/annotation/PRO_0000048120|||http://purl.uniprot.org/annotation/PRO_0000437379 http://togogenome.org/gene/10090:Xaf1 ^@ http://purl.uniprot.org/uniprot/Q5NBU8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||TRAF-type|||XIAP-associated factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000329029|||http://purl.uniprot.org/annotation/VSP_039715 http://togogenome.org/gene/10090:Nfu1 ^@ http://purl.uniprot.org/uniprot/A0A0N4SUH8|||http://purl.uniprot.org/uniprot/Q9QZ23 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Transit Peptide ^@ Mitochondrion|||NFU1 iron-sulfur cluster scaffold homolog, mitochondrial|||NifU|||Scaffold protein Nfu/NifU N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000166192 http://togogenome.org/gene/10090:Or8k3 ^@ http://purl.uniprot.org/uniprot/Q8VGS0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:C2cd2 ^@ http://purl.uniprot.org/uniprot/E9Q3C1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ C2|||C2 domain-containing protein 2|||Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||SMP-LBD ^@ http://purl.uniprot.org/annotation/PRO_0000439647 http://togogenome.org/gene/10090:Fam53b ^@ http://purl.uniprot.org/uniprot/Q8BGR5 ^@ 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 ^@ Disordered|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein FAM53B ^@ http://purl.uniprot.org/annotation/PRO_0000189545|||http://purl.uniprot.org/annotation/VSP_009934 http://togogenome.org/gene/10090:Phlda1 ^@ http://purl.uniprot.org/uniprot/Q62392 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ 11 X 2 AA repeats of P-H|||16 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_0000053898 http://togogenome.org/gene/10090:Ccdc202 ^@ http://purl.uniprot.org/uniprot/Q9CQ47 ^@ Coiled-Coil|||Region ^@ Coiled-Coil|||Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Nkd2 ^@ http://purl.uniprot.org/uniprot/Q8VE28 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Splice Variant ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000301994|||http://purl.uniprot.org/annotation/VSP_027902 http://togogenome.org/gene/10090:Hsd3b7 ^@ http://purl.uniprot.org/uniprot/Q9EQC1 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Transmembrane ^@ 3 beta-hydroxysteroid dehydrogenase type 7|||Helical|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000087792 http://togogenome.org/gene/10090:Paip2 ^@ http://purl.uniprot.org/uniprot/Q9D6V8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ 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_0000058180 http://togogenome.org/gene/10090:ND4 ^@ http://purl.uniprot.org/uniprot/P03911|||http://purl.uniprot.org/uniprot/Q7JCY6 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Helix|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Helical|||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_0000117957|||http://purl.uniprot.org/annotation/PRO_5010143427 http://togogenome.org/gene/10090:Tax1bp1 ^@ http://purl.uniprot.org/uniprot/Q3UKC1 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Oligomerization|||Phosphoserine|||Phosphoserine; by IKKA|||Tax1-binding protein 1 homolog|||UBZ1-type 1|||UBZ1-type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000234555 http://togogenome.org/gene/10090:Krt13 ^@ http://purl.uniprot.org/uniprot/P08730 ^@ 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 ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In isoform 2.|||Keratin, type I cytoskeletal 13|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Polar residues|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063648|||http://purl.uniprot.org/annotation/VSP_016378 http://togogenome.org/gene/10090:Mypop ^@ http://purl.uniprot.org/uniprot/Q8R4U1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Splice Variant ^@ Basic residues|||Disordered|||In isoform 2.|||Myb-like|||Myb-related transcription factor, partner of profilin|||Nuclear localization signal|||Polar residues|||Pro residues|||Reduction in homodimerization.|||Reduction in homodimerization. Abolishes homodimerization; when associated with A-281.|||Reduction in homodimerization. Abolishes homodimerization; when associated with P-281. ^@ http://purl.uniprot.org/annotation/PRO_0000344800|||http://purl.uniprot.org/annotation/VSP_034858|||http://purl.uniprot.org/annotation/VSP_034859 http://togogenome.org/gene/10090:Coq8a ^@ http://purl.uniprot.org/uniprot/Q60936 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide|||Transmembrane ^@ AAAS motif|||Atypical kinase COQ8A, mitochondrial|||Disordered|||Helical|||In isoform 2.|||KxGQ motif|||Mitochondrion|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000000263|||http://purl.uniprot.org/annotation/VSP_022354 http://togogenome.org/gene/10090:Sod2 ^@ http://purl.uniprot.org/uniprot/P09671|||http://purl.uniprot.org/uniprot/Q4FJX9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Transit Peptide ^@ 3'-nitrotyrosine|||Manganese/iron superoxide dismutase C-terminal|||Manganese/iron superoxide dismutase N-terminal|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Reverses IR-Induced increases in superoxide and genomic Instability in SIRT3-deficient mice.|||Superoxide dismutase [Mn], mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000032871 http://togogenome.org/gene/10090:Atp6v1e1 ^@ http://purl.uniprot.org/uniprot/P50518 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ N-acetylalanine|||Phosphotyrosine|||Removed|||V-type proton ATPase subunit E 1 ^@ http://purl.uniprot.org/annotation/PRO_0000117296 http://togogenome.org/gene/10090:Acp1 ^@ http://purl.uniprot.org/uniprot/Q4VAI2|||http://purl.uniprot.org/uniprot/Q561M1|||http://purl.uniprot.org/uniprot/Q9D358 ^@ Active 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|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn ^@ In isoform 2.|||Low molecular weight phosphotyrosine protein phosphatase|||N-acetylalanine|||Nucleophile|||Phosphotyrosine|||Phosphotyrosine protein phosphatase I|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000046559|||http://purl.uniprot.org/annotation/VSP_050726 http://togogenome.org/gene/10090:Arhgap19 ^@ http://purl.uniprot.org/uniprot/E9Q4T1|||http://purl.uniprot.org/uniprot/Q8BRH3 ^@ 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|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||Rho GTPase-activating protein 19|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000280466|||http://purl.uniprot.org/annotation/VSP_023702 http://togogenome.org/gene/10090:Gdap1l1 ^@ http://purl.uniprot.org/uniprot/Q3USC7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ GST C-terminal|||GST N-terminal|||Helical ^@ http://togogenome.org/gene/10090:Mrpl36 ^@ http://purl.uniprot.org/uniprot/Q99N90 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Large ribosomal subunit protein bL36m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000030530 http://togogenome.org/gene/10090:H2bc22 ^@ http://purl.uniprot.org/uniprot/Q8CGP2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice 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-P|||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-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_0000244834|||http://purl.uniprot.org/annotation/VSP_019618 http://togogenome.org/gene/10090:Scap ^@ http://purl.uniprot.org/uniprot/Q6GQT6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||ER export signal|||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|||Helical; Name=8|||Higher level of processed SREBF1 and SREBF2 when expressed in liver.|||Interaction with SREBF2|||Loop-1|||Loop-7|||Loss of ubiquitination; when associated with R-454.|||Loss of ubiquitination; when associated with R-466.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||SSD|||Sterol regulatory element-binding protein cleavage-activating protein|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000315870 http://togogenome.org/gene/10090:Pnpo ^@ http://purl.uniprot.org/uniprot/Q91XF0 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Phosphoserine|||Phosphothreonine|||Pyridoxine-5'-phosphate oxidase ^@ http://purl.uniprot.org/annotation/PRO_0000167784 http://togogenome.org/gene/10090:Gdf6 ^@ http://purl.uniprot.org/uniprot/A2AII0|||http://purl.uniprot.org/uniprot/P43028 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide ^@ Basic and acidic residues|||Basic residues|||Disordered|||Growth/differentiation factor 6|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033919|||http://purl.uniprot.org/annotation/PRO_0000342207|||http://purl.uniprot.org/annotation/PRO_5014296795 http://togogenome.org/gene/10090:Prl7b1 ^@ http://purl.uniprot.org/uniprot/A0A0M6L0K6|||http://purl.uniprot.org/uniprot/Q8CGZ9 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prolactin-7B1 ^@ http://purl.uniprot.org/annotation/PRO_0000045149|||http://purl.uniprot.org/annotation/PRO_5005806179 http://togogenome.org/gene/10090:Cyb561 ^@ http://purl.uniprot.org/uniprot/Q60720|||http://purl.uniprot.org/uniprot/V9GX11 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytochrome b561|||Cytoplasmic|||Decreased protein abundance.|||Helical|||N-acetylmethionine|||No effect on protein abundance.|||No effect on protein abundance. Decreased reduction by ascorbate.|||No effect on protein abundance. Decreased reduction by ascorbate; when associated with A-159.|||No effect on protein abundance. Decreased reduction by ascorbate; when associated with A-86.|||Phosphoserine|||Transmembrane ascorbate-dependent reductase CYB561|||Vesicular|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000151028 http://togogenome.org/gene/10090:Reep6 ^@ http://purl.uniprot.org/uniprot/Q9JM62 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Receptor expression-enhancing protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000101819|||http://purl.uniprot.org/annotation/VSP_016631|||http://purl.uniprot.org/annotation/VSP_016632 http://togogenome.org/gene/10090:Ndufb6 ^@ http://purl.uniprot.org/uniprot/A2AP31|||http://purl.uniprot.org/uniprot/Q3UIU2 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Transmembrane|||Turn ^@ Helical|||N-acetylserine|||N6-acetyllysine|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000233980 http://togogenome.org/gene/10090:Arl13b ^@ http://purl.uniprot.org/uniprot/Q640N2|||http://purl.uniprot.org/uniprot/Q9CUD0 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ ADP-ribosylation factor-like protein 13B|||Abolishes localization to cilium.|||Abolishes palmitoylation and localization to the cilium membrane.|||Basic and acidic residues|||Disordered|||Phosphoserine|||Pro residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000251138 http://togogenome.org/gene/10090:Ccdc69 ^@ http://purl.uniprot.org/uniprot/Q3TCJ8 ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Splice Variant ^@ Coiled-coil domain-containing protein 69|||Disordered|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000328963|||http://purl.uniprot.org/annotation/VSP_032858 http://togogenome.org/gene/10090:Plod3 ^@ http://purl.uniprot.org/uniprot/Q9R0E1 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Accessory region|||Fe2OG dioxygenase|||Important for dimerization|||Loss of lysyl hydroxylase activity. No effect on glycosyltransferase activity. Mutant mice are born at the expected Mendelian rate and have no visible phenotype, excepting decreased hydroxylysine modifications in type IV collagens in the skin.|||Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3|||N-linked (GlcNAc...) asparagine|||Required for glycosyltransferase activity ^@ http://purl.uniprot.org/annotation/PRO_0000024687 http://togogenome.org/gene/10090:Chsy1 ^@ http://purl.uniprot.org/uniprot/Q6ZQ11 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Chondroitin sulfate synthase 1|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000189559 http://togogenome.org/gene/10090:Hsd3b5 ^@ http://purl.uniprot.org/uniprot/Q61694 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||N6-acetyllysine|||NADPH-dependent 3-keto-steroid reductase Hsd3b5|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000087784 http://togogenome.org/gene/10090:Thoc5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0J6|||http://purl.uniprot.org/uniprot/Q8BKT7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes nuclear localization.|||Basic and acidic residues|||Disordered|||Enhances nuclear localization.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with CSF1R|||Interaction with THOC7|||N-acetylserine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||THO complex subunit 5 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000310555 http://togogenome.org/gene/10090:Dnajc10 ^@ http://purl.uniprot.org/uniprot/Q9CUG0|||http://purl.uniprot.org/uniprot/Q9DC23 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-700.|||Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-703.|||Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-700 and A-703.|||Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-591; A-700 and A-703.|||Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-588; A-591; A-700 and A-703.|||Abolishes disulfide reductase activity; when associated with A-158; A-161; A-483; A-588; A-591; A-700 and A-703.|||Abolishes disulfide reductase activity; when associated with A-158; A-480; A-483; A-588; A-591; A-700 and A-703.|||Abolishes disulfide reductase activity; when associated with A-161; A-480; A-483; A-588; A-591; A-700 and A-703.|||DnaJ homolog subfamily C member 10|||Helical|||J|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Redox-active|||Thioredoxin 1|||Thioredoxin 2|||Thioredoxin 3|||Thioredoxin 4|||Trxb 1|||Trxb 2 ^@ http://purl.uniprot.org/annotation/PRO_0000281484 http://togogenome.org/gene/10090:Bean1 ^@ http://purl.uniprot.org/uniprot/B2RR23|||http://purl.uniprot.org/uniprot/E9PVP2|||http://purl.uniprot.org/uniprot/E9Q314|||http://purl.uniprot.org/uniprot/Q9EQG5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant|||Transmembrane ^@ Basic residues|||Disordered|||Helical|||Impairs binding to NEDD4.|||In isoform 2.|||Polar residues|||Protein BEAN1 ^@ http://purl.uniprot.org/annotation/PRO_0000322541|||http://purl.uniprot.org/annotation/VSP_031912 http://togogenome.org/gene/10090:Tsn ^@ http://purl.uniprot.org/uniprot/Q545E6|||http://purl.uniprot.org/uniprot/Q62348 ^@ Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ DNA/RNA binding|||Leucine-zipper|||N6-acetyllysine|||Phosphoserine|||Translin ^@ http://purl.uniprot.org/annotation/PRO_0000191684 http://togogenome.org/gene/10090:Cer1 ^@ http://purl.uniprot.org/uniprot/A2ADM9|||http://purl.uniprot.org/uniprot/O55233 ^@ 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 ^@ CTCK|||Cerberus|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000006712|||http://purl.uniprot.org/annotation/PRO_5014296784 http://togogenome.org/gene/10090:Rpl35 ^@ http://purl.uniprot.org/uniprot/Q6ZWV7 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Modified Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein uL29|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000320063 http://togogenome.org/gene/10090:Krtap5-5 ^@ http://purl.uniprot.org/uniprot/Q2TA51 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1|||10|||11|||12|||13|||14|||15|||15 X 4 AA repeats of C-C-X-P|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 5-5 ^@ http://purl.uniprot.org/annotation/PRO_0000361661 http://togogenome.org/gene/10090:Klhdc3 ^@ http://purl.uniprot.org/uniprot/Q8VEM9 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant ^@ Chain|||Repeat|||Sequence Conflict|||Sequence Variant ^@ Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000228996 http://togogenome.org/gene/10090:Ap4s1 ^@ http://purl.uniprot.org/uniprot/Q9WVL1 ^@ Chain|||Molecule Processing ^@ Chain ^@ AP-4 complex subunit sigma-1 ^@ http://purl.uniprot.org/annotation/PRO_0000193821 http://togogenome.org/gene/10090:Stat5a ^@ http://purl.uniprot.org/uniprot/B2C3G8|||http://purl.uniprot.org/uniprot/P42230|||http://purl.uniprot.org/uniprot/Q3UZ79|||http://purl.uniprot.org/uniprot/Q9JIA0 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Strand|||Turn ^@ Phosphoserine|||Phosphotyrosine|||SH2|||Signal transducer and activator of transcription 5A ^@ http://purl.uniprot.org/annotation/PRO_0000182424 http://togogenome.org/gene/10090:Slitrk1 ^@ http://purl.uniprot.org/uniprot/B2RXM1|||http://purl.uniprot.org/uniprot/Q69Z70|||http://purl.uniprot.org/uniprot/Q810C1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||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|||LRRCT 1|||LRRCT 2|||LRRNT 1|||LRRNT 2|||Phosphoserine|||SLIT and NTRK-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000032674|||http://purl.uniprot.org/annotation/PRO_5014298319 http://togogenome.org/gene/10090:Top1mt ^@ http://purl.uniprot.org/uniprot/Q8R4U6 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Chain|||Region|||Site|||Transit Peptide ^@ DNA topoisomerase I, mitochondrial|||Interaction with DNA|||Mitochondrion|||O-(3'-phospho-DNA)-tyrosine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000384393 http://togogenome.org/gene/10090:Hrk ^@ http://purl.uniprot.org/uniprot/P62816 ^@ Chain|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Motif|||Transmembrane ^@ Activator of apoptosis harakiri|||BH3|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000143107 http://togogenome.org/gene/10090:Trim35 ^@ http://purl.uniprot.org/uniprot/A0A0R4J031|||http://purl.uniprot.org/uniprot/Q8C006 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||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_0000056251|||http://purl.uniprot.org/annotation/VSP_012062|||http://purl.uniprot.org/annotation/VSP_019230 http://togogenome.org/gene/10090:Hgsnat ^@ http://purl.uniprot.org/uniprot/Q3UDW8|||http://purl.uniprot.org/uniprot/Q9CX36 ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Heparan-alpha-glucosaminide N-acetyltransferase|||In isoform 2.|||Lumenal, vesicle|||Lysosomal targeting region|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000273154|||http://purl.uniprot.org/annotation/VSP_040505 http://togogenome.org/gene/10090:Slc17a5 ^@ http://purl.uniprot.org/uniprot/Q8BN82 ^@ 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|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes sialic acid transporter activity. Does not affect L-aspartate and L-glutamate transporter activity.|||Completely abolishes L-aspartate and L-glutamate transporter activity. Retains appreciable H(+)-coupled sialic acid transporter activity.|||Cytoplasmic|||Dileucine internalization motif|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Sialin ^@ http://purl.uniprot.org/annotation/PRO_0000220948|||http://purl.uniprot.org/annotation/VSP_010484|||http://purl.uniprot.org/annotation/VSP_010485|||http://purl.uniprot.org/annotation/VSP_010486 http://togogenome.org/gene/10090:Pde5a ^@ http://purl.uniprot.org/uniprot/Q8CG03 ^@ 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|||Strand|||Turn ^@ GAF 1|||GAF 2|||PDEase|||Phosphoserine|||Proton donor|||cGMP-specific 3',5'-cyclic phosphodiesterase ^@ http://purl.uniprot.org/annotation/PRO_0000198824 http://togogenome.org/gene/10090:Or2y1b ^@ http://purl.uniprot.org/uniprot/Q60883 ^@ 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 2Y1B ^@ http://purl.uniprot.org/annotation/PRO_0000150809 http://togogenome.org/gene/10090:Wdr13 ^@ http://purl.uniprot.org/uniprot/Q32P16|||http://purl.uniprot.org/uniprot/Q8K412|||http://purl.uniprot.org/uniprot/Q91V09|||http://purl.uniprot.org/uniprot/S4R225 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Region|||Repeat ^@ Asymmetric dimethylarginine; alternate|||Disordered|||Omega-N-methylarginine; alternate|||Phosphoserine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat-containing protein 13 ^@ http://purl.uniprot.org/annotation/PRO_0000051362 http://togogenome.org/gene/10090:Arhgap22 ^@ http://purl.uniprot.org/uniprot/Q8BL80 ^@ 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 and isoform 3.|||In isoform 3.|||Loss of function.|||PH|||Phosphoserine|||Polar residues|||Rho GTPase-activating protein 22|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000280470|||http://purl.uniprot.org/annotation/VSP_023706|||http://purl.uniprot.org/annotation/VSP_023707 http://togogenome.org/gene/10090:Ccdc191 ^@ http://purl.uniprot.org/uniprot/J3QQ27 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Eif4ebp1 ^@ http://purl.uniprot.org/uniprot/Q60876 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 4E-binding protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired interaction with RPTOR.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||TOS motif|||YXXXXLphi motif ^@ http://purl.uniprot.org/annotation/PRO_0000190514 http://togogenome.org/gene/10090:Mfsd12 ^@ http://purl.uniprot.org/uniprot/Q3U481 ^@ 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|||In grizzled (gr), mice show a uniformly gray coat color, rather than the expected agouti coat color.|||Major facilitator superfamily domain-containing protein 12|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000274523 http://togogenome.org/gene/10090:Nemp2 ^@ http://purl.uniprot.org/uniprot/Q8CB65 ^@ 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 2.|||Nuclear envelope integral membrane protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000332239|||http://purl.uniprot.org/annotation/VSP_033359|||http://purl.uniprot.org/annotation/VSP_033360 http://togogenome.org/gene/10090:Col5a3 ^@ http://purl.uniprot.org/uniprot/Q9JLI2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Basic residues|||Disordered|||Fibrillar collagen NC1|||Laminin G|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5015099786 http://togogenome.org/gene/10090:2310022A10Rik ^@ http://purl.uniprot.org/uniprot/G5E8E3|||http://purl.uniprot.org/uniprot/Q8R3Y5 ^@ 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 ^@ DUF5577|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Uncharacterized protein C19orf47 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000291861|||http://purl.uniprot.org/annotation/VSP_026277|||http://purl.uniprot.org/annotation/VSP_026278|||http://purl.uniprot.org/annotation/VSP_026279|||http://purl.uniprot.org/annotation/VSP_026280 http://togogenome.org/gene/10090:1700022I11Rik ^@ http://purl.uniprot.org/uniprot/Q3V0E1 ^@ 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|||Uncharacterized protein C9orf131 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000294444 http://togogenome.org/gene/10090:Dus3l ^@ http://purl.uniprot.org/uniprot/A0A0R4IZY9|||http://purl.uniprot.org/uniprot/Q91XI1 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C3H1-type|||C3H1-type 1|||C3H1-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Proton donor|||tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like ^@ http://purl.uniprot.org/annotation/PRO_0000247343|||http://purl.uniprot.org/annotation/VSP_019973|||http://purl.uniprot.org/annotation/VSP_019974 http://togogenome.org/gene/10090:Zswim2 ^@ http://purl.uniprot.org/uniprot/Q0VB10|||http://purl.uniprot.org/uniprot/Q9D9X6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Zinc Finger ^@ Abrogates ubiquitination activity and the ability to promote DR4- and Fas-induced apoptosis.|||Abrogates ubiquitination activity.|||Disordered|||E3 ubiquitin-protein ligase Zswim2|||RING-type|||RING-type 1|||RING-type 2|||SWIM-type|||UBE2D1-binding|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000223098 http://togogenome.org/gene/10090:Lama2 ^@ http://purl.uniprot.org/uniprot/Q5DTP0|||http://purl.uniprot.org/uniprot/Q60675 ^@ Chain|||Coiled-Coil|||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|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ 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|||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-2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017057 http://togogenome.org/gene/10090:Fgf23 ^@ http://purl.uniprot.org/uniprot/Q3U1V5|||http://purl.uniprot.org/uniprot/Q9EPC2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Fibroblast growth factor|||Fibroblast growth factor 23|||O-linked (GalNAc) threonine|||Phosphoserine; by FAM20C ^@ http://purl.uniprot.org/annotation/PRO_0000008999|||http://purl.uniprot.org/annotation/PRO_5010754662 http://togogenome.org/gene/10090:Morn2 ^@ http://purl.uniprot.org/uniprot/Q6UL01 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ MORN 1|||MORN 2|||MORN repeat-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000247458 http://togogenome.org/gene/10090:Osbpl7 ^@ http://purl.uniprot.org/uniprot/Q3TAX1 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||PH ^@ http://togogenome.org/gene/10090:Hectd4 ^@ http://purl.uniprot.org/uniprot/E9Q2E4|||http://purl.uniprot.org/uniprot/Q6GQX8|||http://purl.uniprot.org/uniprot/Q80W01|||http://purl.uniprot.org/uniprot/Q8BRI0 ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||HECT|||Polar residues ^@ http://togogenome.org/gene/10090:Tesmin ^@ http://purl.uniprot.org/uniprot/Q9WTJ6 ^@ 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 ^@ CRC|||In isoform 2.|||Phosphoserine|||Tesmin ^@ http://purl.uniprot.org/annotation/PRO_0000096627|||http://purl.uniprot.org/annotation/VSP_035300 http://togogenome.org/gene/10090:Ccdc50 ^@ http://purl.uniprot.org/uniprot/A0A668KL36|||http://purl.uniprot.org/uniprot/A6H6M8|||http://purl.uniprot.org/uniprot/Q3TNK7|||http://purl.uniprot.org/uniprot/Q810U5 ^@ 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 ^@ Basic and acidic residues|||Coiled-coil|||Coiled-coil domain-containing protein 50|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000066308|||http://purl.uniprot.org/annotation/VSP_014986|||http://purl.uniprot.org/annotation/VSP_014987 http://togogenome.org/gene/10090:Trim2 ^@ http://purl.uniprot.org/uniprot/E9QKC6|||http://purl.uniprot.org/uniprot/Q3UHH4|||http://purl.uniprot.org/uniprot/Q9ESN6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Zinc Finger ^@ B box-type|||Disordered|||Filamin|||NHL|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||NHL 6|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type|||Tripartite motif-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000056196 http://togogenome.org/gene/10090:Krtap19-3 ^@ http://purl.uniprot.org/uniprot/Q925H6 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ 23 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 19-3 ^@ http://purl.uniprot.org/annotation/PRO_0000356215 http://togogenome.org/gene/10090:Sarnp ^@ http://purl.uniprot.org/uniprot/B2RXM7|||http://purl.uniprot.org/uniprot/Q9D1J3 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed|||SAP|||SAP domain-containing ribonucleoprotein ^@ http://purl.uniprot.org/annotation/PRO_0000083919 http://togogenome.org/gene/10090:Gabrd ^@ http://purl.uniprot.org/uniprot/P22933|||http://purl.uniprot.org/uniprot/Q14AH9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit delta|||Helical|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000000469|||http://purl.uniprot.org/annotation/PRO_5014306925 http://togogenome.org/gene/10090:Klk12 ^@ http://purl.uniprot.org/uniprot/B2RVZ0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015087156 http://togogenome.org/gene/10090:Ccdc80 ^@ http://purl.uniprot.org/uniprot/Q8R2G6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 80|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000282419 http://togogenome.org/gene/10090:Asgr1 ^@ http://purl.uniprot.org/uniprot/B1AR34|||http://purl.uniprot.org/uniprot/P34927 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Motif|||Region|||Sequence Conflict|||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|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000046651 http://togogenome.org/gene/10090:Gabrb2 ^@ http://purl.uniprot.org/uniprot/P63137 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit beta-2|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000000460|||http://purl.uniprot.org/annotation/VSP_038829 http://togogenome.org/gene/10090:Rpl27 ^@ http://purl.uniprot.org/uniprot/P61358|||http://purl.uniprot.org/uniprot/Q5BLJ9 ^@ 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_0000126078 http://togogenome.org/gene/10090:Tspan4 ^@ http://purl.uniprot.org/uniprot/Q4FJW7|||http://purl.uniprot.org/uniprot/Q9DCK3 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000219242 http://togogenome.org/gene/10090:Cd82 ^@ http://purl.uniprot.org/uniprot/P40237|||http://purl.uniprot.org/uniprot/Q3UII2 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ CD82 antigen|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219227 http://togogenome.org/gene/10090:Slamf9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J072|||http://purl.uniprot.org/uniprot/Q9D780 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||SLAM family member 9 ^@ http://purl.uniprot.org/annotation/PRO_0000042234|||http://purl.uniprot.org/annotation/PRO_5006451926 http://togogenome.org/gene/10090:Spata32 ^@ http://purl.uniprot.org/uniprot/Q8C5V0 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Polar residues|||Spermatogenesis-associated protein 32 ^@ http://purl.uniprot.org/annotation/PRO_0000420265 http://togogenome.org/gene/10090:Acsl3 ^@ http://purl.uniprot.org/uniprot/E9PUC2|||http://purl.uniprot.org/uniprot/Q9CZW4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ AMP-dependent synthetase/ligase|||Cytoplasmic|||Fatty acid CoA ligase Acsl3|||Helical; Signal-anchor for type III membrane protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000193108 http://togogenome.org/gene/10090:Slfn4 ^@ http://purl.uniprot.org/uniprot/Q3UV10|||http://purl.uniprot.org/uniprot/Q3UV66 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Schlafen AlbA-2 ^@ http://togogenome.org/gene/10090:Pira2 ^@ http://purl.uniprot.org/uniprot/F8VQ94 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5003385298 http://togogenome.org/gene/10090:Hspa13 ^@ http://purl.uniprot.org/uniprot/D3Z0Y0|||http://purl.uniprot.org/uniprot/Q8BM72 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Heat shock 70 kDa protein 13|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000013559|||http://purl.uniprot.org/annotation/PRO_5015088533|||http://purl.uniprot.org/annotation/VSP_013912|||http://purl.uniprot.org/annotation/VSP_013913 http://togogenome.org/gene/10090:Mettl7a2 ^@ http://purl.uniprot.org/uniprot/Q5I0W6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Methyltransferase type 11 ^@ http://togogenome.org/gene/10090:Zim1 ^@ http://purl.uniprot.org/uniprot/Q6NZC6|||http://purl.uniprot.org/uniprot/Q8C393 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Dbndd2 ^@ http://purl.uniprot.org/uniprot/Q330P7|||http://purl.uniprot.org/uniprot/Q9CRD4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Dysbindin domain-containing protein 2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000191004 http://togogenome.org/gene/10090:Or4f4b ^@ http://purl.uniprot.org/uniprot/Q8VF49 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Creb3l2 ^@ http://purl.uniprot.org/uniprot/Q8BH52 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||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|||Leucine-zipper|||Loss of S1P cleavage.|||Loss of S1P cleavage; when associated with A-427.|||Loss of S1P cleavage; when associated with V-430.|||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_0000288068|||http://purl.uniprot.org/annotation/PRO_0000296210 http://togogenome.org/gene/10090:Wdr73 ^@ http://purl.uniprot.org/uniprot/Q9CWR1 ^@ 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 and isoform 4.|||In isoform 3.|||In isoform 4.|||WD 1|||WD 2|||WD 3|||WD repeat-containing protein 73 ^@ http://purl.uniprot.org/annotation/PRO_0000307281|||http://purl.uniprot.org/annotation/VSP_028667|||http://purl.uniprot.org/annotation/VSP_028668|||http://purl.uniprot.org/annotation/VSP_028669|||http://purl.uniprot.org/annotation/VSP_028670 http://togogenome.org/gene/10090:Ecm2 ^@ http://purl.uniprot.org/uniprot/Q5FW85 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Cell attachment site|||Disordered|||Extracellular matrix protein 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_0000287728 http://togogenome.org/gene/10090:Kcnd2 ^@ http://purl.uniprot.org/uniprot/Q9Z0V2 ^@ Binding Site|||Chain|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Abolishes channel activity. Alters potassium channel kinetics in heart myocytes. Abolishes the fast component of I(to) in heart ventricle.|||Abolishes regulation of neuronal A-type current in response to activation of metabotropic glutamate receptors.|||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 normal channel activation and inactivation, for interaction with KCNIP2, and probably other family members as well|||Interaction with KCNIP1|||Interaction with KCNIP1, KCNIP2, and other family members|||No effect on the regulation of neuronal A-type current in response to activation of metabotropic glutamate receptors.|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Potassium voltage-gated channel subfamily D member 2|||Required for dendritic targeting|||S4-S5 linker|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054065 http://togogenome.org/gene/10090:Taf9 ^@ http://purl.uniprot.org/uniprot/Q8VI33 ^@ 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|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Transcription initiation factor TFIID subunit 9 ^@ http://purl.uniprot.org/annotation/PRO_0000118889 http://togogenome.org/gene/10090:Nepn ^@ http://purl.uniprot.org/uniprot/Q9CQ76 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||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|||Nephrocan ^@ http://purl.uniprot.org/annotation/PRO_5004324983 http://togogenome.org/gene/10090:Nrip2 ^@ http://purl.uniprot.org/uniprot/Q9JHR9 ^@ 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.|||Interaction with NR1F2|||LXXLL motif|||Nuclear receptor-interacting protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000271057|||http://purl.uniprot.org/annotation/VSP_022275 http://togogenome.org/gene/10090:Dagla ^@ http://purl.uniprot.org/uniprot/A4FU75|||http://purl.uniprot.org/uniprot/Q6WQJ1 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Abolishes interaction with HOMER1.|||Abolishes interaction with HOMER1. Does not affect enzymatic activity. Fails to associate with the plasma membrane.|||Charge relay system|||Cytoplasmic|||Diacylglycerol lipase-alpha|||Disordered|||Extracellular|||Fungal lipase-like|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000248348 http://togogenome.org/gene/10090:Hmx1 ^@ http://purl.uniprot.org/uniprot/O70218 ^@ Chain|||DNA Binding|||Molecule Processing|||Motif|||Region ^@ Chain|||DNA Binding|||Motif|||Region ^@ Disordered|||HMX family specific domain 1|||HMX family specific domain 2|||Homeobox|||Homeobox protein HMX1 ^@ http://purl.uniprot.org/annotation/PRO_0000278454 http://togogenome.org/gene/10090:Emc6 ^@ http://purl.uniprot.org/uniprot/Q9CQW0 ^@ 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|||ER membrane protein complex subunit 6|||Helical|||Lumenal|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000254157 http://togogenome.org/gene/10090:Fiz1 ^@ http://purl.uniprot.org/uniprot/Q3TRV0|||http://purl.uniprot.org/uniprot/Q9WTJ4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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|||Flt3-interacting zinc finger protein 1|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000046938 http://togogenome.org/gene/10090:Prr19 ^@ http://purl.uniprot.org/uniprot/B2RW88 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic residues|||Disordered|||Polar residues|||Pro residues|||Proline-rich protein 19 ^@ http://purl.uniprot.org/annotation/PRO_0000454452 http://togogenome.org/gene/10090:Mup7 ^@ http://purl.uniprot.org/uniprot/Q58EV3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5015097820 http://togogenome.org/gene/10090:Usp10 ^@ http://purl.uniprot.org/uniprot/P52479 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||G3BP1-binding|||In isoform 2.|||Interaction with p53/TP53|||N-acetylalanine|||Nucleophile|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Proton acceptor|||Removed|||USP|||Ubiquitin carboxyl-terminal hydrolase 10 ^@ http://purl.uniprot.org/annotation/PRO_0000080630|||http://purl.uniprot.org/annotation/VSP_038870 http://togogenome.org/gene/10090:Or8s2 ^@ http://purl.uniprot.org/uniprot/Q8VGU2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pde1a ^@ http://purl.uniprot.org/uniprot/Q61481 ^@ 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 ^@ Calmodulin-binding|||Disordered|||Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PDEase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000198786|||http://purl.uniprot.org/annotation/VSP_004551|||http://purl.uniprot.org/annotation/VSP_060311|||http://purl.uniprot.org/annotation/VSP_060312|||http://purl.uniprot.org/annotation/VSP_060313|||http://purl.uniprot.org/annotation/VSP_060314|||http://purl.uniprot.org/annotation/VSP_060315 http://togogenome.org/gene/10090:Kcnk1 ^@ http://purl.uniprot.org/uniprot/A0A1D5RMH2|||http://purl.uniprot.org/uniprot/O08581 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Abolishes formation of a disulfide-linked heterodimer with KCNK2.|||Abolishes potassium channel activity.|||Cytoplasmic|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||Helical; Name=Pore helix 1|||Helical; Name=Pore helix 2|||Important for increased permeability to Na(+) when K(+) levels are subphysiological|||Important for intracellular retention in recycling endosomes|||Increases channel expression at the cell membrane, resulting in higher channel activity.|||Interchain|||N-linked (GlcNAc...) asparagine|||Part of a hydrophobic barrier that is stochastically dewetted and limits ion permeability|||Phosphoserine|||Potassium channel|||Potassium channel subfamily K member 1|||Selectivity filter 1|||Selectivity filter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000101741 http://togogenome.org/gene/10090:Mdfic ^@ http://purl.uniprot.org/uniprot/Q8BX65 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not affect protein expression and abundance. No effect on cell surface localization and secretion. No effect on interaction with GATA2.|||Extracellular|||Helical|||In isoform 2.|||MDFI|||MyoD family inhibitor domain-containing protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000280223|||http://purl.uniprot.org/annotation/VSP_052336|||http://purl.uniprot.org/annotation/VSP_052337 http://togogenome.org/gene/10090:Or13c3 ^@ http://purl.uniprot.org/uniprot/Q8VG87 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdkn2a ^@ http://purl.uniprot.org/uniprot/P51480|||http://purl.uniprot.org/uniprot/Q64364 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cyclin-dependent kinase inhibitor 2A|||Disordered|||In isoform 2.|||In isoform smARF.|||In plasmacytoma cell lines.|||In some liver tumors.|||In strain: 020, BALB/c, BALB/cJ, C3H/21BG, C3H/HeJ, CBA/J, MA/M4J and PL/J.|||In strain: BALB/c and BALB/cJ.|||In strain: BALB/cJ, C57BL/6J and MOLF/Ei.|||Interaction with CDK5RAP3 and MDM2|||Loss of activity.|||No effect on activity.|||Phosphoserine|||Tumor suppressor ARF ^@ http://purl.uniprot.org/annotation/PRO_0000144178|||http://purl.uniprot.org/annotation/PRO_0000144182|||http://purl.uniprot.org/annotation/VSP_015867|||http://purl.uniprot.org/annotation/VSP_044963 http://togogenome.org/gene/10090:Golga5 ^@ http://purl.uniprot.org/uniprot/Q9QYE6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dimethylated arginine|||Disordered|||Golgin subfamily A member 5|||Helical; Anchor for type IV membrane protein|||Lumenal|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000190062 http://togogenome.org/gene/10090:Zer1 ^@ http://purl.uniprot.org/uniprot/Q80ZJ6 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Splice Variant ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||In isoform 2 and isoform 3.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||N-acetylalanine|||Protein zer-1 homolog|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000066599|||http://purl.uniprot.org/annotation/VSP_014425|||http://purl.uniprot.org/annotation/VSP_014426|||http://purl.uniprot.org/annotation/VSP_014427 http://togogenome.org/gene/10090:Cope ^@ http://purl.uniprot.org/uniprot/O89079 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Coatomer subunit epsilon|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000193852 http://togogenome.org/gene/10090:Psmd13 ^@ http://purl.uniprot.org/uniprot/B2RT97|||http://purl.uniprot.org/uniprot/Q9WVJ2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ 26S proteasome non-ATPase regulatory subunit 13|||N6-acetyllysine|||PCI ^@ http://purl.uniprot.org/annotation/PRO_0000173868 http://togogenome.org/gene/10090:Cggbp1 ^@ http://purl.uniprot.org/uniprot/Q8BHG9 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||CGG triplet repeat-binding protein 1|||Disordered|||Nuclear localization signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000252416 http://togogenome.org/gene/10090:Ctss ^@ http://purl.uniprot.org/uniprot/F6WR04|||http://purl.uniprot.org/uniprot/O70370|||http://purl.uniprot.org/uniprot/Q3UD32|||http://purl.uniprot.org/uniprot/Q8BSZ5 ^@ 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 S|||Cathepsin propeptide inhibitor|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000026315|||http://purl.uniprot.org/annotation/PRO_0000026316|||http://purl.uniprot.org/annotation/PRO_5010754881|||http://purl.uniprot.org/annotation/PRO_5018613003|||http://purl.uniprot.org/annotation/PRO_5018696928 http://togogenome.org/gene/10090:Nrxn1 ^@ http://purl.uniprot.org/uniprot/A0A0H2UH29|||http://purl.uniprot.org/uniprot/E0CY11|||http://purl.uniprot.org/uniprot/E0CZA5|||http://purl.uniprot.org/uniprot/G3UWQ9|||http://purl.uniprot.org/uniprot/P0DI97|||http://purl.uniprot.org/uniprot/Q9CS84 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes heparan sulfate attachment.|||Abolishes heparan sulfate attachment. Does not affect cell surface location.|||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 and isoform 5a.|||In isoform 3a and isoform 4a.|||In isoform 4a and isoform 6.|||In isoform 5a.|||In isoform 6.|||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|||Loss of NLGN1-binding. No effect on CBLN1-binding.|||N-linked (GlcNAc...) asparagine|||Neurexin-1|||Neurexin-1-beta|||Neurexin/syndecan/glycophorin C|||No effect on heparan sulfate attachment.|||O-linked (Xyl...) (heparan sulfate) serine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000043164|||http://purl.uniprot.org/annotation/PRO_0000412630|||http://purl.uniprot.org/annotation/PRO_5003133278|||http://purl.uniprot.org/annotation/VSP_003484|||http://purl.uniprot.org/annotation/VSP_003485|||http://purl.uniprot.org/annotation/VSP_016401|||http://purl.uniprot.org/annotation/VSP_043946|||http://purl.uniprot.org/annotation/VSP_058203|||http://purl.uniprot.org/annotation/VSP_058204 http://togogenome.org/gene/10090:Frat2 ^@ http://purl.uniprot.org/uniprot/Q8K025 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Acidic residues|||Disordered|||GSK-3-binding protein FRAT2|||Involved in GSK-3 binding ^@ http://purl.uniprot.org/annotation/PRO_0000087335 http://togogenome.org/gene/10090:Il18bp ^@ http://purl.uniprot.org/uniprot/Q9Z0M9 ^@ 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 ^@ Disordered|||Ig-like C2-type|||Interleukin-18-binding protein|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014779 http://togogenome.org/gene/10090:Mon2 ^@ http://purl.uniprot.org/uniprot/B9EKJ3|||http://purl.uniprot.org/uniprot/Q80TL7 ^@ 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|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||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_0000297903|||http://purl.uniprot.org/annotation/VSP_027394|||http://purl.uniprot.org/annotation/VSP_027395 http://togogenome.org/gene/10090:Ttc7b ^@ http://purl.uniprot.org/uniprot/E9Q6P5 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ Phosphoserine|||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 7B ^@ http://purl.uniprot.org/annotation/PRO_0000435631 http://togogenome.org/gene/10090:Sema4b ^@ http://purl.uniprot.org/uniprot/Q62179 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Sema|||Semaphorin-4B ^@ http://purl.uniprot.org/annotation/PRO_0000042162 http://togogenome.org/gene/10090:Cga ^@ http://purl.uniprot.org/uniprot/A0A0F7RQH1|||http://purl.uniprot.org/uniprot/P01216 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Glycoprotein hormones alpha chain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000011648|||http://purl.uniprot.org/annotation/PRO_5014203326 http://togogenome.org/gene/10090:Akr1c6 ^@ http://purl.uniprot.org/uniprot/P70694|||http://purl.uniprot.org/uniprot/Q3UEM0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Site ^@ Estradiol 17 beta-dehydrogenase 5|||Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000124652 http://togogenome.org/gene/10090:Tmem179b ^@ http://purl.uniprot.org/uniprot/Q9CY24 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Phosphoserine|||Transmembrane protein 179B ^@ http://purl.uniprot.org/annotation/PRO_0000328988 http://togogenome.org/gene/10090:Fam169a ^@ http://purl.uniprot.org/uniprot/Q5XG69 ^@ 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|||Basic residues|||Disordered|||Phosphoserine|||Polar residues|||Soluble lamin-associated protein of 75 kDa ^@ http://purl.uniprot.org/annotation/PRO_0000320588 http://togogenome.org/gene/10090:Or5b107 ^@ http://purl.uniprot.org/uniprot/Q8VEV7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cycs ^@ http://purl.uniprot.org/uniprot/P62897|||http://purl.uniprot.org/uniprot/Q56A15 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Cytochrome c|||Cytochrome c, somatic|||N-acetylglycine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphotyrosine|||Removed|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000108225 http://togogenome.org/gene/10090:Pla2g15 ^@ http://purl.uniprot.org/uniprot/Q8VEB4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Abolishes enzyme activity.|||Acyl-ester intermediate|||Charge relay system|||N-linked (GlcNAc...) asparagine|||Phospholipase A2 group XV ^@ http://purl.uniprot.org/annotation/PRO_0000017809 http://togogenome.org/gene/10090:Bcar1 ^@ http://purl.uniprot.org/uniprot/Q3TJP4|||http://purl.uniprot.org/uniprot/Q61140 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Breast cancer anti-estrogen resistance protein 1|||Disordered|||Divergent helix-loop-helix motif|||In isoform Cas-A.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH3|||SH3-binding|||Substrate for kinases ^@ http://purl.uniprot.org/annotation/PRO_0000064855|||http://purl.uniprot.org/annotation/VSP_004134 http://togogenome.org/gene/10090:Lin52 ^@ http://purl.uniprot.org/uniprot/Q8CD94 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Phosphoserine|||Protein lin-52 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000252155 http://togogenome.org/gene/10090:Orai3 ^@ http://purl.uniprot.org/uniprot/A3KCG3|||http://purl.uniprot.org/uniprot/Q6P8G8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Protein orai-3 ^@ http://purl.uniprot.org/annotation/PRO_0000234396 http://togogenome.org/gene/10090:Gm10591 ^@ http://purl.uniprot.org/uniprot/P86792|||http://purl.uniprot.org/uniprot/P86793 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Region|||Sequence Conflict|||Signal Peptide ^@ C-C motif chemokine 21b|||C-C motif chemokine 21c|||C-terminal basic extension|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000005222|||http://purl.uniprot.org/annotation/PRO_0000403422 http://togogenome.org/gene/10090:Or4n4b ^@ http://purl.uniprot.org/uniprot/Q14AK5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Il12b ^@ http://purl.uniprot.org/uniprot/P43432|||http://purl.uniprot.org/uniprot/Q3ZAX5 ^@ 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|||Sequence Variant|||Signal Peptide|||Strand|||Turn ^@ Fibronectin type-III|||Ig-like|||Ig-like C2-type|||In strain: B10.S/J and SJL/J.|||Interchain (with C-92 in IL12A and C-74 in IL23A)|||Interleukin-12 subunit beta|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000010933|||http://purl.uniprot.org/annotation/PRO_5014205839 http://togogenome.org/gene/10090:Rab37 ^@ http://purl.uniprot.org/uniprot/Q544E8|||http://purl.uniprot.org/uniprot/Q9JKM7 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict ^@ Cysteine methyl ester|||Disordered|||Effector region|||N-acetylthreonine|||Ras-related protein Rab-37|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121250|||http://purl.uniprot.org/annotation/PRO_0000370829 http://togogenome.org/gene/10090:Cog7 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Q9|||http://purl.uniprot.org/uniprot/Q3UM29 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Sequence Conflict ^@ Conserved oligomeric Golgi complex subunit 7 ^@ http://purl.uniprot.org/annotation/PRO_0000320147 http://togogenome.org/gene/10090:Slc25a17 ^@ http://purl.uniprot.org/uniprot/O70579 ^@ Chain|||Molecule Processing|||Motif|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ Chain|||Motif|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Lumenal|||Necessary for targeting to peroxisomes and interaction with PEX19|||Peroxisomal membrane protein PMP34|||Peroxisome localization signal|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090706 http://togogenome.org/gene/10090:Ube2o ^@ http://purl.uniprot.org/uniprot/Q6ZPJ3 ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ (E3-independent) E2 ubiquitin-conjugating enzyme UBE2O|||Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl thioester intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||UBC core ^@ http://purl.uniprot.org/annotation/PRO_0000280638 http://togogenome.org/gene/10090:Mybphl ^@ http://purl.uniprot.org/uniprot/Q5FW53 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Fibronectin type-III|||Ig-like C2-type 1|||Ig-like C2-type 2|||Myosin-binding protein H-like|||Omega-N-methylarginine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000330020 http://togogenome.org/gene/10090:Or5bw2 ^@ http://purl.uniprot.org/uniprot/Q8VF34 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Epgn ^@ http://purl.uniprot.org/uniprot/Q0VEB7|||http://purl.uniprot.org/uniprot/Q924X1 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EGF-like|||Epigen|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000045463|||http://purl.uniprot.org/annotation/PRO_5014306839 http://togogenome.org/gene/10090:Spon2 ^@ http://purl.uniprot.org/uniprot/Q8BMS2 ^@ 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|||Site ^@ C-linked (Man) tryptophan|||Important for metal ion-dependent interaction with integrin|||Spondin|||Spondin-2|||TSP type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000035871 http://togogenome.org/gene/10090:Enpp1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Q7|||http://purl.uniprot.org/uniprot/G3X9S2|||http://purl.uniprot.org/uniprot/P06802 ^@ 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|||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|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 60% of ENPP1 redirected to apical surface in epithelial cells. 75% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles; when associated with A-32.|||70% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles. 75% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles; when associated with A-31.|||AMP-threonine intermediate|||Abolished ability to hydrolyze 2',3'-cGAMP without affecting ability to hydrolyze ATP.|||Abolishes all phosphodiesterase activity. 10% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate.|||Abolishes all phosphodiesterase activity. 15% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate.|||Abolishes all phosphodiesterase activity. 60% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate.|||Abolishes all phosphodiesterase activity. Abolishes formation of nucleotidylated intermediate.|||Cleavage|||Cytoplasmic|||Decreased phosphodiesterase activity.|||Decreases phosphodiesterase activity by 40%. Decreased formation of nucleotidylated intermediate.|||Decreases phosphodiesterase activity by 50%. Decreased formation of nucleotidylated intermediate.|||Decreases phosphodiesterase activity by 90%. Accumulates nucleotidylated intermediate.|||Decreases phosphodiesterase activity by 95%. 65% activity can be restored by addition of Zn(2+) ions. Accumulates nucleotidylated intermediate.|||Decreases phosphodiesterase activity by 95%. Abolishes formation of nucleotidylated intermediate.|||Decreases phosphodiesterase activity by 95%. Accumulates nucleotidylated intermediate.|||Di-leucine motif|||Disordered|||Ectonucleotide pyrophosphatase/phosphodiesterase family member 1|||Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, secreted form|||Essential for catalytic activity|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In allele ENPP1b.|||In isoform 1.|||In ttw.|||Linker|||Little change in baolateral sorting in epithelial cells.|||Mice display a low bone mass density and show a striking joint disease and calcification of blood vessels. Probably affects protein stability.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes activity with nucleotide phosphates. Confers very low activity with lysophospholipids.|||No change in increased NPP activity in oestoblastic matrix vesicles.|||No effect on basolateral sorting in epithelial cells.|||Nuclease|||Phosphodiesterase|||Phosphoserine|||Phosphothreonine|||SMB|||SMB 1|||SMB 2|||Strongly decreased phosphodiesterase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000188565|||http://purl.uniprot.org/annotation/PRO_0000447134|||http://purl.uniprot.org/annotation/VSP_006748 http://togogenome.org/gene/10090:Mkln1 ^@ http://purl.uniprot.org/uniprot/O89050|||http://purl.uniprot.org/uniprot/Q3UWT3 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Strand ^@ Abolishes targeting to the nucleus.|||CTLH|||Important for location in the cytosol|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||LisH|||Muskelin|||N-acetylalanine|||No effect on predominant location in the cytosol.|||Removed|||Strongly increased location in the nucleus. ^@ http://purl.uniprot.org/annotation/PRO_0000119139 http://togogenome.org/gene/10090:Dkk3 ^@ http://purl.uniprot.org/uniprot/Q9QUN9 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide ^@ DKK-type Cys-1|||DKK-type Cys-2|||Dickkopf-related protein 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000007223 http://togogenome.org/gene/10090:Zfp746 ^@ http://purl.uniprot.org/uniprot/A0A0N4SWG2|||http://purl.uniprot.org/uniprot/Q3U133 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ C2H2-type|||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)|||KRAB|||Polar residues|||Pro residues|||Zinc finger protein 746 ^@ http://purl.uniprot.org/annotation/PRO_0000253729 http://togogenome.org/gene/10090:Cfhr1 ^@ http://purl.uniprot.org/uniprot/Q61406 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Sushi ^@ http://purl.uniprot.org/annotation/PRO_5015098105 http://togogenome.org/gene/10090:Or12j4 ^@ http://purl.uniprot.org/uniprot/Q7TRT7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ftl1 ^@ http://purl.uniprot.org/uniprot/Q9CPX4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ferritin-like diiron ^@ http://togogenome.org/gene/10090:Stam2 ^@ http://purl.uniprot.org/uniprot/O88811|||http://purl.uniprot.org/uniprot/Q3TGH8 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand ^@ Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand ^@ ITAM|||In isoform 2.|||Interaction with HGS|||Interaction with USP8|||Loss of interaction with UBQLN1; when associated with A-176.|||Loss of interaction with UBQLN1; when associated with A-177.|||PxVxL motif|||SH3|||Signal transducing adapter molecule 2|||UIM|||VHS ^@ http://purl.uniprot.org/annotation/PRO_0000190148|||http://purl.uniprot.org/annotation/VSP_014849|||http://purl.uniprot.org/annotation/VSP_014850|||http://purl.uniprot.org/annotation/VSP_014851 http://togogenome.org/gene/10090:Kalrn ^@ http://purl.uniprot.org/uniprot/A2CG49|||http://purl.uniprot.org/uniprot/D3Z4R2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand ^@ Basic and acidic residues|||CRAL-TRIO|||DH|||DH 1|||DH 2|||Disordered|||Fibronectin type-III|||Ig-like|||Ig-like C2-type|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5 and isoform 10.|||In isoform 5 and isoform 8.|||In isoform 5, isoform 8, isoform 9 and isoform 10.|||In isoform 6.|||In isoform 7.|||In isoform 8 and isoform 9.|||Kalirin|||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_0000308173|||http://purl.uniprot.org/annotation/VSP_052562|||http://purl.uniprot.org/annotation/VSP_052563|||http://purl.uniprot.org/annotation/VSP_052564|||http://purl.uniprot.org/annotation/VSP_052565|||http://purl.uniprot.org/annotation/VSP_052566|||http://purl.uniprot.org/annotation/VSP_052567|||http://purl.uniprot.org/annotation/VSP_052568|||http://purl.uniprot.org/annotation/VSP_052569|||http://purl.uniprot.org/annotation/VSP_052570|||http://purl.uniprot.org/annotation/VSP_052571|||http://purl.uniprot.org/annotation/VSP_052572|||http://purl.uniprot.org/annotation/VSP_052573|||http://purl.uniprot.org/annotation/VSP_052574|||http://purl.uniprot.org/annotation/VSP_052575|||http://purl.uniprot.org/annotation/VSP_052576|||http://purl.uniprot.org/annotation/VSP_052577|||http://purl.uniprot.org/annotation/VSP_052578|||http://purl.uniprot.org/annotation/VSP_052579 http://togogenome.org/gene/10090:Chst5 ^@ http://purl.uniprot.org/uniprot/Q9QUP4 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 5|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000085196 http://togogenome.org/gene/10090:Rab11b ^@ http://purl.uniprot.org/uniprot/P46638|||http://purl.uniprot.org/uniprot/Q78ZJ8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region ^@ Citrulline|||Constitutively active mutant locked in the active GTP-bound form; alters endocytic recycling.|||Cysteine methyl ester|||Disordered|||Dominant negative mutant locked in the inactive GDP-bound form; partially relocalizes to the Golgi and alters endocytic recycling.|||Effector region|||N-acetylglycine|||Polar residues|||Ras-related protein Rab-11B|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121159|||http://purl.uniprot.org/annotation/PRO_0000370816 http://togogenome.org/gene/10090:Cth ^@ http://purl.uniprot.org/uniprot/Q8VCN5 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Cystathionine gamma-lyase|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_0000114751 http://togogenome.org/gene/10090:Csf1r ^@ http://purl.uniprot.org/uniprot/P09581|||http://purl.uniprot.org/uniprot/Q0P635|||http://purl.uniprot.org/uniprot/Q3UKC6|||http://purl.uniprot.org/uniprot/Q6NXV8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||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|||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|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes interaction with GRB2.|||Abolishes interaction with PIK3R1. Strongly reduced phosphorylation of PLCG2. No effect on binding to THOC5.|||Activation loop|||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|||Loss of kinase activity.|||Loss of kinase activity. Abolishes binding to THOC5.|||Macrophage colony-stimulating factor 1 receptor|||May alter protein folding or stability. Loss of kinase activity. No effect on interaction with PIK3R1.|||N-linked (GlcNAc...) asparagine|||No effect on binding to THOC5.|||No effect on binding to THOC5. Slightly reduced enhancement of cell proliferation.|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Reduced interaction with CBL. Prolonged signaling, due to reduced internalization and degradation. Reduced interaction with FYN. Promotes cell proliferation. Reduced autophosphorylation at Tyr-807.|||Reduced kinase activity. Strongly reduced phosphorylation of PLCG2. Diminishes binding to THOC5.|||Regulatory juxtamembrane domain|||Slightly impaired signaling.|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000016766|||http://purl.uniprot.org/annotation/PRO_5004230152|||http://purl.uniprot.org/annotation/PRO_5004278147|||http://purl.uniprot.org/annotation/PRO_5014306815 http://togogenome.org/gene/10090:Ifi211 ^@ http://purl.uniprot.org/uniprot/P0DOV1 ^@ 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 ^@ 1|||2|||3|||4|||4 X 7 AA tandem repeats of T-S-T-A-Q-A-[GR]|||Basic and acidic residues|||Disordered|||HIN-200|||In isoform 2.|||Interferon-activable protein 205-B|||Polar residues|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000153722|||http://purl.uniprot.org/annotation/VSP_058589 http://togogenome.org/gene/10090:Vmn1r148 ^@ http://purl.uniprot.org/uniprot/Q9EPS5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mmp24 ^@ http://purl.uniprot.org/uniprot/Q9R0S2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Abolishes proteolytic processing. Gain of function mutant.|||Basic and acidic residues|||Cleavage; by furin|||Cysteine switch|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Impaired recycling affecting its internalization, leading to decreased activity on the plasma surface.|||Loss of function. Does not prevent proteolytic processing.|||Matrix metalloproteinase-24|||PDZ-binding|||Processed matrix metalloproteinase-24|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028848|||http://purl.uniprot.org/annotation/PRO_0000028849|||http://purl.uniprot.org/annotation/PRO_0000302759 http://togogenome.org/gene/10090:Gpr132 ^@ http://purl.uniprot.org/uniprot/Q9Z282 ^@ 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 ^@ Cytoplasmic|||Enhanced surface expression and a lower localization to endosomal vesicles.|||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 132 ^@ http://purl.uniprot.org/annotation/PRO_0000069462 http://togogenome.org/gene/10090:Slc43a2 ^@ http://purl.uniprot.org/uniprot/Q8CGA3 ^@ 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|||Large neutral amino acids transporter small subunit 4|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000307273 http://togogenome.org/gene/10090:Oaf ^@ http://purl.uniprot.org/uniprot/Q8QZR4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Sequence Conflict|||Signal Peptide ^@ Out at first protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000292428 http://togogenome.org/gene/10090:Lzic ^@ http://purl.uniprot.org/uniprot/Q8K3C3 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Protein LZIC ^@ http://purl.uniprot.org/annotation/PRO_0000263692 http://togogenome.org/gene/10090:Ddost ^@ http://purl.uniprot.org/uniprot/O54734 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000021958 http://togogenome.org/gene/10090:Slc19a3 ^@ http://purl.uniprot.org/uniprot/Q99PL8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Can mediate pyridoxine transport; when associated with G-88; I-92; T-94; W-95; S-169 and N-174.|||Can mediate pyridoxine transport; when associated with Q-87; G-88; I-92; T-94; S-169 and N-174.|||Can mediate pyridoxine transport; when associated with Q-87; G-88; I-92; T-94; W-95 and N-174.|||Can mediate pyridoxine transport; when associated with Q-87; G-88; I-92; T-94; W-95 and S-169.|||Can mediate pyridoxine transport; when associated with Q-87; G-88; I-92; W-95; S-169 and N-174.|||Can mediate pyridoxine transport; when associated with Q-87; G-88; T-94; W-95; S-169 and N-174.|||Can mediate pyridoxine transport; when associated with Q-87; I-92; T-94; W-95; S-169 and N-174.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Thiamine transporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000232658 http://togogenome.org/gene/10090:Ddx54 ^@ http://purl.uniprot.org/uniprot/Q8K4L0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ ATP-dependent RNA helicase DDX54|||Basic and acidic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Phosphothreonine|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000055057 http://togogenome.org/gene/10090:Gjb1 ^@ http://purl.uniprot.org/uniprot/A0A654IEJ3|||http://purl.uniprot.org/uniprot/P28230 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Connexin N-terminal|||Cytoplasmic|||Extracellular|||Gap junction beta-1 protein|||Gap junction protein cysteine-rich|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000057851 http://togogenome.org/gene/10090:Tlr2 ^@ http://purl.uniprot.org/uniprot/G3X8Y8|||http://purl.uniprot.org/uniprot/Q9QUN7 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ ATG16L1-binding motif|||Abolishes MYD88-binding and response to microbial cell wall components.|||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|||N-linked (GlcNAc...) asparagine|||TIR|||Toll-like receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000034712|||http://purl.uniprot.org/annotation/PRO_5015091847 http://togogenome.org/gene/10090:Ormdl3 ^@ http://purl.uniprot.org/uniprot/Q9CPZ6 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Hydroxyproline|||Important for ceramide level-sensing|||ORM1-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000215640 http://togogenome.org/gene/10090:Spata31d1a ^@ http://purl.uniprot.org/uniprot/E9QA35|||http://purl.uniprot.org/uniprot/Q8CDS1|||http://purl.uniprot.org/uniprot/Q9CVY6 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues|||SPATA31|||SPATA31F3-like ^@ http://togogenome.org/gene/10090:Ptpro ^@ http://purl.uniprot.org/uniprot/A0A0N4SUY2|||http://purl.uniprot.org/uniprot/E9PVJ6|||http://purl.uniprot.org/uniprot/E9Q4I1|||http://purl.uniprot.org/uniprot/E9Q612 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Fibronectin type-III 6|||Helical|||Loss of tyrosine phosphorylation. Abolishes interaction with FYN and GRB2.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Receptor-type tyrosine-protein phosphatase O|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||protein-tyrosine-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000414059|||http://purl.uniprot.org/annotation/PRO_5003245695 http://togogenome.org/gene/10090:Mta2 ^@ http://purl.uniprot.org/uniprot/Q9R190 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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|||Metastasis-associated protein MTA2|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||SANT ^@ http://purl.uniprot.org/annotation/PRO_0000083497 http://togogenome.org/gene/10090:Gm7168 ^@ http://purl.uniprot.org/uniprot/A0A0R4J163|||http://purl.uniprot.org/uniprot/A0AUV4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Pro residues|||Protein kinase|||Proton acceptor|||Sperm motility kinase Y|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000307876 http://togogenome.org/gene/10090:Rimoc1 ^@ http://purl.uniprot.org/uniprot/Q8BR90 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Splice Variant ^@ In isoform 2.|||N-acetylalanine|||RAB7A-interacting MON1-CCZ1 complex subunit 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000341215|||http://purl.uniprot.org/annotation/VSP_034224|||http://purl.uniprot.org/annotation/VSP_034225 http://togogenome.org/gene/10090:Kctd4 ^@ http://purl.uniprot.org/uniprot/Q9D7X1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ BTB|||BTB/POZ domain-containing protein KCTD4 ^@ http://purl.uniprot.org/annotation/PRO_0000191290 http://togogenome.org/gene/10090:Rtp2 ^@ http://purl.uniprot.org/uniprot/Q80ZI2 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Topological Domain|||Transmembrane|||Zinc Finger ^@ 3CxxC-type|||Cytoplasmic|||Extracellular|||Helical|||Receptor-transporting protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000181992 http://togogenome.org/gene/10090:Nxf2 ^@ http://purl.uniprot.org/uniprot/Q4ZGD8|||http://purl.uniprot.org/uniprot/Q8R499|||http://purl.uniprot.org/uniprot/Q99MW6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ NTF2|||TAP-C ^@ http://togogenome.org/gene/10090:Zbed3 ^@ http://purl.uniprot.org/uniprot/Q3TSB2|||http://purl.uniprot.org/uniprot/Q9D0L1 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Coiled-Coil|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ BED-type|||Decreases the interaction with AXIN1, GSK3B-mediated beta-catenin phosphorylation, cytoplasmic beta-catenin accumulation and Wnt-mediated transcription activation.|||Disordered|||PPPSP motif; required for interaction with AXIN1|||Zinc finger BED domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000421257 http://togogenome.org/gene/10090:Ddx18 ^@ http://purl.uniprot.org/uniprot/B2RUM8|||http://purl.uniprot.org/uniprot/Q8K363 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ ATP-dependent RNA helicase DDX18|||Basic and acidic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Polar residues|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000055002 http://togogenome.org/gene/10090:Hint1 ^@ http://purl.uniprot.org/uniprot/P70349 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site ^@ Adenosine 5'-monophosphoramidase HINT1|||HIT|||Histidine triad motif|||Loss of desumoylase activity.|||Loss of interaction with CALM1. No effect on desumoylase activity.|||N-acetylalanine|||N6-acetyllysine|||No effect on desumoylase activity.|||Phosphoserine|||Reduced interaction with SUMO2.|||Removed|||Significanly reduced interaction with SUMO2.|||Significanly reduced interaction with SUMO2. Loss of desumoylase activity.|||Tele-AMP-histidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000109782 http://togogenome.org/gene/10090:Epc2 ^@ http://purl.uniprot.org/uniprot/Q3TNY4|||http://purl.uniprot.org/uniprot/Q8C0I4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Disordered|||Enhancer of polycomb C-terminal|||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_0000239296 http://togogenome.org/gene/10090:Arcn1 ^@ http://purl.uniprot.org/uniprot/Q5XJY5 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Coatomer subunit delta|||Disordered|||MHD|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000193842 http://togogenome.org/gene/10090:Slc12a2 ^@ http://purl.uniprot.org/uniprot/E9QM38|||http://purl.uniprot.org/uniprot/P55012 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Abolished interaction witzh STK39/SPAK and subsequent phosphorylatuon and activation.|||Amino acid permease N-terminal|||Amino acid permease/ SLC12A|||Basic and acidic residues|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Helical|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RFXV motif 1|||RFXV motif 2|||Reduced potassium ion transmembrane transport.|||SLC12A transporter C-terminal|||Solute carrier family 12 member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000178024 http://togogenome.org/gene/10090:Ovol2 ^@ http://purl.uniprot.org/uniprot/Q3TIV4|||http://purl.uniprot.org/uniprot/Q8CIV7 ^@ 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 ^@ C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Causes obesity in mice. Obesity develops with normal food intake and reduced energy expenditure. Mice are cold intolerant with defective brown/beige adipose tissues. Reduces interaction with CEBPA.|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Transcription factor Ovo-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000047014|||http://purl.uniprot.org/annotation/VSP_013576|||http://purl.uniprot.org/annotation/VSP_013577|||http://purl.uniprot.org/annotation/VSP_013578 http://togogenome.org/gene/10090:Odad3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1K3|||http://purl.uniprot.org/uniprot/Q8BSN3 ^@ 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.|||Outer dynein arm-docking complex subunit 3 ^@ http://purl.uniprot.org/annotation/PRO_0000321527|||http://purl.uniprot.org/annotation/VSP_031786|||http://purl.uniprot.org/annotation/VSP_031787|||http://purl.uniprot.org/annotation/VSP_031788 http://togogenome.org/gene/10090:Adh6a ^@ http://purl.uniprot.org/uniprot/E9Q5Z6|||http://purl.uniprot.org/uniprot/Q9D932 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Enoyl reductase (ER) ^@ http://togogenome.org/gene/10090:Iscu ^@ http://purl.uniprot.org/uniprot/Q9D7P6 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Site|||Strand|||Transit Peptide|||Turn ^@ Cysteine persulfide|||Cysteine persulfide intermediate|||Does not affect core iron sulfur assembly complex formation. Abolishes sulhydratation.|||Iron-sulfur cluster assembly enzyme ISCU|||Mediates ISCU dimerization and de novo [2Fe-2S] cluster assembly|||Mitochondrion|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000019693 http://togogenome.org/gene/10090:Padi2 ^@ http://purl.uniprot.org/uniprot/Q08642|||http://purl.uniprot.org/uniprot/Q3TBF1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Citrulline|||N-acetylmethionine|||Nucleophile|||Protein-arginine deiminase (PAD) N-terminal|||Protein-arginine deiminase (PAD) central|||Protein-arginine deiminase C-terminal|||Protein-arginine deiminase type-2 ^@ http://purl.uniprot.org/annotation/PRO_0000220027 http://togogenome.org/gene/10090:Tex21 ^@ http://purl.uniprot.org/uniprot/Q497Q3|||http://purl.uniprot.org/uniprot/Q9D4K1|||http://purl.uniprot.org/uniprot/Q9R0U9 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Lgi2 ^@ http://purl.uniprot.org/uniprot/Q50DZ7|||http://purl.uniprot.org/uniprot/Q8K4Z0 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide|||Splice Variant ^@ EAR|||EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||EAR 7|||In isoform 2.|||LRR 1|||LRR 2|||LRRCT|||LRRNT|||Leucine-rich repeat LGI family member 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017709|||http://purl.uniprot.org/annotation/PRO_5009971028|||http://purl.uniprot.org/annotation/VSP_007680|||http://purl.uniprot.org/annotation/VSP_007681 http://togogenome.org/gene/10090:Cabp7 ^@ http://purl.uniprot.org/uniprot/Q5NCJ7|||http://purl.uniprot.org/uniprot/Q91ZM8 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Topological Domain|||Transmembrane ^@ Calcium-binding protein 7|||Cytoplasmic|||EF-hand|||EF-hand 1|||EF-hand 2|||Extracellular|||Helical|||Helical; Anchor for type IV membrane protein ^@ http://purl.uniprot.org/annotation/PRO_0000073527 http://togogenome.org/gene/10090:Zfp507 ^@ http://purl.uniprot.org/uniprot/Q6ZPY5 ^@ 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 ^@ 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 507 ^@ http://purl.uniprot.org/annotation/PRO_0000349309 http://togogenome.org/gene/10090:Aftph ^@ http://purl.uniprot.org/uniprot/H3BJH7|||http://purl.uniprot.org/uniprot/Q80WT5 ^@ 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 ^@ Aftiphilin|||Aftiphilin clathrin-binding box|||Basic and acidic residues|||CLTCL1/Clathrin-binding|||Clathrin-binding|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||WXXF motif 1|||WXXF motif 2|||WXXF motif 3 ^@ http://purl.uniprot.org/annotation/PRO_0000064489|||http://purl.uniprot.org/annotation/VSP_013242 http://togogenome.org/gene/10090:Snx16 ^@ http://purl.uniprot.org/uniprot/Q3TLM7|||http://purl.uniprot.org/uniprot/Q8C080 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||PX|||Phosphoserine|||Polar residues|||Sorting nexin-16 ^@ http://purl.uniprot.org/annotation/PRO_0000236204 http://togogenome.org/gene/10090:Vmn1r15 ^@ http://purl.uniprot.org/uniprot/Q14C10 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Phgr1 ^@ http://purl.uniprot.org/uniprot/Q8K0G7 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Proline, histidine and glycine-rich protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000395030|||http://purl.uniprot.org/annotation/VSP_039349 http://togogenome.org/gene/10090:Ppm1n ^@ http://purl.uniprot.org/uniprot/Q8BGL1 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ PPM-type phosphatase|||Probable protein phosphatase 1N ^@ http://purl.uniprot.org/annotation/PRO_0000349232 http://togogenome.org/gene/10090:Tlk2 ^@ http://purl.uniprot.org/uniprot/B1ASU9|||http://purl.uniprot.org/uniprot/B7ZC85|||http://purl.uniprot.org/uniprot/O55047|||http://purl.uniprot.org/uniprot/Q6NZC4 ^@ Active Site|||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|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||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.|||Phosphoserine|||Phosphoserine; by CHEK1|||Polar residues|||Protein kinase|||Proton acceptor|||Required for interaction with TLK1 and DYNLL1/LC8|||Serine/threonine-protein kinase tousled-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000086755|||http://purl.uniprot.org/annotation/VSP_050574|||http://purl.uniprot.org/annotation/VSP_050575|||http://purl.uniprot.org/annotation/VSP_050576 http://togogenome.org/gene/10090:Lrrc14b ^@ http://purl.uniprot.org/uniprot/Q3UJB3 ^@ 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_0000344241 http://togogenome.org/gene/10090:Or2y1g ^@ http://purl.uniprot.org/uniprot/Q8VFA7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Stx19 ^@ http://purl.uniprot.org/uniprot/Q8R1Q0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Syntaxin-19|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000263710 http://togogenome.org/gene/10090:Fam181b ^@ http://purl.uniprot.org/uniprot/A0A140LHM6 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Gm14819 ^@ http://purl.uniprot.org/uniprot/Q62478 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Gna13 ^@ http://purl.uniprot.org/uniprot/P27601|||http://purl.uniprot.org/uniprot/Q8K086 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein subunit alpha-13|||Phosphothreonine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000203774 http://togogenome.org/gene/10090:Semp2l1 ^@ http://purl.uniprot.org/uniprot/E9PXF3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Ubiquitin-like protease family profile ^@ http://togogenome.org/gene/10090:Them5 ^@ http://purl.uniprot.org/uniprot/Q9CQJ0 ^@ Active Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Active Site|||Chain|||Splice Variant ^@ Acyl-coenzyme A thioesterase THEM5|||In isoform 2.|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000284520|||http://purl.uniprot.org/annotation/VSP_024556 http://togogenome.org/gene/10090:Or6c6 ^@ http://purl.uniprot.org/uniprot/Q7TRI2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H2ac7 ^@ http://purl.uniprot.org/uniprot/B2RVF0|||http://purl.uniprot.org/uniprot/C0HKE1|||http://purl.uniprot.org/uniprot/C0HKE2|||http://purl.uniprot.org/uniprot/C0HKE3|||http://purl.uniprot.org/uniprot/C0HKE4|||http://purl.uniprot.org/uniprot/C0HKE5|||http://purl.uniprot.org/uniprot/C0HKE6|||http://purl.uniprot.org/uniprot/C0HKE7|||http://purl.uniprot.org/uniprot/C0HKE8|||http://purl.uniprot.org/uniprot/C0HKE9 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Histone H2A type 1-C|||Histone H2A type 1-D|||Histone H2A type 1-E|||Histone H2A type 1-G|||Histone H2A type 1-I|||Histone H2A type 1-N|||Histone H2A type 1-O|||Histone H2A type 1-P|||Histone H2A/H2B/H3|||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_0000439715|||http://purl.uniprot.org/annotation/PRO_0000439716|||http://purl.uniprot.org/annotation/PRO_0000439717|||http://purl.uniprot.org/annotation/PRO_0000439718|||http://purl.uniprot.org/annotation/PRO_0000439719|||http://purl.uniprot.org/annotation/PRO_0000439720|||http://purl.uniprot.org/annotation/PRO_0000439721|||http://purl.uniprot.org/annotation/PRO_0000439722|||http://purl.uniprot.org/annotation/PRO_0000439723 http://togogenome.org/gene/10090:Rbm25 ^@ http://purl.uniprot.org/uniprot/B2RY56 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Necessary for nuclear speckle localization|||PWI|||Phosphoserine|||Polar residues|||RNA-binding protein 25|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000368187 http://togogenome.org/gene/10090:Tmem72 ^@ http://purl.uniprot.org/uniprot/Q8C3K5 ^@ 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 72 ^@ http://purl.uniprot.org/annotation/PRO_0000319056 http://togogenome.org/gene/10090:Vmn1r158 ^@ http://purl.uniprot.org/uniprot/G3UY92 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hnrnpll ^@ http://purl.uniprot.org/uniprot/Q921F4 ^@ 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 ^@ Acidic residues|||Alters RRM 1 stability. Abolishes regulation of alternative splicing.|||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.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000081610|||http://purl.uniprot.org/annotation/VSP_013290|||http://purl.uniprot.org/annotation/VSP_013291|||http://purl.uniprot.org/annotation/VSP_026132|||http://purl.uniprot.org/annotation/VSP_026133 http://togogenome.org/gene/10090:Adm2 ^@ http://purl.uniprot.org/uniprot/Q7TNK8 ^@ Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Disulfide Bond|||Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Adrenomedullin-2|||Disordered|||Intermedin-short|||Tyrosine amide ^@ http://purl.uniprot.org/annotation/PRO_0000000980|||http://purl.uniprot.org/annotation/PRO_0000000981|||http://purl.uniprot.org/annotation/PRO_0000000982 http://togogenome.org/gene/10090:Sh3glb2 ^@ http://purl.uniprot.org/uniprot/A2AWI7|||http://purl.uniprot.org/uniprot/A2AWI9|||http://purl.uniprot.org/uniprot/B0LDS3|||http://purl.uniprot.org/uniprot/Q8R3V5 ^@ 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 ^@ BAR|||Endophilin-B2|||In isoform 1.|||In isoform 3.|||Membrane-binding amphipathic helix|||N-acetylmethionine|||Phosphoserine|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000146756|||http://purl.uniprot.org/annotation/VSP_009280|||http://purl.uniprot.org/annotation/VSP_028795 http://togogenome.org/gene/10090:Gramd4 ^@ http://purl.uniprot.org/uniprot/D3YUE7|||http://purl.uniprot.org/uniprot/Q5U4C7|||http://purl.uniprot.org/uniprot/Q8CB44 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Transmembrane ^@ Basic residues|||Disordered|||GRAM|||GRAM domain-containing protein 4|||Helical|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000328743 http://togogenome.org/gene/10090:Vmn1r214 ^@ http://purl.uniprot.org/uniprot/Q8R279 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Snx31 ^@ http://purl.uniprot.org/uniprot/Q6P8Y7 ^@ 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.|||PX|||Sorting nexin-31 ^@ http://purl.uniprot.org/annotation/PRO_0000331604|||http://purl.uniprot.org/annotation/VSP_033263 http://togogenome.org/gene/10090:Pnkp ^@ http://purl.uniprot.org/uniprot/E9Q9A5|||http://purl.uniprot.org/uniprot/G5E8N7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||PNK FHA ^@ http://togogenome.org/gene/10090:Magix ^@ http://purl.uniprot.org/uniprot/Q3TZ57|||http://purl.uniprot.org/uniprot/Q4KL35 ^@ 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 ^@ Basic and acidic residues|||Disordered|||PDZ|||PDZ domain-containing protein MAGIX|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000310543 http://togogenome.org/gene/10090:Dennd1a ^@ http://purl.uniprot.org/uniprot/Q8K382 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Clathrin box|||DENN domain-containing protein 1A|||Disordered|||FXDXF motif|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000242681 http://togogenome.org/gene/10090:Zfp54 ^@ http://purl.uniprot.org/uniprot/E9PW05 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||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; degenerate|||C2H2-type 9|||KRAB|||Required for nuclear localization|||Zinc finger protein 54 ^@ http://purl.uniprot.org/annotation/PRO_0000446016 http://togogenome.org/gene/10090:Faim2 ^@ http://purl.uniprot.org/uniprot/Q8K097 ^@ 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_0000179088|||http://purl.uniprot.org/annotation/VSP_008994 http://togogenome.org/gene/10090:Polr1e ^@ http://purl.uniprot.org/uniprot/Q3V1B9|||http://purl.uniprot.org/uniprot/Q8K202 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ DNA-directed RNA polymerase I subunit RPA49|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000073957|||http://purl.uniprot.org/annotation/VSP_013536|||http://purl.uniprot.org/annotation/VSP_013537|||http://purl.uniprot.org/annotation/VSP_013538 http://togogenome.org/gene/10090:Maz ^@ http://purl.uniprot.org/uniprot/F8VPK3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Or5d41 ^@ http://purl.uniprot.org/uniprot/Q8VFG1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or5t5 ^@ http://purl.uniprot.org/uniprot/Q8VF14 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ppa1 ^@ http://purl.uniprot.org/uniprot/Q9D819 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ Inorganic pyrophosphatase|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000137569 http://togogenome.org/gene/10090:Fam163a ^@ http://purl.uniprot.org/uniprot/A9ZNB6|||http://purl.uniprot.org/uniprot/Q8CAA5 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Protein FAM163A ^@ http://purl.uniprot.org/annotation/PRO_0000280257 http://togogenome.org/gene/10090:Btbd6 ^@ http://purl.uniprot.org/uniprot/G5E817|||http://purl.uniprot.org/uniprot/Q8K2J9 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Signal Peptide|||Splice Variant ^@ BTB|||BTB/POZ domain-containing protein 6|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000186214|||http://purl.uniprot.org/annotation/PRO_5015091891|||http://purl.uniprot.org/annotation/VSP_061437 http://togogenome.org/gene/10090:Tmem176a ^@ http://purl.uniprot.org/uniprot/Q9DCS1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Phosphoserine|||Transmembrane protein 176A ^@ http://purl.uniprot.org/annotation/PRO_0000279873 http://togogenome.org/gene/10090:Hemk1 ^@ http://purl.uniprot.org/uniprot/Q921L7 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ MTRF1L release factor glutamine methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000157179 http://togogenome.org/gene/10090:Rbm44 ^@ http://purl.uniprot.org/uniprot/Q3V089 ^@ 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|||RNA-binding protein 44|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000294175 http://togogenome.org/gene/10090:Ncapd2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0H7|||http://purl.uniprot.org/uniprot/Q8K2Z4 ^@ 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|||Bipartite nuclear localization signal|||Condensin complex subunit 1|||Condensin complex subunit 1 C-terminal|||Condensin complex subunit 1 N-terminal|||Disordered|||In isoform 2.|||Interaction with SMC2 and SMC4|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000095036|||http://purl.uniprot.org/annotation/VSP_007246 http://togogenome.org/gene/10090:Alg14 ^@ http://purl.uniprot.org/uniprot/Q9D081 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||UDP-N-acetylglucosamine transferase subunit ALG14 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000265117 http://togogenome.org/gene/10090:Itih1 ^@ http://purl.uniprot.org/uniprot/F8WJ05|||http://purl.uniprot.org/uniprot/Q61702 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Aspartate 1-(chondroitin 4-sulfate)-ester|||Inter-alpha-trypsin inhibitor heavy chain H1|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphothreonine|||S-linked (Hex...) cysteine|||VIT|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000016509|||http://purl.uniprot.org/annotation/PRO_0000016510|||http://purl.uniprot.org/annotation/PRO_0000016511|||http://purl.uniprot.org/annotation/PRO_5003379624 http://togogenome.org/gene/10090:Ankrd54 ^@ http://purl.uniprot.org/uniprot/A7YB12|||http://purl.uniprot.org/uniprot/Q91WK7 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Accumulation within the nucleus; when associated with A-289.|||Accumulation within the nucleus; when associated with A-291.|||Ankyrin repeat domain-containing protein 54|||Disordered|||Increases the cytoplasmic protein content; when associated with A-98.|||Increases the cytoplasmic protein content; when associated with A-99.|||LYN-binding|||N-acetylalanine|||Nuclear export signal (NES)|||Nuclear localization signal (NLS)|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000274494 http://togogenome.org/gene/10090:Vmn1r225 ^@ http://purl.uniprot.org/uniprot/Q8R2A5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:M6pr ^@ http://purl.uniprot.org/uniprot/P24668|||http://purl.uniprot.org/uniprot/Q3UKQ5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cation-dependent mannose-6-phosphate receptor|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||MRH|||MRH domain-containing protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000019227|||http://purl.uniprot.org/annotation/PRO_5014309143 http://togogenome.org/gene/10090:Tmsb15b2 ^@ http://purl.uniprot.org/uniprot/A2AF31 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Capn5 ^@ http://purl.uniprot.org/uniprot/O08688|||http://purl.uniprot.org/uniprot/Q3TPL4|||http://purl.uniprot.org/uniprot/Q3UTF3 ^@ 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|||Region|||Sequence Variant ^@ C2|||Calpain catalytic|||Calpain-5|||Domain III ^@ http://purl.uniprot.org/annotation/PRO_0000207714 http://togogenome.org/gene/10090:Chchd3 ^@ http://purl.uniprot.org/uniprot/Q9CRB9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||Loss of SAMM50-binding. Reduced affinity toward OPA1. No effect on IMMT-binding.|||MICOS complex subunit Mic19|||N-myristoyl glycine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000129164 http://togogenome.org/gene/10090:Unc93a2 ^@ http://purl.uniprot.org/uniprot/B2RWK3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Hgf ^@ http://purl.uniprot.org/uniprot/Q08048|||http://purl.uniprot.org/uniprot/Q8C9G5 ^@ 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|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Apple|||Hepatocyte growth factor|||Hepatocyte growth factor alpha chain|||Hepatocyte growth factor beta chain|||In isoform NK1.|||In isoform Short.|||Interchain (between alpha and beta chains)|||Kringle|||Kringle 1|||Kringle 2|||Kringle 3|||Kringle 4|||N-linked (GlcNAc...) asparagine|||PAN|||Peptidase S1|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000028093|||http://purl.uniprot.org/annotation/PRO_0000028094|||http://purl.uniprot.org/annotation/PRO_5004307367|||http://purl.uniprot.org/annotation/VSP_005408|||http://purl.uniprot.org/annotation/VSP_044345|||http://purl.uniprot.org/annotation/VSP_044346 http://togogenome.org/gene/10090:Snw1 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1E2|||http://purl.uniprot.org/uniprot/Q3TM37|||http://purl.uniprot.org/uniprot/Q9CSN1|||http://purl.uniprot.org/uniprot/Q9CV75 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region ^@ 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_0000084828 http://togogenome.org/gene/10090:Lrrc8d ^@ http://purl.uniprot.org/uniprot/Q8BGR2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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|||Phosphoserine|||Polar residues|||Volume-regulated anion channel subunit LRRC8D ^@ http://purl.uniprot.org/annotation/PRO_0000084494 http://togogenome.org/gene/10090:Ska3 ^@ http://purl.uniprot.org/uniprot/Q8C263 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Spindle and kinetochore-associated protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000089879 http://togogenome.org/gene/10090:Pcdh11x ^@ http://purl.uniprot.org/uniprot/B1AZR7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Cadherin|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5002760036 http://togogenome.org/gene/10090:Zranb3 ^@ http://purl.uniprot.org/uniprot/Q6NZP1|||http://purl.uniprot.org/uniprot/Q8BUI4|||http://purl.uniprot.org/uniprot/Q9D3Z7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ APIM motif|||Basic and acidic residues|||DEAH box|||DNA annealing helicase activity|||DNA annealing helicase and endonuclease ZRANB3|||Disordered|||Endonuclease activity|||HNH|||Helicase ATP-binding|||Helicase C-terminal|||PIP-box|||RanBP2-type ^@ http://purl.uniprot.org/annotation/PRO_0000278183 http://togogenome.org/gene/10090:Lrrc24 ^@ http://purl.uniprot.org/uniprot/Q8BHA1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000231597 http://togogenome.org/gene/10090:Kif17 ^@ http://purl.uniprot.org/uniprot/A2AM72|||http://purl.uniprot.org/uniprot/Q99PW8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region ^@ Abolishes interaction with APBA1. Abolishes transport of vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules.|||Basic and acidic residues|||Disordered|||Kinesin motor|||Kinesin-like protein KIF17|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000125451 http://togogenome.org/gene/10090:Or10g9 ^@ http://purl.uniprot.org/uniprot/Q8VH10 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp335 ^@ http://purl.uniprot.org/uniprot/A2A5K6|||http://purl.uniprot.org/uniprot/Q6P5F4 ^@ 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 ^@ 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)|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger protein 335 ^@ http://purl.uniprot.org/annotation/PRO_0000419259 http://togogenome.org/gene/10090:Adam4 ^@ http://purl.uniprot.org/uniprot/Q8CGQ2 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Disintegrin|||EGF-like|||Helical|||Peptidase M12B ^@ http://purl.uniprot.org/annotation/PRO_5015099106 http://togogenome.org/gene/10090:Slc2a4 ^@ http://purl.uniprot.org/uniprot/P14142 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||Interaction with SRFBP1|||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_0000050364 http://togogenome.org/gene/10090:Ankrd9 ^@ http://purl.uniprot.org/uniprot/Q8BH83 ^@ Chain|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Motif|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000066904 http://togogenome.org/gene/10090:Sst ^@ http://purl.uniprot.org/uniprot/P60041|||http://purl.uniprot.org/uniprot/Q545V6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide ^@ Antrin|||Neuronostatin|||Somatostatin-14|||Somatostatin-28|||Somatostatin/Cortistatin C-terminal|||Somatostatin/Cortistatin C-terminal domain-containing protein|||Threonine amide ^@ http://purl.uniprot.org/annotation/PRO_0000033092|||http://purl.uniprot.org/annotation/PRO_0000033093|||http://purl.uniprot.org/annotation/PRO_0000033094|||http://purl.uniprot.org/annotation/PRO_0000033095|||http://purl.uniprot.org/annotation/PRO_0000447377|||http://purl.uniprot.org/annotation/PRO_5014309635 http://togogenome.org/gene/10090:ccdc198 ^@ http://purl.uniprot.org/uniprot/Q9CPZ1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Affects the subcellular localization. Detected in the nucleus.|||Basic and acidic residues|||Disordered|||Factor associated with metabolism and energy|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089914 http://togogenome.org/gene/10090:Slc22a20 ^@ http://purl.uniprot.org/uniprot/Q80UJ1 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Solute carrier family 22 member 20 ^@ http://purl.uniprot.org/annotation/PRO_0000220512 http://togogenome.org/gene/10090:Lce1b ^@ http://purl.uniprot.org/uniprot/Q9D149 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Grm2 ^@ http://purl.uniprot.org/uniprot/Q14BI2 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||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|||Important for interaction with HTR2A|||Metabotropic glutamate receptor 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000306249 http://togogenome.org/gene/10090:Dpm1 ^@ http://purl.uniprot.org/uniprot/O70152 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Dolichol-phosphate mannosyltransferase subunit 1|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000059171 http://togogenome.org/gene/10090:Prl2c5 ^@ http://purl.uniprot.org/uniprot/Q9JLV9 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prolactin-2C5 ^@ http://purl.uniprot.org/annotation/PRO_5008180054|||http://purl.uniprot.org/annotation/VSP_058802 http://togogenome.org/gene/10090:Mlf1 ^@ http://purl.uniprot.org/uniprot/Q3V042|||http://purl.uniprot.org/uniprot/Q8JZS2|||http://purl.uniprot.org/uniprot/Q9QWV4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 70% reduction in binding to YWHAZ and increased nuclear localization.|||Basic and acidic residues|||Disordered|||Interaction with COPS3|||Myeloid leukemia factor 1|||No effect on binding to YWHAZ.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000220753 http://togogenome.org/gene/10090:Or8c17 ^@ http://purl.uniprot.org/uniprot/L7N210 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H2ac15 ^@ http://purl.uniprot.org/uniprot/Q8CGP7 ^@ Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region ^@ 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-K|||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_0000227509 http://togogenome.org/gene/10090:Gsx1 ^@ http://purl.uniprot.org/uniprot/B2RQ55|||http://purl.uniprot.org/uniprot/P31315 ^@ 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|||GS homeobox 1|||Homeobox|||SNAG domain ^@ http://purl.uniprot.org/annotation/PRO_0000048895 http://togogenome.org/gene/10090:Ccdc103 ^@ http://purl.uniprot.org/uniprot/Q9D9P2 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Coiled-coil domain-containing protein 103 ^@ http://purl.uniprot.org/annotation/PRO_0000263637 http://togogenome.org/gene/10090:Rnf10 ^@ http://purl.uniprot.org/uniprot/D3Z1N2|||http://purl.uniprot.org/uniprot/H7BX06|||http://purl.uniprot.org/uniprot/Q3UIW5 ^@ 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|||Disordered|||E3 ubiquitin-protein ligase RNF10|||In isoform 2.|||Phosphoserine|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000259586|||http://purl.uniprot.org/annotation/VSP_021479|||http://purl.uniprot.org/annotation/VSP_021480|||http://purl.uniprot.org/annotation/VSP_021481 http://togogenome.org/gene/10090:Vps8 ^@ http://purl.uniprot.org/uniprot/D3YUP0|||http://purl.uniprot.org/uniprot/Q0P5W1 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||RING-type|||RING-type; atypical|||Vacuolar protein sorting-associated protein 8 homolog|||WD ^@ http://purl.uniprot.org/annotation/PRO_0000278268|||http://purl.uniprot.org/annotation/VSP_023252|||http://purl.uniprot.org/annotation/VSP_023253|||http://purl.uniprot.org/annotation/VSP_023254|||http://purl.uniprot.org/annotation/VSP_023255 http://togogenome.org/gene/10090:Atp11b ^@ http://purl.uniprot.org/uniprot/Q6DFW5 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Helical|||Phospholipid-transporting ATPase IF ^@ http://purl.uniprot.org/annotation/PRO_0000452279 http://togogenome.org/gene/10090:Cactin ^@ http://purl.uniprot.org/uniprot/A1L013|||http://purl.uniprot.org/uniprot/Q9CS00 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Splicing factor Cactin|||Splicing factor Cactin C-terminal|||Splicing factor cactin central ^@ http://purl.uniprot.org/annotation/PRO_0000231618 http://togogenome.org/gene/10090:Nppa ^@ http://purl.uniprot.org/uniprot/P05125 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Abolishes maturation and cleavage by CORIN.|||Atrial natriuretic peptide|||Atriopeptin-1|||Atriopeptin-2|||Atriopeptin-3|||Auriculin-A|||Auriculin-B|||Auriculin-C|||Auriculin-D|||Cleavage; by CORIN|||Cleavage; by MME|||Disordered|||Does not affect maturation and cleavage by CORIN.|||Important for degradation of atrial natriuretic peptide by IDE|||Kaliuretic peptide|||Long-acting natriuretic peptide|||Natriuretic peptides A|||Phosphoserine|||Urodilatin|||Vessel dilator ^@ http://purl.uniprot.org/annotation/PRO_0000001495|||http://purl.uniprot.org/annotation/PRO_0000001496|||http://purl.uniprot.org/annotation/PRO_0000001497|||http://purl.uniprot.org/annotation/PRO_0000001498|||http://purl.uniprot.org/annotation/PRO_0000001499|||http://purl.uniprot.org/annotation/PRO_0000391784|||http://purl.uniprot.org/annotation/PRO_0000449735|||http://purl.uniprot.org/annotation/PRO_0000449736|||http://purl.uniprot.org/annotation/PRO_0000449737|||http://purl.uniprot.org/annotation/PRO_0000449738|||http://purl.uniprot.org/annotation/PRO_0000449739|||http://purl.uniprot.org/annotation/PRO_0000449740|||http://purl.uniprot.org/annotation/PRO_0000449741|||http://purl.uniprot.org/annotation/PRO_0000449742|||http://purl.uniprot.org/annotation/PRO_0000449743 http://togogenome.org/gene/10090:Cnot4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1K1|||http://purl.uniprot.org/uniprot/E9QA19|||http://purl.uniprot.org/uniprot/Q05BG1|||http://purl.uniprot.org/uniprot/Q3TMD4|||http://purl.uniprot.org/uniprot/Q8BT14 ^@ 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|||Turn|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Asymmetric dimethylarginine|||C3H1-type|||CCR4-NOT transcription complex subunit 4|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RING-type|||RING-type; degenerate|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081680|||http://purl.uniprot.org/annotation/VSP_009930|||http://purl.uniprot.org/annotation/VSP_009931 http://togogenome.org/gene/10090:Ndst3 ^@ http://purl.uniprot.org/uniprot/D3YXE5|||http://purl.uniprot.org/uniprot/E9PZJ4|||http://purl.uniprot.org/uniprot/Q9EQH7 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3|||Cytoplasmic|||For sulfotransferase activity|||Helical|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate N-deacetylase 3|||Heparan sulfate N-sulfotransferase 3|||Heparan sulphate-N-deacetylase|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Sulfotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000225660|||http://purl.uniprot.org/annotation/VSP_017407|||http://purl.uniprot.org/annotation/VSP_017408|||http://purl.uniprot.org/annotation/VSP_017409 http://togogenome.org/gene/10090:Onecut1 ^@ http://purl.uniprot.org/uniprot/O08755 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Strand ^@ Basic residues|||CUT|||Disordered|||Hepatocyte nuclear factor 6|||Homeobox|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000202403 http://togogenome.org/gene/10090:Ube2q2 ^@ http://purl.uniprot.org/uniprot/D3Z647|||http://purl.uniprot.org/uniprot/Q8K2Z8 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||In isoform 2.|||In strain: FVB/N.|||Polar residues|||UBC core|||Ubiquitin-conjugating enzyme E2 Q2 ^@ http://purl.uniprot.org/annotation/PRO_0000223880|||http://purl.uniprot.org/annotation/VSP_017300 http://togogenome.org/gene/10090:Ap3s2 ^@ http://purl.uniprot.org/uniprot/Q6PAL3|||http://purl.uniprot.org/uniprot/Q8BSZ2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ AP complex mu/sigma subunit|||AP-3 complex subunit sigma-2 ^@ http://purl.uniprot.org/annotation/PRO_0000193818 http://togogenome.org/gene/10090:Sgms1 ^@ http://purl.uniprot.org/uniprot/Q8VCQ6 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||Phosphatidylcholine:ceramide cholinephosphotransferase 1|||Phosphoserine|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000221069|||http://purl.uniprot.org/annotation/VSP_027225|||http://purl.uniprot.org/annotation/VSP_027226|||http://purl.uniprot.org/annotation/VSP_050673 http://togogenome.org/gene/10090:Abitram ^@ http://purl.uniprot.org/uniprot/Q80ZQ9 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein Abitram ^@ http://purl.uniprot.org/annotation/PRO_0000291929 http://togogenome.org/gene/10090:Cts8 ^@ http://purl.uniprot.org/uniprot/Q9JI81 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cathepsin 8|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000442172|||http://purl.uniprot.org/annotation/PRO_5008452492 http://togogenome.org/gene/10090:Tctn3 ^@ http://purl.uniprot.org/uniprot/Q8R2Q6 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Tectonic-3 ^@ http://purl.uniprot.org/annotation/PRO_0000229802|||http://purl.uniprot.org/annotation/VSP_017767|||http://purl.uniprot.org/annotation/VSP_017768|||http://purl.uniprot.org/annotation/VSP_017769|||http://purl.uniprot.org/annotation/VSP_017770 http://togogenome.org/gene/10090:Svs5 ^@ http://purl.uniprot.org/uniprot/P30933|||http://purl.uniprot.org/uniprot/Q545K7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Disordered|||Polar residues|||Seminal vesicle secretory protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000022454|||http://purl.uniprot.org/annotation/PRO_5014309569 http://togogenome.org/gene/10090:Calb1 ^@ http://purl.uniprot.org/uniprot/P12658 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Calbindin|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||Interaction with RANBP9|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073473 http://togogenome.org/gene/10090:Rabl2 ^@ http://purl.uniprot.org/uniprot/E9Q9D5 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In Mot; male sterility characterized by reduced sperm output, and sperm with aberrant motility and short tails.|||In isoform 1.|||In isoform 3.|||Rab-like protein 2A ^@ http://purl.uniprot.org/annotation/PRO_0000424709|||http://purl.uniprot.org/annotation/VSP_053487|||http://purl.uniprot.org/annotation/VSP_053488|||http://purl.uniprot.org/annotation/VSP_053489 http://togogenome.org/gene/10090:Fos ^@ http://purl.uniprot.org/uniprot/P01101 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region ^@ Almost no EGF-mediated phosphorylation, greatly reduced cellular transformation, and reduced AP1 activity by 20%; when associated with A-325. No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-325;and A-374.|||Almost no EGF-mediated phosphorylation, greatly reduced cellular transformation, and reduced AP1 activity by 20%; when associated with A-331. No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-331 and A-374.|||Basic motif; required for the activation of phospholipid synthesis, but not for CDS1-binding|||Complete loss of activation of phospholipid synthesis. No effect on CDS1-binding.|||Disordered|||Disrupts interaction with SMARCB1, SMARCD1, ARID1A and JUN.|||Enhanced EGF- and RSK-mediated transformation; when associated with D-362.|||Enhanced EGF- and RSK-mediated transformation; when associated with D-374.|||Enhanced EGF- and RSK-mediated transformation; when associated with E-362.|||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 enhancement of EGF- and RSK-mediated transformation; when associated with E-374.|||Leucine-zipper|||No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-232; A-325 and A-331.|||No effect on PDGF-stimulated enhancement of transcriptional activity. Completely abolishes PDGF-stimulated enhancement of transcriptional activity; when associated with A-325; A-331 and A-374.|||No effect on activation of phospholipid synthesis, nor on CDS1-binding.|||No effect on activation of phospholipid synthesis.|||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|||Reduced phosphorylation by ERK.|||Reduced phosphorylation by ERK. Reduced AP1 activity by 65%.|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076467 http://togogenome.org/gene/10090:Kit ^@ http://purl.uniprot.org/uniprot/P05532 ^@ 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 PIK3R1.|||Abolishes interaction with PTPN11/SHP-2.|||Abolishes interaction with PTPN6/SHP-1.|||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 W37; impaired protein stability and loss of kinase activity.|||In W41; decreased kinase activity.|||In W42; loss of kinase activity and impaired internalization after exposure to KITLG/SCF.|||In Wv.|||In isoform 2.|||In isoform 3.|||Loss-of-function mutation abolishing ligand binding.|||Mast/stem cell growth factor receptor Kit|||Mice display white fur, hearing loss, anemia and mast cell deficiency, plus sterility in both males and females.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKC/PRKCA|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000016755|||http://purl.uniprot.org/annotation/VSP_041868|||http://purl.uniprot.org/annotation/VSP_041869|||http://purl.uniprot.org/annotation/VSP_041870 http://togogenome.org/gene/10090:Armcx5 ^@ http://purl.uniprot.org/uniprot/Q3UZB0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||Armadillo repeat-containing X-linked protein 5|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000191373 http://togogenome.org/gene/10090:Fthl17c ^@ http://purl.uniprot.org/uniprot/A2AHC6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ferritin-like diiron ^@ http://togogenome.org/gene/10090:Sppl2b ^@ http://purl.uniprot.org/uniprot/Q3TD49 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||PA|||PAL|||Signal peptide peptidase-like 2B ^@ http://purl.uniprot.org/annotation/PRO_0000236076|||http://purl.uniprot.org/annotation/VSP_018571|||http://purl.uniprot.org/annotation/VSP_018572 http://togogenome.org/gene/10090:Ppp2r2d ^@ http://purl.uniprot.org/uniprot/Q925E7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ 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_0000071434 http://togogenome.org/gene/10090:Slc49a4 ^@ http://purl.uniprot.org/uniprot/Q8BFQ6 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Di-leucine motif; mediates lysosomal localization|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Solute carrier family 49 member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000271339 http://togogenome.org/gene/10090:Lman2 ^@ http://purl.uniprot.org/uniprot/Q9DBH5 ^@ 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_0000017667 http://togogenome.org/gene/10090:Psmb1 ^@ http://purl.uniprot.org/uniprot/O09061 ^@ Chain|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Secondary Structure|||Strand|||Turn ^@ Chain|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Strand|||Turn ^@ N-acetylmethionine|||N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphotyrosine|||Proteasome subunit beta type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000148031|||http://purl.uniprot.org/annotation/PRO_0000259624 http://togogenome.org/gene/10090:Or6c214 ^@ http://purl.uniprot.org/uniprot/Q8VGI9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Esp6 ^@ http://purl.uniprot.org/uniprot/A8R0U0 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015086687 http://togogenome.org/gene/10090:Gkap1 ^@ http://purl.uniprot.org/uniprot/Q9JMB0 ^@ 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 ^@ Affects phosphorylation by PKG.|||Disordered|||Does not affect phosphorylation by PKG.|||G kinase-anchoring protein 1|||Interaction with IRS1|||Phosphoserine|||Phosphoserine; by PKG|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315655 http://togogenome.org/gene/10090:Calm1 ^@ http://purl.uniprot.org/uniprot/P0DP26|||http://purl.uniprot.org/uniprot/P0DP27|||http://purl.uniprot.org/uniprot/P0DP28|||http://purl.uniprot.org/uniprot/Q3UKW2 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand ^@ Calmodulin-1|||Calmodulin-2|||Calmodulin-3|||Decreases interaction with SCN8A in the absence of calcium.|||Disordered|||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|||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_0000439935|||http://purl.uniprot.org/annotation/PRO_0000439936|||http://purl.uniprot.org/annotation/PRO_0000439937 http://togogenome.org/gene/10090:Wnt10a ^@ http://purl.uniprot.org/uniprot/P70701 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Phosphothreonine|||Protein Wnt-10a ^@ http://purl.uniprot.org/annotation/PRO_0000041461 http://togogenome.org/gene/10090:Cyth2 ^@ http://purl.uniprot.org/uniprot/P63034|||http://purl.uniprot.org/uniprot/Q99KH2 ^@ 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 phosphatidylinositol 3,4,5-trisphosphate binding.|||C-terminal autoinhibitory region|||Cytohesin-2|||In isoform 2.|||In isoform 3.|||Increased phosphatidylinositol 3,4,5-trisphosphate binding.|||PH|||SEC7|||Strongly reduces phosphatidylinositol 3,4,5-trisphosphate binding. ^@ http://purl.uniprot.org/annotation/PRO_0000120198|||http://purl.uniprot.org/annotation/VSP_006037|||http://purl.uniprot.org/annotation/VSP_006038 http://togogenome.org/gene/10090:Pitx3 ^@ http://purl.uniprot.org/uniprot/O35160 ^@ Chain|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||DNA Binding|||Modified Residue|||Motif|||Region ^@ Disordered|||Homeobox|||Nuclear localization signal|||OAR|||Phosphoserine|||Pituitary homeobox 3 ^@ http://purl.uniprot.org/annotation/PRO_0000049230 http://togogenome.org/gene/10090:Tdpoz4 ^@ http://purl.uniprot.org/uniprot/Q6YCH2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ BTB|||MATH|||TD and POZ domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000191626 http://togogenome.org/gene/10090:Vmn2r50 ^@ http://purl.uniprot.org/uniprot/E9PW61 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245427 http://togogenome.org/gene/10090:Ngb ^@ http://purl.uniprot.org/uniprot/Q3USR6|||http://purl.uniprot.org/uniprot/Q5ZPR7|||http://purl.uniprot.org/uniprot/Q9ER97 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Globin|||Globin family profile|||Improved binding of dioxygen and carbon monoxide to the iron atom.|||Neuroglobin|||distal binding residue|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000053392 http://togogenome.org/gene/10090:Ctsg ^@ http://purl.uniprot.org/uniprot/P28293|||http://purl.uniprot.org/uniprot/Q059V7 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cathepsin G|||Charge relay system|||Important for antimicrobial activity|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027514|||http://purl.uniprot.org/annotation/PRO_0000027515|||http://purl.uniprot.org/annotation/PRO_5014306677 http://togogenome.org/gene/10090:A2m ^@ http://purl.uniprot.org/uniprot/Q6GQT1 ^@ Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Alpha-2-macroglobulin-P|||Bait region|||Interchain (with C-284)|||Interchain (with C-437)|||Isoglutamyl cysteine thioester (Cys-Gln)|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000271402 http://togogenome.org/gene/10090:B4galt6 ^@ http://purl.uniprot.org/uniprot/Q3UUA9|||http://purl.uniprot.org/uniprot/Q9WVK5 ^@ 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|||Topological Domain|||Transmembrane ^@ Beta-1,4-galactosyltransferase 6|||Cytoplasmic|||Galactosyltransferase C-terminal|||Galactosyltransferase N-terminal|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000080548 http://togogenome.org/gene/10090:Zfp575 ^@ http://purl.uniprot.org/uniprot/B2RX29|||http://purl.uniprot.org/uniprot/Q3TXZ1 ^@ 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|||C2H2-type 5|||C2H2-type 6|||Disordered|||Zinc finger protein 575 ^@ http://purl.uniprot.org/annotation/PRO_0000047666 http://togogenome.org/gene/10090:Sult3a2 ^@ http://purl.uniprot.org/uniprot/G5E904 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Clec4a3 ^@ http://purl.uniprot.org/uniprot/Q8JZX6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Hacd4 ^@ http://purl.uniprot.org/uniprot/A2AKM2 ^@ Active Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 4 ^@ http://purl.uniprot.org/annotation/PRO_0000313731|||http://purl.uniprot.org/annotation/VSP_030124 http://togogenome.org/gene/10090:Zfp944 ^@ http://purl.uniprot.org/uniprot/E9PUS4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Inmt ^@ http://purl.uniprot.org/uniprot/P40936 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Indolethylamine N-methyltransferase|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000159713 http://togogenome.org/gene/10090:Ehhadh ^@ http://purl.uniprot.org/uniprot/Q9DBM2 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ 3-hydroxyacyl-CoA dehydrogenase|||Enoyl-CoA hydratase / isomerase|||Important for catalytic activity|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Peroxisomal bifunctional enzyme|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000109248 http://togogenome.org/gene/10090:Defa36 ^@ http://purl.uniprot.org/uniprot/K9J724 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Mammalian defensins ^@ http://purl.uniprot.org/annotation/PRO_5015096006 http://togogenome.org/gene/10090:Or4f62 ^@ http://purl.uniprot.org/uniprot/Q7TQW6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kank4 ^@ http://purl.uniprot.org/uniprot/Q6P9J5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||KN motif and ankyrin repeat domain-containing protein 4|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000244365 http://togogenome.org/gene/10090:Kcnj16 ^@ http://purl.uniprot.org/uniprot/Q9Z307 ^@ Chain|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Modified Residue|||Motif|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Inward rectifier potassium channel 16|||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_0000154976 http://togogenome.org/gene/10090:Epdr1 ^@ http://purl.uniprot.org/uniprot/Q99M71 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ In isoform 2.|||Mammalian ependymin-related protein 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000322976|||http://purl.uniprot.org/annotation/VSP_031977 http://togogenome.org/gene/10090:Tnfaip3 ^@ http://purl.uniprot.org/uniprot/Q3TBB9|||http://purl.uniprot.org/uniprot/Q60769|||http://purl.uniprot.org/uniprot/Q7TQD1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ A20-type|||A20-type 1|||A20-type 2|||A20-type 3|||A20-type 4|||A20-type 5|||A20-type 6|||A20-type 7|||Disordered|||Interaction with RIPK1|||Interaction with TNIP1|||Interaction with ubiquitin|||Loss of deubiquitinating activity, does not disassemble TRAF6:UBE2N ubiquitin ligase complex, abolioshes TAX1BP1 interaction with UBE2N.|||Loss of deubiquitinating activity.|||N-acetylalanine|||Nucleophile|||OTU|||Phosphoserine|||Proton acceptor|||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|||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_0000188793 http://togogenome.org/gene/10090:Rps6kb1 ^@ http://purl.uniprot.org/uniprot/Q3UXD8|||http://purl.uniprot.org/uniprot/Q8BSK8|||http://purl.uniprot.org/uniprot/Q8C3J7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ AGC-kinase C-terminal|||Acidic residues|||Autoinhibitory domain|||Disordered|||In isoform Alpha II.|||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_0000024344|||http://purl.uniprot.org/annotation/VSP_018840 http://togogenome.org/gene/10090:Rbmxl2 ^@ http://purl.uniprot.org/uniprot/Q9DAE2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Pro residues|||RRM ^@ http://togogenome.org/gene/10090:Ampd3 ^@ http://purl.uniprot.org/uniprot/O08739 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ AMP deaminase 3|||Disordered|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000194411 http://togogenome.org/gene/10090:Fmo5 ^@ http://purl.uniprot.org/uniprot/P97872|||http://purl.uniprot.org/uniprot/Q3TRA1 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Transmembrane ^@ Dimethylated arginine|||Flavin-containing monooxygenase 5|||Helical|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000147666 http://togogenome.org/gene/10090:Rtn4rl2 ^@ http://purl.uniprot.org/uniprot/Q7M6Z0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||GPI-anchor amidated glycine|||Important for interaction with MAG|||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_0000046050|||http://purl.uniprot.org/annotation/PRO_0000046051 http://togogenome.org/gene/10090:Gm15107 ^@ http://purl.uniprot.org/uniprot/B1B0X0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rsad2 ^@ http://purl.uniprot.org/uniprot/Q8CBB9 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N6-acetyllysine|||Radical SAM core|||S-adenosylmethionine-dependent nucleotide dehydratase RSAD2 ^@ http://purl.uniprot.org/annotation/PRO_0000309584 http://togogenome.org/gene/10090:Creb3l4 ^@ http://purl.uniprot.org/uniprot/Q9D2A5 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||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|||Lowers translocation to the nucleus.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Processed cyclic AMP-responsive element-binding protein 3-like protein 4|||Required for transcriptional activation|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000288081|||http://purl.uniprot.org/annotation/PRO_0000296221|||http://purl.uniprot.org/annotation/VSP_025639 http://togogenome.org/gene/10090:Timm8a1 ^@ http://purl.uniprot.org/uniprot/Q9WVA2 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Modified Residue|||Motif ^@ Mitochondrial import inner membrane translocase subunit Tim8 A|||Phosphoserine|||Twin CX3C motif ^@ http://purl.uniprot.org/annotation/PRO_0000193585 http://togogenome.org/gene/10090:Serinc5 ^@ http://purl.uniprot.org/uniprot/Q8BHJ6 ^@ 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|||Serine incorporator 5 ^@ http://purl.uniprot.org/annotation/PRO_0000330632 http://togogenome.org/gene/10090:Map2k7 ^@ http://purl.uniprot.org/uniprot/Q8CE90 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Cleavage; by anthrax lethal factor|||D domain|||DVD domain|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 7|||In isoform 2 and isoform 8.|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 7 and isoform 8.|||In isoform 5.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by MAP3K|||Phosphothreonine; by MAP3K|||Protein kinase|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000271406|||http://purl.uniprot.org/annotation/VSP_052264|||http://purl.uniprot.org/annotation/VSP_052265|||http://purl.uniprot.org/annotation/VSP_052266|||http://purl.uniprot.org/annotation/VSP_052267|||http://purl.uniprot.org/annotation/VSP_052268|||http://purl.uniprot.org/annotation/VSP_052269|||http://purl.uniprot.org/annotation/VSP_052270|||http://purl.uniprot.org/annotation/VSP_052271 http://togogenome.org/gene/10090:Or6x1 ^@ http://purl.uniprot.org/uniprot/Q8VFN6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Agtr1b ^@ http://purl.uniprot.org/uniprot/P29755|||http://purl.uniprot.org/uniprot/Q32MF7|||http://purl.uniprot.org/uniprot/Q8BU69 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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|||S-palmitoyl cysteine|||Type-1 angiotensin II receptor B ^@ http://purl.uniprot.org/annotation/PRO_0000069156 http://togogenome.org/gene/10090:Pfkl ^@ http://purl.uniprot.org/uniprot/P12382 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ ATP-dependent 6-phosphofructokinase, liver type|||C-terminal regulatory PFK domain 2|||Interdomain linker|||N-acetylalanine|||N-terminal catalytic PFK domain 1|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Removed|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000112022 http://togogenome.org/gene/10090:Gorasp1 ^@ http://purl.uniprot.org/uniprot/Q3TCN5|||http://purl.uniprot.org/uniprot/Q91X51 ^@ 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 ^@ Disordered|||Essential for interaction with GOLGA2/GM130|||GRASP|||Golgi reassembly-stacking protein 1|||N-myristoyl glycine|||PDZ GRASP-type|||PDZ GRASP-type 1|||PDZ GRASP-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087571 http://togogenome.org/gene/10090:Rhot1 ^@ http://purl.uniprot.org/uniprot/Q8BG51 ^@ 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|||EF-hand 1|||EF-hand 2|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Miro 1|||Miro 2|||Mitochondrial Rho GTPase 1|||Mitochondrial intermembrane ^@ http://purl.uniprot.org/annotation/PRO_0000239314|||http://purl.uniprot.org/annotation/VSP_019159|||http://purl.uniprot.org/annotation/VSP_019160|||http://purl.uniprot.org/annotation/VSP_019161 http://togogenome.org/gene/10090:Tubb2a ^@ http://purl.uniprot.org/uniprot/Q7TMM9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region ^@ 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|||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_0000262650 http://togogenome.org/gene/10090:Xkr4 ^@ http://purl.uniprot.org/uniprot/Q5GH67 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Transmembrane ^@ Cleavage; by caspase-3, caspase-6 and caspase-7|||Disordered|||Displays constitutive phospholipid scramblase activity.|||Helical|||In 1DA mutant; abolished cleavage by caspase, preventing phospholipid scramblase activity.|||Phosphoserine|||Polar residues|||XK-related protein 4|||XK-related protein 4, processed form ^@ http://purl.uniprot.org/annotation/PRO_0000190778|||http://purl.uniprot.org/annotation/PRO_0000453290 http://togogenome.org/gene/10090:Or2ah1 ^@ http://purl.uniprot.org/uniprot/A2ASV3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cabin1 ^@ http://purl.uniprot.org/uniprot/G3X8Q1|||http://purl.uniprot.org/uniprot/Q6PFH4|||http://purl.uniprot.org/uniprot/Q80X22 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat ^@ Acidic residues|||Basic and acidic residues|||Calcineurin-binding protein cabin-1 MEF2-binding|||Disordered|||Polar residues|||TPR ^@ http://togogenome.org/gene/10090:Dppa4 ^@ http://purl.uniprot.org/uniprot/E9PUG8|||http://purl.uniprot.org/uniprot/Q8CCG4 ^@ 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|||Developmental pluripotency-associated protein 2/4 C-terminal|||Developmental pluripotency-associated protein 4|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000239269 http://togogenome.org/gene/10090:Zkscan6 ^@ http://purl.uniprot.org/uniprot/Q810A1 ^@ 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|||Disordered|||KRAB|||Polar residues|||SCAN box|||Zinc finger protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000047341 http://togogenome.org/gene/10090:Htr3b ^@ http://purl.uniprot.org/uniprot/Q9JHJ5 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide|||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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000312290 http://togogenome.org/gene/10090:Atp6v1a ^@ http://purl.uniprot.org/uniprot/P50516 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Phosphoserine; by AMPK|||Reduces the interaction with CRYAB and MTOR.|||Significant loss in AMPK-mediated phosphorylation.|||V-type proton ATPase catalytic subunit A ^@ http://purl.uniprot.org/annotation/PRO_0000144561|||http://purl.uniprot.org/annotation/VSP_024628|||http://purl.uniprot.org/annotation/VSP_024629 http://togogenome.org/gene/10090:Psen2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1F2|||http://purl.uniprot.org/uniprot/Q3U4P5|||http://purl.uniprot.org/uniprot/Q61144 ^@ Active Site|||Chain|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||PAL|||Phosphoserine|||Presenilin-2 CTF subunit|||Presenilin-2 NTF subunit ^@ http://purl.uniprot.org/annotation/PRO_0000025607|||http://purl.uniprot.org/annotation/PRO_0000025608|||http://purl.uniprot.org/annotation/VSP_008383|||http://purl.uniprot.org/annotation/VSP_008384 http://togogenome.org/gene/10090:Mrps18a ^@ http://purl.uniprot.org/uniprot/Q99N85 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein mL66|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000030626 http://togogenome.org/gene/10090:Nkx2-6 ^@ http://purl.uniprot.org/uniprot/P43688|||http://purl.uniprot.org/uniprot/Q9CVN3 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Homeobox protein Nkx-2.6 ^@ http://purl.uniprot.org/annotation/PRO_0000048942 http://togogenome.org/gene/10090:Hsf1 ^@ http://purl.uniprot.org/uniprot/A0A075F5C6|||http://purl.uniprot.org/uniprot/A0A075F6C2|||http://purl.uniprot.org/uniprot/A0A075F882|||http://purl.uniprot.org/uniprot/A0A075F891|||http://purl.uniprot.org/uniprot/P38532|||http://purl.uniprot.org/uniprot/Q52L52 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant ^@ 9aaTAD|||D domain|||DNA-binding domain|||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|||HSF-type DNA-binding|||Heat shock factor protein 1|||Hydrophobic repeat HR-A/B|||Hydrophobic repeat HR-C|||In isoform 1.|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphoserine; by CAMK2A|||Phosphoserine; by MAPK12|||Phosphoserine; by MAPKAPK2|||Phosphoserine; by PKA|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphothreonine; by CK2|||Polar residues|||Regulatory domain|||Transactivation domain ^@ http://purl.uniprot.org/annotation/PRO_0000124568|||http://purl.uniprot.org/annotation/VSP_002416 http://togogenome.org/gene/10090:Map3k2 ^@ http://purl.uniprot.org/uniprot/G5E8L8 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PB1|||Polar residues|||Protein kinase ^@ http://togogenome.org/gene/10090:Thap1 ^@ http://purl.uniprot.org/uniprot/Q8CHW1 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Coiled-Coil|||Motif|||Zinc Finger ^@ HCFC1-binding motif (HBM)|||THAP domain-containing protein 1|||THAP-type ^@ http://purl.uniprot.org/annotation/PRO_0000068639 http://togogenome.org/gene/10090:Mfsd11 ^@ http://purl.uniprot.org/uniprot/Q8BJ51 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||UNC93-like protein MFSD11 ^@ http://purl.uniprot.org/annotation/PRO_0000305021|||http://purl.uniprot.org/annotation/VSP_028189 http://togogenome.org/gene/10090:AF067063 ^@ http://purl.uniprot.org/uniprot/O70618 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Pakap ^@ http://purl.uniprot.org/uniprot/O54931|||http://purl.uniprot.org/uniprot/Q8C9L6 ^@ 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|||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, isoform 2 and isoform 3.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 7.|||No effect on binding to RII.|||PALM2-AKAP2 fusion protein|||PKA-RII subunit binding domain|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces binding to RII. ^@ http://purl.uniprot.org/annotation/PRO_0000020657|||http://purl.uniprot.org/annotation/VSP_062023|||http://purl.uniprot.org/annotation/VSP_062024|||http://purl.uniprot.org/annotation/VSP_062025|||http://purl.uniprot.org/annotation/VSP_062026|||http://purl.uniprot.org/annotation/VSP_062027|||http://purl.uniprot.org/annotation/VSP_062028|||http://purl.uniprot.org/annotation/VSP_062029 http://togogenome.org/gene/10090:Krt26 ^@ http://purl.uniprot.org/uniprot/Q3TRJ4 ^@ 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|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type I cytoskeletal 26|||Linker 1|||Linker 12|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000312698 http://togogenome.org/gene/10090:Tbc1d16 ^@ http://purl.uniprot.org/uniprot/A2ABG4|||http://purl.uniprot.org/uniprot/Q6PFC0|||http://purl.uniprot.org/uniprot/Q8BXD8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Rab-GAP TBC ^@ http://togogenome.org/gene/10090:Nap1l3 ^@ http://purl.uniprot.org/uniprot/Q794H2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Nucleosome assembly protein 1-like 3|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000236211 http://togogenome.org/gene/10090:Trpa1 ^@ http://purl.uniprot.org/uniprot/Q8BLA8|||http://purl.uniprot.org/uniprot/V5TCP9 ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Repeat|||Site|||Topological Domain|||Transmembrane ^@ 4-hydroxyproline; transient|||ANK|||ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Almost complete loss in cinnamaldehyde or cold-evoked response.|||Alternate|||Alternate; transient; in hyperoxia; unknown whether inter- or intrachain|||Cysteine sulfenic acid (-SOH); transient; in hyperoxia|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Important decrease in cinnamaldehyde or cold-evoked response.|||Important residue for activation by the scorpion wasabi receptor toxin|||Ion transport|||Key residue for activation by the scorpion wasabi receptor toxin|||N-linked (GlcNAc...) asparagine|||Pore-forming|||Transient receptor potential cation channel subfamily A member 1|||Very important decrease in cinnamaldehyde or cold-evoked response.|||covalent|||covalent; Cys highly reactive ^@ http://purl.uniprot.org/annotation/PRO_0000215370 http://togogenome.org/gene/10090:Septin1 ^@ http://purl.uniprot.org/uniprot/D3Z3V3|||http://purl.uniprot.org/uniprot/P42209 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Disordered|||G1 motif|||G3 motif|||G4 motif|||Important for dimerization|||Phosphoserine|||Phosphoserine; by AURKB|||Phosphothreonine|||Polar residues|||Septin-1|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173514 http://togogenome.org/gene/10090:Arhgap27 ^@ http://purl.uniprot.org/uniprot/A2AB59|||http://purl.uniprot.org/uniprot/A2AKN5 ^@ 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.|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Rho GTPase-activating protein 27|||Rho-GAP|||SH3|||WW 1|||WW 2|||WW 3 ^@ http://purl.uniprot.org/annotation/PRO_0000317579|||http://purl.uniprot.org/annotation/VSP_031057 http://togogenome.org/gene/10090:Ksr1 ^@ http://purl.uniprot.org/uniprot/A0A2I3BR95|||http://purl.uniprot.org/uniprot/Q3UV75|||http://purl.uniprot.org/uniprot/Q61097 ^@ 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|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Abolishes one phosphorylation site. Decreases phosphorylation by PKA.|||Acidic residues|||Associates almost exclusively with the membrane. Loss of MAP2K2 and MAP2K2 binding and recruitment to the membrane. Loss of MAP kinase-mediated inhibition of ELK1 phosphorylation. No effect on the interaction with YWHAE.|||Constitutive targeting to the plasma membrane; when associated with A-297. No effect on interaction with MARK3. Abolishes phosphorylation by MARK3.|||Constitutive targeting to the plasma membrane; when associated with A-392.|||Decrease in MARK3 binding; when associated with A-397. No effect on interaction with MARK3.|||Decrease in MARK3 binding; when associated with A-401. Abolishes interaction with MARK3. Reduces phosphorylation of S-392 by MARK3.|||Decrease in MEK binding.|||Disordered|||Impairs interaction with BRAF and association with membrane ruffles; when associated with A-78.|||In isoform 2.|||Kinase suppressor of Ras 1|||Loss of ATP binding and reduces MAPK1 and MAPK3 phosphorylation levels. Loss of kinase activity towards MAP2K1 in vitro. Abnormal constitutive interaction with CRAF. No effect on the interaction with BRAF and MAP2K1.|||Mediates association with membranes|||No effect on ATP binding and MAPK1 and MAPK3 phosphorylation levels. No effect on the interaction with MAP2K1.|||No effect on interaction with MARK3.|||No effect on phosphorylation of S-392 by MARK3.|||No effect on the interaction with MAP2K1, MAP2K2 and YWHAE. Abolishes interaction with BRAF. Abolishes location at membrane ruffles.|||Partial decrease in MAP2K1 and MAP2K2 binding. No effect on the interaction with YWHAE.|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by MARK3|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Reduces interaction with MARK3. Reduces phosphorylation of S-392 by MARK3.|||Reduces phosphorylation of S-392 by MARK3.|||Severe decrease in MAP2K1 and MAP2K2 binding. No effect on the interaction with YWHAE. ^@ http://purl.uniprot.org/annotation/PRO_0000086230|||http://purl.uniprot.org/annotation/VSP_012232|||http://purl.uniprot.org/annotation/VSP_012233 http://togogenome.org/gene/10090:Cfap20dc ^@ http://purl.uniprot.org/uniprot/Q6P2K3 ^@ 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 CFAP20DC ^@ http://purl.uniprot.org/annotation/PRO_0000317182 http://togogenome.org/gene/10090:Gm3558 ^@ http://purl.uniprot.org/uniprot/Q5FWC9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Rsrc1 ^@ http://purl.uniprot.org/uniprot/Q9DBU6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Serine/Arginine-related protein 53 ^@ http://purl.uniprot.org/annotation/PRO_0000097497 http://togogenome.org/gene/10090:Adamts13 ^@ http://purl.uniprot.org/uniprot/A2ALB3|||http://purl.uniprot.org/uniprot/A7LM19|||http://purl.uniprot.org/uniprot/Q769J6 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ A disintegrin and metalloproteinase with thrombospondin motifs 13|||CUB 1|||CUB 2|||Cell attachment site|||Cysteine-rich|||Disintegrin|||In Adamts13S.|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc...) serine|||O-linked (Fuc...) threonine|||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_0000247512|||http://purl.uniprot.org/annotation/PRO_0000247513 http://togogenome.org/gene/10090:Hspa8 ^@ http://purl.uniprot.org/uniprot/P63017 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||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|||Heat shock cognate 71 kDa protein|||Interaction with BAG1|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||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_0000078271 http://togogenome.org/gene/10090:Eif4ebp3 ^@ http://purl.uniprot.org/uniprot/Q80VV3 ^@ Chain|||Molecule Processing|||Motif|||Region ^@ Chain|||Motif|||Region ^@ Disordered|||Eukaryotic translation initiation factor 4E-binding protein 3|||TOS motif|||YXXXXLphi motif ^@ http://purl.uniprot.org/annotation/PRO_0000190519 http://togogenome.org/gene/10090:Ube2l6 ^@ http://purl.uniprot.org/uniprot/Q9QZU9 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Glycyl thioester intermediate|||UBC core|||Ubiquitin/ISG15-conjugating enzyme E2 L6 ^@ http://purl.uniprot.org/annotation/PRO_0000082479 http://togogenome.org/gene/10090:Mfap4 ^@ http://purl.uniprot.org/uniprot/Q9D1H9 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Signal Peptide|||Splice Variant ^@ Cell attachment site|||Fibrinogen C-terminal|||In isoform 2.|||Microfibril-associated glycoprotein 4|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009135|||http://purl.uniprot.org/annotation/VSP_013482 http://togogenome.org/gene/10090:Gm5796 ^@ http://purl.uniprot.org/uniprot/E9Q7M8 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Scart2 ^@ http://purl.uniprot.org/uniprot/B3F5L4|||http://purl.uniprot.org/uniprot/B3F5L5|||http://purl.uniprot.org/uniprot/Q8C9T4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||SRCR|||SRCR domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5014312011|||http://purl.uniprot.org/annotation/PRO_5015087263|||http://purl.uniprot.org/annotation/PRO_5015087265 http://togogenome.org/gene/10090:Pou4f3 ^@ http://purl.uniprot.org/uniprot/Q63955 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Motif|||Sequence Conflict ^@ Homeobox|||POU domain, class 4, transcription factor 3|||POU-IV box|||POU-specific ^@ http://purl.uniprot.org/annotation/PRO_0000100743 http://togogenome.org/gene/10090:Slc30a6 ^@ http://purl.uniprot.org/uniprot/J3QMX8|||http://purl.uniprot.org/uniprot/Q8BJM5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Zinc transporter 6 ^@ http://purl.uniprot.org/annotation/PRO_0000312574 http://togogenome.org/gene/10090:Tbc1d15 ^@ http://purl.uniprot.org/uniprot/Q7TPU5|||http://purl.uniprot.org/uniprot/Q9CXF4 ^@ 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|||Rab-GAP TBC|||Removed|||TBC1 domain family member 15 ^@ http://purl.uniprot.org/annotation/PRO_0000208043 http://togogenome.org/gene/10090:Nbeal2 ^@ http://purl.uniprot.org/uniprot/E9Q9L6 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ BEACH|||BEACH-type PH|||Disordered|||Polar residues|||WD ^@ http://togogenome.org/gene/10090:Foxe3 ^@ http://purl.uniprot.org/uniprot/Q9QY14 ^@ 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 E3|||In dyl; negative regulation of lens epithelial cell proliferation; positive regulation of lens fiber cell differentiation; positive regulation of epithelial cell apoptotic process; loss of sequence-specific DNA binding.|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000091830 http://togogenome.org/gene/10090:Cyb5d1 ^@ http://purl.uniprot.org/uniprot/Q5NCY3 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant ^@ Cytochrome b5 domain-containing protein 1|||Cytochrome b5 heme-binding|||In isoform 2.|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000312316|||http://purl.uniprot.org/annotation/VSP_029825|||http://purl.uniprot.org/annotation/VSP_029826 http://togogenome.org/gene/10090:Eif4a1 ^@ http://purl.uniprot.org/uniprot/P60843|||http://purl.uniprot.org/uniprot/Q3TLL6|||http://purl.uniprot.org/uniprot/Q5F2A7 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ DEAD box|||DEAD-box RNA helicase Q|||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|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Q motif|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000054935 http://togogenome.org/gene/10090:Phf10 ^@ http://purl.uniprot.org/uniprot/K4DI61|||http://purl.uniprot.org/uniprot/Q9D8M7 ^@ 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|||Disordered|||Essential to induce neural progenitor proliferation|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||PHD finger protein 10|||PHD-type|||PHD-type 1; degenerate|||PHD-type 2; degenerate|||Phosphoserine|||Polar residues|||SAY ^@ http://purl.uniprot.org/annotation/PRO_0000059298|||http://purl.uniprot.org/annotation/VSP_013441 http://togogenome.org/gene/10090:Lrig1 ^@ http://purl.uniprot.org/uniprot/P70193 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||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 1|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014828 http://togogenome.org/gene/10090:Or2t48 ^@ http://purl.uniprot.org/uniprot/Q8VGD9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nudt8 ^@ http://purl.uniprot.org/uniprot/Q9CR24 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif ^@ Mitochondrial coenzyme A diphosphatase NUDT8|||N6-succinyllysine|||Nudix box|||Nudix hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000019949 http://togogenome.org/gene/10090:Ccnq ^@ http://purl.uniprot.org/uniprot/Q8QZR8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Cyclin-Q|||Disordered|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000297568 http://togogenome.org/gene/10090:Pla2g4c ^@ http://purl.uniprot.org/uniprot/Q64GA5 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Region|||Splice Variant ^@ Cytosolic phospholipase A2 gamma|||Disordered|||In isoform 2.|||Nucleophile|||PLA2c|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000440671|||http://purl.uniprot.org/annotation/VSP_058982 http://togogenome.org/gene/10090:Avil ^@ http://purl.uniprot.org/uniprot/O88398|||http://purl.uniprot.org/uniprot/Q3TBC5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Advillin|||Core|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||Gelsolin-like 6|||HP|||Headpiece|||Phosphotyrosine|||Required for interaction with F-actin ^@ http://purl.uniprot.org/annotation/PRO_0000218737 http://togogenome.org/gene/10090:Ptbp1 ^@ http://purl.uniprot.org/uniprot/P17225|||http://purl.uniprot.org/uniprot/Q8CB58 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polypyrimidine tract-binding protein 1|||RRM|||RRM 1|||RRM 2|||RRM 3|||RRM 4 ^@ http://purl.uniprot.org/annotation/PRO_0000081738|||http://purl.uniprot.org/annotation/VSP_061654 http://togogenome.org/gene/10090:Or4p8 ^@ http://purl.uniprot.org/uniprot/Q8VG47 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mrps21 ^@ http://purl.uniprot.org/uniprot/P58059 ^@ Chain|||Molecule Processing ^@ Chain ^@ Small ribosomal subunit protein bS21m ^@ http://purl.uniprot.org/annotation/PRO_0000178414 http://togogenome.org/gene/10090:Mgarp ^@ http://purl.uniprot.org/uniprot/Q8VI64 ^@ 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|||Helical; Anchor for type IV membrane protein|||Mitochondrial intermembrane|||Polar residues|||Protein MGARP ^@ http://purl.uniprot.org/annotation/PRO_0000318765 http://togogenome.org/gene/10090:Wipf2 ^@ http://purl.uniprot.org/uniprot/Q6PEV3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Asymmetric dimethylarginine|||Binds actin|||Disordered|||Polar residues|||Pro residues|||WAS/WASL-interacting protein family member 2|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000065976 http://togogenome.org/gene/10090:Prima1 ^@ http://purl.uniprot.org/uniprot/F8VQJ2|||http://purl.uniprot.org/uniprot/Q3USW1|||http://purl.uniprot.org/uniprot/Q3V3K1|||http://purl.uniprot.org/uniprot/Q810F0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decrease in ACHE tetramer recruitment to membrane rafts.|||Disordered|||Does not abolish the localization of ACHE.|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on ACHE tetramer recruitment to membrane rafts.|||No effect on ACHE tetramer recruitment to membrane rafts; when associated with 138-A--A-142.|||No effect on ACHE tetramer recruitment to membrane rafts; when associated with A-131.|||PRAD|||Polar residues|||Pro residues|||Proline-rich membrane anchor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000022108|||http://purl.uniprot.org/annotation/PRO_5003385303|||http://purl.uniprot.org/annotation/PRO_5004230290|||http://purl.uniprot.org/annotation/VSP_008496|||http://purl.uniprot.org/annotation/VSP_008497 http://togogenome.org/gene/10090:Hsp90b1 ^@ http://purl.uniprot.org/uniprot/P08113|||http://purl.uniprot.org/uniprot/Q3UAD6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Site ^@ Acidic residues|||Disordered|||Endoplasmin|||Histidine kinase/HSP90-like ATPase|||Histidine kinase/HSP90-like ATPase domain-containing protein|||Important for ATP hydrolysis|||Interchain|||Loss of CNPY3-binding.|||N-linked (GlcNAc...) asparagine|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000013599|||http://purl.uniprot.org/annotation/PRO_5010843409 http://togogenome.org/gene/10090:Bend4 ^@ http://purl.uniprot.org/uniprot/P86174 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ BEN|||BEN domain-containing protein 4|||Disordered|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000364182 http://togogenome.org/gene/10090:Prkce ^@ http://purl.uniprot.org/uniprot/P16054 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ AGC-kinase C-terminal|||C2|||Disordered|||Interaction with actin|||Loss of interaction with YWHAB and defects in the completion of cytokinesis.|||Loss of localization to the perinuclear region. Loss of translocation to the nucleus upon PMA stimulation.|||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_0000055698 http://togogenome.org/gene/10090:Msi2 ^@ http://purl.uniprot.org/uniprot/B1AT13|||http://purl.uniprot.org/uniprot/Q3TE41|||http://purl.uniprot.org/uniprot/Q920Q6 ^@ 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.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RNA-binding protein Musashi homolog 2|||RRM|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081653|||http://purl.uniprot.org/annotation/VSP_011172|||http://purl.uniprot.org/annotation/VSP_011173|||http://purl.uniprot.org/annotation/VSP_011174 http://togogenome.org/gene/10090:Cd101 ^@ http://purl.uniprot.org/uniprot/A8E0Y8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||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|||In strain: NOD/MrkTac.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000363951 http://togogenome.org/gene/10090:Gprc5d ^@ http://purl.uniprot.org/uniprot/Q0VEL2|||http://purl.uniprot.org/uniprot/Q3UUY8|||http://purl.uniprot.org/uniprot/Q9JIL6 ^@ 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|||Extracellular|||G-protein coupled receptor family C group 5 member D|||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. ^@ http://purl.uniprot.org/annotation/PRO_0000206898|||http://purl.uniprot.org/annotation/VSP_010009|||http://purl.uniprot.org/annotation/VSP_010010 http://togogenome.org/gene/10090:Cyb5b ^@ http://purl.uniprot.org/uniprot/Q9CQX2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Propeptide|||Sequence Conflict|||Transmembrane ^@ Cytochrome b5 heme-binding|||Cytochrome b5 type B|||Helical|||N6-acetyllysine|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000006473|||http://purl.uniprot.org/annotation/PRO_0000006474 http://togogenome.org/gene/10090:Nup35 ^@ http://purl.uniprot.org/uniprot/Q8R4R6 ^@ 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|||Nucleoporin NUP35|||Phosphoserine|||Phosphothreonine|||RRM Nup35-type ^@ http://purl.uniprot.org/annotation/PRO_0000234295 http://togogenome.org/gene/10090:Invs ^@ http://purl.uniprot.org/uniprot/A0JNT0|||http://purl.uniprot.org/uniprot/A2AM57|||http://purl.uniprot.org/uniprot/Q3TYB3 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ ANK|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Alms1 ^@ http://purl.uniprot.org/uniprot/A0A1D5RMI8|||http://purl.uniprot.org/uniprot/Q8K4E0 ^@ 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 ^@ 1|||10|||11|||12|||13|||14|||15|||16|||17|||17 X 47 AA approximate tandem repeat|||2|||3|||4|||5|||6|||7|||8|||9|||ALMS motif|||Acidic residues|||Basic and acidic residues|||Centrosome-associated protein ALMS1|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000225593|||http://purl.uniprot.org/annotation/VSP_017350 http://togogenome.org/gene/10090:Add2 ^@ http://purl.uniprot.org/uniprot/Q8C0Y2|||http://purl.uniprot.org/uniprot/Q9QYB8 ^@ 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|||Basic residues|||Beta-adducin|||Class II aldolase/adducin N-terminal|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with calmodulin|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000218534|||http://purl.uniprot.org/annotation/VSP_000184|||http://purl.uniprot.org/annotation/VSP_000185|||http://purl.uniprot.org/annotation/VSP_022596 http://togogenome.org/gene/10090:Smoc1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1E4|||http://purl.uniprot.org/uniprot/E9QKW2|||http://purl.uniprot.org/uniprot/Q8BLY1 ^@ 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 ^@ Disordered|||EF-hand 1|||EF-hand 2|||In isoform 2.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||SPARC-related modular calcium-binding protein 1|||Thyroglobulin type-1|||Thyroglobulin type-1 1|||Thyroglobulin type-1 2 ^@ http://purl.uniprot.org/annotation/PRO_0000020317|||http://purl.uniprot.org/annotation/PRO_5003243331|||http://purl.uniprot.org/annotation/PRO_5006452000|||http://purl.uniprot.org/annotation/VSP_008721 http://togogenome.org/gene/10090:Pi15 ^@ http://purl.uniprot.org/uniprot/A0A0R4J126|||http://purl.uniprot.org/uniprot/Q8BS03 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Peptidase inhibitor 15|||SCP ^@ http://purl.uniprot.org/annotation/PRO_0000287624|||http://purl.uniprot.org/annotation/PRO_0000287625|||http://purl.uniprot.org/annotation/PRO_5015044297 http://togogenome.org/gene/10090:Trip11 ^@ http://purl.uniprot.org/uniprot/E9Q512 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||GRIP|||Polar residues ^@ http://togogenome.org/gene/10090:Hint2 ^@ http://purl.uniprot.org/uniprot/Q5M9J2|||http://purl.uniprot.org/uniprot/Q9D0S9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Signal Peptide|||Transit Peptide ^@ Adenosine 5'-monophosphoramidase HINT2|||HIT|||Histidine triad motif|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Tele-AMP-histidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000109787|||http://purl.uniprot.org/annotation/PRO_5014309899 http://togogenome.org/gene/10090:Phf20 ^@ http://purl.uniprot.org/uniprot/Q8BLG0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ A.T hook|||Abolishes Methyllysine-binding.|||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_0000059311|||http://purl.uniprot.org/annotation/VSP_007762 http://togogenome.org/gene/10090:Tm2d1 ^@ http://purl.uniprot.org/uniprot/Q99MB3 ^@ 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 1 ^@ http://purl.uniprot.org/annotation/PRO_0000298979|||http://purl.uniprot.org/annotation/VSP_027494 http://togogenome.org/gene/10090:Slc19a2 ^@ http://purl.uniprot.org/uniprot/Q9EQN9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Essential for pyridoxine transport|||Extracellular|||Helical|||In isoform 2.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Thiamine transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000441105|||http://purl.uniprot.org/annotation/VSP_059029 http://togogenome.org/gene/10090:H2al1a ^@ http://purl.uniprot.org/uniprot/Q5M8Q2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Histone H2A-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000440627 http://togogenome.org/gene/10090:Pde8b ^@ http://purl.uniprot.org/uniprot/E9PX38|||http://purl.uniprot.org/uniprot/E9PXX4|||http://purl.uniprot.org/uniprot/E9PYP0|||http://purl.uniprot.org/uniprot/E9Q8J6|||http://purl.uniprot.org/uniprot/Q8BI47 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PAS|||PDEase|||Polar residues|||Proton donor ^@ http://togogenome.org/gene/10090:Mgat5b ^@ http://purl.uniprot.org/uniprot/Q765H6 ^@ 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 ^@ Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000288612|||http://purl.uniprot.org/annotation/VSP_025736|||http://purl.uniprot.org/annotation/VSP_025737|||http://purl.uniprot.org/annotation/VSP_025738 http://togogenome.org/gene/10090:Or14c45 ^@ http://purl.uniprot.org/uniprot/Q7TS07 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or4c107 ^@ http://purl.uniprot.org/uniprot/Q7TR08 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or5d47 ^@ http://purl.uniprot.org/uniprot/A2BHP6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cpa4 ^@ http://purl.uniprot.org/uniprot/Q6P8K8 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Carboxypeptidase A4|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004359|||http://purl.uniprot.org/annotation/PRO_0000004360 http://togogenome.org/gene/10090:Raph1 ^@ http://purl.uniprot.org/uniprot/F2Z3U3|||http://purl.uniprot.org/uniprot/G5E867 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||PH|||Polar residues|||Pro residues|||Ras-associating ^@ http://togogenome.org/gene/10090:Ngfr ^@ http://purl.uniprot.org/uniprot/Q9Z0W1 ^@ 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 ^@ Cytoplasmic|||Death|||Disordered|||Extracellular|||Helical|||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/PRO_0000034592 http://togogenome.org/gene/10090:Abca12 ^@ http://purl.uniprot.org/uniprot/E9Q876 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Transmembrane ^@ ABC transporter 1|||ABC transporter 2|||Disordered|||Glucosylceramide transporter ABCA12|||Helical|||In a mouse model for harlequin ichthyosis (HI), homozygous mice are embryonic lethal but occasionally pups are found in the first few hours after birth but die and are severely dehydrated and fail to suckle normally. Homozygous pups show hallmarks of HI desease including hyperkeratosis, abnormal extracellular lipid lamellae and defects in cornified envelope processing. At 14.5 dpc and 15.5 dpc homozygous embryos appear normal; however from 16.5 dpc onwards they are characterized by an absence of normal skin folds around the trunk and limbs. As development progressed, embryos develop a taut, thick epidermis and multiple contractures affecting the limbs. Late stage embryos are smaller.|||In a mouse model for harlequin ichthyosis (HI), smooth skin (smsk) mutant mice show a pronounced perinatal lethal skin phenotype in 25% of the offspring and newborn mutant pups die within a few hours after birth, and appear severely dehydrated with dry cracking skin. Smsk homozygous mutants embryos show a normal appearance at 14.5 dpc, but at 16.5 dpc develop a partial absence of normal skin folds around the trunk and limbs, and by 18.5 dpc develop a taut, thick skin and limb contractures.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000452550 http://togogenome.org/gene/10090:1700056E22Rik ^@ http://purl.uniprot.org/uniprot/F7CNM6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Ube2d1 ^@ http://purl.uniprot.org/uniprot/P61080|||http://purl.uniprot.org/uniprot/Q3UFQ4 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ Glycyl thioester intermediate|||UBC core|||Ubiquitin-conjugating enzyme E2 D1 ^@ http://purl.uniprot.org/annotation/PRO_0000082461 http://togogenome.org/gene/10090:Lamc3 ^@ http://purl.uniprot.org/uniprot/Q9R0B6 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Domain II and I|||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_0000017080 http://togogenome.org/gene/10090:Prr3 ^@ http://purl.uniprot.org/uniprot/E9Q601|||http://purl.uniprot.org/uniprot/Q3V0R7|||http://purl.uniprot.org/uniprot/Q811B5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Zinc Finger ^@ C3H1-type|||Disordered|||Proline-rich protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000213890 http://togogenome.org/gene/10090:Cert1 ^@ http://purl.uniprot.org/uniprot/Q9EQG9 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Ceramide transfer protein|||Disordered|||FFAT|||In isoform 2.|||In isoform 3.|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||START ^@ http://purl.uniprot.org/annotation/PRO_0000220666|||http://purl.uniprot.org/annotation/VSP_006277|||http://purl.uniprot.org/annotation/VSP_028735|||http://purl.uniprot.org/annotation/VSP_028736 http://togogenome.org/gene/10090:Mospd3 ^@ http://purl.uniprot.org/uniprot/Q05DT5|||http://purl.uniprot.org/uniprot/Q3V4A2|||http://purl.uniprot.org/uniprot/Q8BGG6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||MSP|||Motile sperm domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000213466 http://togogenome.org/gene/10090:Or8w1 ^@ http://purl.uniprot.org/uniprot/Q8VG97 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rpl39 ^@ http://purl.uniprot.org/uniprot/P62892 ^@ Chain|||Molecule Processing ^@ Chain ^@ Large ribosomal subunit protein eL39 ^@ http://purl.uniprot.org/annotation/PRO_0000127025 http://togogenome.org/gene/10090:Ccdc62 ^@ http://purl.uniprot.org/uniprot/E9PVD1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 62|||Disordered|||LXXLL motif 1|||LXXLL motif 2|||Loss of interaction with GOPC. Does not localize to the acrosome. Homozygous mutant mice are infertile and show deformed sperm with reduced motility. ^@ http://purl.uniprot.org/annotation/PRO_0000415823 http://togogenome.org/gene/10090:Trim3 ^@ http://purl.uniprot.org/uniprot/Q3TDT0|||http://purl.uniprot.org/uniprot/Q9R1R2 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Zinc Finger ^@ B box-type|||Disordered|||Filamin|||Interaction with KIF21B|||N-acetylalanine|||NHL|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||NHL 6|||Phosphoserine|||RING-type|||Removed|||Tripartite motif-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000056198 http://togogenome.org/gene/10090:Nr5a1 ^@ http://purl.uniprot.org/uniprot/P33242 ^@ 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|||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|||Turn|||Zinc Finger ^@ Abolishes ligand binding and reduces transactivation; when associated with W-270.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||In strain: C3H/HeJ and DBA/2J; does not change transcriptional activity.|||N6-acetyllysine|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine; by CDK7|||Pro residues|||Reduced lipid binding and transactivation. Abolishes ligand binding and reduces transactivation; when associated with F-345.|||Steroidogenic factor 1|||Strongly reduced transactivation.|||Strongly reduced transactivation; when associated with D-440.|||Strongly reduced transactivation; when associated with D-442. ^@ http://purl.uniprot.org/annotation/PRO_0000053732|||http://purl.uniprot.org/annotation/VSP_003715 http://togogenome.org/gene/10090:Ccdc96 ^@ http://purl.uniprot.org/uniprot/Q9CR92 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Coiled-coil domain-containing protein 96|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000234098 http://togogenome.org/gene/10090:Rpl6 ^@ http://purl.uniprot.org/uniprot/P47911|||http://purl.uniprot.org/uniprot/Q3UCH0 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL6|||Large ribosomal subunit protein uL6 N-terminal|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000171010 http://togogenome.org/gene/10090:Tgm6 ^@ http://purl.uniprot.org/uniprot/Q14CG3|||http://purl.uniprot.org/uniprot/Q8BM11 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent ^@ Transglutaminase-like ^@ http://togogenome.org/gene/10090:Fam50a ^@ http://purl.uniprot.org/uniprot/A0A158SIT3|||http://purl.uniprot.org/uniprot/Q9WV03 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Nuclear localization signal|||Protein FAM50A|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000068285 http://togogenome.org/gene/10090:Pex13 ^@ http://purl.uniprot.org/uniprot/Q9D0K1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Helical|||Interaction with PEX19|||Peroxisomal matrix|||Peroxisomal membrane protein PEX13|||Phosphoserine|||Pro residues|||SH3|||Targeting to peroxisomes ^@ http://purl.uniprot.org/annotation/PRO_0000240662 http://togogenome.org/gene/10090:Crat ^@ http://purl.uniprot.org/uniprot/P47934 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn ^@ Carnitine O-acetyltransferase|||Increases activity towards short-chain fatty acids.|||Lowers activity towards short-chain fatty acids.|||Lowers activity towards short-chain fatty acids. Strong increase in activity towards medium chain fatty acids.|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000210173 http://togogenome.org/gene/10090:Ang6 ^@ http://purl.uniprot.org/uniprot/Q5GAN0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_5015020044 http://togogenome.org/gene/10090:Rab7 ^@ http://purl.uniprot.org/uniprot/P51150 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict|||Strand|||Turn ^@ Cysteine methyl ester|||Effector region|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-acetylthreonine|||Phosphoserine|||Ras-related protein Rab-7a|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121122 http://togogenome.org/gene/10090:Acta1 ^@ http://purl.uniprot.org/uniprot/P68134 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn ^@ Actin, alpha skeletal muscle|||Actin, alpha skeletal muscle, intermediate form|||Interaction with alpha-actinin|||Methionine (R)-sulfoxide|||N-acetylcysteine; in intermediate form|||N6-malonyllysine|||N6-methyllysine|||Removed|||Tele-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000442805|||http://purl.uniprot.org/annotation/PRO_0000442806 http://togogenome.org/gene/10090:Slitrk3 ^@ http://purl.uniprot.org/uniprot/Q810B9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||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 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_0000032678 http://togogenome.org/gene/10090:Impa2 ^@ http://purl.uniprot.org/uniprot/Q91UZ5 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Inositol monophosphatase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000142521 http://togogenome.org/gene/10090:Slc7a13 ^@ http://purl.uniprot.org/uniprot/Q91WN3 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||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|||Solute carrier family 7 member 13 ^@ http://purl.uniprot.org/annotation/PRO_0000330726 http://togogenome.org/gene/10090:Pitpnm2 ^@ http://purl.uniprot.org/uniprot/Q6NS55|||http://purl.uniprot.org/uniprot/Q6ZPQ6 ^@ 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|||DDHD|||Disordered|||In isoform 2.|||Membrane-associated phosphatidylinositol transfer protein 2|||Omega-N-methylarginine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000232742|||http://purl.uniprot.org/annotation/VSP_017964 http://togogenome.org/gene/10090:Or5b119 ^@ http://purl.uniprot.org/uniprot/Q8VEV6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Noct ^@ http://purl.uniprot.org/uniprot/B2RTJ8|||http://purl.uniprot.org/uniprot/O35710 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Region|||Splice Variant|||Transit Peptide ^@ Disordered|||Endonuclease/exonuclease/phosphatase|||In isoform 2.|||Interaction with PPARG|||Mitochondrion|||Nocturnin ^@ http://purl.uniprot.org/annotation/PRO_0000218569|||http://purl.uniprot.org/annotation/VSP_016677 http://togogenome.org/gene/10090:Tas2r107 ^@ http://purl.uniprot.org/uniprot/Q7M725 ^@ 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 107 ^@ http://purl.uniprot.org/annotation/PRO_0000248252 http://togogenome.org/gene/10090:Or4f59 ^@ http://purl.uniprot.org/uniprot/Q8VF10 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Snap29 ^@ http://purl.uniprot.org/uniprot/Q9ERB0 ^@ 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|||Phosphoserine|||Synaptosomal-associated protein 29|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000213602 http://togogenome.org/gene/10090:Ect2l ^@ http://purl.uniprot.org/uniprot/F7CKP4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ DH|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Aspn ^@ http://purl.uniprot.org/uniprot/A6H6K1|||http://purl.uniprot.org/uniprot/Q99MQ4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Asporin|||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|||Partial inhibition of BMP2-induced cytodifferentiation; when associated with E-170.|||Partial inhibition of BMP2-induced cytodifferentiation; when associated with E-219.|||Rescues the inhibitory effects of ASPN on BMP2-induced cytodifferentiation. ^@ http://purl.uniprot.org/annotation/PRO_0000032729|||http://purl.uniprot.org/annotation/PRO_0000032730|||http://purl.uniprot.org/annotation/PRO_5014296998 http://togogenome.org/gene/10090:Tal1 ^@ http://purl.uniprot.org/uniprot/P22091|||http://purl.uniprot.org/uniprot/Q3TZH7 ^@ 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 ^@ BHLH|||Disordered|||Phosphoserine|||Phosphoserine; by MAPK|||Polar residues|||Pro residues|||Remains stable, even in the face of severe hypoxia.|||T-cell acute lymphocytic leukemia protein 1 homolog|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127455 http://togogenome.org/gene/10090:Dusp21 ^@ http://purl.uniprot.org/uniprot/Q9D9D8 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Region ^@ Dual specificity phosphatase 21|||Phosphocysteine intermediate|||Sufficient for mitochondrial localization|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000411986 http://togogenome.org/gene/10090:Spry2 ^@ http://purl.uniprot.org/uniprot/B2RS85|||http://purl.uniprot.org/uniprot/Q9QXV8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Abolishes FGF2-induced lens fiber differentiation via inhibition of FGF-mediated ERK1/2 phosphorylation.|||Basic and acidic residues|||Cleavage; by FAP|||Disordered|||Polar residues|||Protein sprouty homolog 2|||Required for interaction with CAV1|||Required for interaction with TESK1|||SPR ^@ http://purl.uniprot.org/annotation/PRO_0000076902 http://togogenome.org/gene/10090:Trpm4 ^@ http://purl.uniprot.org/uniprot/A0A1B0GS49|||http://purl.uniprot.org/uniprot/Q7TN37 ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Calmodulin-binding|||Cytoplasmic|||Decreased selectivity for monovalent cations and increased permeability for Ca(2+).|||Decreases channel sensitivity to inhibition by ATP.|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Ion transport|||Mediates modulation by decavanadate and PIP2-binding|||Near loss of channel sensitivity to inhibition by ATP.|||Phosphoserine|||Phosphoserine; by PKC|||Pore-forming|||Selectivity filter|||Strongly decreased selectivity for monovalent cations and increased permeability for Ca(2+).|||Strongly decreases channel sensitivity to inhibition by ATP.|||TRPM SLOG|||Transient receptor potential cation channel subfamily M member 4|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000259530|||http://purl.uniprot.org/annotation/VSP_021444|||http://purl.uniprot.org/annotation/VSP_021445 http://togogenome.org/gene/10090:Ddhd1 ^@ http://purl.uniprot.org/uniprot/E9QQ38|||http://purl.uniprot.org/uniprot/F8WHP5|||http://purl.uniprot.org/uniprot/F8WIJ5|||http://purl.uniprot.org/uniprot/Q80YA3 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ DDHD|||Disordered|||In isoform 2.|||Phospholipase DDHD1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079846|||http://purl.uniprot.org/annotation/VSP_008630 http://togogenome.org/gene/10090:Or1e1c ^@ http://purl.uniprot.org/uniprot/E9Q4M1|||http://purl.uniprot.org/uniprot/Q8VGI2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp157 ^@ http://purl.uniprot.org/uniprot/Q6PCM4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Rab3gap2 ^@ http://purl.uniprot.org/uniprot/A0A0A6YWM5|||http://purl.uniprot.org/uniprot/E9QKE4|||http://purl.uniprot.org/uniprot/Q3UEY3|||http://purl.uniprot.org/uniprot/Q8BMG7|||http://purl.uniprot.org/uniprot/Q8BYZ6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Rab3 GTPase-activating protein non-catalytic subunit|||Rab3-GAP regulatory subunit N-terminal|||Rab3GAP regulatory subunit C-terminal|||Rab3GAP regulatory subunit C-terminal domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000191663|||http://purl.uniprot.org/annotation/PRO_5004303842|||http://purl.uniprot.org/annotation/VSP_013313 http://togogenome.org/gene/10090:Fkbp1a ^@ http://purl.uniprot.org/uniprot/P26883|||http://purl.uniprot.org/uniprot/Q1JUQ8|||http://purl.uniprot.org/uniprot/Q3UKJ3 ^@ 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|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP1A ^@ http://purl.uniprot.org/annotation/PRO_0000075290 http://togogenome.org/gene/10090:Defb11 ^@ http://purl.uniprot.org/uniprot/Q8R2I7 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 11 ^@ http://purl.uniprot.org/annotation/PRO_0000006939 http://togogenome.org/gene/10090:Usp17lb ^@ http://purl.uniprot.org/uniprot/E9Q9U0 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of deubiquitinating activity.|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein B ^@ http://purl.uniprot.org/annotation/PRO_0000437666|||http://purl.uniprot.org/annotation/VSP_058560 http://togogenome.org/gene/10090:Mvk ^@ http://purl.uniprot.org/uniprot/Q3UEB4|||http://purl.uniprot.org/uniprot/Q9R008 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent ^@ GHMP kinase C-terminal|||GHMP kinase N-terminal|||Mevalonate kinase|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000156658 http://togogenome.org/gene/10090:Krt7 ^@ http://purl.uniprot.org/uniprot/Q9DCV7 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Dimethylated arginine; alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Head|||IF rod|||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_0000307635 http://togogenome.org/gene/10090:Stab1 ^@ http://purl.uniprot.org/uniprot/G3X973 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ EGF-like|||FAS1|||Helical|||Link ^@ http://purl.uniprot.org/annotation/PRO_5015091818 http://togogenome.org/gene/10090:Xlr4b ^@ http://purl.uniprot.org/uniprot/Q9JJQ7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Aldh3a1 ^@ http://purl.uniprot.org/uniprot/P47739|||http://purl.uniprot.org/uniprot/Q3UNF5 ^@ 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|||Sequence Conflict|||Sequence Variant ^@ Aldehyde dehydrogenase|||Aldehyde dehydrogenase, dimeric NADP-preferring|||In allele Ald3a1c.|||N-acetylserine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056471 http://togogenome.org/gene/10090:Dnali1 ^@ http://purl.uniprot.org/uniprot/Q8BVN8 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict ^@ Axonemal dynein light intermediate polypeptide 1|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000114677 http://togogenome.org/gene/10090:Pitpna ^@ http://purl.uniprot.org/uniprot/P53810|||http://purl.uniprot.org/uniprot/Q3TGI6|||http://purl.uniprot.org/uniprot/Q5ND42 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Strand|||Turn ^@ Disordered|||N6-acetyllysine|||Phosphatidylinositol transfer protein alpha isoform|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000191640 http://togogenome.org/gene/10090:Cdon ^@ http://purl.uniprot.org/uniprot/Q32MD9 ^@ 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 ^@ Basic and acidic residues|||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|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000234055 http://togogenome.org/gene/10090:Golm2 ^@ http://purl.uniprot.org/uniprot/E9PZJ6|||http://purl.uniprot.org/uniprot/Q6P2L7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 3.|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein GOLM2 ^@ http://purl.uniprot.org/annotation/PRO_0000291844|||http://purl.uniprot.org/annotation/VSP_026263|||http://purl.uniprot.org/annotation/VSP_026264|||http://purl.uniprot.org/annotation/VSP_026265 http://togogenome.org/gene/10090:Sat1 ^@ http://purl.uniprot.org/uniprot/P48026|||http://purl.uniprot.org/uniprot/Q3V2Q2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Strand|||Turn ^@ Diamine acetyltransferase 1|||N-acetyltransferase|||Proton donor|||Reduced activity. ^@ http://purl.uniprot.org/annotation/PRO_0000074593 http://togogenome.org/gene/10090:Zfand4 ^@ http://purl.uniprot.org/uniprot/D3Z3C6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand|||Turn|||Zinc Finger ^@ AN1-type|||AN1-type zinc finger protein 4|||Disordered|||Polar residues|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000416000 http://togogenome.org/gene/10090:Gnai3 ^@ http://purl.uniprot.org/uniprot/Q9DC51 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region ^@ G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(i) subunit alpha-3|||N-myristoyl glycine|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000203693 http://togogenome.org/gene/10090:Coq9 ^@ http://purl.uniprot.org/uniprot/Q8K1Z0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Ubiquinone biosynthesis protein COQ9, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000228638 http://togogenome.org/gene/10090:Nsd3 ^@ http://purl.uniprot.org/uniprot/D3Z357|||http://purl.uniprot.org/uniprot/Q6P2L6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||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 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||PHD-type|||PHD-type 1|||PHD-type 2|||PHD-type 3|||PHD-type 4; atypical|||PWWP|||PWWP 1|||PWWP 2|||Phosphoserine|||Polar residues|||Post-SET|||Pro residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000259522|||http://purl.uniprot.org/annotation/VSP_021431|||http://purl.uniprot.org/annotation/VSP_021432|||http://purl.uniprot.org/annotation/VSP_021433|||http://purl.uniprot.org/annotation/VSP_021434|||http://purl.uniprot.org/annotation/VSP_021435|||http://purl.uniprot.org/annotation/VSP_021436|||http://purl.uniprot.org/annotation/VSP_021437|||http://purl.uniprot.org/annotation/VSP_021438 http://togogenome.org/gene/10090:Il1r2 ^@ http://purl.uniprot.org/uniprot/P27931|||http://purl.uniprot.org/uniprot/Q4FK69 ^@ 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|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Interleukin-1 receptor type 2, membrane form|||Interleukin-1 receptor type 2, soluble form|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015440|||http://purl.uniprot.org/annotation/PRO_0000415349 http://togogenome.org/gene/10090:Stard10 ^@ http://purl.uniprot.org/uniprot/Q0VG22|||http://purl.uniprot.org/uniprot/Q9JMD3 ^@ 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|||N-acetylmethionine|||N6-succinyllysine|||Phosphoserine|||START|||START domain-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000220662 http://togogenome.org/gene/10090:Tiam1 ^@ http://purl.uniprot.org/uniprot/E9Q1R7|||http://purl.uniprot.org/uniprot/G3UWG2|||http://purl.uniprot.org/uniprot/Q3UHH6|||http://purl.uniprot.org/uniprot/Q3UVX2|||http://purl.uniprot.org/uniprot/Q6P1D6 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic residues|||DH|||Disordered|||PDZ|||PH|||Polar residues|||RBD ^@ http://togogenome.org/gene/10090:Rfpl4 ^@ http://purl.uniprot.org/uniprot/Q8VH31 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000394967 http://togogenome.org/gene/10090:Chga ^@ http://purl.uniprot.org/uniprot/P26339 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mass|||Modified Residue|||Peptide|||Region|||Signal Peptide ^@ Basic and acidic residues|||Beta-granin|||Catestatin|||Chromogranin-A|||Disordered|||GE-25|||Glycine amide|||Methionine sulfoxide|||O-linked (Xyl...) (chondroitin sulfate) serine|||Pancreastatin|||Phosphoserine|||Polar residues|||Pyrrolidone carboxylic acid|||Serpinin|||Serpinin-RRG|||WE-14|||With pyrrolidone carboxylic acid at Gln-438.|||p-Glu serpinin precursor ^@ http://purl.uniprot.org/annotation/PRO_0000005422|||http://purl.uniprot.org/annotation/PRO_0000005423|||http://purl.uniprot.org/annotation/PRO_0000005424|||http://purl.uniprot.org/annotation/PRO_0000005425|||http://purl.uniprot.org/annotation/PRO_0000432687|||http://purl.uniprot.org/annotation/PRO_0000432688|||http://purl.uniprot.org/annotation/PRO_0000432689|||http://purl.uniprot.org/annotation/PRO_0000432690|||http://purl.uniprot.org/annotation/PRO_0000432691 http://togogenome.org/gene/10090:Aktip ^@ http://purl.uniprot.org/uniprot/D3Z632|||http://purl.uniprot.org/uniprot/Q05BP5|||http://purl.uniprot.org/uniprot/Q64362 ^@ 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 ^@ AKT-interacting protein|||Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||UBC core ^@ http://purl.uniprot.org/annotation/PRO_0000082610 http://togogenome.org/gene/10090:Zfp772 ^@ http://purl.uniprot.org/uniprot/Q3UQL6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Fam172a ^@ http://purl.uniprot.org/uniprot/E9QMA2|||http://purl.uniprot.org/uniprot/Q3TNH5|||http://purl.uniprot.org/uniprot/Q6PFX1 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant ^@ Cotranscriptional regulator FAM172A|||Disordered|||Fails to interact with AGO2.|||Fails to interacts with AGO2. Decreases nuclear localization.|||In isoform 2.|||In isoform 3.|||Loss of nucleophilicity of Ser-294.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000320932|||http://purl.uniprot.org/annotation/VSP_031750|||http://purl.uniprot.org/annotation/VSP_031751|||http://purl.uniprot.org/annotation/VSP_031752 http://togogenome.org/gene/10090:Tmem183a ^@ http://purl.uniprot.org/uniprot/Q9CSF0|||http://purl.uniprot.org/uniprot/Q9JJB9 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 183 ^@ http://purl.uniprot.org/annotation/PRO_0000089252 http://togogenome.org/gene/10090:Gfer ^@ http://purl.uniprot.org/uniprot/P56213 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||ERV/ALR sulfhydryl oxidase|||FAD-linked sulfhydryl oxidase ALR|||Interchain (with C-197)|||Interchain (with C-88)|||Redox-active ^@ http://purl.uniprot.org/annotation/PRO_0000208549 http://togogenome.org/gene/10090:Txnrd3 ^@ http://purl.uniprot.org/uniprot/Q3UY43|||http://purl.uniprot.org/uniprot/Q99MD6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non standard residue|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non standard residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolishes thioredoxin reductase, glutaredoxin and gluthioine reductase activities.|||Asymmetric dimethylarginine; alternate|||Cysteinyl-selenocysteine (Cys-Sec)|||Disordered|||FAD/NAD(P)-binding|||Glutaredoxin|||N6-succinyllysine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Pro residues|||Proton acceptor|||Pyridine nucleotide-disulphide oxidoreductase dimerisation|||Redox-active|||Selenocysteine|||Thioredoxin reductase 3|||Thioredoxin reductase activity reduced to 21%. Glutaredoxin activity reduced to 14%. Glutathione reductase activity reduced to 18%. ^@ http://purl.uniprot.org/annotation/PRO_0000320696 http://togogenome.org/gene/10090:Serpinb6a ^@ http://purl.uniprot.org/uniprot/F8WIV2|||http://purl.uniprot.org/uniprot/Q4FJQ6|||http://purl.uniprot.org/uniprot/Q60854 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Domain Extent|||Modified Residue|||Site ^@ N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Reactive bond|||Serpin|||Serpin B6 ^@ http://purl.uniprot.org/annotation/PRO_0000094107 http://togogenome.org/gene/10090:Tcstv1 ^@ http://purl.uniprot.org/uniprot/O70619 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Bcat1 ^@ http://purl.uniprot.org/uniprot/P24288|||http://purl.uniprot.org/uniprot/Q3TJN1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Branched-chain-amino-acid aminotransferase, cytosolic|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_0000103293 http://togogenome.org/gene/10090:Lingo2 ^@ http://purl.uniprot.org/uniprot/B2RQD4|||http://purl.uniprot.org/uniprot/Q3URE9 ^@ 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|||Helical|||Ig-like|||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_0000324390|||http://purl.uniprot.org/annotation/PRO_5014298344 http://togogenome.org/gene/10090:Gm5901 ^@ http://purl.uniprot.org/uniprot/D3YVJ1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Sfi1 ^@ http://purl.uniprot.org/uniprot/Q3UZY0 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||HAT 1|||HAT 2|||HAT 3|||HAT 5|||HAT 6|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with CETN2|||Protein SFI1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000334622|||http://purl.uniprot.org/annotation/VSP_033709|||http://purl.uniprot.org/annotation/VSP_033710|||http://purl.uniprot.org/annotation/VSP_033711|||http://purl.uniprot.org/annotation/VSP_033712|||http://purl.uniprot.org/annotation/VSP_033713|||http://purl.uniprot.org/annotation/VSP_033714|||http://purl.uniprot.org/annotation/VSP_033715|||http://purl.uniprot.org/annotation/VSP_033716 http://togogenome.org/gene/10090:Oxr1 ^@ http://purl.uniprot.org/uniprot/B1H3M0|||http://purl.uniprot.org/uniprot/E9Q0A7|||http://purl.uniprot.org/uniprot/Q4KMM3 ^@ 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|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||LysM|||Mediates oxidative antimutator activity|||Oxidation resistance protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TLDc ^@ http://purl.uniprot.org/annotation/PRO_0000231646|||http://purl.uniprot.org/annotation/VSP_039015|||http://purl.uniprot.org/annotation/VSP_039016 http://togogenome.org/gene/10090:Efcab10 ^@ http://purl.uniprot.org/uniprot/Q9D581 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ EF-hand 1|||EF-hand 2|||EF-hand calcium-binding domain-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000340681 http://togogenome.org/gene/10090:Mall ^@ http://purl.uniprot.org/uniprot/Q91X49 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Transmembrane ^@ Helical|||MAL-like protein|||MARVEL ^@ http://purl.uniprot.org/annotation/PRO_0000156812 http://togogenome.org/gene/10090:Slc27a4 ^@ http://purl.uniprot.org/uniprot/Q91VE0 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Long-chain fatty acid transport protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000193211 http://togogenome.org/gene/10090:Ubtd1 ^@ http://purl.uniprot.org/uniprot/Q91WB7 ^@ 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 1|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000242675 http://togogenome.org/gene/10090:Dedd ^@ http://purl.uniprot.org/uniprot/Q3U001|||http://purl.uniprot.org/uniprot/Q9Z1L3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ DED|||Death effector domain-containing protein|||Disordered|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000191275 http://togogenome.org/gene/10090:Zfp385b ^@ http://purl.uniprot.org/uniprot/A2AS57|||http://purl.uniprot.org/uniprot/G5E8Y8|||http://purl.uniprot.org/uniprot/Q80ZR3|||http://purl.uniprot.org/uniprot/Q8BXJ8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||C2H2-type|||Disordered|||In isoform 2.|||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_0000191813|||http://purl.uniprot.org/annotation/VSP_015981 http://togogenome.org/gene/10090:Specc1 ^@ http://purl.uniprot.org/uniprot/A0A0J9YTU3|||http://purl.uniprot.org/uniprot/A0A0J9YUF8|||http://purl.uniprot.org/uniprot/A0A0J9YUR2|||http://purl.uniprot.org/uniprot/Q3UPB2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ppcs ^@ http://purl.uniprot.org/uniprot/Q8VDG5 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Splice Variant ^@ In isoform 2.|||N-acetylalanine|||Phosphopantothenate--cysteine ligase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000182041|||http://purl.uniprot.org/annotation/VSP_010244 http://togogenome.org/gene/10090:Lage3 ^@ http://purl.uniprot.org/uniprot/A0A158SIT5|||http://purl.uniprot.org/uniprot/Q9CR70 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||EKC/KEOPS complex subunit Lage3|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000218925 http://togogenome.org/gene/10090:Or5p66 ^@ http://purl.uniprot.org/uniprot/Q8VFD2 ^@ 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 5P66 ^@ http://purl.uniprot.org/annotation/PRO_0000150845 http://togogenome.org/gene/10090:Zfp771 ^@ http://purl.uniprot.org/uniprot/Q8BJ90 ^@ Chain|||Crosslink|||Modification|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Crosslink|||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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 771 ^@ http://purl.uniprot.org/annotation/PRO_0000280440 http://togogenome.org/gene/10090:Dlg3 ^@ http://purl.uniprot.org/uniprot/A2BEE9|||http://purl.uniprot.org/uniprot/A2BEF2|||http://purl.uniprot.org/uniprot/P70175|||http://purl.uniprot.org/uniprot/Q52KF7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disks large homolog 3|||Disordered|||Guanylate kinase-like|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000094558 http://togogenome.org/gene/10090:Ercc6 ^@ http://purl.uniprot.org/uniprot/F8VPZ5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Acidic residues|||Basic and acidic residues|||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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||N-terminal domain; essential for its chromatin remodeling activity|||N6-methylated lysine; by EHMT2|||Phosphoserine|||Phosphoserine; by CDK2|||Polar residues|||Ubiquitin-binding domain (UBD)|||Winged-helix domain (WHD) ^@ http://purl.uniprot.org/annotation/PRO_0000448242 http://togogenome.org/gene/10090:C8b ^@ http://purl.uniprot.org/uniprot/Q8BH35 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant ^@ C-linked (Man) tryptophan|||Complement component C8 beta chain|||Disordered|||EGF-like|||In isoform 2.|||In strain: MSM/Ms.|||In strain: Mae/Stm and MSM/Ms.|||In strain: Mae/Stm.|||LDL-receptor class A|||MACPF|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||TSP type-1 1|||TSP type-1 2 ^@ http://purl.uniprot.org/annotation/PRO_0000023593|||http://purl.uniprot.org/annotation/PRO_0000023594|||http://purl.uniprot.org/annotation/VSP_016666 http://togogenome.org/gene/10090:Mad2l1 ^@ http://purl.uniprot.org/uniprot/Q5HZH8|||http://purl.uniprot.org/uniprot/Q9Z1B5 ^@ 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 ^@ HORMA|||Mitotic spindle assembly checkpoint protein MAD2A|||N-acetylalanine|||Phosphoserine|||Removed|||Required for assuming the closed conformation and for interaction with CDC20 ^@ http://purl.uniprot.org/annotation/PRO_0000126118 http://togogenome.org/gene/10090:Or14a258 ^@ http://purl.uniprot.org/uniprot/Q7TS03 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fxr2 ^@ http://purl.uniprot.org/uniprot/Q6P5B5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Agenet-like|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Kansl2 ^@ http://purl.uniprot.org/uniprot/Q8BQR4 ^@ 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.|||KAT8 regulatory NSL complex subunit 2|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000278293|||http://purl.uniprot.org/annotation/VSP_023275|||http://purl.uniprot.org/annotation/VSP_042532|||http://purl.uniprot.org/annotation/VSP_042533 http://togogenome.org/gene/10090:Fsd2 ^@ http://purl.uniprot.org/uniprot/Q8BZ52|||http://purl.uniprot.org/uniprot/Q8C1E6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Sequence Conflict ^@ B30.2/SPRY|||Fibronectin type III and SPRY domain-containing protein 2|||Fibronectin type-III 1|||Fibronectin type-III 2 ^@ http://purl.uniprot.org/annotation/PRO_0000317363 http://togogenome.org/gene/10090:Lcn2 ^@ http://purl.uniprot.org/uniprot/P11672 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Strand|||Turn ^@ N-linked (GlcNAc...) asparagine|||Neutrophil gelatinase-associated lipocalin|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000017934 http://togogenome.org/gene/10090:Tmem42 ^@ http://purl.uniprot.org/uniprot/A0A1L1SRQ7|||http://purl.uniprot.org/uniprot/Q9CR22 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 42 ^@ http://purl.uniprot.org/annotation/PRO_0000284496 http://togogenome.org/gene/10090:Cytip ^@ http://purl.uniprot.org/uniprot/Q91VY6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict ^@ Cytohesin-interacting protein|||Interaction with CYTH1|||PDZ ^@ http://purl.uniprot.org/annotation/PRO_0000097062 http://togogenome.org/gene/10090:Cacul1 ^@ http://purl.uniprot.org/uniprot/E9PV69|||http://purl.uniprot.org/uniprot/Q3TAW5|||http://purl.uniprot.org/uniprot/Q8R0X2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ CDK2-associated and cullin domain-containing protein 1|||Cullin N-terminal|||Disordered|||In isoform 2.|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000119818|||http://purl.uniprot.org/annotation/VSP_013938|||http://purl.uniprot.org/annotation/VSP_013939 http://togogenome.org/gene/10090:Vmn2r117 ^@ http://purl.uniprot.org/uniprot/K7N6V1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908811 http://togogenome.org/gene/10090:Asf1a ^@ http://purl.uniprot.org/uniprot/Q9CQE6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Modified Residue|||Motif|||Region ^@ Histone chaperone ASF1A|||Interaction with histone H3, CHAF1B, and HIRA|||Phosphoserine|||Required for interaction with HIRA ^@ http://purl.uniprot.org/annotation/PRO_0000284013 http://togogenome.org/gene/10090:Mnat1 ^@ http://purl.uniprot.org/uniprot/P51949 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger ^@ CDK-activating kinase assembly factor MAT1|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||RING-type|||UIM ^@ http://purl.uniprot.org/annotation/PRO_0000055933 http://togogenome.org/gene/10090:Gm13289 ^@ http://purl.uniprot.org/uniprot/Q8CD73 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099103 http://togogenome.org/gene/10090:Clca2 ^@ http://purl.uniprot.org/uniprot/Q8BG22 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Calcium-activated chloride channel regulator 2|||Cleavage; by autolysis|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Metalloprotease domain|||N-linked (GlcNAc...) asparagine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000333696|||http://purl.uniprot.org/annotation/VSP_033515 http://togogenome.org/gene/10090:Brip1 ^@ http://purl.uniprot.org/uniprot/Q5SXJ3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||DEAH box|||Disordered|||Fanconi anemia group J protein homolog|||Helicase ATP-binding|||Interaction with BRCA1|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000055174 http://togogenome.org/gene/10090:H2-M5 ^@ http://purl.uniprot.org/uniprot/A7VMS3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015086582 http://togogenome.org/gene/10090:4930444P10Rik ^@ http://purl.uniprot.org/uniprot/Q9D5G1 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Basic residues|||Disordered ^@ http://togogenome.org/gene/10090:Sec63 ^@ http://purl.uniprot.org/uniprot/Q8VHE0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Cytoplasmic|||Disordered|||Helical|||J|||Lumenal|||Phosphoserine|||Phosphothreonine|||Polar residues|||SEC63 1|||SEC63 2|||Translocation protein SEC63 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000071098 http://togogenome.org/gene/10090:Slc22a6 ^@ http://purl.uniprot.org/uniprot/Q8VC69 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Complete loss of PAH transport activity.|||Cytoplasmic|||Decreased cell surface expression level and PAH transport activity. 80% decrease of PAH transport activity; when associated with A-49; A-122 and A-183. Complete loss of PAH transport activity; when associated with A-49; A-78; A-99; A-122; A-172; A-183; A-200; A-362; A-335; A-379; A-402 and A-427.|||Decreased cell surface expression level and PAH transport activity. Complete loss of PAH transport activity; when associated with A-49; A-78; A-99; A-122; A-172; A-200; A-362; A-335; A-379; A-402; A-427 and A-434.|||Decreased cell surface expression level and PAH transport activity. Complete loss of PAH transport activity; when associated with A-49; A-78; A-99; A-172; A-183; A-200; A-362; A-335; A-379; A-402; A-427 and A-434.|||Decreased cell surface expression level and PAH transport activity. Complete loss of PAH transport activity; when associated with A-78; A-99; A-122; A-172; A-183; A-200; A-362; A-335; A-379; A-402; A-427 and A-434.|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Solute carrier family 22 member 6 ^@ http://purl.uniprot.org/annotation/PRO_0000324168 http://togogenome.org/gene/10090:Defb5 ^@ http://purl.uniprot.org/uniprot/Q9EPV9 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ Beta-defensin 5 ^@ http://purl.uniprot.org/annotation/PRO_0000006931 http://togogenome.org/gene/10090:Ifna13 ^@ http://purl.uniprot.org/uniprot/A0A7R8C3J8|||http://purl.uniprot.org/uniprot/Q80SU4 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Interferon alpha-13|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_5000090349|||http://purl.uniprot.org/annotation/PRO_5030857174 http://togogenome.org/gene/10090:Tnfaip6 ^@ http://purl.uniprot.org/uniprot/O08859|||http://purl.uniprot.org/uniprot/Q3USX6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ CUB|||Disordered|||Link|||N-linked (GlcNAc...) asparagine|||Polar residues|||Tumor necrosis factor-inducible gene 6 protein ^@ http://purl.uniprot.org/annotation/PRO_0000026693|||http://purl.uniprot.org/annotation/PRO_5014309167 http://togogenome.org/gene/10090:Dnal1 ^@ http://purl.uniprot.org/uniprot/Q05A62 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant ^@ Dynein axonemal light chain 1|||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_0000281131|||http://purl.uniprot.org/annotation/VSP_023983|||http://purl.uniprot.org/annotation/VSP_023984|||http://purl.uniprot.org/annotation/VSP_023985 http://togogenome.org/gene/10090:Vta1 ^@ http://purl.uniprot.org/uniprot/Q9CR26 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Interaction with CHMP5|||Interaction with IST1|||Interaction with VPS4B|||N-acetylalanine|||Polar residues|||Removed|||Vacuolar protein sorting-associated protein VTA1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089510 http://togogenome.org/gene/10090:Ficd ^@ http://purl.uniprot.org/uniprot/Q8BIX9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Fido|||Helical; Signal-anchor for type II membrane protein|||Important for autoinhibition of adenylyltransferase activity|||In isoform 2.|||Inhibitory (S/T)XXXE(G/N) motif|||Lumenal|||N-linked (GlcNAc...) asparagine|||O-AMP-threonine; by autocatalysis|||Protein adenylyltransferase FICD|||TPR 1|||TPR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000317302|||http://purl.uniprot.org/annotation/VSP_030934 http://togogenome.org/gene/10090:Izumo4 ^@ http://purl.uniprot.org/uniprot/D3Z690 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Izumo sperm-egg fusion protein 4|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000416109|||http://purl.uniprot.org/annotation/VSP_042504|||http://purl.uniprot.org/annotation/VSP_042505 http://togogenome.org/gene/10090:Msantd4 ^@ http://purl.uniprot.org/uniprot/Q91YU3 ^@ 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_0000311831 http://togogenome.org/gene/10090:Ctxn1 ^@ http://purl.uniprot.org/uniprot/Q3TYB7|||http://purl.uniprot.org/uniprot/Q8K129 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Cortexin-1|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000079501 http://togogenome.org/gene/10090:Ppp1r26 ^@ http://purl.uniprot.org/uniprot/Q6A025 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Protein phosphatase 1 regulatory subunit 26 ^@ http://purl.uniprot.org/annotation/PRO_0000309219 http://togogenome.org/gene/10090:Keg1 ^@ http://purl.uniprot.org/uniprot/Q9DCY0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Glycine N-acyltransferase-like protein Keg1|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000281876 http://togogenome.org/gene/10090:Medag ^@ http://purl.uniprot.org/uniprot/Q14BA6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Mesenteric estrogen-dependent adipogenesis protein ^@ http://purl.uniprot.org/annotation/PRO_0000274334|||http://purl.uniprot.org/annotation/VSP_022716 http://togogenome.org/gene/10090:Rpgrip1l ^@ http://purl.uniprot.org/uniprot/Q8CG73 ^@ 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|||C2 1|||C2 2|||Disordered|||Polar residues|||Protein fantom ^@ http://purl.uniprot.org/annotation/PRO_0000291268 http://togogenome.org/gene/10090:Or6c1 ^@ http://purl.uniprot.org/uniprot/Q8VGJ2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Eml5 ^@ http://purl.uniprot.org/uniprot/Q8BQM8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict ^@ Acidic residues|||Disordered|||Echinoderm microtubule-associated protein-like 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_0000284396 http://togogenome.org/gene/10090:Nek2 ^@ http://purl.uniprot.org/uniprot/O35942|||http://purl.uniprot.org/uniprot/Q6PFG1 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Interaction with CEP85|||Interaction with PCNT|||Interaction with SAV1 and STK3/MST2|||Leucine-zipper|||Necessary for interaction with MAD1L1|||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_0000086422 http://togogenome.org/gene/10090:Btbd16 ^@ http://purl.uniprot.org/uniprot/E9Q173 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ BTB|||BTB/POZ domain-containing protein 16 ^@ http://purl.uniprot.org/annotation/PRO_0000416102 http://togogenome.org/gene/10090:Tnfsf11 ^@ http://purl.uniprot.org/uniprot/O35235 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Tumor necrosis factor ligand superfamily member 11, membrane form|||Tumor necrosis factor ligand superfamily member 11, soluble form ^@ http://purl.uniprot.org/annotation/PRO_0000034516|||http://purl.uniprot.org/annotation/PRO_0000034517|||http://purl.uniprot.org/annotation/VSP_006448|||http://purl.uniprot.org/annotation/VSP_006449 http://togogenome.org/gene/10090:P2ry4 ^@ http://purl.uniprot.org/uniprot/Q0VBT7|||http://purl.uniprot.org/uniprot/Q9JJS7 ^@ 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|||P2Y purinoceptor 4 ^@ http://purl.uniprot.org/annotation/PRO_0000070022 http://togogenome.org/gene/10090:Afg3l2 ^@ http://purl.uniprot.org/uniprot/Q8JZQ2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Site|||Transit Peptide|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Transit Peptide|||Transmembrane ^@ AFG3-like protein 2|||Absence of proteolytic activity. Loss of its processing into the mature form.|||Basic and acidic residues|||Disordered|||Helical|||In par.|||Mitochondrion|||N6-succinyllysine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000442313|||http://purl.uniprot.org/annotation/PRO_0000442314 http://togogenome.org/gene/10090:Parp1 ^@ http://purl.uniprot.org/uniprot/Q921K2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BRCT|||Basic and acidic residues|||Disordered|||PADR1 zinc-binding|||PARP alpha-helical|||PARP catalytic|||PARP-type|||WGR ^@ http://togogenome.org/gene/10090:Lhfpl3 ^@ http://purl.uniprot.org/uniprot/A0A0G2JGI3|||http://purl.uniprot.org/uniprot/Q9CTN8 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||LHFPL tetraspan subfamily member 3 protein ^@ http://purl.uniprot.org/annotation/PRO_0000244767 http://togogenome.org/gene/10090:Zfp612 ^@ http://purl.uniprot.org/uniprot/A0A1D5RMC2|||http://purl.uniprot.org/uniprot/Q3TRD7|||http://purl.uniprot.org/uniprot/Q3V041 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Nfix ^@ http://purl.uniprot.org/uniprot/E9PUH7|||http://purl.uniprot.org/uniprot/P70257|||http://purl.uniprot.org/uniprot/Q3TYK3|||http://purl.uniprot.org/uniprot/Q5CZY4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ 9aaTAD|||Asymmetric dimethylarginine|||CTF/NF-I|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform NFIX1 and isoform NFIX2.|||In isoform NFIX2.|||Nuclear factor 1 X-type|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000100205|||http://purl.uniprot.org/annotation/VSP_003563|||http://purl.uniprot.org/annotation/VSP_007546|||http://purl.uniprot.org/annotation/VSP_007547 http://togogenome.org/gene/10090:Mrgprb5 ^@ http://purl.uniprot.org/uniprot/Q91ZB9|||http://purl.uniprot.org/uniprot/W8W3Q3 ^@ 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|||Mas-related G-protein coupled receptor member B5|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000305301 http://togogenome.org/gene/10090:Hoxa1 ^@ http://purl.uniprot.org/uniprot/B9EHK7|||http://purl.uniprot.org/uniprot/D3Z4E1|||http://purl.uniprot.org/uniprot/Q8BNI8 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic residues|||Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Marveld3 ^@ http://purl.uniprot.org/uniprot/G3X8Q2|||http://purl.uniprot.org/uniprot/G3X9A4|||http://purl.uniprot.org/uniprot/Q9D956 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||MARVEL|||MARVEL domain-containing protein 3|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000271530|||http://purl.uniprot.org/annotation/VSP_022323 http://togogenome.org/gene/10090:Upf1 ^@ http://purl.uniprot.org/uniprot/Q9EPU0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ C3H|||C4|||CC/SHH/C|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Regulator of nonsense transcripts 1|||Sufficient for interaction with RENT2|||Upf1 CH-rich|||[ST]-Q motif 1|||[ST]-Q motif 2 ^@ http://purl.uniprot.org/annotation/PRO_0000080717|||http://purl.uniprot.org/annotation/VSP_025764 http://togogenome.org/gene/10090:5430401F13Rik ^@ http://purl.uniprot.org/uniprot/E9Q328|||http://purl.uniprot.org/uniprot/Q9D3N7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5004325064|||http://purl.uniprot.org/annotation/PRO_5015090363 http://togogenome.org/gene/10090:1600012H06Rik ^@ http://purl.uniprot.org/uniprot/Q9DAY5 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||UPF0669 protein C6orf120 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000297664 http://togogenome.org/gene/10090:Bet1 ^@ http://purl.uniprot.org/uniprot/O35623 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Topological Domain|||Transmembrane ^@ BET1 homolog|||Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Phosphoserine|||Vesicular|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000206885 http://togogenome.org/gene/10090:Sucnr1 ^@ http://purl.uniprot.org/uniprot/Q99MT6 ^@ 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|||Succinate receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000070135 http://togogenome.org/gene/10090:Fam210b ^@ http://purl.uniprot.org/uniprot/Q9D8B6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transit Peptide|||Transmembrane ^@ DUF1279|||Disordered|||Helical|||Mitochondrion|||Polar residues|||Protein FAM210B, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000079452 http://togogenome.org/gene/10090:Gnaz ^@ http://purl.uniprot.org/uniprot/O70443|||http://purl.uniprot.org/uniprot/Q542R8 ^@ 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 ^@ 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_0000203697 http://togogenome.org/gene/10090:Senp6 ^@ http://purl.uniprot.org/uniprot/F6Z9A1|||http://purl.uniprot.org/uniprot/Q6P7W0 ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||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 2.|||Phosphoserine|||Phosphothreonine|||Protease|||Sentrin-specific protease 6|||Ubiquitin-like protease family profile ^@ http://purl.uniprot.org/annotation/PRO_0000267608|||http://purl.uniprot.org/annotation/VSP_021943 http://togogenome.org/gene/10090:Or6d13 ^@ http://purl.uniprot.org/uniprot/Q7TS32 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H2bc12 ^@ http://purl.uniprot.org/uniprot/B2RVD5|||http://purl.uniprot.org/uniprot/Q8CGP1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||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 H2A/H2B/H3|||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-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_0000244833 http://togogenome.org/gene/10090:Itga3 ^@ http://purl.uniprot.org/uniprot/Q62470 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||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-3|||Integrin alpha-3 heavy chain|||Integrin alpha-3 light chain|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000016241|||http://purl.uniprot.org/annotation/PRO_0000016242|||http://purl.uniprot.org/annotation/PRO_0000016243|||http://purl.uniprot.org/annotation/VSP_002722|||http://purl.uniprot.org/annotation/VSP_041797 http://togogenome.org/gene/10090:Ice2 ^@ http://purl.uniprot.org/uniprot/Q3UZ18 ^@ 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.|||Little elongation complex subunit 2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000297965|||http://purl.uniprot.org/annotation/VSP_027442|||http://purl.uniprot.org/annotation/VSP_027443 http://togogenome.org/gene/10090:Capn9 ^@ http://purl.uniprot.org/uniprot/Q9D805 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Calpain catalytic|||Calpain-9|||Disordered|||Domain III|||Domain IV|||EF-hand 1|||EF-hand 2|||EF-hand 3 ^@ http://purl.uniprot.org/annotation/PRO_0000207723 http://togogenome.org/gene/10090:Socs1 ^@ http://purl.uniprot.org/uniprot/O35716 ^@ 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 ^@ Abolishes interaction with elongin BC complex; when associated with F-179.|||Abolishes interaction with elongin BC complex; when associated with P-175.|||Disordered|||Extended SH2 subdomain (ESS)|||Interaction with Elongin BC complex|||Kinase inhibitory region (KIR)|||Loss of IL-6 signal transduction suppression. No effect on binding to TYK2.|||Loss of JAK signal transduction suppression.|||Loss of JAK signal transduction suppression. Destabilization of SOCS1.|||Loss of JAK signal transduction suppression. Reduced binding to JH1.|||Loss of LIF signal transduction suppression. Loss of binding to KIT. No effect on binding to VAV.|||Loss of binding to JH1/Y-1007 of JAK2 and loss of signal transduction suppression.|||No effect on JAK signal transduction inhibition nor on binding to JH1.|||No effect on JAK signal transduction suppression nor on binding to JH1.|||No effect on JAK signal transduction suppression.|||No effect on LIF signal transduction suppression.|||Polar residues|||Reduced binding to JH1.|||SH2|||SOCS box|||Some loss of JAK signal transduction signaling. Reduced binding to JH1.|||Suppressor of cytokine signaling 1 ^@ http://purl.uniprot.org/annotation/PRO_0000181236 http://togogenome.org/gene/10090:Prdx6b ^@ http://purl.uniprot.org/uniprot/Q8BG37 ^@ Active Site|||Domain Extent|||Region|||Site ^@ Active Site|||Domain Extent ^@ Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity|||Thioredoxin ^@ http://togogenome.org/gene/10090:Manbal ^@ http://purl.uniprot.org/uniprot/A2BGN7 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Rcn1 ^@ http://purl.uniprot.org/uniprot/Q05186 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||N-linked (GlcNAc...) asparagine; partial|||Phosphoserine|||Prevents secretion from ER|||Reticulocalbin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000004146 http://togogenome.org/gene/10090:Or5ac22 ^@ http://purl.uniprot.org/uniprot/E9Q8M0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r61 ^@ http://purl.uniprot.org/uniprot/W4VSP5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical|||Vomeronasal type-1 receptor ^@ http://purl.uniprot.org/annotation/PRO_5015102297 http://togogenome.org/gene/10090:Cntn1 ^@ http://purl.uniprot.org/uniprot/P12960 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ 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|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000014687|||http://purl.uniprot.org/annotation/PRO_0000014688 http://togogenome.org/gene/10090:Suv39h2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J074|||http://purl.uniprot.org/uniprot/Q9EQQ0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic residues|||Chromo|||Disordered|||Histone-lysine N-methyltransferase SUV39H2|||Phosphoserine|||Post-SET|||Pre-SET|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000186060 http://togogenome.org/gene/10090:Polr2h ^@ http://purl.uniprot.org/uniprot/Q923G2 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ DNA-directed RNA polymerases I, II, and III subunit RPABC3|||N-acetylalanine|||Non-specific ssDNA binding|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073998 http://togogenome.org/gene/10090:Fam110a ^@ http://purl.uniprot.org/uniprot/Q8R184 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Protein FAM110A ^@ http://purl.uniprot.org/annotation/PRO_0000079436 http://togogenome.org/gene/10090:Fam24b ^@ http://purl.uniprot.org/uniprot/Q9DAL9 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Protein FAM24A-like ^@ http://purl.uniprot.org/annotation/PRO_0000353118 http://togogenome.org/gene/10090:Mbd3 ^@ http://purl.uniprot.org/uniprot/Q9Z2D8 ^@ 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 ^@ Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||MBD|||Methyl-CpG-binding domain protein 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000096263|||http://purl.uniprot.org/annotation/VSP_011082 http://togogenome.org/gene/10090:Or5g29 ^@ http://purl.uniprot.org/uniprot/Q8VF76 ^@ 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 5G29 ^@ http://purl.uniprot.org/annotation/PRO_0000150857 http://togogenome.org/gene/10090:Mybph ^@ http://purl.uniprot.org/uniprot/P70402 ^@ 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|||Fibronectin type-III 1|||Fibronectin type-III 2|||Ig-like C2-type 1|||Ig-like C2-type 2|||Myosin-binding protein H|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000072699 http://togogenome.org/gene/10090:Ppil1 ^@ http://purl.uniprot.org/uniprot/B9EJX8|||http://purl.uniprot.org/uniprot/Q9D0W5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site ^@ Loss of isomerase activity. No phenotype when introduced in mice, animals are viable and fertile with no microcephaly or defective cortical lamination; no splicing defect.|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase-like 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000064165 http://togogenome.org/gene/10090:Btf3l4 ^@ http://purl.uniprot.org/uniprot/A2A7Z4|||http://purl.uniprot.org/uniprot/Q9CQH7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N6-methyllysine|||NAC-A/B|||Phosphothreonine|||Transcription factor BTF3 homolog 4 ^@ http://purl.uniprot.org/annotation/PRO_0000213558 http://togogenome.org/gene/10090:Rbm7 ^@ http://purl.uniprot.org/uniprot/Q14A95|||http://purl.uniprot.org/uniprot/Q3U5M9|||http://purl.uniprot.org/uniprot/Q9CQT2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Does not phosphorylated by MAPK14/p38-alpha-activated MAPKAPK2/MK2. Does not affect localization. Does not affect interaction with ZCCHC8.|||N-acetylglycine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Polar residues|||RNA-binding protein 7|||RRM|||Removed|||ZCCHC8 binding ^@ http://purl.uniprot.org/annotation/PRO_0000081762 http://togogenome.org/gene/10090:Ncdn ^@ http://purl.uniprot.org/uniprot/Q9Z0E0 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Asymmetric dimethylarginine|||In isoform 2.|||N-acetylserine|||Neurochondrin|||Phosphoserine|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000324618|||http://purl.uniprot.org/annotation/VSP_032317 http://togogenome.org/gene/10090:Amdhd1 ^@ http://purl.uniprot.org/uniprot/Q9DBA8 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Probable imidazolonepropionase ^@ http://purl.uniprot.org/annotation/PRO_0000282583 http://togogenome.org/gene/10090:Vmn1r23 ^@ http://purl.uniprot.org/uniprot/Q8R2D0 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Zfp791 ^@ http://purl.uniprot.org/uniprot/Q497V9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Arrdc3 ^@ http://purl.uniprot.org/uniprot/Q7TPQ9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Arrestin domain-containing protein 3|||Disordered|||PPxY motif 1|||PPxY motif 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000244350 http://togogenome.org/gene/10090:Sytl5 ^@ http://purl.uniprot.org/uniprot/A2AF58|||http://purl.uniprot.org/uniprot/Q80T23 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C2|||C2 1|||C2 2|||Disordered|||FYVE-type|||In isoform 2.|||Phosphoserine|||Polar residues|||RabBD|||Synaptotagmin-like protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000190220|||http://purl.uniprot.org/annotation/VSP_007905 http://togogenome.org/gene/10090:Or1j1 ^@ http://purl.uniprot.org/uniprot/Q60879 ^@ 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 1J1 ^@ http://purl.uniprot.org/annotation/PRO_0000150804 http://togogenome.org/gene/10090:Chd4 ^@ http://purl.uniprot.org/uniprot/Q3ULG0|||http://purl.uniprot.org/uniprot/Q6PDQ2|||http://purl.uniprot.org/uniprot/Q8BM83 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||CHD N-terminal|||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|||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_0000080229 http://togogenome.org/gene/10090:Shh ^@ http://purl.uniprot.org/uniprot/Q62226 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Motif|||Mutagenesis Site|||Signal Peptide|||Site|||Strand|||Turn ^@ Cardin-Weintraub|||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.|||Cholesterol glycine ester|||Cleavage; by autolysis|||Does not affect signaling activity in any of Shh signaling assays and causes no apparent defects in cholesterol-mediated autoprocessing reactions.|||Essential for auto-cleavage|||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.|||Involved in auto-cleavage|||Involved in cholesterol transfer|||Moderately reduces Ptch1 binding in vitro and signaling potency in chicken embryo neural plate explant assays compared with wild-type sequence.|||N-linked (GlcNAc...) asparagine|||N-palmitoyl cysteine|||Shows no change in activities at different temperatures.|||Sonic hedgehog protein|||Sonic hedgehog protein N-product|||Strongly reduces effects of in vivo overexpression; impairs multimer formation; does not affect subcellular location to lipid rafts. Homozygous mice are characterized by a smaller size and holoprosencephaly at 10.5 dpc, and shortening of limbs at 13.5 dpc. They die soon after birth. ^@ http://purl.uniprot.org/annotation/PRO_0000013211|||http://purl.uniprot.org/annotation/PRO_0000013212 http://togogenome.org/gene/10090:Nbdy ^@ http://purl.uniprot.org/uniprot/A0A140LJI0 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5013040151 http://togogenome.org/gene/10090:Hhla1 ^@ http://purl.uniprot.org/uniprot/Q3TYV2 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||HERV-H LTR-associating protein 1 homolog|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000394220 http://togogenome.org/gene/10090:Kat7 ^@ http://purl.uniprot.org/uniprot/Q1AJD0|||http://purl.uniprot.org/uniprot/Q3TD41|||http://purl.uniprot.org/uniprot/Q3UGF2|||http://purl.uniprot.org/uniprot/Q5SVQ0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C2HC MYST-type|||CCHHC-type|||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|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||MYST-type HAT|||N6-acetyllysine|||N6-acetyllysine; by autocatalysis|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000051570|||http://purl.uniprot.org/annotation/VSP_014582|||http://purl.uniprot.org/annotation/VSP_014583|||http://purl.uniprot.org/annotation/VSP_014584 http://togogenome.org/gene/10090:Fez1 ^@ http://purl.uniprot.org/uniprot/Q8K0X8 ^@ 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|||Fasciculation and elongation protein zeta-1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000189526 http://togogenome.org/gene/10090:Prlr ^@ http://purl.uniprot.org/uniprot/G3UVW6|||http://purl.uniprot.org/uniprot/Q08501|||http://purl.uniprot.org/uniprot/Q3TNP6|||http://purl.uniprot.org/uniprot/Q8C5N1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||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|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform PRL-R1.|||In isoform PRL-R2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Prolactin receptor|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010978|||http://purl.uniprot.org/annotation/PRO_5015091585|||http://purl.uniprot.org/annotation/VSP_001721|||http://purl.uniprot.org/annotation/VSP_001722|||http://purl.uniprot.org/annotation/VSP_001723|||http://purl.uniprot.org/annotation/VSP_001724 http://togogenome.org/gene/10090:1700129C05Rik ^@ http://purl.uniprot.org/uniprot/Q9CQ77 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Skil ^@ http://purl.uniprot.org/uniprot/D3Z7C5|||http://purl.uniprot.org/uniprot/Q3TB81|||http://purl.uniprot.org/uniprot/Q60665 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||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|||Ski-like protein|||c-SKI SMAD4-binding ^@ http://purl.uniprot.org/annotation/PRO_0000129388|||http://purl.uniprot.org/annotation/VSP_014265 http://togogenome.org/gene/10090:Or8g21 ^@ http://purl.uniprot.org/uniprot/Q8VG16 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pcdh7 ^@ http://purl.uniprot.org/uniprot/A0A0A6YY83|||http://purl.uniprot.org/uniprot/A2RS43|||http://purl.uniprot.org/uniprot/E9Q2S0|||http://purl.uniprot.org/uniprot/Q3USI1|||http://purl.uniprot.org/uniprot/Q8CA35 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Cadherin|||Cadherin domain-containing protein|||Disordered|||Helical|||Polar residues|||Protocadherin ^@ http://purl.uniprot.org/annotation/PRO_5002035541|||http://purl.uniprot.org/annotation/PRO_5004230164|||http://purl.uniprot.org/annotation/PRO_5015086068|||http://purl.uniprot.org/annotation/PRO_5015090361 http://togogenome.org/gene/10090:Riok3 ^@ http://purl.uniprot.org/uniprot/Q9DBU3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase RIO3 ^@ http://purl.uniprot.org/annotation/PRO_0000213530 http://togogenome.org/gene/10090:Lrrc4b ^@ http://purl.uniprot.org/uniprot/P0C192 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Disordered|||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_0000232387 http://togogenome.org/gene/10090:Kif1b ^@ http://purl.uniprot.org/uniprot/A2AH75|||http://purl.uniprot.org/uniprot/Q3UY61|||http://purl.uniprot.org/uniprot/Q60575|||http://purl.uniprot.org/uniprot/Q6PB45 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||FHA|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with KBP|||Kinesin motor|||Kinesin-like protein KIF1B|||N-acetylserine|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000125408|||http://purl.uniprot.org/annotation/VSP_002862|||http://purl.uniprot.org/annotation/VSP_002863|||http://purl.uniprot.org/annotation/VSP_002864|||http://purl.uniprot.org/annotation/VSP_002865 http://togogenome.org/gene/10090:Or10j7 ^@ http://purl.uniprot.org/uniprot/E9Q8X1|||http://purl.uniprot.org/uniprot/Q8VG31 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tmem198b ^@ http://purl.uniprot.org/uniprot/Q8CFU0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ DUF4203|||Helical ^@ http://togogenome.org/gene/10090:Rft1 ^@ http://purl.uniprot.org/uniprot/Q8C3B8 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Protein RFT1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000311287|||http://purl.uniprot.org/annotation/VSP_029509|||http://purl.uniprot.org/annotation/VSP_029510 http://togogenome.org/gene/10090:Rnf141 ^@ http://purl.uniprot.org/uniprot/Q99MB7 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Zinc Finger ^@ N-myristoyl glycine|||RING finger protein 141|||RING-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056102 http://togogenome.org/gene/10090:Rpap3 ^@ http://purl.uniprot.org/uniprot/Q9D706 ^@ Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Repeat ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000302795 http://togogenome.org/gene/10090:Clpp ^@ http://purl.uniprot.org/uniprot/O88696 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Chain|||Modified Residue|||Region|||Transit Peptide ^@ ATP-dependent Clp protease proteolytic subunit, mitochondrial|||Disordered|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000005517 http://togogenome.org/gene/10090:Ssu2 ^@ http://purl.uniprot.org/uniprot/Q8C3L1 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disordered|||Mice carrying this mutant show narrowed dental pulp cavities, increased dentin thickness, and abnormal tooth attrition, as well as anomalies in the number and organization of dentinal tubules, indicating dysplasia of the mineralized dentin; the width of the predentin zone is reduced in heterozygous animals or null in homozygotes, with significantly increased numbers of odontoblasts in the pulp cavity compared to wild-type mice.|||Protein SSUH2 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000260083 http://togogenome.org/gene/10090:Ankzf1 ^@ http://purl.uniprot.org/uniprot/J3QM81|||http://purl.uniprot.org/uniprot/Q80UU1 ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ANK|||ANK 1|||ANK 2|||Basic and acidic residues|||C2H2-type|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||VCP/p97-interacting motif (VIM)|||VLRF1|||tRNA endonuclease ANKZF1 ^@ http://purl.uniprot.org/annotation/PRO_0000247279|||http://purl.uniprot.org/annotation/VSP_019961|||http://purl.uniprot.org/annotation/VSP_019962 http://togogenome.org/gene/10090:Slc25a12 ^@ http://purl.uniprot.org/uniprot/Q8BH59 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ 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|||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_0000090599 http://togogenome.org/gene/10090:Cstdc4 ^@ http://purl.uniprot.org/uniprot/B2RV77 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Cystatin ^@ http://togogenome.org/gene/10090:Nr1h2 ^@ http://purl.uniprot.org/uniprot/Q60644|||http://purl.uniprot.org/uniprot/Q8BP65 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Region|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000053533 http://togogenome.org/gene/10090:Tmod1 ^@ http://purl.uniprot.org/uniprot/P49813 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Tropomodulin-1|||Tropomyosin-binding ^@ http://purl.uniprot.org/annotation/PRO_0000186129 http://togogenome.org/gene/10090:Prl6a1 ^@ http://purl.uniprot.org/uniprot/A0A0M6L0L9|||http://purl.uniprot.org/uniprot/O35257 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prolactin-6A1 ^@ http://purl.uniprot.org/annotation/PRO_0000045210|||http://purl.uniprot.org/annotation/PRO_5015043319 http://togogenome.org/gene/10090:Gtf2a1 ^@ http://purl.uniprot.org/uniprot/Q0VGZ0|||http://purl.uniprot.org/uniprot/Q149E9|||http://purl.uniprot.org/uniprot/Q99PM3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Acidic residues|||Cleavage; by TASP1|||Disordered|||N-acetylalanine|||Phosphoserine; by TAF1|||Polar residues|||Removed|||Transcription initiation factor IIA alpha chain|||Transcription initiation factor IIA beta chain|||Transcription initiation factor IIA subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000042595|||http://purl.uniprot.org/annotation/PRO_0000042596|||http://purl.uniprot.org/annotation/PRO_0000042597 http://togogenome.org/gene/10090:Or8d1b ^@ http://purl.uniprot.org/uniprot/Q9EQA0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:B3gat2 ^@ http://purl.uniprot.org/uniprot/P59270 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Interaction with galactose moiety of substrate glycoprotein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000195173|||http://purl.uniprot.org/annotation/VSP_001796|||http://purl.uniprot.org/annotation/VSP_001797 http://togogenome.org/gene/10090:Skint8 ^@ http://purl.uniprot.org/uniprot/A7XV07 ^@ 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|||Helical|||Ig-like C1-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Selection and upkeep of intraepithelial T-cells protein 8 ^@ http://purl.uniprot.org/annotation/PRO_5000271643|||http://purl.uniprot.org/annotation/VSP_034892|||http://purl.uniprot.org/annotation/VSP_034893|||http://purl.uniprot.org/annotation/VSP_034894|||http://purl.uniprot.org/annotation/VSP_034895 http://togogenome.org/gene/10090:Gtpbp8 ^@ http://purl.uniprot.org/uniprot/Q9CY28 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant ^@ EngB-type G|||GTP-binding protein 8|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000338613|||http://purl.uniprot.org/annotation/VSP_034058 http://togogenome.org/gene/10090:Pcgf3 ^@ http://purl.uniprot.org/uniprot/Q8BTQ0 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Region|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform 2.|||Interaction with BCORL1|||Polycomb group RING finger protein 3|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000277865|||http://purl.uniprot.org/annotation/VSP_023116|||http://purl.uniprot.org/annotation/VSP_023117 http://togogenome.org/gene/10090:Ccdc116 ^@ http://purl.uniprot.org/uniprot/A0A338P7I8|||http://purl.uniprot.org/uniprot/Q80X53 ^@ 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|||Coiled-coil domain-containing protein 116|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000254054 http://togogenome.org/gene/10090:Rnf121 ^@ http://purl.uniprot.org/uniprot/Q8R1Z9 ^@ 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.|||In isoform 3.|||N-acetylalanine|||RING-type; atypical|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000261408|||http://purl.uniprot.org/annotation/VSP_021683|||http://purl.uniprot.org/annotation/VSP_021684 http://togogenome.org/gene/10090:Or10z1 ^@ http://purl.uniprot.org/uniprot/E9Q0Y7|||http://purl.uniprot.org/uniprot/Q7TRW4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vrtn ^@ http://purl.uniprot.org/uniprot/Q3SYK4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Vertnin ^@ http://purl.uniprot.org/annotation/PRO_0000404600 http://togogenome.org/gene/10090:Dll1 ^@ http://purl.uniprot.org/uniprot/Q61483 ^@ Chain|||Compositionally Biased Region|||Crosslink|||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|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cleavage; by ADAM protease|||Cleavage; by MMP14|||Cytoplasmic|||DSL|||Decreases Notch signaling pathway.|||Delta-like protein 1|||Disordered|||Dll1-derived cell-associated form|||Dll1-intracellular form|||Dll1-soluble form|||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|||Highly decreases Notch signaling pathway. Multi-ubiquitination pattern is reduced, although it does appear to be mono-ubiquitinated. Interacts with MIB1. Loss of cis and trans interaction with NOTCH1. Increases its association with lipid raft microdomains.|||Highly decreases Notch signaling pathway. Multi-ubiquitination pattern is reduced, although it does appear to be mono-ubiquitinated. Interacts with MIB1. Loss of cis interaction with NOTCH1.|||Interaction with MAGI1|||N-linked (GlcNAc...) asparagine|||Not phosphorylated; when associated with A-693 and A-696. Not phosphorylated and doesn't prevent phosphorylation at S-693 and S-696. Reduces NOTCH1 transactivation; when associated with A-693 and A-696. Reduces cell surface levels of proteins; when associated with A-693 and A-696. Increases ectodomain shedding; when associated with A-693 and A-696.|||Not phosphorylated; when associated with V-638 and A-693. Not phosphorylated and doesn't prevent phosphorylation at T-638 and S-693, Reduces NOTCH1 transactivation; when associated with V-638 and A-693. Reduces cell surface levels of proteins; when associated with V-638 and A-693. Increases ectodomain shedding; when associated with V-638 and A-693.|||Not phosphorylated; when associated with V-638 and A-696. Not phosphorylated and prevents phosphorylation at S-696. Reduces NOTCH1 transactivation; when associated with V-638 and A-696. Reduces cell surface levels of proteins; when associated with V-638 and A-696. Increases ectodomain shedding; when associated with V-638 and A-696.|||Phosphoserine|||Phosphoserine; by PKB|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000007507|||http://purl.uniprot.org/annotation/PRO_0000434830|||http://purl.uniprot.org/annotation/PRO_0000434831|||http://purl.uniprot.org/annotation/PRO_0000434832 http://togogenome.org/gene/10090:Hcn1 ^@ http://purl.uniprot.org/uniprot/O88704 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes conductivity.|||Abolishes conductivity; when associated with A-349 and A-350.|||Abolishes conductivity; when associated with A-349 and A-351.|||Abolishes conductivity; when associated with A-350 and A-351.|||Abolishes sensitivity to sulfhydryl modification.|||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|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1|||Pro residues|||Reduces affinity for cAMP and impairs tetramerization.|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054108 http://togogenome.org/gene/10090:Leprot ^@ http://purl.uniprot.org/uniprot/O89013 ^@ 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 gene-related protein ^@ http://purl.uniprot.org/annotation/PRO_0000215195|||http://purl.uniprot.org/annotation/VSP_039718 http://togogenome.org/gene/10090:Cnp ^@ http://purl.uniprot.org/uniprot/P16330|||http://purl.uniprot.org/uniprot/Q3TYL9|||http://purl.uniprot.org/uniprot/Q3TYV5 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ 2',3'-cyclic-nucleotide 3'-phosphodiesterase|||Cyclic nucleotide phosphodiesterase catalytic|||Cysteine methyl ester|||In isoform CNPI.|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Proton donor|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000089962|||http://purl.uniprot.org/annotation/PRO_0000422297|||http://purl.uniprot.org/annotation/VSP_004172 http://togogenome.org/gene/10090:Ndufab1 ^@ http://purl.uniprot.org/uniprot/Q569N0|||http://purl.uniprot.org/uniprot/Q9CR21 ^@ 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_0000000562 http://togogenome.org/gene/10090:Taf1c ^@ http://purl.uniprot.org/uniprot/Q6PDZ2 ^@ 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|||Phosphothreonine|||Polar residues|||TATA box-binding protein-associated factor RNA polymerase I subunit C ^@ http://purl.uniprot.org/annotation/PRO_0000118864 http://togogenome.org/gene/10090:Pxdc1 ^@ http://purl.uniprot.org/uniprot/Q8JZU6 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||PX|||PX domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000297574|||http://purl.uniprot.org/annotation/VSP_027284|||http://purl.uniprot.org/annotation/VSP_027285|||http://purl.uniprot.org/annotation/VSP_027286 http://togogenome.org/gene/10090:Tram2 ^@ http://purl.uniprot.org/uniprot/Q924Z5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||TLC|||Translocating chain-associated membrane protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000185533 http://togogenome.org/gene/10090:Mmaa ^@ http://purl.uniprot.org/uniprot/Q8C7H1 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Sequence Conflict|||Transit Peptide ^@ Methylmalonic aciduria type A homolog, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000002286 http://togogenome.org/gene/10090:Apoa1 ^@ http://purl.uniprot.org/uniprot/Q00623 ^@ Chain|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn ^@ Chain|||Helix|||Mass|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn ^@ 1|||10|||10 X approximate tandem repeats|||2|||3; half-length|||4|||5|||6|||7; truncated|||8|||9; half-length|||Apolipoprotein A-I|||In strain: BALB/c, C3H and ICR.|||Methionine sulfoxide|||Proapolipoprotein A-I|||Strain BALB/c. Without methionine sulfoxide.|||Strain C57BL/6. With 1 methionine sulfoxide.|||Strain C57BL/6. Without methionine sulfoxide.|||Truncated apolipoprotein A-I ^@ http://purl.uniprot.org/annotation/PRO_0000001946|||http://purl.uniprot.org/annotation/PRO_0000416576|||http://purl.uniprot.org/annotation/PRO_0000425326 http://togogenome.org/gene/10090:Shisa2 ^@ http://purl.uniprot.org/uniprot/Q8QZV2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Protein shisa-2 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000022616 http://togogenome.org/gene/10090:Zscan22 ^@ http://purl.uniprot.org/uniprot/Q3TQC3|||http://purl.uniprot.org/uniprot/Q8BGS5|||http://purl.uniprot.org/uniprot/Q8C5G3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues|||SCAN box ^@ http://togogenome.org/gene/10090:Tdpoz8 ^@ http://purl.uniprot.org/uniprot/B7ZWN5|||http://purl.uniprot.org/uniprot/Q3UT66 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ BTB|||MATH ^@ http://togogenome.org/gene/10090:Ccdc138 ^@ http://purl.uniprot.org/uniprot/Q0VF22 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Region ^@ Coiled-coil domain-containing protein 138|||Disordered|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000288456 http://togogenome.org/gene/10090:Tra2b ^@ http://purl.uniprot.org/uniprot/F8WJG3|||http://purl.uniprot.org/uniprot/P62996 ^@ 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 ^@ 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.|||Linker|||N-acetylserine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||RRM|||Removed|||Transformer-2 protein homolog beta ^@ http://purl.uniprot.org/annotation/PRO_0000081984|||http://purl.uniprot.org/annotation/VSP_011509|||http://purl.uniprot.org/annotation/VSP_011510 http://togogenome.org/gene/10090:Ralb ^@ http://purl.uniprot.org/uniprot/Q8CCG5|||http://purl.uniprot.org/uniprot/Q9JIW9 ^@ 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|||Disordered|||Effector region|||Ras-related protein Ral-B|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000082699|||http://purl.uniprot.org/annotation/PRO_0000281351 http://togogenome.org/gene/10090:Foxc1 ^@ http://purl.uniprot.org/uniprot/Q61572 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disordered|||Fork-head|||Forkhead box protein C1|||Inhibits interaction with GLI2. Decreased nuclear colocalization with GLI2. No effect on DNA-binding. Decreased Ihh-induced transcriptional activity and transcription coactivator activity with GLI2.|||No effect on protein stability, inhibited sumoylation, increased transcriptional activity; when associated with R-229.|||No effect on protein stability, inhibited sumoylation, increased transcriptional activity; when associated with R-258.|||No effect on sumoylation; when associated with 6-A--A-9; A-237; A-243 and A-320.|||No effect on sumoylation; when associated with 6-A--A-9; A-237; A-243 and A-521.|||No effect on sumoylation; when associated with 6-A--A-9; A-237; A-320 and A-521.|||No effect on sumoylation; when associated with 6-A--A-9; A-243; A-320 and A-521.|||No effect on sumoylation; when associated with A-237; A-243; A-320 and A-521.|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000091807 http://togogenome.org/gene/10090:Klc3 ^@ http://purl.uniprot.org/uniprot/Q91W40 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||Kinesin light chain 3|||Phosphoserine|||Phosphothreonine|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5 ^@ http://purl.uniprot.org/annotation/PRO_0000230786 http://togogenome.org/gene/10090:Arnt ^@ http://purl.uniprot.org/uniprot/P53762|||http://purl.uniprot.org/uniprot/Q3ULM2 ^@ 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 ^@ Aryl hydrocarbon receptor nuclear translocator|||BHLH|||DNA-binding|||Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Impairs heterodimer formation with EPAS1; when associated with A-366. Impairs heterodimer formation with HIF1A; when associated with A-366. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.|||Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.|||Disordered|||Does not affect transcription factor activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Highly reduces transcription activity. Impairs interaction with AHR. Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability.|||Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability.|||Impairs heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.|||In isoform Short.|||Interfers with transcription factor activity.|||Markedly decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.|||Markedly decreases heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Impairs heterodimer formation with EPAS1; when associated with N-448. Impairs heterodimer formation with HIF1A; when associated with N-448. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.|||Markedly decreases heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.|||Mediates the transcription activity and dimerization of the AHR:ARNT complex|||N-acetylalanine|||PAC|||PAS|||PAS 1|||PAS 2|||Phosphoserine|||Polar residues|||Reduces DNA binding.|||Reduces DNA binding. Decreases transcription factor activity.|||Reduces transcription activity. Markedly reduces interaction with AHR. Impairs heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability.|||Removed|||Required for heterodimer formation with EPAS1|||Required for heterodimer formation with HIF1A|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127119|||http://purl.uniprot.org/annotation/VSP_002093 http://togogenome.org/gene/10090:Fubp3 ^@ http://purl.uniprot.org/uniprot/A2AJ72|||http://purl.uniprot.org/uniprot/Q3TIX6|||http://purl.uniprot.org/uniprot/Q8BYI4 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Far upstream element-binding protein C-terminal|||K Homology|||Polar residues ^@ http://togogenome.org/gene/10090:Sanbr ^@ http://purl.uniprot.org/uniprot/Q68FF0 ^@ 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 ^@ BTB|||Disordered|||In isoform 2.|||Polar residues|||SANT|||SANT and BTB domain regulator of class switch recombination ^@ http://purl.uniprot.org/annotation/PRO_0000324599|||http://purl.uniprot.org/annotation/VSP_032303 http://togogenome.org/gene/10090:Psmb5 ^@ http://purl.uniprot.org/uniprot/O55234 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Propeptide|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Propeptide|||Sequence Conflict|||Strand|||Turn ^@ Nucleophile|||Proteasome subunit beta type-5|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000026591|||http://purl.uniprot.org/annotation/PRO_0000026592 http://togogenome.org/gene/10090:Cdk17 ^@ http://purl.uniprot.org/uniprot/Q8K0D0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Cyclin-dependent kinase 17|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086488|||http://purl.uniprot.org/annotation/VSP_010640|||http://purl.uniprot.org/annotation/VSP_010641 http://togogenome.org/gene/10090:Ctns ^@ http://purl.uniprot.org/uniprot/P57757|||http://purl.uniprot.org/uniprot/Q542U5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Abolished cystine transport. Abolished interaction with components of the v-ATPase and Ragulator complexes. Does not affect ability to lysosomal localization of LAMP2A.|||Cystinosin|||Cytoplasmic|||Helical|||Lumenal|||Lysosomal targeting motif|||N-linked (GlcNAc...) asparagine|||PQ-loop 1|||PQ-loop 2|||protonated residue following cystine-binding ^@ http://purl.uniprot.org/annotation/PRO_0000205515|||http://purl.uniprot.org/annotation/PRO_5014309543 http://togogenome.org/gene/10090:Acan ^@ http://purl.uniprot.org/uniprot/Q61282 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Aggrecan core protein|||C-type lectin|||CS-1|||CS-2|||Cell attachment site|||Disordered|||G1-A|||G1-B|||G1-B'|||G2-B|||G2-B'|||G3|||Ig-like V-type|||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|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_0000017507 http://togogenome.org/gene/10090:Slc6a18 ^@ http://purl.uniprot.org/uniprot/A0A217FL56|||http://purl.uniprot.org/uniprot/O88576 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreases protein abundance. Strong decreases of cell surface localization. Strong decreases on alanine uptake 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|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||No effect on protein abundance. Almost complete loss of cell surface localization. Decreases alanine uptake activity.|||No effect on protein abundance. Increases localization to the cell membrane. Increases alanine uptake activity.|||No effect on protein abundance. No effect on cell surface expression. Decreases alanine uptake activity.|||No effect on protein abundance. No effect on cell surface localization. Decreases alanine uptake activity.|||No effect on protein abundance. No effect on cell surface localization. Increases alanine uptake activity.|||No effect on protein abundance. No effect on cell surface localization. No effect on alanine uptake activity.|||No effect on protein abundance. Strong decrease of cell surface localization. Decreases alanine uptake.|||No effect on protein abundance. Strong decreases of cell surface localization. Decreases alanine uptake activity.|||No effect on protein abundance. Strong decreases of cell surface localization. Decreases alanine uptake.|||Sodium-dependent neutral amino acid transporter B(0)AT3 ^@ http://purl.uniprot.org/annotation/PRO_0000214807|||http://purl.uniprot.org/annotation/VSP_050363|||http://purl.uniprot.org/annotation/VSP_050364|||http://purl.uniprot.org/annotation/VSP_050365|||http://purl.uniprot.org/annotation/VSP_050366|||http://purl.uniprot.org/annotation/VSP_050367|||http://purl.uniprot.org/annotation/VSP_050697 http://togogenome.org/gene/10090:Pigc ^@ http://purl.uniprot.org/uniprot/Q9CXR4 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit C ^@ http://purl.uniprot.org/annotation/PRO_0000058432 http://togogenome.org/gene/10090:Haus5 ^@ http://purl.uniprot.org/uniprot/Q9D786 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ HAUS augmin-like complex subunit 5|||In isoform 2.|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000050777|||http://purl.uniprot.org/annotation/VSP_013929|||http://purl.uniprot.org/annotation/VSP_013930 http://togogenome.org/gene/10090:Glb1l ^@ http://purl.uniprot.org/uniprot/Q8VC60 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Beta-galactosidase-1-like protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000313606|||http://purl.uniprot.org/annotation/VSP_030060|||http://purl.uniprot.org/annotation/VSP_030061|||http://purl.uniprot.org/annotation/VSP_030062 http://togogenome.org/gene/10090:Wnt4 ^@ http://purl.uniprot.org/uniprot/P22724 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-4 ^@ http://purl.uniprot.org/annotation/PRO_0000041422 http://togogenome.org/gene/10090:Or4c100 ^@ http://purl.uniprot.org/uniprot/Q7TR16 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dynlt2a3 ^@ http://purl.uniprot.org/uniprot/P11985 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Disordered|||Dynein light chain Tctex-type protein 2|||In T-haplotype.|||In isoform 2.|||Requires 2 nucleotide substitutions; in T-haplotype. ^@ http://purl.uniprot.org/annotation/PRO_0000072471|||http://purl.uniprot.org/annotation/VSP_004449 http://togogenome.org/gene/10090:Papln ^@ http://purl.uniprot.org/uniprot/B7ZN28|||http://purl.uniprot.org/uniprot/Q9EPX2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide ^@ BPTI/Kunitz inhibitor|||Disordered|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||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_0000324551|||http://purl.uniprot.org/annotation/PRO_5015087436 http://togogenome.org/gene/10090:Mrpl12 ^@ http://purl.uniprot.org/uniprot/Q9DB15 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Large ribosomal subunit protein bL12m|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000030459 http://togogenome.org/gene/10090:Cx3cl1 ^@ http://purl.uniprot.org/uniprot/O35188 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chemokine and involved in interaction with ITGAV:ITGB3 and ITGA4:ITGB1|||Cleavage; to produce soluble form|||Cytoplasmic|||Disordered|||Extracellular|||Fractalkine|||Helical|||Mucin-like stalk|||Polar residues|||Processed fractalkine ^@ http://purl.uniprot.org/annotation/PRO_0000005253|||http://purl.uniprot.org/annotation/PRO_0000296225 http://togogenome.org/gene/10090:Zfp598 ^@ http://purl.uniprot.org/uniprot/Q80YR4 ^@ 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|||C2H2-type|||Disordered|||E3 ubiquitin-protein ligase ZNF598|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000250569|||http://purl.uniprot.org/annotation/VSP_020666|||http://purl.uniprot.org/annotation/VSP_020667 http://togogenome.org/gene/10090:Hoxa2 ^@ http://purl.uniprot.org/uniprot/P31245 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region ^@ Antp-type hexapeptide|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Hox-A2 ^@ http://purl.uniprot.org/annotation/PRO_0000200037 http://togogenome.org/gene/10090:Sumf2 ^@ http://purl.uniprot.org/uniprot/Q8BPG6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Inactive C-alpha-formylglycine-generating enzyme 2|||N-linked (GlcNAc...) asparagine|||Non-canonical ER retention motif|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000033460 http://togogenome.org/gene/10090:Mtmr3 ^@ http://purl.uniprot.org/uniprot/B1ATD5|||http://purl.uniprot.org/uniprot/Q80U24 ^@ Active Site|||Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||FYVE-type|||Myotubularin phosphatase|||Phosphocysteine intermediate|||Polar residues ^@ http://togogenome.org/gene/10090:Unc13d ^@ http://purl.uniprot.org/uniprot/B2RUP2|||http://purl.uniprot.org/uniprot/Q80UG7 ^@ 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 ^@ C2|||C2 1|||C2 2|||Disordered|||In isoform 2.|||Interaction with RAB27A|||MHD1|||MHD2|||Phosphoserine|||Protein unc-13 homolog D ^@ http://purl.uniprot.org/annotation/PRO_0000382950|||http://purl.uniprot.org/annotation/VSP_037950 http://togogenome.org/gene/10090:Bves ^@ http://purl.uniprot.org/uniprot/Q9ES83 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Almost abolishes cAMP-binding. Interaction with KCNK2 is not inhibited by cAMP.|||Blood vessel epicardial substance|||Cytoplasmic|||Decreases cAMP-binding.|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||No effect on cAMP-binding.|||Phosphoserine|||Polar residues|||Required for interaction with CAV3|||Required for interaction with KCNK2 ^@ http://purl.uniprot.org/annotation/PRO_0000046792 http://togogenome.org/gene/10090:Insrr ^@ http://purl.uniprot.org/uniprot/Q3UQC8|||http://purl.uniprot.org/uniprot/Q9WTL4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||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|||Protein kinase|||Proton acceptor|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000016704|||http://purl.uniprot.org/annotation/PRO_0000016705|||http://purl.uniprot.org/annotation/PRO_0000016706|||http://purl.uniprot.org/annotation/PRO_5004230133 http://togogenome.org/gene/10090:Ufm1 ^@ http://purl.uniprot.org/uniprot/P61961 ^@ Chain|||Crosslink|||Helix|||Modification|||Molecule Processing|||Propeptide|||Secondary Structure|||Strand ^@ Chain|||Crosslink|||Helix|||Propeptide|||Strand ^@ Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)|||Removed in mature form|||Ubiquitin-fold modifier 1 ^@ http://purl.uniprot.org/annotation/PRO_0000042126|||http://purl.uniprot.org/annotation/PRO_0000042127 http://togogenome.org/gene/10090:Pcdha11 ^@ http://purl.uniprot.org/uniprot/Q91Y19 ^@ 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|||Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099521 http://togogenome.org/gene/10090:Cdh10 ^@ http://purl.uniprot.org/uniprot/P70408 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-10|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000126646|||http://purl.uniprot.org/annotation/PRO_0000269662 http://togogenome.org/gene/10090:Tnfrsf13c ^@ http://purl.uniprot.org/uniprot/Q3SXS6|||http://purl.uniprot.org/uniprot/Q9D8D0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Essential for TNFSF13B/TALL1/BAFF/BLyS binding|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||TNFR-Cys; truncated|||Tumor necrosis factor receptor superfamily member 13C|||Tumour necrosis factor receptor 13C TALL-1 binding ^@ http://purl.uniprot.org/annotation/PRO_0000058934|||http://purl.uniprot.org/annotation/VSP_006506 http://togogenome.org/gene/10090:Rpusd3 ^@ http://purl.uniprot.org/uniprot/B7ZMQ0|||http://purl.uniprot.org/uniprot/Q14AI6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Disordered|||In isoform 2.|||Mitochondrial mRNA pseudouridine synthase Rpusd3|||Mitochondrion|||Pseudouridine synthase RsuA/RluA-like ^@ http://purl.uniprot.org/annotation/PRO_0000300823|||http://purl.uniprot.org/annotation/VSP_027871 http://togogenome.org/gene/10090:Rbx1 ^@ http://purl.uniprot.org/uniprot/P62878 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Zinc Finger ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000056014|||http://purl.uniprot.org/annotation/PRO_0000423265 http://togogenome.org/gene/10090:Fbxo46 ^@ http://purl.uniprot.org/uniprot/Q8BG80 ^@ 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|||Phosphothreonine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000119951 http://togogenome.org/gene/10090:Gm20920 ^@ http://purl.uniprot.org/uniprot/A0A087WRK1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Obox1 ^@ http://purl.uniprot.org/uniprot/Q9D350 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Cd8b1 ^@ http://purl.uniprot.org/uniprot/P10300|||http://purl.uniprot.org/uniprot/Q3TEK8 ^@ 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|||Helical|||Ig-like|||Ig-like V-type|||Ig-like domain-containing protein|||In allele Lyt-3-alpha.|||In allele Lyt-3A.|||N-linked (GlcNAc...) asparagine|||T-cell surface glycoprotein CD8 beta chain ^@ http://purl.uniprot.org/annotation/PRO_0000014644|||http://purl.uniprot.org/annotation/PRO_5010843279 http://togogenome.org/gene/10090:Slc25a46 ^@ http://purl.uniprot.org/uniprot/Q9CQS4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial outer membrane protein SLC25A46|||Phosphoserine|||Phosphothreonine|||Solcar 1|||Solcar 2 ^@ http://purl.uniprot.org/annotation/PRO_0000291829 http://togogenome.org/gene/10090:Tlnrd1 ^@ http://purl.uniprot.org/uniprot/Q9ERE8 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylalanine|||Removed|||Talin rod domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000096442 http://togogenome.org/gene/10090:F830045P16Rik ^@ http://purl.uniprot.org/uniprot/Q8BJ95 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Ig-like ^@ http://togogenome.org/gene/10090:Akr1b10 ^@ http://purl.uniprot.org/uniprot/G5E895|||http://purl.uniprot.org/uniprot/Q8BIV6 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Site ^@ Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor ^@ http://togogenome.org/gene/10090:Pgap1 ^@ http://purl.uniprot.org/uniprot/Q3UQY2|||http://purl.uniprot.org/uniprot/Q3UUQ7 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||GPI inositol-deacylase|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000277624|||http://purl.uniprot.org/annotation/VSP_023045|||http://purl.uniprot.org/annotation/VSP_023046 http://togogenome.org/gene/10090:Gp9 ^@ http://purl.uniprot.org/uniprot/O88186 ^@ 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|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Platelet glycoprotein IX ^@ http://purl.uniprot.org/annotation/PRO_0000378456 http://togogenome.org/gene/10090:Or2at1 ^@ http://purl.uniprot.org/uniprot/E9Q519 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trpv1 ^@ http://purl.uniprot.org/uniprot/Q3V318|||http://purl.uniprot.org/uniprot/Q704Y3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 10-fold less potently activated by the Scolopendra mutilans RhTx toxin.|||13-fold less potently activated by the Scolopendra mutilans RhTx toxin.|||17-fold less potently activated by the Scolopendra mutilans RhTx toxin.|||8-fold less potently activated by the Scolopendra mutilans RhTx toxin.|||AD|||ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with calmodulin|||Ion transport|||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|||Pro residues|||Required for PIP2-mediated channel inhibition|||Selectivity filter|||Transient receptor potential cation channel subfamily V member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000215339|||http://purl.uniprot.org/annotation/VSP_013430 http://togogenome.org/gene/10090:Tlr11 ^@ http://purl.uniprot.org/uniprot/Q6R5P0|||http://purl.uniprot.org/uniprot/V9GWT0 ^@ 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 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-linked (GlcNAc...) asparagine|||TIR|||Toll-like receptor 11 ^@ http://purl.uniprot.org/annotation/PRO_0000042793 http://togogenome.org/gene/10090:Or4c35 ^@ http://purl.uniprot.org/uniprot/Q8VGN9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dpys ^@ http://purl.uniprot.org/uniprot/Q9EQF5 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Dihydropyrimidinase|||N6-carboxylysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||via carbamate group ^@ http://purl.uniprot.org/annotation/PRO_0000165907 http://togogenome.org/gene/10090:Zmiz1 ^@ http://purl.uniprot.org/uniprot/Q3V215|||http://purl.uniprot.org/uniprot/Q6P1E1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000218988|||http://purl.uniprot.org/annotation/VSP_012187 http://togogenome.org/gene/10090:Klk1b9 ^@ http://purl.uniprot.org/uniprot/P15949 ^@ 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|||Kallikrein 1-related peptidase b9|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027979|||http://purl.uniprot.org/annotation/PRO_0000027980 http://togogenome.org/gene/10090:Gtf2h3 ^@ http://purl.uniprot.org/uniprot/Q8VD76 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Zinc Finger ^@ C4-type|||General transcription factor IIH subunit 3 ^@ http://purl.uniprot.org/annotation/PRO_0000119252 http://togogenome.org/gene/10090:Atp7a ^@ http://purl.uniprot.org/uniprot/A2AG68|||http://purl.uniprot.org/uniprot/Q64430 ^@ Active Site|||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|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane ^@ 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|||Has no effect on trafficking from endosome to TGN.|||Helical|||Impaired endocytosis associated with retention at the plasma membrane.|||Impaired trafficking from endosome to TGN.|||In MD.|||N-linked (GlcNAc...) asparagine|||PDZD11-binding|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000046312 http://togogenome.org/gene/10090:Psg26 ^@ http://purl.uniprot.org/uniprot/Q4KL65 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Serping1 ^@ http://purl.uniprot.org/uniprot/P97290 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Plasma protease C1 inhibitor|||Polar residues|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000032515 http://togogenome.org/gene/10090:Mrps30 ^@ http://purl.uniprot.org/uniprot/Q9D0G0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Large ribosomal subunit protein mL65 ^@ http://purl.uniprot.org/annotation/PRO_0000087721 http://togogenome.org/gene/10090:Pgghg ^@ http://purl.uniprot.org/uniprot/Q8BP56 ^@ 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.|||In isoform 3.|||Protein-glucosylgalactosylhydroxylysine glucosidase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000329005|||http://purl.uniprot.org/annotation/VSP_032897|||http://purl.uniprot.org/annotation/VSP_032898|||http://purl.uniprot.org/annotation/VSP_032899|||http://purl.uniprot.org/annotation/VSP_032900 http://togogenome.org/gene/10090:Fbxl9 ^@ http://purl.uniprot.org/uniprot/A0A1B0GQY9|||http://purl.uniprot.org/uniprot/Q3UG51 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ F-box ^@ http://togogenome.org/gene/10090:Ticam2 ^@ http://purl.uniprot.org/uniprot/Q8BJQ4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||N-myristoyl glycine|||Phosphotyrosine|||Removed|||Results in exclusive localization to early endosomes and no effect on ability to promote LPS-induced IL6 and CCL5 production; when associated with E-15 and E-17.|||Results in exclusive localization to early endosomes and no effect on ability to promote LPS-induced IL6 and CCL5 production; when associated with E-7 and E-15.|||Results in exclusive localization to early endosomes and no effect on ability to promote LPS-induced IL6 and CCL5 production; when associated with E-7 and E-17.|||Results in relocalization from membrane to cytosol; impairs ability to promote LPS-induced IL6 and CCL5 production.|||TIR|||TIR domain-containing adapter molecule 2 ^@ http://purl.uniprot.org/annotation/PRO_0000317690 http://togogenome.org/gene/10090:Mfsd4a ^@ http://purl.uniprot.org/uniprot/Q6PDC8 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Major facilitator superfamily domain-containing protein 4A ^@ http://purl.uniprot.org/annotation/PRO_0000273396|||http://purl.uniprot.org/annotation/VSP_022541|||http://purl.uniprot.org/annotation/VSP_022542|||http://purl.uniprot.org/annotation/VSP_022543 http://togogenome.org/gene/10090:Ccnc ^@ http://purl.uniprot.org/uniprot/Q3U6Q7|||http://purl.uniprot.org/uniprot/Q3UXL9|||http://purl.uniprot.org/uniprot/Q62447|||http://purl.uniprot.org/uniprot/Q8CAS3 ^@ 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 ^@ Cyclin N-terminal|||Cyclin-C|||Cyclin-like|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080421 http://togogenome.org/gene/10090:Notum ^@ http://purl.uniprot.org/uniprot/Q8R116 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Abolishes enzyme activity. Unable to mediate serine depalmitoleoylation of WNT proteins.|||Charge relay system|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Palmitoleoyl-protein carboxylesterase NOTUM|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000318756|||http://purl.uniprot.org/annotation/VSP_031295|||http://purl.uniprot.org/annotation/VSP_031296 http://togogenome.org/gene/10090:Vstm4 ^@ http://purl.uniprot.org/uniprot/T1NXB5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Mass|||Modification|||Molecule Processing|||Peptide|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mass|||Peptide|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like|||N-linked (GlcNAc...) asparagine|||Peptide Lv|||V-set and transmembrane domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000431304|||http://purl.uniprot.org/annotation/PRO_0000431305 http://togogenome.org/gene/10090:Smurf2 ^@ http://purl.uniprot.org/uniprot/A2A5Z6|||http://purl.uniprot.org/uniprot/Q9CSE3 ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Splice Variant ^@ C2|||E3 ubiquitin-protein ligase SMURF2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||WW 1|||WW 2|||WW 3 ^@ http://purl.uniprot.org/annotation/PRO_0000358318|||http://purl.uniprot.org/annotation/VSP_036055|||http://purl.uniprot.org/annotation/VSP_036056 http://togogenome.org/gene/10090:Cd19 ^@ http://purl.uniprot.org/uniprot/P25918|||http://purl.uniprot.org/uniprot/Q3TQG5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Acidic residues|||B-lymphocyte antigen CD19|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014649|||http://purl.uniprot.org/annotation/PRO_0000014650 http://togogenome.org/gene/10090:Trpc4ap ^@ http://purl.uniprot.org/uniprot/Q3TB80|||http://purl.uniprot.org/uniprot/Q9JLV2 ^@ 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 ^@ In isoform 2.|||Interaction with TNFRSF1A|||N-acetylalanine|||Removed|||Short transient receptor potential channel 4-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000072642|||http://purl.uniprot.org/annotation/VSP_003983 http://togogenome.org/gene/10090:Abcg3 ^@ http://purl.uniprot.org/uniprot/Q99P81 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ABC transmembrane type-2|||ABC transporter|||ATP-binding cassette sub-family G member 3|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6 ^@ http://purl.uniprot.org/annotation/PRO_0000093391 http://togogenome.org/gene/10090:Hilpda ^@ http://purl.uniprot.org/uniprot/Q9JLS0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Hypoxia-inducible lipid droplet-associated protein|||Required for targeting to lipid droplets ^@ http://purl.uniprot.org/annotation/PRO_0000083977 http://togogenome.org/gene/10090:Cfap418 ^@ http://purl.uniprot.org/uniprot/Q3UJP5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Cilia- and flagella-associated protein 418|||Disordered|||Required for interaction with FAM161A ^@ http://purl.uniprot.org/annotation/PRO_0000271059 http://togogenome.org/gene/10090:Fjx1 ^@ http://purl.uniprot.org/uniprot/Q8BQB4 ^@ 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|||Four-jointed box protein 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000333046 http://togogenome.org/gene/10090:Pmel ^@ http://purl.uniprot.org/uniprot/Q60696 ^@ 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|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ 1|||10|||10 X 13 AA approximate tandem repeats, RPT domain|||2|||3|||4|||5|||6|||7|||8|||9|||Amyloidogenic unit|||Cleavage; by ADAM metalloproteinases|||Cleavage; by furin-like proprotein convertase|||Cytoplasmic|||Disordered|||ER exit signal|||Endocytosis signal|||Essential for fibril formation|||Forms abnormal block-like assemblies devoid of fibrillar sheet structure. Does not affect protein maturation. Does not affect fibril formation.|||Forms abnormal block-like assemblies devoid of fibrillar sheet structure; when associated with 304-P--T-429 del.|||Helical|||In Silver.|||Interchain (in monomeric form)|||Intrachain (in dimeric form)|||Kringle-like fold|||Lumenal|||M-alpha|||M-beta|||Melanocyte protein PMEL|||N-linked (GlcNAc...) asparagine|||PKD ^@ http://purl.uniprot.org/annotation/PRO_0000024713|||http://purl.uniprot.org/annotation/PRO_0000386649|||http://purl.uniprot.org/annotation/PRO_0000386650 http://togogenome.org/gene/10090:Crhr2 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLK7|||http://purl.uniprot.org/uniprot/E9QNK5|||http://purl.uniprot.org/uniprot/Q3UQP0|||http://purl.uniprot.org/uniprot/Q5ERJ2|||http://purl.uniprot.org/uniprot/Q60748 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||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|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||Corticotropin-releasing factor receptor 2|||Cytoplasmic|||Disordered|||Disrupts internal salt bridge and abrogates ligand recognition.|||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.|||N-linked (GlcNAc...) asparagine|||Not cleaved ^@ http://purl.uniprot.org/annotation/PRO_0000012821|||http://purl.uniprot.org/annotation/PRO_5003243347|||http://purl.uniprot.org/annotation/PRO_5008929781|||http://purl.uniprot.org/annotation/PRO_5015097493|||http://purl.uniprot.org/annotation/PRO_5015097873|||http://purl.uniprot.org/annotation/VSP_053568 http://togogenome.org/gene/10090:Adamts20 ^@ http://purl.uniprot.org/uniprot/P59511|||http://purl.uniprot.org/uniprot/Q3UQW9 ^@ 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 20|||Disintegrin|||Disordered|||GON|||In isoform 2.|||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_0000029208|||http://purl.uniprot.org/annotation/PRO_0000029209|||http://purl.uniprot.org/annotation/VSP_007606|||http://purl.uniprot.org/annotation/VSP_007607 http://togogenome.org/gene/10090:Hsph1 ^@ http://purl.uniprot.org/uniprot/Q61699 ^@ 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|||Heat shock protein 105 kDa|||In isoform HSP105-beta.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000078285|||http://purl.uniprot.org/annotation/VSP_002429 http://togogenome.org/gene/10090:Elovl4 ^@ http://purl.uniprot.org/uniprot/Q9EQC4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Di-lysine motif|||Disordered|||Elongation of very long chain fatty acids protein 4|||Helical|||Loss of N-glycosylation. No effect on fatty acid elongase activity.|||Loss of fatty acid elongase activity.|||Loss of localization to the endoplasmic reticulum. Loss of fatty acid elongase activity.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000207545 http://togogenome.org/gene/10090:Ublcp1 ^@ http://purl.uniprot.org/uniprot/Q8BGR9 ^@ 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|||Splice Variant|||Strand|||Turn ^@ FCP1 homology|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Removed|||Ubiquitin-like|||Ubiquitin-like domain-containing CTD phosphatase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000242641|||http://purl.uniprot.org/annotation/VSP_019458 http://togogenome.org/gene/10090:Lrtm1 ^@ http://purl.uniprot.org/uniprot/A6H6T2|||http://purl.uniprot.org/uniprot/Q8BXQ3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||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 1|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000279757|||http://purl.uniprot.org/annotation/PRO_5014296999 http://togogenome.org/gene/10090:Rasgrp2 ^@ http://purl.uniprot.org/uniprot/Q9QUG9 ^@ Binding Site|||Chain|||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|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||EF-hand 1|||EF-hand 2|||In isoform 2.|||In isoform 3.|||N-terminal Ras-GEF|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||RAS guanyl-releasing protein 2|||Ras-GEF ^@ http://purl.uniprot.org/annotation/PRO_0000315609|||http://purl.uniprot.org/annotation/VSP_030577|||http://purl.uniprot.org/annotation/VSP_030578|||http://purl.uniprot.org/annotation/VSP_030579 http://togogenome.org/gene/10090:Actrt2 ^@ http://purl.uniprot.org/uniprot/Q9D9L5 ^@ Chain|||Molecule Processing ^@ Chain ^@ Actin-related protein T2 ^@ http://purl.uniprot.org/annotation/PRO_0000089145 http://togogenome.org/gene/10090:Slc35a2 ^@ http://purl.uniprot.org/uniprot/A2AER4|||http://purl.uniprot.org/uniprot/Q3UIP1|||http://purl.uniprot.org/uniprot/Q9JIH0|||http://purl.uniprot.org/uniprot/Q9R0M8 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||UDP-galactose translocator ^@ http://purl.uniprot.org/annotation/PRO_0000213354 http://togogenome.org/gene/10090:Car6 ^@ http://purl.uniprot.org/uniprot/P18761|||http://purl.uniprot.org/uniprot/Q3TTT1|||http://purl.uniprot.org/uniprot/Q3V197 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide ^@ Alpha-carbonic anhydrase|||Alpha-carbonic anhydrase domain-containing protein|||Carbonic anhydrase 6|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004242|||http://purl.uniprot.org/annotation/PRO_5004229671|||http://purl.uniprot.org/annotation/PRO_5004230337 http://togogenome.org/gene/10090:Vac14 ^@ http://purl.uniprot.org/uniprot/Q80WQ2 ^@ 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|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||In ingls; loss of interaction with Pikfyve but not with Fig4.|||Mediates interaction with the PDZ domain of NOS1|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein VAC14 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000300486 http://togogenome.org/gene/10090:Necab1 ^@ http://purl.uniprot.org/uniprot/Q8BG18 ^@ 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|||Region|||Sequence Conflict ^@ ABM|||Disordered|||EF-hand 1|||EF-hand 2|||N-terminal EF-hand calcium-binding protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000282610 http://togogenome.org/gene/10090:Fut7 ^@ http://purl.uniprot.org/uniprot/E2D0W5|||http://purl.uniprot.org/uniprot/Q11131|||http://purl.uniprot.org/uniprot/Q3SWS0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Alpha-(1,3)-fucosyltransferase 7|||Cytoplasmic|||Fucosyltransferase N-terminal|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000221114|||http://purl.uniprot.org/annotation/VSP_001781 http://togogenome.org/gene/10090:Cfap206 ^@ http://purl.uniprot.org/uniprot/Q6PE87 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Cilia- and flagella-associated protein 206|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000358910|||http://purl.uniprot.org/annotation/VSP_036124|||http://purl.uniprot.org/annotation/VSP_036125 http://togogenome.org/gene/10090:Ubxn6 ^@ http://purl.uniprot.org/uniprot/Q99PL6 ^@ 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.|||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_0000211026|||http://purl.uniprot.org/annotation/VSP_007454 http://togogenome.org/gene/10090:Scnn1b ^@ http://purl.uniprot.org/uniprot/A2RS45|||http://purl.uniprot.org/uniprot/Q9WU38 ^@ 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 ^@ Amiloride-sensitive sodium channel subunit beta|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000181269 http://togogenome.org/gene/10090:Sf3b1 ^@ http://purl.uniprot.org/uniprot/G5E866|||http://purl.uniprot.org/uniprot/Q3US00|||http://purl.uniprot.org/uniprot/Q8C2Y9 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Splicing factor 3B subunit 1 ^@ http://togogenome.org/gene/10090:Phf20l1 ^@ http://purl.uniprot.org/uniprot/A0A5S8DHC4|||http://purl.uniprot.org/uniprot/Q8CCJ9 ^@ 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 ^@ Agenet|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1 and isoform 3.|||In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||N6-acetyllysine|||PHD finger protein 20-like protein 1|||PHD-type|||Phosphoserine|||Polar residues|||Tudor|||Tudor 1|||Tudor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000336002|||http://purl.uniprot.org/annotation/VSP_033785|||http://purl.uniprot.org/annotation/VSP_033786|||http://purl.uniprot.org/annotation/VSP_033788|||http://purl.uniprot.org/annotation/VSP_033789|||http://purl.uniprot.org/annotation/VSP_033790|||http://purl.uniprot.org/annotation/VSP_040409|||http://purl.uniprot.org/annotation/VSP_040410|||http://purl.uniprot.org/annotation/VSP_040411|||http://purl.uniprot.org/annotation/VSP_040412|||http://purl.uniprot.org/annotation/VSP_040413|||http://purl.uniprot.org/annotation/VSP_040414 http://togogenome.org/gene/10090:Eif4e2 ^@ http://purl.uniprot.org/uniprot/D3YUV9|||http://purl.uniprot.org/uniprot/D3Z729|||http://purl.uniprot.org/uniprot/G3X9H1|||http://purl.uniprot.org/uniprot/Q0P688|||http://purl.uniprot.org/uniprot/Q8BMB3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||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|||N6-acetyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000193665 http://togogenome.org/gene/10090:Cyp2d40 ^@ http://purl.uniprot.org/uniprot/Q6P8N9 ^@ Binding Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Lrp12 ^@ http://purl.uniprot.org/uniprot/Q8BUJ9 ^@ 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|||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_0000017340|||http://purl.uniprot.org/annotation/VSP_009821 http://togogenome.org/gene/10090:Gfod2 ^@ http://purl.uniprot.org/uniprot/Q9CYH5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Glucose-fructose oxidoreductase domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000282973 http://togogenome.org/gene/10090:Tcp10a ^@ http://purl.uniprot.org/uniprot/Q80W76 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Centromere protein J C-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Nup37 ^@ http://purl.uniprot.org/uniprot/Q9CWU9 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ Nucleoporin Nup37|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000051110 http://togogenome.org/gene/10090:Or2w6 ^@ http://purl.uniprot.org/uniprot/Q8VFH0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ptch2 ^@ http://purl.uniprot.org/uniprot/O35595 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protein patched homolog 2|||SSD ^@ http://purl.uniprot.org/annotation/PRO_0000205971 http://togogenome.org/gene/10090:Mrps36 ^@ http://purl.uniprot.org/uniprot/Q9CQX8|||http://purl.uniprot.org/uniprot/Q9D6T9 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Alpha-ketoglutarate dehydrogenase component 4|||Basic and acidic residues|||Disordered|||N-acetylglycine|||N6-succinyllysine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087734 http://togogenome.org/gene/10090:Prpf6 ^@ http://purl.uniprot.org/uniprot/Q91YR7 ^@ 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|||HAT 8|||HAT 9|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pre-mRNA-processing factor 6 ^@ http://purl.uniprot.org/annotation/PRO_0000205760|||http://purl.uniprot.org/annotation/VSP_002063|||http://purl.uniprot.org/annotation/VSP_002064 http://togogenome.org/gene/10090:Zbtb7c ^@ http://purl.uniprot.org/uniprot/Q8VCZ7 ^@ 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 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_0000337870 http://togogenome.org/gene/10090:D630003M21Rik ^@ http://purl.uniprot.org/uniprot/A2AC60|||http://purl.uniprot.org/uniprot/Q8BWG4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Uncharacterized protein KIAA1755 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000317285 http://togogenome.org/gene/10090:Cmtm4 ^@ http://purl.uniprot.org/uniprot/Q8CJ61 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Transmembrane ^@ CKLF-like MARVEL transmembrane domain-containing protein 4|||Disordered|||Helical|||MARVEL|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000186104 http://togogenome.org/gene/10090:Srgap2 ^@ http://purl.uniprot.org/uniprot/Q91Z67 ^@ 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 ^@ Abolished RAC1 GTPase activity. Abolished ability to induce neurite branching. No effect on filopodia biogenesis and neurite outgrowth.|||Abolished interaction with HOMER1.|||Basic and acidic residues|||Disordered|||F-BAR|||Loss of the ability to induce filopodia and to initiate neurite outgrowth. Abolished interaction with GPHN.|||Phosphoserine|||Polar residues|||Rho-GAP|||SH3|||SLIT-ROBO Rho GTPase-activating protein 2|||Symmetric dimethylarginine; by PRMT5 ^@ http://purl.uniprot.org/annotation/PRO_0000056768 http://togogenome.org/gene/10090:Ankle2 ^@ http://purl.uniprot.org/uniprot/Q6P1H6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ ANK|||Ankyrin repeat and LEM domain-containing protein 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LEM|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000280243|||http://purl.uniprot.org/annotation/VSP_023576|||http://purl.uniprot.org/annotation/VSP_023577|||http://purl.uniprot.org/annotation/VSP_023578|||http://purl.uniprot.org/annotation/VSP_023579 http://togogenome.org/gene/10090:Isg15 ^@ http://purl.uniprot.org/uniprot/Q4FJR9|||http://purl.uniprot.org/uniprot/Q64339 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Mass|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Site|||Strand ^@ Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Interacts with activating enzyme|||Involved in the ligation of specific target proteins|||LRLRGG|||Removed in mature form|||S-nitrosocysteine|||Ubiquitin-like|||Ubiquitin-like 1|||Ubiquitin-like 2|||Ubiquitin-like protein ISG15 ^@ http://purl.uniprot.org/annotation/PRO_0000035988|||http://purl.uniprot.org/annotation/PRO_0000035989 http://togogenome.org/gene/10090:Ces2a ^@ http://purl.uniprot.org/uniprot/Q8QZR3 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Acyl-ester intermediate|||Charge relay system|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Pyrethroid hydrolase Ces2a ^@ http://purl.uniprot.org/annotation/PRO_0000424210|||http://purl.uniprot.org/annotation/VSP_053352 http://togogenome.org/gene/10090:Prl2c3 ^@ http://purl.uniprot.org/uniprot/A0A0M5HDY5|||http://purl.uniprot.org/uniprot/P04768 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prolactin-2C3 ^@ http://purl.uniprot.org/annotation/PRO_0000032968|||http://purl.uniprot.org/annotation/PRO_5005803015 http://togogenome.org/gene/10090:Igf2 ^@ http://purl.uniprot.org/uniprot/P09535 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Disulfide Bond|||Peptide|||Propeptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ A|||B|||C|||D|||Disordered|||E peptide|||Important for interaction with integrin|||In isoform 2.|||Insulin-like growth factor II|||Preptin ^@ http://purl.uniprot.org/annotation/PRO_0000015720|||http://purl.uniprot.org/annotation/PRO_0000015721|||http://purl.uniprot.org/annotation/PRO_0000370377|||http://purl.uniprot.org/annotation/VSP_059113 http://togogenome.org/gene/10090:Elapor1 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQC6|||http://purl.uniprot.org/uniprot/A2AFS3 ^@ 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|||Endosome/lysosome-associated apoptosis and autophagy regulator 1|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||MRH|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000286601|||http://purl.uniprot.org/annotation/PRO_5001967179|||http://purl.uniprot.org/annotation/VSP_025118|||http://purl.uniprot.org/annotation/VSP_025119|||http://purl.uniprot.org/annotation/VSP_025120 http://togogenome.org/gene/10090:Borcs8 ^@ http://purl.uniprot.org/uniprot/D3Z373|||http://purl.uniprot.org/uniprot/Q9D6Y4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ BLOC-1-related complex subunit 8|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000269844 http://togogenome.org/gene/10090:Rdh1 ^@ http://purl.uniprot.org/uniprot/Q8CGV4|||http://purl.uniprot.org/uniprot/Q8VIJ7 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5004316923|||http://purl.uniprot.org/annotation/PRO_5015099095 http://togogenome.org/gene/10090:Nup88 ^@ http://purl.uniprot.org/uniprot/Q5QNU0|||http://purl.uniprot.org/uniprot/Q8CEC0 ^@ 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 and isoform 3.|||In isoform 3.|||N-acetylalanine|||Nuclear pore complex protein Nup88|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000204888|||http://purl.uniprot.org/annotation/VSP_011195|||http://purl.uniprot.org/annotation/VSP_011196 http://togogenome.org/gene/10090:Ipo13 ^@ http://purl.uniprot.org/uniprot/Q8K0C1 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Splice Variant ^@ 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|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000120759|||http://purl.uniprot.org/annotation/VSP_010936|||http://purl.uniprot.org/annotation/VSP_010937 http://togogenome.org/gene/10090:Anp32b ^@ http://purl.uniprot.org/uniprot/Q9EST5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Splice Variant ^@ Acidic leucine-rich nuclear phosphoprotein 32 family member B|||Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000236252|||http://purl.uniprot.org/annotation/VSP_023520|||http://purl.uniprot.org/annotation/VSP_023521 http://togogenome.org/gene/10090:Tdrp ^@ http://purl.uniprot.org/uniprot/Q8C5P7 ^@ 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|||Testis development-related protein ^@ http://purl.uniprot.org/annotation/PRO_0000308220|||http://purl.uniprot.org/annotation/VSP_028924 http://togogenome.org/gene/10090:Lclat1 ^@ http://purl.uniprot.org/uniprot/B0V2Q7|||http://purl.uniprot.org/uniprot/Q3UN02 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Transmembrane ^@ HXXXXD motif|||Helical|||Lysocardiolipin acyltransferase 1|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phospholipid/glycerol acyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000291578 http://togogenome.org/gene/10090:Itga2b ^@ http://purl.uniprot.org/uniprot/Q9QUM0 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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-IIb|||Integrin alpha-IIb heavy chain|||Integrin alpha-IIb light chain|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000016278|||http://purl.uniprot.org/annotation/PRO_0000016279|||http://purl.uniprot.org/annotation/PRO_0000016280 http://togogenome.org/gene/10090:Or14j10 ^@ http://purl.uniprot.org/uniprot/Q923Q6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Riiad1 ^@ http://purl.uniprot.org/uniprot/Q3KNY5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ RIIa|||RIIa domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000342468 http://togogenome.org/gene/10090:Nkiras2 ^@ http://purl.uniprot.org/uniprot/Q9CR56 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Effector region|||NF-kappa-B inhibitor-interacting Ras-like protein 2|||Small GTPase-like ^@ http://purl.uniprot.org/annotation/PRO_0000225680 http://togogenome.org/gene/10090:Zar1 ^@ http://purl.uniprot.org/uniprot/Q80SU3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Zinc Finger ^@ 3CxxC-type|||Basic and acidic residues|||Disordered|||Does not regulate formation of MARDO membraneless compartment; when associated with A-154.|||Does not regulate formation of MARDO membraneless compartment; when associated with A-161.|||In 4CS mutant; abolished binding to the 3'-UTR of maternal mRNAs; when associated with S-269, S-296 and S-313.|||In 4CS mutant; abolished binding to the 3'-UTR of maternal mRNAs; when associated with S-269, S-296 and S-341.|||In 4CS mutant; abolished binding to the 3'-UTR of maternal mRNAs; when associated with S-269, S-313 and S-341.|||In 4CS mutant; abolished binding to the 3'-UTR of maternal mRNAs; when associated with S-296, S-313 and S-341.|||Mimics phosphorylation state; does not regulate formation of MARDO membraneless compartment; when associated with D-154.|||Mimics phosphorylation state; does not regulate formation of MARDO membraneless compartment; when associated with D-161.|||Phosphoserine; by CDK1|||Phosphothreonine; by CDK1|||Polar residues|||Zygote arrest protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000187012 http://togogenome.org/gene/10090:Adgrd1 ^@ http://purl.uniprot.org/uniprot/B2RXV6|||http://purl.uniprot.org/uniprot/Q80T32 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Adhesion G-protein coupled receptor D1|||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|||N-linked (GlcNAc...) asparagine|||Pentraxin (PTX)|||Polar residues|||Stachel ^@ http://purl.uniprot.org/annotation/PRO_0000307113|||http://purl.uniprot.org/annotation/PRO_5015087161 http://togogenome.org/gene/10090:Smox ^@ http://purl.uniprot.org/uniprot/A2ANQ4|||http://purl.uniprot.org/uniprot/Q3TLR8|||http://purl.uniprot.org/uniprot/Q3UPW5|||http://purl.uniprot.org/uniprot/Q99K82 ^@ 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|||Splice Variant ^@ Amine oxidase|||Basic and acidic residues|||Disordered|||In isoform 10.|||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.|||No change in enzymatic activity.|||Spermine oxidase ^@ http://purl.uniprot.org/annotation/PRO_0000099878|||http://purl.uniprot.org/annotation/VSP_011127|||http://purl.uniprot.org/annotation/VSP_011128|||http://purl.uniprot.org/annotation/VSP_011129|||http://purl.uniprot.org/annotation/VSP_011130|||http://purl.uniprot.org/annotation/VSP_011131|||http://purl.uniprot.org/annotation/VSP_011132|||http://purl.uniprot.org/annotation/VSP_011133|||http://purl.uniprot.org/annotation/VSP_011134|||http://purl.uniprot.org/annotation/VSP_011135|||http://purl.uniprot.org/annotation/VSP_011136|||http://purl.uniprot.org/annotation/VSP_011137|||http://purl.uniprot.org/annotation/VSP_011138 http://togogenome.org/gene/10090:Crip1 ^@ http://purl.uniprot.org/uniprot/P63254 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Cysteine-rich protein 1|||LIM zinc-binding|||N6-acetyllysine|||Omega-N-methylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000075708 http://togogenome.org/gene/10090:Pth2 ^@ http://purl.uniprot.org/uniprot/A0A1B0GR43|||http://purl.uniprot.org/uniprot/Q91W27 ^@ Chain|||Experimental Information|||Molecule Processing|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Tuberoinfundibular peptide of 39 residues ^@ http://purl.uniprot.org/annotation/PRO_0000045944|||http://purl.uniprot.org/annotation/PRO_0000045945|||http://purl.uniprot.org/annotation/PRO_5015060651 http://togogenome.org/gene/10090:Pik3c3 ^@ http://purl.uniprot.org/uniprot/Q6PF93 ^@ 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 ^@ Activation loop|||C2 PI3K-type|||Catalytic loop|||Disordered|||G-loop|||In isoform 2.|||Loss of phosphorylation but no loss of autophagic function; when associated with A-163.|||Loss of phosphorylation but no loss of autophagic function; when associated with A-165.|||PI3K/PI4K catalytic|||PIK helical|||Phosphatidylinositol 3-kinase catalytic subunit type 3|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine; by AMPK|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000088803|||http://purl.uniprot.org/annotation/VSP_016459|||http://purl.uniprot.org/annotation/VSP_016460 http://togogenome.org/gene/10090:Glt8d1 ^@ http://purl.uniprot.org/uniprot/Q6NSU3 ^@ 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|||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_0000288529|||http://purl.uniprot.org/annotation/VSP_025707|||http://purl.uniprot.org/annotation/VSP_025708 http://togogenome.org/gene/10090:Clstn1 ^@ http://purl.uniprot.org/uniprot/Q9EPL2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Almost completely abolishes KLC1-binding.|||CTF1-alpha|||Cadherin 1|||Cadherin 2|||Calsyntenin-1|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Marked reduction in KLC1-binding.|||Marked reduction in KLC1-binding; when associated with A-903. Marked alteration in anterograde axonal transport.|||Marked reduction in KLC1-binding; when associated with A-972. Marked alteration in anterograde axonal transport.|||N-linked (GlcNAc...) asparagine|||Soluble Alc-alpha ^@ http://purl.uniprot.org/annotation/PRO_0000004022|||http://purl.uniprot.org/annotation/PRO_0000323599|||http://purl.uniprot.org/annotation/PRO_0000323600|||http://purl.uniprot.org/annotation/VSP_032036 http://togogenome.org/gene/10090:Nav2 ^@ http://purl.uniprot.org/uniprot/Q6ZPE7|||http://purl.uniprot.org/uniprot/Q8BJG0|||http://purl.uniprot.org/uniprot/Q8BYE8|||http://purl.uniprot.org/uniprot/Q8BYJ2|||http://purl.uniprot.org/uniprot/V9GX91|||http://purl.uniprot.org/uniprot/V9GXT3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Uchl4 ^@ http://purl.uniprot.org/uniprot/B2RTM4|||http://purl.uniprot.org/uniprot/P58321 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Site ^@ Important for enzyme activity|||Interaction with ubiquitin|||Nucleophile|||Phosphoserine|||Proton donor|||Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site|||Ubiquitin carboxyl-terminal hydrolase isozyme L4 ^@ http://purl.uniprot.org/annotation/PRO_0000211064 http://togogenome.org/gene/10090:Srp19 ^@ http://purl.uniprot.org/uniprot/G5E8T3|||http://purl.uniprot.org/uniprot/Q9D104 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Ercc4 ^@ http://purl.uniprot.org/uniprot/Q3UEU6|||http://purl.uniprot.org/uniprot/Q9QZD4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||DNA repair endonuclease XPF|||Disordered|||ERCC4|||Helicase-like|||HhH2, dimerization with ERCC1|||Leucine-zipper 1|||Leucine-zipper 2|||N6-acetyllysine|||Nuclear localization signal|||Nuclease|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000198854 http://togogenome.org/gene/10090:Sec16b ^@ http://purl.uniprot.org/uniprot/Q91XT4 ^@ 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|||Central conserved domain (CCD); required for localization to endoplasmic reticulum exit sites|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein transport protein Sec16B ^@ http://purl.uniprot.org/annotation/PRO_0000341975 http://togogenome.org/gene/10090:Or56b2j ^@ http://purl.uniprot.org/uniprot/Q7TRP6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gpr82 ^@ http://purl.uniprot.org/uniprot/Q8BZR0 ^@ 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_0000303082 http://togogenome.org/gene/10090:Cpn2 ^@ http://purl.uniprot.org/uniprot/Q9DBB9 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||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_0000020990 http://togogenome.org/gene/10090:Sptlc1 ^@ http://purl.uniprot.org/uniprot/O35704 ^@ 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|||Interaction with SPTLC2|||Lumenal|||Phosphotyrosine; by ABL|||Serine palmitoyltransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000163855 http://togogenome.org/gene/10090:Galnt2 ^@ http://purl.uniprot.org/uniprot/Q6PB93 ^@ Binding 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 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||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|||Phosphoserine|||Polypeptide N-acetylgalactosaminyltransferase 2|||Polypeptide N-acetylgalactosaminyltransferase 2 soluble form|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000012267|||http://purl.uniprot.org/annotation/PRO_0000223392|||http://purl.uniprot.org/annotation/VSP_011201 http://togogenome.org/gene/10090:Ucn2 ^@ http://purl.uniprot.org/uniprot/Q99ML8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Modified Residue|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||Urocortin-2|||Valine amide; partial ^@ http://purl.uniprot.org/annotation/PRO_0000006241|||http://purl.uniprot.org/annotation/PRO_0000006242 http://togogenome.org/gene/10090:Wnt5a ^@ http://purl.uniprot.org/uniprot/P22725 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Abolishes glycosylation; when associated with Q-114, Q-120 and Q-312.|||Abolishes glycosylation; when associated with Q-114, Q-120 and Q-326.|||Abolishes glycosylation; when associated with Q-114, Q-312 and Q-326.|||Abolishes glycosylation; when associated with Q-120, Q-312 and Q-326.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on secretion.|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-5a ^@ http://purl.uniprot.org/annotation/PRO_0000041428|||http://purl.uniprot.org/annotation/PRO_0000352797|||http://purl.uniprot.org/annotation/VSP_035595 http://togogenome.org/gene/10090:Dgke ^@ http://purl.uniprot.org/uniprot/Q9R1C6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Transmembrane|||Zinc Finger ^@ DAGKc|||Diacylglycerol kinase epsilon|||Helical|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000218465 http://togogenome.org/gene/10090:Fbn1 ^@ http://purl.uniprot.org/uniprot/Q61554 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Asprosin|||C-terminal domain|||Cell attachment site|||Cleavage; by furin|||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|||Interaction with MFAP4|||N-linked (GlcNAc...) asparagine|||N-terminal domain|||O-linked (Glc) serine|||Phosphoserine|||TB 1|||TB 2|||TB 3|||TB 4|||TB 5|||TB 6|||TB 7|||TB 8|||TB 9 ^@ http://purl.uniprot.org/annotation/PRO_0000007582|||http://purl.uniprot.org/annotation/PRO_0000436883|||http://purl.uniprot.org/annotation/PRO_0000436884 http://togogenome.org/gene/10090:Khdc3 ^@ http://purl.uniprot.org/uniprot/Q9CWU5 ^@ 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 DNA double-strand break repair and subsequent regulation of apoptosis. Abolishes localization to the mitochondrion. No effect on localization to centrosomes or centrosome integrity.|||Abolishes localization to the nucleus and enhances localization to the mitochondrion. Reduces stalled replication fork restart. Abolishes ATR-mediated phosphorylation of S-151. No effect on phosphorylation and activation of ATR. No effect on localization to centrosomes or centrosome integrity.|||Disordered|||In isoform 2.|||In isoform 3.|||Involved in RNA binding|||KH domain-containing protein 3|||KH; atypical|||No effect on localization at replication forks, nascent DNA degradation following DNA damage, restart of stalled replication forks or levels of DNA damage.|||Not required for interaction with OOEP|||Phosphoserine|||Phosphoserine; by ATR|||Phosphothreonine|||Reduces restart of stalled replication forks and cells show an increase in DNA double strand breaks. Decreases phosphorylation of ATR at 'S-428'. Reduces TRIM25 ubiquitination of BLM and subsequent localization to DNA replication forks. Reduces phosphorylation and activation of ATR. No effect on Filia distribution at replication forks or nascent DNA degradation following DNA damage. Not effect on interaction with OOEP.|||Required for interaction with NUMA1 and regulation of apoptosis in response to DNA damage ^@ http://purl.uniprot.org/annotation/PRO_0000407378|||http://purl.uniprot.org/annotation/VSP_040950|||http://purl.uniprot.org/annotation/VSP_040951|||http://purl.uniprot.org/annotation/VSP_040952 http://togogenome.org/gene/10090:Arhgef26 ^@ http://purl.uniprot.org/uniprot/D3YYY8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ DH|||Disordered|||PH|||Polar residues|||SH3 ^@ http://togogenome.org/gene/10090:Lsm11 ^@ http://purl.uniprot.org/uniprot/Q5SUH5|||http://purl.uniprot.org/uniprot/Q8BUV6 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Does not inhibit interaction with ZNF473 and histone 3'-end processing.|||Does not inhibit interaction with ZNF473. Reduces weakly histone 3' end processing.|||Does not inhibit interaction with ZNF473. Strongly reduces histone 3' end processing.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||SM 1|||SM 2|||Sm|||U7 snRNA-associated Sm-like protein LSm11 ^@ http://purl.uniprot.org/annotation/PRO_0000125588 http://togogenome.org/gene/10090:Exd1 ^@ http://purl.uniprot.org/uniprot/Q8CDF7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ 3'-5' exonuclease|||Basic and acidic residues|||Disordered|||piRNA biogenesis protein EXD1 ^@ http://purl.uniprot.org/annotation/PRO_0000337245 http://togogenome.org/gene/10090:Pmm2 ^@ http://purl.uniprot.org/uniprot/Q545N8|||http://purl.uniprot.org/uniprot/Q9Z2M7 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ N6-acetyllysine|||Nucleophile|||Phosphomannomutase 2|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000199696 http://togogenome.org/gene/10090:Mapk9 ^@ http://purl.uniprot.org/uniprot/Q5NCK8|||http://purl.uniprot.org/uniprot/Q8C094|||http://purl.uniprot.org/uniprot/Q9WTU6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||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_0000186274|||http://purl.uniprot.org/annotation/VSP_004836|||http://purl.uniprot.org/annotation/VSP_004837 http://togogenome.org/gene/10090:Or52w1 ^@ http://purl.uniprot.org/uniprot/Q8VF03 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Brms1l ^@ http://purl.uniprot.org/uniprot/Q3U1T3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||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_0000305310|||http://purl.uniprot.org/annotation/VSP_028347|||http://purl.uniprot.org/annotation/VSP_028348 http://togogenome.org/gene/10090:Tmed8 ^@ http://purl.uniprot.org/uniprot/Q3UHI4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Acidic residues|||Disordered|||GOLD|||N6-acetyllysine|||Polar residues|||Protein TMED8 ^@ http://purl.uniprot.org/annotation/PRO_0000322983 http://togogenome.org/gene/10090:Thap4 ^@ http://purl.uniprot.org/uniprot/A0A0J9YU08|||http://purl.uniprot.org/uniprot/Q6P3Z3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||HCFC1-binding motif (HBM)|||In isoform 2.|||Nitrobindin|||Peroxynitrite isomerase THAP4|||Phosphoserine|||Polar residues|||THAP-type|||THAP4-like heme-binding beta-barrel|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000247858|||http://purl.uniprot.org/annotation/VSP_020080|||http://purl.uniprot.org/annotation/VSP_020081 http://togogenome.org/gene/10090:Mas1 ^@ http://purl.uniprot.org/uniprot/P30554|||http://purl.uniprot.org/uniprot/Q0VB49 ^@ 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|||Proto-oncogene Mas ^@ http://purl.uniprot.org/annotation/PRO_0000069715 http://togogenome.org/gene/10090:Pfn2 ^@ http://purl.uniprot.org/uniprot/Q9JJV2 ^@ 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.|||In isoform 3.|||N-acetylalanine|||Profilin-2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000199576|||http://purl.uniprot.org/annotation/VSP_005218|||http://purl.uniprot.org/annotation/VSP_024736 http://togogenome.org/gene/10090:2200002D01Rik ^@ http://purl.uniprot.org/uniprot/Q9D809 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Krtap16-1 ^@ http://purl.uniprot.org/uniprot/A2A5X5 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ 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|||Disordered|||Keratin-associated protein 16-1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000348960 http://togogenome.org/gene/10090:Gbp3 ^@ http://purl.uniprot.org/uniprot/Q61107 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict ^@ GB1/RHD3-type G|||GTPase domain (Globular)|||Guanylate-binding protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000261160 http://togogenome.org/gene/10090:Rabgap1l ^@ http://purl.uniprot.org/uniprot/A6H6A9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Arginine finger|||Disordered|||Glutamine finger|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss GTPase-activating (GAP) activity.|||Loss of interaction with ANK2. Loss of colocalization and cotransportation on motile vesicles with ANK2.|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rab GTPase-activating protein 1-like|||Rab-GAP TBC ^@ http://purl.uniprot.org/annotation/PRO_0000348055|||http://purl.uniprot.org/annotation/VSP_052925|||http://purl.uniprot.org/annotation/VSP_052926|||http://purl.uniprot.org/annotation/VSP_052927|||http://purl.uniprot.org/annotation/VSP_052928|||http://purl.uniprot.org/annotation/VSP_052929|||http://purl.uniprot.org/annotation/VSP_052930|||http://purl.uniprot.org/annotation/VSP_052931|||http://purl.uniprot.org/annotation/VSP_052932 http://togogenome.org/gene/10090:Selenow ^@ http://purl.uniprot.org/uniprot/P63300 ^@ Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non standard residue|||Secondary Structure|||Strand|||Turn ^@ Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Non standard residue|||Strand|||Turn ^@ Cysteinyl-selenocysteine (Cys-Sec); redox-active|||Disrupts redox reaction.|||Impairs protection against hydrogen peroxide-induced toxicity.|||Increased sensitivity to hydrogen peroxide-induced toxicity.|||S-glutathionyl cysteine|||Selenocysteine|||Selenoprotein W ^@ http://purl.uniprot.org/annotation/PRO_0000097680 http://togogenome.org/gene/10090:Hdac6 ^@ http://purl.uniprot.org/uniprot/Q3UG37|||http://purl.uniprot.org/uniprot/Q9Z2V5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ 1|||2|||Basic and acidic residues|||Disordered|||Histone deacetylase|||Histone deacetylase 1|||Histone deacetylase 2|||Histone deacetylase 6|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||UBP-type|||Ubiquitin binding ^@ http://purl.uniprot.org/annotation/PRO_0000114704 http://togogenome.org/gene/10090:Tbc1d19 ^@ http://purl.uniprot.org/uniprot/Q8VDV7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Rab-GAP TBC ^@ http://togogenome.org/gene/10090:Slit1 ^@ http://purl.uniprot.org/uniprot/Q80TR4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide ^@ 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|||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 23|||LRRNT 3|||LRRNT 4|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Slit homolog 1 protein ^@ http://purl.uniprot.org/annotation/PRO_0000007723 http://togogenome.org/gene/10090:Tas2r136 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0W1|||http://purl.uniprot.org/uniprot/Q7TQA8 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ 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|||Taste receptor type 2 member 136 ^@ http://purl.uniprot.org/annotation/PRO_0000082271 http://togogenome.org/gene/10090:Shroom1 ^@ http://purl.uniprot.org/uniprot/Q5SX79 ^@ 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 ^@ ASD1|||ASD2|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein Shroom1 ^@ http://purl.uniprot.org/annotation/PRO_0000286062|||http://purl.uniprot.org/annotation/VSP_024963 http://togogenome.org/gene/10090:Snrnp40 ^@ http://purl.uniprot.org/uniprot/Q6PE01 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Modified Residue|||Repeat|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||U5 small nuclear ribonucleoprotein 40 kDa protein|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051418 http://togogenome.org/gene/10090:Parp11 ^@ http://purl.uniprot.org/uniprot/Q8BML7|||http://purl.uniprot.org/uniprot/Q8CFF0 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Splice Variant ^@ ADP-ribosyl aspartic acid|||ADP-ribosylcysteine|||In isoform 2.|||In isoform 3.|||N6-(ADP-ribosyl)lysine|||PARP catalytic|||Protein mono-ADP-ribosyltransferase PARP11|||WWE ^@ http://purl.uniprot.org/annotation/PRO_0000273420|||http://purl.uniprot.org/annotation/VSP_022557|||http://purl.uniprot.org/annotation/VSP_022558 http://togogenome.org/gene/10090:Dynap ^@ http://purl.uniprot.org/uniprot/Q9D7M5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ CLLAC-motif containing|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Klk14 ^@ http://purl.uniprot.org/uniprot/A0A0B6VSR0|||http://purl.uniprot.org/uniprot/Q8CGR5 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Kallikrein-14|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000378340|||http://purl.uniprot.org/annotation/PRO_0000378341|||http://purl.uniprot.org/annotation/PRO_5014221784 http://togogenome.org/gene/10090:Obox2 ^@ http://purl.uniprot.org/uniprot/E9PXV9 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ilf2 ^@ http://purl.uniprot.org/uniprot/Q9CXY6 ^@ 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 ^@ Acidic residues|||Asymmetric dimethylarginine; alternate|||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_0000126064 http://togogenome.org/gene/10090:Gm5938 ^@ http://purl.uniprot.org/uniprot/A2AEN9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5002642654 http://togogenome.org/gene/10090:Ddn ^@ http://purl.uniprot.org/uniprot/Q80TS7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ 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_0000079862 http://togogenome.org/gene/10090:Or2ab1 ^@ http://purl.uniprot.org/uniprot/Q5NCC7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp319 ^@ http://purl.uniprot.org/uniprot/Q9ERR8 ^@ 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|||Polar residues|||Zinc finger protein 319 ^@ http://purl.uniprot.org/annotation/PRO_0000047528 http://togogenome.org/gene/10090:Defb7 ^@ http://purl.uniprot.org/uniprot/Q91V70 ^@ Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Secondary Structure|||Signal Peptide|||Strand ^@ Disulfide Bond|||Helix|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide|||Strand ^@ Beta-defensin 7|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000006933|||http://purl.uniprot.org/annotation/PRO_0000006934 http://togogenome.org/gene/10090:Krt88 ^@ http://purl.uniprot.org/uniprot/Q9CPR6 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ IF rod ^@ http://togogenome.org/gene/10090:Xpnpep2 ^@ http://purl.uniprot.org/uniprot/B1AVD1|||http://purl.uniprot.org/uniprot/B1AVD2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Creatinase N-terminal|||GPI-anchor amidated alanine|||N-linked (GlcNAc...) asparagine|||Peptidase M24|||Peptidase M24 C-terminal|||Removed in mature form|||Xaa-Pro aminopeptidase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000438729|||http://purl.uniprot.org/annotation/PRO_5002760482|||http://purl.uniprot.org/annotation/PRO_5008409937 http://togogenome.org/gene/10090:Aldh9a1 ^@ http://purl.uniprot.org/uniprot/Q3TMT4|||http://purl.uniprot.org/uniprot/Q3V1N7|||http://purl.uniprot.org/uniprot/Q9JLJ2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Signal Peptide|||Splice Variant ^@ 4-trimethylaminobutyraldehyde dehydrogenase|||Aldehyde dehydrogenase|||Aldehyde dehydrogenase domain-containing protein|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056486|||http://purl.uniprot.org/annotation/PRO_5004230472|||http://purl.uniprot.org/annotation/VSP_061582 http://togogenome.org/gene/10090:Smad7 ^@ http://purl.uniprot.org/uniprot/B2RPW6|||http://purl.uniprot.org/uniprot/O35253 ^@ Binding Site|||Chain|||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 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Important for interaction with SMURF2|||In isoform B.|||MH1|||MH2|||Mothers against decapentaplegic homolog 7|||N6-acetyllysine; alternate|||No effect on stability, nuclear localization or inhibitory function in TGFB signaling. Abolishes transcriptional activity.|||No effect.|||PY-motif|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000090873|||http://purl.uniprot.org/annotation/VSP_006181 http://togogenome.org/gene/10090:Dock4 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VLY2|||http://purl.uniprot.org/uniprot/P59764 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 4|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH3|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000189991|||http://purl.uniprot.org/annotation/VSP_060556|||http://purl.uniprot.org/annotation/VSP_060557 http://togogenome.org/gene/10090:Pkig ^@ http://purl.uniprot.org/uniprot/O70139|||http://purl.uniprot.org/uniprot/Q3TP50 ^@ 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_0000154543 http://togogenome.org/gene/10090:Or7g29 ^@ http://purl.uniprot.org/uniprot/Q8VFF4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vdac1 ^@ http://purl.uniprot.org/uniprot/Q60932 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Beta stranded|||Decreased localization of SQSTM1/p62 to damaged mitochondria; when associated with R-25; R-33 and 122-R-R-123.|||Decreased localization of SQSTM1/p62 to damaged mitochondria; when associated with R-25; R-33 and R-66.|||Decreased localization of SQSTM1/p62 to damaged mitochondria; when associated with R-25; R-66 and 122-R-R-123.|||Decreased localization of SQSTM1/p62 to damaged mitochondria; when associated with R-33; R-66 and 122-R-R-123.|||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 Mt-VDAC1.|||Involved in ceramide and phosphatidylcholine binding. Critical for channel structural stability and gating|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||No effect on localization of SQSTM1/p62 to damaged mitochondria.|||Phosphoserine|||Phosphoserine; by NEK1|||Phosphothreonine|||Phosphotyrosine|||Removed|||Voltage-dependent anion-selective channel protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000050500|||http://purl.uniprot.org/annotation/VSP_005075 http://togogenome.org/gene/10090:Gnb3 ^@ http://purl.uniprot.org/uniprot/Q54AE3|||http://purl.uniprot.org/uniprot/Q61011 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Repeat ^@ Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000127700 http://togogenome.org/gene/10090:Abce1 ^@ http://purl.uniprot.org/uniprot/P61222|||http://purl.uniprot.org/uniprot/Q3TJM9|||http://purl.uniprot.org/uniprot/Q3UHY8 ^@ 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 ^@ 4Fe-4S ferredoxin-type|||4Fe-4S ferredoxin-type 1|||4Fe-4S ferredoxin-type 2|||ABC transporter|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family E member 1|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000093317 http://togogenome.org/gene/10090:Tepp ^@ http://purl.uniprot.org/uniprot/Q6IMH0 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Sperm microtubule inner protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000325778|||http://purl.uniprot.org/annotation/VSP_032404 http://togogenome.org/gene/10090:Ebi3 ^@ http://purl.uniprot.org/uniprot/O35228|||http://purl.uniprot.org/uniprot/Q3U1K3 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III domain-containing protein|||Interleukin-27 subunit beta|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000010938|||http://purl.uniprot.org/annotation/PRO_5014309178 http://togogenome.org/gene/10090:Maf1 ^@ http://purl.uniprot.org/uniprot/Q9D0U6 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1 and SUMO2)|||Phosphoserine|||Phosphoserine; by MTOR|||Phosphothreonine|||Polar residues|||Repressor of RNA polymerase III transcription MAF1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000213974 http://togogenome.org/gene/10090:Arl5b ^@ http://purl.uniprot.org/uniprot/Q9D4P0 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding ^@ ADP-ribosylation factor-like protein 5B|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207471 http://togogenome.org/gene/10090:Gpr50 ^@ http://purl.uniprot.org/uniprot/O88495 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||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|||Melatonin-related receptor ^@ http://purl.uniprot.org/annotation/PRO_0000069879 http://togogenome.org/gene/10090:Tigd3 ^@ http://purl.uniprot.org/uniprot/Q7TM95 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Region ^@ DDE-1|||Disordered|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||Tigger transposable element-derived protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000271091 http://togogenome.org/gene/10090:Rfx5 ^@ http://purl.uniprot.org/uniprot/Q9JL61 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||DNA-binding protein Rfx5|||Disordered|||Leucine-rich region; critical for dimer formation and for interaction with RFXAP|||N-acetylalanine|||N-terminal domain|||Phosphoserine|||Pro residues|||PxLPxI/L motif; mediates interaction with RFXANK|||RFX-type winged-helix|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000419167 http://togogenome.org/gene/10090:Myh11 ^@ http://purl.uniprot.org/uniprot/A0A2R8VHF9|||http://purl.uniprot.org/uniprot/E9QPE7 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Actin-binding|||Basic and acidic residues|||Disordered|||Myosin N-terminal SH3-like|||Myosin motor|||Polar residues ^@ http://togogenome.org/gene/10090:Gm9758 ^@ http://purl.uniprot.org/uniprot/Q80ZT2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Mphosph10 ^@ http://purl.uniprot.org/uniprot/Q810V0|||http://purl.uniprot.org/uniprot/Q9CYN7|||http://purl.uniprot.org/uniprot/Q9D7V6 ^@ 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 ^@ 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_0000121536 http://togogenome.org/gene/10090:Tysnd1 ^@ http://purl.uniprot.org/uniprot/Q9DBA6 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Region|||Site ^@ Charge relay system|||Cleavage|||Peroxisomal leader peptide-processing protease|||Peroxisomal leader peptide-processing protease, 10 kDa form|||Peroxisomal leader peptide-processing protease, 49 kDa form|||Serine protease ^@ http://purl.uniprot.org/annotation/PRO_0000286127|||http://purl.uniprot.org/annotation/PRO_0000286128|||http://purl.uniprot.org/annotation/PRO_0000286129 http://togogenome.org/gene/10090:Ceacam2 ^@ http://purl.uniprot.org/uniprot/Q925P2 ^@ 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 ^@ Carcinoembryonic antigen-related cell adhesion molecule 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||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 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000287095|||http://purl.uniprot.org/annotation/VSP_025300|||http://purl.uniprot.org/annotation/VSP_025301 http://togogenome.org/gene/10090:Akr1b8 ^@ http://purl.uniprot.org/uniprot/P45377 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Site|||Strand|||Turn ^@ Aldose reductase-related protein 2|||Lowers pKa of active site Tyr|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000124631 http://togogenome.org/gene/10090:Serpinb9c ^@ http://purl.uniprot.org/uniprot/I7HJI5|||http://purl.uniprot.org/uniprot/Q80WW4|||http://purl.uniprot.org/uniprot/Q9D6A7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Iqca ^@ http://purl.uniprot.org/uniprot/E9QMY8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ AAA+ ATPase|||Basic residues|||Disordered ^@ http://togogenome.org/gene/10090:Fam90a1a ^@ http://purl.uniprot.org/uniprot/A2A4E2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Zinc knuckle ^@ http://togogenome.org/gene/10090:Sfta2 ^@ http://purl.uniprot.org/uniprot/E9PXB6 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Surfactant-associated protein 2 ^@ http://purl.uniprot.org/annotation/PRO_5003245479 http://togogenome.org/gene/10090:Ptpmt1 ^@ http://purl.uniprot.org/uniprot/Q3U926|||http://purl.uniprot.org/uniprot/Q66GT5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Transit Peptide|||Turn ^@ Disordered|||Does not affect mitochondrion localization.|||Fails to dephosphorylate PGP in vitro.|||Fails to dephosphorylate PGP in vitro. Does not affect level of Akt phosphorylation.|||Loss of mitochondrion localization.|||Mitochondrion|||N6-succinyllysine|||Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1|||Phosphocysteine intermediate|||Polar residues|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000025424 http://togogenome.org/gene/10090:P2rx4 ^@ http://purl.uniprot.org/uniprot/D3YYR5|||http://purl.uniprot.org/uniprot/D3Z5U5|||http://purl.uniprot.org/uniprot/Q9Z256|||http://purl.uniprot.org/uniprot/Q9Z257 ^@ Binding Site|||Disulfide Bond|||Glycosylation Site|||Modification|||Region|||Site|||Transmembrane ^@ Binding Site|||Disulfide Bond|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine ^@ http://togogenome.org/gene/10090:Plin5 ^@ http://purl.uniprot.org/uniprot/Q8BVZ1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||Essential for lipid droplet targeting|||In isoform 2.|||Interaction with LIPE|||Interaction with PNPLA2 and ABHD5|||Necessary for mitochondria recruitment at the lipid droplet surface|||Perilipin-5|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000338983|||http://purl.uniprot.org/annotation/VSP_034085 http://togogenome.org/gene/10090:Pla2g3 ^@ http://purl.uniprot.org/uniprot/Q6AXH0|||http://purl.uniprot.org/uniprot/Q8BZT7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Group 3 secretory phospholipase A2|||N-linked (GlcNAc...) asparagine|||Phospholipase A2|||Phospholipase A2-like|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5004270657|||http://purl.uniprot.org/annotation/PRO_5015099043 http://togogenome.org/gene/10090:Mcfd2 ^@ http://purl.uniprot.org/uniprot/D0EW11|||http://purl.uniprot.org/uniprot/Q8K5B2 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Signal Peptide ^@ EF-hand|||EF-hand 1|||EF-hand 2|||Multiple coagulation factor deficiency protein 2 homolog|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000004160|||http://purl.uniprot.org/annotation/PRO_5010111017 http://togogenome.org/gene/10090:Il22b ^@ http://purl.uniprot.org/uniprot/Q9JJY8 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Interleukin-22b|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015385 http://togogenome.org/gene/10090:Zfp408 ^@ http://purl.uniprot.org/uniprot/H7BX78|||http://purl.uniprot.org/uniprot/Q3V1D8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Defa24 ^@ http://purl.uniprot.org/uniprot/Q5G865 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Alpha-defensin 24|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000300074|||http://purl.uniprot.org/annotation/PRO_0000300075 http://togogenome.org/gene/10090:Or52b4 ^@ http://purl.uniprot.org/uniprot/E9PXN3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdca8 ^@ http://purl.uniprot.org/uniprot/Q8BHX3 ^@ 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|||Borealin|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by TTK|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000247076|||http://purl.uniprot.org/annotation/VSP_019922|||http://purl.uniprot.org/annotation/VSP_019923|||http://purl.uniprot.org/annotation/VSP_019924 http://togogenome.org/gene/10090:Speer4e ^@ http://purl.uniprot.org/uniprot/K7N6S8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Apol8 ^@ http://purl.uniprot.org/uniprot/A2VDH7 ^@ Coiled-Coil|||Region|||Transmembrane ^@ Coiled-Coil|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Ppfibp1 ^@ http://purl.uniprot.org/uniprot/Q8C8U0 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Liprin-beta-1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM 1|||SAM 2|||SAM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000191035|||http://purl.uniprot.org/annotation/VSP_012095|||http://purl.uniprot.org/annotation/VSP_012096 http://togogenome.org/gene/10090:Prdx3 ^@ http://purl.uniprot.org/uniprot/P20108 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Cysteine sulfenic acid (-SOH) intermediate|||Interchain (with C-109); in linked form|||Interchain (with C-230); 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_0000023783 http://togogenome.org/gene/10090:Larp1 ^@ http://purl.uniprot.org/uniprot/Q6ZQ58 ^@ 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 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|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Removed|||Required for interaction with PABPC1|||Required for interaction with RPTOR and for repression of mRNAs with a 5'TOP motif ^@ http://purl.uniprot.org/annotation/PRO_0000207610|||http://purl.uniprot.org/annotation/VSP_015116 http://togogenome.org/gene/10090:Vwa3a ^@ http://purl.uniprot.org/uniprot/Q3UVV9 ^@ 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|||VWFA 1|||VWFA 2|||von Willebrand factor A domain-containing protein 3A ^@ http://purl.uniprot.org/annotation/PRO_0000324625 http://togogenome.org/gene/10090:Or5p72 ^@ http://purl.uniprot.org/uniprot/Q8VG08 ^@ 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 5P72 ^@ http://purl.uniprot.org/annotation/PRO_0000150851 http://togogenome.org/gene/10090:Tspo2 ^@ http://purl.uniprot.org/uniprot/Q9CRZ8 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Translocator protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000292006 http://togogenome.org/gene/10090:Erg ^@ http://purl.uniprot.org/uniprot/A0A384DVA0|||http://purl.uniprot.org/uniprot/B7ZND4|||http://purl.uniprot.org/uniprot/E9PY05|||http://purl.uniprot.org/uniprot/P81270|||http://purl.uniprot.org/uniprot/Q3UQJ4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||ETS|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||In isoform 2.|||In isoform 5.|||PNT|||Phosphoserine|||Polar residues|||Transcriptional regulator ERG ^@ http://purl.uniprot.org/annotation/PRO_0000204104|||http://purl.uniprot.org/annotation/VSP_007641|||http://purl.uniprot.org/annotation/VSP_007642|||http://purl.uniprot.org/annotation/VSP_026585 http://togogenome.org/gene/10090:Gabarapl2 ^@ http://purl.uniprot.org/uniprot/P60521 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict|||Site ^@ Chain|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Site ^@ Cleavage; by ATG4B|||Gamma-aminobutyric acid receptor-associated protein-like 2|||N6-acetyllysine|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Phosphoserine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000212374|||http://purl.uniprot.org/annotation/PRO_0000423071 http://togogenome.org/gene/10090:Mef2d ^@ http://purl.uniprot.org/uniprot/E9QKT0|||http://purl.uniprot.org/uniprot/Q63943|||http://purl.uniprot.org/uniprot/Q921S6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Abolishes phosphorylation by PKA. No change in protein levels. Loss of protein stability on PKA stimulation mediated repression. No change in interaction with HDAC4 in response to PKA; when associated with A-121.|||Abolishes phosphorylation by PKA. No change in protein levels. Loss of protein stability on PKA stimulation. Loss of PKA-mediated repression. No change in interaction with HDAC4 in response to PKA; when associated with A-190.|||Beta domain|||Cleavage|||Disordered|||Dramatic decrease in DNA-binding.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||In isoform Muscle.|||Loss of calpain/Cdk5-mediated neuron apoptosis.|||MADS-box|||Mef2-type|||Myocyte-specific enhancer factor 2D|||N6-acetyllysine|||N6-acetyllysine; alternate|||No change in DNA-binding activity.|||Phosphoserine|||Phosphoserine; by MAPK7|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000199436|||http://purl.uniprot.org/annotation/VSP_006253|||http://purl.uniprot.org/annotation/VSP_006254 http://togogenome.org/gene/10090:Caap1 ^@ http://purl.uniprot.org/uniprot/Q3TUU0|||http://purl.uniprot.org/uniprot/Q8VDY9 ^@ Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Crosslink|||Modified Residue|||Region|||Sequence Conflict ^@ Caspase activity and apoptosis inhibitor 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000089718 http://togogenome.org/gene/10090:Nabp2 ^@ http://purl.uniprot.org/uniprot/Q8R2Y9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region ^@ Disordered|||OB|||Phosphothreonine; by ATM|||Polar residues|||SOSS complex subunit B1 ^@ http://purl.uniprot.org/annotation/PRO_0000333960 http://togogenome.org/gene/10090:Vmn1r114 ^@ http://purl.uniprot.org/uniprot/L7N226 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc25a21 ^@ http://purl.uniprot.org/uniprot/B6CI26|||http://purl.uniprot.org/uniprot/Q3TRZ4|||http://purl.uniprot.org/uniprot/Q8BZ09 ^@ 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|||Mitochondrial 2-oxodicarboxylate carrier|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090645 http://togogenome.org/gene/10090:P2ry2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J289|||http://purl.uniprot.org/uniprot/P35383 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Decrease in receptor activation.|||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|||No effect on receptor activation.|||P2Y purinoceptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000070015 http://togogenome.org/gene/10090:Cadps ^@ http://purl.uniprot.org/uniprot/Q80TJ1 ^@ 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 ^@ Acidic residues|||C2|||Calcium-dependent secretion activator 1|||Disordered|||In isoform 2.|||In isoform 4.|||Interaction with DRD2|||MHD1|||Mediates targeting and association with DCVs|||PH|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053865|||http://purl.uniprot.org/annotation/VSP_016809|||http://purl.uniprot.org/annotation/VSP_016811|||http://purl.uniprot.org/annotation/VSP_016813|||http://purl.uniprot.org/annotation/VSP_016814 http://togogenome.org/gene/10090:Lefty1 ^@ http://purl.uniprot.org/uniprot/Q64280 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Signal Peptide ^@ Left-right determination factor 1|||N-linked (GlcNAc...) asparagine|||Or 135 ^@ http://purl.uniprot.org/annotation/PRO_0000033808|||http://purl.uniprot.org/annotation/PRO_0000033809 http://togogenome.org/gene/10090:Or7a39 ^@ http://purl.uniprot.org/uniprot/Q7TQU9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r122 ^@ http://purl.uniprot.org/uniprot/O35190 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5004158203 http://togogenome.org/gene/10090:Neto2 ^@ http://purl.uniprot.org/uniprot/Q8BNJ6 ^@ 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|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ CUB 1|||CUB 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||LDL-receptor class A|||N-linked (GlcNAc...) asparagine|||Neuropilin and tolloid-like protein 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000021802|||http://purl.uniprot.org/annotation/VSP_012858|||http://purl.uniprot.org/annotation/VSP_012859 http://togogenome.org/gene/10090:Mfap3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1C7|||http://purl.uniprot.org/uniprot/Q922T2 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Microfibril-associated glycoprotein 3|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014866|||http://purl.uniprot.org/annotation/PRO_5015044317 http://togogenome.org/gene/10090:Asrgl1 ^@ http://purl.uniprot.org/uniprot/Q8C0M9 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Isoaspartyl peptidase/L-asparaginase alpha chain|||Isoaspartyl peptidase/L-asparaginase beta chain|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000420559|||http://purl.uniprot.org/annotation/PRO_0000420560 http://togogenome.org/gene/10090:Zfp433 ^@ http://purl.uniprot.org/uniprot/A0A0J9YUD4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Aqp4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Z3|||http://purl.uniprot.org/uniprot/P55088|||http://purl.uniprot.org/uniprot/Q50H70|||http://purl.uniprot.org/uniprot/Q8BR89 ^@ Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Aquaporin-4|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||In isoform 1.|||In isoform 3.|||Loss of phosphorylation by PKG (in vitro). No effect on location at cell membrane.|||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_0000063949|||http://purl.uniprot.org/annotation/VSP_003233|||http://purl.uniprot.org/annotation/VSP_003234 http://togogenome.org/gene/10090:Strn4 ^@ http://purl.uniprot.org/uniprot/P58404 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Calmodulin-binding|||Caveolin-binding|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Striatin-4|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051240|||http://purl.uniprot.org/annotation/VSP_013815 http://togogenome.org/gene/10090:Clcn3 ^@ http://purl.uniprot.org/uniprot/A0A6Q6Q7B9|||http://purl.uniprot.org/uniprot/P51791|||http://purl.uniprot.org/uniprot/Q790S0|||http://purl.uniprot.org/uniprot/Q8K4W8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Motif|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes outwardly-rectifying currents.|||CBS|||CBS 1|||CBS 2|||Cytoplasmic|||Di-leucine internalization motif; mediates targeting to late endosome and lysosome membranes|||H(+)/Cl(-) exchange transporter 3|||Helical|||IP motif; mediates targeting to recycling endosomes|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 5.|||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_0000094439|||http://purl.uniprot.org/annotation/VSP_036899|||http://purl.uniprot.org/annotation/VSP_060627|||http://purl.uniprot.org/annotation/VSP_060628 http://togogenome.org/gene/10090:4930519F16Rik ^@ http://purl.uniprot.org/uniprot/Q8K3S1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5004312137 http://togogenome.org/gene/10090:H2-Q6 ^@ http://purl.uniprot.org/uniprot/P79568 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015096862 http://togogenome.org/gene/10090:Kctd14 ^@ http://purl.uniprot.org/uniprot/A0A0U1RNG7|||http://purl.uniprot.org/uniprot/A0A0U1RPG8|||http://purl.uniprot.org/uniprot/Q5EER8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Sult1b1 ^@ http://purl.uniprot.org/uniprot/Q9QWG7 ^@ 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.|||Proton acceptor|||Sulfotransferase 1B1 ^@ http://purl.uniprot.org/annotation/PRO_0000085162|||http://purl.uniprot.org/annotation/VSP_012509 http://togogenome.org/gene/10090:Prss59 ^@ http://purl.uniprot.org/uniprot/Q9D9G7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015099685 http://togogenome.org/gene/10090:Paip2b ^@ http://purl.uniprot.org/uniprot/A0A158RFV3|||http://purl.uniprot.org/uniprot/Q91W45 ^@ 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|||Polar residues|||Polyadenylate-binding protein-interacting protein 2B ^@ http://purl.uniprot.org/annotation/PRO_0000317295 http://togogenome.org/gene/10090:Ifnz ^@ http://purl.uniprot.org/uniprot/Q8BQT1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099018 http://togogenome.org/gene/10090:Fbll1 ^@ http://purl.uniprot.org/uniprot/Q80WS3 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region ^@ Disordered|||Omega-N-methylarginine|||rRNA/tRNA 2'-O-methyltransferase fibrillarin-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000331763 http://togogenome.org/gene/10090:Cckar ^@ http://purl.uniprot.org/uniprot/O08786|||http://purl.uniprot.org/uniprot/Q3TPL0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cholecystokinin receptor type 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|||N-linked (GlcNAc...) asparagine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069224 http://togogenome.org/gene/10090:Tmem63c ^@ http://purl.uniprot.org/uniprot/Q8CBX0 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ Calcium permeable stress-gated cation channel 1|||Disordered|||Helical|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000280731 http://togogenome.org/gene/10090:Rpl17 ^@ http://purl.uniprot.org/uniprot/Q9CPR4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic residues|||Disordered|||Large ribosomal subunit protein uL22 ^@ http://purl.uniprot.org/annotation/PRO_0000125333 http://togogenome.org/gene/10090:Rab33b ^@ http://purl.uniprot.org/uniprot/O35963 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Strand|||Turn ^@ Affects interaction with ATG16L1.|||Cysteine methyl ester|||Does not affect interaction with ATG16L1. Induces lipidation of LC3.|||Ras-related protein Rab-33B|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121240 http://togogenome.org/gene/10090:Ppp1r3c ^@ http://purl.uniprot.org/uniprot/Q7TMB3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes binding to PP1 but has no effect on binding to glycogen synthase, glycogen phosphorylase or glycogen; when associated with A-85.|||Abolishes binding to PP1 but has no effect on binding to glycogen synthase, glycogen phosphorylase or glycogen; when associated with A-87.|||Abolishes binding to glycogen synthase and glycogen phosphorylase but has no effect on binding to PP1 or glycogen; when associated with A-247.|||Abolishes binding to glycogen synthase and glycogen phosphorylase but has no effect on binding to PP1 or glycogen; when associated with A-250.|||CBM21|||Interaction with EPM2A|||PP1-binding motif|||Protein phosphatase 1 regulatory subunit 3C ^@ http://purl.uniprot.org/annotation/PRO_0000285928 http://togogenome.org/gene/10090:Efna2 ^@ http://purl.uniprot.org/uniprot/P52801|||http://purl.uniprot.org/uniprot/Q3USB4 ^@ 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 ^@ Ephrin RBD|||Ephrin RBD domain-containing protein|||Ephrin-A2|||GPI-anchor amidated asparagine|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000008363|||http://purl.uniprot.org/annotation/PRO_0000008364|||http://purl.uniprot.org/annotation/PRO_5004230283 http://togogenome.org/gene/10090:Filip1l ^@ http://purl.uniprot.org/uniprot/E0CYH7|||http://purl.uniprot.org/uniprot/E0CYM1 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Cortactin-binding protein-2 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gm14147 ^@ http://purl.uniprot.org/uniprot/A2AQX6 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Protein kinase ^@ http://togogenome.org/gene/10090:Cp ^@ http://purl.uniprot.org/uniprot/G3X8Q5|||http://purl.uniprot.org/uniprot/Q61147|||http://purl.uniprot.org/uniprot/Q8BU82 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Ceruloplasmin|||F5/8 type A 1|||F5/8 type A 2|||F5/8 type A 3|||Helical|||N-linked (GlcNAc...) asparagine|||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_0000002913|||http://purl.uniprot.org/annotation/PRO_5015091816 http://togogenome.org/gene/10090:Ntng1 ^@ http://purl.uniprot.org/uniprot/Q8R4G0 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ GPI-anchor amidated serine|||In isoform 1B.|||In isoform 1C.|||In isoform 1D.|||In isoform 1E.|||In isoform 1F.|||In isoform 1G.|||In isoform 1H.|||In isoform 1I.|||In isoform 1J.|||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_0000017093|||http://purl.uniprot.org/annotation/PRO_0000017094|||http://purl.uniprot.org/annotation/VSP_050546|||http://purl.uniprot.org/annotation/VSP_050547|||http://purl.uniprot.org/annotation/VSP_050548|||http://purl.uniprot.org/annotation/VSP_050549|||http://purl.uniprot.org/annotation/VSP_050550|||http://purl.uniprot.org/annotation/VSP_050551|||http://purl.uniprot.org/annotation/VSP_050552|||http://purl.uniprot.org/annotation/VSP_050553|||http://purl.uniprot.org/annotation/VSP_050554|||http://purl.uniprot.org/annotation/VSP_050555|||http://purl.uniprot.org/annotation/VSP_050556|||http://purl.uniprot.org/annotation/VSP_050557|||http://purl.uniprot.org/annotation/VSP_050558|||http://purl.uniprot.org/annotation/VSP_050559|||http://purl.uniprot.org/annotation/VSP_050560|||http://purl.uniprot.org/annotation/VSP_050561 http://togogenome.org/gene/10090:Ppp1r3d ^@ http://purl.uniprot.org/uniprot/A2AJW4 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ CBM21|||Disordered ^@ http://togogenome.org/gene/10090:Rpusd2 ^@ http://purl.uniprot.org/uniprot/Q149F1 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Phosphothreonine|||Polar residues|||Pseudouridylate synthase RPUSD2 ^@ http://purl.uniprot.org/annotation/PRO_0000300820 http://togogenome.org/gene/10090:Srsf3 ^@ http://purl.uniprot.org/uniprot/P84104 ^@ 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 ^@ 2 X approximate repeats, basic|||B-1|||B-2|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform Short.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||RRM|||Serine/arginine-rich splicing factor 3|||Sufficient for interaction with NXF1 ^@ http://purl.uniprot.org/annotation/PRO_0000081924|||http://purl.uniprot.org/annotation/VSP_005861|||http://purl.uniprot.org/annotation/VSP_005862 http://togogenome.org/gene/10090:Vmn2r82 ^@ http://purl.uniprot.org/uniprot/G3UWA2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015091570 http://togogenome.org/gene/10090:Cracdl ^@ http://purl.uniprot.org/uniprot/E9Q3M9|||http://purl.uniprot.org/uniprot/Q6GQT3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF4592|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Or6c203 ^@ http://purl.uniprot.org/uniprot/Q8VGC5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bmpr1a ^@ http://purl.uniprot.org/uniprot/P36895|||http://purl.uniprot.org/uniprot/Q53Z43 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Bone morphogenetic protein receptor type-1A|||Cytoplasmic|||Extracellular|||GS|||Helical|||Mediates specificity for BMP ligand|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Proton acceptor|||Reduced glycosylation and increased protein stability; when associated with Q-314 and Q-373.|||Reduced glycosylation and increased protein stability; when associated with Q-373 and Q-373.|||Reduced glycosylation and increased protein stability; when associated with Q-73 and Q-314.|||receptor protein serine/threonine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000024411|||http://purl.uniprot.org/annotation/PRO_5014309572 http://togogenome.org/gene/10090:Smco3 ^@ http://purl.uniprot.org/uniprot/Q8BQM7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Transmembrane ^@ Helical|||Single-pass membrane and coiled-coil domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000336989 http://togogenome.org/gene/10090:Acad12 ^@ http://purl.uniprot.org/uniprot/D3Z7X0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA dehydrogenase/oxidase N-terminal|||Acyl-CoA oxidase/dehydrogenase middle ^@ http://togogenome.org/gene/10090:Adam32 ^@ http://purl.uniprot.org/uniprot/Q8K410 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 32|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000029140|||http://purl.uniprot.org/annotation/PRO_0000029141|||http://purl.uniprot.org/annotation/VSP_012052 http://togogenome.org/gene/10090:Pdzd7 ^@ http://purl.uniprot.org/uniprot/E9Q9W7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ domain-containing protein 7|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000445738|||http://purl.uniprot.org/annotation/VSP_059952|||http://purl.uniprot.org/annotation/VSP_059953|||http://purl.uniprot.org/annotation/VSP_059954|||http://purl.uniprot.org/annotation/VSP_059955|||http://purl.uniprot.org/annotation/VSP_059956|||http://purl.uniprot.org/annotation/VSP_059957|||http://purl.uniprot.org/annotation/VSP_059958 http://togogenome.org/gene/10090:Neurog1 ^@ http://purl.uniprot.org/uniprot/P70660 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Neurogenin-1|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127397 http://togogenome.org/gene/10090:Gemin7 ^@ http://purl.uniprot.org/uniprot/Q9CWY4 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Gem-associated protein 7|||N-acetylmethionine|||SUZ-C|||Sm ^@ http://purl.uniprot.org/annotation/PRO_0000087463 http://togogenome.org/gene/10090:Or1j14 ^@ http://purl.uniprot.org/uniprot/Q8VGK7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tnnc1 ^@ http://purl.uniprot.org/uniprot/P19123 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||N-acetylmethionine|||Phosphoserine|||Troponin C, slow skeletal and cardiac muscles ^@ http://purl.uniprot.org/annotation/PRO_0000073698 http://togogenome.org/gene/10090:Dnmt3a ^@ http://purl.uniprot.org/uniprot/O88508 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ADD|||Basic and acidic residues|||DNA (cytosine-5)-methyltransferase 3A|||Decreased protein abundance.|||Disordered|||GATA-type; atypical|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||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.|||Loss of activity. Strongly reduces substrate binding.|||No effect on activity.|||No effect on localization.|||Omega-N-methylarginine|||PHD-type; atypical|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues|||Prevents accumulation in pericentric heterochromatin.|||Reduces DNA-binding capacity. No effect on activity.|||Reduces activity about 10-fold.|||Reduces activity about 15-fold.|||Reduces activity about 15-fold. Loss of substrate binding.|||Reduces activity about 2-fold. Reduces DNA-binding capacity.|||Reduces activity about 20-fold. Loss of substrate binding.|||Reduces activity about 3-fold.|||Reduces activity about 3-fold. Reduces DNA-binding capacity.|||Reduces activity about 30-fold. Reduces DNA-binding capacity.|||Reduces activity about 5-fold. Reduces DNA-binding capacity. Abolished cysteine-methylation.|||Reduces activity about 6-fold. Reduces DNA-binding capacity.|||S-methylcysteine; by autocatalysis|||SAM-dependent MTase C5-type|||Strongly reduces substrate binding. No effect on activity.|||The protein is stably expressed. ^@ http://purl.uniprot.org/annotation/PRO_0000088044|||http://purl.uniprot.org/annotation/VSP_009423 http://togogenome.org/gene/10090:Zfp981 ^@ http://purl.uniprot.org/uniprot/A2A8V7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Atg7 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQN4|||http://purl.uniprot.org/uniprot/Q3TM87|||http://purl.uniprot.org/uniprot/Q9D906 ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict ^@ FAP motif|||Glycyl thioester intermediate|||Instead of the formation of an intermediate complex with a thiol ester bond between ATG7 (E1-like enzyme) and GABARAPL1 (MAP1LC3, GABARAP or GABARAPL; substrates), a stable complex with an O-ester bond is formed.|||Phosphoserine|||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_0000212807 http://togogenome.org/gene/10090:Mycbp2 ^@ http://purl.uniprot.org/uniprot/Q7TPH6 ^@ 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|||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|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Abolished guanosine exchange factor (GEF) activity for Ran.|||Basic and acidic residues|||Basic residues|||DOC|||Disordered|||E3 ubiquitin-protein ligase MYCBP2|||Filamin|||Important for catalysis|||In isoform 2.|||PHR domain 1|||PHR domain 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RAE1 binding|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RING-type; atypical|||Tandem cysteine domain ^@ http://purl.uniprot.org/annotation/PRO_0000055964|||http://purl.uniprot.org/annotation/VSP_014184 http://togogenome.org/gene/10090:Zfp131 ^@ http://purl.uniprot.org/uniprot/Q8K3J5 ^@ 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 ^@ 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.|||In isoform 3.|||Nuclear localization signal 1|||Nuclear localization signal 2|||Phosphoserine|||Zinc finger protein 131 ^@ http://purl.uniprot.org/annotation/PRO_0000047414|||http://purl.uniprot.org/annotation/VSP_016924|||http://purl.uniprot.org/annotation/VSP_016925|||http://purl.uniprot.org/annotation/VSP_016926 http://togogenome.org/gene/10090:Gp5 ^@ http://purl.uniprot.org/uniprot/Q9QZU3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Non-terminal Residue|||Signal Peptide|||Transmembrane ^@ Helical|||LRRCT ^@ http://purl.uniprot.org/annotation/PRO_5015099937 http://togogenome.org/gene/10090:St6galnac3 ^@ http://purl.uniprot.org/uniprot/Q9WUV2 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149276 http://togogenome.org/gene/10090:Tafa4 ^@ http://purl.uniprot.org/uniprot/Q7TPG5 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Sequence Conflict|||Signal Peptide ^@ Chemokine-like protein TAFA-4 ^@ http://purl.uniprot.org/annotation/PRO_0000042730 http://togogenome.org/gene/10090:6430548M08Rik ^@ http://purl.uniprot.org/uniprot/Q3TA40|||http://purl.uniprot.org/uniprot/Q8BQB5|||http://purl.uniprot.org/uniprot/Q8R0A7 ^@ 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|||SBF1/SBF2|||Uncharacterized protein KIAA0513 ^@ http://purl.uniprot.org/annotation/PRO_0000050758 http://togogenome.org/gene/10090:Bik ^@ http://purl.uniprot.org/uniprot/O70337 ^@ Chain|||Molecule Processing|||Motif|||Region|||Site|||Transmembrane ^@ Chain|||Motif|||Region|||Site|||Transmembrane ^@ BH3|||Bcl-2-interacting killer|||Cleavage; by RHBDL4/RHBDD1|||Helical|||Leucine-zipper ^@ http://purl.uniprot.org/annotation/PRO_0000419202 http://togogenome.org/gene/10090:Tmem185b ^@ http://purl.uniprot.org/uniprot/Q8R3R5 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 185B ^@ http://purl.uniprot.org/annotation/PRO_0000188010 http://togogenome.org/gene/10090:Tnmd ^@ http://purl.uniprot.org/uniprot/Q9EP64 ^@ 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 ^@ BRICHOS|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Tenomodulin ^@ http://purl.uniprot.org/annotation/PRO_0000144309 http://togogenome.org/gene/10090:Nherf1 ^@ http://purl.uniprot.org/uniprot/P70441|||http://purl.uniprot.org/uniprot/Q3TG37 ^@ 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|||In isoform 2.|||N-acetylserine|||Na(+)/H(+) exchange regulatory cofactor NHE-RF1|||PDZ|||PDZ 1|||PDZ 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000096800|||http://purl.uniprot.org/annotation/VSP_027877|||http://purl.uniprot.org/annotation/VSP_027878 http://togogenome.org/gene/10090:Trim71 ^@ http://purl.uniprot.org/uniprot/Q1PSW8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Zinc Finger ^@ Abolishes E3 ubiquitin-protein ligase activity; when associated with A-15.|||Abolishes E3 ubiquitin-protein ligase activity; when associated with L-12.|||B box-type 1; atypical|||B box-type 2|||Disordered|||E3 ubiquitin-protein ligase TRIM71|||Filamin|||N-acetylalanine|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||NHL 6|||Polar residues|||RING-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000279512 http://togogenome.org/gene/10090:Rln1 ^@ http://purl.uniprot.org/uniprot/A2RTV8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Insulin-like ^@ http://purl.uniprot.org/annotation/PRO_5015086073 http://togogenome.org/gene/10090:Or5b98 ^@ http://purl.uniprot.org/uniprot/Q8VF19 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rnf149 ^@ http://purl.uniprot.org/uniprot/Q3U2C5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNF149|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PA|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000261612|||http://purl.uniprot.org/annotation/VSP_021734 http://togogenome.org/gene/10090:Rps27a ^@ http://purl.uniprot.org/uniprot/P62983|||http://purl.uniprot.org/uniprot/Q642L7 ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Site|||Strand|||Zinc Finger ^@ ADP-ribosylglycine|||C4-type|||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|||N6-acetyllysine|||Phosphoserine; by PINK1|||Small ribosomal subunit protein eS31|||Ubiquitin|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000137663|||http://purl.uniprot.org/annotation/PRO_0000396479 http://togogenome.org/gene/10090:Casp7 ^@ http://purl.uniprot.org/uniprot/P97864|||http://purl.uniprot.org/uniprot/Q4FJQ4 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Abolished cleavage and activation; when associated with A-198.|||Abolished cleavage and activation; when associated with A-23.|||Caspase family p10|||Caspase family p20|||Caspase-7 subunit p11|||Caspase-7 subunit p20|||Cleavage; by CAPN1|||Disordered|||Exosite|||Involved in allosteric regulation|||Loop L1|||Loop L2|||Loop L3|||Loop L4|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000004624|||http://purl.uniprot.org/annotation/PRO_0000004625|||http://purl.uniprot.org/annotation/PRO_0000004626|||http://purl.uniprot.org/annotation/PRO_0000004627 http://togogenome.org/gene/10090:Dnaaf6b ^@ http://purl.uniprot.org/uniprot/Q8C6P5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PIH1D1/2/3 CS-like ^@ http://togogenome.org/gene/10090:Gm1140 ^@ http://purl.uniprot.org/uniprot/A2BH01 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Usp25 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPP4|||http://purl.uniprot.org/uniprot/P57080 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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|||Nucleophile|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Proton acceptor|||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_0000080654 http://togogenome.org/gene/10090:Vmn1r86 ^@ http://purl.uniprot.org/uniprot/L7N213 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cntnap3 ^@ http://purl.uniprot.org/uniprot/E9PY62 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||EGF-like|||F5/8 type C|||Fibrinogen C-terminal|||Helical|||Laminin G ^@ http://purl.uniprot.org/annotation/PRO_5003243023 http://togogenome.org/gene/10090:Cnn1 ^@ http://purl.uniprot.org/uniprot/B2RSH3|||http://purl.uniprot.org/uniprot/Q08091|||http://purl.uniprot.org/uniprot/Q8CBQ2 ^@ 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 ^@ Calponin-1|||Calponin-homology (CH)|||Calponin-like 1|||Calponin-like 2|||Calponin-like 3|||In isoform Beta.|||Phosphoserine; by ROCK2|||Phosphothreonine; by ROCK2 ^@ http://purl.uniprot.org/annotation/PRO_0000204768|||http://purl.uniprot.org/annotation/VSP_000755 http://togogenome.org/gene/10090:Svep1 ^@ http://purl.uniprot.org/uniprot/A2AVA0 ^@ 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 ^@ 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 1|||HYR 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pentraxin (PTX)|||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_5000057616|||http://purl.uniprot.org/annotation/VSP_031629|||http://purl.uniprot.org/annotation/VSP_031630 http://togogenome.org/gene/10090:Fam89b ^@ http://purl.uniprot.org/uniprot/Q7TMI7|||http://purl.uniprot.org/uniprot/Q9QUI1 ^@ 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 ^@ Disordered|||In isoform 2.|||LRR|||Leucine repeat adapter protein 25|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000420996|||http://purl.uniprot.org/annotation/VSP_045017 http://togogenome.org/gene/10090:Efr3b ^@ http://purl.uniprot.org/uniprot/Q6ZQ18 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ In isoform 2.|||Phosphoserine|||Protein EFR3 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000312296|||http://purl.uniprot.org/annotation/VSP_029808 http://togogenome.org/gene/10090:Pex5l ^@ http://purl.uniprot.org/uniprot/D3YYH0|||http://purl.uniprot.org/uniprot/F8SLP5|||http://purl.uniprot.org/uniprot/F8SLP6|||http://purl.uniprot.org/uniprot/F8SLP7|||http://purl.uniprot.org/uniprot/F8SLP8|||http://purl.uniprot.org/uniprot/F8SLP9|||http://purl.uniprot.org/uniprot/F8SLQ1|||http://purl.uniprot.org/uniprot/F8SLQ3|||http://purl.uniprot.org/uniprot/F8SLQ4|||http://purl.uniprot.org/uniprot/F8SLQ5|||http://purl.uniprot.org/uniprot/F8SLQ6|||http://purl.uniprot.org/uniprot/Q8C437 ^@ 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|||Disordered|||In isoform 3.|||In isoform 4.|||PEX5-related protein|||Phosphoserine|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6 ^@ http://purl.uniprot.org/annotation/PRO_0000106318|||http://purl.uniprot.org/annotation/VSP_010437|||http://purl.uniprot.org/annotation/VSP_010439 http://togogenome.org/gene/10090:Or2ag1 ^@ http://purl.uniprot.org/uniprot/Q9EPF7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp809 ^@ http://purl.uniprot.org/uniprot/G3X9G7 ^@ 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 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 809 ^@ http://purl.uniprot.org/annotation/PRO_0000431687|||http://purl.uniprot.org/annotation/VSP_057362|||http://purl.uniprot.org/annotation/VSP_057363 http://togogenome.org/gene/10090:Atp5j ^@ http://purl.uniprot.org/uniprot/P97450 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ ATP synthase-coupling factor 6, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000002529 http://togogenome.org/gene/10090:Taar3 ^@ http://purl.uniprot.org/uniprot/D8KZH8|||http://purl.uniprot.org/uniprot/Q5QD16 ^@ 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|||Trace amine-associated receptor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000070150 http://togogenome.org/gene/10090:Art1 ^@ http://purl.uniprot.org/uniprot/Q545U9|||http://purl.uniprot.org/uniprot/Q60935 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ GPI-anchor amidated serine|||GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1|||N-linked (GlcNAc...) asparagine|||NAD(P)(+)--arginine ADP-ribosyltransferase|||Removed in mature form|||TR mART core ^@ http://purl.uniprot.org/annotation/PRO_0000019313|||http://purl.uniprot.org/annotation/PRO_0000019314|||http://purl.uniprot.org/annotation/PRO_5015020034 http://togogenome.org/gene/10090:Ifna5 ^@ http://purl.uniprot.org/uniprot/Q810G2 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015098952 http://togogenome.org/gene/10090:Mc4r ^@ http://purl.uniprot.org/uniprot/P56450 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||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|||Interchain|||Melanocortin receptor 4|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069724 http://togogenome.org/gene/10090:Or2t46 ^@ http://purl.uniprot.org/uniprot/Q5NCD2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kazn ^@ http://purl.uniprot.org/uniprot/G3UY74|||http://purl.uniprot.org/uniprot/Q69ZS8|||http://purl.uniprot.org/uniprot/Q8BJ43 ^@ 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 and isoform 3.|||In isoform 2.|||In isoform 3.|||Kazrin|||Phosphoserine|||Polar residues|||SAM|||SAM 1|||SAM 2|||SAM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000322454|||http://purl.uniprot.org/annotation/VSP_031904|||http://purl.uniprot.org/annotation/VSP_031905|||http://purl.uniprot.org/annotation/VSP_031906|||http://purl.uniprot.org/annotation/VSP_031907 http://togogenome.org/gene/10090:Wwp2 ^@ http://purl.uniprot.org/uniprot/I3RSH5|||http://purl.uniprot.org/uniprot/Q3TXI7|||http://purl.uniprot.org/uniprot/Q9DBH0 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ C2|||Disordered|||Glycyl thioester intermediate|||HECT|||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_0000120339 http://togogenome.org/gene/10090:Fgd2 ^@ http://purl.uniprot.org/uniprot/Q8BY35 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ DH|||Disordered|||FYVE, RhoGEF and PH domain-containing protein 2|||FYVE-type|||Loss of early endosome localization; when associated with K-454.|||Loss of early endosome localization; when associated with T-455.|||No effect on early endosome localization and reduced JNK1 activation; when associated with A-287.|||No effect on early endosome localization and reduced JNK1 activation; when associated with A-288.|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000080943 http://togogenome.org/gene/10090:Pole2 ^@ http://purl.uniprot.org/uniprot/O54956 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ DNA polymerase epsilon subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000071563 http://togogenome.org/gene/10090:Slc7a6 ^@ http://purl.uniprot.org/uniprot/Q8BGK6 ^@ 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|||Extracellular|||Helical|||In isoform 2.|||Phosphoserine|||Y+L amino acid transporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000341478|||http://purl.uniprot.org/annotation/VSP_052833|||http://purl.uniprot.org/annotation/VSP_052834 http://togogenome.org/gene/10090:Rhobtb2 ^@ http://purl.uniprot.org/uniprot/Q91V93 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ BTB 1|||BTB 2|||Disordered|||Rho-like|||Rho-related BTB domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000198963 http://togogenome.org/gene/10090:Tmem204 ^@ http://purl.uniprot.org/uniprot/Q7TQI0 ^@ 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 204 ^@ http://purl.uniprot.org/annotation/PRO_0000089866 http://togogenome.org/gene/10090:Lypd6b ^@ http://purl.uniprot.org/uniprot/Q9D7F2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ GPI-anchor amidated serine|||In isoform 1.|||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_0000321952|||http://purl.uniprot.org/annotation/PRO_0000321953|||http://purl.uniprot.org/annotation/VSP_060613 http://togogenome.org/gene/10090:Saa1 ^@ http://purl.uniprot.org/uniprot/P05366|||http://purl.uniprot.org/uniprot/Q5I0U6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Important for amyloid formation|||Serum amyloid A protein|||Serum amyloid A-1 protein ^@ http://purl.uniprot.org/annotation/PRO_0000031588|||http://purl.uniprot.org/annotation/PRO_5014309835 http://togogenome.org/gene/10090:Rpl14 ^@ http://purl.uniprot.org/uniprot/Q9CR57 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1-1; approximate|||1-2|||1-3|||1-4|||2 X 3 AA tandem repeats of K-G-Q|||2-1|||2-2|||4 X 5 AA tandem repeats of Q-K-A-[APS]-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 ^@ http://purl.uniprot.org/annotation/PRO_0000132032 http://togogenome.org/gene/10090:Cmc2 ^@ http://purl.uniprot.org/uniprot/Q8K199 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Domain Extent|||Motif|||Region ^@ CHCH|||COX assembly mitochondrial protein 2 homolog|||Cx9C motif 1|||Cx9C motif 2|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000192944 http://togogenome.org/gene/10090:E030030I06Rik ^@ http://purl.uniprot.org/uniprot/Q8BLG7|||http://purl.uniprot.org/uniprot/Q8BW91 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gm21188 ^@ http://purl.uniprot.org/uniprot/Q3T9V6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ndufa11 ^@ http://purl.uniprot.org/uniprot/G5E814 ^@ Disulfide Bond|||Modification ^@ Disulfide Bond ^@ ^@ http://togogenome.org/gene/10090:Nr2c2 ^@ http://purl.uniprot.org/uniprot/G3X9W4|||http://purl.uniprot.org/uniprot/P49117|||http://purl.uniprot.org/uniprot/Q3ZAS1 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Enhanced transcriptional activation; Greatly enhanced transcriptional activation; when associated with A-15.|||Enhanced transcriptional activation; Greatly enhanced transcriptional activation; when associated with A-68.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||NR C4-type|||NR LBD|||No effect on transcriptional activation.|||Nuclear receptor|||Nuclear receptor subfamily 2 group C member 2|||Phosphoserine|||Phosphoserine; by MAPK|||Some repression of transcriptional activation; Repressed transcriptional activity by about 10-fold; when associated with E-19.|||Some repression of transcriptional activation; Repressed transcriptional activity by about 10-fold; when associated with E-68. ^@ http://purl.uniprot.org/annotation/PRO_0000053589 http://togogenome.org/gene/10090:Cstf3 ^@ http://purl.uniprot.org/uniprot/Q99LI7 ^@ Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||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|||N-acetylserine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000205723 http://togogenome.org/gene/10090:Tmub1 ^@ http://purl.uniprot.org/uniprot/Q9JMG3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Required to release iHOPS from membranes|||Transmembrane and ubiquitin-like domain-containing protein 1|||Ubiquitin-like|||iHOPS ^@ http://purl.uniprot.org/annotation/PRO_0000114923|||http://purl.uniprot.org/annotation/PRO_0000435489|||http://purl.uniprot.org/annotation/VSP_058102 http://togogenome.org/gene/10090:Il22ra2 ^@ http://purl.uniprot.org/uniprot/Q80XF5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site ^@ Abolishes IL22-binding.|||Critical for IL22-binding|||Fibronectin type-III 1|||Fibronectin type-III 2|||Interleukin-22 receptor subunit alpha-2 ^@ http://purl.uniprot.org/annotation/PRO_0000011017 http://togogenome.org/gene/10090:Gtsf1 ^@ http://purl.uniprot.org/uniprot/Q9DAN6 ^@ Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Strand|||Turn|||Zinc Finger ^@ CHHC U11-48K-type 1|||CHHC U11-48K-type 2|||Gametocyte-specific factor 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000221622 http://togogenome.org/gene/10090:Pcdhgb2 ^@ http://purl.uniprot.org/uniprot/Q91XX7 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (Man...) serine ^@ http://purl.uniprot.org/annotation/PRO_5015099527 http://togogenome.org/gene/10090:Sla2 ^@ http://purl.uniprot.org/uniprot/Q8R4L0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes interaction with ZAP70, and its inhibitory function.|||Abolishes isoform 2.|||Abolishes localization to membranes.|||Disordered|||Does not affect its inhibitory function.|||In isoform 2.|||N-myristoyl glycine|||Polar residues|||Removed|||SH2|||SH3|||SLA C-terminal|||Src-like-adapter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000022353|||http://purl.uniprot.org/annotation/VSP_018795 http://togogenome.org/gene/10090:Gucy1b1 ^@ http://purl.uniprot.org/uniprot/O54865|||http://purl.uniprot.org/uniprot/Q3UTI4|||http://purl.uniprot.org/uniprot/Q80YP4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Non-terminal Residue ^@ Guanylate cyclase|||Guanylate cyclase soluble subunit beta-1|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000074117 http://togogenome.org/gene/10090:BC030500 ^@ http://purl.uniprot.org/uniprot/Q8K0R8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Pcm1 ^@ http://purl.uniprot.org/uniprot/Q9R0L6 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Mediates interaction with DZIP1|||N-acetylalanine|||N6-acetyllysine|||Pericentriolar material 1 protein|||Phosphoserine|||Phosphoserine; by PLK4|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000274038|||http://purl.uniprot.org/annotation/VSP_022612 http://togogenome.org/gene/10090:Lypd6 ^@ http://purl.uniprot.org/uniprot/Q8BPP5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Motif|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated asparagine|||Ly6/PLAUR domain-containing protein 6|||N-linked (GlcNAc...) asparagine|||NxI motif|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036179|||http://purl.uniprot.org/annotation/PRO_0000457042 http://togogenome.org/gene/10090:Cdhr2 ^@ http://purl.uniprot.org/uniprot/E9Q7P9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||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|||Helical|||Mediates interaction with USH1C and MYO7B and is required for proper localization to microvilli tips and function in microvilli organization|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003243107 http://togogenome.org/gene/10090:Ttll8 ^@ http://purl.uniprot.org/uniprot/A4Q9F1|||http://purl.uniprot.org/uniprot/Q8C0V2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Site ^@ Basic and acidic residues|||Decreased monoglycylation activity.|||Decreased monoglycylation activity; when associated with E-104.|||Decreased monoglycylation activity; when associated with E-106.|||Decreased monoglycylation activity; when associated with E-93.|||Decreased monoglycylation activity; when associated with E-96.|||Decreased monoglycylation activity; when associated with N-328.|||Decreased monoglycylation activity; when associated with N-330.|||Disordered|||Essential for specifying initiation versus elongation step of the polyglycylase activity|||Polar residues|||Pro residues|||Protein monoglycylase TTLL8|||TTL ^@ http://purl.uniprot.org/annotation/PRO_0000326164 http://togogenome.org/gene/10090:Or11h6 ^@ http://purl.uniprot.org/uniprot/Q7TRL9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dmbt1 ^@ http://purl.uniprot.org/uniprot/A0A140LI59|||http://purl.uniprot.org/uniprot/E9QPG8|||http://purl.uniprot.org/uniprot/Q60997 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Abolishes phosphorylation.|||CUB|||CUB 1|||CUB 2|||CUB 3|||CUB 4|||CUB 5|||Deleted in malignant brain tumors 1 protein|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||SRCR|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4|||SRCR 5|||SRCR 6|||SRCR 7|||SRCR 8|||ZP ^@ http://purl.uniprot.org/annotation/PRO_0000045388|||http://purl.uniprot.org/annotation/PRO_5030168486|||http://purl.uniprot.org/annotation/PRO_5039971245|||http://purl.uniprot.org/annotation/VSP_016851|||http://purl.uniprot.org/annotation/VSP_016852|||http://purl.uniprot.org/annotation/VSP_016853 http://togogenome.org/gene/10090:Hdac2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J008|||http://purl.uniprot.org/uniprot/P70288|||http://purl.uniprot.org/uniprot/Q3TMT1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Does not affect S-nitrosylation.|||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|||Impairs S-nitrosylation. Abolishes S-nitrosylation; when associated with A-262.|||Impairs S-nitrosylation. Abolishes S-nitrosylation; when associated with A-274.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Proton acceptor|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000114694 http://togogenome.org/gene/10090:Lgals4 ^@ http://purl.uniprot.org/uniprot/Q3UL35|||http://purl.uniprot.org/uniprot/Q8K419 ^@ 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 ^@ Galectin|||Galectin 1|||Galectin 2|||Galectin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000076935 http://togogenome.org/gene/10090:Cmtr1 ^@ http://purl.uniprot.org/uniprot/Q9DBC3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Bipartite nuclear localization signal|||Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1|||Disordered|||G-patch|||Interaction with POLR2A|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Proton acceptor|||RrmJ-type SAM-dependent 2'-O-MTase|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000251240 http://togogenome.org/gene/10090:BC051019 ^@ http://purl.uniprot.org/uniprot/Q3UQ01|||http://purl.uniprot.org/uniprot/Q9JJR6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ DUF4537|||Disordered|||Polar residues|||Uncharacterized protein C11orf16 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089833 http://togogenome.org/gene/10090:Nckipsd ^@ http://purl.uniprot.org/uniprot/Q9ESJ4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Disordered|||NCK-interacting protein with SH3 domain|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000072131 http://togogenome.org/gene/10090:Meioc ^@ http://purl.uniprot.org/uniprot/A2AG06 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Meiosis-specific coiled-coil domain-containing protein MEIOC ^@ http://purl.uniprot.org/annotation/PRO_0000393412|||http://purl.uniprot.org/annotation/VSP_038974 http://togogenome.org/gene/10090:Gm5150 ^@ http://purl.uniprot.org/uniprot/Q1AN92 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097052 http://togogenome.org/gene/10090:Wdr47 ^@ http://purl.uniprot.org/uniprot/Q8CGF6 ^@ 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 ^@ CTLH|||Disordered|||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_0000051398 http://togogenome.org/gene/10090:Taf6 ^@ http://purl.uniprot.org/uniprot/Q62311 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Transcription initiation factor TFIID subunit 6 ^@ http://purl.uniprot.org/annotation/PRO_0000118874 http://togogenome.org/gene/10090:Prn ^@ http://purl.uniprot.org/uniprot/A0A075B668 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Prion/Doppel protein beta-ribbon ^@ http://togogenome.org/gene/10090:Trib3 ^@ http://purl.uniprot.org/uniprot/Q8K4K2 ^@ 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|||Interaction with DDIT3/CHOP|||Pro residues|||Protein kinase|||Tribbles homolog 3 ^@ http://purl.uniprot.org/annotation/PRO_0000131867 http://togogenome.org/gene/10090:Mme ^@ http://purl.uniprot.org/uniprot/Q61391 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||Neprilysin|||Peptidase M13|||Phosphoserine|||Proton donor|||Removed|||Stop-transfer sequence ^@ http://purl.uniprot.org/annotation/PRO_0000078214 http://togogenome.org/gene/10090:Or8g28 ^@ http://purl.uniprot.org/uniprot/Q9EQB5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nexmif ^@ http://purl.uniprot.org/uniprot/Q5DTT1 ^@ 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.|||Neurite extension and migration factor|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000257845|||http://purl.uniprot.org/annotation/VSP_021372 http://togogenome.org/gene/10090:Bicdl2 ^@ http://purl.uniprot.org/uniprot/Q8CHW5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ BICD family-like cargo adapter 2|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000302862 http://togogenome.org/gene/10090:Spag11b ^@ http://purl.uniprot.org/uniprot/Q3UW43 ^@ 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 ^@ In isoform 2.|||Sperm-associated antigen 11B ^@ http://purl.uniprot.org/annotation/PRO_5015097509|||http://purl.uniprot.org/annotation/VSP_061386|||http://purl.uniprot.org/annotation/VSP_061387|||http://purl.uniprot.org/annotation/VSP_061388 http://togogenome.org/gene/10090:Hnrnph1 ^@ http://purl.uniprot.org/uniprot/O35737|||http://purl.uniprot.org/uniprot/Q3TNG9|||http://purl.uniprot.org/uniprot/Q811L7|||http://purl.uniprot.org/uniprot/Q8C2Q7 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat ^@ 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|||N-acetylmethionine|||N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H, N-terminally processed|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||RRM|||RRM 1|||RRM 2|||RRM 3|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000081858|||http://purl.uniprot.org/annotation/PRO_0000367120 http://togogenome.org/gene/10090:Zdhhc13 ^@ http://purl.uniprot.org/uniprot/Q9CWU2 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Cytoplasmic|||DHHC|||Helical|||Lumenal|||N-acetylmethionine|||Palmitoyltransferase ZDHHC13|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212889 http://togogenome.org/gene/10090:Ccdc15 ^@ http://purl.uniprot.org/uniprot/Q8C9M2 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Splice Variant ^@ Coiled-coil domain-containing protein 15|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4. ^@ http://purl.uniprot.org/annotation/PRO_0000307716|||http://purl.uniprot.org/annotation/VSP_028797|||http://purl.uniprot.org/annotation/VSP_028798|||http://purl.uniprot.org/annotation/VSP_028799 http://togogenome.org/gene/10090:Traf2 ^@ http://purl.uniprot.org/uniprot/P39429|||http://purl.uniprot.org/uniprot/Q3U8L1|||http://purl.uniprot.org/uniprot/Q8C6X9 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger ^@ Abolished ubiquitination by the SCF(FBXL2) complex.|||Almost abolishes interaction with BIRC2; when associated with A-292.|||Almost abolishes interaction with BIRC2; when associated with A-294.|||Decreased interaction with FBXL2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Important for interaction with BIRC2 and BIRC3|||In isoform 2.|||Loss of autoubiquitination.|||MATH|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKC|||RING-type|||Reduces interaction with BIRC2.|||Removed|||TNF receptor-associated factor 2|||TRAF-type|||TRAF-type 1|||TRAF-type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000056400|||http://purl.uniprot.org/annotation/VSP_007402 http://togogenome.org/gene/10090:Kremen1 ^@ http://purl.uniprot.org/uniprot/Q99N43 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ CUB|||Complete loss of apoptotic activity.|||Cytoplasmic|||Essential for apoptotic activity|||Extracellular|||Helical|||Kremen protein 1|||Kringle|||N-linked (GlcNAc...) asparagine|||Significant reduction of apoptotic activity.|||WSC ^@ http://purl.uniprot.org/annotation/PRO_0000021565 http://togogenome.org/gene/10090:Hpn ^@ http://purl.uniprot.org/uniprot/E9Q5P0|||http://purl.uniprot.org/uniprot/G3UWE8|||http://purl.uniprot.org/uniprot/O35453 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes catalytic activity.|||Charge relay system|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||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_0000027843|||http://purl.uniprot.org/annotation/PRO_0000027844|||http://purl.uniprot.org/annotation/VSP_007232 http://togogenome.org/gene/10090:Entrep3 ^@ http://purl.uniprot.org/uniprot/E9Q6C9|||http://purl.uniprot.org/uniprot/Q5HZJ5 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||Protein ENTREP3 ^@ http://purl.uniprot.org/annotation/PRO_0000393335 http://togogenome.org/gene/10090:Tex28 ^@ http://purl.uniprot.org/uniprot/B1AYN9 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Pbx2 ^@ http://purl.uniprot.org/uniprot/O35984|||http://purl.uniprot.org/uniprot/Q4FJL3 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ 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_0000049238 http://togogenome.org/gene/10090:Ces1f ^@ http://purl.uniprot.org/uniprot/Q91WU0 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Acyl-ester intermediate|||Carboxylesterase 1F|||Charge relay system|||In isoform 2.|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_5006993881|||http://purl.uniprot.org/annotation/VSP_058396|||http://purl.uniprot.org/annotation/VSP_058397 http://togogenome.org/gene/10090:Klrc1 ^@ http://purl.uniprot.org/uniprot/E9QAJ6|||http://purl.uniprot.org/uniprot/Q9WU32|||http://purl.uniprot.org/uniprot/Q9WVJ8|||http://purl.uniprot.org/uniprot/Q9Z202 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Mrps27 ^@ http://purl.uniprot.org/uniprot/Q8BK72 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ Chain|||Coiled-Coil|||Repeat|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||PPR 1|||PPR 2|||Small ribosomal subunit protein mS27 ^@ http://purl.uniprot.org/annotation/PRO_0000261586 http://togogenome.org/gene/10090:Gal3st4 ^@ http://purl.uniprot.org/uniprot/E9Q7N6|||http://purl.uniprot.org/uniprot/Q3V1B8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Qrich2 ^@ http://purl.uniprot.org/uniprot/Q3V2A7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Variant ^@ Disordered|||Glutamine-rich protein 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000447710 http://togogenome.org/gene/10090:Ctsc ^@ http://purl.uniprot.org/uniprot/P97821|||http://purl.uniprot.org/uniprot/Q3U7T5|||http://purl.uniprot.org/uniprot/Q3UBY5|||http://purl.uniprot.org/uniprot/Q8BQL3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Signal Peptide ^@ Cathepsin C exclusion|||Dipeptidyl peptidase 1|||Dipeptidyl peptidase 1 exclusion domain chain|||Dipeptidyl peptidase 1 heavy chain|||Dipeptidyl peptidase 1 light chain|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000026346|||http://purl.uniprot.org/annotation/PRO_0000026347|||http://purl.uniprot.org/annotation/PRO_0000026348|||http://purl.uniprot.org/annotation/PRO_0000026349|||http://purl.uniprot.org/annotation/PRO_5014205830|||http://purl.uniprot.org/annotation/PRO_5015097471|||http://purl.uniprot.org/annotation/PRO_5018722361 http://togogenome.org/gene/10090:Accsl ^@ http://purl.uniprot.org/uniprot/Q3UX83 ^@ 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.|||N6-(pyridoxal phosphate)lysine|||Polar residues|||Probable inactive 1-aminocyclopropane-1-carboxylate synthase-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000337058|||http://purl.uniprot.org/annotation/VSP_033860 http://togogenome.org/gene/10090:Slc6a6 ^@ http://purl.uniprot.org/uniprot/O35316|||http://purl.uniprot.org/uniprot/Q3UPI8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium- and chloride-dependent taurine transporter ^@ http://purl.uniprot.org/annotation/PRO_0000214768 http://togogenome.org/gene/10090:Amn ^@ http://purl.uniprot.org/uniprot/Q99JB7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Interaction with CUBN|||N-linked (GlcNAc...) asparagine|||Protein amnionless|||Soluble protein amnionless|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000020703|||http://purl.uniprot.org/annotation/PRO_0000447652 http://togogenome.org/gene/10090:Slc44a3 ^@ http://purl.uniprot.org/uniprot/Q921V7 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Transmembrane ^@ Choline transporter-like protein 3|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000191721 http://togogenome.org/gene/10090:Pigp ^@ http://purl.uniprot.org/uniprot/B8JK65|||http://purl.uniprot.org/uniprot/B8JK66|||http://purl.uniprot.org/uniprot/B8JK67|||http://purl.uniprot.org/uniprot/Q6P8Q9|||http://purl.uniprot.org/uniprot/Q9JHG1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||KH-like RNA-binding|||PIG-P|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit P ^@ http://purl.uniprot.org/annotation/PRO_0000191784 http://togogenome.org/gene/10090:Or1o11 ^@ http://purl.uniprot.org/uniprot/Q8VFA1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ran ^@ http://purl.uniprot.org/uniprot/P62827 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ 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|||Interaction with RANBP1|||Loss of interaction with NEMP1.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||No effect on RANBP10-binding. Loss of interaction with NEMP1.|||Phosphothreonine|||Removed|||Strongly decreases interaction with RANGRF. Partial decrease in RANBP10-binding. No effect on interaction with NEMP1 and KPNB1. ^@ http://purl.uniprot.org/annotation/PRO_0000208697 http://togogenome.org/gene/10090:Chrna5 ^@ http://purl.uniprot.org/uniprot/Q2MKA5|||http://purl.uniprot.org/uniprot/Q8BIE9 ^@ 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 ^@ Associated with receptor activation|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||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_0000304938|||http://purl.uniprot.org/annotation/PRO_5022269968|||http://purl.uniprot.org/annotation/VSP_028132 http://togogenome.org/gene/10090:Ss18l1 ^@ http://purl.uniprot.org/uniprot/Q8BW22 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Calcium-responsive transactivator|||Disordered|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000391346 http://togogenome.org/gene/10090:Or4c106 ^@ http://purl.uniprot.org/uniprot/Q7TR10 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc47a1 ^@ http://purl.uniprot.org/uniprot/Q8K0H1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Multidrug and toxin extrusion protein 1|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000312846|||http://purl.uniprot.org/annotation/VSP_029906|||http://purl.uniprot.org/annotation/VSP_029907 http://togogenome.org/gene/10090:Dyrk2 ^@ http://purl.uniprot.org/uniprot/Q5U4C9 ^@ 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 ^@ Disordered|||Dual specificity tyrosine-phosphorylation-regulated kinase 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_0000291265 http://togogenome.org/gene/10090:Dmrtc2 ^@ http://purl.uniprot.org/uniprot/Q8CGW9 ^@ 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 C2|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000244107 http://togogenome.org/gene/10090:Mrgbp ^@ http://purl.uniprot.org/uniprot/Q9DAT2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||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.|||MRG/MORF4L-binding protein|||N-acetylglycine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000215877|||http://purl.uniprot.org/annotation/VSP_003793 http://togogenome.org/gene/10090:Txndc16 ^@ http://purl.uniprot.org/uniprot/Q7TN22 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Mediates endoplasmic reticulum retention|||N-linked (GlcNAc...) asparagine|||Thioredoxin|||Thioredoxin domain-containing protein 16 ^@ http://purl.uniprot.org/annotation/PRO_0000257790|||http://purl.uniprot.org/annotation/VSP_021364 http://togogenome.org/gene/10090:Dcaf8 ^@ http://purl.uniprot.org/uniprot/Q8N7N5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Splice Variant ^@ Basic and acidic residues|||DDB1- and CUL4-associated factor 8|||Disordered|||In isoform 2.|||Nuclear export signal|||Omega-N-methylarginine; by PRMT1|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000296958|||http://purl.uniprot.org/annotation/VSP_027266|||http://purl.uniprot.org/annotation/VSP_027267 http://togogenome.org/gene/10090:Or10ad1 ^@ http://purl.uniprot.org/uniprot/E9PZS7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hoxb1 ^@ http://purl.uniprot.org/uniprot/P17919 ^@ 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-B1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000200108 http://togogenome.org/gene/10090:Pxylp1 ^@ http://purl.uniprot.org/uniprot/Q8BHA9 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 2-phosphoxylose phosphatase 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000314925 http://togogenome.org/gene/10090:Chpf2 ^@ http://purl.uniprot.org/uniprot/Q3UU43 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Disordered|||Hexosyltransferase|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5015097501 http://togogenome.org/gene/10090:Mtr ^@ http://purl.uniprot.org/uniprot/A6H5Y3 ^@ 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 ^@ AdoMet activation|||B12-binding|||B12-binding N-terminal|||Hcy-binding|||Methionine synthase|||Phosphothreonine|||Pterin-binding|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000312901 http://togogenome.org/gene/10090:Slc22a19 ^@ http://purl.uniprot.org/uniprot/Q8VCA0 ^@ 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|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 19 ^@ http://purl.uniprot.org/annotation/PRO_0000441094 http://togogenome.org/gene/10090:Wfdc9 ^@ http://purl.uniprot.org/uniprot/Q3UW41 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Protein WFDC9 ^@ http://purl.uniprot.org/annotation/PRO_0000293712 http://togogenome.org/gene/10090:C1qtnf12 ^@ http://purl.uniprot.org/uniprot/Q8R2Z0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Abolishes multimeric complex formation.|||Abolishes protein processing.|||Adipolin fC1QTNF12|||Adipolin gC1QTNF12|||C1q|||Cleavage; by FURIN|||Decreased N-glycosylation.|||Disordered|||Enhances protein processing.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes protein processing.|||Not glycosylated|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000284355|||http://purl.uniprot.org/annotation/PRO_0000430249 http://togogenome.org/gene/10090:Dhfr ^@ http://purl.uniprot.org/uniprot/P00375|||http://purl.uniprot.org/uniprot/Q544T5 ^@ 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 ^@ DHFR|||Dihydrofolate reductase|||In L-5178-Y cell line; methotrexate-resistant, requires 2 nucleotide substitutions.|||In a form with an abnormally low affinity for methotrexate.|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000186364 http://togogenome.org/gene/10090:Defb37 ^@ http://purl.uniprot.org/uniprot/Q7TMD2 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 37 ^@ http://purl.uniprot.org/annotation/PRO_0000006949 http://togogenome.org/gene/10090:Aire ^@ http://purl.uniprot.org/uniprot/B2MVU6|||http://purl.uniprot.org/uniprot/Q3ZB65|||http://purl.uniprot.org/uniprot/Q3ZB71|||http://purl.uniprot.org/uniprot/Q9Z0E3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger ^@ Abolishes interaction with histone H3.|||Autoimmune regulator|||Disordered|||HSR|||In isoform 1b, isoform 1d, isoform 2b, isoform 2d, isoform 3b and isoform 3d.|||In isoform 1c, isoform 1d, isoform 2c, isoform 2d, isoform 3c and isoform 3d.|||In isoform 2a, isoform 2b, isoform 2c and isoform 2d.|||In isoform 3a, isoform 3b, isoform 3c and isoform 3d.|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||No effect on interaction with histone H3.|||Nuclear localization signal|||PHD-type|||PHD-type 1|||PHD-type 2|||Polar residues|||Reduces interaction with histone H3.|||SAND ^@ http://purl.uniprot.org/annotation/PRO_0000064514|||http://purl.uniprot.org/annotation/VSP_004091|||http://purl.uniprot.org/annotation/VSP_004092|||http://purl.uniprot.org/annotation/VSP_004093|||http://purl.uniprot.org/annotation/VSP_004094|||http://purl.uniprot.org/annotation/VSP_004095 http://togogenome.org/gene/10090:Upf3a ^@ http://purl.uniprot.org/uniprot/Q3ULJ3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||UPF3 ^@ http://togogenome.org/gene/10090:Pck1 ^@ http://purl.uniprot.org/uniprot/Q9Z2V4 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region ^@ N6-acetyllysine|||N6-acetyllysine; by p300/EP300|||Omega-loop|||Phosphoenolpyruvate carboxykinase, cytosolic [GTP]|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000103628 http://togogenome.org/gene/10090:Cdh19 ^@ http://purl.uniprot.org/uniprot/E9Q3A7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245645 http://togogenome.org/gene/10090:Gmnc ^@ http://purl.uniprot.org/uniprot/Q3URY2 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Splice Variant ^@ Disordered|||Geminin coiled-coil domain-containing protein 1|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000346426|||http://purl.uniprot.org/annotation/VSP_034992|||http://purl.uniprot.org/annotation/VSP_034993 http://togogenome.org/gene/10090:Impdh1 ^@ http://purl.uniprot.org/uniprot/P50096 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ CBS 1|||CBS 2|||Inosine-5'-monophosphate dehydrogenase 1|||Omega-N-methylarginine|||Phosphoserine|||Proton acceptor|||Thioimidate intermediate|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000093671 http://togogenome.org/gene/10090:Spats2l ^@ http://purl.uniprot.org/uniprot/E9PVQ3|||http://purl.uniprot.org/uniprot/Q91WJ7 ^@ 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|||Basic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||SPATS2-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000307700|||http://purl.uniprot.org/annotation/VSP_028793 http://togogenome.org/gene/10090:Pou5f1 ^@ http://purl.uniprot.org/uniprot/A0A2I6EDI9|||http://purl.uniprot.org/uniprot/P20263 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||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|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ 9aaTAD|||Absence of phosphorylation. Reduced protein degradation. Reduced self-renewal ability in ES cells. No change in FBXW4 binding. Loss of FBXW8 binding.|||Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 55% lower expression of YES1.|||Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 70% lower expression of YES1. Reduced DNA binding. No change in nuclear location. No change in nuclear localization. Absence of sumoylation; when associated with R-215 and R-244.|||DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Homeobox|||Loss of MAPK9 binding. Absence of Ser-347 phosphorylation.|||Loss of self-renewal ability in iPS cells.|||No change in DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location.|||No change in DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location. No loss of ability to bind SOX2. Reduced levels of CHD4 and SMARCA4 in a POU5F1 pulldown assay.|||No change in DNA binding. No change in nuclear location.|||No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location.|||No change in DNA binding. Reduced self-renewal ability in iPS cells. No change in nuclear location.|||No change in sumoylation. No change in sumoylation; when associated with R-215. Loss of sumoylation; when associated with R-118 and R-215. No change in nuclear localization; when associated with R-118 and R-215.|||No change in sumoylation; when associated with R-244. Loss of sumoylation. No change in nuclear localization; when associated with R-118 and R-244.|||POU domain, class 5, transcription factor 1|||POU-specific|||Phosphoserine|||Phosphoserine; by MAPK|||Phosphoserine; by MAPK8 and MAPK9|||Phosphothreonine|||Polar residues|||Reduced DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location. ^@ http://purl.uniprot.org/annotation/PRO_0000100749 http://togogenome.org/gene/10090:Or5p54 ^@ http://purl.uniprot.org/uniprot/Q8VFC9 ^@ 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 5P54 ^@ http://purl.uniprot.org/annotation/PRO_0000150834 http://togogenome.org/gene/10090:Vmn1r93 ^@ http://purl.uniprot.org/uniprot/K7N6B8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pcdhb13 ^@ http://purl.uniprot.org/uniprot/Q91Y06 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099541 http://togogenome.org/gene/10090:Eps8 ^@ http://purl.uniprot.org/uniprot/Q08509|||http://purl.uniprot.org/uniprot/Q3U2Z5|||http://purl.uniprot.org/uniprot/Q3UFL4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand ^@ Abolishes barbed-end actin-binding without affecting actin bundling activity.|||Amphipathic helix|||Basic and acidic residues|||Disordered|||Does not detach from actin following BDNF treatment; when associated with A-624.|||Does not detach from actin following BDNF treatment; when associated with A-628.|||Effector region|||Epidermal growth factor receptor kinase substrate 8|||Helix bundle 1|||Helix bundle 2|||Helix bundle 3|||Helix bundle 4|||Impairs both actin capping and bundling activities.|||Mimicks phosphorylation state; promotes detachment from actin in absence of BDNF treatment; when associated with E-624.|||Mimicks phosphorylation state; promotes detachment from actin in absence of BDNF treatment; when associated with E-628.|||PID|||PTB|||Phosphoserine|||Phosphoserine; by MAPK|||Phosphothreonine|||Phosphothreonine; by MAPK|||Polar residues|||Pro residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000086995 http://togogenome.org/gene/10090:Tgfb2 ^@ http://purl.uniprot.org/uniprot/A0A0A6YXU9|||http://purl.uniprot.org/uniprot/P27090|||http://purl.uniprot.org/uniprot/Q3TWH5|||http://purl.uniprot.org/uniprot/Q8CDZ9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Strand ^@ Interchain|||Latency-associated peptide|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile|||Transforming growth factor beta|||Transforming growth factor beta-2|||Transforming growth factor beta-2 proprotein ^@ http://purl.uniprot.org/annotation/PRO_0000033786|||http://purl.uniprot.org/annotation/PRO_0000033787|||http://purl.uniprot.org/annotation/PRO_0000456181|||http://purl.uniprot.org/annotation/PRO_5016196282 http://togogenome.org/gene/10090:Rdh5 ^@ http://purl.uniprot.org/uniprot/O55240 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Proton acceptor|||Retinol dehydrogenase 5 ^@ http://purl.uniprot.org/annotation/PRO_0000419633 http://togogenome.org/gene/10090:Odam ^@ http://purl.uniprot.org/uniprot/A1E960 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||Interaction with ARHGEF5|||O-linked (GalNAc...) threonine|||Odontogenic ameloblast-associated protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5000183880 http://togogenome.org/gene/10090:Zswim4 ^@ http://purl.uniprot.org/uniprot/Q8C7B8 ^@ 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_0000223102 http://togogenome.org/gene/10090:Cdh1 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZW5|||http://purl.uniprot.org/uniprot/P09803 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Adheres to and takes up L.monocytogenes InlA coated beads.|||Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-1|||Cleavage; by a metalloproteinase|||Cleavage; by caspase-3|||Cleavage; by gamma-secretase/PS1|||Cytoplasmic|||Disordered|||E-Cad/CTF1|||E-Cad/CTF2|||E-Cad/CTF3|||Extracellular|||Helical|||Increased affinity for L.monocytogenes InlA. Greatly increased affinity; when associated with P-172.|||N-linked (GlcNAc...) asparagine|||O-linked (Man...) serine|||O-linked (Man...) threonine|||Phosphoserine|||Phosphotyrosine; by SRC|||Required for binding CTNND1 and PSEN1|||Required for binding alpha, beta and gamma catenins ^@ http://purl.uniprot.org/annotation/PRO_0000003717|||http://purl.uniprot.org/annotation/PRO_0000003718|||http://purl.uniprot.org/annotation/PRO_0000236070|||http://purl.uniprot.org/annotation/PRO_0000236071|||http://purl.uniprot.org/annotation/PRO_0000236072|||http://purl.uniprot.org/annotation/PRO_5015044280 http://togogenome.org/gene/10090:Aif1 ^@ http://purl.uniprot.org/uniprot/O70200|||http://purl.uniprot.org/uniprot/Q4FJL9 ^@ 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 ^@ Allograft inflammatory factor 1|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2; degenerate|||N-acetylserine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073867 http://togogenome.org/gene/10090:Vmn1r75 ^@ http://purl.uniprot.org/uniprot/Q8R289 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gas2l2 ^@ http://purl.uniprot.org/uniprot/Q5SSG4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||GAR|||GAS2-like protein 2|||Interaction with ADORA2A and GNAS|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000190445 http://togogenome.org/gene/10090:Sec11c ^@ http://purl.uniprot.org/uniprot/Q9D8V7 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Region|||Topological Domain|||Transmembrane ^@ C-terminal short (CTS) helix|||Charge relay system|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Signal peptidase complex catalytic subunit SEC11C ^@ http://purl.uniprot.org/annotation/PRO_0000109549 http://togogenome.org/gene/10090:Prkch ^@ http://purl.uniprot.org/uniprot/P23298|||http://purl.uniprot.org/uniprot/Q3UKY1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger ^@ AGC-kinase C-terminal|||C2|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Protein kinase|||Protein kinase C eta type|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000055706 http://togogenome.org/gene/10090:Rfng ^@ http://purl.uniprot.org/uniprot/O09009 ^@ 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 ^@ Beta-1,3-N-acetylglucosaminyltransferase radical fringe|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219186 http://togogenome.org/gene/10090:Slc35e4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0N3|||http://purl.uniprot.org/uniprot/Q8K3D6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ EamA|||Helical|||Solute carrier family 35 member E4|||Sugar phosphate transporter ^@ http://purl.uniprot.org/annotation/PRO_0000298928 http://togogenome.org/gene/10090:Serpina3j ^@ http://purl.uniprot.org/uniprot/D3Z451 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Serpin ^@ http://purl.uniprot.org/annotation/PRO_5015088524 http://togogenome.org/gene/10090:Orm3 ^@ http://purl.uniprot.org/uniprot/J3JRU4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Signal Peptide ^@ Alpha-1-acid glycoprotein|||Lipocalin/cytosolic fatty-acid binding|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_5015094048 http://togogenome.org/gene/10090:Klra6 ^@ http://purl.uniprot.org/uniprot/Q60653 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Killer cell lectin-like receptor 6|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046684 http://togogenome.org/gene/10090:Sftpd ^@ http://purl.uniprot.org/uniprot/P50404 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide ^@ Basic and acidic residues|||C-type lectin|||Collagen-like|||Disordered|||N-linked (GlcNAc...) asparagine|||Pulmonary surfactant-associated protein D|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000017466 http://togogenome.org/gene/10090:H1f9 ^@ http://purl.uniprot.org/uniprot/Q5SWB1|||http://purl.uniprot.org/uniprot/Q9QYL0 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||H15|||Phosphoserine|||Spermatid-specific linker histone H1-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000196015 http://togogenome.org/gene/10090:Klk10 ^@ http://purl.uniprot.org/uniprot/Q99M20 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015099610 http://togogenome.org/gene/10090:Dcun1d4 ^@ http://purl.uniprot.org/uniprot/B7ZMU0|||http://purl.uniprot.org/uniprot/Q8C5X2|||http://purl.uniprot.org/uniprot/Q8CCA0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region ^@ Basic and acidic residues|||DCN1-like protein 4|||DCUN1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000129504 http://togogenome.org/gene/10090:Zfp212 ^@ http://purl.uniprot.org/uniprot/G3X8R7|||http://purl.uniprot.org/uniprot/Q6P238|||http://purl.uniprot.org/uniprot/Q6ZPF1 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Ap1m2 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZX6|||http://purl.uniprot.org/uniprot/A0A0R4J1L4|||http://purl.uniprot.org/uniprot/Q9WVP1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ AP-1 complex subunit mu-2|||In isoform 2.|||MHD ^@ http://purl.uniprot.org/annotation/PRO_0000193773|||http://purl.uniprot.org/annotation/VSP_000170 http://togogenome.org/gene/10090:Noxo1 ^@ http://purl.uniprot.org/uniprot/Q8VCM2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||NADPH oxidase organizer 1|||PX|||Proline-rich region; mediates mutually exclusive interactions with itself and NOXA1|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000227595|||http://purl.uniprot.org/annotation/VSP_017562|||http://purl.uniprot.org/annotation/VSP_017563 http://togogenome.org/gene/10090:Dynlt1b ^@ http://purl.uniprot.org/uniprot/P51807 ^@ 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 ^@ Dynein light chain Tctex-type 1|||Interaction with GNB1|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000195153 http://togogenome.org/gene/10090:Snap47 ^@ http://purl.uniprot.org/uniprot/Q8R570 ^@ 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.|||Synaptosomal-associated protein 47|||t-SNARE coiled-coil homology 1|||t-SNARE coiled-coil homology 2 ^@ http://purl.uniprot.org/annotation/PRO_0000307152|||http://purl.uniprot.org/annotation/VSP_028615|||http://purl.uniprot.org/annotation/VSP_028616 http://togogenome.org/gene/10090:Abhd12b ^@ http://purl.uniprot.org/uniprot/G3UZN6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serine aminopeptidase S33 ^@ http://togogenome.org/gene/10090:Hipk3 ^@ http://purl.uniprot.org/uniprot/A2RRJ7|||http://purl.uniprot.org/uniprot/Q3UST3|||http://purl.uniprot.org/uniprot/Q9ERH7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 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); alternate|||Homeodomain-interacting protein kinase 3|||Impairs catalytic activity and abolishes interaction with DAXX.|||Impairs catalytic activity.|||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_0000085999 http://togogenome.org/gene/10090:Flt3 ^@ http://purl.uniprot.org/uniprot/Q00342|||http://purl.uniprot.org/uniprot/Q3TQF1|||http://purl.uniprot.org/uniprot/Q3UEW6 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like domain-containing protein|||Important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of ligand binding|||Loss of kinase activity; no effect on FIZ1-binding.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Receptor-type tyrosine-protein kinase FLT3|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000016779|||http://purl.uniprot.org/annotation/PRO_5004229678|||http://purl.uniprot.org/annotation/PRO_5015097479 http://togogenome.org/gene/10090:Znhit1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1S6|||http://purl.uniprot.org/uniprot/D3YZ33|||http://purl.uniprot.org/uniprot/Q8R331 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||HIT-type|||Interaction with NR1D2|||Nuclear localization signal|||Phosphothreonine; by MAPK11 and MAPK14|||Zinc finger HIT domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000173547 http://togogenome.org/gene/10090:Krt10 ^@ http://purl.uniprot.org/uniprot/A2A513|||http://purl.uniprot.org/uniprot/P02535 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Asymmetric dimethylarginine; alternate|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In isoform 2 and isoform 3.|||In isoform 3.|||Interchain|||Keratin, type I cytoskeletal 10|||Linker 1|||Linker 12|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063643|||http://purl.uniprot.org/annotation/VSP_021100|||http://purl.uniprot.org/annotation/VSP_021101|||http://purl.uniprot.org/annotation/VSP_021102|||http://purl.uniprot.org/annotation/VSP_021103 http://togogenome.org/gene/10090:Tchh ^@ http://purl.uniprot.org/uniprot/A0A0B4J1F9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||EF-hand ^@ http://togogenome.org/gene/10090:C2cd4c ^@ http://purl.uniprot.org/uniprot/Q5HZI2 ^@ 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 ^@ C2|||C2 calcium-dependent domain-containing protein 4C|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000293735 http://togogenome.org/gene/10090:Pno1 ^@ http://purl.uniprot.org/uniprot/Q9CPS7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||KH|||RNA-binding protein PNO1 ^@ http://purl.uniprot.org/annotation/PRO_0000270541 http://togogenome.org/gene/10090:Tec ^@ http://purl.uniprot.org/uniprot/P24604|||http://purl.uniprot.org/uniprot/Q3TH41|||http://purl.uniprot.org/uniprot/Q3U436|||http://purl.uniprot.org/uniprot/Q8CFK4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||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|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Btk-type|||Impairs kinase activity.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 6.|||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_0000088171|||http://purl.uniprot.org/annotation/VSP_005012|||http://purl.uniprot.org/annotation/VSP_005013|||http://purl.uniprot.org/annotation/VSP_005014|||http://purl.uniprot.org/annotation/VSP_005015|||http://purl.uniprot.org/annotation/VSP_005016 http://togogenome.org/gene/10090:Rasl12 ^@ http://purl.uniprot.org/uniprot/Q08AT1 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Ras-like protein family member 12 ^@ http://purl.uniprot.org/annotation/PRO_0000333869 http://togogenome.org/gene/10090:Adam30 ^@ http://purl.uniprot.org/uniprot/Q811Q3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Disintegrin|||EGF-like|||Helical|||Peptidase M12B ^@ http://purl.uniprot.org/annotation/PRO_5015098942 http://togogenome.org/gene/10090:Vmn1r16 ^@ http://purl.uniprot.org/uniprot/K7N775 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ogfod2 ^@ http://purl.uniprot.org/uniprot/Q9CQ04 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2|||Fe2OG dioxygenase ^@ http://purl.uniprot.org/annotation/PRO_0000288979 http://togogenome.org/gene/10090:Fam25a ^@ http://purl.uniprot.org/uniprot/Q8CF02 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein FAM25C ^@ http://purl.uniprot.org/annotation/PRO_0000270920 http://togogenome.org/gene/10090:Fxyd4 ^@ http://purl.uniprot.org/uniprot/Q9D2W0 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||FXYD domain-containing ion transport regulator 4|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000010367 http://togogenome.org/gene/10090:Snn ^@ http://purl.uniprot.org/uniprot/P61807|||http://purl.uniprot.org/uniprot/Q5M8P0 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Mitochondrial intermembrane|||Phosphoserine|||Stannin|||Stannin cytoplasmic|||Stannin transmembrane|||Stannin unstructured linker ^@ http://purl.uniprot.org/annotation/PRO_0000072015 http://togogenome.org/gene/10090:Trub2 ^@ http://purl.uniprot.org/uniprot/H3BKT7|||http://purl.uniprot.org/uniprot/Q91WG3 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||Nucleophile|||Polar residues|||Pseudouridine synthase II N-terminal|||Pseudouridylate synthase TRUB2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000252091 http://togogenome.org/gene/10090:Cfap300 ^@ http://purl.uniprot.org/uniprot/Q8CC70 ^@ Chain|||Molecule Processing ^@ Chain ^@ Cilia- and flagella-associated protein 300 ^@ http://purl.uniprot.org/annotation/PRO_0000444628 http://togogenome.org/gene/10090:Scrn1 ^@ http://purl.uniprot.org/uniprot/Q9CZC8 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Secernin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000221437 http://togogenome.org/gene/10090:Sfrp4 ^@ http://purl.uniprot.org/uniprot/Q9Z1N6 ^@ 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 ^@ Basic residues|||Disordered|||FZ|||N-linked (GlcNAc...) asparagine|||NTR|||Polar residues|||Secreted frizzled-related sequence protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000032552 http://togogenome.org/gene/10090:Cyp3a41a ^@ http://purl.uniprot.org/uniprot/Q9JMA7 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Cytochrome P450 3A41|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051813 http://togogenome.org/gene/10090:Gm3776 ^@ http://purl.uniprot.org/uniprot/Q6P8Q0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ GST C-terminal|||GST N-terminal ^@ http://togogenome.org/gene/10090:Cyp4x1 ^@ http://purl.uniprot.org/uniprot/Q6A152 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Cytochrome P450 4X1|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000421683 http://togogenome.org/gene/10090:Pih1d1 ^@ http://purl.uniprot.org/uniprot/Q9CQJ2 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Strand ^@ Abolishes binding to TELO2-phosphopeptide.|||Interacts with TELO2|||No effect on binding to TELO2-phosphopeptide.|||PIH1 domain-containing protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000307329 http://togogenome.org/gene/10090:Lsg1 ^@ http://purl.uniprot.org/uniprot/Q3UM18 ^@ 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|||In isoform 2.|||Large subunit GTPase 1 homolog|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000324555|||http://purl.uniprot.org/annotation/VSP_032275 http://togogenome.org/gene/10090:Tmem132a ^@ http://purl.uniprot.org/uniprot/Q922P8 ^@ 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 ^@ Acidic residues|||Binds to HSPA5/GRP78|||Confers cellular localization similar to full-length form|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 132A ^@ http://purl.uniprot.org/annotation/PRO_0000287097 http://togogenome.org/gene/10090:Or4c115 ^@ http://purl.uniprot.org/uniprot/F7BL62 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zc3h13 ^@ http://purl.uniprot.org/uniprot/A0A2I3BPQ5|||http://purl.uniprot.org/uniprot/E9Q784|||http://purl.uniprot.org/uniprot/Q8BHW0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C3H1-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger CCCH domain-containing protein 13 ^@ http://purl.uniprot.org/annotation/PRO_0000434521 http://togogenome.org/gene/10090:D8Ertd738e ^@ http://purl.uniprot.org/uniprot/Q8R1F0 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Leydig cell tumor 10 kDa protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000255271 http://togogenome.org/gene/10090:Cntn2 ^@ http://purl.uniprot.org/uniprot/Q61330 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Cell attachment site|||Contactin-2|||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_0000014697|||http://purl.uniprot.org/annotation/PRO_0000014698 http://togogenome.org/gene/10090:Srp54b ^@ http://purl.uniprot.org/uniprot/P14576 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||M-domain|||NG-domain|||Signal recognition particle subunit SRP54 ^@ http://purl.uniprot.org/annotation/PRO_0000101194|||http://purl.uniprot.org/annotation/VSP_014953|||http://purl.uniprot.org/annotation/VSP_014954 http://togogenome.org/gene/10090:Ankrd12 ^@ http://purl.uniprot.org/uniprot/G5E893|||http://purl.uniprot.org/uniprot/Q05CM6|||http://purl.uniprot.org/uniprot/Q80TP9 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat ^@ ANK|||Basic and acidic residues|||Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Isyna1 ^@ http://purl.uniprot.org/uniprot/Q9JHU9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Inositol-3-phosphate synthase 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000324630 http://togogenome.org/gene/10090:Bag6 ^@ http://purl.uniprot.org/uniprot/G3UZT6|||http://purl.uniprot.org/uniprot/Q3UF95|||http://purl.uniprot.org/uniprot/Q9Z1R2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Site ^@ 1|||2|||3|||4|||4 X 29 AA approximate repeats|||BAG-similar domain, required and sufficient for interaction with UBL4A|||Basic and acidic residues|||Cleavage; by CASP3|||Disordered|||Large proline-rich protein BAG6|||N-acetylmethionine|||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_0000114898 http://togogenome.org/gene/10090:Igfl3 ^@ http://purl.uniprot.org/uniprot/Q6B9Z0 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Insulin growth factor-like family member ^@ http://purl.uniprot.org/annotation/PRO_0000045063 http://togogenome.org/gene/10090:Tmem131 ^@ http://purl.uniprot.org/uniprot/O70472|||http://purl.uniprot.org/uniprot/Q9CSR0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Polar residues|||Pro residues|||Transmembrane protein 131 ^@ http://purl.uniprot.org/annotation/PRO_0000097539 http://togogenome.org/gene/10090:Elf2 ^@ http://purl.uniprot.org/uniprot/Q3TVH6|||http://purl.uniprot.org/uniprot/Q9JHC9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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 and isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204088|||http://purl.uniprot.org/annotation/VSP_014159|||http://purl.uniprot.org/annotation/VSP_014160 http://togogenome.org/gene/10090:Mup5 ^@ http://purl.uniprot.org/uniprot/P11591 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ Major urinary protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000017931 http://togogenome.org/gene/10090:Bpifa6 ^@ http://purl.uniprot.org/uniprot/Q0VGU8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipid-binding serum glycoprotein N-terminal ^@ http://purl.uniprot.org/annotation/PRO_5015097004 http://togogenome.org/gene/10090:Sh3bgrl3 ^@ http://purl.uniprot.org/uniprot/Q91VW3 ^@ 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_0000220750 http://togogenome.org/gene/10090:Gse1 ^@ http://purl.uniprot.org/uniprot/Q3U3C9 ^@ 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 ^@ Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Genetic suppressor element 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000262925|||http://purl.uniprot.org/annotation/VSP_021822|||http://purl.uniprot.org/annotation/VSP_021823|||http://purl.uniprot.org/annotation/VSP_021824 http://togogenome.org/gene/10090:Itgb7 ^@ http://purl.uniprot.org/uniprot/P26011 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||Integrin beta-7|||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_0000016353 http://togogenome.org/gene/10090:Tmem106c ^@ http://purl.uniprot.org/uniprot/Q80VP8 ^@ Chain|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||Removed|||Transmembrane protein 106C ^@ http://purl.uniprot.org/annotation/PRO_0000243901 http://togogenome.org/gene/10090:Lcor ^@ http://purl.uniprot.org/uniprot/A4FTY7|||http://purl.uniprot.org/uniprot/Q6ZPI3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH psq-type|||Interaction with nuclear receptors|||Ligand-dependent corepressor|||Nuclear localization signal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000236808 http://togogenome.org/gene/10090:Rims1 ^@ http://purl.uniprot.org/uniprot/Q99NE5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger ^@ Abolishes interaction with RAB3A.|||Basic and acidic residues|||C2 1|||C2 2|||Disordered|||FYVE-type|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 7.|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||RabBD|||Regulating synaptic membrane exocytosis protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000190199|||http://purl.uniprot.org/annotation/VSP_022230|||http://purl.uniprot.org/annotation/VSP_022231|||http://purl.uniprot.org/annotation/VSP_022232|||http://purl.uniprot.org/annotation/VSP_022233|||http://purl.uniprot.org/annotation/VSP_022234|||http://purl.uniprot.org/annotation/VSP_022235|||http://purl.uniprot.org/annotation/VSP_022236|||http://purl.uniprot.org/annotation/VSP_022237|||http://purl.uniprot.org/annotation/VSP_022238 http://togogenome.org/gene/10090:Zbtb39 ^@ http://purl.uniprot.org/uniprot/Q6PDK0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BTB|||C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Cercam ^@ http://purl.uniprot.org/uniprot/A3KGW5|||http://purl.uniprot.org/uniprot/B2RSF7 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Signal Peptide ^@ Disordered|||Inactive glycosyltransferase 25 family member 3|||N-linked (GlcNAc...) asparagine|||Polar residues|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000309545|||http://purl.uniprot.org/annotation/PRO_5015087149 http://togogenome.org/gene/10090:Dhrs7c ^@ http://purl.uniprot.org/uniprot/Q8CHS7 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Signal Peptide ^@ Dehydrogenase/reductase SDR family member 7C|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000333756 http://togogenome.org/gene/10090:Zcchc14 ^@ http://purl.uniprot.org/uniprot/A2RTC2|||http://purl.uniprot.org/uniprot/Q8VIG0 ^@ 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 ^@ Basic and acidic residues|||CCHC-type|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Zinc finger CCHC domain-containing protein 14 ^@ http://purl.uniprot.org/annotation/PRO_0000150976|||http://purl.uniprot.org/annotation/VSP_013844|||http://purl.uniprot.org/annotation/VSP_013845 http://togogenome.org/gene/10090:Srrm3 ^@ http://purl.uniprot.org/uniprot/H7BWX3|||http://purl.uniprot.org/uniprot/Q80WV7 ^@ 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|||Basic residues|||CWF21|||Disordered|||In isoform 2.|||Polar residues|||Serine/arginine repetitive matrix protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000341376|||http://purl.uniprot.org/annotation/VSP_034270|||http://purl.uniprot.org/annotation/VSP_034271 http://togogenome.org/gene/10090:Lyar ^@ http://purl.uniprot.org/uniprot/Q08288 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||C2HC LYAR-type 1|||C2HC LYAR-type 2|||Cell growth-regulating nucleolar protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084529 http://togogenome.org/gene/10090:Uckl1 ^@ http://purl.uniprot.org/uniprot/Q91YL3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Polar residues|||Uridine-cytidine kinase-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000164461 http://togogenome.org/gene/10090:Nbr1 ^@ http://purl.uniprot.org/uniprot/A1L329|||http://purl.uniprot.org/uniprot/A2A4N5|||http://purl.uniprot.org/uniprot/A2A4N8|||http://purl.uniprot.org/uniprot/P97432|||http://purl.uniprot.org/uniprot/Q05BC8|||http://purl.uniprot.org/uniprot/Q6ZQK3 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ ATG8 family proteins-binding|||Basic and acidic residues|||Disordered|||Next to BRCA1 gene 1 protein|||PB1|||Phosphoserine|||Phosphothreonine|||Polar residues|||UBA|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000096747 http://togogenome.org/gene/10090:Cltc ^@ http://purl.uniprot.org/uniprot/Q68FD5 ^@ 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 ^@ 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 1|||Distal segment|||Flexible linker|||Globular terminal domain|||Heavy chain arm|||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_0000205779 http://togogenome.org/gene/10090:Atp1b2 ^@ http://purl.uniprot.org/uniprot/P14231|||http://purl.uniprot.org/uniprot/Q3UR55 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||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_0000219105 http://togogenome.org/gene/10090:Srsf6 ^@ http://purl.uniprot.org/uniprot/Q3TWW8 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by DYRK1A|||RRM 1|||RRM 2|||Serine/arginine-rich splicing factor 6 ^@ http://purl.uniprot.org/annotation/PRO_0000426095 http://togogenome.org/gene/10090:Ermn ^@ http://purl.uniprot.org/uniprot/Q5EBJ4 ^@ 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|||Basic and acidic residues|||Binds actin|||Disordered|||Ermin|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314749 http://togogenome.org/gene/10090:Igsf9b ^@ http://purl.uniprot.org/uniprot/A0A1L1SR84 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Fibronectin type-III|||Helical|||Ig-like|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5009681974 http://togogenome.org/gene/10090:Fev ^@ http://purl.uniprot.org/uniprot/E0CXR7|||http://purl.uniprot.org/uniprot/Q8QZW2 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Region ^@ ETS|||May mediate active transcriptional repression|||Protein FEV ^@ http://purl.uniprot.org/annotation/PRO_0000344205 http://togogenome.org/gene/10090:Exosc8 ^@ http://purl.uniprot.org/uniprot/Q546F8|||http://purl.uniprot.org/uniprot/Q571G2|||http://purl.uniprot.org/uniprot/Q9D753 ^@ 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 ^@ Exoribonuclease phosphorolytic|||Exosome complex component RRP43|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000139968 http://togogenome.org/gene/10090:Gm8369 ^@ http://purl.uniprot.org/uniprot/E9PZI3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Sec23ip ^@ http://purl.uniprot.org/uniprot/A0AUN0|||http://purl.uniprot.org/uniprot/G3X928 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ DDHD|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Or5af1 ^@ http://purl.uniprot.org/uniprot/Q7TRZ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gpt ^@ http://purl.uniprot.org/uniprot/Q566C3|||http://purl.uniprot.org/uniprot/Q8QZR5 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Alanine aminotransferase 1|||Aminotransferase class I/classII|||N-acetylalanine|||N6-(pyridoxal phosphate)lysine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000123934 http://togogenome.org/gene/10090:Catsperd ^@ http://purl.uniprot.org/uniprot/E9Q9F6 ^@ 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 ^@ Cation channel sperm-associated auxiliary subunit delta|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000416884|||http://purl.uniprot.org/annotation/VSP_042980|||http://purl.uniprot.org/annotation/VSP_042981|||http://purl.uniprot.org/annotation/VSP_042982 http://togogenome.org/gene/10090:Tom1l1 ^@ http://purl.uniprot.org/uniprot/Q8BZR6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||GAT|||Polar residues|||VHS ^@ http://togogenome.org/gene/10090:Or2h1 ^@ http://purl.uniprot.org/uniprot/Q7TRL3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gfm1 ^@ http://purl.uniprot.org/uniprot/Q8K0D5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Elongation factor G, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000007441 http://togogenome.org/gene/10090:Dgkz ^@ http://purl.uniprot.org/uniprot/A0A668KL90|||http://purl.uniprot.org/uniprot/A2AHJ7|||http://purl.uniprot.org/uniprot/A2AHK0|||http://purl.uniprot.org/uniprot/Q80UP3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ ANK|||ANK 1|||ANK 2|||Basic and acidic residues|||DAGKc|||Diacylglycerol kinase zeta|||Disordered|||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_0000218469 http://togogenome.org/gene/10090:Brinp1 ^@ http://purl.uniprot.org/uniprot/Q920P3 ^@ 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 1|||In isoform 2.|||MACPF|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000045767|||http://purl.uniprot.org/annotation/VSP_017024|||http://purl.uniprot.org/annotation/VSP_017025 http://togogenome.org/gene/10090:Arhgef39 ^@ http://purl.uniprot.org/uniprot/Q66JY6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ DH|||In isoform 2.|||PH|||Rho guanine nucleotide exchange factor 39 ^@ http://purl.uniprot.org/annotation/PRO_0000291865|||http://purl.uniprot.org/annotation/VSP_026287 http://togogenome.org/gene/10090:Fcer1a ^@ http://purl.uniprot.org/uniprot/P20489 ^@ 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|||Sequence Conflict|||Signal Peptide|||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_0000015162 http://togogenome.org/gene/10090:Ly6g6e ^@ http://purl.uniprot.org/uniprot/Q8K1T6 ^@ 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.|||Lymphocyte antigen 6G6e|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_5010146328|||http://purl.uniprot.org/annotation/VSP_059015 http://togogenome.org/gene/10090:Gm10220 ^@ http://purl.uniprot.org/uniprot/K7N660 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cmc4 ^@ http://purl.uniprot.org/uniprot/A3KGA5|||http://purl.uniprot.org/uniprot/Q61908 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Domain Extent|||Motif ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||Cx9C motif-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000096615 http://togogenome.org/gene/10090:Vmn1r184 ^@ http://purl.uniprot.org/uniprot/E9Q2N4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pmvk ^@ http://purl.uniprot.org/uniprot/Q3THA3|||http://purl.uniprot.org/uniprot/Q9D1G2 ^@ 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.|||Phosphomevalonate kinase ^@ http://purl.uniprot.org/annotation/PRO_0000058473|||http://purl.uniprot.org/annotation/VSP_007649|||http://purl.uniprot.org/annotation/VSP_007650|||http://purl.uniprot.org/annotation/VSP_007651 http://togogenome.org/gene/10090:Mapre3 ^@ http://purl.uniprot.org/uniprot/D3Z6G3|||http://purl.uniprot.org/uniprot/Q2UZW7|||http://purl.uniprot.org/uniprot/Q6PER3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ APC-binding|||Acidic residues|||Calponin-homology (CH)|||DCTN1-binding|||Disordered|||EB1 C-terminal|||Microtubule-associated protein RP/EB family member 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000213429 http://togogenome.org/gene/10090:Or55b10 ^@ http://purl.uniprot.org/uniprot/Q9WU94 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r259 ^@ http://purl.uniprot.org/uniprot/D3YTX5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mtx1 ^@ http://purl.uniprot.org/uniprot/A0A6I8MWZ8|||http://purl.uniprot.org/uniprot/Q8R5C0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Metaxin glutathione S-transferase|||Mitochondrial outer membrane transport complex Sam37/metaxin N-terminal ^@ http://togogenome.org/gene/10090:Alx4 ^@ http://purl.uniprot.org/uniprot/O35137 ^@ 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 ^@ Disordered|||Homeobox|||Homeobox protein aristaless-like 4|||In lst; abolishes DNA binding and transcriptional activation.|||OAR|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000048815 http://togogenome.org/gene/10090:Slc39a14 ^@ http://purl.uniprot.org/uniprot/Q75N73 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||HHHGHXHX-motif|||Helical|||In isoform 2.|||Metal cation symporter ZIP14|||N-linked (GlcNAc...) asparagine|||When overexpressed ubiquitously in conditional knockin mice, perinatally lethal; when overexpressed in osteoblasts in conditional knockin mice, produces a severe skeletal phenotype marked by a drastic increase in cortical thickness due to an enhanced endosteal bone formation; when overexpressed in osteoclasts in conditional knockin mice, no effect on bone hemostasis.|||XEXPHE-motif ^@ http://purl.uniprot.org/annotation/PRO_0000312195|||http://purl.uniprot.org/annotation/VSP_060552 http://togogenome.org/gene/10090:Abcc10 ^@ http://purl.uniprot.org/uniprot/Q8R4P9 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||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|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000253577|||http://purl.uniprot.org/annotation/VSP_021081|||http://purl.uniprot.org/annotation/VSP_021082|||http://purl.uniprot.org/annotation/VSP_021083 http://togogenome.org/gene/10090:Mc3r ^@ http://purl.uniprot.org/uniprot/P33033|||http://purl.uniprot.org/uniprot/Q544G7 ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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|||Melanocortin receptor 3|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069719 http://togogenome.org/gene/10090:Brsk2 ^@ http://purl.uniprot.org/uniprot/G3FEZ6|||http://purl.uniprot.org/uniprot/Q69Z98 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KEN box|||Loss of kinase activity.|||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_0000274036|||http://purl.uniprot.org/annotation/VSP_022605|||http://purl.uniprot.org/annotation/VSP_022606|||http://purl.uniprot.org/annotation/VSP_022607|||http://purl.uniprot.org/annotation/VSP_022608 http://togogenome.org/gene/10090:Gtf2ird1 ^@ http://purl.uniprot.org/uniprot/Q5XJY7|||http://purl.uniprot.org/uniprot/Q6PD35|||http://purl.uniprot.org/uniprot/Q8BP10|||http://purl.uniprot.org/uniprot/Q9JI57 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||GTF2I-like 1|||GTF2I-like 2|||GTF2I-like 3|||GTF2I-like 4|||GTF2I-like 5|||GTF2I-like 6|||General transcription factor II-I repeat domain-containing protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1, isoform 3, isoform 7, isoform 9 and isoform 10.|||In isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 3, isoform 4, isoform 8 and isoform 10.|||In isoform 6 and isoform 7.|||In isoform 9.|||Nuclear localization signal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000083871|||http://purl.uniprot.org/annotation/VSP_003874|||http://purl.uniprot.org/annotation/VSP_003875|||http://purl.uniprot.org/annotation/VSP_003876|||http://purl.uniprot.org/annotation/VSP_021376|||http://purl.uniprot.org/annotation/VSP_021377 http://togogenome.org/gene/10090:Dtx3 ^@ http://purl.uniprot.org/uniprot/E9Q3J1|||http://purl.uniprot.org/uniprot/Q80V91 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Disordered|||Pro residues|||Probable E3 ubiquitin-protein ligase DTX3|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000219086 http://togogenome.org/gene/10090:Zfp663 ^@ http://purl.uniprot.org/uniprot/Q6NXM6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Arid3a ^@ http://purl.uniprot.org/uniprot/A0A0R4J1A7|||http://purl.uniprot.org/uniprot/Q62431 ^@ 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 ^@ ARID|||AT-rich interactive domain-containing protein 3A|||Abolishes cytosolic localization.|||Abolishes nuclear localization.|||Acidic|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homodimerization|||Impairs DNA-binding.|||Important for cytoplasmic localization|||Important for nuclear localization|||No effect on cellular location.|||Phosphoserine|||Phosphothreonine|||Polar residues|||REKLES ^@ http://purl.uniprot.org/annotation/PRO_0000200579 http://togogenome.org/gene/10090:Syce2 ^@ http://purl.uniprot.org/uniprot/E9PYH4|||http://purl.uniprot.org/uniprot/Q505B8 ^@ 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|||Disordered|||In isoform 2.|||Polar residues|||Synaptonemal complex central element protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000262563|||http://purl.uniprot.org/annotation/VSP_021788 http://togogenome.org/gene/10090:Mtx2 ^@ http://purl.uniprot.org/uniprot/O88441|||http://purl.uniprot.org/uniprot/Q8C454 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Metaxin glutathione S-transferase|||Metaxin-2|||Mitochondrial outer membrane transport complex Sam37/metaxin N-terminal|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000220996 http://togogenome.org/gene/10090:Sema3e ^@ http://purl.uniprot.org/uniprot/P70275 ^@ 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 ^@ Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3E ^@ http://purl.uniprot.org/annotation/PRO_0000032318 http://togogenome.org/gene/10090:Hddc3 ^@ http://purl.uniprot.org/uniprot/Q9D114 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1|||HD|||N-acetylglycine|||N6-acetyllysine|||Nucleophile|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000263111 http://togogenome.org/gene/10090:Hamp2 ^@ http://purl.uniprot.org/uniprot/Q80T19 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Signal Peptide ^@ Hepcidin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000013397|||http://purl.uniprot.org/annotation/PRO_0000013398 http://togogenome.org/gene/10090:Izumo1 ^@ http://purl.uniprot.org/uniprot/Q9D9J7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||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|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes adhesion to oocytes.|||Almost no change in fusion-facilitating activity.|||Cytoplasmic|||Decreases adhesion to oocytes.|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Important for interaction with IZUMO1R|||Izumo sperm-egg fusion protein 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Strongly decreases adhesion to oocytes. ^@ http://purl.uniprot.org/annotation/PRO_0000045483 http://togogenome.org/gene/10090:Fbxw2 ^@ http://purl.uniprot.org/uniprot/A2AUF9|||http://purl.uniprot.org/uniprot/Q8BS25|||http://purl.uniprot.org/uniprot/Q8CCH8|||http://purl.uniprot.org/uniprot/Q9CPQ6|||http://purl.uniprot.org/uniprot/Q9QUH1 ^@ Domain Extent|||Region|||Repeat ^@ Domain Extent|||Repeat ^@ F-box|||WD ^@ http://togogenome.org/gene/10090:Primpol ^@ http://purl.uniprot.org/uniprot/Q6P1E7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ DNA-directed primase/polymerase protein|||Disordered|||In isoform 2.|||Interaction with RPA1|||Polar residues|||RPA1-binding motif 1|||RPA1-binding motif 2|||Zinc knuckle motif ^@ http://purl.uniprot.org/annotation/PRO_0000279396|||http://purl.uniprot.org/annotation/VSP_023420|||http://purl.uniprot.org/annotation/VSP_023421 http://togogenome.org/gene/10090:0610040J01Rik ^@ http://purl.uniprot.org/uniprot/Q99K99 ^@ 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|||Phosphothreonine|||Polar residues|||Uncharacterized protein C4orf19 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000286562 http://togogenome.org/gene/10090:Or8b1c ^@ http://purl.uniprot.org/uniprot/L7N1X5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fech ^@ http://purl.uniprot.org/uniprot/P22315|||http://purl.uniprot.org/uniprot/Q4QRK2 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide ^@ Disordered|||Ferrochelatase, mitochondrial|||In Fechm1Pas.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000008874 http://togogenome.org/gene/10090:Ptrh1 ^@ http://purl.uniprot.org/uniprot/Q8BW00 ^@ Chain|||Molecule Processing ^@ Chain ^@ Probable peptidyl-tRNA hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000240442 http://togogenome.org/gene/10090:Cd59b ^@ http://purl.uniprot.org/uniprot/P58019 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ CD59B glycoprotein|||GPI-anchor amidated asparagine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036114|||http://purl.uniprot.org/annotation/PRO_0000036115 http://togogenome.org/gene/10090:Inhca ^@ http://purl.uniprot.org/uniprot/Q9DBD0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Turn ^@ Confers ability to bind ferric iron and carbonate; when associated with R-143.|||Confers ability to bind ferric iron and carbonate; when associated with Y-207.|||Inhibitor of carbonic anhydrase|||N-linked (GlcNAc...) asparagine|||Transferrin-like 1|||Transferrin-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000415376 http://togogenome.org/gene/10090:Olah ^@ http://purl.uniprot.org/uniprot/Q8R197 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Chain|||Modified Residue ^@ N-acetylmethionine|||S-acyl fatty acid synthase thioesterase, medium chain ^@ http://purl.uniprot.org/annotation/PRO_0000180359 http://togogenome.org/gene/10090:Or51b4 ^@ http://purl.uniprot.org/uniprot/F8VQ01 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Taldo1 ^@ http://purl.uniprot.org/uniprot/Q93092 ^@ Active 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|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ In isoform 2.|||Leads to expression of isoform 1 only.|||Leads to expression of isoform 2 only.|||Mainly expressed in the cytoplasm; when associated with A-7 and A-10.|||Mainly expressed in the cytoplasm; when associated with A-7 and A-8.|||Mainly expressed in the cytoplasm; when associated with A-8 and A-10.|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Schiff-base intermediate with substrate|||Transaldolase ^@ http://purl.uniprot.org/annotation/PRO_0000173565|||http://purl.uniprot.org/annotation/VSP_061596 http://togogenome.org/gene/10090:Nol8 ^@ http://purl.uniprot.org/uniprot/E9QKD1|||http://purl.uniprot.org/uniprot/Q3UHX0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||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.|||Nucleolar protein 8|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000239444|||http://purl.uniprot.org/annotation/VSP_052057 http://togogenome.org/gene/10090:Crybg1 ^@ http://purl.uniprot.org/uniprot/E9PVP1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Beta/gamma crystallin 'Greek key'|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tgfb3 ^@ http://purl.uniprot.org/uniprot/Q3TRQ9|||http://purl.uniprot.org/uniprot/Q91YU7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Interchain|||TGF-beta family profile|||Transforming growth factor beta ^@ http://purl.uniprot.org/annotation/PRO_5015099512 http://togogenome.org/gene/10090:Vezf1 ^@ http://purl.uniprot.org/uniprot/Q5SXC4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ccn1 ^@ http://purl.uniprot.org/uniprot/P18406|||http://purl.uniprot.org/uniprot/Q3TX21 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Signal Peptide ^@ CCN family member 1|||CTCK|||Heparin-binding|||IGFBP N-terminal|||Phosphoserine|||Protein CYR61|||TSP type-1|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000014399|||http://purl.uniprot.org/annotation/PRO_5014309116 http://togogenome.org/gene/10090:Apol10b ^@ http://purl.uniprot.org/uniprot/G3X9K7 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Abhd8 ^@ http://purl.uniprot.org/uniprot/Q8R0P8 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ AB hydrolase-1|||Charge relay system|||Disordered|||Pro residues|||Protein ABHD8 ^@ http://purl.uniprot.org/annotation/PRO_0000281384 http://togogenome.org/gene/10090:Tex12 ^@ http://purl.uniprot.org/uniprot/Q9CR81 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Testis-expressed protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000072494 http://togogenome.org/gene/10090:Ech1 ^@ http://purl.uniprot.org/uniprot/O35459 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Site|||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_0000007418 http://togogenome.org/gene/10090:Ms4a5 ^@ http://purl.uniprot.org/uniprot/Q810P8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Gpr63 ^@ http://purl.uniprot.org/uniprot/Q9EQQ3 ^@ 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|||Probable G-protein coupled receptor 63 ^@ http://purl.uniprot.org/annotation/PRO_0000069582 http://togogenome.org/gene/10090:Gzmg ^@ http://purl.uniprot.org/uniprot/P13366|||http://purl.uniprot.org/uniprot/Q4KL28 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Granzyme G|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027411|||http://purl.uniprot.org/annotation/PRO_0000027412|||http://purl.uniprot.org/annotation/PRO_5014309381 http://togogenome.org/gene/10090:Axin1 ^@ http://purl.uniprot.org/uniprot/E9QMJ8|||http://purl.uniprot.org/uniprot/O35625|||http://purl.uniprot.org/uniprot/Q14DJ8 ^@ Chain|||Coiled-Coil|||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 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Abolishes binding of PIAS1 and PIAS2. Dramatically reduces sumoylation and abolishes AXIN1-mediated JNK activation. No effect on homodimerization nor on Wnt-signaling.|||Axin-1|||DIX|||Decreased sumoylation followed by increased ubiquitination; when associated with A-858.|||Decreased sumoylation followed by increased ubiquitination; when associated with A-861.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Greatly reduced GSK3B-mediated phosphorylation and large effect on the inhibitory activity in Wnt-signaling; when associated with A-480 and A-492.|||Greatly reduced GSK3B-mediated phosphorylation; when associated with A-480 and A-485.|||Greatly reduced GSK3B-mediated phosphorylation; when associated with A-485 and A-492.|||In isoform 2.|||Interaction with GSK3B|||Interaction with HIPK2|||Interaction with PPP2CA|||Interaction with RNF111|||Interaction with SIAH1|||Interaction with TP53|||Interaction with beta-catenin|||Little effect on inhibitory activity on Wnt-signaling.|||No effect on phosphorylation. Little effect on inhibitory activity on Wnt-signaling.|||Phosphoserine|||Phosphoserine; by CK1|||Phosphoserine; by GSK3-beta|||Phosphothreonine; by GSK3-beta|||Polar residues|||RGS|||Tankyrase-binding motif ^@ http://purl.uniprot.org/annotation/PRO_0000220889|||http://purl.uniprot.org/annotation/VSP_000452 http://togogenome.org/gene/10090:Or8d2 ^@ http://purl.uniprot.org/uniprot/Q7TRB8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gpatch3 ^@ http://purl.uniprot.org/uniprot/Q8BIY1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||G patch domain-containing protein 3|||G-patch ^@ http://purl.uniprot.org/annotation/PRO_0000087569 http://togogenome.org/gene/10090:Syt17 ^@ http://purl.uniprot.org/uniprot/Q920M7 ^@ 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 ^@ C2 1|||C2 2|||Disordered|||Phosphoserine|||Polar residues|||Synaptotagmin-17 ^@ http://purl.uniprot.org/annotation/PRO_0000311937 http://togogenome.org/gene/10090:Mptx1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J077|||http://purl.uniprot.org/uniprot/Q8R1M8 ^@ 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 ^@ Mucosal pentraxin|||N-linked (GlcNAc...) asparagine|||Pentraxin (PTX)|||Pentraxin family member ^@ http://purl.uniprot.org/annotation/PRO_0000342393|||http://purl.uniprot.org/annotation/PRO_5005967681 http://togogenome.org/gene/10090:Aldh1a2 ^@ http://purl.uniprot.org/uniprot/Q62148 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Site ^@ Nucleophile|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Retinal dehydrogenase 2|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000056423 http://togogenome.org/gene/10090:Rfc4 ^@ http://purl.uniprot.org/uniprot/Q99J62 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ N-acetylmethionine|||N6-acetyllysine|||Replication factor C subunit 4 ^@ http://purl.uniprot.org/annotation/PRO_0000244008 http://togogenome.org/gene/10090:Poglut2 ^@ http://purl.uniprot.org/uniprot/Q9JHP7 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Glycosylation Site|||Motif|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Filamin|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Protein O-glucosyltransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000247164|||http://purl.uniprot.org/annotation/VSP_019935|||http://purl.uniprot.org/annotation/VSP_019936 http://togogenome.org/gene/10090:Iqch ^@ http://purl.uniprot.org/uniprot/B2RUB3|||http://purl.uniprot.org/uniprot/Q9D2K4 ^@ 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|||IQ|||IQ domain-containing protein H|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000282566|||http://purl.uniprot.org/annotation/VSP_024197 http://togogenome.org/gene/10090:Fancb ^@ http://purl.uniprot.org/uniprot/Q5XJY6 ^@ Chain|||Molecule Processing ^@ Chain ^@ Fanconi anemia group B protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000087182 http://togogenome.org/gene/10090:Pudp ^@ http://purl.uniprot.org/uniprot/Q9D5U5 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Nucleophile|||Proton donor|||Pseudouridine-5'-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000320103 http://togogenome.org/gene/10090:Plod2 ^@ http://purl.uniprot.org/uniprot/E9Q718|||http://purl.uniprot.org/uniprot/Q9R0B9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Fe2OG dioxygenase|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Phosphothreonine|||Phosphotyrosine|||Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2|||procollagen-lysine 5-dioxygenase ^@ http://purl.uniprot.org/annotation/PRO_0000024684|||http://purl.uniprot.org/annotation/PRO_5003243100 http://togogenome.org/gene/10090:Plekhf2 ^@ http://purl.uniprot.org/uniprot/Q91WB4 ^@ 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_0000251601 http://togogenome.org/gene/10090:Rgs17 ^@ http://purl.uniprot.org/uniprot/G5E8E0|||http://purl.uniprot.org/uniprot/Q8BR34|||http://purl.uniprot.org/uniprot/Q9QZB0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Phosphotyrosine|||Polar residues|||RGS|||Regulator of G-protein signaling 17 ^@ http://purl.uniprot.org/annotation/PRO_0000204225 http://togogenome.org/gene/10090:Or52e2 ^@ http://purl.uniprot.org/uniprot/Q8VGV8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Klf16 ^@ http://purl.uniprot.org/uniprot/B2RPU7|||http://purl.uniprot.org/uniprot/P58334 ^@ 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 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 16|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000047159 http://togogenome.org/gene/10090:Cdk5rap1 ^@ http://purl.uniprot.org/uniprot/Q8BTW8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||MTTase N-terminal|||Mitochondrial tRNA methylthiotransferase CDK5RAP1|||Mitochondrion|||Radical SAM core|||TRAM ^@ http://purl.uniprot.org/annotation/PRO_0000141765 http://togogenome.org/gene/10090:Zfp998 ^@ http://purl.uniprot.org/uniprot/K7N769|||http://purl.uniprot.org/uniprot/Q8C1L2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Esyt2 ^@ http://purl.uniprot.org/uniprot/Q3TZZ7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ C2 1|||C2 2|||C2 3|||Cytoplasmic|||Disordered|||Extended synaptotagmin-2|||Helical|||In isoform 2.|||Lumenal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane|||SMP-LTD ^@ http://purl.uniprot.org/annotation/PRO_0000278259|||http://purl.uniprot.org/annotation/VSP_023243 http://togogenome.org/gene/10090:Prim1 ^@ http://purl.uniprot.org/uniprot/P20664 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict ^@ DNA primase small subunit|||N-acetylmethionine|||Zinc knuckle motif ^@ http://purl.uniprot.org/annotation/PRO_0000046731 http://togogenome.org/gene/10090:Wdfy3 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLV7|||http://purl.uniprot.org/uniprot/G3UYW1|||http://purl.uniprot.org/uniprot/Q6VNB8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Splice Variant|||Zinc Finger ^@ BEACH|||BEACH-type PH|||Basic and acidic residues|||Disordered|||FYVE-type|||In isoform 2.|||Interaction with ATG5|||Interaction with SQSTM1|||LIR|||Phosphoserine|||Polar residues|||Sufficient for translocalization to p62 bodies/ALIS|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat and FYVE domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000242694|||http://purl.uniprot.org/annotation/VSP_019477|||http://purl.uniprot.org/annotation/VSP_019478 http://togogenome.org/gene/10090:Cpeb3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J102|||http://purl.uniprot.org/uniprot/D3Z1R6|||http://purl.uniprot.org/uniprot/Q7TN99 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Abolishes phosphorylation by PKA.|||Asymmetric dimethylarginine|||Cleavage; by CAPN2|||Cytoplasmic polyadenylation element-binding protein 3|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Polar residues|||Pro residues|||RRM|||RRM 1|||RRM 2|||Reduces phosphorylation by PKA.|||Required for RNA-binding activity ^@ http://purl.uniprot.org/annotation/PRO_0000269262|||http://purl.uniprot.org/annotation/VSP_022036|||http://purl.uniprot.org/annotation/VSP_022037|||http://purl.uniprot.org/annotation/VSP_022038|||http://purl.uniprot.org/annotation/VSP_022039|||http://purl.uniprot.org/annotation/VSP_058565 http://togogenome.org/gene/10090:Zfp53 ^@ http://purl.uniprot.org/uniprot/Q9Z117 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Ttc21a ^@ http://purl.uniprot.org/uniprot/Q8C0S4 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||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_0000291916|||http://purl.uniprot.org/annotation/VSP_026304|||http://purl.uniprot.org/annotation/VSP_026305 http://togogenome.org/gene/10090:Or5b118 ^@ http://purl.uniprot.org/uniprot/Q7TQQ8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Galnt15 ^@ http://purl.uniprot.org/uniprot/Q9D2N8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Acidic residues|||Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 15|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059138 http://togogenome.org/gene/10090:Kdm2a ^@ http://purl.uniprot.org/uniprot/F6YRW4|||http://purl.uniprot.org/uniprot/P59997 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||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|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ ADP-ribosylarginine|||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.|||JmjC|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Lysine-specific demethylase 2A|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000119856|||http://purl.uniprot.org/annotation/VSP_017471|||http://purl.uniprot.org/annotation/VSP_017472|||http://purl.uniprot.org/annotation/VSP_017473|||http://purl.uniprot.org/annotation/VSP_017474 http://togogenome.org/gene/10090:Lrp2bp ^@ http://purl.uniprot.org/uniprot/Q9D4C6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||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_0000315709|||http://purl.uniprot.org/annotation/VSP_030665 http://togogenome.org/gene/10090:Vmn1r119 ^@ http://purl.uniprot.org/uniprot/E9Q4H3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nadk2 ^@ http://purl.uniprot.org/uniprot/Q8C5H8|||http://purl.uniprot.org/uniprot/Q9CUB4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||NAD kinase 2, mitochondrial|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000296293|||http://purl.uniprot.org/annotation/VSP_027194|||http://purl.uniprot.org/annotation/VSP_027195|||http://purl.uniprot.org/annotation/VSP_027196 http://togogenome.org/gene/10090:Cd4 ^@ http://purl.uniprot.org/uniprot/P06332|||http://purl.uniprot.org/uniprot/Q3TSV7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||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|||Phosphoserine|||S-palmitoyl cysteine|||T-cell surface glycoprotein CD4 ^@ http://purl.uniprot.org/annotation/PRO_0000014627|||http://purl.uniprot.org/annotation/PRO_5014309121|||http://purl.uniprot.org/annotation/VSP_002489 http://togogenome.org/gene/10090:Slc25a28 ^@ http://purl.uniprot.org/uniprot/Q8R0Z5 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Region|||Repeat|||Sequence Conflict|||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.|||Mitoferrin-2|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000235256|||http://purl.uniprot.org/annotation/VSP_018416 http://togogenome.org/gene/10090:Dnajc14 ^@ http://purl.uniprot.org/uniprot/Q921R4 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Disordered|||DnaJ homolog subfamily C member 14|||Helical|||In strain: Czech II.|||J|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000247494 http://togogenome.org/gene/10090:P4ha2 ^@ http://purl.uniprot.org/uniprot/Q3UQ81|||http://purl.uniprot.org/uniprot/Q5SX74|||http://purl.uniprot.org/uniprot/Q5SX75|||http://purl.uniprot.org/uniprot/Q60716 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Repeat|||Signal Peptide|||Splice Variant ^@ Fe2OG dioxygenase|||In isoform IIa.|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Prolyl 4-hydroxylase subunit alpha-2|||TPR|||procollagen-proline 4-dioxygenase ^@ http://purl.uniprot.org/annotation/PRO_0000022727|||http://purl.uniprot.org/annotation/PRO_5004262714|||http://purl.uniprot.org/annotation/PRO_5015098024|||http://purl.uniprot.org/annotation/VSP_004507 http://togogenome.org/gene/10090:Mgat4b ^@ http://purl.uniprot.org/uniprot/Q812F8 ^@ Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000288594 http://togogenome.org/gene/10090:Sf3b5 ^@ http://purl.uniprot.org/uniprot/Q923D4 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Site ^@ 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_0000220758 http://togogenome.org/gene/10090:Potefam3d ^@ http://purl.uniprot.org/uniprot/A0A0J9YUH2 ^@ Region|||Repeat ^@ Region|||Repeat ^@ ANK|||Disordered ^@ http://togogenome.org/gene/10090:Scel ^@ http://purl.uniprot.org/uniprot/Q14DU0|||http://purl.uniprot.org/uniprot/Q9EQG3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ 1|||10|||11|||12|||13|||14|||15|||15 X approximate tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||LIM zinc-binding|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||Sciellin ^@ http://purl.uniprot.org/annotation/PRO_0000075904 http://togogenome.org/gene/10090:Zfp446 ^@ http://purl.uniprot.org/uniprot/E9Q6F9|||http://purl.uniprot.org/uniprot/Q149D4|||http://purl.uniprot.org/uniprot/Q8C9M8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||SCAN box ^@ http://togogenome.org/gene/10090:Haspin ^@ http://purl.uniprot.org/uniprot/A0A0R4J0P2|||http://purl.uniprot.org/uniprot/Q9Z0R0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase haspin ^@ http://purl.uniprot.org/annotation/PRO_0000085990 http://togogenome.org/gene/10090:Stx1a ^@ http://purl.uniprot.org/uniprot/O35526|||http://purl.uniprot.org/uniprot/Q497P1|||http://purl.uniprot.org/uniprot/Q5D0A4 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||Helical; Anchor for type IV membrane protein|||Phosphoserine|||Phosphoserine; by DAPK1|||Syntaxin-1A|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000210187 http://togogenome.org/gene/10090:Gli1 ^@ http://purl.uniprot.org/uniprot/P47806 ^@ 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 ^@ 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)|||Interaction with DNA|||Interaction with SUFU|||N6-acetyllysine|||Polar residues|||Pro residues|||Zinc finger protein GLI1 ^@ http://purl.uniprot.org/annotation/PRO_0000047198 http://togogenome.org/gene/10090:Araf ^@ http://purl.uniprot.org/uniprot/P04627|||http://purl.uniprot.org/uniprot/Q8CAD1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||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_0000085623 http://togogenome.org/gene/10090:Car2 ^@ http://purl.uniprot.org/uniprot/P00920 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase 2|||N-acetylserine|||Phosphoserine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000077419 http://togogenome.org/gene/10090:Marchf6 ^@ http://purl.uniprot.org/uniprot/Q6ZQ89 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ 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_0000274299|||http://purl.uniprot.org/annotation/VSP_022702|||http://purl.uniprot.org/annotation/VSP_022703|||http://purl.uniprot.org/annotation/VSP_022704 http://togogenome.org/gene/10090:Bbs7 ^@ http://purl.uniprot.org/uniprot/Q8K2G4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ Bardet-Biedl syndrome 7 protein homolog|||In isoform 2.|||In isoform 3.|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000064847|||http://purl.uniprot.org/annotation/VSP_008851|||http://purl.uniprot.org/annotation/VSP_008852|||http://purl.uniprot.org/annotation/VSP_008853 http://togogenome.org/gene/10090:Sult2a6 ^@ http://purl.uniprot.org/uniprot/B2RVI8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Kctd19 ^@ http://purl.uniprot.org/uniprot/Q562E2 ^@ 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 ^@ BTB 1|||BTB 2|||BTB/POZ domain-containing protein KCTD19|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000313588|||http://purl.uniprot.org/annotation/VSP_030044 http://togogenome.org/gene/10090:Ttll11 ^@ http://purl.uniprot.org/uniprot/A4Q9F4 ^@ 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|||Site|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Essential for specifying alpha-elongation versus initiation step of the polyglutamylase activity|||In isoform 2 and isoform 3.|||In isoform 3.|||Polar residues|||TTL|||Tubulin polyglutamylase TTLL11|||c-MTBD region ^@ http://purl.uniprot.org/annotation/PRO_0000326165|||http://purl.uniprot.org/annotation/VSP_052718|||http://purl.uniprot.org/annotation/VSP_052719 http://togogenome.org/gene/10090:Psd ^@ http://purl.uniprot.org/uniprot/Q5DTT2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||PH|||PH and SEC7 domain-containing protein 1|||Phosphoserine|||Polar residues|||Pro residues|||SEC7|||Significantly impaired guanine nucleotide exchange factor activity on ARF6 in PC12 cells. ^@ http://purl.uniprot.org/annotation/PRO_0000334161|||http://purl.uniprot.org/annotation/VSP_033637|||http://purl.uniprot.org/annotation/VSP_033638|||http://purl.uniprot.org/annotation/VSP_041569 http://togogenome.org/gene/10090:Ripk2 ^@ http://purl.uniprot.org/uniprot/P58801|||http://purl.uniprot.org/uniprot/Q547H1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolishes protein-kinase activity. Does not affect ubiquitination by PELI3.|||Activation segment (AS)|||CARD|||Disordered|||Does not prevent polyubiquitination by PELI3.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helix alphaC|||Mimics phosphorylation; does not promote stabilization of RIPK2.|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by autocatalysis|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Receptor-interacting serine/threonine-protein kinase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000086609 http://togogenome.org/gene/10090:Pcca ^@ http://purl.uniprot.org/uniprot/Q3UGC8|||http://purl.uniprot.org/uniprot/Q91ZA3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ ATP-grasp|||Biotin carboxylation|||Biotinyl-binding|||Lipoyl-binding|||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_0000002838 http://togogenome.org/gene/10090:Cdnf ^@ http://purl.uniprot.org/uniprot/Q8CC36 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Cerebral dopamine neurotrophic factor ^@ http://purl.uniprot.org/annotation/PRO_0000281138 http://togogenome.org/gene/10090:Fbxl12 ^@ http://purl.uniprot.org/uniprot/Q9EPX5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ F-box|||F-box/LRR-repeat protein 12|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8 ^@ http://purl.uniprot.org/annotation/PRO_0000119858 http://togogenome.org/gene/10090:Il1rapl2 ^@ http://purl.uniprot.org/uniprot/Q0VBP3|||http://purl.uniprot.org/uniprot/Q9ERS6 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||TIR|||X-linked interleukin-1 receptor accessory protein-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000015460|||http://purl.uniprot.org/annotation/PRO_5014306832|||http://purl.uniprot.org/annotation/VSP_008056|||http://purl.uniprot.org/annotation/VSP_008057 http://togogenome.org/gene/10090:Tmem87a ^@ http://purl.uniprot.org/uniprot/A2AQJ5|||http://purl.uniprot.org/uniprot/A2AQJ6|||http://purl.uniprot.org/uniprot/Q8BXN9 ^@ 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 and isoform 3.|||In isoform 3.|||Increased mechanosensitive channel activity in Tmem87a-expressing cells; when associated with G-292.|||Increased mechanosensitive channel activity in Tmem87a-expressing cells; when associated with L-271.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Transmembrane protein 87A ^@ http://purl.uniprot.org/annotation/PRO_0000270752|||http://purl.uniprot.org/annotation/VSP_022210|||http://purl.uniprot.org/annotation/VSP_022211|||http://purl.uniprot.org/annotation/VSP_022212 http://togogenome.org/gene/10090:Rpl22l1 ^@ http://purl.uniprot.org/uniprot/Q9D7S7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ In isoform 2.|||Phosphoserine|||Ribosomal protein eL22-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000240633|||http://purl.uniprot.org/annotation/VSP_019380 http://togogenome.org/gene/10090:Rab5if ^@ http://purl.uniprot.org/uniprot/Q9CQT9 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||GEL complex subunit OPTI|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000079416 http://togogenome.org/gene/10090:Shf ^@ http://purl.uniprot.org/uniprot/Q8CG80 ^@ 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.|||Phosphoserine|||Phosphotyrosine|||SH2|||SH2 domain-containing adapter protein F ^@ http://purl.uniprot.org/annotation/PRO_0000322559|||http://purl.uniprot.org/annotation/VSP_052700 http://togogenome.org/gene/10090:Ehd4 ^@ http://purl.uniprot.org/uniprot/Q3TM70|||http://purl.uniprot.org/uniprot/Q9EQP2 ^@ 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|||Region|||Strand|||Turn ^@ Disordered|||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_0000146115 http://togogenome.org/gene/10090:Kctd7 ^@ http://purl.uniprot.org/uniprot/Q8BJK1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ BTB|||BTB/POZ domain-containing protein KCTD7|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000251474 http://togogenome.org/gene/10090:Gm14305 ^@ http://purl.uniprot.org/uniprot/A2BE23 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Nptxr ^@ http://purl.uniprot.org/uniprot/A0A9R1SP20 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ntsr2 ^@ http://purl.uniprot.org/uniprot/P70310 ^@ Chain|||Disulfide Bond|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||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|||Neurotensin receptor type 2|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069950 http://togogenome.org/gene/10090:Pate14 ^@ http://purl.uniprot.org/uniprot/Q3UN54 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prostate and testis expressed protein 14|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000238926 http://togogenome.org/gene/10090:9430015G10Rik ^@ http://purl.uniprot.org/uniprot/A2ASP7 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015086034 http://togogenome.org/gene/10090:Tceal8 ^@ http://purl.uniprot.org/uniprot/Q9CZY2 ^@ 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|||Transcription elongation factor A protein-like 8 ^@ http://purl.uniprot.org/annotation/PRO_0000239217 http://togogenome.org/gene/10090:Fndc4 ^@ http://purl.uniprot.org/uniprot/B9EI95|||http://purl.uniprot.org/uniprot/Q3TR08 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||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_0000271380 http://togogenome.org/gene/10090:St6galnac1 ^@ http://purl.uniprot.org/uniprot/Q9QZ39 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Knockin mice display compromised mucus barriers, dysbiosis with reduced bacterial diversity, as well as susceptibility to intestinal inflammation.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149270 http://togogenome.org/gene/10090:Crb2 ^@ http://purl.uniprot.org/uniprot/Q80YA8 ^@ 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|||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|||Extracellular|||Helical|||Interaction with EPB41L5|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||N-linked (GlcNAc...) asparagine|||O-linked (Glc...) serine|||Protein crumbs homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000055626 http://togogenome.org/gene/10090:Or10a3m ^@ http://purl.uniprot.org/uniprot/Q8VFZ4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Acsf2 ^@ http://purl.uniprot.org/uniprot/Q8VCW8 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Medium-chain acyl-CoA ligase ACSF2, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000315795 http://togogenome.org/gene/10090:Adam6b ^@ http://purl.uniprot.org/uniprot/Q6IMH7 ^@ Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Disulfide Bond|||Domain Extent|||Transmembrane ^@ Disintegrin|||EGF-like|||Helical|||Peptidase M12B ^@ http://togogenome.org/gene/10090:Pdzrn4 ^@ http://purl.uniprot.org/uniprot/B9EKP7|||http://purl.uniprot.org/uniprot/E9PUZ9|||http://purl.uniprot.org/uniprot/E9Q5P6|||http://purl.uniprot.org/uniprot/Q3UXJ7|||http://purl.uniprot.org/uniprot/Q69Z24 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||PDZ|||Polar residues|||RING-type ^@ http://togogenome.org/gene/10090:Gins3 ^@ http://purl.uniprot.org/uniprot/Q9CY94 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ DNA replication complex GINS protein PSF3|||Not essential for folding and stability of GINS complex, but may regulate accessibility to the central complex pore ^@ http://purl.uniprot.org/annotation/PRO_0000327616 http://togogenome.org/gene/10090:Or1j19 ^@ http://purl.uniprot.org/uniprot/Q8VGK3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trmt1 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZW7|||http://purl.uniprot.org/uniprot/E9PWD4|||http://purl.uniprot.org/uniprot/Q3TX08 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ C3H1-type|||Disordered|||Phosphoserine|||Trm1 methyltransferase|||tRNA (guanine(26)-N(2))-dimethyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000147672 http://togogenome.org/gene/10090:Or7d9 ^@ http://purl.uniprot.org/uniprot/E9PVX1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp987 ^@ http://purl.uniprot.org/uniprot/Q32P14 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Doc2a ^@ http://purl.uniprot.org/uniprot/Q7TNF0 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region ^@ C2 1|||C2 2|||Disordered|||Double C2-like domain-containing protein alpha|||Interaction with UNC13D|||Interaction with UNC13D and DYNLT1 ^@ http://purl.uniprot.org/annotation/PRO_0000079966 http://togogenome.org/gene/10090:Atoh7 ^@ http://purl.uniprot.org/uniprot/Q9Z2E5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Transcription factor Atoh7|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000292407 http://togogenome.org/gene/10090:Mief2 ^@ http://purl.uniprot.org/uniprot/Q5NCS9 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Helix|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Helical|||Mitochondrial dynamics protein MID49|||Mitochondrial intermembrane ^@ http://purl.uniprot.org/annotation/PRO_0000310446 http://togogenome.org/gene/10090:Gm6760 ^@ http://purl.uniprot.org/uniprot/Q0ZNK3 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Scn2b ^@ http://purl.uniprot.org/uniprot/Q1MXF8|||http://purl.uniprot.org/uniprot/Q56A07 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binds SCN2A|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Interchain; with alpha subunit|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium channel subunit beta-2 ^@ http://purl.uniprot.org/annotation/PRO_0000045177|||http://purl.uniprot.org/annotation/PRO_5009970192 http://togogenome.org/gene/10090:Gpr182 ^@ http://purl.uniprot.org/uniprot/G3X9R9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Atp6v0a1 ^@ http://purl.uniprot.org/uniprot/Q3TXT5|||http://purl.uniprot.org/uniprot/Q3TY98|||http://purl.uniprot.org/uniprot/Q9Z1G4 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform A1-I and isoform A1-III.|||In isoform A1-I.|||Phosphothreonine|||Phosphotyrosine|||V-type proton ATPase 116 kDa subunit a 1|||Vacuolar ^@ http://purl.uniprot.org/annotation/PRO_0000119212|||http://purl.uniprot.org/annotation/VSP_000342|||http://purl.uniprot.org/annotation/VSP_000343 http://togogenome.org/gene/10090:Znhit2 ^@ http://purl.uniprot.org/uniprot/Q9QY66 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||HIT-type|||N-acetylmethionine|||Phosphothreonine|||Zinc finger HIT domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000173549 http://togogenome.org/gene/10090:Tango6 ^@ http://purl.uniprot.org/uniprot/Q8C3S2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||HEAT 1|||HEAT 2|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Transport and Golgi organization protein 6 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000305060|||http://purl.uniprot.org/annotation/VSP_028206|||http://purl.uniprot.org/annotation/VSP_028207|||http://purl.uniprot.org/annotation/VSP_028208 http://togogenome.org/gene/10090:Nlrp4g ^@ http://purl.uniprot.org/uniprot/Q3UWL9|||http://purl.uniprot.org/uniprot/Q66JP4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ NACHT|||Pyrin ^@ http://togogenome.org/gene/10090:Vmn2r95 ^@ http://purl.uniprot.org/uniprot/A0A338P6T0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5016375678 http://togogenome.org/gene/10090:Smim19 ^@ http://purl.uniprot.org/uniprot/E9PUT6|||http://purl.uniprot.org/uniprot/Q80ZU4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Small integral membrane protein 19 ^@ http://purl.uniprot.org/annotation/PRO_0000264627 http://togogenome.org/gene/10090:Tomm20l ^@ http://purl.uniprot.org/uniprot/Q9D4V6 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Mitochondrial intermembrane|||TOMM20-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000317748 http://togogenome.org/gene/10090:Nipsnap1 ^@ http://purl.uniprot.org/uniprot/O55125|||http://purl.uniprot.org/uniprot/Q5SVF7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||NIPSNAP|||Phosphoserine|||Protein NipSnap homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000221147 http://togogenome.org/gene/10090:Triml2 ^@ http://purl.uniprot.org/uniprot/E9PW10 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ B30.2/SPRY|||Disordered ^@ http://togogenome.org/gene/10090:Ccl24 ^@ http://purl.uniprot.org/uniprot/Q3U0A4|||http://purl.uniprot.org/uniprot/Q9JKC0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ C-C motif chemokine|||C-C motif chemokine 24|||Chemokine interleukin-8-like|||Disordered|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000005233|||http://purl.uniprot.org/annotation/PRO_5014205825 http://togogenome.org/gene/10090:Clec2e ^@ http://purl.uniprot.org/uniprot/H7BWZ4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Heca ^@ http://purl.uniprot.org/uniprot/Q3V1N5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Headcase middle ^@ http://togogenome.org/gene/10090:AW209491 ^@ http://purl.uniprot.org/uniprot/Q91WD4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ UPF0415 protein C7orf25 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000279530 http://togogenome.org/gene/10090:Esp23 ^@ http://purl.uniprot.org/uniprot/A8R0V5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015086677 http://togogenome.org/gene/10090:Plekhh3 ^@ http://purl.uniprot.org/uniprot/Q8VCE9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||FERM|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||MyTH4|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family H member 3|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000311109|||http://purl.uniprot.org/annotation/VSP_029399|||http://purl.uniprot.org/annotation/VSP_029400|||http://purl.uniprot.org/annotation/VSP_029401 http://togogenome.org/gene/10090:Rps6ka1 ^@ http://purl.uniprot.org/uniprot/E9PWV3|||http://purl.uniprot.org/uniprot/P18653|||http://purl.uniprot.org/uniprot/Q505N6|||http://purl.uniprot.org/uniprot/Q810V8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ AGC-kinase C-terminal|||Disordered|||Phosphoserine|||Phosphoserine; by PDPK1|||Phosphothreonine|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Ribosomal protein S6 kinase alpha-1 ^@ http://purl.uniprot.org/annotation/PRO_0000086199 http://togogenome.org/gene/10090:Or52a24 ^@ http://purl.uniprot.org/uniprot/K7N6B2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pigm ^@ http://purl.uniprot.org/uniprot/Q8C2R7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||GPI mannosyltransferase 1|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000246215 http://togogenome.org/gene/10090:Dnajc11 ^@ http://purl.uniprot.org/uniprot/Q5U458 ^@ 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|||Sequence Conflict ^@ DnaJ homolog subfamily C member 11|||J|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000247158 http://togogenome.org/gene/10090:Lcmt2 ^@ http://purl.uniprot.org/uniprot/Q8BYR1 ^@ 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 ^@ Disordered|||In isoform 2.|||Polar residues|||tRNA wybutosine-synthesizing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000204424|||http://purl.uniprot.org/annotation/VSP_010357|||http://purl.uniprot.org/annotation/VSP_010358 http://togogenome.org/gene/10090:Tldc2 ^@ http://purl.uniprot.org/uniprot/E9PZS3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||TLDc ^@ http://togogenome.org/gene/10090:Bmpr1b ^@ http://purl.uniprot.org/uniprot/B2RRZ4|||http://purl.uniprot.org/uniprot/P36898|||http://purl.uniprot.org/uniprot/Q3USS1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Bone morphogenetic protein receptor type-1B|||Cytoplasmic|||Disordered|||Extracellular|||GS|||Helical|||Loss of kinase activity. No effect on cell membrane location.|||No effect on kinase activity. No effect on cell membrane location.|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000024413 http://togogenome.org/gene/10090:Ralgapa1 ^@ http://purl.uniprot.org/uniprot/A0A1W2P712|||http://purl.uniprot.org/uniprot/A0A1W2P832|||http://purl.uniprot.org/uniprot/Q3U5E2|||http://purl.uniprot.org/uniprot/Q6GYP7 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 1S.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||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_0000056754|||http://purl.uniprot.org/annotation/VSP_011330|||http://purl.uniprot.org/annotation/VSP_011331|||http://purl.uniprot.org/annotation/VSP_011332|||http://purl.uniprot.org/annotation/VSP_011333|||http://purl.uniprot.org/annotation/VSP_011334|||http://purl.uniprot.org/annotation/VSP_011335|||http://purl.uniprot.org/annotation/VSP_011336|||http://purl.uniprot.org/annotation/VSP_011337|||http://purl.uniprot.org/annotation/VSP_011338 http://togogenome.org/gene/10090:Vamp3 ^@ http://purl.uniprot.org/uniprot/P63024 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Domain Extent|||Region|||Site|||Topological Domain|||Transmembrane ^@ (Microbial infection) Cleavage; by C.botulinum neurotoxin type X (BoNT/X)|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Anchor for type IV membrane protein|||Vesicle-associated membrane protein 3|||Vesicular|||v-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000206729 http://togogenome.org/gene/10090:Abcb10 ^@ http://purl.uniprot.org/uniprot/Q9JI39 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||ATP-binding cassette sub-family B member 10, mitochondrial|||Affects ATP hydrolysis but not binding.|||Decreases ATP binding about 50%.|||Does not affect ABCB10 glutathionylation.|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||Prevents ABCB10 glutathionylation.|||S-glutathionyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000000256 http://togogenome.org/gene/10090:Bop1 ^@ http://purl.uniprot.org/uniprot/P97452 ^@ 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|||Phosphoserine|||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_0000050886 http://togogenome.org/gene/10090:Tor1a ^@ http://purl.uniprot.org/uniprot/Q3TV62|||http://purl.uniprot.org/uniprot/Q9ER39 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide ^@ Interaction with KLC1|||Interaction with SNAPIN|||Interaction with SYNE3|||N-linked (GlcNAc...) asparagine|||Nuclear envelope abnormalities specific to neurons.|||Torsin|||Torsin-1A ^@ http://purl.uniprot.org/annotation/PRO_0000005508|||http://purl.uniprot.org/annotation/PRO_5014309180 http://togogenome.org/gene/10090:Frmd3 ^@ http://purl.uniprot.org/uniprot/Q8BHD4|||http://purl.uniprot.org/uniprot/Q8BV94 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ FERM|||FERM domain-containing protein 3|||Helical|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000318099|||http://purl.uniprot.org/annotation/VSP_031168|||http://purl.uniprot.org/annotation/VSP_031169|||http://purl.uniprot.org/annotation/VSP_031170 http://togogenome.org/gene/10090:Rps6 ^@ http://purl.uniprot.org/uniprot/P62754|||http://purl.uniprot.org/uniprot/Q5BLK1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ (3R)-3-hydroxyarginine|||ADP-ribosyl glutamic acid|||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_0000137313 http://togogenome.org/gene/10090:Ube2e3 ^@ http://purl.uniprot.org/uniprot/P52483 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||Loss of enzymatic activity, interaction with IPO11, nuclear import, and effect on cell growth.|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 E3 ^@ http://purl.uniprot.org/annotation/PRO_0000082475 http://togogenome.org/gene/10090:Cep112 ^@ http://purl.uniprot.org/uniprot/Q3TV83|||http://purl.uniprot.org/uniprot/Q5PR68|||http://purl.uniprot.org/uniprot/Q9DAQ8 ^@ 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 ^@ Basic and acidic residues|||Centrosomal protein of 112 kDa|||DUF4485|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000234509|||http://purl.uniprot.org/annotation/VSP_018340|||http://purl.uniprot.org/annotation/VSP_018341 http://togogenome.org/gene/10090:Egfl8 ^@ http://purl.uniprot.org/uniprot/B9EJ41|||http://purl.uniprot.org/uniprot/Q6GUQ1 ^@ 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 ^@ EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EMI|||Epidermal growth factor-like protein 8|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000007532|||http://purl.uniprot.org/annotation/PRO_5014300262|||http://purl.uniprot.org/annotation/VSP_026672 http://togogenome.org/gene/10090:Or2ag18 ^@ http://purl.uniprot.org/uniprot/Q8VFM5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trappc4 ^@ http://purl.uniprot.org/uniprot/Q9ES56 ^@ Chain|||Molecule Processing ^@ Chain ^@ Trafficking protein particle complex subunit 4 ^@ http://purl.uniprot.org/annotation/PRO_0000211570 http://togogenome.org/gene/10090:Ifnb1 ^@ http://purl.uniprot.org/uniprot/P01575|||http://purl.uniprot.org/uniprot/Q0VE17 ^@ Chain|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Turn ^@ Chain|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Turn ^@ Interferon beta|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000016403|||http://purl.uniprot.org/annotation/PRO_5014306850 http://togogenome.org/gene/10090:Vdac2 ^@ http://purl.uniprot.org/uniprot/Q60930 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Sequence Conflict|||Site|||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|||Involved in ceramide and phosphatidylcholine binding|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Voltage-dependent anion-selective channel protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000050506 http://togogenome.org/gene/10090:Ythdc1 ^@ http://purl.uniprot.org/uniprot/E9Q5K9|||http://purl.uniprot.org/uniprot/Q8C4W4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Abolished binding to N6-methyladenosine (m6A)-containing RNAs; when associated with A-378.|||Abolished binding to N6-methyladenosine (m6A)-containing RNAs; when associated with A-429.|||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 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||YTH|||YTH domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000425545|||http://purl.uniprot.org/annotation/VSP_053719|||http://purl.uniprot.org/annotation/VSP_053720 http://togogenome.org/gene/10090:Cyp3a41b ^@ http://purl.uniprot.org/uniprot/Q9JMA7 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Cytochrome P450 3A41|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051813 http://togogenome.org/gene/10090:Col4a4 ^@ http://purl.uniprot.org/uniprot/Q9QZR9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ 7S domain|||Basic and acidic residues|||Cell attachment site|||Cleavage; by collagenase|||Collagen IV NC1|||Collagen alpha-4(IV) chain|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Or C-1472 with C-1558|||Or C-1505 with C-1561|||Or C-1580 with C-1675|||Or C-1614 with C-1678|||Pro residues|||Triple-helical region ^@ http://purl.uniprot.org/annotation/PRO_0000283793|||http://purl.uniprot.org/annotation/VSP_052356|||http://purl.uniprot.org/annotation/VSP_052357 http://togogenome.org/gene/10090:Spn ^@ http://purl.uniprot.org/uniprot/P15702|||http://purl.uniprot.org/uniprot/Q544C5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ CD43 cytoplasmic tail|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Leukosialin|||Loss of phosphorylation, interaction with EZR and localization to the uropodium.|||N-linked (GlcNAc...) asparagine|||No effect on its interaction with RDX.|||No loss of phosphorylation or localization to the uropodium. Loss of interaction with EZR.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PKC/PRKCQ|||Phosphothreonine|||Polar residues|||Reduced phosphorylation. Significant loss of phosphorylation; when associated with A-343.|||Reduced phosphorylation. Significant loss of phosphorylation; when associated with A-347.|||Required for interaction with EZR, MSN and RDX and for co-localization to microvilli|||Significant reduction in interaction with RDX. ^@ http://purl.uniprot.org/annotation/PRO_0000021589|||http://purl.uniprot.org/annotation/PRO_0000443407|||http://purl.uniprot.org/annotation/PRO_5014309571 http://togogenome.org/gene/10090:Amhr2 ^@ http://purl.uniprot.org/uniprot/Q8K592 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Anti-Muellerian hormone type-2 receptor|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000260265 http://togogenome.org/gene/10090:Xpo5 ^@ http://purl.uniprot.org/uniprot/Q924C1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Exportin-5|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Necessary for interaction with ILF3|||Necessary for interaction with Ran|||Pre-siRNA binding ^@ http://purl.uniprot.org/annotation/PRO_0000235300|||http://purl.uniprot.org/annotation/VSP_018462|||http://purl.uniprot.org/annotation/VSP_018463|||http://purl.uniprot.org/annotation/VSP_018464|||http://purl.uniprot.org/annotation/VSP_018465 http://togogenome.org/gene/10090:Polr2c ^@ http://purl.uniprot.org/uniprot/P97760 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ DNA-directed RNA polymerase II subunit RPB3|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000132744 http://togogenome.org/gene/10090:Pglyrp3 ^@ http://purl.uniprot.org/uniprot/A1A547 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide ^@ 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_0000295274 http://togogenome.org/gene/10090:Hnrnpm ^@ http://purl.uniprot.org/uniprot/Q3THB3|||http://purl.uniprot.org/uniprot/Q570Z0|||http://purl.uniprot.org/uniprot/Q9D0E1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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_0000081865|||http://purl.uniprot.org/annotation/VSP_011933 http://togogenome.org/gene/10090:Slc8a2 ^@ http://purl.uniprot.org/uniprot/Q8K596 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Calx-beta 1|||Calx-beta 2|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Putative calmodulin-binding region|||Sodium/calcium exchanger 2 ^@ http://purl.uniprot.org/annotation/PRO_0000434796|||http://purl.uniprot.org/annotation/VSP_057980 http://togogenome.org/gene/10090:Idnk ^@ http://purl.uniprot.org/uniprot/Q8R0J8 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Probable gluconokinase ^@ http://purl.uniprot.org/annotation/PRO_0000327371 http://togogenome.org/gene/10090:Ftcd ^@ http://purl.uniprot.org/uniprot/Q91XD4 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region ^@ Cyclodeaminase/cyclohydrolase|||For cyclodeaminase activity|||For formimidoyltransferase activity|||Formimidoyltransferase-cyclodeaminase|||Formiminotransferase C-subdomain|||Formiminotransferase N-subdomain|||Linker|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000087360 http://togogenome.org/gene/10090:4931408C20Rik ^@ http://purl.uniprot.org/uniprot/E9PWP9|||http://purl.uniprot.org/uniprot/Q3V0G6 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues|||SPATA31 ^@ http://togogenome.org/gene/10090:E2f3 ^@ http://purl.uniprot.org/uniprot/O35261|||http://purl.uniprot.org/uniprot/Q3TMJ9|||http://purl.uniprot.org/uniprot/Q3UZJ0|||http://purl.uniprot.org/uniprot/Q6PCM3|||http://purl.uniprot.org/uniprot/Q6ZQJ8 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Cyclin A/CDK2 binding|||DEF box|||Dimerization|||Disordered|||E2F/DP family winged-helix DNA-binding|||Leucine-zipper|||Polar residues|||Pro residues|||Retinoblastoma protein binding|||Transactivation|||Transcription factor E2F3 ^@ http://purl.uniprot.org/annotation/PRO_0000219467 http://togogenome.org/gene/10090:Igfbp4 ^@ http://purl.uniprot.org/uniprot/P47879 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ IGFBP N-terminal|||Insulin-like growth factor-binding protein 4|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000014383 http://togogenome.org/gene/10090:Nup133 ^@ http://purl.uniprot.org/uniprot/Q8CDZ5|||http://purl.uniprot.org/uniprot/Q8R0G9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylmethionine|||N6-acetyllysine|||Nuclear pore complex protein Nup133|||Nucleoporin Nup133/Nup155-like C-terminal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000204839 http://togogenome.org/gene/10090:Ndufa9 ^@ http://purl.uniprot.org/uniprot/Q9DC69 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000019993 http://togogenome.org/gene/10090:Col11a1 ^@ http://purl.uniprot.org/uniprot/Q3UST0|||http://purl.uniprot.org/uniprot/Q61245 ^@ 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|||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|||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|||Disordered|||Fibrillar collagen NC1|||In isoform Short.|||Interchain|||Laminin G|||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_0000005777|||http://purl.uniprot.org/annotation/PRO_0000005778|||http://purl.uniprot.org/annotation/PRO_0000005779|||http://purl.uniprot.org/annotation/VSP_001147 http://togogenome.org/gene/10090:Rtp4 ^@ http://purl.uniprot.org/uniprot/Q9ER80 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane|||Zinc Finger ^@ 3CxxC-type|||Cytoplasmic|||Disordered|||Helical|||Pro residues|||Receptor-transporting protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000181996 http://togogenome.org/gene/10090:Ino80c ^@ http://purl.uniprot.org/uniprot/Q8BHA0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||INO80 complex subunit C|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079318 http://togogenome.org/gene/10090:Ginm1 ^@ http://purl.uniprot.org/uniprot/Q3UN36|||http://purl.uniprot.org/uniprot/Q91WR6 ^@ 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_0000019544|||http://purl.uniprot.org/annotation/PRO_5015097487 http://togogenome.org/gene/10090:Clec18a ^@ http://purl.uniprot.org/uniprot/Q7TSQ1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Splice Variant ^@ C-type lectin|||C-type lectin domain family 18 member A|||Disordered|||EGF-like|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||SCP ^@ http://purl.uniprot.org/annotation/PRO_0000324318|||http://purl.uniprot.org/annotation/VSP_032208|||http://purl.uniprot.org/annotation/VSP_032209|||http://purl.uniprot.org/annotation/VSP_032210|||http://purl.uniprot.org/annotation/VSP_032211 http://togogenome.org/gene/10090:Pcdhgc3 ^@ http://purl.uniprot.org/uniprot/Q91XX1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099493 http://togogenome.org/gene/10090:Scrg1 ^@ http://purl.uniprot.org/uniprot/O88745|||http://purl.uniprot.org/uniprot/Q543T5 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Scrapie-responsive protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000022284|||http://purl.uniprot.org/annotation/PRO_5014309617 http://togogenome.org/gene/10090:Ttyh1 ^@ http://purl.uniprot.org/uniprot/Q9D3A9 ^@ 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 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein tweety homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000312241|||http://purl.uniprot.org/annotation/VSP_029762|||http://purl.uniprot.org/annotation/VSP_029763|||http://purl.uniprot.org/annotation/VSP_029765 http://togogenome.org/gene/10090:Cdip1 ^@ http://purl.uniprot.org/uniprot/Q9DB75 ^@ 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.|||LITAF|||Membrane-binding amphipathic helix|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000280337|||http://purl.uniprot.org/annotation/VSP_023632 http://togogenome.org/gene/10090:Adad1 ^@ http://purl.uniprot.org/uniprot/Q5SUE7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ A to I editase|||Adenosine deaminase domain-containing protein 1|||DRBM|||Disordered|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000309521|||http://purl.uniprot.org/annotation/VSP_029227|||http://purl.uniprot.org/annotation/VSP_029228|||http://purl.uniprot.org/annotation/VSP_029229 http://togogenome.org/gene/10090:Cnot11 ^@ http://purl.uniprot.org/uniprot/Q9CWN7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ CCR4-NOT transcription complex subunit 11|||Disordered|||Omega-N-methylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000089358 http://togogenome.org/gene/10090:Snu13 ^@ http://purl.uniprot.org/uniprot/Q9D0T1 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ 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|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000136779|||http://purl.uniprot.org/annotation/PRO_0000423262 http://togogenome.org/gene/10090:Melk ^@ http://purl.uniprot.org/uniprot/Q61846 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ Autoinhibitory region|||KA1|||Loss of kinase activity.|||Maternal embryonic leucine zipper kinase|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||UBA-like ^@ http://purl.uniprot.org/annotation/PRO_0000086324 http://togogenome.org/gene/10090:Ctf1 ^@ http://purl.uniprot.org/uniprot/Q60753 ^@ Chain|||Molecule Processing ^@ Chain ^@ Cardiotrophin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000058763 http://togogenome.org/gene/10090:Wdr59 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLJ8|||http://purl.uniprot.org/uniprot/Q8C0M0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C4-type|||Disordered|||GATOR2 complex protein WDR59|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||RING-type; atypical|||RWD|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8 ^@ http://purl.uniprot.org/annotation/PRO_0000280722|||http://purl.uniprot.org/annotation/VSP_023885|||http://purl.uniprot.org/annotation/VSP_023886 http://togogenome.org/gene/10090:Epb41l4a ^@ http://purl.uniprot.org/uniprot/P52963|||http://purl.uniprot.org/uniprot/Q3USC8 ^@ 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 ^@ Band 4.1-like protein 4A|||Basic and acidic residues|||Disordered|||FERM|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000219402 http://togogenome.org/gene/10090:Lipt1 ^@ http://purl.uniprot.org/uniprot/Q8C894|||http://purl.uniprot.org/uniprot/Q8VCM4 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Transit Peptide ^@ BPL/LPL catalytic|||Lipoyltransferase 1, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000017857 http://togogenome.org/gene/10090:Nfat5 ^@ http://purl.uniprot.org/uniprot/A0A1U6URG8|||http://purl.uniprot.org/uniprot/Q3UZ77|||http://purl.uniprot.org/uniprot/Q9WV30 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice 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|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Nuclear factor of activated T-cells 5|||Phosphoserine|||Phosphothreonine; by CDK5|||Polar residues|||RHD ^@ http://purl.uniprot.org/annotation/PRO_0000205184|||http://purl.uniprot.org/annotation/VSP_058789|||http://purl.uniprot.org/annotation/VSP_058790|||http://purl.uniprot.org/annotation/VSP_058791|||http://purl.uniprot.org/annotation/VSP_058792|||http://purl.uniprot.org/annotation/VSP_058793 http://togogenome.org/gene/10090:Faah ^@ http://purl.uniprot.org/uniprot/O08914 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||INTRAMEM|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Acyl-ester intermediate|||Charge relay system|||Cytoplasmic|||Fatty-acid amide hydrolase 1|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000105265 http://togogenome.org/gene/10090:Spag9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J196|||http://purl.uniprot.org/uniprot/B8X349|||http://purl.uniprot.org/uniprot/E9PUD1|||http://purl.uniprot.org/uniprot/Q58A65|||http://purl.uniprot.org/uniprot/Q6PA03 ^@ 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|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ C-Jun-amino-terminal kinase-interacting protein 4|||Disordered|||Helical|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RH1|||RH2 ^@ http://purl.uniprot.org/annotation/PRO_0000234077|||http://purl.uniprot.org/annotation/VSP_018225|||http://purl.uniprot.org/annotation/VSP_018226|||http://purl.uniprot.org/annotation/VSP_018227|||http://purl.uniprot.org/annotation/VSP_018228|||http://purl.uniprot.org/annotation/VSP_018229|||http://purl.uniprot.org/annotation/VSP_018230 http://togogenome.org/gene/10090:Bmt2 ^@ http://purl.uniprot.org/uniprot/Q8BXK4 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Region ^@ Disordered|||S-adenosylmethionine sensor upstream of mTORC1 ^@ http://purl.uniprot.org/annotation/PRO_0000321540 http://togogenome.org/gene/10090:Zfp109 ^@ http://purl.uniprot.org/uniprot/Q9R166 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Krt33a ^@ http://purl.uniprot.org/uniprot/Q8K0Y2 ^@ 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-I|||Linker 1|||Linker 12|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000366205 http://togogenome.org/gene/10090:Tbc1d7 ^@ http://purl.uniprot.org/uniprot/Q9D0K0 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ In isoform 2.|||Rab-GAP TBC|||TBC1 domain family member 7 ^@ http://purl.uniprot.org/annotation/PRO_0000208032|||http://purl.uniprot.org/annotation/VSP_044187 http://togogenome.org/gene/10090:Unc119b ^@ http://purl.uniprot.org/uniprot/Q8C4B4 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||Protein unc-119 homolog B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000337229|||http://purl.uniprot.org/annotation/VSP_033985 http://togogenome.org/gene/10090:Slco2a1 ^@ http://purl.uniprot.org/uniprot/Q3TED0|||http://purl.uniprot.org/uniprot/Q9EPT5 ^@ 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|||Region|||Sequence Conflict|||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.|||Kazal-like|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||No effect.|||Solute carrier organic anion transporter family member 2A1 ^@ http://purl.uniprot.org/annotation/PRO_0000191059|||http://purl.uniprot.org/annotation/VSP_006128|||http://purl.uniprot.org/annotation/VSP_006129 http://togogenome.org/gene/10090:Hpse2 ^@ http://purl.uniprot.org/uniprot/B2RY83 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ Inactive heparanase-2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000418888 http://togogenome.org/gene/10090:Epb41l2 ^@ http://purl.uniprot.org/uniprot/O70318|||http://purl.uniprot.org/uniprot/Q3UNQ6|||http://purl.uniprot.org/uniprot/Q7TPN6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Band 4.1 C-terminal|||Band 4.1-like protein 2|||Basic and acidic residues|||C-terminal (CTD)|||Disordered|||FERM|||Hydrophilic|||N-acetylthreonine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Spectrin--actin-binding ^@ http://purl.uniprot.org/annotation/PRO_0000219398 http://togogenome.org/gene/10090:Lum ^@ http://purl.uniprot.org/uniprot/P51885 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Repeat|||Sequence Conflict|||Signal Peptide ^@ 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_0000032734 http://togogenome.org/gene/10090:Pcf11 ^@ http://purl.uniprot.org/uniprot/G3X9Z4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||CID|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pre-mRNA cleavage complex 2 protein Pcf11|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000458461 http://togogenome.org/gene/10090:Mtmr9 ^@ http://purl.uniprot.org/uniprot/Q9Z2D0 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site ^@ GRAM|||Loss of cell membrane recruitment following EGF stimulation.|||Myotubularin phosphatase|||Myotubularin-related protein 9|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000094944 http://togogenome.org/gene/10090:Klri1 ^@ http://purl.uniprot.org/uniprot/B2KG20 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||ITIM motif 1|||ITIM motif 2|||Killer cell lectin-like receptor subfamily I member 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000442199 http://togogenome.org/gene/10090:Galnt11 ^@ http://purl.uniprot.org/uniprot/Q921L8 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||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|||Phosphoserine|||Polypeptide N-acetylgalactosaminyltransferase 11|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059126 http://togogenome.org/gene/10090:Qtrt2 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPN7|||http://purl.uniprot.org/uniprot/B8ZXI1|||http://purl.uniprot.org/uniprot/Z4YJE9 ^@ 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.|||Queuine tRNA-ribosyltransferase accessory subunit 2|||tRNA-guanine(15) transglycosylase-like ^@ http://purl.uniprot.org/annotation/PRO_0000383924|||http://purl.uniprot.org/annotation/VSP_038046 http://togogenome.org/gene/10090:Scgb1b30 ^@ http://purl.uniprot.org/uniprot/A2BH64 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5002642812 http://togogenome.org/gene/10090:Slc5a8 ^@ http://purl.uniprot.org/uniprot/Q8BYF6 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Sodium-coupled monocarboxylate transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000334500 http://togogenome.org/gene/10090:Zfp268 ^@ http://purl.uniprot.org/uniprot/B1ASQ7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ctag2 ^@ http://purl.uniprot.org/uniprot/Q9D9S4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gata2 ^@ http://purl.uniprot.org/uniprot/O09100|||http://purl.uniprot.org/uniprot/Q3U320 ^@ 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 ^@ Asymmetric dimethylarginine|||Disordered|||Endothelial transcription factor GATA-2|||GATA-type|||GATA-type 1|||GATA-type 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000083404 http://togogenome.org/gene/10090:Ssxb3 ^@ http://purl.uniprot.org/uniprot/Q6XAS4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB|||KRAB-related ^@ http://togogenome.org/gene/10090:Chst10 ^@ http://purl.uniprot.org/uniprot/A2RSS2|||http://purl.uniprot.org/uniprot/Q6PGK7 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 10|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000189658|||http://purl.uniprot.org/annotation/VSP_012989|||http://purl.uniprot.org/annotation/VSP_012990|||http://purl.uniprot.org/annotation/VSP_012991 http://togogenome.org/gene/10090:Rasd1 ^@ http://purl.uniprot.org/uniprot/O35626 ^@ 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|||Dexamethasone-induced Ras-related protein 1|||Effector region|||Removed in mature form|||S-farnesyl cysteine|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000082718|||http://purl.uniprot.org/annotation/PRO_0000281373 http://togogenome.org/gene/10090:Slc5a4b ^@ http://purl.uniprot.org/uniprot/Q2VPB3|||http://purl.uniprot.org/uniprot/Q91ZP4 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Solute carrier family 5 member 4B ^@ http://purl.uniprot.org/annotation/PRO_0000458212 http://togogenome.org/gene/10090:Nudcd2 ^@ http://purl.uniprot.org/uniprot/E0CYQ2|||http://purl.uniprot.org/uniprot/Q9CQ48 ^@ 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|||Region|||Sequence Conflict|||Strand ^@ CS|||Disordered|||N-acetylserine|||NudC domain-containing protein 2|||Phosphoserine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057983 http://togogenome.org/gene/10090:Cyp11a1 ^@ http://purl.uniprot.org/uniprot/Q9QZ82 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Transit Peptide ^@ Cholesterol side-chain cleavage enzyme, mitochondrial|||Disordered|||Mitochondrion|||Polar residues|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000003587 http://togogenome.org/gene/10090:Dnah10 ^@ http://purl.uniprot.org/uniprot/D3YYQ8 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ AAA+ ATPase ^@ http://togogenome.org/gene/10090:Abhd3 ^@ http://purl.uniprot.org/uniprot/Q91ZH7 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ AB hydrolase-1|||Charge relay system|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Loss of phospholipase activity.|||Phospholipase ABHD3 ^@ http://purl.uniprot.org/annotation/PRO_0000280209|||http://purl.uniprot.org/annotation/VSP_023564 http://togogenome.org/gene/10090:Txnip ^@ http://purl.uniprot.org/uniprot/Q8BG60 ^@ Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ 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_0000250490|||http://purl.uniprot.org/annotation/VSP_020653 http://togogenome.org/gene/10090:Mrln ^@ http://purl.uniprot.org/uniprot/Q9CV60 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Abolishes interaction with ATP2A1/SERCA1.|||Cytoplasmic|||Does not affect interaction with ATP2A1.|||Helical|||Lumenal|||Myoregulin ^@ http://purl.uniprot.org/annotation/PRO_0000432709 http://togogenome.org/gene/10090:Idh3a ^@ http://purl.uniprot.org/uniprot/Q9D6R2 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Critical for catalysis|||Homozygous mutant mice exhibit retinal degeneration.|||In isoform 2.|||Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000014438|||http://purl.uniprot.org/annotation/VSP_014517 http://togogenome.org/gene/10090:Gm5168 ^@ http://purl.uniprot.org/uniprot/Q4KL04 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Dcdc2b ^@ http://purl.uniprot.org/uniprot/J3KML0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Doublecortin|||Polar residues ^@ http://togogenome.org/gene/10090:Or10ak8 ^@ http://purl.uniprot.org/uniprot/L7MTV4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Penk ^@ http://purl.uniprot.org/uniprot/P22005|||http://purl.uniprot.org/uniprot/Q3UXY8 ^@ Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Disulfide Bond|||Modified Residue|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage; by CTSL|||Disordered|||Leu-enkephalin|||Met-enkephalin|||Met-enkephalin-Arg-Phe|||Met-enkephalin-Arg-Ser-Leu|||PENK(114-133)|||PENK(143-184)|||PENK(238-259)|||Phosphoserine|||Synenkephalin ^@ http://purl.uniprot.org/annotation/PRO_0000008268|||http://purl.uniprot.org/annotation/PRO_0000008269|||http://purl.uniprot.org/annotation/PRO_0000008270|||http://purl.uniprot.org/annotation/PRO_0000008272|||http://purl.uniprot.org/annotation/PRO_0000008274|||http://purl.uniprot.org/annotation/PRO_0000008275|||http://purl.uniprot.org/annotation/PRO_0000008276|||http://purl.uniprot.org/annotation/PRO_0000008277|||http://purl.uniprot.org/annotation/PRO_0000008278|||http://purl.uniprot.org/annotation/PRO_0000008280|||http://purl.uniprot.org/annotation/PRO_0000377694|||http://purl.uniprot.org/annotation/PRO_0000377695|||http://purl.uniprot.org/annotation/PRO_0000377696 http://togogenome.org/gene/10090:Myo1e ^@ http://purl.uniprot.org/uniprot/E9Q634|||http://purl.uniprot.org/uniprot/Q8C123 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Actin-binding|||Disordered|||IQ|||Myosin motor|||Phosphoserine|||Polar residues|||Pro residues|||SH3|||TH1|||Unconventional myosin-Ie ^@ http://purl.uniprot.org/annotation/PRO_0000415664 http://togogenome.org/gene/10090:Tmem25 ^@ http://purl.uniprot.org/uniprot/Q9DCF1 ^@ 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|||Helical|||Ig-like|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 25 ^@ http://purl.uniprot.org/annotation/PRO_0000014985|||http://purl.uniprot.org/annotation/VSP_012942 http://togogenome.org/gene/10090:Clba1 ^@ http://purl.uniprot.org/uniprot/Q8BHN9 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Uncharacterized protein CLBA1 ^@ http://purl.uniprot.org/annotation/PRO_0000274388 http://togogenome.org/gene/10090:Ptchd3 ^@ http://purl.uniprot.org/uniprot/Q0EEE2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Patched domain-containing protein 3|||SSD ^@ http://purl.uniprot.org/annotation/PRO_0000309263|||http://purl.uniprot.org/annotation/VSP_029100|||http://purl.uniprot.org/annotation/VSP_029101 http://togogenome.org/gene/10090:Wipf3 ^@ http://purl.uniprot.org/uniprot/D3Z5R4|||http://purl.uniprot.org/uniprot/E9Q2D0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||WH2 ^@ http://togogenome.org/gene/10090:Ak3 ^@ http://purl.uniprot.org/uniprot/Q9WTP7 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ GTP:AMP phosphotransferase AK3, mitochondrial|||LID|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||NMP|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000158923 http://togogenome.org/gene/10090:Dll3 ^@ http://purl.uniprot.org/uniprot/O88516|||http://purl.uniprot.org/uniprot/Q3UND5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DSL|||Delta-like protein 3|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like domain-containing protein|||Extracellular|||Helical|||In isoform 1. ^@ http://purl.uniprot.org/annotation/PRO_0000007510|||http://purl.uniprot.org/annotation/PRO_5014309172|||http://purl.uniprot.org/annotation/VSP_001376 http://togogenome.org/gene/10090:Defb8 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0D9|||http://purl.uniprot.org/uniprot/Q91V82 ^@ Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Helix|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand ^@ Beta-defensin 8 ^@ http://purl.uniprot.org/annotation/PRO_0000006935|||http://purl.uniprot.org/annotation/PRO_0000006936|||http://purl.uniprot.org/annotation/PRO_5006451967 http://togogenome.org/gene/10090:Bhlhb9 ^@ http://purl.uniprot.org/uniprot/Q6PB60 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||G protein-coupled receptor associated sorting protein 3|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000334664 http://togogenome.org/gene/10090:Lonrf1 ^@ http://purl.uniprot.org/uniprot/A0A182DWE6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Lon N-terminal|||RING-type ^@ http://togogenome.org/gene/10090:Gm12695 ^@ http://purl.uniprot.org/uniprot/A2AGB2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Uncharacterized protein C1orf87 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000284490 http://togogenome.org/gene/10090:Usp35 ^@ http://purl.uniprot.org/uniprot/M0QWN7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||USP ^@ http://togogenome.org/gene/10090:4930503E14Rik ^@ http://purl.uniprot.org/uniprot/Q9D583 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:Inca1 ^@ http://purl.uniprot.org/uniprot/Q6PKN7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Modified Residue|||Motif|||Region|||Splice Variant ^@ In isoform 2.|||Interaction with CCNA1 and CCNA1/CDK2 complex; essential for CDK2 inhibitory activity|||Nuclear localization signal|||Phosphothreonine|||Protein INCA1 ^@ http://purl.uniprot.org/annotation/PRO_0000331514|||http://purl.uniprot.org/annotation/VSP_033236 http://togogenome.org/gene/10090:Tars ^@ http://purl.uniprot.org/uniprot/Q9D0R2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Impairs post-transfer editing activity but no effect on aminoacylation activity; when associated with A-154.|||Impairs post-transfer editing activity but no effect on aminoacylation activity; when associated with A-158.|||N6-acetyllysine|||Phosphothreonine|||Phosphotyrosine|||TGS|||Threonine--tRNA ligase 1, cytoplasmic ^@ http://purl.uniprot.org/annotation/PRO_0000101120 http://togogenome.org/gene/10090:Klf6 ^@ http://purl.uniprot.org/uniprot/Q8BPQ2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ly6l ^@ http://purl.uniprot.org/uniprot/H3BJG9 ^@ 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 serine|||Lymphocyte antigen 6L|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000438095|||http://purl.uniprot.org/annotation/PRO_5003580898 http://togogenome.org/gene/10090:Vps26b ^@ http://purl.uniprot.org/uniprot/Q8C0E2 ^@ 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 ^@ Disrupts interaction with SNX27.|||Disrupts interaction with VPS35:VPS29 dimer; no endosomal localization.|||Disrupts interaction with VPS35:VPS29 dimer; no endosomal localization; when associated with S-245.|||Disrupts interaction with VPS35:VPS29 dimer; no endosomal localization; when associated with S-247.|||In isoform 2.|||No endosomal localization; no effect on interaction with VPS35:VPS29 dimer.|||No endosomal localization; no effect on interaction with VPS35:VPS29 dimer; when associated with E-199.|||No endosomal localization; no effect on interaction with VPS35:VPS29 dimer; when associated with S-197.|||Phosphoserine|||Vacuolar protein sorting-associated protein 26B ^@ http://purl.uniprot.org/annotation/PRO_0000247090|||http://purl.uniprot.org/annotation/VSP_019927 http://togogenome.org/gene/10090:Mroh7 ^@ http://purl.uniprot.org/uniprot/A2AVR2 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Transmembrane ^@ Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||Helical|||Maestro heat-like repeat-containing protein family member 7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000286867 http://togogenome.org/gene/10090:Or5p6 ^@ http://purl.uniprot.org/uniprot/Q8VG04 ^@ 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 5P6 ^@ http://purl.uniprot.org/annotation/PRO_0000150837 http://togogenome.org/gene/10090:4933402N03Rik ^@ http://purl.uniprot.org/uniprot/Q8CDT9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Uncharacterized protein C10orf120 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000458769 http://togogenome.org/gene/10090:Gpat2 ^@ http://purl.uniprot.org/uniprot/Q0KK35|||http://purl.uniprot.org/uniprot/Q14DK4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acyltransferase|||Cytoplasmic|||Disordered|||Does not affect ability to promote piRNA biosynthesis.|||Glycerol-3-phosphate acyltransferase 2, mitochondrial|||HXXXXD motif|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||Mitochondrial intermembrane|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000325854|||http://purl.uniprot.org/annotation/VSP_032457|||http://purl.uniprot.org/annotation/VSP_032458 http://togogenome.org/gene/10090:Pcdhb18 ^@ http://purl.uniprot.org/uniprot/Q3USI6|||http://purl.uniprot.org/uniprot/Q91Y02 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Transmembrane ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin domain-containing protein|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-18 ^@ http://purl.uniprot.org/annotation/PRO_0000432743|||http://purl.uniprot.org/annotation/PRO_5004230322 http://togogenome.org/gene/10090:Tgif2 ^@ http://purl.uniprot.org/uniprot/A2AVY9|||http://purl.uniprot.org/uniprot/Q3TZS1|||http://purl.uniprot.org/uniprot/Q8C0Y1 ^@ Chain|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Homeobox|||Homeobox protein TGIF2|||Homeobox; TALE-type|||Phosphothreonine|||Repressive function ^@ http://purl.uniprot.org/annotation/PRO_0000049322 http://togogenome.org/gene/10090:Recql ^@ http://purl.uniprot.org/uniprot/E9Q3N0|||http://purl.uniprot.org/uniprot/Q3UUK0|||http://purl.uniprot.org/uniprot/Q9Z129 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ ATP-dependent DNA helicase Q1|||Basic and acidic residues|||DEVH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform Beta.|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000205050|||http://purl.uniprot.org/annotation/VSP_005567 http://togogenome.org/gene/10090:Gpr162 ^@ http://purl.uniprot.org/uniprot/Q3UN16 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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|||Phosphoserine|||Pro residues|||Probable G-protein coupled receptor 162 ^@ http://purl.uniprot.org/annotation/PRO_0000069648 http://togogenome.org/gene/10090:Vmn1r81 ^@ http://purl.uniprot.org/uniprot/Q8R286 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp936 ^@ http://purl.uniprot.org/uniprot/Q3ULA8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dnaja1 ^@ http://purl.uniprot.org/uniprot/P63037|||http://purl.uniprot.org/uniprot/Q5NTY0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Repeat|||Zinc Finger ^@ Basic and acidic residues|||CR-type|||CXXCXGXG motif|||Cysteine methyl ester|||Disordered|||DnaJ homolog subfamily A member 1|||J|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000071009|||http://purl.uniprot.org/annotation/PRO_0000396753 http://togogenome.org/gene/10090:Ganc ^@ http://purl.uniprot.org/uniprot/A2AQJ8|||http://purl.uniprot.org/uniprot/Q8BVW0 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Disordered|||Glycoside hydrolase family 31 N-terminal|||In isoform 2.|||Neutral alpha-glucosidase C|||Nucleophile|||Polar residues|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000185366|||http://purl.uniprot.org/annotation/VSP_010619|||http://purl.uniprot.org/annotation/VSP_010620|||http://purl.uniprot.org/annotation/VSP_010621 http://togogenome.org/gene/10090:Mettl7b ^@ http://purl.uniprot.org/uniprot/Q9DD20 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Thiol S-methyltransferase TMT1B ^@ http://purl.uniprot.org/annotation/PRO_0000251923 http://togogenome.org/gene/10090:Or4c11 ^@ http://purl.uniprot.org/uniprot/A2ATJ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gm17019 ^@ http://purl.uniprot.org/uniprot/K7N6W5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ino80d ^@ http://purl.uniprot.org/uniprot/B1AT32|||http://purl.uniprot.org/uniprot/Q66JY2 ^@ 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 residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||INO80 complex subunit D|||In isoform 4.|||Phosphoserine|||Polar residues|||Potential DNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000319586|||http://purl.uniprot.org/annotation/VSP_060240 http://togogenome.org/gene/10090:Fam205a3 ^@ http://purl.uniprot.org/uniprot/C0HKD1|||http://purl.uniprot.org/uniprot/C0HKD2|||http://purl.uniprot.org/uniprot/C0HKD3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Protein SPATA31F1-2|||Protein SPATA31F1-3|||Protein SPATA31F1-4 ^@ http://purl.uniprot.org/annotation/PRO_0000341305|||http://purl.uniprot.org/annotation/PRO_0000444751|||http://purl.uniprot.org/annotation/PRO_0000444752 http://togogenome.org/gene/10090:Eif4a3 ^@ http://purl.uniprot.org/uniprot/Q91VC3 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict ^@ DEAD box|||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|||N-acetylalanine; in Eukaryotic initiation factor 4A-III, N-terminally processed|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Q motif|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000054944|||http://purl.uniprot.org/annotation/PRO_0000423269 http://togogenome.org/gene/10090:Serpinb12 ^@ http://purl.uniprot.org/uniprot/Q9D7P9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Site ^@ Disordered|||Polar residues|||Reactive bond|||Serpin B12 ^@ http://purl.uniprot.org/annotation/PRO_0000094120 http://togogenome.org/gene/10090:Osbpl1a ^@ http://purl.uniprot.org/uniprot/Q3V156|||http://purl.uniprot.org/uniprot/Q91XL9 ^@ 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 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand ^@ ANK 1|||ANK 2|||ANK 3|||Basic and acidic residues|||Disordered|||FFAT|||In isoform 2.|||In isoform 3.|||Interaction with RAB7A|||Oxysterol-binding protein-related protein 1|||PH|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000100368|||http://purl.uniprot.org/annotation/VSP_017723|||http://purl.uniprot.org/annotation/VSP_017724 http://togogenome.org/gene/10090:Plcb2 ^@ http://purl.uniprot.org/uniprot/A3KGF7|||http://purl.uniprot.org/uniprot/E9PYI3|||http://purl.uniprot.org/uniprot/Q3V3V2 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||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|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2|||Acidic residues|||C2|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295683|||http://purl.uniprot.org/annotation/VSP_026981|||http://purl.uniprot.org/annotation/VSP_026982|||http://purl.uniprot.org/annotation/VSP_026983|||http://purl.uniprot.org/annotation/VSP_026984|||http://purl.uniprot.org/annotation/VSP_026985|||http://purl.uniprot.org/annotation/VSP_026986 http://togogenome.org/gene/10090:Parp16 ^@ http://purl.uniprot.org/uniprot/Q7TMM8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Nicotinamide-stacking aromate|||PARP alpha-helical|||PARP catalytic|||Protein mono-ADP-ribosyltransferase PARP16 ^@ http://purl.uniprot.org/annotation/PRO_0000252438 http://togogenome.org/gene/10090:H2bc27 ^@ http://purl.uniprot.org/uniprot/Q9D2U9 ^@ 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|||H2B.U histone 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-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_0000244837 http://togogenome.org/gene/10090:Krt75 ^@ http://purl.uniprot.org/uniprot/Q8BGZ7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Chain|||Domain Extent|||Mutagenesis Site|||Region|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type II cytoskeletal 75|||Linker 1|||Linker 12|||Mice develop hair and nail defects resembling pachyonychia congenita.|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000314888 http://togogenome.org/gene/10090:Nagpa ^@ http://purl.uniprot.org/uniprot/Q8BJ48 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EGF-like|||Helical|||Lumenal|||Mediates the interaction with AP4M1|||N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase|||N-linked (GlcNAc...) asparagine|||NPF internalization motif|||Removed in mature form|||Tyrosine-based internalization motif ^@ http://purl.uniprot.org/annotation/PRO_0000021789|||http://purl.uniprot.org/annotation/PRO_0000424660 http://togogenome.org/gene/10090:Or51ab3 ^@ http://purl.uniprot.org/uniprot/A6H6I6|||http://purl.uniprot.org/uniprot/E9PYB4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ddah2 ^@ http://purl.uniprot.org/uniprot/Q99LD8 ^@ 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_0000171122 http://togogenome.org/gene/10090:Ccdc47 ^@ http://purl.uniprot.org/uniprot/Q0VBU4|||http://purl.uniprot.org/uniprot/Q9D024 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||PAT complex subunit CCDC47 ^@ http://purl.uniprot.org/annotation/PRO_0000235799|||http://purl.uniprot.org/annotation/PRO_5015097000|||http://purl.uniprot.org/annotation/VSP_018479|||http://purl.uniprot.org/annotation/VSP_018480 http://togogenome.org/gene/10090:Ap2m1 ^@ http://purl.uniprot.org/uniprot/P84091|||http://purl.uniprot.org/uniprot/Q3TWV4|||http://purl.uniprot.org/uniprot/Q5FWI9|||http://purl.uniprot.org/uniprot/Q6A0C9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Strand|||Turn ^@ AP-2 complex subunit mu|||MHD|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000193775 http://togogenome.org/gene/10090:Mansc4 ^@ http://purl.uniprot.org/uniprot/Q3UU94 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||MANSC|||MANSC domain-containing protein 4|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000349177 http://togogenome.org/gene/10090:Eci1 ^@ http://purl.uniprot.org/uniprot/P42125 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ Enoyl-CoA delta isomerase 1, mitochondrial|||Important for catalytic activity|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000007421 http://togogenome.org/gene/10090:Myo1a ^@ http://purl.uniprot.org/uniprot/O88329 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Actin-binding|||IQ 1|||IQ 2|||IQ 3|||Myosin motor|||TH1|||Unconventional myosin-Ia ^@ http://purl.uniprot.org/annotation/PRO_0000123439 http://togogenome.org/gene/10090:Vamp4 ^@ http://purl.uniprot.org/uniprot/O70480|||http://purl.uniprot.org/uniprot/Q8BSN6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane ^@ (Microbial infection) Cleavage; by C.botulinum neurotoxin type X (BoNT/X)|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||Phosphoserine|||V-SNARE coiled-coil homology|||Vesicle-associated membrane protein 4|||Vesicular|||v-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000206732 http://togogenome.org/gene/10090:Slc16a7 ^@ http://purl.uniprot.org/uniprot/O70451|||http://purl.uniprot.org/uniprot/Q149G3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic 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|||Major facilitator superfamily (MFS) profile|||May be protonated during monocarboxylate transport|||Monocarboxylate transporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000211388 http://togogenome.org/gene/10090:Stard5 ^@ http://purl.uniprot.org/uniprot/Q9EPQ7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ START|||StAR-related lipid transfer protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000220670 http://togogenome.org/gene/10090:Krt2 ^@ http://purl.uniprot.org/uniprot/Q3TTY5 ^@ 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.|||Keratin, type II cytoskeletal 2 epidermal|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000283763 http://togogenome.org/gene/10090:Gm9376 ^@ http://purl.uniprot.org/uniprot/G3UW68 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Cldn13 ^@ http://purl.uniprot.org/uniprot/Q547B2|||http://purl.uniprot.org/uniprot/Q9Z0S4 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Claudin-13|||Cytoplasmic|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000144768 http://togogenome.org/gene/10090:Samd13 ^@ http://purl.uniprot.org/uniprot/D3YUG0|||http://purl.uniprot.org/uniprot/G5E8V6|||http://purl.uniprot.org/uniprot/Q80ZP0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||J|||SAM|||Sterile alpha motif domain-containing protein 13 ^@ http://purl.uniprot.org/annotation/PRO_0000416122 http://togogenome.org/gene/10090:Fan1 ^@ http://purl.uniprot.org/uniprot/Q69ZT1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Splice Variant|||Zinc Finger ^@ D-box|||Disordered|||Fanconi-associated nuclease 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KEN box|||Polar residues|||UBZ4-type|||VRR-NUC ^@ http://purl.uniprot.org/annotation/PRO_0000311225|||http://purl.uniprot.org/annotation/VSP_029431|||http://purl.uniprot.org/annotation/VSP_029432|||http://purl.uniprot.org/annotation/VSP_029433|||http://purl.uniprot.org/annotation/VSP_029434|||http://purl.uniprot.org/annotation/VSP_029435|||http://purl.uniprot.org/annotation/VSP_029436 http://togogenome.org/gene/10090:Stra6 ^@ http://purl.uniprot.org/uniprot/A0A0R4J115|||http://purl.uniprot.org/uniprot/O70491 ^@ Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Interaction with RBP1|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Receptor for retinol uptake STRA6 ^@ http://purl.uniprot.org/annotation/PRO_0000311229 http://togogenome.org/gene/10090:Kcnip2 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPB0|||http://purl.uniprot.org/uniprot/Q3YAA4|||http://purl.uniprot.org/uniprot/Q3YAB1|||http://purl.uniprot.org/uniprot/Q3YAB2|||http://purl.uniprot.org/uniprot/Q3YAB3|||http://purl.uniprot.org/uniprot/Q9JJ69 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 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.|||In isoform 4.|||Interaction with KCND2|||Kv channel-interacting protein 2|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000073822|||http://purl.uniprot.org/annotation/PRO_5023848366|||http://purl.uniprot.org/annotation/VSP_015059|||http://purl.uniprot.org/annotation/VSP_015060|||http://purl.uniprot.org/annotation/VSP_015061 http://togogenome.org/gene/10090:Prr13 ^@ http://purl.uniprot.org/uniprot/Q9CQJ5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic residues|||Disordered|||Proline-rich protein 13 ^@ http://purl.uniprot.org/annotation/PRO_0000243947 http://togogenome.org/gene/10090:Lysmd3 ^@ http://purl.uniprot.org/uniprot/Q99LE3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||LysM|||LysM and putative peptidoglycan-binding domain-containing protein 3|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000248008 http://togogenome.org/gene/10090:Or8k3b ^@ http://purl.uniprot.org/uniprot/Q7TR63 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pdcd1lg2 ^@ http://purl.uniprot.org/uniprot/Q3U304|||http://purl.uniprot.org/uniprot/Q9WUL5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes the binding to PDCD1.|||Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells.|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||No effect on PDCD1 binding.|||Programmed cell death 1 ligand 2|||Significantly reduces the binding to PDCD1. ^@ http://purl.uniprot.org/annotation/PRO_0000014556|||http://purl.uniprot.org/annotation/PRO_5014309202 http://togogenome.org/gene/10090:Ankrd40 ^@ http://purl.uniprot.org/uniprot/Q5SUE8 ^@ 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 1|||ANK 2|||Ankyrin repeat domain-containing protein 40|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000244369|||http://purl.uniprot.org/annotation/VSP_019554|||http://purl.uniprot.org/annotation/VSP_019555|||http://purl.uniprot.org/annotation/VSP_019556|||http://purl.uniprot.org/annotation/VSP_019557 http://togogenome.org/gene/10090:Fam78b ^@ http://purl.uniprot.org/uniprot/Q8BQN5 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein FAM78B ^@ http://purl.uniprot.org/annotation/PRO_0000265115 http://togogenome.org/gene/10090:Ccdc33 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0H2|||http://purl.uniprot.org/uniprot/D3YU68|||http://purl.uniprot.org/uniprot/E9QQ55|||http://purl.uniprot.org/uniprot/Q3ULW6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ C2|||Coiled-coil domain-containing protein 33|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5. ^@ http://purl.uniprot.org/annotation/PRO_0000307644|||http://purl.uniprot.org/annotation/VSP_028760|||http://purl.uniprot.org/annotation/VSP_028761|||http://purl.uniprot.org/annotation/VSP_028762|||http://purl.uniprot.org/annotation/VSP_028763|||http://purl.uniprot.org/annotation/VSP_028764|||http://purl.uniprot.org/annotation/VSP_028765|||http://purl.uniprot.org/annotation/VSP_028766|||http://purl.uniprot.org/annotation/VSP_028767|||http://purl.uniprot.org/annotation/VSP_028768|||http://purl.uniprot.org/annotation/VSP_028769 http://togogenome.org/gene/10090:Phyh ^@ http://purl.uniprot.org/uniprot/O35386 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ N6-succinyllysine|||Peroxisome|||Phytanoyl-CoA dioxygenase, peroxisomal ^@ http://purl.uniprot.org/annotation/PRO_0000024054 http://togogenome.org/gene/10090:Polg2 ^@ http://purl.uniprot.org/uniprot/Q3V3E7|||http://purl.uniprot.org/uniprot/Q9QZM2 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Anticodon-binding|||DNA polymerase subunit gamma-2, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000007315 http://togogenome.org/gene/10090:Pik3r3 ^@ http://purl.uniprot.org/uniprot/Q3UXE9|||http://purl.uniprot.org/uniprot/Q64143 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue ^@ Phosphatidylinositol 3-kinase regulatory subunit gamma|||Phosphotyrosine|||SH2|||SH2 1|||SH2 2 ^@ http://purl.uniprot.org/annotation/PRO_0000080768 http://togogenome.org/gene/10090:Lsm4 ^@ http://purl.uniprot.org/uniprot/Q9CY46|||http://purl.uniprot.org/uniprot/Q9QXA5 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Sm|||U6 snRNA-associated Sm-like protein LSm4 ^@ http://purl.uniprot.org/annotation/PRO_0000125565 http://togogenome.org/gene/10090:Tmem138 ^@ http://purl.uniprot.org/uniprot/Q9D6G5 ^@ 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 138 ^@ http://purl.uniprot.org/annotation/PRO_0000285701|||http://purl.uniprot.org/annotation/VSP_024893|||http://purl.uniprot.org/annotation/VSP_024894 http://togogenome.org/gene/10090:Or4c12 ^@ http://purl.uniprot.org/uniprot/Q8VEZ1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dnajc30 ^@ http://purl.uniprot.org/uniprot/P59041 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Transit Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transit Peptide|||Transmembrane ^@ Disordered|||DnaJ homolog subfamily C member 30, mitochondrial|||Helical|||J|||Mitochondrion|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000071138 http://togogenome.org/gene/10090:Banf1 ^@ http://purl.uniprot.org/uniprot/O54962 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Barrier-to-autointegration factor|||Barrier-to-autointegration factor, N-terminally processed|||HhH|||N-acetylmethionine|||N-acetylthreonine; in Barrier-to-autointegration factor, N-terminally processed|||Phosphoserine; by VRK1 and VRK2|||Phosphothreonine; by VRK1 and VRK2|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000221027|||http://purl.uniprot.org/annotation/PRO_0000423191 http://togogenome.org/gene/10090:Sox11 ^@ http://purl.uniprot.org/uniprot/Q7M6Y2 ^@ 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|||HMG box|||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_0000048751 http://togogenome.org/gene/10090:Uhrf1 ^@ http://purl.uniprot.org/uniprot/Q8VDF2 ^@ 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Abolishes binding to histone H3K9me3 and ability to repress transcription of target genes.|||Abolishes enzymatic activity.|||Basic and acidic residues|||Disordered|||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|||In isoform 2.|||Linker|||N6-acetyllysine|||N6-acetyllysine; alternate|||PHD-type|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by PKA|||Polar residues|||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|||Tudor-like 1|||Tudor-like 2|||Ubiquitin-like|||YDG ^@ http://purl.uniprot.org/annotation/PRO_0000056145|||http://purl.uniprot.org/annotation/VSP_044395 http://togogenome.org/gene/10090:Coro6 ^@ http://purl.uniprot.org/uniprot/B9EIZ7|||http://purl.uniprot.org/uniprot/Q920M5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant ^@ Coronin-6|||DUF1899|||Disordered|||In isoform B and isoform D.|||In isoform C.|||In isoform D.|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000050932|||http://purl.uniprot.org/annotation/VSP_011749|||http://purl.uniprot.org/annotation/VSP_011750|||http://purl.uniprot.org/annotation/VSP_021487 http://togogenome.org/gene/10090:Avpr1b ^@ http://purl.uniprot.org/uniprot/Q9WU02 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||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|||Vasopressin V1b receptor ^@ http://purl.uniprot.org/annotation/PRO_0000070204 http://togogenome.org/gene/10090:Acrbp ^@ http://purl.uniprot.org/uniprot/Q3V140 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Acidic residues|||Acrosin-binding protein|||Acrosin-binding protein, mature form|||Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Pro-ACR binding|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000227517|||http://purl.uniprot.org/annotation/PRO_0000449369|||http://purl.uniprot.org/annotation/PRO_0000449370|||http://purl.uniprot.org/annotation/VSP_051965|||http://purl.uniprot.org/annotation/VSP_051966 http://togogenome.org/gene/10090:Tmem168 ^@ http://purl.uniprot.org/uniprot/Q91VX9 ^@ 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 168 ^@ http://purl.uniprot.org/annotation/PRO_0000284631 http://togogenome.org/gene/10090:Myd88 ^@ http://purl.uniprot.org/uniprot/P22366|||http://purl.uniprot.org/uniprot/Q3U7M4 ^@ 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 ^@ Death|||In isoform 2.|||Intermediate domain|||Myeloid differentiation primary response protein MyD88|||Phosphoserine|||Prevents dimerization of death domains and activation of JNK and NF-kappa-B.|||TIR ^@ http://purl.uniprot.org/annotation/PRO_0000096667|||http://purl.uniprot.org/annotation/VSP_038888 http://togogenome.org/gene/10090:Muc20 ^@ http://purl.uniprot.org/uniprot/E9PUF1|||http://purl.uniprot.org/uniprot/Q8BUE7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ 1|||2|||3|||4|||5|||Approximate repeats|||Disordered|||Interaction with MET|||Involved in oligomerization|||Mucin-20|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317470|||http://purl.uniprot.org/annotation/PRO_5003242969 http://togogenome.org/gene/10090:Gsk3b ^@ http://purl.uniprot.org/uniprot/E9QAQ5|||http://purl.uniprot.org/uniprot/Q5KU03|||http://purl.uniprot.org/uniprot/Q9WV60 ^@ 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 ^@ Disordered|||Glycogen synthase kinase-3 beta|||Inhibits interaction with AXIN1 and ZBED3.|||Loss of phosphorylation; No inhibition of activity and constitutively active.|||Phosphoserine|||Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK3|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085981 http://togogenome.org/gene/10090:Sin3b ^@ http://purl.uniprot.org/uniprot/Q3TN09|||http://purl.uniprot.org/uniprot/Q62141 ^@ 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 1, isoform 2 and isoform 3.|||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_0000121540|||http://purl.uniprot.org/annotation/VSP_008225|||http://purl.uniprot.org/annotation/VSP_008226|||http://purl.uniprot.org/annotation/VSP_008227|||http://purl.uniprot.org/annotation/VSP_008228|||http://purl.uniprot.org/annotation/VSP_014187 http://togogenome.org/gene/10090:Spata2 ^@ http://purl.uniprot.org/uniprot/Q8K004 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||PIM motif|||PUB|||Spermatogenesis-associated protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000445574|||http://purl.uniprot.org/annotation/VSP_059905|||http://purl.uniprot.org/annotation/VSP_059906 http://togogenome.org/gene/10090:Rab39b ^@ http://purl.uniprot.org/uniprot/Q8BHC1 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif ^@ Cysteine methyl ester|||Effector region|||Phosphoserine|||Ras-related protein Rab-39B|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121256 http://togogenome.org/gene/10090:Cyp2c54 ^@ http://purl.uniprot.org/uniprot/Q6XVG2 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Cytochrome P450 2C54|||N6-acetyllysine|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000282958 http://togogenome.org/gene/10090:Dhx32 ^@ http://purl.uniprot.org/uniprot/D3Z4E3|||http://purl.uniprot.org/uniprot/Q8BZS9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Helicase-associated|||In isoform 2.|||N-acetylmethionine|||Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32 ^@ http://purl.uniprot.org/annotation/PRO_0000292664|||http://purl.uniprot.org/annotation/VSP_026428 http://togogenome.org/gene/10090:Zcchc4 ^@ http://purl.uniprot.org/uniprot/Q08EK6|||http://purl.uniprot.org/uniprot/Q8BKW4 ^@ 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 ^@ CCHC-type|||DHHC|||Disordered|||GRF-type|||In isoform 2.|||Regulatory loop|||rRNA N6-adenosine-methyltransferase ZCCHC4 ^@ http://purl.uniprot.org/annotation/PRO_0000150953|||http://purl.uniprot.org/annotation/VSP_017013 http://togogenome.org/gene/10090:Olfm1 ^@ http://purl.uniprot.org/uniprot/G3X9Q7|||http://purl.uniprot.org/uniprot/O88998|||http://purl.uniprot.org/uniprot/Q8R357 ^@ Chain|||Coiled-Coil|||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|||Turn ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Abolishes retention in the endoplasmic reticulum so that the protein is secreted.|||Endoplasmic reticulum retention signal|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Interchain|||N-linked (GlcNAc...) asparagine|||Noelin|||Olfactomedin-like ^@ http://purl.uniprot.org/annotation/PRO_0000020075|||http://purl.uniprot.org/annotation/PRO_5015091833|||http://purl.uniprot.org/annotation/PRO_5015099337|||http://purl.uniprot.org/annotation/VSP_003762|||http://purl.uniprot.org/annotation/VSP_003763|||http://purl.uniprot.org/annotation/VSP_003764 http://togogenome.org/gene/10090:Gfpt2 ^@ http://purl.uniprot.org/uniprot/Q3V0X4|||http://purl.uniprot.org/uniprot/Q9Z2Z9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ 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_0000135284 http://togogenome.org/gene/10090:Srsf11 ^@ http://purl.uniprot.org/uniprot/E9Q6E5|||http://purl.uniprot.org/uniprot/Q3UIX4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||RRM ^@ http://togogenome.org/gene/10090:Mvb12a ^@ http://purl.uniprot.org/uniprot/Q78HU3 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Disordered|||Interaction with TSG101, VPS37B and VPS28|||MABP|||Multivesicular body subunit 12A|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||SH3-binding|||UMA ^@ http://purl.uniprot.org/annotation/PRO_0000249070 http://togogenome.org/gene/10090:Cd207 ^@ http://purl.uniprot.org/uniprot/Q8VBX4 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000223694 http://togogenome.org/gene/10090:Prps1 ^@ http://purl.uniprot.org/uniprot/Q9D7G0 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Region|||Sequence Conflict ^@ Binding of phosphoribosylpyrophosphate|||Ribose-phosphate pyrophosphokinase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000141072 http://togogenome.org/gene/10090:Fhad1 ^@ http://purl.uniprot.org/uniprot/A6PWD2 ^@ 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|||FHA|||Forkhead-associated domain-containing protein 1|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000349366|||http://purl.uniprot.org/annotation/VSP_035370|||http://purl.uniprot.org/annotation/VSP_035371|||http://purl.uniprot.org/annotation/VSP_035372|||http://purl.uniprot.org/annotation/VSP_035373|||http://purl.uniprot.org/annotation/VSP_035374|||http://purl.uniprot.org/annotation/VSP_035375|||http://purl.uniprot.org/annotation/VSP_035376|||http://purl.uniprot.org/annotation/VSP_035377 http://togogenome.org/gene/10090:Ikbkb ^@ http://purl.uniprot.org/uniprot/A0A0R4J0T4|||http://purl.uniprot.org/uniprot/O88351|||http://purl.uniprot.org/uniprot/Q5D0E0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hydroxyproline|||Inhibitor of nuclear factor kappa-B kinase subunit beta|||Leucine-zipper|||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_0000086014 http://togogenome.org/gene/10090:Agrp ^@ http://purl.uniprot.org/uniprot/P56473|||http://purl.uniprot.org/uniprot/Q3UU47 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Region|||Signal Peptide|||Site ^@ Agouti|||Agouti domain-containing protein|||Agouti-related protein|||Cleavage; by PCSK1|||Interaction with melanocortin receptors ^@ http://purl.uniprot.org/annotation/PRO_0000001035|||http://purl.uniprot.org/annotation/PRO_0000434045|||http://purl.uniprot.org/annotation/PRO_5014309234 http://togogenome.org/gene/10090:Tmem223 ^@ http://purl.uniprot.org/uniprot/Q9CQE2 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Transmembrane protein 223 ^@ http://purl.uniprot.org/annotation/PRO_0000321834 http://togogenome.org/gene/10090:Prkacb ^@ http://purl.uniprot.org/uniprot/P68181 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Splice Variant ^@ AGC-kinase C-terminal|||Deamidated asparagine|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Removed|||cAMP-dependent protein kinase catalytic subunit beta ^@ http://purl.uniprot.org/annotation/PRO_0000086061|||http://purl.uniprot.org/annotation/VSP_017372|||http://purl.uniprot.org/annotation/VSP_017373|||http://purl.uniprot.org/annotation/VSP_017374|||http://purl.uniprot.org/annotation/VSP_017375|||http://purl.uniprot.org/annotation/VSP_017376 http://togogenome.org/gene/10090:Eya1 ^@ http://purl.uniprot.org/uniprot/F6YST4|||http://purl.uniprot.org/uniprot/P97767|||http://purl.uniprot.org/uniprot/Q6PAJ8|||http://purl.uniprot.org/uniprot/Q8C9D0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Eyes absent homolog 1|||In isoform 2.|||Markedly reduced sumoylation; when associated with R-43.|||Markedly reduced sumoylation; when associated with R-459.|||Nucleophile|||Polar residues|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000218644|||http://purl.uniprot.org/annotation/VSP_001487|||http://purl.uniprot.org/annotation/VSP_001488 http://togogenome.org/gene/10090:Reln ^@ http://purl.uniprot.org/uniprot/Q60841 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Abolishes ApoER2-binding.|||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|||Fails to assemble into disulfide-bonded multimers, while still exhibiting non-covalently associated high molecular weight oligomeric states in solution; retains binding to LRP8 and VLDR receptors but fails to show signaling activity.|||In isoform 2.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) asparagine|||Reelin ^@ http://purl.uniprot.org/annotation/PRO_0000030305|||http://purl.uniprot.org/annotation/VSP_005577|||http://purl.uniprot.org/annotation/VSP_005578 http://togogenome.org/gene/10090:Or8b3b ^@ http://purl.uniprot.org/uniprot/E9PVZ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ndufs7 ^@ http://purl.uniprot.org/uniprot/Q9DC70 ^@ Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Strand|||Transit Peptide|||Turn ^@ Disordered|||Mitochondrion|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000020028 http://togogenome.org/gene/10090:Reck ^@ http://purl.uniprot.org/uniprot/A2RSP9|||http://purl.uniprot.org/uniprot/Q9Z0J1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Turn ^@ 5 X Knot repeats|||Decreased interaction with ADGRA2.|||Does not affect interaction with ADGRA2.|||GPI-anchor amidated serine|||Kazal-like|||Kazal-like 1|||Kazal-like 2|||Kazal-like 2; degenerate|||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_0000016585|||http://purl.uniprot.org/annotation/PRO_0000016586|||http://purl.uniprot.org/annotation/PRO_5014296821 http://togogenome.org/gene/10090:Arl11 ^@ http://purl.uniprot.org/uniprot/Q6P3A9 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Sequence Conflict ^@ ADP-ribosylation factor-like protein 11|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207480 http://togogenome.org/gene/10090:Wdr81 ^@ http://purl.uniprot.org/uniprot/Q5ND34|||http://purl.uniprot.org/uniprot/Q6P8W0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Acidic residues|||BEACH|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Necessary and sufficient for the interaction with SQSTM1|||Polar residues|||Progressive ataxia associated with Purkinje cell death. Retinal thinning due to photoreceptor cell death.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat-containing protein 81 ^@ http://purl.uniprot.org/annotation/PRO_0000247245|||http://purl.uniprot.org/annotation/VSP_019956|||http://purl.uniprot.org/annotation/VSP_019957 http://togogenome.org/gene/10090:Or2n1b ^@ http://purl.uniprot.org/uniprot/Q8VG94 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tomm5 ^@ http://purl.uniprot.org/uniprot/B1AXP6 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Crosslink|||Modified Residue|||Splice Variant|||Transmembrane ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrial import receptor subunit TOM5 homolog|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000351151|||http://purl.uniprot.org/annotation/VSP_052943|||http://purl.uniprot.org/annotation/VSP_052944|||http://purl.uniprot.org/annotation/VSP_052945 http://togogenome.org/gene/10090:Cav1 ^@ http://purl.uniprot.org/uniprot/P49817 ^@ Chain|||Crosslink|||Experimental Information|||INTRAMEM|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain ^@ Chain|||Crosslink|||INTRAMEM|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain ^@ 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 isoform 2.|||Interaction with CAVIN3|||Interacts with SPRY1, SPRY2, SPRY3 and SPRY4|||Interacts with SPRY1, SPRY2, and SPRY4|||N-acetylserine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by ABL1 and INSR|||Removed|||Required for homooligomerization|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000004766|||http://purl.uniprot.org/annotation/VSP_018693 http://togogenome.org/gene/10090:Meox2 ^@ http://purl.uniprot.org/uniprot/P32443 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Homeobox|||Homeobox protein MOX-2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049198 http://togogenome.org/gene/10090:Ripply1 ^@ http://purl.uniprot.org/uniprot/Q2WG77 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Motif|||Region ^@ Acidic residues|||Disordered|||Pro residues|||Protein ripply1|||Ripply homology domain|||WRPW motif ^@ http://purl.uniprot.org/annotation/PRO_0000307757 http://togogenome.org/gene/10090:Ciao2a ^@ http://purl.uniprot.org/uniprot/Q9DCL2 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Cytosolic iron-sulfur assembly component 2A ^@ http://purl.uniprot.org/annotation/PRO_0000212690 http://togogenome.org/gene/10090:Btbd9 ^@ http://purl.uniprot.org/uniprot/A0A494B989|||http://purl.uniprot.org/uniprot/Q8C726 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ BACK|||BTB|||BTB/POZ domain-containing protein 9|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000186218 http://togogenome.org/gene/10090:Zfp708 ^@ http://purl.uniprot.org/uniprot/A0A087WPV0|||http://purl.uniprot.org/uniprot/F2Z422|||http://purl.uniprot.org/uniprot/F8VPP0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Fmc1 ^@ http://purl.uniprot.org/uniprot/Q9CR13 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Protein FMC1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000328781 http://togogenome.org/gene/10090:Gm10267 ^@ http://purl.uniprot.org/uniprot/M0QWD8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Kazal-like ^@ http://purl.uniprot.org/annotation/PRO_5004004042 http://togogenome.org/gene/10090:Tst ^@ http://purl.uniprot.org/uniprot/P52196|||http://purl.uniprot.org/uniprot/Q545S0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region ^@ Cysteine persulfide intermediate|||Hinge|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Phosphoserine|||Rhodanese|||Rhodanese 1|||Rhodanese 2|||Thiosulfate sulfurtransferase ^@ http://purl.uniprot.org/annotation/PRO_0000139396 http://togogenome.org/gene/10090:Vmn1r204 ^@ http://purl.uniprot.org/uniprot/I7HIK1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cmtm7 ^@ http://purl.uniprot.org/uniprot/Q9ESD6 ^@ 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_0000186111|||http://purl.uniprot.org/annotation/VSP_008267 http://togogenome.org/gene/10090:Cfc1 ^@ http://purl.uniprot.org/uniprot/P97766 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Cryptic protein|||EGF-like|||GPI-anchor amidated aspartate|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000044631|||http://purl.uniprot.org/annotation/PRO_0000395409 http://togogenome.org/gene/10090:Oser1 ^@ http://purl.uniprot.org/uniprot/Q9D722 ^@ 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 residues|||Disordered|||In strain: NOD.|||Oxidative stress-responsive serine-rich protein 1|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079454 http://togogenome.org/gene/10090:Klhl10 ^@ http://purl.uniprot.org/uniprot/B2RTD7|||http://purl.uniprot.org/uniprot/Q9D5V2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict ^@ BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 10|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000119113 http://togogenome.org/gene/10090:Lad1 ^@ http://purl.uniprot.org/uniprot/P57016 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ 6 X SEK repeats|||Basic and acidic residues|||Disordered|||Ladinin-1|||Phosphoserine|||Polar residues|||SEK 1|||SEK 2|||SEK 3|||SEK 4|||SEK 5|||SEK 6 ^@ http://purl.uniprot.org/annotation/PRO_0000084350 http://togogenome.org/gene/10090:Vmn1r39 ^@ http://purl.uniprot.org/uniprot/G3UWE6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Amd2 ^@ http://purl.uniprot.org/uniprot/D3Z6H8 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site ^@ Cleavage (non-hydrolytic); by autolysis|||Phosphoserine|||Proton acceptor; for processing activity|||Proton donor; for catalytic activity|||Pyruvic acid (Ser); by autocatalysis|||S-adenosylmethionine decarboxylase 2 alpha chain|||S-adenosylmethionine decarboxylase 2 beta chain|||Schiff-base intermediate with substrate; via pyruvic acid ^@ http://purl.uniprot.org/annotation/PRO_0000029965|||http://purl.uniprot.org/annotation/PRO_0000029966 http://togogenome.org/gene/10090:Slc39a8 ^@ http://purl.uniprot.org/uniprot/Q91W10 ^@ 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.|||Metal cation symporter ZIP8|||N-linked (GlcNAc...) asparagine|||XEXPHE-motif ^@ http://purl.uniprot.org/annotation/PRO_0000312708|||http://purl.uniprot.org/annotation/VSP_029886|||http://purl.uniprot.org/annotation/VSP_029887 http://togogenome.org/gene/10090:Abcd2 ^@ http://purl.uniprot.org/uniprot/Q61285 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||ATP-binding cassette sub-family D member 2|||Helical|||Interaction with PEX19|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000093307 http://togogenome.org/gene/10090:Apba2 ^@ http://purl.uniprot.org/uniprot/P98084 ^@ 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 ^@ Acidic residues|||Amyloid-beta A4 precursor protein-binding family A member 2|||Basic and acidic residues|||Disordered|||PDZ 1|||PDZ 2|||PID|||Phosphoserine|||Polar residues|||STXBP1-binding ^@ http://purl.uniprot.org/annotation/PRO_0000064617 http://togogenome.org/gene/10090:Steap3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1G9|||http://purl.uniprot.org/uniprot/E9QN92|||http://purl.uniprot.org/uniprot/Q8CI59 ^@ 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|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cleavage; by RHBDL4/RHBDD1|||Cytoplasmic|||Disordered|||Ferric oxidoreductase|||Helical|||In fragile-red; loss of endosomal membrane localization; 2-fold decrease in ferric-chelate reductase activity.|||In isoform 2.|||Loss of ferric-chelate reductase activity.|||Metalloreductase STEAP3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pyrroline-5-carboxylate reductase catalytic N-terminal|||Vesicular|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000285172|||http://purl.uniprot.org/annotation/VSP_024832 http://togogenome.org/gene/10090:Pon1 ^@ http://purl.uniprot.org/uniprot/P52430 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Not cleaved|||Proton acceptor|||Serum paraoxonase/arylesterase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000223282 http://togogenome.org/gene/10090:Smg5 ^@ http://purl.uniprot.org/uniprot/Q3UZS1|||http://purl.uniprot.org/uniprot/Q6ZPY2 ^@ 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|||Basic residues|||Disordered|||In isoform 2.|||In strain: B5/EGFP.|||In strain: Czech II.|||N-acetylserine|||Nonsense-mediated mRNA decay factor SMG5|||PIN|||PINc|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000076323|||http://purl.uniprot.org/annotation/VSP_016590|||http://purl.uniprot.org/annotation/VSP_016591 http://togogenome.org/gene/10090:Tor1aip2 ^@ http://purl.uniprot.org/uniprot/Q8BYU6|||http://purl.uniprot.org/uniprot/Q9ER81 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Interaction with TOR1A|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Torsin-1A-interacting protein 2|||Torsin-1A-interacting protein 2, isoform IFRG15 ^@ http://purl.uniprot.org/annotation/PRO_0000228839|||http://purl.uniprot.org/annotation/PRO_0000421072 http://togogenome.org/gene/10090:Mbtps1 ^@ http://purl.uniprot.org/uniprot/Q9WTZ2 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Charge relay system|||Cleavage; by autolysis|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Membrane-bound transcription factor site-1 protease|||N-linked (GlcNAc...) asparagine|||Peptidase S8|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000027053|||http://purl.uniprot.org/annotation/PRO_0000027054 http://togogenome.org/gene/10090:Gtf3c6 ^@ http://purl.uniprot.org/uniprot/Q9D8P7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||General transcription factor 3C polypeptide 6|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314059 http://togogenome.org/gene/10090:Slc16a2 ^@ http://purl.uniprot.org/uniprot/O70324|||http://purl.uniprot.org/uniprot/Q05BA2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 1|||2|||2 X 22 AA approximate tandem repeats|||Basic and acidic 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|||Major facilitator superfamily (MFS) profile|||Monocarboxylate transporter 8|||N-acetylalanine|||Phosphothreonine|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000211402 http://togogenome.org/gene/10090:Zfp68 ^@ http://purl.uniprot.org/uniprot/Q8BLK6|||http://purl.uniprot.org/uniprot/Q9Z116 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Duox2 ^@ http://purl.uniprot.org/uniprot/A0A494BAW1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||EF-hand|||FAD-binding FR-type|||Helical|||NAD(P)H oxidase (H2O2-forming)|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5019792486 http://togogenome.org/gene/10090:Hsd17b3 ^@ http://purl.uniprot.org/uniprot/P70385 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ 17-beta-hydroxysteroid dehydrogenase type 3|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054574 http://togogenome.org/gene/10090:Sympk ^@ http://purl.uniprot.org/uniprot/Q80X82 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ 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|||Interaction with HSF1|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Symplekin ^@ http://purl.uniprot.org/annotation/PRO_0000072386 http://togogenome.org/gene/10090:Arih2 ^@ http://purl.uniprot.org/uniprot/Q3TK92|||http://purl.uniprot.org/uniprot/Q9Z1K6 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ Acidic residues|||Ariadne domain|||Disordered|||E3 ubiquitin-protein ligase ARIH2|||IBR-type|||Phosphoserine|||RING-type|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain|||UBA-like ^@ http://purl.uniprot.org/annotation/PRO_0000055756 http://togogenome.org/gene/10090:Hcar1 ^@ http://purl.uniprot.org/uniprot/A0A4Y1JWM1|||http://purl.uniprot.org/uniprot/E9PZR8|||http://purl.uniprot.org/uniprot/Q8C131 ^@ 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|||Hydroxycarboxylic acid receptor 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069587 http://togogenome.org/gene/10090:Jag2 ^@ http://purl.uniprot.org/uniprot/Q9QYE5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein jagged-2 ^@ http://purl.uniprot.org/annotation/PRO_0000007630 http://togogenome.org/gene/10090:Vmn1r63 ^@ http://purl.uniprot.org/uniprot/Q9EPT1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rnf39 ^@ http://purl.uniprot.org/uniprot/A2RT81 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ B30.2/SPRY|||Disordered|||RING-type ^@ http://togogenome.org/gene/10090:Rhbdl3 ^@ http://purl.uniprot.org/uniprot/P58873 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Transmembrane ^@ EF-hand 1|||EF-hand 2|||Helical|||Nucleophile|||Rhomboid-related protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000206178 http://togogenome.org/gene/10090:Wdr3 ^@ http://purl.uniprot.org/uniprot/Q8BHB4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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 3 ^@ http://purl.uniprot.org/annotation/PRO_0000330941 http://togogenome.org/gene/10090:Crybg3 ^@ http://purl.uniprot.org/uniprot/A0A384DV78|||http://purl.uniprot.org/uniprot/Q80W49 ^@ 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 ^@ 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|||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 3|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000325759|||http://purl.uniprot.org/annotation/VSP_032387|||http://purl.uniprot.org/annotation/VSP_032388|||http://purl.uniprot.org/annotation/VSP_032389 http://togogenome.org/gene/10090:Slc45a3 ^@ http://purl.uniprot.org/uniprot/Q8K0H7 ^@ 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_0000122521 http://togogenome.org/gene/10090:Qrfp ^@ http://purl.uniprot.org/uniprot/Q8CE23 ^@ Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||Phenylalanine amide|||QRF-amide ^@ http://purl.uniprot.org/annotation/PRO_0000010088|||http://purl.uniprot.org/annotation/PRO_0000010089 http://togogenome.org/gene/10090:Or5g26 ^@ http://purl.uniprot.org/uniprot/Q9QY00 ^@ 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 5G26 ^@ http://purl.uniprot.org/annotation/PRO_0000150829 http://togogenome.org/gene/10090:Rtn1 ^@ http://purl.uniprot.org/uniprot/Q05CD8|||http://purl.uniprot.org/uniprot/Q4FJL2|||http://purl.uniprot.org/uniprot/Q4FZ95|||http://purl.uniprot.org/uniprot/Q7M6W1|||http://purl.uniprot.org/uniprot/Q8K0T0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Polar residues|||Reticulon|||Reticulon-1 ^@ http://purl.uniprot.org/annotation/PRO_0000168159 http://togogenome.org/gene/10090:Col9a1 ^@ http://purl.uniprot.org/uniprot/G3X995|||http://purl.uniprot.org/uniprot/Q05722|||http://purl.uniprot.org/uniprot/Q8BSQ4|||http://purl.uniprot.org/uniprot/Q8CEP0|||http://purl.uniprot.org/uniprot/Q9CT83|||http://purl.uniprot.org/uniprot/Q9D0D2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||Collagen alpha-1(IX) 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|||Collagen-like 9|||Disordered|||In isoform Short.|||Interchain|||Laminin G|||Laminin G domain-containing protein|||Laminin G-like|||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_0000005766|||http://purl.uniprot.org/annotation/PRO_5004307223|||http://purl.uniprot.org/annotation/PRO_5015091820|||http://purl.uniprot.org/annotation/PRO_5015099672|||http://purl.uniprot.org/annotation/VSP_001143|||http://purl.uniprot.org/annotation/VSP_001144 http://togogenome.org/gene/10090:2510009E07Rik ^@ http://purl.uniprot.org/uniprot/Q6GQU0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Polar residues|||UPF0524 protein C3orf70 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000319977 http://togogenome.org/gene/10090:Dusp14 ^@ http://purl.uniprot.org/uniprot/Q542U4|||http://purl.uniprot.org/uniprot/Q9JLY7 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Dual specificity protein phosphatase 14|||Phosphocysteine intermediate|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094823 http://togogenome.org/gene/10090:Zwint ^@ http://purl.uniprot.org/uniprot/Q9CQU5 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Interaction with NDC80 and ZW10|||Phosphoserine|||ZW10 interactor ^@ http://purl.uniprot.org/annotation/PRO_0000066595 http://togogenome.org/gene/10090:Gm2012 ^@ http://purl.uniprot.org/uniprot/B1B0R1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Tbx2 ^@ http://purl.uniprot.org/uniprot/Q3UET7|||http://purl.uniprot.org/uniprot/Q60707 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes phosphorylation.|||Attenuated repression of Adam10 transcription.|||Basic and acidic residues|||Disordered|||Phosphoserine|||Pro residues|||Repression domain 1 (RD1)|||T-box|||T-box transcription factor TBX2 ^@ http://purl.uniprot.org/annotation/PRO_0000184427 http://togogenome.org/gene/10090:Nos1ap ^@ http://purl.uniprot.org/uniprot/Q9D3A8 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein|||Disordered|||In isoform 2.|||Interaction with NOS1|||PDZ-binding|||PID|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000089317|||http://purl.uniprot.org/annotation/VSP_012462|||http://purl.uniprot.org/annotation/VSP_012463 http://togogenome.org/gene/10090:Cryzl2 ^@ http://purl.uniprot.org/uniprot/Q3UNZ8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ In isoform 2.|||N6-acetyllysine|||N6-succinyllysine|||Quinone oxidoreductase-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000341239|||http://purl.uniprot.org/annotation/VSP_034229|||http://purl.uniprot.org/annotation/VSP_034230 http://togogenome.org/gene/10090:Pde4b ^@ http://purl.uniprot.org/uniprot/B1AWD0|||http://purl.uniprot.org/uniprot/Q3TTI9|||http://purl.uniprot.org/uniprot/Q6IQY6|||http://purl.uniprot.org/uniprot/Q80VK8|||http://purl.uniprot.org/uniprot/Q8VBU5 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PDEase|||Phosphodiesterase 4 upstream conserved regions (UCR)|||Proton donor ^@ http://togogenome.org/gene/10090:Hic2 ^@ http://purl.uniprot.org/uniprot/Q9JLZ6 ^@ 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 ^@ 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_0000046946|||http://purl.uniprot.org/annotation/VSP_010499 http://togogenome.org/gene/10090:Tex11 ^@ http://purl.uniprot.org/uniprot/Q14AT2 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Testis-expressed protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000296956|||http://purl.uniprot.org/annotation/VSP_027262|||http://purl.uniprot.org/annotation/VSP_027263 http://togogenome.org/gene/10090:Dcaf8l ^@ http://purl.uniprot.org/uniprot/A2AHY8 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ Acidic residues|||Disordered|||Polar residues|||WD ^@ http://togogenome.org/gene/10090:Or13p10 ^@ http://purl.uniprot.org/uniprot/L7MU75 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tgoln1 ^@ http://purl.uniprot.org/uniprot/Q4FJY3|||http://purl.uniprot.org/uniprot/Q62313 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 1|||2|||3|||4|||5|||6|||6 X 8 AA tandem repeats|||Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Endocytosis signal|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Trans-Golgi network integral membrane protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000022485|||http://purl.uniprot.org/annotation/PRO_5014309366 http://togogenome.org/gene/10090:Arglu1 ^@ http://purl.uniprot.org/uniprot/Q3UL36 ^@ 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.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000288439|||http://purl.uniprot.org/annotation/VSP_025675|||http://purl.uniprot.org/annotation/VSP_025676 http://togogenome.org/gene/10090:Ccnd2 ^@ http://purl.uniprot.org/uniprot/P30280|||http://purl.uniprot.org/uniprot/Q4FK45 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Cyclin N-terminal|||Disordered|||G1/S-specific cyclin-D2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080438 http://togogenome.org/gene/10090:Gadd45a ^@ http://purl.uniprot.org/uniprot/P48316|||http://purl.uniprot.org/uniprot/Q3UMH6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Growth arrest and DNA damage-inducible protein GADD45 alpha|||Phosphothreonine|||Ribosomal protein eL8/eL30/eS12/Gadd45 ^@ http://purl.uniprot.org/annotation/PRO_0000148332 http://togogenome.org/gene/10090:Klra2 ^@ http://purl.uniprot.org/uniprot/A0FK58|||http://purl.uniprot.org/uniprot/E9Q433|||http://purl.uniprot.org/uniprot/Q9D3R1 ^@ Coiled-Coil|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ C-type lectin|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Asic3 ^@ http://purl.uniprot.org/uniprot/Q6X1Y6 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acid-sensing ion channel 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Potassium ion selectivity and permeability ^@ http://purl.uniprot.org/annotation/PRO_0000181302|||http://purl.uniprot.org/annotation/VSP_015606|||http://purl.uniprot.org/annotation/VSP_015607 http://togogenome.org/gene/10090:Gabrr3 ^@ http://purl.uniprot.org/uniprot/B2RXA8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_5015087165 http://togogenome.org/gene/10090:Cdadc1 ^@ http://purl.uniprot.org/uniprot/G3UW39|||http://purl.uniprot.org/uniprot/Q8BMD5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Bipartite nuclear localization signal|||CMP/dCMP-type deaminase|||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.|||In isoform 6.|||Nuclear export signal|||Polar residues|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000300493|||http://purl.uniprot.org/annotation/VSP_027817|||http://purl.uniprot.org/annotation/VSP_027818|||http://purl.uniprot.org/annotation/VSP_027819|||http://purl.uniprot.org/annotation/VSP_027820|||http://purl.uniprot.org/annotation/VSP_027821|||http://purl.uniprot.org/annotation/VSP_027822|||http://purl.uniprot.org/annotation/VSP_027823|||http://purl.uniprot.org/annotation/VSP_027824 http://togogenome.org/gene/10090:Tspyl5 ^@ http://purl.uniprot.org/uniprot/Q69ZB3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Testis-specific Y-encoded-like protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000307278 http://togogenome.org/gene/10090:H2-D1 ^@ http://purl.uniprot.org/uniprot/P01899|||http://purl.uniprot.org/uniprot/Q792Z7 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Disordered|||Extracellular|||Glycyl serine ester (Ser-Gly) (interchain with G-Cter in ubiquitin); alternate|||H-2 class I histocompatibility antigen, D-B alpha chain|||Helical|||Ig-like|||Ig-like C1-type|||In K-less, no effect on ubiquitination; when associated with R-55, R-155, R-170, R-197, R-210, R-220, R-267 and R-277.|||In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-210, R-220 and R-267.|||In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-210, R-220 and R-277.|||In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-210, R-267 and R-277.|||In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-197, R-220, R-267 and R-277.|||In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-170, R-210, R-220, R-267 and R-277.|||In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-155, R-197, R-210, R-220, R-267 and R-277.|||In K-less, no effect on ubiquitination; when associated with R-55, R-92, R-170, R-197, R-210, R-220, R-267 and R-277.|||In K-less, no effect on ubiquitination; when associated with R-92, R-155, R-170, R-197, R-210, R-220, R-267 and R-277.|||In Ld KCST-less, strongly impairs ubiquitination; when associated with I-337; R-340; 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores ubiquitination; when associated I-337; R-340; 350-A--A-352; A-356 and 360-R-R-361.|||In Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337 and 360-R-R-361.|||In Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337; 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; 350-A--A-352; A-356 and 360-R-R-361.|||In Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; I-337; R-340 and 350-A--A-356. In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340; 350-A--A-352; A-356 and 360-R-R-361.|||In Ld KCST-less, strongly impairs ubiquitination; when associated with R-332; R-340; 350-A--A-356 and 360-R-R-361. In Ld tail 1S, restores ubiquitination; when associated R-332; R-340; 350-A--A-352; A-356 and 360-R-R-361.|||In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340 and A-356.|||In Ld tail 1S, restores ubiquitination; when associated R-332; I-337; R-340; A-356 and 360-R-R-361.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000018923|||http://purl.uniprot.org/annotation/PRO_5014310802 http://togogenome.org/gene/10090:Lce3e ^@ http://purl.uniprot.org/uniprot/F8VQJ0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Azin2 ^@ http://purl.uniprot.org/uniprot/A8Y5E7|||http://purl.uniprot.org/uniprot/B2RSR5|||http://purl.uniprot.org/uniprot/Q6P078|||http://purl.uniprot.org/uniprot/Q8BVM4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Antizyme inhibitor 2|||Disordered|||Does not inhibit interaction with OAZ1.|||Does not inhibit interaction with OAZ1. Reduces interaction with OAZ1; when associated with A-116. Strongly reduces interaction with OAZ1 and unable to abrogate the inhibitory effect of OAZ1 on ornithine decarboxylase (ODC) activity and polyamine uptake; when associated with A-139 and A-140.|||Does not inhibit interaction with OAZ1. Reduces interaction with OAZ1; when associated with A-142.|||Necessary for polyamine uptake stimulation|||Orn/DAP/Arg decarboxylase 2 C-terminal|||Orn/DAP/Arg decarboxylase 2 N-terminal|||Strongly reduces interaction with OAZ1 and unable to abrogate both the inhibitory effect of OAZ1 on ornithine decarboxylase (ODC) activity and polyamine uptake; when associated with A-139 and A-142.|||Strongly reduces interaction with OAZ1 and unable to abrogate both the inhibitory effect of OAZ1 on ornithine decarboxylase (ODC) activity and polyamine uptake; when associated with A-140 and A-142. ^@ http://purl.uniprot.org/annotation/PRO_0000149945 http://togogenome.org/gene/10090:Spink8 ^@ http://purl.uniprot.org/uniprot/Q09TK9|||http://purl.uniprot.org/uniprot/Q8C1F8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Site ^@ Kazal-like|||Reactive bond|||Serine protease inhibitor Kazal-type 8 ^@ http://purl.uniprot.org/annotation/PRO_0000302140|||http://purl.uniprot.org/annotation/PRO_5015099060 http://togogenome.org/gene/10090:Mdm1 ^@ http://purl.uniprot.org/uniprot/B2RPU6|||http://purl.uniprot.org/uniprot/B7SNM8|||http://purl.uniprot.org/uniprot/E9PW14|||http://purl.uniprot.org/uniprot/E9Q0B1|||http://purl.uniprot.org/uniprot/Q9D067 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nuclear protein MDM1|||Phosphoserine|||Polar 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|||ST]-E-Y-X(3)-F motif 4; required for efficient microtubule binding and stabilization ^@ http://purl.uniprot.org/annotation/PRO_0000299060|||http://purl.uniprot.org/annotation/VSP_027548|||http://purl.uniprot.org/annotation/VSP_027549|||http://purl.uniprot.org/annotation/VSP_027550|||http://purl.uniprot.org/annotation/VSP_027551|||http://purl.uniprot.org/annotation/VSP_027552 http://togogenome.org/gene/10090:Zpr1 ^@ http://purl.uniprot.org/uniprot/Q62384 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger ^@ Chain|||Helix|||Region|||Strand|||Turn|||Zinc Finger ^@ C4-type 1|||C4-type 2|||Disordered|||Zinc finger protein ZPR1 ^@ http://purl.uniprot.org/annotation/PRO_0000119037 http://togogenome.org/gene/10090:Dbx1 ^@ http://purl.uniprot.org/uniprot/P52950 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000048864 http://togogenome.org/gene/10090:Snx24 ^@ http://purl.uniprot.org/uniprot/Q9CRB0 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ N-acetylmethionine|||PX|||Phosphoserine|||Sorting nexin-24 ^@ http://purl.uniprot.org/annotation/PRO_0000213873 http://togogenome.org/gene/10090:Gfral ^@ http://purl.uniprot.org/uniprot/Q6SJE0 ^@ 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|||Extracellular|||GDNF family receptor alpha-like|||Helical|||In isoform B.|||N-linked (GlcNAc...) asparagine|||Required for interaction with GDF15 ^@ http://purl.uniprot.org/annotation/PRO_0000240125|||http://purl.uniprot.org/annotation/VSP_019295|||http://purl.uniprot.org/annotation/VSP_019296 http://togogenome.org/gene/10090:Adamts4 ^@ http://purl.uniprot.org/uniprot/Q8BNJ2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ A disintegrin and metalloproteinase with thrombospondin motifs 4|||Cysteine switch|||Disintegrin|||Disordered|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Polar residues|||Spacer|||TSP type-1|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029166|||http://purl.uniprot.org/annotation/PRO_0000029167 http://togogenome.org/gene/10090:Hnrnpa1 ^@ http://purl.uniprot.org/uniprot/P49312|||http://purl.uniprot.org/uniprot/Q5EBP8 ^@ 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 ^@ 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 isoform Short.|||N-acetylmethionine|||N-acetylserine; in Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed|||N6-acetyllysine; alternate|||Nuclear targeting sequence|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by MKNK2|||Polar residues|||RNA-binding RGG-box|||RRM|||RRM 1|||RRM 2|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000081830|||http://purl.uniprot.org/annotation/PRO_0000424511|||http://purl.uniprot.org/annotation/VSP_005825 http://togogenome.org/gene/10090:Eme2 ^@ http://purl.uniprot.org/uniprot/Q56A04 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Probable crossover junction endonuclease EME2 ^@ http://purl.uniprot.org/annotation/PRO_0000317374 http://togogenome.org/gene/10090:Shisa8 ^@ http://purl.uniprot.org/uniprot/J3QNX5 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protein shisa-8 ^@ http://purl.uniprot.org/annotation/PRO_5011942382 http://togogenome.org/gene/10090:Zfta ^@ http://purl.uniprot.org/uniprot/Q4VA45|||http://purl.uniprot.org/uniprot/Q6PCY2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Pro residues|||SPIN-DOC-like zinc-finger|||Zinc finger translocation-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000393910 http://togogenome.org/gene/10090:Evpl ^@ http://purl.uniprot.org/uniprot/Q9D952 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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_0000078148 http://togogenome.org/gene/10090:Khdrbs1 ^@ http://purl.uniprot.org/uniprot/Q60749 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes phosphorylation, abolishes CD44 splicing regulation; when associated with A-58 and A-71.|||Abolishes phosphorylation, abolishes CD44 splicing regulation; when associated with A-58 and A-84.|||Abolishes phosphorylation, abolishes CD44 splicing regulation; when associated with A-71 and A-84.|||Abolishes splicing regulation.|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Asymmetric dimethylarginine; by PRMT1|||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|||Interaction with HNRNPA1|||Interaction with ZBTB7A|||Involved in homodimerization|||KH|||KH domain-containing, RNA-binding, signal transduction-associated protein 1|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Omega-N-methylarginine; by PRMT1|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by MAPK1|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Phosphotyrosine|||Phosphotyrosine; by PTK6 ^@ http://purl.uniprot.org/annotation/PRO_0000050125 http://togogenome.org/gene/10090:Metap1 ^@ http://purl.uniprot.org/uniprot/Q4VAA9|||http://purl.uniprot.org/uniprot/Q8BP48 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Zinc Finger ^@ C6H2-type|||MYND-like zinc finger|||Methionine aminopeptidase 1|||N-acetylalanine|||Peptidase M24|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000148968 http://togogenome.org/gene/10090:Derl2 ^@ http://purl.uniprot.org/uniprot/Q3U957|||http://purl.uniprot.org/uniprot/Q8BNI4 ^@ 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|||Derlin-2|||Disordered|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In isoform 2.|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000219046|||http://purl.uniprot.org/annotation/VSP_011085 http://togogenome.org/gene/10090:Or5h23 ^@ http://purl.uniprot.org/uniprot/L7N1Z8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kdm4b ^@ http://purl.uniprot.org/uniprot/Q91VY5 ^@ Binding Site|||Chain|||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|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||In isoform 2.|||JmjC|||JmjN|||Lysine-specific demethylase 4B|||N6-acetyllysine|||PHD-type 1|||PHD-type 2|||Pro residues|||Tudor 1|||Tudor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000183176|||http://purl.uniprot.org/annotation/VSP_018309|||http://purl.uniprot.org/annotation/VSP_018310 http://togogenome.org/gene/10090:Gtf2b ^@ http://purl.uniprot.org/uniprot/P62915|||http://purl.uniprot.org/uniprot/Q3ULN2 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Zinc Finger ^@ 1|||2|||Core promoter DNA-binding|||N6-acetyllysine; by autocatalysis|||Necessary for TATA box-bound TBP complex formation|||Phosphoserine|||TFIIB-type|||Transcription initiation factor IIB ^@ http://purl.uniprot.org/annotation/PRO_0000119294 http://togogenome.org/gene/10090:Chac2 ^@ http://purl.uniprot.org/uniprot/Q9CQG1 ^@ 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.|||Proton acceptor|||Putative glutathione-specific gamma-glutamylcyclotransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000314913|||http://purl.uniprot.org/annotation/VSP_030429 http://togogenome.org/gene/10090:Pspn ^@ http://purl.uniprot.org/uniprot/A1L3Q1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_5015085919 http://togogenome.org/gene/10090:Lrrc2 ^@ http://purl.uniprot.org/uniprot/Q8VDB8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ 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_0000084492 http://togogenome.org/gene/10090:Morf4l1 ^@ http://purl.uniprot.org/uniprot/P60762|||http://purl.uniprot.org/uniprot/Q569V4 ^@ 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 ^@ Chromo|||Disordered|||In isoform 2.|||Interaction with KAT8|||Interaction with RB1-1|||Interaction with RB1-2|||MRG|||Mortality factor 4-like protein 1|||N6-acetyllysine|||Nuclear localization signal|||Polar residues|||Sufficient for interaction with PHF12|||Sufficient for interaction with SIN3A|||Tudor-knot ^@ http://purl.uniprot.org/annotation/PRO_0000088765|||http://purl.uniprot.org/annotation/VSP_012890 http://togogenome.org/gene/10090:Trmt1l ^@ http://purl.uniprot.org/uniprot/A0A0R4J0U8|||http://purl.uniprot.org/uniprot/A2RSY6 ^@ 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|||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|||TRMT1-like protein|||Trm1 methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000317570|||http://purl.uniprot.org/annotation/VSP_031044|||http://purl.uniprot.org/annotation/VSP_031045|||http://purl.uniprot.org/annotation/VSP_031046|||http://purl.uniprot.org/annotation/VSP_031047 http://togogenome.org/gene/10090:Scpep1 ^@ http://purl.uniprot.org/uniprot/Q920A5 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Retinoid-inducible serine carboxypeptidase ^@ http://purl.uniprot.org/annotation/PRO_0000004285 http://togogenome.org/gene/10090:Hbb-y ^@ http://purl.uniprot.org/uniprot/P02104|||http://purl.uniprot.org/uniprot/Q9CR49 ^@ 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 ^@ Globin family profile|||Hemoglobin subunit epsilon-Y2|||Phosphoserine|||Removed|||distal binding residue|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000053219 http://togogenome.org/gene/10090:Carf ^@ http://purl.uniprot.org/uniprot/A8VI08|||http://purl.uniprot.org/uniprot/Q8VHI4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Calcium-responsive transcription factor|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000076173 http://togogenome.org/gene/10090:Mark1 ^@ http://purl.uniprot.org/uniprot/Q14DQ3|||http://purl.uniprot.org/uniprot/Q8VHJ5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||KA1|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphothreonine|||Phosphothreonine; by LKB1 and TAOK1|||Phosphothreonine; by PKC/PRKCZ|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase MARK1|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000086299 http://togogenome.org/gene/10090:Gm3383 ^@ http://purl.uniprot.org/uniprot/A6NAR8|||http://purl.uniprot.org/uniprot/A6NAV5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cyp24a1 ^@ http://purl.uniprot.org/uniprot/Q64441 ^@ Binding Site|||Chain|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Transit Peptide ^@ 1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial|||Mitochondrion|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000003616 http://togogenome.org/gene/10090:Bcl9 ^@ http://purl.uniprot.org/uniprot/Q9D219 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||B-cell CLL/lymphoma 9 protein|||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_0000064886 http://togogenome.org/gene/10090:Tubb6 ^@ http://purl.uniprot.org/uniprot/Q3UMM1|||http://purl.uniprot.org/uniprot/Q922F4 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif ^@ 5-glutamyl polyglutamate|||MREI motif|||Phosphoserine; by CDK1|||Tubulin beta-6 chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase ^@ http://purl.uniprot.org/annotation/PRO_0000048256 http://togogenome.org/gene/10090:Cenpt ^@ http://purl.uniprot.org/uniprot/Q3TJM4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Centromere protein T|||Disordered|||Flexible stalk domain|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000249516 http://togogenome.org/gene/10090:Hbs1l ^@ http://purl.uniprot.org/uniprot/L7N209|||http://purl.uniprot.org/uniprot/Q3TGM7|||http://purl.uniprot.org/uniprot/Q69ZS7 ^@ 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|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Turn ^@ Disordered|||G1|||G2|||G3|||G4|||G5|||HBS1-like protein|||HBS1-like protein N-terminal|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tr-type G|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000091492|||http://purl.uniprot.org/annotation/VSP_013626|||http://purl.uniprot.org/annotation/VSP_013627|||http://purl.uniprot.org/annotation/VSP_013628 http://togogenome.org/gene/10090:Il31 ^@ http://purl.uniprot.org/uniprot/Q6EAL8 ^@ 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_0000274571 http://togogenome.org/gene/10090:Syne2 ^@ http://purl.uniprot.org/uniprot/Q6ZWQ0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Actin-binding|||Basic and acidic residues|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||Impairs interaction with F-actin; when assocoated with A-128.|||Impairs interaction with F-actin; when assocoated with A-131.|||In isoform 2.|||In isoform 3.|||Interchain (with C-577 in SUN2); alternate|||Interchain (with C-759 in SUN1); alternate|||KASH|||Nesprin-2|||Perinuclear space|||Phosphoserine|||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 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||Sufficient for interaction with SUN2 ^@ http://purl.uniprot.org/annotation/PRO_0000392210|||http://purl.uniprot.org/annotation/VSP_038799|||http://purl.uniprot.org/annotation/VSP_038800|||http://purl.uniprot.org/annotation/VSP_038801|||http://purl.uniprot.org/annotation/VSP_038802 http://togogenome.org/gene/10090:Ptk6 ^@ http://purl.uniprot.org/uniprot/Q05AA8|||http://purl.uniprot.org/uniprot/Q64434 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Increase in the kinase activation level.|||Linker|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Protein-tyrosine kinase 6|||Proton acceptor|||SH2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000088134 http://togogenome.org/gene/10090:Myh1 ^@ http://purl.uniprot.org/uniprot/Q5SX40 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region ^@ Actin-binding|||Disordered|||IQ|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-1|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pros-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000123392 http://togogenome.org/gene/10090:Gpnmb ^@ http://purl.uniprot.org/uniprot/Q99P91 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cell attachment site|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||PKD|||Phosphoserine|||Pro residues|||Transmembrane glycoprotein NMB ^@ http://purl.uniprot.org/annotation/PRO_0000024710 http://togogenome.org/gene/10090:Eif1a ^@ http://purl.uniprot.org/uniprot/Q4FJR7|||http://purl.uniprot.org/uniprot/Q60872 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Eukaryotic translation initiation factor 1A|||S1-like ^@ http://purl.uniprot.org/annotation/PRO_0000145106 http://togogenome.org/gene/10090:Mmp15 ^@ http://purl.uniprot.org/uniprot/O54732 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Motif|||Propeptide|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cysteine switch|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Matrix metalloproteinase-15|||N-linked (GlcNAc...) asparagine|||Pro residues|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028810|||http://purl.uniprot.org/annotation/PRO_0000028811 http://togogenome.org/gene/10090:Kif1c ^@ http://purl.uniprot.org/uniprot/O35071|||http://purl.uniprot.org/uniprot/Q3V3Y9|||http://purl.uniprot.org/uniprot/Q8VI89 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||FHA|||Kinesin motor|||Kinesin-like protein KIF1C|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000125411 http://togogenome.org/gene/10090:Nrarp ^@ http://purl.uniprot.org/uniprot/Q91ZA8 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Repeat|||Splice Variant ^@ ANK 1|||ANK 2|||In isoform 2.|||Notch-regulated ankyrin repeat-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000325080|||http://purl.uniprot.org/annotation/VSP_032380|||http://purl.uniprot.org/annotation/VSP_032381 http://togogenome.org/gene/10090:Mis18bp1 ^@ http://purl.uniprot.org/uniprot/Q80WQ8 ^@ 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.|||In isoform 3.|||Mis18-binding protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||SANT|||SANTA ^@ http://purl.uniprot.org/annotation/PRO_0000379895|||http://purl.uniprot.org/annotation/VSP_037731|||http://purl.uniprot.org/annotation/VSP_037732|||http://purl.uniprot.org/annotation/VSP_037733 http://togogenome.org/gene/10090:Rfc2 ^@ http://purl.uniprot.org/uniprot/Q4KL82|||http://purl.uniprot.org/uniprot/Q9WUK4 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ AAA+ ATPase|||Disordered|||N-acetylmethionine|||N6-acetyllysine|||Replication factor C subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000121767 http://togogenome.org/gene/10090:Pate9 ^@ http://purl.uniprot.org/uniprot/Q3UW02 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015097519 http://togogenome.org/gene/10090:Lemd2 ^@ http://purl.uniprot.org/uniprot/Q6DVA0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Interaction with lamin A/C complexes|||LEM|||LEM domain-containing protein 2|||N-acetylalanine|||Phosphoserine|||Reduced Lemd2 protein levels. Disorganization of heterochromatin associated with the nuclear envelope in cardiomyocytes. Increased DNA double-strand breaks in the heart. Dilation of the atrial and ventricular chambers, severe systolic dysfunction and cardiac fibrosis leading to premature death. No defects in skeletal muscle observed.|||Removed|||Required for nuclear retention and interaction with LMNA isoform C|||Winged-Helix (WH) ^@ http://purl.uniprot.org/annotation/PRO_0000285250 http://togogenome.org/gene/10090:Lactb ^@ http://purl.uniprot.org/uniprot/B2RWI2|||http://purl.uniprot.org/uniprot/Q9EP89 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Transit Peptide|||Transmembrane ^@ Acyl-ester intermediate|||Basic and acidic residues|||Beta-lactamase-related|||Disordered|||Helical|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Polar residues|||Serine beta-lactamase-like protein LACTB, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000195477 http://togogenome.org/gene/10090:Chchd1 ^@ http://purl.uniprot.org/uniprot/Q9CQA6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Motif|||Region ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||Polar residues|||Small ribosomal subunit protein mS37 ^@ http://purl.uniprot.org/annotation/PRO_0000129159 http://togogenome.org/gene/10090:Folh1 ^@ http://purl.uniprot.org/uniprot/O35409|||http://purl.uniprot.org/uniprot/Q0VDM6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Charge relay system|||Cytoplasmic|||Extracellular|||Glutamate carboxypeptidase 2|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||NAALADase|||Nucleophile; for NAALADase activity|||PA|||Peptidase M28|||Phosphoserine|||Transferrin receptor-like dimerisation ^@ http://purl.uniprot.org/annotation/PRO_0000174118 http://togogenome.org/gene/10090:Or10ab5 ^@ http://purl.uniprot.org/uniprot/Q8VF20 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zbtb12 ^@ http://purl.uniprot.org/uniprot/Q9Z150 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB|||C2H2-type|||Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Cib2 ^@ http://purl.uniprot.org/uniprot/Q544Z8|||http://purl.uniprot.org/uniprot/Q9Z309 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site ^@ Calcium and integrin-binding family member 2|||Causes deafness; decreases interaction with TMC1 and TMC2; abolishes localization of TMC1 to stereocilia; reduces localization of TMC2 to stereocilia; reduces calcium permeability and conductance of MET channels in hair cells.|||Causes deafness; decreases interaction with TMC1 and TMC2; reduces MET currents.|||Causes deafness; disrupts interaction with TMC1 and TMC2; abolishes MET currents; abolishes localization of TMC1 and TMC2 to stereocilia.|||Causes profound deafness. Does not disrupt localization in hair cell stereocilia. No obvious indications of vestibular dysfunction.|||Disrupts interaction with TMC1.|||Disrupts interaction with TMC1. Disrupts mechanoelectrical transduction (MET) in hair cells.|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Weakens interaction with TMC1. ^@ http://purl.uniprot.org/annotation/PRO_0000073535 http://togogenome.org/gene/10090:Prcd ^@ http://purl.uniprot.org/uniprot/Q00LT2 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Lipid Binding|||Mutagenesis Site|||Region ^@ Disordered|||Loss of N-terminal lipidation. Fails to localize to the photoreceptor outer segment.|||Photoreceptor disk component PRCD|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000280354 http://togogenome.org/gene/10090:Rab4a ^@ http://purl.uniprot.org/uniprot/P56371 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict ^@ 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_0000121094 http://togogenome.org/gene/10090:Ube2j2 ^@ http://purl.uniprot.org/uniprot/B0QZM1|||http://purl.uniprot.org/uniprot/B1ASK8|||http://purl.uniprot.org/uniprot/Q6P073 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Glycyl thioester intermediate|||Helical|||Helical; Anchor for type IV membrane protein|||Loss of catalytic activity. Slows down degradation of misfolded proteins from the ER.|||Lumenal|||Polar residues|||UBC core|||Ubiquitin-conjugating enzyme E2 J2 ^@ http://purl.uniprot.org/annotation/PRO_0000082597 http://togogenome.org/gene/10090:Ppm1a ^@ http://purl.uniprot.org/uniprot/P49443|||http://purl.uniprot.org/uniprot/Q9EQE3 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue ^@ N-myristoyl glycine|||PPM-type phosphatase|||Phosphoserine|||Protein phosphatase 1A|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057742 http://togogenome.org/gene/10090:Sh3rf3 ^@ http://purl.uniprot.org/uniprot/Q8C120 ^@ 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 ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase SH3RF3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with RAC1|||Phosphoserine|||Polar residues|||RING-type|||SH3 1|||SH3 2|||SH3 3|||SH3 4 ^@ http://purl.uniprot.org/annotation/PRO_0000284884|||http://purl.uniprot.org/annotation/VSP_024718|||http://purl.uniprot.org/annotation/VSP_024719|||http://purl.uniprot.org/annotation/VSP_024720|||http://purl.uniprot.org/annotation/VSP_024721|||http://purl.uniprot.org/annotation/VSP_024722|||http://purl.uniprot.org/annotation/VSP_024723|||http://purl.uniprot.org/annotation/VSP_024724|||http://purl.uniprot.org/annotation/VSP_024725 http://togogenome.org/gene/10090:Or7e174 ^@ http://purl.uniprot.org/uniprot/Q8VFI8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Csgalnact2 ^@ http://purl.uniprot.org/uniprot/Q8C1F4 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chondroitin sulfate N-acetylgalactosaminyltransferase 2|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000189567 http://togogenome.org/gene/10090:Adh5 ^@ http://purl.uniprot.org/uniprot/P28474|||http://purl.uniprot.org/uniprot/Q6P5I3 ^@ 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|||Site ^@ Alcohol dehydrogenase class-3|||Alcohol dehydrogenase-like C-terminal|||Alcohol dehydrogenase-like N-terminal|||Important for FDH activity and activation by fatty acids|||N-acetylalanine|||N6-succinyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000160760 http://togogenome.org/gene/10090:Ifi44 ^@ http://purl.uniprot.org/uniprot/Q8BV66 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Interferon-induced protein 44|||TLDc ^@ http://purl.uniprot.org/annotation/PRO_0000337871 http://togogenome.org/gene/10090:Gpr180 ^@ http://purl.uniprot.org/uniprot/Q8BPS4 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Helical|||Integral membrane protein GPR180|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000239663 http://togogenome.org/gene/10090:Miga2 ^@ http://purl.uniprot.org/uniprot/Q8BK03 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||FFAT|||Helical|||In isoform 2.|||Mitoguardin 2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000313659|||http://purl.uniprot.org/annotation/VSP_030093|||http://purl.uniprot.org/annotation/VSP_030094 http://togogenome.org/gene/10090:Scn5a ^@ http://purl.uniprot.org/uniprot/A0A0R4J1M7|||http://purl.uniprot.org/uniprot/K3W4N7|||http://purl.uniprot.org/uniprot/Q8C3I3|||http://purl.uniprot.org/uniprot/Q9JJV9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Dimethylated arginine; alternate|||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 isoform 2.|||Interaction with FGF13|||Interaction with NEDD4, NEDD4L and WWP2|||Ion transport|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues|||Pore-forming|||Sodium channel protein type 5 subunit alpha|||Sodium ion transport-associated|||Voltage-gated Na+ ion channel cytoplasmic ^@ http://purl.uniprot.org/annotation/PRO_0000376895|||http://purl.uniprot.org/annotation/VSP_037444 http://togogenome.org/gene/10090:Zswim1 ^@ http://purl.uniprot.org/uniprot/Q9CWV7 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Region|||Zinc Finger ^@ Disordered|||SWIM-type|||Zinc finger SWIM domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000223096 http://togogenome.org/gene/10090:Olfm5 ^@ http://purl.uniprot.org/uniprot/Q8BU90 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Olfactomedin-like ^@ http://purl.uniprot.org/annotation/PRO_5015099034 http://togogenome.org/gene/10090:Nmb ^@ http://purl.uniprot.org/uniprot/D3Z621|||http://purl.uniprot.org/uniprot/Q9CR53 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Chain|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide ^@ Methionine amide|||Neuromedin-B|||Neuromedin-B-32 ^@ http://purl.uniprot.org/annotation/PRO_0000003020|||http://purl.uniprot.org/annotation/PRO_0000003021|||http://purl.uniprot.org/annotation/PRO_0000003022|||http://purl.uniprot.org/annotation/PRO_5003052632 http://togogenome.org/gene/10090:Vmo1 ^@ http://purl.uniprot.org/uniprot/Q5SXG7 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Vitelline membrane outer layer protein 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000036408 http://togogenome.org/gene/10090:Defa3 ^@ http://purl.uniprot.org/uniprot/P28310 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Alpha-defensin 3|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000006821|||http://purl.uniprot.org/annotation/PRO_0000006822 http://togogenome.org/gene/10090:Gje1 ^@ http://purl.uniprot.org/uniprot/Q9CX92 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Gap junction epsilon-1 protein|||Helical|||In Aey12; dominant negative mutation. Viable and fertile with a small eye phenotype. The lens is absent and only the lens envelope remains. The retina is misfolded and poorly differentiated. Heterozygotes show variable degrees of lens opacity and abnormal primary lens fiber elongation. Defects are apparent from embryonic stage 12.5 dpc onwards. ^@ http://purl.uniprot.org/annotation/PRO_0000317612 http://togogenome.org/gene/10090:Ott ^@ http://purl.uniprot.org/uniprot/Q62012 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tmem130 ^@ http://purl.uniprot.org/uniprot/Q6NXM3 ^@ 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|||Helical|||N-linked (GlcNAc...) asparagine|||PKD|||Transmembrane protein 130 ^@ http://purl.uniprot.org/annotation/PRO_0000278277 http://togogenome.org/gene/10090:Aadacl2fm2 ^@ http://purl.uniprot.org/uniprot/W4VSP6 ^@ Active Site|||Domain Extent|||Region|||Site|||Transmembrane ^@ Active Site|||Domain Extent|||Transmembrane ^@ Alpha/beta hydrolase fold-3|||Helical ^@ http://togogenome.org/gene/10090:Helq ^@ http://purl.uniprot.org/uniprot/Q2VPA6 ^@ 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|||Helicase POLQ-like|||In isoform 2.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000329061|||http://purl.uniprot.org/annotation/VSP_032949|||http://purl.uniprot.org/annotation/VSP_032950|||http://purl.uniprot.org/annotation/VSP_032951|||http://purl.uniprot.org/annotation/VSP_032952 http://togogenome.org/gene/10090:Spdl1 ^@ http://purl.uniprot.org/uniprot/Q923A2 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylmethionine|||Phosphoserine|||Protein Spindly ^@ http://purl.uniprot.org/annotation/PRO_0000274518 http://togogenome.org/gene/10090:Plekhs1 ^@ http://purl.uniprot.org/uniprot/Q8BW88 ^@ 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 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Pleckstrin homology domain-containing family S member 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000320676|||http://purl.uniprot.org/annotation/VSP_031732|||http://purl.uniprot.org/annotation/VSP_031733|||http://purl.uniprot.org/annotation/VSP_031734|||http://purl.uniprot.org/annotation/VSP_031735|||http://purl.uniprot.org/annotation/VSP_031736 http://togogenome.org/gene/10090:Esp36 ^@ http://purl.uniprot.org/uniprot/A8R0W9 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015086684 http://togogenome.org/gene/10090:Ptpru ^@ http://purl.uniprot.org/uniprot/B1AUH1|||http://purl.uniprot.org/uniprot/Q3V360|||http://purl.uniprot.org/uniprot/Q80ZN2 ^@ Active Site|||Binding Site|||Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||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|||Mediates interaction with CTNNB1|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Receptor-type tyrosine-protein phosphatase U|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000371659|||http://purl.uniprot.org/annotation/PRO_5004296074|||http://purl.uniprot.org/annotation/VSP_037086 http://togogenome.org/gene/10090:Or52ae7 ^@ http://purl.uniprot.org/uniprot/E9Q564 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mtch1 ^@ http://purl.uniprot.org/uniprot/Q791T5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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.|||Mitochondrial carrier homolog 1|||Mitochondrial intermembrane|||Omega-N-methylarginine|||Solcar 1|||Solcar 2 ^@ http://purl.uniprot.org/annotation/PRO_0000232386|||http://purl.uniprot.org/annotation/VSP_017883 http://togogenome.org/gene/10090:Tmprss11g ^@ http://purl.uniprot.org/uniprot/Q8BZ10 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||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 11G catalytic chain|||Transmembrane protease serine 11G non-catalytic chain ^@ http://purl.uniprot.org/annotation/PRO_0000027837|||http://purl.uniprot.org/annotation/PRO_0000027838 http://togogenome.org/gene/10090:Rp1l1 ^@ http://purl.uniprot.org/uniprot/A1L340|||http://purl.uniprot.org/uniprot/Q8CGM2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Doublecortin|||Doublecortin 1|||Doublecortin 2|||Polar residues|||Retinitis pigmentosa 1-like 1 protein ^@ http://purl.uniprot.org/annotation/PRO_0000097407 http://togogenome.org/gene/10090:Bod1l ^@ http://purl.uniprot.org/uniprot/E9Q6J5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice 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 isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000434111|||http://purl.uniprot.org/annotation/VSP_057902|||http://purl.uniprot.org/annotation/VSP_057903 http://togogenome.org/gene/10090:Tcf20 ^@ http://purl.uniprot.org/uniprot/Q66JM6|||http://purl.uniprot.org/uniprot/Q80U46|||http://purl.uniprot.org/uniprot/Q9EPQ8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||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 isoform 2.|||Leucine-zipper|||Loss of interaction with RNF4; when associated with S-1702; R-1736 and V-1737.|||Loss of interaction with RNF4; when associated with T-1629 and S-1702.|||Loss of interaction with RNF4; when associated with T-1629; R-1736 and V-1737.|||N6-acetyllysine|||Nuclear localization signal|||Omega-N-methylarginine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduces the inhibitory effect of the atypical PHD domain.|||Transcription factor 20 ^@ http://purl.uniprot.org/annotation/PRO_0000072449|||http://purl.uniprot.org/annotation/VSP_003986 http://togogenome.org/gene/10090:Ralgps2 ^@ http://purl.uniprot.org/uniprot/Q9ERD6 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||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_0000322601|||http://purl.uniprot.org/annotation/VSP_031972|||http://purl.uniprot.org/annotation/VSP_031973|||http://purl.uniprot.org/annotation/VSP_031974|||http://purl.uniprot.org/annotation/VSP_031975 http://togogenome.org/gene/10090:Rundc3a ^@ http://purl.uniprot.org/uniprot/O08576 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||Interaction with RAP2A|||Phosphoserine|||Phosphothreonine|||RUN|||RUN domain-containing protein 3A ^@ http://purl.uniprot.org/annotation/PRO_0000324156|||http://purl.uniprot.org/annotation/VSP_032157|||http://purl.uniprot.org/annotation/VSP_032158|||http://purl.uniprot.org/annotation/VSP_032159|||http://purl.uniprot.org/annotation/VSP_032160 http://togogenome.org/gene/10090:Traf3ip2 ^@ http://purl.uniprot.org/uniprot/Q8N7N6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region ^@ Disordered|||E3 ubiquitin ligase TRAF3IP2|||Impairs IL17A-mediated signaling.|||Polar residues|||SEFIR ^@ http://purl.uniprot.org/annotation/PRO_0000450859 http://togogenome.org/gene/10090:Zfp563 ^@ http://purl.uniprot.org/uniprot/B8JJZ9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Nxpe5 ^@ http://purl.uniprot.org/uniprot/E0CX47|||http://purl.uniprot.org/uniprot/E9PXC9 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Erfe ^@ http://purl.uniprot.org/uniprot/Q6PGN1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Abolishes glycosylation. Abolishes secretion; when associated with Q-229.|||Abolishes glycosylation. Abolishes secretion; when associated with Q-281.|||Abolishes secretion as a result of protein misfolding, protein is retained in the endoplasmic reticulum.|||Abolishes secretion.|||C1q|||Disordered|||Enhances secretion and favors trimer formation.|||Enhances secretion and reduces the formation of higher molecular weight oligomers.|||Erythroferrone|||Hydroxyproline|||N-linked (GlcNAc...) asparagine|||No effect on secretion or protein folding.|||No effect on secretion.|||Polar residues|||Pro residues|||Required for correct protein folding in the endoplasmic reticulum ^@ http://purl.uniprot.org/annotation/PRO_0000340251 http://togogenome.org/gene/10090:Ddx3y ^@ http://purl.uniprot.org/uniprot/Q3TUR4|||http://purl.uniprot.org/uniprot/Q62095 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ 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|||N-acetylserine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Q motif|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000055012 http://togogenome.org/gene/10090:Frmd7 ^@ http://purl.uniprot.org/uniprot/A2AD83 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent ^@ FERM|||FERM domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000391462 http://togogenome.org/gene/10090:Cep170 ^@ http://purl.uniprot.org/uniprot/H7BX26|||http://purl.uniprot.org/uniprot/Q6A065 ^@ 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|||Centrosomal protein of 170 kDa|||Disordered|||FHA|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Targeting to centrosomes|||Targeting to microtubules ^@ http://purl.uniprot.org/annotation/PRO_0000282888|||http://purl.uniprot.org/annotation/VSP_024243|||http://purl.uniprot.org/annotation/VSP_024244|||http://purl.uniprot.org/annotation/VSP_024245|||http://purl.uniprot.org/annotation/VSP_024246 http://togogenome.org/gene/10090:Asb6 ^@ http://purl.uniprot.org/uniprot/Q91ZU1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 6|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066934 http://togogenome.org/gene/10090:Rptn ^@ http://purl.uniprot.org/uniprot/P97347 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ 1-1|||1-10|||1-11|||1-12|||1-13|||1-14|||1-15|||1-16|||1-17|||1-18|||1-19|||1-2|||1-20|||1-21|||1-22|||1-23|||1-24|||1-25|||1-26|||1-3|||1-4|||1-5|||1-6|||1-7|||1-8|||1-9|||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|||2-3|||2-4|||2-5|||2-6|||2-7|||2-8|||2-9|||22 X 12 AA approximate tandem repeats of Q-K-G-R-Q-D-Q-S-P-H-Q-G|||48 X 12 AA approximate tandem repeats of Q-[KT]-[GD]-[RS]-Q-[DG]-Q-S-[PS]-H-X-G|||Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||Polar residues|||Repetin|||S-100-like ^@ http://purl.uniprot.org/annotation/PRO_0000144041 http://togogenome.org/gene/10090:Odf2l ^@ http://purl.uniprot.org/uniprot/Q9D478 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant ^@ In isoform 2 and isoform 3.|||In isoform 3.|||Protein BCAP ^@ http://purl.uniprot.org/annotation/PRO_0000308910|||http://purl.uniprot.org/annotation/VSP_029061|||http://purl.uniprot.org/annotation/VSP_029062 http://togogenome.org/gene/10090:Ism2 ^@ http://purl.uniprot.org/uniprot/D3Z6A3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ AMOP|||Basic and acidic residues|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5003052441 http://togogenome.org/gene/10090:Camk1 ^@ http://purl.uniprot.org/uniprot/Q3UY68|||http://purl.uniprot.org/uniprot/Q91YS8 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase type 1|||Calmodulin-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Nuclear export signal|||Phosphothreonine; by CaMKK1 and CaMKK2|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086077 http://togogenome.org/gene/10090:Agbl1 ^@ http://purl.uniprot.org/uniprot/D3Z1M2|||http://purl.uniprot.org/uniprot/Q09M05 ^@ 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 deglutamylase activity; when associated with Q-806.|||Abolishes deglutamylase activity; when associated with S-803.|||Acidic residues|||Cytosolic carboxypeptidase 4|||Cytosolic carboxypeptidase N-terminal|||Disordered|||In isoform 2.|||In isoform 3 and isoform 2.|||In isoform 3.|||Nucleophile|||Peptidase M14 carboxypeptidase A ^@ http://purl.uniprot.org/annotation/PRO_0000305000|||http://purl.uniprot.org/annotation/VSP_060162|||http://purl.uniprot.org/annotation/VSP_060163|||http://purl.uniprot.org/annotation/VSP_060164|||http://purl.uniprot.org/annotation/VSP_060165|||http://purl.uniprot.org/annotation/VSP_060166 http://togogenome.org/gene/10090:Phldb1 ^@ http://purl.uniprot.org/uniprot/Q6PDH0 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||FHA|||In isoform 2.|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology-like domain family B member 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053892|||http://purl.uniprot.org/annotation/VSP_016741|||http://purl.uniprot.org/annotation/VSP_016742|||http://purl.uniprot.org/annotation/VSP_016743 http://togogenome.org/gene/10090:Ppp6r1 ^@ http://purl.uniprot.org/uniprot/Q7TSI3 ^@ 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|||Interaction with PPP6C|||Phosphoserine|||Phosphothreonine|||Polar residues|||Serine/threonine-protein phosphatase 6 regulatory subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000046097 http://togogenome.org/gene/10090:Tlr7 ^@ http://purl.uniprot.org/uniprot/P58681|||http://purl.uniprot.org/uniprot/Q548J0|||http://purl.uniprot.org/uniprot/Q599W9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In kika; mice develop autoimmunity with splenomegaly, multiple autoantibodies, and increased total and activated B cells, germinal centers, plasma cells and memory CD4+ T cells.|||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 28|||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_0000034734 http://togogenome.org/gene/10090:Lrrc30 ^@ http://purl.uniprot.org/uniprot/Q3UV48 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 30 ^@ http://purl.uniprot.org/annotation/PRO_0000310987 http://togogenome.org/gene/10090:Or3a1b ^@ http://purl.uniprot.org/uniprot/Q8VFX6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Yy2 ^@ http://purl.uniprot.org/uniprot/Q3TTC2 ^@ 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|||Mediates transcriptional activation|||Mediates transcriptional repression|||Transcription factor YY2 ^@ http://purl.uniprot.org/annotation/PRO_0000323761 http://togogenome.org/gene/10090:Cyp4a31 ^@ http://purl.uniprot.org/uniprot/F8WGU9 ^@ Binding Site|||Site ^@ Binding Site ^@ ^@ http://togogenome.org/gene/10090:Vim ^@ http://purl.uniprot.org/uniprot/P20152|||http://purl.uniprot.org/uniprot/Q5FWJ3 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ 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|||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 CaMK2|||Phosphoserine; by CaMK2, PKA, PKC and ROCK2|||Phosphoserine; by PKA|||Phosphoserine; by PKA and PKC|||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_0000063756 http://togogenome.org/gene/10090:Col9a2 ^@ http://purl.uniprot.org/uniprot/I7HJR1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Disordered|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5003710351 http://togogenome.org/gene/10090:Spop ^@ http://purl.uniprot.org/uniprot/Q6ZWS8|||http://purl.uniprot.org/uniprot/Q9DBZ2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ BTB|||Important for binding substrate proteins|||Important for homodimerization|||MATH|||Required for nuclear localization|||Speckle-type POZ protein ^@ http://purl.uniprot.org/annotation/PRO_0000191622 http://togogenome.org/gene/10090:Amot ^@ http://purl.uniprot.org/uniprot/Q8VHG2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Angiomotin|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||PDZ-binding|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000190669|||http://purl.uniprot.org/annotation/VSP_027108|||http://purl.uniprot.org/annotation/VSP_027109 http://togogenome.org/gene/10090:Gm15091 ^@ http://purl.uniprot.org/uniprot/B1AZM2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rpl23a ^@ http://purl.uniprot.org/uniprot/P62751|||http://purl.uniprot.org/uniprot/Q5M9M5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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|||Large ribosomal subunit protein uL23 N-terminal|||N,N,N-trimethylalanine; by NTM1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000129468 http://togogenome.org/gene/10090:Ifi203 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0H6|||http://purl.uniprot.org/uniprot/E9PUG6|||http://purl.uniprot.org/uniprot/E9QAN9|||http://purl.uniprot.org/uniprot/O35368 ^@ 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|||HIN-200|||In isoform 2.|||In isoform 3.|||Interferon-activable protein 203|||Polar residues|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000153720|||http://purl.uniprot.org/annotation/VSP_033652|||http://purl.uniprot.org/annotation/VSP_033653|||http://purl.uniprot.org/annotation/VSP_033654 http://togogenome.org/gene/10090:Ticrr ^@ http://purl.uniprot.org/uniprot/Q8BQ33 ^@ 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|||Phosphothreonine|||Polar residues|||Pro residues|||Treslin ^@ http://purl.uniprot.org/annotation/PRO_0000296624 http://togogenome.org/gene/10090:Rbm39 ^@ http://purl.uniprot.org/uniprot/Q0VGU9|||http://purl.uniprot.org/uniprot/Q3U313|||http://purl.uniprot.org/uniprot/Q3UXT6|||http://purl.uniprot.org/uniprot/Q8VH51 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Activating domain|||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.|||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_0000081815|||http://purl.uniprot.org/annotation/VSP_005821|||http://purl.uniprot.org/annotation/VSP_005822 http://togogenome.org/gene/10090:Zfp395 ^@ http://purl.uniprot.org/uniprot/E9Q5N9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:H3c15 ^@ http://purl.uniprot.org/uniprot/B9EI85|||http://purl.uniprot.org/uniprot/P84228 ^@ Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||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 H2A/H2B/H3|||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; 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_0000221250 http://togogenome.org/gene/10090:Ago3 ^@ http://purl.uniprot.org/uniprot/Q8CJF9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Interaction with guide RNA|||N-acetylmethionine|||PAZ|||Phosphoserine|||Piwi|||Protein argonaute-3 ^@ http://purl.uniprot.org/annotation/PRO_0000194062 http://togogenome.org/gene/10090:Sh3yl1 ^@ http://purl.uniprot.org/uniprot/O08641 ^@ 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.|||In isoform 3.|||SH3|||SH3 domain-containing YSC84-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000341561|||http://purl.uniprot.org/annotation/VSP_034336|||http://purl.uniprot.org/annotation/VSP_034337 http://togogenome.org/gene/10090:Greb1 ^@ http://purl.uniprot.org/uniprot/E0CXG4|||http://purl.uniprot.org/uniprot/Q3UHK3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||GREB1 C-terminal|||GREB1 N-terminal|||Helical|||Polar residues|||Protein GREB1 ^@ http://purl.uniprot.org/annotation/PRO_0000320945 http://togogenome.org/gene/10090:Vmn1r219 ^@ http://purl.uniprot.org/uniprot/Q8R271 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Il10 ^@ http://purl.uniprot.org/uniprot/A0A7R8GUQ3|||http://purl.uniprot.org/uniprot/P18893|||http://purl.uniprot.org/uniprot/Q3U879 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Signal Peptide|||Turn ^@ Interleukin family protein|||Interleukin-10|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015367|||http://purl.uniprot.org/annotation/PRO_5031595721|||http://purl.uniprot.org/annotation/PRO_5031595940 http://togogenome.org/gene/10090:Rwdd2b ^@ http://purl.uniprot.org/uniprot/Q99M03 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ RWD|||RWD domain-containing protein 2B ^@ http://purl.uniprot.org/annotation/PRO_0000079505 http://togogenome.org/gene/10090:Dennd2c ^@ http://purl.uniprot.org/uniprot/E9Q4E4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||UDENN ^@ http://togogenome.org/gene/10090:Nt5c3b ^@ http://purl.uniprot.org/uniprot/Q3UFY7 ^@ 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 ^@ 7-methylguanosine phosphate-specific 5'-nucleotidase|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000328949|||http://purl.uniprot.org/annotation/VSP_032851|||http://purl.uniprot.org/annotation/VSP_032852|||http://purl.uniprot.org/annotation/VSP_032853|||http://purl.uniprot.org/annotation/VSP_032854|||http://purl.uniprot.org/annotation/VSP_046298 http://togogenome.org/gene/10090:Cenpn ^@ http://purl.uniprot.org/uniprot/Q9CZW2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ Centromere protein N|||In isoform 2.|||In isoform 3.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000249495|||http://purl.uniprot.org/annotation/VSP_020443|||http://purl.uniprot.org/annotation/VSP_020444|||http://purl.uniprot.org/annotation/VSP_020445 http://togogenome.org/gene/10090:Fam171b ^@ http://purl.uniprot.org/uniprot/Q14CH0 ^@ Chain|||Compositionally Biased Region|||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|||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|||Phosphoserine|||Protein FAM171B ^@ http://purl.uniprot.org/annotation/PRO_0000287149|||http://purl.uniprot.org/annotation/VSP_025343 http://togogenome.org/gene/10090:Sebox ^@ http://purl.uniprot.org/uniprot/P70368 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Disordered|||Homeobox|||Homeobox protein SEBOX|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000311337 http://togogenome.org/gene/10090:Hibch ^@ http://purl.uniprot.org/uniprot/Q8QZS1 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Transit Peptide ^@ 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000284930 http://togogenome.org/gene/10090:Adam23 ^@ http://purl.uniprot.org/uniprot/Q9R1V7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 23|||EGF-like|||Extracellular|||Helical|||In isoform Beta.|||In isoform Delta.|||In isoform Gamma.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B ^@ http://purl.uniprot.org/annotation/PRO_0000029120|||http://purl.uniprot.org/annotation/PRO_0000029121|||http://purl.uniprot.org/annotation/VSP_012047|||http://purl.uniprot.org/annotation/VSP_012048|||http://purl.uniprot.org/annotation/VSP_012049|||http://purl.uniprot.org/annotation/VSP_012050 http://togogenome.org/gene/10090:Vmn1r42 ^@ http://purl.uniprot.org/uniprot/Q05A83|||http://purl.uniprot.org/uniprot/Q8VBS7 ^@ 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|||Vomeronasal type-1 receptor 42 ^@ http://purl.uniprot.org/annotation/PRO_0000239961 http://togogenome.org/gene/10090:Ankrd63 ^@ http://purl.uniprot.org/uniprot/A2ARS0 ^@ 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_0000411003 http://togogenome.org/gene/10090:Caps2 ^@ http://purl.uniprot.org/uniprot/E9Q2J8|||http://purl.uniprot.org/uniprot/Q8BUG5 ^@ 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|||Calcyphosin-2|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000073542|||http://purl.uniprot.org/annotation/VSP_014411|||http://purl.uniprot.org/annotation/VSP_014412 http://togogenome.org/gene/10090:Tmx2 ^@ http://purl.uniprot.org/uniprot/D3Z2J6|||http://purl.uniprot.org/uniprot/Q9D710 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Di-lysine motif|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Thioredoxin|||Thioredoxin-related transmembrane protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000315754 http://togogenome.org/gene/10090:Mafk ^@ http://purl.uniprot.org/uniprot/Q3UP84|||http://purl.uniprot.org/uniprot/Q61827 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ BZIP|||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_0000076504 http://togogenome.org/gene/10090:Gcc1 ^@ http://purl.uniprot.org/uniprot/Q9D4H2 ^@ 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 ^@ Disordered|||GRIP|||GRIP and coiled-coil domain-containing protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000190073 http://togogenome.org/gene/10090:Epha6 ^@ http://purl.uniprot.org/uniprot/G1K381 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site|||Transmembrane ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Acidic residues|||Disordered|||Eph LBD|||Fibronectin type-III|||Helical|||Polar residues|||Protein kinase|||SAM ^@ http://togogenome.org/gene/10090:Snx3 ^@ http://purl.uniprot.org/uniprot/Q78ZM0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ PX ^@ http://togogenome.org/gene/10090:Llgl1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0S4|||http://purl.uniprot.org/uniprot/Q80Y17 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||Lethal giant larvae (Lgl)-like C-terminal|||Lethal giant larvae homologue 2|||Lethal(2) giant larvae protein homolog 1|||Phosphoserine|||Phosphothreonine|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000232726 http://togogenome.org/gene/10090:Lrriq1 ^@ http://purl.uniprot.org/uniprot/Q0P5X1 ^@ 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|||IQ 1|||IQ 2|||IQ 3|||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|||Leucine-rich repeat and IQ domain-containing protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000313626|||http://purl.uniprot.org/annotation/VSP_040541|||http://purl.uniprot.org/annotation/VSP_040542 http://togogenome.org/gene/10090:Atp2a3 ^@ http://purl.uniprot.org/uniprot/E9Q559|||http://purl.uniprot.org/uniprot/Q3U1K2|||http://purl.uniprot.org/uniprot/Q3U6T4|||http://purl.uniprot.org/uniprot/Q64518|||http://purl.uniprot.org/uniprot/Q8C213|||http://purl.uniprot.org/uniprot/Q8R0X5 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase C-terminal|||Cation-transporting P-type ATPase N-terminal|||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|||In isoform SERCA3B.|||In isoform SERCA3C.|||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_0000046203|||http://purl.uniprot.org/annotation/VSP_060850|||http://purl.uniprot.org/annotation/VSP_060851 http://togogenome.org/gene/10090:Tbcb ^@ http://purl.uniprot.org/uniprot/Q9D1E6 ^@ 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 ^@ CAP-Gly|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PAK1|||Phosphotyrosine|||Tubulin-folding cofactor B ^@ http://purl.uniprot.org/annotation/PRO_0000083535 http://togogenome.org/gene/10090:Uqcc4 ^@ http://purl.uniprot.org/uniprot/Q6RUT7 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Disordered|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Ubiquinol-cytochrome c reductase complex assembly factor 4 ^@ http://purl.uniprot.org/annotation/PRO_0000348603 http://togogenome.org/gene/10090:Adh1 ^@ http://purl.uniprot.org/uniprot/P00329|||http://purl.uniprot.org/uniprot/Q3UKA4 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Alcohol dehydrogenase 1|||Enoyl reductase (ER)|||N-acetylserine|||N6-succinyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000160666 http://togogenome.org/gene/10090:Lyl1 ^@ http://purl.uniprot.org/uniprot/A0A571BE88|||http://purl.uniprot.org/uniprot/P27792 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ BHLH|||Disordered|||Phosphoserine|||Protein lyl-1|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127263 http://togogenome.org/gene/10090:Grm8 ^@ http://purl.uniprot.org/uniprot/B7ZMR4|||http://purl.uniprot.org/uniprot/P47743|||http://purl.uniprot.org/uniprot/Q05BD6 ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Abolishes sumoylation. Abolishes sumoylation; when associated with R-868 and R-872.|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 3 profile|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Metabotropic glutamate receptor 8|||N-linked (GlcNAc...) asparagine|||No change in sumoylation. Abolishes sumoylation; when associated with R-868 and R-882.|||No change in sumoylation. Abolishes sumoylation; when associated with R-872 and R-882. ^@ http://purl.uniprot.org/annotation/PRO_0000012942 http://togogenome.org/gene/10090:Dpp7 ^@ http://purl.uniprot.org/uniprot/Q9ET22 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Dipeptidyl peptidase 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000027316|||http://purl.uniprot.org/annotation/PRO_0000027317 http://togogenome.org/gene/10090:Scgb2b10 ^@ http://purl.uniprot.org/uniprot/A0A089N5R6 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5001847739 http://togogenome.org/gene/10090:Zfp281 ^@ http://purl.uniprot.org/uniprot/Q99LI5 ^@ 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 ^@ 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)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 281 ^@ http://purl.uniprot.org/annotation/PRO_0000420492 http://togogenome.org/gene/10090:Gucy2e ^@ http://purl.uniprot.org/uniprot/P52785 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Guanylate cyclase|||Helical|||Interchain|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Retinal guanylyl cyclase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000012383 http://togogenome.org/gene/10090:Dipk2b ^@ http://purl.uniprot.org/uniprot/Q3TQ46|||http://purl.uniprot.org/uniprot/Q8C3I9 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Divergent protein kinase domain 2B|||FAM69 protein-kinase|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000353115 http://togogenome.org/gene/10090:Ctrb1 ^@ http://purl.uniprot.org/uniprot/Q9CR35 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Sequence Conflict|||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_0000285874|||http://purl.uniprot.org/annotation/PRO_0000285875|||http://purl.uniprot.org/annotation/PRO_0000285876|||http://purl.uniprot.org/annotation/PRO_0000285877 http://togogenome.org/gene/10090:Cyp20a1 ^@ http://purl.uniprot.org/uniprot/Q80Y48|||http://purl.uniprot.org/uniprot/Q8BKE6 ^@ Binding Site|||Chain|||Coiled-Coil|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Transmembrane ^@ Cytochrome P450 20A1|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000318096 http://togogenome.org/gene/10090:Nudt13 ^@ http://purl.uniprot.org/uniprot/Q8JZU0 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Motif|||Transit Peptide ^@ Mitochondrion|||NAD(P)H pyrophosphatase NUDT13, mitochondrial|||Nudix box|||Nudix hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000057112 http://togogenome.org/gene/10090:Atp5j2 ^@ http://purl.uniprot.org/uniprot/P56135 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Transmembrane ^@ ATP synthase subunit f, mitochondrial|||Helical|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194825 http://togogenome.org/gene/10090:Ephx1 ^@ http://purl.uniprot.org/uniprot/E9PWK1|||http://purl.uniprot.org/uniprot/Q9D379 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dimethylated arginine|||Epoxide hydrolase 1|||Epoxide hydrolase N-terminal|||Helical; Signal-anchor for type III membrane protein|||N6-acetyllysine|||Nucleophile|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000080856 http://togogenome.org/gene/10090:Npy6r ^@ http://purl.uniprot.org/uniprot/Q61212 ^@ 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 6|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069943 http://togogenome.org/gene/10090:Ifi44l ^@ http://purl.uniprot.org/uniprot/Q9BDB7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Peptide|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Interferon-induced protein 44-like|||Minor histocompatibility antigen HA-28|||TLDc ^@ http://purl.uniprot.org/annotation/PRO_0000337846|||http://purl.uniprot.org/annotation/PRO_0000342087|||http://purl.uniprot.org/annotation/VSP_034010 http://togogenome.org/gene/10090:Acot2 ^@ http://purl.uniprot.org/uniprot/Q6P2K2|||http://purl.uniprot.org/uniprot/Q9QYR9 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase|||Acyl-coenzyme A thioesterase 2, mitochondrial|||BAAT/Acyl-CoA thioester hydrolase C-terminal|||Charge relay system|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000034065 http://togogenome.org/gene/10090:Myot ^@ http://purl.uniprot.org/uniprot/A0A509|||http://purl.uniprot.org/uniprot/Q9JIF9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 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_0000072688 http://togogenome.org/gene/10090:Pet100 ^@ http://purl.uniprot.org/uniprot/P0DJE0 ^@ Chain|||Molecule Processing|||Region|||Transit Peptide|||Transmembrane ^@ Chain|||Transit Peptide|||Transmembrane ^@ Helical|||Mitochondrion|||Protein PET100 homolog, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000415814 http://togogenome.org/gene/10090:Myo9a ^@ http://purl.uniprot.org/uniprot/D3Z3A8|||http://purl.uniprot.org/uniprot/Q8C170 ^@ 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|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Actin-binding|||Basic and acidic residues|||Disordered|||Helical|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||In isoform 2.|||Myosin motor|||Neck or regulatory domain|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ras-associating|||Rho-GAP|||Tail|||Unconventional myosin-IXa ^@ http://purl.uniprot.org/annotation/PRO_0000348441|||http://purl.uniprot.org/annotation/VSP_035161 http://togogenome.org/gene/10090:Tmem258 ^@ http://purl.uniprot.org/uniprot/E9Q853|||http://purl.uniprot.org/uniprot/P61166|||http://purl.uniprot.org/uniprot/Q60FD1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Transmembrane ^@ Helical|||N-acetylmethionine|||Transmembrane protein 258 ^@ http://purl.uniprot.org/annotation/PRO_0000221143 http://togogenome.org/gene/10090:Or10j5 ^@ http://purl.uniprot.org/uniprot/Q62007 ^@ 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 10J5 ^@ http://purl.uniprot.org/annotation/PRO_0000454829 http://togogenome.org/gene/10090:Or2a14 ^@ http://purl.uniprot.org/uniprot/K9J725 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ube2v1 ^@ http://purl.uniprot.org/uniprot/B7ZBY7|||http://purl.uniprot.org/uniprot/Q569Y6|||http://purl.uniprot.org/uniprot/Q9CZY3 ^@ 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.|||N-acetylalanine|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 variant 1 ^@ http://purl.uniprot.org/annotation/PRO_0000082601|||http://purl.uniprot.org/annotation/VSP_011528 http://togogenome.org/gene/10090:Sgpp2 ^@ http://purl.uniprot.org/uniprot/Q810K3 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Region|||Site|||Transmembrane ^@ Helical|||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_0000114481 http://togogenome.org/gene/10090:Bicdl1 ^@ http://purl.uniprot.org/uniprot/A0JNT9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes Rab6-binding.|||BICD family-like cargo adapter 1|||CC1 box|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000302859|||http://purl.uniprot.org/annotation/VSP_027970|||http://purl.uniprot.org/annotation/VSP_027971|||http://purl.uniprot.org/annotation/VSP_027972|||http://purl.uniprot.org/annotation/VSP_027973|||http://purl.uniprot.org/annotation/VSP_027974|||http://purl.uniprot.org/annotation/VSP_027975 http://togogenome.org/gene/10090:Lpar1 ^@ http://purl.uniprot.org/uniprot/P61793|||http://purl.uniprot.org/uniprot/Q544V2 ^@ Binding 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 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||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 isoform 2.|||Lysophosphatidic acid receptor 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000069418|||http://purl.uniprot.org/annotation/VSP_001986 http://togogenome.org/gene/10090:Ctsz ^@ http://purl.uniprot.org/uniprot/Q545I6|||http://purl.uniprot.org/uniprot/Q9WUU7 ^@ 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|||Cathepsin Z|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal|||cathepsin X ^@ http://purl.uniprot.org/annotation/PRO_0000026287|||http://purl.uniprot.org/annotation/PRO_0000026288|||http://purl.uniprot.org/annotation/PRO_5014205871 http://togogenome.org/gene/10090:Gm12887 ^@ http://purl.uniprot.org/uniprot/B1AVM1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5002761859 http://togogenome.org/gene/10090:Syngr3 ^@ http://purl.uniprot.org/uniprot/Q8R191 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||MARVEL|||N-acetylmethionine|||Polar residues|||Synaptogyrin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000183997 http://togogenome.org/gene/10090:Usp40 ^@ http://purl.uniprot.org/uniprot/Q8BWR4 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 40 ^@ http://purl.uniprot.org/annotation/PRO_0000080671|||http://purl.uniprot.org/annotation/VSP_022171|||http://purl.uniprot.org/annotation/VSP_022172|||http://purl.uniprot.org/annotation/VSP_022173|||http://purl.uniprot.org/annotation/VSP_022174 http://togogenome.org/gene/10090:Cibar1 ^@ http://purl.uniprot.org/uniprot/A0A8Q0KEJ4|||http://purl.uniprot.org/uniprot/Q8BP22|||http://purl.uniprot.org/uniprot/Z4YJZ2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transit Peptide ^@ Acidic residues|||BAR-like|||CBY1-interacting BAR domain-containing protein 1|||Disordered|||Mitochondrion|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000287081 http://togogenome.org/gene/10090:4930568D16Rik ^@ http://purl.uniprot.org/uniprot/A2AUQ7 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-acetyllactosaminide alpha-1,3-galactosyltransferase-like 1|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000428936 http://togogenome.org/gene/10090:Camp ^@ http://purl.uniprot.org/uniprot/P51437 ^@ Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Cathelin-like domain (CLD)|||Cathelin-related antimicrobial peptide ^@ http://purl.uniprot.org/annotation/PRO_0000435275|||http://purl.uniprot.org/annotation/PRO_0000435276 http://togogenome.org/gene/10090:Tas2r108 ^@ http://purl.uniprot.org/uniprot/Q9JKT3 ^@ 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 4 ^@ http://purl.uniprot.org/annotation/PRO_0000082210 http://togogenome.org/gene/10090:Vsig8 ^@ http://purl.uniprot.org/uniprot/Q6P3A4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||V-set and immunoglobulin domain-containing protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000313628|||http://purl.uniprot.org/annotation/VSP_030071 http://togogenome.org/gene/10090:Mrpl2 ^@ http://purl.uniprot.org/uniprot/Q9D773 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Large ribosomal subunit protein uL2m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000261641 http://togogenome.org/gene/10090:9130023H24Rik ^@ http://purl.uniprot.org/uniprot/Q8BG98 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Gpatch8 ^@ http://purl.uniprot.org/uniprot/A2A6A1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||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)|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000379799 http://togogenome.org/gene/10090:Amy2a2 ^@ http://purl.uniprot.org/uniprot/P00688 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ In A1 and B(C).|||In A1, B(A) and B(C).|||In A1, B(A) and B(C); requires 2 nucleotide substitutions.|||In A1, B(C) and AMY-2.2Y.|||In AMY-2.2Y.|||In B(A).|||In B(C).|||In B1.|||Nucleophile|||Pancreatic alpha-amylase 2a5|||Proton donor|||Pyrrolidone carboxylic acid|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000001398 http://togogenome.org/gene/10090:Sprr2a3 ^@ http://purl.uniprot.org/uniprot/Q4KL71|||http://purl.uniprot.org/uniprot/Q9CQK8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||4|||5|||5 X 9 AA approximate tandem repeats|||Small proline-rich protein 2A1|||Small proline-rich protein 2A3 ^@ http://purl.uniprot.org/annotation/PRO_0000150014|||http://purl.uniprot.org/annotation/PRO_0000425580 http://togogenome.org/gene/10090:Ppp3ca ^@ http://purl.uniprot.org/uniprot/P63328 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand|||Turn ^@ 3'-nitrotyrosine|||Autoinhibitory domain|||Autoinhibitory segment|||Calcineurin B binding|||Calmodulin-binding|||Catalytic|||Disordered|||Greatly reduces inhibition of calcineurin phosphatase activity.|||In isoform 2.|||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.|||Interaction with PxIxIF motif in substrate|||Interaction with PxVP motif in substrate|||Loss of catalytic activity. Loss of interaction with PPP3R1/calreticulin B and calmodulin.|||N-acetylserine|||Phosphoserine|||Polar residues|||Protein phosphatase 3 catalytic subunit alpha|||Proton donor|||Removed|||SAPNY motif ^@ http://purl.uniprot.org/annotation/PRO_0000058823|||http://purl.uniprot.org/annotation/VSP_018563 http://togogenome.org/gene/10090:Or2y6 ^@ http://purl.uniprot.org/uniprot/Q7TQT7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lpar2 ^@ http://purl.uniprot.org/uniprot/Q9JL06 ^@ Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Lipid Binding|||Motif|||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 2|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069426 http://togogenome.org/gene/10090:Gpr19 ^@ http://purl.uniprot.org/uniprot/Q61121 ^@ 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|||Probable G-protein coupled receptor 19 ^@ http://purl.uniprot.org/annotation/PRO_0000069539|||http://purl.uniprot.org/annotation/VSP_016527 http://togogenome.org/gene/10090:Or6c2b ^@ http://purl.uniprot.org/uniprot/Q8K501 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp940 ^@ http://purl.uniprot.org/uniprot/Q8R2Q3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Dnajb12 ^@ http://purl.uniprot.org/uniprot/Q9QYI4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||DnaJ homolog subfamily B member 12|||Helical|||J|||N-acetylmethionine|||Polar residues|||Pros-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000071038 http://togogenome.org/gene/10090:Gba2 ^@ http://purl.uniprot.org/uniprot/Q69ZF3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Non-lysosomal glucosylceramidase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000283759 http://togogenome.org/gene/10090:Gm21627 ^@ http://purl.uniprot.org/uniprot/A0A087WRK1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Esrp1 ^@ http://purl.uniprot.org/uniprot/F8WGU3|||http://purl.uniprot.org/uniprot/Q3US41 ^@ 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 ^@ Epithelial splicing regulatory protein 1|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000273047|||http://purl.uniprot.org/annotation/VSP_022468|||http://purl.uniprot.org/annotation/VSP_022469|||http://purl.uniprot.org/annotation/VSP_022470|||http://purl.uniprot.org/annotation/VSP_022471|||http://purl.uniprot.org/annotation/VSP_022472|||http://purl.uniprot.org/annotation/VSP_022473 http://togogenome.org/gene/10090:Mfsd13a ^@ http://purl.uniprot.org/uniprot/Q6PDE8 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 180 ^@ http://purl.uniprot.org/annotation/PRO_0000256225 http://togogenome.org/gene/10090:Tinf2 ^@ http://purl.uniprot.org/uniprot/Q8K1K3 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||TERF1-interacting nuclear factor 2 N-terminal ^@ http://togogenome.org/gene/10090:Plac8l1 ^@ http://purl.uniprot.org/uniprot/Q08EJ0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ PLAC8-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000311397 http://togogenome.org/gene/10090:Or4e5 ^@ http://purl.uniprot.org/uniprot/Q0VEP0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gm5114 ^@ http://purl.uniprot.org/uniprot/Q8CDW0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF4629|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Inpp5d ^@ http://purl.uniprot.org/uniprot/Q9ES52 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5 and isoform 6.|||Interaction with DAB2|||Loss of function.|||NPXY motif 1|||NPXY motif 2|||Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH2|||SH3-binding 1|||SH3-binding 2|||SH3-binding 3|||Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-1021.|||Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-918. ^@ http://purl.uniprot.org/annotation/PRO_0000302867|||http://purl.uniprot.org/annotation/VSP_027980|||http://purl.uniprot.org/annotation/VSP_027981|||http://purl.uniprot.org/annotation/VSP_027982|||http://purl.uniprot.org/annotation/VSP_027983|||http://purl.uniprot.org/annotation/VSP_027984 http://togogenome.org/gene/10090:Fam217b ^@ http://purl.uniprot.org/uniprot/A2AJW5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Emc7 ^@ http://purl.uniprot.org/uniprot/Q14C26|||http://purl.uniprot.org/uniprot/Q9EP72 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||ER membrane protein complex subunit 7|||ER membrane protein complex subunit 7 beta-sandwich|||Helical|||Lumenal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000240862|||http://purl.uniprot.org/annotation/PRO_5014306932 http://togogenome.org/gene/10090:Rangrf ^@ http://purl.uniprot.org/uniprot/Q9JIB0 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Deficient in binding to RAN-GTP and in GTP release activity.|||Increases GTP release from RAN.|||Interaction with RAN|||Ran guanine nucleotide release factor ^@ http://purl.uniprot.org/annotation/PRO_0000330637 http://togogenome.org/gene/10090:Nhlrc4 ^@ http://purl.uniprot.org/uniprot/Q3UP44 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ NHL 1|||NHL 2|||NHL-repeat-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000395107 http://togogenome.org/gene/10090:Vmn2r55 ^@ http://purl.uniprot.org/uniprot/G3UWZ4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 3 profile|||Helical ^@ http://togogenome.org/gene/10090:Baiap2l1 ^@ http://purl.uniprot.org/uniprot/Q9DBJ3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Binds F-actin|||Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1|||Disordered|||IMD|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000247855 http://togogenome.org/gene/10090:Pcdhga10 ^@ http://purl.uniprot.org/uniprot/Q91XY9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099529 http://togogenome.org/gene/10090:A530021J07Rik ^@ http://purl.uniprot.org/uniprot/Q8BS29 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Plcd4 ^@ http://purl.uniprot.org/uniprot/Q8K3R3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4|||Acidic residues|||C2|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||GBA|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||PDZ-binding|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Substrate binding ^@ http://purl.uniprot.org/annotation/PRO_0000306826|||http://purl.uniprot.org/annotation/VSP_028503|||http://purl.uniprot.org/annotation/VSP_028504|||http://purl.uniprot.org/annotation/VSP_028505|||http://purl.uniprot.org/annotation/VSP_028506 http://togogenome.org/gene/10090:Ccdc57 ^@ http://purl.uniprot.org/uniprot/Q6PHN1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Centrosomal targeting domain|||Coiled-coil domain-containing protein 57|||Disordered|||Microtubule binding domain|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288872 http://togogenome.org/gene/10090:Nat1 ^@ http://purl.uniprot.org/uniprot/P50294 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ Acyl-thioester intermediate|||Arylamine N-acetyltransferase 1|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000107908 http://togogenome.org/gene/10090:Pcdha8 ^@ http://purl.uniprot.org/uniprot/Q91Y12 ^@ 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|||Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099542 http://togogenome.org/gene/10090:Or51ai2 ^@ http://purl.uniprot.org/uniprot/Q9EPN9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clec4n ^@ http://purl.uniprot.org/uniprot/Q3U3M9|||http://purl.uniprot.org/uniprot/Q3V2N1|||http://purl.uniprot.org/uniprot/Q9JKF4 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 6 member A|||Cytoplasmic|||Does not affect association with Fc receptor gamma chain.|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046636|||http://purl.uniprot.org/annotation/VSP_012846|||http://purl.uniprot.org/annotation/VSP_012847 http://togogenome.org/gene/10090:Adgra2 ^@ http://purl.uniprot.org/uniprot/Q91ZV8 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Adhesion G protein-coupled receptor A2|||Basic residues|||Cleavage; by thrombin|||Cytoplasmic|||Disordered|||Extracellular|||Fails to interact with DLG1. No effect on cell surface localization.|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Ig-like|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||N-linked (GlcNAc...) asparagine|||No effect on potentiation of WNT7A signaling.|||PDZ-binding|||Phosphoserine|||Polar residues|||RGD ^@ http://purl.uniprot.org/annotation/PRO_0000012899 http://togogenome.org/gene/10090:9930111J21Rik1 ^@ http://purl.uniprot.org/uniprot/Q5SVP0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||IRG-type G ^@ http://togogenome.org/gene/10090:Hapstr1 ^@ http://purl.uniprot.org/uniprot/Q14AM7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||HUWE1-associated protein modifying stress responses|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000297628 http://togogenome.org/gene/10090:Zfp950 ^@ http://purl.uniprot.org/uniprot/A0A0U1RP12|||http://purl.uniprot.org/uniprot/A0A0U1RQ46|||http://purl.uniprot.org/uniprot/Q8BL88 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Eif1b ^@ http://purl.uniprot.org/uniprot/Q9CXU9 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Eukaryotic translation initiation factor 1b|||N-acetylserine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000130559 http://togogenome.org/gene/10090:Slit3 ^@ http://purl.uniprot.org/uniprot/B2RX06|||http://purl.uniprot.org/uniprot/Q3UHN1|||http://purl.uniprot.org/uniprot/Q9WVB4|||http://purl.uniprot.org/uniprot/Q9Z0Y6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Signal Peptide ^@ 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|||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 3 protein ^@ http://purl.uniprot.org/annotation/PRO_0000007733|||http://purl.uniprot.org/annotation/PRO_5002781898|||http://purl.uniprot.org/annotation/PRO_5004230170 http://togogenome.org/gene/10090:Commd10 ^@ http://purl.uniprot.org/uniprot/Q3TKN7|||http://purl.uniprot.org/uniprot/Q8JZY2 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ COMM|||COMM domain-containing protein 10|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000077406 http://togogenome.org/gene/10090:Defa41 ^@ http://purl.uniprot.org/uniprot/D3YX02 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Mammalian defensins|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003052957 http://togogenome.org/gene/10090:Or4l1 ^@ http://purl.uniprot.org/uniprot/E9PZU2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kcnh5 ^@ http://purl.uniprot.org/uniprot/Q920E3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||CAD (involved in subunit assembly)|||Calmodulin-binding|||Cytoplasmic|||Disordered|||Extracellular|||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|||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_0000054011 http://togogenome.org/gene/10090:Kcnj9 ^@ http://purl.uniprot.org/uniprot/P48543|||http://purl.uniprot.org/uniprot/Q544N3 ^@ Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||G protein-activated inward rectifier potassium channel 3|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Inward rectifier potassium channel C-terminal|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000154951 http://togogenome.org/gene/10090:Etf1 ^@ http://purl.uniprot.org/uniprot/Q3TF02|||http://purl.uniprot.org/uniprot/Q8BWY3 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Strand ^@ 4-hydroxylysine|||Eukaryotic peptide chain release factor subunit 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||N5-methylglutamine|||NIKS motif; plays an important role in translational termination|||Phosphothreonine|||Removed|||eRF1 ^@ http://purl.uniprot.org/annotation/PRO_0000143140 http://togogenome.org/gene/10090:Vav1 ^@ http://purl.uniprot.org/uniprot/E9PXI0|||http://purl.uniprot.org/uniprot/P27870|||http://purl.uniprot.org/uniprot/Q3U9E2|||http://purl.uniprot.org/uniprot/Q3UAV5|||http://purl.uniprot.org/uniprot/Q8VDU4 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Abolishes transforming activity.|||Calponin-homology (CH)|||DH|||PH|||Phorbol-ester/DAG-type|||Phosphotyrosine|||Proto-oncogene vav|||SH2|||SH3|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000080981 http://togogenome.org/gene/10090:Myo6 ^@ http://purl.uniprot.org/uniprot/Q64331|||http://purl.uniprot.org/uniprot/Q8BK95 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Strand|||Turn ^@ Actin-binding|||Disordered|||IQ|||In Snell's waltzer.|||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_0000123465 http://togogenome.org/gene/10090:Bach1 ^@ http://purl.uniprot.org/uniprot/P97302|||http://purl.uniprot.org/uniprot/Q3URL4|||http://purl.uniprot.org/uniprot/Q3US24 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ BTB|||BZIP|||Basic and acidic residues|||Basic motif|||Disordered|||Leucine-zipper|||Phosphoserine|||Polar residues|||Transcription regulator protein BACH1|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076455 http://togogenome.org/gene/10090:Slc17a6 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0A6|||http://purl.uniprot.org/uniprot/Q8BLE7 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Vesicular|||Vesicular glutamate transporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000318170 http://togogenome.org/gene/10090:Arhgap33 ^@ http://purl.uniprot.org/uniprot/A0A140LHW2|||http://purl.uniprot.org/uniprot/Q3UQS4|||http://purl.uniprot.org/uniprot/Q80YF9 ^@ 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 ^@ Basic and acidic residues|||Disordered|||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_0000056722 http://togogenome.org/gene/10090:Zbtb22 ^@ http://purl.uniprot.org/uniprot/Q3TXW4|||http://purl.uniprot.org/uniprot/Q9Z0G7 ^@ 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|||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_0000047518 http://togogenome.org/gene/10090:Fn1 ^@ http://purl.uniprot.org/uniprot/A0A087WR50|||http://purl.uniprot.org/uniprot/A0A087WS56|||http://purl.uniprot.org/uniprot/A0A087WSN6|||http://purl.uniprot.org/uniprot/B7ZNJ1|||http://purl.uniprot.org/uniprot/B9EHT6|||http://purl.uniprot.org/uniprot/P11276|||http://purl.uniprot.org/uniprot/Q3TBB4|||http://purl.uniprot.org/uniprot/Q3UGY5|||http://purl.uniprot.org/uniprot/Q3UH17|||http://purl.uniprot.org/uniprot/Q3UHL6|||http://purl.uniprot.org/uniprot/Q3UHR1|||http://purl.uniprot.org/uniprot/Q3UZF9 ^@ Chain|||Crosslink|||DNA Binding|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand ^@ 65% decrease in cross-linking efficiency; when associated with L-35.|||65% decrease in cross-linking efficiency; when associated with L-36.|||99% decrease in cross-linking efficiency; when associated with A-35 and A-36.|||99% decrease in cross-linking efficiency; when associated with A-35 and A-48.|||99% decrease in cross-linking efficiency; when associated with A-36 and A-48.|||Anastellin|||Cell attachment site|||Cell-attachment|||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|||Interchain (with C-2458)|||Interchain (with C-2462)|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Pyrrolidone carboxylic acid|||Required for binding to Lilrb4a|||Sulfotyrosine|||V region (type III connecting segment, IIICS) ^@ http://purl.uniprot.org/annotation/PRO_0000019236|||http://purl.uniprot.org/annotation/PRO_0000390480|||http://purl.uniprot.org/annotation/PRO_5001831860|||http://purl.uniprot.org/annotation/PRO_5004229420|||http://purl.uniprot.org/annotation/PRO_5004229965|||http://purl.uniprot.org/annotation/PRO_5004230149|||http://purl.uniprot.org/annotation/PRO_5015029550|||http://purl.uniprot.org/annotation/PRO_5015029551|||http://purl.uniprot.org/annotation/PRO_5015087440|||http://purl.uniprot.org/annotation/PRO_5015087492|||http://purl.uniprot.org/annotation/PRO_5015097482 http://togogenome.org/gene/10090:Rwdd4a ^@ http://purl.uniprot.org/uniprot/Q9CPR1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||RWD|||RWD domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000076308 http://togogenome.org/gene/10090:Rspo3 ^@ http://purl.uniprot.org/uniprot/Q2TJ95 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||FU 1|||FU 2|||N-linked (GlcNAc...) asparagine|||R-spondin-3|||TSP type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000234444 http://togogenome.org/gene/10090:Galr2 ^@ http://purl.uniprot.org/uniprot/O88854|||http://purl.uniprot.org/uniprot/Q8BKB0 ^@ 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|||Galanin receptor type 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 ^@ http://purl.uniprot.org/annotation/PRO_0000069467 http://togogenome.org/gene/10090:Serpinb3b ^@ http://purl.uniprot.org/uniprot/Q9D1Q5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Map3k20 ^@ http://purl.uniprot.org/uniprot/Q3TRG2|||http://purl.uniprot.org/uniprot/Q9ESL4 ^@ 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|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||C-terminal domain (CTD)|||Causes a split-hand/split-foot phenotype in knockin mice. Gain-of-function mutant that cases a constitutive ribotoxic stress response (RSR).|||Disordered|||In isoform 3.|||In isoform ZAKbeta.|||Leucine-zipper|||Loss of kinase activity.|||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) ^@ http://purl.uniprot.org/annotation/PRO_0000086339|||http://purl.uniprot.org/annotation/VSP_051745|||http://purl.uniprot.org/annotation/VSP_051746|||http://purl.uniprot.org/annotation/VSP_051747|||http://purl.uniprot.org/annotation/VSP_051748 http://togogenome.org/gene/10090:Calu ^@ http://purl.uniprot.org/uniprot/O35887|||http://purl.uniprot.org/uniprot/Q3TQD1|||http://purl.uniprot.org/uniprot/Q3TUF3|||http://purl.uniprot.org/uniprot/Q3UG11|||http://purl.uniprot.org/uniprot/Q6XLQ8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Non-terminal Residue|||Signal Peptide ^@ Calumenin|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||EF-hand domain-containing protein|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000004154|||http://purl.uniprot.org/annotation/PRO_5004229658|||http://purl.uniprot.org/annotation/PRO_5004230114|||http://purl.uniprot.org/annotation/PRO_5014309163|||http://purl.uniprot.org/annotation/PRO_5015098595 http://togogenome.org/gene/10090:Or6z7 ^@ http://purl.uniprot.org/uniprot/Q60889 ^@ 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 6Z7 ^@ http://purl.uniprot.org/annotation/PRO_0000150805 http://togogenome.org/gene/10090:Kcnj11 ^@ http://purl.uniprot.org/uniprot/Q61743 ^@ Chain|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ ATP-sensitive inward rectifier potassium channel 11|||Cytoplasmic|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Phosphoserine; by MAPK1|||Phosphothreonine; by MAPK1|||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_0000154958 http://togogenome.org/gene/10090:Strip2 ^@ http://purl.uniprot.org/uniprot/B2RW20|||http://purl.uniprot.org/uniprot/Q8C9H6 ^@ 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|||Far11/STRP C-terminal|||Far11/STRP N-terminal|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Striatin-interacting proteins 2 ^@ http://purl.uniprot.org/annotation/PRO_0000187023|||http://purl.uniprot.org/annotation/VSP_014870|||http://purl.uniprot.org/annotation/VSP_019001|||http://purl.uniprot.org/annotation/VSP_019002 http://togogenome.org/gene/10090:Prr22 ^@ http://purl.uniprot.org/uniprot/F6TNE3 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Rhox13 ^@ http://purl.uniprot.org/uniprot/F6YCR7 ^@ 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|||Homeobox|||Homeobox protein Rhox13 ^@ http://purl.uniprot.org/annotation/PRO_0000435030 http://togogenome.org/gene/10090:Pde3a ^@ http://purl.uniprot.org/uniprot/B2RR84|||http://purl.uniprot.org/uniprot/Q9Z0X4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||Interaction with SLFN12|||PDEase|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton donor|||cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A ^@ http://purl.uniprot.org/annotation/PRO_0000198800 http://togogenome.org/gene/10090:Cyb5rl ^@ http://purl.uniprot.org/uniprot/B1AS42 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant ^@ FAD-binding FR-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||NADH-cytochrome b5 reductase-like|||Oxidoreductase-like ^@ http://purl.uniprot.org/annotation/PRO_0000337042|||http://purl.uniprot.org/annotation/VSP_033848|||http://purl.uniprot.org/annotation/VSP_033849|||http://purl.uniprot.org/annotation/VSP_033850|||http://purl.uniprot.org/annotation/VSP_033851|||http://purl.uniprot.org/annotation/VSP_033852|||http://purl.uniprot.org/annotation/VSP_033853 http://togogenome.org/gene/10090:Or8s5 ^@ http://purl.uniprot.org/uniprot/Q8VET7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Twist1 ^@ http://purl.uniprot.org/uniprot/P26687 ^@ 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 ^@ Disordered|||High transactivation activity.|||Intermediate transactivation activity.|||Low transactivation activity.|||Polar residues|||Sufficient for transactivation activity|||Twist-related protein 1|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127488 http://togogenome.org/gene/10090:Anxa13 ^@ http://purl.uniprot.org/uniprot/Q99JG3 ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Repeat ^@ Chain|||Initiator Methionine|||Lipid Binding|||Repeat ^@ Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A13|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067515 http://togogenome.org/gene/10090:Car5b ^@ http://purl.uniprot.org/uniprot/Q9QZA0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase 5B, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000004238 http://togogenome.org/gene/10090:Fam83f ^@ http://purl.uniprot.org/uniprot/A0A0R4J033|||http://purl.uniprot.org/uniprot/Q3UKU4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||FAM83 N-terminal|||N-acetylalanine|||Phosphoserine|||Polar residues|||Protein FAM83F|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000314951 http://togogenome.org/gene/10090:Pik3ca ^@ http://purl.uniprot.org/uniprot/P42337 ^@ 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 binding to HRAS and KRAS; does not affect kinase activity; displays defective development of the lymphatic vasculature, resulting in perinatal appearance of chylous ascites and is highly resistant to endogenous Ras oncogene-induced tumorigenesis; when associated with A-227.|||Abolishes binding to HRAS and KRAS; does not affect kinase activity; displays defective development of the lymphatic vasculature, resulting in perinatal appearance of chylous ascites and is highly resistant to endogenous Ras oncogene-induced tumorigenesis; when associated with D-208.|||Activation loop|||C2 PI3K-type|||Catalytic loop|||G-loop|||Loss of kinase activity; displays early embryonic lethality at 10-11 dpc and severe defects in angiogenic sprouting and vascular remodeling. Heterozygous mice yield adult mice with markedly impaired insulin signaling and reduced activation of effector pathways such as Akt/PKB.|||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_0000088786 http://togogenome.org/gene/10090:Hyal4 ^@ http://purl.uniprot.org/uniprot/L0MX76|||http://purl.uniprot.org/uniprot/Q05A56 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Hyaluronidase-4|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000302000 http://togogenome.org/gene/10090:Nlrc5 ^@ http://purl.uniprot.org/uniprot/C3VPR6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand ^@ 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|||NACHT|||Protein NLRC5 ^@ http://purl.uniprot.org/annotation/PRO_0000397867|||http://purl.uniprot.org/annotation/VSP_039702|||http://purl.uniprot.org/annotation/VSP_039703 http://togogenome.org/gene/10090:Hspa14 ^@ http://purl.uniprot.org/uniprot/Q99M31 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ Heat shock 70 kDa protein 14|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000289947|||http://purl.uniprot.org/annotation/VSP_026032 http://togogenome.org/gene/10090:Eddm13 ^@ http://purl.uniprot.org/uniprot/E9Q7F5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Epididymal protein 13 ^@ http://purl.uniprot.org/annotation/PRO_5003243118 http://togogenome.org/gene/10090:Pals2 ^@ http://purl.uniprot.org/uniprot/B9EHZ5|||http://purl.uniprot.org/uniprot/Q3UN60|||http://purl.uniprot.org/uniprot/Q9JLB0 ^@ 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 ^@ Guanylate kinase-like|||In isoform Alpha.|||L27|||L27 1|||L27 2|||PDZ|||Phosphotyrosine|||Protein PALS2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000094585|||http://purl.uniprot.org/annotation/VSP_003161 http://togogenome.org/gene/10090:Hspa9 ^@ http://purl.uniprot.org/uniprot/P38647 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In MOT-1.|||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|||Stress-70 protein, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000013564 http://togogenome.org/gene/10090:Tbc1d23 ^@ http://purl.uniprot.org/uniprot/Q8K0F1 ^@ 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 ^@ Fails to inhibit LPS-induced cytokine production.|||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_0000287498|||http://purl.uniprot.org/annotation/VSP_025520|||http://purl.uniprot.org/annotation/VSP_025521 http://togogenome.org/gene/10090:Krt77 ^@ http://purl.uniprot.org/uniprot/Q08EK5|||http://purl.uniprot.org/uniprot/Q6IFZ6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||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_0000063712 http://togogenome.org/gene/10090:Dpep3 ^@ http://purl.uniprot.org/uniprot/Q9DA79 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide ^@ Dipeptidase 3|||Disordered|||GPI-anchor amidated serine|||Interchain|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000231613|||http://purl.uniprot.org/annotation/PRO_0000231614 http://togogenome.org/gene/10090:Sox18 ^@ http://purl.uniprot.org/uniprot/P43680 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict ^@ 9aaTAD|||Disordered|||HMG box|||Important for transcriptional activation|||Interaction with DNA|||Sox C-terminal|||Transcription factor SOX-18 ^@ http://purl.uniprot.org/annotation/PRO_0000048768 http://togogenome.org/gene/10090:Ncoa5 ^@ http://purl.uniprot.org/uniprot/B7ZC24|||http://purl.uniprot.org/uniprot/Q91W39 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region ^@ 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_0000094412 http://togogenome.org/gene/10090:Chad ^@ http://purl.uniprot.org/uniprot/O55226|||http://purl.uniprot.org/uniprot/Q3TYW1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide ^@ Basic and acidic residues|||Chondroadherin|||Disordered|||LRR 1|||LRR 10|||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_0000032774|||http://purl.uniprot.org/annotation/PRO_5014309189 http://togogenome.org/gene/10090:Jmjd4 ^@ http://purl.uniprot.org/uniprot/Q8BFT6 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant ^@ 2-oxoglutarate and iron-dependent oxygenase JMJD4|||In isoform 3.|||In isoform 4.|||JmjC ^@ http://purl.uniprot.org/annotation/PRO_0000291960|||http://purl.uniprot.org/annotation/VSP_026326|||http://purl.uniprot.org/annotation/VSP_026327|||http://purl.uniprot.org/annotation/VSP_026328 http://togogenome.org/gene/10090:Pla2g2c ^@ http://purl.uniprot.org/uniprot/A2APR1|||http://purl.uniprot.org/uniprot/P48076 ^@ 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|||Sequence Conflict|||Signal Peptide ^@ Group IIC secretory phospholipase A2|||N-linked (GlcNAc...) asparagine|||Phospholipase A2 ^@ http://purl.uniprot.org/annotation/PRO_0000022753|||http://purl.uniprot.org/annotation/PRO_5015019324 http://togogenome.org/gene/10090:Klhl40 ^@ http://purl.uniprot.org/uniprot/A0A0R4J166|||http://purl.uniprot.org/uniprot/Q9D783 ^@ 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-like protein 40 ^@ http://purl.uniprot.org/annotation/PRO_0000274236|||http://purl.uniprot.org/annotation/VSP_022683|||http://purl.uniprot.org/annotation/VSP_022684 http://togogenome.org/gene/10090:Spata31d1c ^@ http://purl.uniprot.org/uniprot/E9QAF1|||http://purl.uniprot.org/uniprot/Q3V093 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||SPATA31|||SPATA31F3-like ^@ http://togogenome.org/gene/10090:Rae1 ^@ http://purl.uniprot.org/uniprot/Q8C570 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000237586 http://togogenome.org/gene/10090:Mfn2 ^@ http://purl.uniprot.org/uniprot/Q80U63 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Helical; Name=1|||Helical; Name=2|||In isoform 2.|||Mitochondrial intermembrane|||Mitofusin-2|||Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regions|||Phosphoserine|||Phosphothreonine; by PINK1 ^@ http://purl.uniprot.org/annotation/PRO_0000127676|||http://purl.uniprot.org/annotation/VSP_010365|||http://purl.uniprot.org/annotation/VSP_010366 http://togogenome.org/gene/10090:Scg3 ^@ http://purl.uniprot.org/uniprot/P47867 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Secretogranin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000005462|||http://purl.uniprot.org/annotation/VSP_042877 http://togogenome.org/gene/10090:Gip ^@ http://purl.uniprot.org/uniprot/P48756 ^@ Experimental Information|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Gastric inhibitory polypeptide ^@ http://purl.uniprot.org/annotation/PRO_0000011217|||http://purl.uniprot.org/annotation/PRO_0000011218|||http://purl.uniprot.org/annotation/PRO_0000011219 http://togogenome.org/gene/10090:Tbl1xr1 ^@ http://purl.uniprot.org/uniprot/Q8BHJ5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ Abolishes interaction with MECP2.|||Disordered|||Does not affect interaction with MECP2.|||F-box-like|||F-box-like/WD repeat-containing protein TBL1XR1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||LisH|||Mildly affects interaction with MECP2.|||N-acetylserine|||N6-acetyllysine|||Polar residues|||Removed|||Significantly decreases interaction with MECP2.|||Substantially reduces interaction with MECP2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||Weakly decreases interaction with MECP2. ^@ http://purl.uniprot.org/annotation/PRO_0000051267 http://togogenome.org/gene/10090:Fpgt ^@ http://purl.uniprot.org/uniprot/G5E8F4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Fucose-1-phosphate guanylyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000436384 http://togogenome.org/gene/10090:Gm20767 ^@ http://purl.uniprot.org/uniprot/O70517|||http://purl.uniprot.org/uniprot/Q3USZ4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Prr30 ^@ http://purl.uniprot.org/uniprot/Q9D9B7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Proline-rich protein 30 ^@ http://purl.uniprot.org/annotation/PRO_0000312278 http://togogenome.org/gene/10090:Tmem256 ^@ http://purl.uniprot.org/uniprot/Q5F285 ^@ 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_0000287171 http://togogenome.org/gene/10090:Reps2 ^@ http://purl.uniprot.org/uniprot/B9EI38|||http://purl.uniprot.org/uniprot/Q3UHE9|||http://purl.uniprot.org/uniprot/Q80XA6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ Disordered|||EF-hand|||EH|||EH 1|||EH 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_0000073832 http://togogenome.org/gene/10090:Necab3 ^@ http://purl.uniprot.org/uniprot/Q9D6J4 ^@ 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 ^@ ABM|||Disordered|||EF-hand|||In isoform 2.|||N-terminal EF-hand calcium-binding protein 3|||Required for interaction with APBA3 ^@ http://purl.uniprot.org/annotation/PRO_0000073864|||http://purl.uniprot.org/annotation/VSP_000740 http://togogenome.org/gene/10090:Cdc23 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1W7|||http://purl.uniprot.org/uniprot/G3X8W7|||http://purl.uniprot.org/uniprot/Q8BGZ4 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant ^@ Cdc23|||Cell division cycle protein 23 homolog|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||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_0000106271|||http://purl.uniprot.org/annotation/VSP_037679 http://togogenome.org/gene/10090:Armh3 ^@ http://purl.uniprot.org/uniprot/Q6PD19 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Armadillo-like helical domain-containing protein 3|||Helical|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000284516|||http://purl.uniprot.org/annotation/VSP_035671|||http://purl.uniprot.org/annotation/VSP_035672|||http://purl.uniprot.org/annotation/VSP_035673 http://togogenome.org/gene/10090:Wt1 ^@ http://purl.uniprot.org/uniprot/Q199A7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Erbin ^@ http://purl.uniprot.org/uniprot/B2RUJ2|||http://purl.uniprot.org/uniprot/B2RUK2|||http://purl.uniprot.org/uniprot/B7ZNX6|||http://purl.uniprot.org/uniprot/Q80TH2 ^@ 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 ^@ Decreases interaction with NOD2.|||Disordered|||Erbin|||In isoform 1.|||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|||PDZ|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000188302|||http://purl.uniprot.org/annotation/VSP_010808|||http://purl.uniprot.org/annotation/VSP_010809 http://togogenome.org/gene/10090:Or51a10 ^@ http://purl.uniprot.org/uniprot/Q924X8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mien1 ^@ http://purl.uniprot.org/uniprot/Q9CQ86 ^@ Chain|||Disulfide Bond|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide ^@ Chain|||Disulfide Bond|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide ^@ Migration and invasion enhancer 1|||N-acetylserine|||No effect on interaction with GPX1.|||Redox-active|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000265100|||http://purl.uniprot.org/annotation/PRO_0000396009 http://togogenome.org/gene/10090:Or8k28 ^@ http://purl.uniprot.org/uniprot/A2AK62 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp719 ^@ http://purl.uniprot.org/uniprot/Q8BIV1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Fndc8 ^@ http://purl.uniprot.org/uniprot/B2RQ03|||http://purl.uniprot.org/uniprot/Q9D2H8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ Fibronectin type III domain-containing protein 8|||Fibronectin type-III|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000284532|||http://purl.uniprot.org/annotation/VSP_024559 http://togogenome.org/gene/10090:Lats1 ^@ http://purl.uniprot.org/uniprot/Q8BYR2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ AGC-kinase C-terminal|||Basic and acidic residues|||Disordered|||Interaction with YAP1|||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_0000086233 http://togogenome.org/gene/10090:H4c11 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Tuba1b ^@ http://purl.uniprot.org/uniprot/P05213 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ 3'-nitrotyrosine|||5-glutamyl polyglutamate|||Detyrosinated tubulin alpha-1B chain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||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_0000048121|||http://purl.uniprot.org/annotation/PRO_0000437387 http://togogenome.org/gene/10090:Osr2 ^@ http://purl.uniprot.org/uniprot/Q91ZD1 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ Chain|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||Protein odd-skipped-related 2 ^@ http://purl.uniprot.org/annotation/PRO_0000047008|||http://purl.uniprot.org/annotation/VSP_017122 http://togogenome.org/gene/10090:Ccdc12 ^@ http://purl.uniprot.org/uniprot/Q8R344 ^@ 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 ^@ Coiled-coil domain-containing protein 12|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000076192 http://togogenome.org/gene/10090:Klhl18 ^@ http://purl.uniprot.org/uniprot/E9Q4F2 ^@ 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 18 ^@ http://purl.uniprot.org/annotation/PRO_0000449196 http://togogenome.org/gene/10090:Rgs4 ^@ http://purl.uniprot.org/uniprot/O08899|||http://purl.uniprot.org/uniprot/Q5D078 ^@ Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Lipid Binding|||Sequence Conflict ^@ RGS|||Regulator of G-protein signaling 4|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000204186 http://togogenome.org/gene/10090:Tmem273 ^@ http://purl.uniprot.org/uniprot/E9PVZ2 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015090357 http://togogenome.org/gene/10090:Lbr ^@ http://purl.uniprot.org/uniprot/Q3U9G9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Basic residues|||Delta(14)-sterol reductase LBR|||Disordered|||Helical|||N6-acetyllysine|||Nuclear|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Tudor ^@ http://purl.uniprot.org/annotation/PRO_0000227909 http://togogenome.org/gene/10090:Apc2 ^@ http://purl.uniprot.org/uniprot/G5E832 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Adenomatous polyposis coli N-terminal dimerisation|||Adenomatous polyposis coli protein basic|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Stim2 ^@ http://purl.uniprot.org/uniprot/A5CVE4|||http://purl.uniprot.org/uniprot/P83093 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EF-hand|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||SAM|||Stromal interaction molecule 2 ^@ http://purl.uniprot.org/annotation/PRO_0000218282 http://togogenome.org/gene/10090:Postn ^@ http://purl.uniprot.org/uniprot/A0A097BW18|||http://purl.uniprot.org/uniprot/A0A097BW21|||http://purl.uniprot.org/uniprot/Q62009 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||EMI|||FAS1|||FAS1 1|||FAS1 2|||FAS1 3|||FAS1 4|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Periostin|||S-cysteinyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000008790|||http://purl.uniprot.org/annotation/PRO_5001933180|||http://purl.uniprot.org/annotation/PRO_5010018531|||http://purl.uniprot.org/annotation/VSP_050666|||http://purl.uniprot.org/annotation/VSP_050667|||http://purl.uniprot.org/annotation/VSP_050668 http://togogenome.org/gene/10090:Smo ^@ http://purl.uniprot.org/uniprot/P56726|||http://purl.uniprot.org/uniprot/Q4VBD5|||http://purl.uniprot.org/uniprot/Q8BJN8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||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|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||FZ|||Failure to localize to primary cilia. Loss of cholesterol-induced activity.|||Frizzled/Smoothened 7TM|||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|||Interaction with BBS5 and BBS7|||Interaction with DLG5|||Loss of activity and cilium localization.|||Loss of activity in response to SHH.|||Loss of activity.|||Loss of cholesterol binding and reduced SHH-induced activation. No effect on basal signaling.|||Loss of cholesterol-induced activity.|||Loss of sterol binding and reduced response to SHH.|||Loss of sterol binding.|||N-linked (GlcNAc...) asparagine|||No effect on sterol binding.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein smoothened|||Reduced activity in response to SHH.|||Reduced protein levels, reduced activity and loss of localization to cilia.|||Reduced sterol binding.|||Remains responsive to SHH and 20S-hydroxycholesterol. Reduced basal signaling.|||Required for interaction with PRKACA ^@ http://purl.uniprot.org/annotation/PRO_0000013016|||http://purl.uniprot.org/annotation/PRO_5015097696 http://togogenome.org/gene/10090:Tpbgl ^@ http://purl.uniprot.org/uniprot/Q8C013 ^@ 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_0000419457 http://togogenome.org/gene/10090:Mcee ^@ http://purl.uniprot.org/uniprot/Q9D1I5 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Methylmalonyl-CoA epimerase, mitochondrial|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||VOC ^@ http://purl.uniprot.org/annotation/PRO_0000012284 http://togogenome.org/gene/10090:Or5m10 ^@ http://purl.uniprot.org/uniprot/A2ASU6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trmt13 ^@ http://purl.uniprot.org/uniprot/Q8BYH3 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Zinc Finger ^@ Basic and acidic residues|||CHHC U11-48K-type|||Disordered|||tRNA:m(4)X modification enzyme TRM13 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000236679 http://togogenome.org/gene/10090:C1ql4 ^@ http://purl.uniprot.org/uniprot/Q4ZJM9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Signal Peptide ^@ C1q|||Collagen-like|||Complement C1q-like protein 4|||Disordered|||Does not affect homo-, nor heterooligomerization with C1QL1, C1QL2 and C1QL3; when associated with A-28. Increased secretion; when associated with A-28. Does not impair inhibition of adipocyte differentiation; when associated with A-28.|||Does not affect homo-, nor heterooligomerization with C1QL1, C1QL2 and C1QL3; when associated with A-32. Increased secretion; when associated with A-32. Does not impair inhibition of adipocyte differentiation; when associated with A-32.|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000274339 http://togogenome.org/gene/10090:Hmgn2 ^@ http://purl.uniprot.org/uniprot/P09602|||http://purl.uniprot.org/uniprot/Q5BL14 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region ^@ ADP-ribosylserine; alternate|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6-acetyllysine; alternate|||Non-histone chromosomal protein HMG-17|||Phosphoserine|||Phosphoserine; alternate|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000206698 http://togogenome.org/gene/10090:H2al1f ^@ http://purl.uniprot.org/uniprot/Q5M8Q2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Histone H2A-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000440627 http://togogenome.org/gene/10090:Slc22a17 ^@ http://purl.uniprot.org/uniprot/Q9D9E0 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Solute carrier family 22 member 17 ^@ http://purl.uniprot.org/annotation/PRO_0000398633|||http://purl.uniprot.org/annotation/VSP_039789 http://togogenome.org/gene/10090:Vps35 ^@ http://purl.uniprot.org/uniprot/Q3TRJ1|||http://purl.uniprot.org/uniprot/Q9EQH3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||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_0000065897 http://togogenome.org/gene/10090:Pdgfd ^@ http://purl.uniprot.org/uniprot/Q925I7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ CUB|||Cleavage|||In isoform 2.|||In isoform 3.|||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_0000250190|||http://purl.uniprot.org/annotation/PRO_0000250191|||http://purl.uniprot.org/annotation/VSP_020616|||http://purl.uniprot.org/annotation/VSP_020617|||http://purl.uniprot.org/annotation/VSP_020618 http://togogenome.org/gene/10090:Mier3 ^@ http://purl.uniprot.org/uniprot/B9EHL0|||http://purl.uniprot.org/uniprot/Q3UHF3 ^@ 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|||ELM2|||In isoform 2.|||Mesoderm induction early response protein 3|||Phosphoserine|||Phosphothreonine|||Polar residues|||SANT ^@ http://purl.uniprot.org/annotation/PRO_0000313682|||http://purl.uniprot.org/annotation/VSP_030104|||http://purl.uniprot.org/annotation/VSP_030105 http://togogenome.org/gene/10090:Rnf44 ^@ http://purl.uniprot.org/uniprot/E9PUC0|||http://purl.uniprot.org/uniprot/Q3UHJ8 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||RING finger protein 44|||RING-type|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000273414|||http://purl.uniprot.org/annotation/VSP_022550|||http://purl.uniprot.org/annotation/VSP_022551 http://togogenome.org/gene/10090:Or4p23 ^@ http://purl.uniprot.org/uniprot/Q7TR12 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wdr37 ^@ http://purl.uniprot.org/uniprot/Q05BF4|||http://purl.uniprot.org/uniprot/Q8C8P3|||http://purl.uniprot.org/uniprot/Q8CBE3 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||In mouse mutant radical; reduced circulating B cells.|||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_0000051388 http://togogenome.org/gene/10090:Or1ab2 ^@ http://purl.uniprot.org/uniprot/Q7TRY0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ctdsp1 ^@ http://purl.uniprot.org/uniprot/P58466|||http://purl.uniprot.org/uniprot/Q5I0X8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Site ^@ 4-aspartylphosphate intermediate|||Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1|||Disordered|||FCP1 homology|||Leads to enhanced neuronal differentiation of stem cells; when associated with E-96.|||Leads to enhanced neuronal differentiation of stem cells; when associated with N-98.|||N-acetylmethionine|||Proton donor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000212573 http://togogenome.org/gene/10090:Slc4a10 ^@ http://purl.uniprot.org/uniprot/B1AWV9|||http://purl.uniprot.org/uniprot/Q5DTL9|||http://purl.uniprot.org/uniprot/Q8C943|||http://purl.uniprot.org/uniprot/R4H243 ^@ Binding Site|||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|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Band 3 cytoplasmic|||Basic residues|||Bicarbonate transporter-like transmembrane|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2, isoform 3, isoform 5, isoform 7 and isoform 9.|||In isoform 3, isoform 4, isoform 7 and isoform 8.|||In isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10.|||In isoform 9 and isoform 10.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced recovery of intracellular sodium-dependent pH.|||Sodium-driven chloride bicarbonate exchanger ^@ http://purl.uniprot.org/annotation/PRO_0000245241|||http://purl.uniprot.org/annotation/VSP_019654|||http://purl.uniprot.org/annotation/VSP_060132|||http://purl.uniprot.org/annotation/VSP_060133|||http://purl.uniprot.org/annotation/VSP_060134 http://togogenome.org/gene/10090:Hlcs ^@ http://purl.uniprot.org/uniprot/Q3TZ03|||http://purl.uniprot.org/uniprot/Q920N2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ BPL/LPL catalytic|||Biotin--protein ligase|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000064980 http://togogenome.org/gene/10090:Nif3l1 ^@ http://purl.uniprot.org/uniprot/Q9EQ80 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Mediates interaction with COPS2|||N6-acetyllysine|||NIF3-like protein 1|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000147354 http://togogenome.org/gene/10090:2700049A03Rik ^@ http://purl.uniprot.org/uniprot/E9PV87|||http://purl.uniprot.org/uniprot/E9Q0E2 ^@ 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|||Phosphothreonine|||Polar residues|||Pro residues|||Protein TALPID3|||Required for centrosomal localization ^@ http://purl.uniprot.org/annotation/PRO_0000420181 http://togogenome.org/gene/10090:1700123K08Rik ^@ http://purl.uniprot.org/uniprot/Q9D991 ^@ Domain Extent|||Region ^@ Domain Extent ^@ N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Dusp29 ^@ http://purl.uniprot.org/uniprot/Q8BK84 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site ^@ Does not affect AMPK activity.|||Dual specificity phosphatase 29|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000295879 http://togogenome.org/gene/10090:Zzef1 ^@ http://purl.uniprot.org/uniprot/A0A140LJ04|||http://purl.uniprot.org/uniprot/Q5SSH7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||DOC|||Disordered|||EF-hand|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||ZZ-type|||ZZ-type 1|||ZZ-type 2|||Zinc finger ZZ-type and EF-hand domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000289001|||http://purl.uniprot.org/annotation/VSP_025876|||http://purl.uniprot.org/annotation/VSP_025877 http://togogenome.org/gene/10090:Fkbp8 ^@ http://purl.uniprot.org/uniprot/O35465 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP8|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000075332|||http://purl.uniprot.org/annotation/VSP_034487 http://togogenome.org/gene/10090:Prrc2a ^@ http://purl.uniprot.org/uniprot/Q7TSC1 ^@ 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 ^@ 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|||Basic and acidic residues|||Disordered|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein PRRC2A ^@ http://purl.uniprot.org/annotation/PRO_0000064831 http://togogenome.org/gene/10090:Mpeg1 ^@ http://purl.uniprot.org/uniprot/A1L314|||http://purl.uniprot.org/uniprot/E9QN37 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn ^@ Abolished binding to target membranes.|||Abolishes ubiquitination and antibacterial activity and results in diffuse perinuclear distribution.|||Beta stranded; Name=TMH1|||Beta stranded; Name=TMH2|||Cleavage; by LGMN|||Cleavage; by trypsin|||Helical|||MACPF|||Macrophage-expressed gene 1 protein|||Macrophage-expressed gene 1 protein, processed form|||N-linked (GlcNAc...) asparagine|||P2 ^@ http://purl.uniprot.org/annotation/PRO_0000459023|||http://purl.uniprot.org/annotation/PRO_5000142312|||http://purl.uniprot.org/annotation/PRO_5003246286 http://togogenome.org/gene/10090:Or9g19 ^@ http://purl.uniprot.org/uniprot/Q7TR96 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||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|||Olfactory receptor 9G19 ^@ http://purl.uniprot.org/annotation/PRO_0000393947 http://togogenome.org/gene/10090:Pde6c ^@ http://purl.uniprot.org/uniprot/Q91ZQ1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Splice Variant ^@ Basic and acidic residues|||Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'|||Cysteine methyl ester|||Disordered|||GAF 1|||GAF 2|||In isoform 2.|||PDEase|||Proton donor|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000226068|||http://purl.uniprot.org/annotation/PRO_0000370789|||http://purl.uniprot.org/annotation/VSP_017422 http://togogenome.org/gene/10090:Rpl7l1 ^@ http://purl.uniprot.org/uniprot/Q9D8M4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Large ribosomal subunit protein uL30-like 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000346777 http://togogenome.org/gene/10090:Hoxc5 ^@ http://purl.uniprot.org/uniprot/P32043 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Motif|||Region|||Sequence Conflict ^@ Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-C5 ^@ http://purl.uniprot.org/annotation/PRO_0000200170 http://togogenome.org/gene/10090:Tex22 ^@ http://purl.uniprot.org/uniprot/Q9D9U4 ^@ 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|||Testis-expressed protein 22 ^@ http://purl.uniprot.org/annotation/PRO_0000410918 http://togogenome.org/gene/10090:Ccdc71l ^@ http://purl.uniprot.org/uniprot/E9Q4T4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic residues|||Disordered ^@ http://togogenome.org/gene/10090:Trim33 ^@ http://purl.uniprot.org/uniprot/E9QME5|||http://purl.uniprot.org/uniprot/E9QP19|||http://purl.uniprot.org/uniprot/Q99PP7 ^@ 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|||Splice Variant|||Zinc Finger ^@ Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||B box-type|||B box-type 1|||B box-type 2|||Basic and acidic residues|||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 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_0000056396|||http://purl.uniprot.org/annotation/VSP_012068 http://togogenome.org/gene/10090:Or14a259 ^@ http://purl.uniprot.org/uniprot/Q7TS02 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rnps1 ^@ http://purl.uniprot.org/uniprot/Q99M28 ^@ 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.|||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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RNA-binding protein with serine-rich domain 1|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081817|||http://purl.uniprot.org/annotation/VSP_016244 http://togogenome.org/gene/10090:Nrbf2 ^@ http://purl.uniprot.org/uniprot/Q8VCQ3 ^@ Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Nuclear receptor interaction motif|||Nuclear receptor-binding factor 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000235817 http://togogenome.org/gene/10090:Ccn5 ^@ http://purl.uniprot.org/uniprot/A2AHD1|||http://purl.uniprot.org/uniprot/Q9Z0G4 ^@ 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 ^@ CCN family member 5|||IGFBP N-terminal|||N-linked (GlcNAc...) asparagine|||TSP type-1|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000014410|||http://purl.uniprot.org/annotation/PRO_5015086021 http://togogenome.org/gene/10090:Klrb1 ^@ http://purl.uniprot.org/uniprot/A0A1U9W1A8|||http://purl.uniprot.org/uniprot/Q0ZUP1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Killer cell lectin-like receptor subfamily B member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000317213 http://togogenome.org/gene/10090:Aspg ^@ http://purl.uniprot.org/uniprot/A0JNU3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ 60 kDa lysophospholipase|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Acyl-ester intermediate|||Asparaginase|||Asparaginase/glutaminase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000324164 http://togogenome.org/gene/10090:Rplp0 ^@ http://purl.uniprot.org/uniprot/P14869|||http://purl.uniprot.org/uniprot/Q5M8R8 ^@ 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 ^@ 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)|||Large ribosomal subunit protein uL10|||Large ribosomal subunit protein uL10-like insertion|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000154759 http://togogenome.org/gene/10090:Tstd1 ^@ http://purl.uniprot.org/uniprot/E9PY03 ^@ Active Site|||Domain Extent|||Region|||Site ^@ Active Site|||Domain Extent ^@ Cysteine persulfide intermediate|||Rhodanese ^@ http://togogenome.org/gene/10090:Cdc20b ^@ http://purl.uniprot.org/uniprot/D3Z3I0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ Cell division cycle protein 20 homolog B|||Disordered|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000458670 http://togogenome.org/gene/10090:Cops2 ^@ http://purl.uniprot.org/uniprot/P61202|||http://purl.uniprot.org/uniprot/Q3V3N6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ COP9 signalosome complex subunit 2|||In isoform 2.|||Mediates interaction with NIF3L1|||PCI ^@ http://purl.uniprot.org/annotation/PRO_0000120969|||http://purl.uniprot.org/annotation/VSP_011885 http://togogenome.org/gene/10090:Vmn2r22 ^@ http://purl.uniprot.org/uniprot/E9Q7S8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003243123 http://togogenome.org/gene/10090:Acnat2 ^@ http://purl.uniprot.org/uniprot/Q8BGG9 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Motif|||Sequence Conflict|||Splice Variant ^@ Acyl-coenzyme A amino acid N-acyltransferase 2|||Charge relay system|||In isoform 2.|||Microbody targeting signal ^@ http://purl.uniprot.org/annotation/PRO_0000352775|||http://purl.uniprot.org/annotation/VSP_052954 http://togogenome.org/gene/10090:Il1rn ^@ http://purl.uniprot.org/uniprot/P25085|||http://purl.uniprot.org/uniprot/Q542C7 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Interleukin-1|||Interleukin-1 receptor antagonist protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015330|||http://purl.uniprot.org/annotation/PRO_5010843980|||http://purl.uniprot.org/annotation/VSP_002652 http://togogenome.org/gene/10090:Mea1 ^@ http://purl.uniprot.org/uniprot/Q64327 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Male-enhanced antigen 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000096342 http://togogenome.org/gene/10090:Actn1 ^@ http://purl.uniprot.org/uniprot/A1BN54|||http://purl.uniprot.org/uniprot/Q7TPR4 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Site|||Strand ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Strand ^@ Actin-binding|||Alpha-actinin-1|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||EF-hand|||EF-hand 1|||EF-hand 2|||Interaction with DDN|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine; by FAK1|||Shows less organization of the circumferential actin-filament network compared to controls.|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4 ^@ http://purl.uniprot.org/annotation/PRO_0000073432 http://togogenome.org/gene/10090:Slpi ^@ http://purl.uniprot.org/uniprot/P97430|||http://purl.uniprot.org/uniprot/Q548X8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Region|||Signal Peptide|||Site ^@ Antileukoproteinase|||Elastase inhibitory domain|||Loss of antimicrobial activity.|||Loss of antimicrobial activity; when associated with A-92.|||Loss of antimicrobial activity; when associated with A-96.|||Reactive bond for chymotrypsin, trypsin and elastase|||WAP|||WAP 1|||WAP 2 ^@ http://purl.uniprot.org/annotation/PRO_0000041356|||http://purl.uniprot.org/annotation/PRO_5014309602 http://togogenome.org/gene/10090:Laptm4b ^@ http://purl.uniprot.org/uniprot/B2CZK6|||http://purl.uniprot.org/uniprot/Q91XQ6 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Helical|||Lysosomal-associated transmembrane protein 4B|||Required for NEDD4 interaction ^@ http://purl.uniprot.org/annotation/PRO_0000249723 http://togogenome.org/gene/10090:Or5b124 ^@ http://purl.uniprot.org/uniprot/Q8VFQ5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lhx8 ^@ http://purl.uniprot.org/uniprot/O35652 ^@ 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 ^@ Disordered|||Homeobox|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx8|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000075797 http://togogenome.org/gene/10090:Or4g17 ^@ http://purl.uniprot.org/uniprot/Q8VF29 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cct4 ^@ http://purl.uniprot.org/uniprot/P80315|||http://purl.uniprot.org/uniprot/Q564F4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||T-complex protein 1 subunit delta ^@ http://purl.uniprot.org/annotation/PRO_0000128333 http://togogenome.org/gene/10090:Snx32 ^@ http://purl.uniprot.org/uniprot/Q80ZJ7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PX|||Polar residues|||Sorting nexin-32 ^@ http://purl.uniprot.org/annotation/PRO_0000320708 http://togogenome.org/gene/10090:Asxl1 ^@ http://purl.uniprot.org/uniprot/P59598|||http://purl.uniprot.org/uniprot/Q24JP2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Zinc Finger ^@ Basic and acidic residues|||DEUBAD|||Disordered|||HTH HARE-type|||Interaction with NCOA1|||LXXLL motif 1|||LXXLL motif 2|||Nuclear localization signal|||PHD-type; atypical|||Phosphoserine|||Polar residues|||Polycomb group protein ASXL1|||Required for interaction with RARA ^@ http://purl.uniprot.org/annotation/PRO_0000059322 http://togogenome.org/gene/10090:Taok2 ^@ http://purl.uniprot.org/uniprot/Q6ZQ29 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Transmembrane ^@ Acidic residues|||Disordered|||Helical|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase TAO2 ^@ http://purl.uniprot.org/annotation/PRO_0000086734|||http://purl.uniprot.org/annotation/VSP_040543|||http://purl.uniprot.org/annotation/VSP_040544 http://togogenome.org/gene/10090:Hdac4 ^@ http://purl.uniprot.org/uniprot/Q6NZM9 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||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 SUMO)|||Histone deacetylase|||Histone deacetylase 4|||In isoform 2.|||Interaction with MEF2A|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000281033|||http://purl.uniprot.org/annotation/VSP_023952|||http://purl.uniprot.org/annotation/VSP_023953 http://togogenome.org/gene/10090:Tspan18 ^@ http://purl.uniprot.org/uniprot/Q80WR1 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-18 ^@ http://purl.uniprot.org/annotation/PRO_0000219269 http://togogenome.org/gene/10090:Msrb2 ^@ http://purl.uniprot.org/uniprot/Q78J03 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Strand|||Transit Peptide|||Turn ^@ Disordered|||Methionine-R-sulfoxide reductase B2, mitochondrial|||Mitochondrion|||MsrB|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000327243 http://togogenome.org/gene/10090:Hnrnpc ^@ http://purl.uniprot.org/uniprot/Q9Z204 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||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|||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); 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 and isoform 5.|||In isoform 4.|||In isoform C1, isoform 3 and isoform 4.|||N-acetylalanine|||N6-acetyllysine; alternate|||Nuclear localization signal|||Phosphoserine|||Polar residues|||RRM|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000081845|||http://purl.uniprot.org/annotation/VSP_005832|||http://purl.uniprot.org/annotation/VSP_005833|||http://purl.uniprot.org/annotation/VSP_019227 http://togogenome.org/gene/10090:Eml1 ^@ http://purl.uniprot.org/uniprot/D3Z4J9|||http://purl.uniprot.org/uniprot/Q05BC3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||Echinoderm microtubule-associated protein-like 1|||HELP|||Impairs tubulin binding.|||In isoform 2.|||In isoform 3.|||Polar residues|||Tandem atypical propeller in EMLs|||WD|||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_0000284386|||http://purl.uniprot.org/annotation/VSP_024477|||http://purl.uniprot.org/annotation/VSP_024478 http://togogenome.org/gene/10090:Rab43 ^@ http://purl.uniprot.org/uniprot/Q8CG50 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif ^@ Cysteine methyl ester|||Effector region|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-43|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000244616 http://togogenome.org/gene/10090:Myadml2 ^@ http://purl.uniprot.org/uniprot/Q08AU7 ^@ 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.|||MARVEL 1|||MARVEL 2|||Myeloid-associated differentiation marker-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000332207|||http://purl.uniprot.org/annotation/VSP_033351|||http://purl.uniprot.org/annotation/VSP_033352 http://togogenome.org/gene/10090:Usp22 ^@ http://purl.uniprot.org/uniprot/Q5DU02 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger ^@ N6-acetyllysine|||Nucleophile|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 22 ^@ http://purl.uniprot.org/annotation/PRO_0000080651 http://togogenome.org/gene/10090:Stx12 ^@ http://purl.uniprot.org/uniprot/Q9ER00 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||N-acetylserine|||Phosphoserine|||Removed|||Syntaxin-12|||Vesicular|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000210224 http://togogenome.org/gene/10090:Mex3b ^@ http://purl.uniprot.org/uniprot/F8WJD6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Pro residues|||RING-type ^@ http://togogenome.org/gene/10090:Kif3c ^@ http://purl.uniprot.org/uniprot/O35066|||http://purl.uniprot.org/uniprot/Q571A6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Disordered|||Globular|||Kinesin motor|||Kinesin-like protein KIF3C|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000125398 http://togogenome.org/gene/10090:Cds2 ^@ http://purl.uniprot.org/uniprot/A2AMQ5|||http://purl.uniprot.org/uniprot/Q6PBC0|||http://purl.uniprot.org/uniprot/Q8BX08|||http://purl.uniprot.org/uniprot/Q99L43 ^@ 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|||Phosphatidate cytidylyltransferase 2|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000090717 http://togogenome.org/gene/10090:Saxo1 ^@ http://purl.uniprot.org/uniprot/B1AXP3 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Zfhx4 ^@ http://purl.uniprot.org/uniprot/E9Q5A7|||http://purl.uniprot.org/uniprot/Q6P8L4 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Homeobox|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Chic1 ^@ http://purl.uniprot.org/uniprot/A2RT09|||http://purl.uniprot.org/uniprot/Q8CBW7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Acidic residues|||Cysteine-rich hydrophobic domain-containing protein 1|||Disordered|||Golgin subfamily A member 7/ERF4|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000189555 http://togogenome.org/gene/10090:Cox7b ^@ http://purl.uniprot.org/uniprot/P56393 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Helix|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Cytochrome c oxidase subunit 7B, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000006159 http://togogenome.org/gene/10090:Gal3st1 ^@ http://purl.uniprot.org/uniprot/Q9JHE4 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||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_0000085202 http://togogenome.org/gene/10090:Ptgds ^@ http://purl.uniprot.org/uniprot/O09114 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ In isoform 2.|||Loss of enzyme activity. No effect on ligand binding.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Prostaglandin-H2 D-isomerase|||Pyrrolidone carboxylic acid|||Reduces enzyme activity by about half. Reduces enzyme activity tenfold; when associated with A-45 and A-81.|||Reduces enzyme activity by about half. Reduces enzyme activity tenfold; when associated with A-67 and A-81.|||Slightly reduced enzyme activity. half. Reduces enzyme activity tenfold; when associated with A-45 and A-67. ^@ http://purl.uniprot.org/annotation/PRO_0000017947|||http://purl.uniprot.org/annotation/VSP_041029 http://togogenome.org/gene/10090:Chchd6 ^@ http://purl.uniprot.org/uniprot/E9Q4M4|||http://purl.uniprot.org/uniprot/Q91VN4 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||MICOS complex subunit Mic25|||N-myristoyl glycine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000129170 http://togogenome.org/gene/10090:Cul1 ^@ http://purl.uniprot.org/uniprot/Q9WTX6 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Crosslink|||Modified Residue|||Sequence Conflict ^@ Cullin-1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||Omega-N-methylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000119788 http://togogenome.org/gene/10090:Nsmce2 ^@ http://purl.uniprot.org/uniprot/Q91VT1 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ E3 SUMO-protein ligase NSE2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||SP-RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000270940|||http://purl.uniprot.org/annotation/VSP_022250 http://togogenome.org/gene/10090:Kat2b ^@ http://purl.uniprot.org/uniprot/B2RR30|||http://purl.uniprot.org/uniprot/Q9JHD1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Turn ^@ Basic and acidic residues|||Bromo|||Disordered|||Histone acetyltransferase KAT2B|||N-acetyltransferase|||Polar residues|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000322986 http://togogenome.org/gene/10090:Rad50 ^@ http://purl.uniprot.org/uniprot/Q5SV02 ^@ Binding Site|||Coiled-Coil|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Domain Extent ^@ Zinc-hook ^@ http://togogenome.org/gene/10090:Chrna1 ^@ http://purl.uniprot.org/uniprot/P04756|||http://purl.uniprot.org/uniprot/Q05A24 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Acetylcholine receptor subunit alpha|||Associated with receptor activation|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000306|||http://purl.uniprot.org/annotation/PRO_5014306688 http://togogenome.org/gene/10090:Slc38a1 ^@ http://purl.uniprot.org/uniprot/Q8K2P7 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Affects N-glycosylation. Abolishes Nglycosylation; when associated with Q-251 and Q-310. Does not affect cell membrane localization. Abolishes L-glutamine transport activity; when associated with Q-251.|||Affects N-glycosylation. Abolishes Nglycosylation; when associated with Q-257 and Q-310. Does not affect cell membrane localization. Abolishes L-glutamine transport activity; when associated with Q-257.|||Cytoplasmic|||Does not affect N-glycosylation. Abolishes Nglycosylation; when associated with Q-251 and Q-257. Does not affect cell membrane localization.|||Does not affect N-glycosylation. Does not affect cell membrane localization.|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Sodium-coupled neutral amino acid symporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000310476|||http://purl.uniprot.org/annotation/VSP_029305|||http://purl.uniprot.org/annotation/VSP_029306|||http://purl.uniprot.org/annotation/VSP_029307|||http://purl.uniprot.org/annotation/VSP_029308 http://togogenome.org/gene/10090:Alcam ^@ http://purl.uniprot.org/uniprot/E9Q3Q6|||http://purl.uniprot.org/uniprot/Q3TTY3|||http://purl.uniprot.org/uniprot/Q54AJ5|||http://purl.uniprot.org/uniprot/Q61490 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014660|||http://purl.uniprot.org/annotation/PRO_5003245858|||http://purl.uniprot.org/annotation/PRO_5009971115 http://togogenome.org/gene/10090:Fam183b ^@ http://purl.uniprot.org/uniprot/A0A0R4J0N6|||http://purl.uniprot.org/uniprot/D2D553|||http://purl.uniprot.org/uniprot/Q5NC57 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||Protein FAM183B ^@ http://purl.uniprot.org/annotation/PRO_0000340272|||http://purl.uniprot.org/annotation/VSP_034207 http://togogenome.org/gene/10090:Tmem186 ^@ http://purl.uniprot.org/uniprot/Q78HW2|||http://purl.uniprot.org/uniprot/Q9CR76 ^@ 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|||Disordered|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Transmembrane protein 186 ^@ http://purl.uniprot.org/annotation/PRO_0000279440 http://togogenome.org/gene/10090:Cyp2b13 ^@ http://purl.uniprot.org/uniprot/A6H6J2 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Cytochrome P450 ^@ http://purl.uniprot.org/annotation/PRO_5015086521 http://togogenome.org/gene/10090:Hoxc9 ^@ http://purl.uniprot.org/uniprot/P09633 ^@ Chain|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Modified Residue|||Region ^@ Disordered|||Homeobox|||Homeobox protein Hox-C9|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000200185 http://togogenome.org/gene/10090:Lipc ^@ http://purl.uniprot.org/uniprot/P27656|||http://purl.uniprot.org/uniprot/Q3TYU0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Essential for determining substrate specificity|||Hepatic triacylglycerol lipase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PLAT ^@ http://purl.uniprot.org/annotation/PRO_0000017770 http://togogenome.org/gene/10090:Bcl11b ^@ http://purl.uniprot.org/uniprot/A0A0R4J1E1|||http://purl.uniprot.org/uniprot/Q99PV8 ^@ 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|||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 gamma induced thymic lymphomas.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000047105|||http://purl.uniprot.org/annotation/VSP_009566|||http://purl.uniprot.org/annotation/VSP_009568 http://togogenome.org/gene/10090:Syngr4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0K3|||http://purl.uniprot.org/uniprot/D3Z3G3|||http://purl.uniprot.org/uniprot/Q9Z1L2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||MARVEL|||Polar residues|||Synaptogyrin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000183999 http://togogenome.org/gene/10090:Ptpa ^@ http://purl.uniprot.org/uniprot/P58389|||http://purl.uniprot.org/uniprot/Q543N6 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylalanine|||Removed|||Serine/threonine-protein phosphatase 2A activator ^@ http://purl.uniprot.org/annotation/PRO_0000071525 http://togogenome.org/gene/10090:Ugt1a5 ^@ http://purl.uniprot.org/uniprot/B2RT14|||http://purl.uniprot.org/uniprot/Q6XL48 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||UDP-glucuronosyltransferase ^@ http://purl.uniprot.org/annotation/PRO_5005144156|||http://purl.uniprot.org/annotation/PRO_5015019388 http://togogenome.org/gene/10090:Myo7b ^@ http://purl.uniprot.org/uniprot/Q99MZ6 ^@ 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 ^@ Actin-binding|||FERM 1|||FERM 2|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||IQ 6|||Mediates interaction with ANKS4B|||Mediates interaction with CDHR2, CDHR5 and USH1C|||MyTH4 1|||MyTH4 2|||MyTH4 3|||Myosin motor|||Phosphoserine|||Phosphothreonine|||SH3|||Unconventional myosin-VIIb ^@ http://purl.uniprot.org/annotation/PRO_0000329047 http://togogenome.org/gene/10090:Slc34a1 ^@ http://purl.uniprot.org/uniprot/Q9D2V6 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Hsd17b11 ^@ http://purl.uniprot.org/uniprot/Q9EQ06 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Signal Peptide|||Splice Variant ^@ Estradiol 17-beta-dehydrogenase 11|||In isoform 2.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000031971|||http://purl.uniprot.org/annotation/VSP_015013|||http://purl.uniprot.org/annotation/VSP_015014 http://togogenome.org/gene/10090:Rab40c ^@ http://purl.uniprot.org/uniprot/Q0PD11|||http://purl.uniprot.org/uniprot/Q8VHQ4 ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Region ^@ Disordered|||Ras-related protein Rab-40C|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000121262 http://togogenome.org/gene/10090:Fcmr ^@ http://purl.uniprot.org/uniprot/A0A0G2LB91|||http://purl.uniprot.org/uniprot/A1KXC4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fas apoptotic inhibitory molecule 3|||Helical|||Ig-like|||Immunoglobulin V-set|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284422|||http://purl.uniprot.org/annotation/PRO_5002547199 http://togogenome.org/gene/10090:Jmjd8 ^@ http://purl.uniprot.org/uniprot/A0A9L6H220|||http://purl.uniprot.org/uniprot/Q3TA59 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ JmjC|||JmjC domain-containing protein 8|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000344532|||http://purl.uniprot.org/annotation/PRO_5040195845 http://togogenome.org/gene/10090:Cd302 ^@ http://purl.uniprot.org/uniprot/Q9DCG2 ^@ 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 ^@ C-type lectin|||CD302 antigen|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000252333|||http://purl.uniprot.org/annotation/VSP_020910 http://togogenome.org/gene/10090:Gopc ^@ http://purl.uniprot.org/uniprot/Q8BH60 ^@ 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|||Splice Variant ^@ Golgi-associated PDZ and coiled-coil motif-containing protein|||In isoform 2.|||N-acetylserine|||PDZ|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087543|||http://purl.uniprot.org/annotation/VSP_016065 http://togogenome.org/gene/10090:Rgcc ^@ http://purl.uniprot.org/uniprot/Q9DBX1 ^@ 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|||Phosphothreonine|||Polar residues|||Regulator of cell cycle RGCC ^@ http://purl.uniprot.org/annotation/PRO_0000274702 http://togogenome.org/gene/10090:Dlgap3 ^@ http://purl.uniprot.org/uniprot/B1AS06|||http://purl.uniprot.org/uniprot/Q3TY61|||http://purl.uniprot.org/uniprot/Q6PFD5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||Basic residues|||Disks large-associated protein 3|||Disordered|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000174295 http://togogenome.org/gene/10090:Or14j8 ^@ http://purl.uniprot.org/uniprot/Q7TRJ0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zbtb2 ^@ http://purl.uniprot.org/uniprot/Q3V1Q5|||http://purl.uniprot.org/uniprot/Q3V3W4|||http://purl.uniprot.org/uniprot/Q69ZI2 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue|||Region ^@ BTB|||C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Nynrin ^@ http://purl.uniprot.org/uniprot/Q5DTZ0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Integrase catalytic|||Polar residues|||Pro residues|||Protein NYNRIN|||RNase H type-1|||RNase NYN ^@ http://purl.uniprot.org/annotation/PRO_0000314175 http://togogenome.org/gene/10090:Cited4 ^@ http://purl.uniprot.org/uniprot/A2A7E7|||http://purl.uniprot.org/uniprot/Q9WUL8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant ^@ Cbp/p300-interacting transactivator 4|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000233310|||http://purl.uniprot.org/annotation/VSP_052035|||http://purl.uniprot.org/annotation/VSP_052036 http://togogenome.org/gene/10090:Fzd9 ^@ http://purl.uniprot.org/uniprot/Q9R216 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||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_0000013004 http://togogenome.org/gene/10090:Gab3 ^@ http://purl.uniprot.org/uniprot/Q8BSM5 ^@ 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 ^@ Acidic residues|||Disordered|||GRB2-associated-binding protein 3|||PH|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000318940 http://togogenome.org/gene/10090:Dbh ^@ http://purl.uniprot.org/uniprot/Q64237 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cleavage|||Cytoplasmic|||DOMON|||Disordered|||Dopamine beta-hydroxylase|||Helical; Signal-anchor for type II membrane protein|||Interchain|||Intragranular|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by CaMK|||Polar residues|||Soluble dopamine beta-hydroxylase ^@ http://purl.uniprot.org/annotation/PRO_0000006357|||http://purl.uniprot.org/annotation/PRO_0000308210 http://togogenome.org/gene/10090:Atp1a1 ^@ http://purl.uniprot.org/uniprot/Q8VDN2 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Propeptide|||Region|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||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_0000002485|||http://purl.uniprot.org/annotation/PRO_0000002486 http://togogenome.org/gene/10090:Csn1s2a ^@ http://purl.uniprot.org/uniprot/A0A0G2JET6|||http://purl.uniprot.org/uniprot/A0A0G2JGC6|||http://purl.uniprot.org/uniprot/Q02862|||http://purl.uniprot.org/uniprot/Q3TP41|||http://purl.uniprot.org/uniprot/Q547D1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Modified Residue|||Region|||Signal Peptide ^@ Alpha-S2-casein-like A|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000004467|||http://purl.uniprot.org/annotation/PRO_5012587989|||http://purl.uniprot.org/annotation/PRO_5012610446|||http://purl.uniprot.org/annotation/PRO_5014309596|||http://purl.uniprot.org/annotation/PRO_5015097449 http://togogenome.org/gene/10090:Adissp ^@ http://purl.uniprot.org/uniprot/Q9D1K7 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Adipose-secreted signaling protein|||N-acetylalanine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000079420 http://togogenome.org/gene/10090:Ifit2 ^@ http://purl.uniprot.org/uniprot/Q64112|||http://purl.uniprot.org/uniprot/Q6GTM0 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||Interferon-induced protein with tetratricopeptide repeats 2|||N-acetylserine|||Removed|||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_0000106348 http://togogenome.org/gene/10090:Mpo ^@ http://purl.uniprot.org/uniprot/P11247|||http://purl.uniprot.org/uniprot/Q571G0|||http://purl.uniprot.org/uniprot/Q7TMS4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Cysteine sulfenic acid (-SOH)|||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/PRO_0000023657|||http://purl.uniprot.org/annotation/PRO_0000023658|||http://purl.uniprot.org/annotation/PRO_0000023659|||http://purl.uniprot.org/annotation/PRO_0000023660|||http://purl.uniprot.org/annotation/PRO_5004250865|||http://purl.uniprot.org/annotation/PRO_5004291627 http://togogenome.org/gene/10090:Gpx7 ^@ http://purl.uniprot.org/uniprot/Q3TNK3|||http://purl.uniprot.org/uniprot/Q99LJ6 ^@ Active Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Signal Peptide ^@ Glutathione peroxidase|||Glutathione peroxidase 7 ^@ http://purl.uniprot.org/annotation/PRO_0000013085|||http://purl.uniprot.org/annotation/PRO_5009970796 http://togogenome.org/gene/10090:Pbx4 ^@ http://purl.uniprot.org/uniprot/Q99NE9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Splice Variant ^@ Disordered|||Homeobox; TALE-type|||In isoform 2.|||PBC|||PBC-A|||PBC-B|||Polar residues|||Pre-B-cell leukemia transcription factor 4|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000049242|||http://purl.uniprot.org/annotation/VSP_008617|||http://purl.uniprot.org/annotation/VSP_008618 http://togogenome.org/gene/10090:Oog2 ^@ http://purl.uniprot.org/uniprot/Q7TPX8 ^@ 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|||Oogenesin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000440972 http://togogenome.org/gene/10090:Large1 ^@ http://purl.uniprot.org/uniprot/Q059X9|||http://purl.uniprot.org/uniprot/Q9Z1M7 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Glucuronyltransferase activity|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Xylosyl- and glucuronyltransferase LARGE1|||Xylosyltransferase activity ^@ http://purl.uniprot.org/annotation/PRO_0000206061 http://togogenome.org/gene/10090:Ttc21b ^@ http://purl.uniprot.org/uniprot/E9PVK4|||http://purl.uniprot.org/uniprot/Q0HA38 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ 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_0000291918 http://togogenome.org/gene/10090:Defb3 ^@ http://purl.uniprot.org/uniprot/Q9WTL0 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Signal Peptide ^@ Beta-defensin 3 ^@ http://purl.uniprot.org/annotation/PRO_0000006928|||http://purl.uniprot.org/annotation/PRO_0000006929 http://togogenome.org/gene/10090:Sel1l ^@ http://purl.uniprot.org/uniprot/Q5DTL8|||http://purl.uniprot.org/uniprot/Q6GTY4|||http://purl.uniprot.org/uniprot/Q9Z2G6 ^@ 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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes homodimerization.|||Abolishes homodimerization; when associated with 515-A-A-516.|||Abolishes homodimerization; when associated with A-519.|||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_0000022296|||http://purl.uniprot.org/annotation/PRO_5014310450|||http://purl.uniprot.org/annotation/VSP_004384 http://togogenome.org/gene/10090:Slc25a33 ^@ http://purl.uniprot.org/uniprot/Q3TZX3 ^@ 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 33 ^@ http://purl.uniprot.org/annotation/PRO_0000291786 http://togogenome.org/gene/10090:Glb1l3 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSK9|||http://purl.uniprot.org/uniprot/A2RSQ1 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Signal Peptide|||Splice Variant ^@ Beta-galactosidase|||Beta-galactosidase-1-like protein 3|||Glycoside hydrolase 35 catalytic|||In isoform 2.|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000283029|||http://purl.uniprot.org/annotation/PRO_5008408611|||http://purl.uniprot.org/annotation/VSP_024289 http://togogenome.org/gene/10090:Oxa1l ^@ http://purl.uniprot.org/uniprot/Q8BGA9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Disordered|||Helical|||Mitochondrial inner membrane protein OXA1L|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000020353 http://togogenome.org/gene/10090:Tnfrsf1b ^@ http://purl.uniprot.org/uniprot/P25119|||http://purl.uniprot.org/uniprot/Q545P4 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 1B ^@ http://purl.uniprot.org/annotation/PRO_0000034550|||http://purl.uniprot.org/annotation/PRO_5014309642 http://togogenome.org/gene/10090:Tmem17 ^@ http://purl.uniprot.org/uniprot/Q8K0U3 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 17 ^@ http://purl.uniprot.org/annotation/PRO_0000255261 http://togogenome.org/gene/10090:Speer4f1 ^@ http://purl.uniprot.org/uniprot/Q9D5Q6 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Dapk1 ^@ http://purl.uniprot.org/uniprot/Q3UKP8|||http://purl.uniprot.org/uniprot/Q80YE7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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|||In isoform 2.|||Phosphoserine|||Phosphoserine; by MAPK1|||Phosphoserine; by RPS6KA1 and RPS6KA3|||Phosphoserine; by autocatalysis|||Protein kinase|||Proton acceptor|||Roc ^@ http://purl.uniprot.org/annotation/PRO_0000085911|||http://purl.uniprot.org/annotation/VSP_050629 http://togogenome.org/gene/10090:Washc2 ^@ http://purl.uniprot.org/uniprot/Q6PGL7 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||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 2|||LFa 3|||LFa 4|||LFa 5|||LFa 6|||LFa 7|||LFa 8|||LFa 9|||Phosphoserine|||Phosphothreonine|||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 2 ^@ http://purl.uniprot.org/annotation/PRO_0000317433|||http://purl.uniprot.org/annotation/VSP_030949 http://togogenome.org/gene/10090:Pttg1 ^@ http://purl.uniprot.org/uniprot/Q9CQJ7 ^@ 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 ^@ D-box|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||SH3-binding|||Securin|||Strongly reduces transactivation and transforming capability.|||TEK-box 1|||TEK-box 2 ^@ http://purl.uniprot.org/annotation/PRO_0000206362|||http://purl.uniprot.org/annotation/VSP_006998|||http://purl.uniprot.org/annotation/VSP_006999 http://togogenome.org/gene/10090:Tnfrsf21 ^@ http://purl.uniprot.org/uniprot/Q9EPU5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||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|||Lipid Binding|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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_0000034603 http://togogenome.org/gene/10090:Mki67 ^@ http://purl.uniprot.org/uniprot/E9PVX6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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 2.|||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|||Polar residues|||Proliferation marker protein Ki-67 ^@ http://purl.uniprot.org/annotation/PRO_0000437535|||http://purl.uniprot.org/annotation/VSP_058551 http://togogenome.org/gene/10090:Gm773 ^@ http://purl.uniprot.org/uniprot/Q3TML4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Rspo1 ^@ http://purl.uniprot.org/uniprot/B1ASC1|||http://purl.uniprot.org/uniprot/Q9Z132 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||FU 1|||FU 2|||N-linked (GlcNAc...) asparagine|||Polar residues|||R-spondin Fu-CRD|||R-spondin-1|||TSP type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000234437|||http://purl.uniprot.org/annotation/PRO_5015087032 http://togogenome.org/gene/10090:Cyp2c70 ^@ http://purl.uniprot.org/uniprot/Q91W64 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Sequence Conflict|||Signal Peptide ^@ Cytochrome P450 2C70|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051726 http://togogenome.org/gene/10090:Pnpla3 ^@ http://purl.uniprot.org/uniprot/E9QNZ9|||http://purl.uniprot.org/uniprot/Q91WW7 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ 1-acylglycerol-3-phosphate O-acyltransferase Pnpla3|||Cytoplasmic|||DGA/G|||Disordered|||GXGXXG|||GXSXG|||Helical|||Helical; Signal-anchor for type II membrane protein|||Increases 1-acylglycerol-3-phosphate O-acyltransferase activity 2-fold; promotes hepatic lipid synthesis.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PNPLA|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000064459 http://togogenome.org/gene/10090:Kif24 ^@ http://purl.uniprot.org/uniprot/Q6NWW5 ^@ 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 ^@ Disordered|||In isoform 2.|||Interaction with MPHOSPH9|||Kinesin motor|||Kinesin-like protein KIF24|||Phosphoserine|||Phosphoserine; by NEK2|||Phosphothreonine; by NEK2|||Polar residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000278249|||http://purl.uniprot.org/annotation/VSP_023214 http://togogenome.org/gene/10090:Runx3 ^@ http://purl.uniprot.org/uniprot/Q3U1Q3 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Runt ^@ http://togogenome.org/gene/10090:Or5ak22 ^@ http://purl.uniprot.org/uniprot/Q8VGC6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp58 ^@ http://purl.uniprot.org/uniprot/P16372 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||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 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 58 ^@ http://purl.uniprot.org/annotation/PRO_0000047302 http://togogenome.org/gene/10090:Enah ^@ http://purl.uniprot.org/uniprot/A0A0A6YW06|||http://purl.uniprot.org/uniprot/E9QKQ9|||http://purl.uniprot.org/uniprot/E9QLZ9|||http://purl.uniprot.org/uniprot/Q03173 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ 1|||2|||3|||4|||5|||6|||7|||7 X 5 AA tandem repeats of [LM]-E-[QR]-[EQ]-[QR]|||Basic and acidic residues|||Disordered|||EVH2|||EVH2 block A|||EVH2 block B|||EVH2 block C|||In isoform 1.|||In isoform 2 and isoform 6.|||In isoform 2, isoform 3 and isoform 6.|||In isoform 4.|||In isoform 6.|||KLKR|||No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. Loss of cell mobility function; when associated with A-637.|||No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. No loss of cell mobility function. when associated with A-255.|||No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. No loss of cell mobility function. when associated with D-255.|||No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. No loss of cell mobility function; when associated with D-637.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein enabled homolog|||WH1 ^@ http://purl.uniprot.org/annotation/PRO_0000086972|||http://purl.uniprot.org/annotation/VSP_007255|||http://purl.uniprot.org/annotation/VSP_007257|||http://purl.uniprot.org/annotation/VSP_007258|||http://purl.uniprot.org/annotation/VSP_007259|||http://purl.uniprot.org/annotation/VSP_007260|||http://purl.uniprot.org/annotation/VSP_010565 http://togogenome.org/gene/10090:Lrfn2 ^@ http://purl.uniprot.org/uniprot/Q80TG9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||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 DLG4-binding.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014840 http://togogenome.org/gene/10090:Btbd35f10 ^@ http://purl.uniprot.org/uniprot/A2CG92 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Pacrg ^@ http://purl.uniprot.org/uniprot/Q9DAK2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Parkin coregulated gene protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000058170 http://togogenome.org/gene/10090:Oga ^@ http://purl.uniprot.org/uniprot/Q9EQQ9 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ 2-fold decrease in substrate affinity and 96% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. 40% recovery of activity in the presence of sodium azide.|||2-fold increase in substrate affinity and 77% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. No recovery of activity in the presence of sodium azide.|||3-fold increase in substrate affinity and 90% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. 70% recovery of activity in the presence of sodium azide.|||Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||GH84|||In isoform 2.|||In isoform 3.|||No change in substrate affinity but 60% reduction in O-GlcNAcase activity.|||No effect on O-GlcNAcase activity.|||Phosphoserine|||Protein O-GlcNAcase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000252119|||http://purl.uniprot.org/annotation/VSP_020870|||http://purl.uniprot.org/annotation/VSP_020871|||http://purl.uniprot.org/annotation/VSP_020872 http://togogenome.org/gene/10090:Agpat5 ^@ http://purl.uniprot.org/uniprot/Q9D1E8 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Motif|||Sequence Conflict|||Transmembrane ^@ 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon|||HXXXXD motif|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000208201 http://togogenome.org/gene/10090:Isy1 ^@ http://purl.uniprot.org/uniprot/Q69ZQ2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Turn ^@ Acidic residues|||Disordered|||N6-acetyllysine|||Phosphoserine|||Pre-mRNA-splicing factor ISY1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000235814 http://togogenome.org/gene/10090:Pax8 ^@ http://purl.uniprot.org/uniprot/Q00288 ^@ 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 ^@ Disordered|||PAI subdomain|||Paired|||Paired box protein Pax-8|||Phosphoserine|||Polar residues|||RED subdomain ^@ http://purl.uniprot.org/annotation/PRO_0000050198 http://togogenome.org/gene/10090:Casc3 ^@ http://purl.uniprot.org/uniprot/Q8K3W3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Accumulation in the nucleus.|||Acidic residues|||Basic and acidic residues|||Disordered|||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_0000089325 http://togogenome.org/gene/10090:Zfp74 ^@ http://purl.uniprot.org/uniprot/Q80W31 ^@ 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 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 569 ^@ http://purl.uniprot.org/annotation/PRO_0000047660 http://togogenome.org/gene/10090:Anapc7 ^@ http://purl.uniprot.org/uniprot/Q9WVM3 ^@ 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 ^@ Acidic residues|||Anaphase-promoting complex subunit 7|||Disordered|||N6-acetyllysine|||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_0000106262 http://togogenome.org/gene/10090:Ager ^@ http://purl.uniprot.org/uniprot/Q62151 ^@ 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 ^@ Advanced glycosylation end product-specific receptor|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 13.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014924|||http://purl.uniprot.org/annotation/VSP_058075|||http://purl.uniprot.org/annotation/VSP_058076|||http://purl.uniprot.org/annotation/VSP_058077|||http://purl.uniprot.org/annotation/VSP_058078|||http://purl.uniprot.org/annotation/VSP_058079|||http://purl.uniprot.org/annotation/VSP_058080|||http://purl.uniprot.org/annotation/VSP_058081|||http://purl.uniprot.org/annotation/VSP_058082|||http://purl.uniprot.org/annotation/VSP_058083|||http://purl.uniprot.org/annotation/VSP_058084|||http://purl.uniprot.org/annotation/VSP_058085|||http://purl.uniprot.org/annotation/VSP_058086|||http://purl.uniprot.org/annotation/VSP_058087|||http://purl.uniprot.org/annotation/VSP_058088|||http://purl.uniprot.org/annotation/VSP_058089|||http://purl.uniprot.org/annotation/VSP_058090|||http://purl.uniprot.org/annotation/VSP_058091|||http://purl.uniprot.org/annotation/VSP_058092|||http://purl.uniprot.org/annotation/VSP_058093|||http://purl.uniprot.org/annotation/VSP_058094 http://togogenome.org/gene/10090:Phrf1 ^@ http://purl.uniprot.org/uniprot/A6H619 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||PHD and RING finger domain-containing protein 1|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000354662|||http://purl.uniprot.org/annotation/VSP_052978|||http://purl.uniprot.org/annotation/VSP_052979 http://togogenome.org/gene/10090:Lrrc39 ^@ http://purl.uniprot.org/uniprot/Q8BGI7 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ 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_0000232581 http://togogenome.org/gene/10090:Tm4sf20 ^@ http://purl.uniprot.org/uniprot/Q9CQY8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cleavage|||Cytoplasmic|||Helical|||Lumenal|||Transmembrane 4 L6 family member 20 ^@ http://purl.uniprot.org/annotation/PRO_0000251229 http://togogenome.org/gene/10090:Or4a2 ^@ http://purl.uniprot.org/uniprot/Q8VGM8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Uprt ^@ http://purl.uniprot.org/uniprot/B1AVZ0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Polar residues|||Uracil phosphoribosyltransferase homolog ^@ http://purl.uniprot.org/annotation/PRO_0000413215 http://togogenome.org/gene/10090:1700006A11Rik ^@ http://purl.uniprot.org/uniprot/B9EHI3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Rho-GAP ^@ http://togogenome.org/gene/10090:Sult1e1 ^@ http://purl.uniprot.org/uniprot/Q9D566 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Desi2 ^@ http://purl.uniprot.org/uniprot/Q8BIB9|||http://purl.uniprot.org/uniprot/Q9D291 ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent ^@ Deubiquitinase DESI2|||PPPDE ^@ http://purl.uniprot.org/annotation/PRO_0000221631 http://togogenome.org/gene/10090:Lrrtm4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1T4|||http://purl.uniprot.org/uniprot/E9Q8Y9|||http://purl.uniprot.org/uniprot/Q80XG9|||http://purl.uniprot.org/uniprot/Q8BYQ8 ^@ 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|||Repeat|||Sequence Conflict|||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_0000018359|||http://purl.uniprot.org/annotation/PRO_5003243132|||http://purl.uniprot.org/annotation/PRO_5006452028|||http://purl.uniprot.org/annotation/VSP_014193|||http://purl.uniprot.org/annotation/VSP_014194 http://togogenome.org/gene/10090:B3gnt5 ^@ http://purl.uniprot.org/uniprot/Q8BGY6 ^@ 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|||Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000289210 http://togogenome.org/gene/10090:Gm15114 ^@ http://purl.uniprot.org/uniprot/B1B0X6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gng12 ^@ http://purl.uniprot.org/uniprot/Q9DAS9 ^@ 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-12|||N-acetylserine|||Phosphoserine|||Phosphotyrosine|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000012669|||http://purl.uniprot.org/annotation/PRO_0000012670 http://togogenome.org/gene/10090:Septin10 ^@ http://purl.uniprot.org/uniprot/A0A0R4J233|||http://purl.uniprot.org/uniprot/A0A1W2P6J7|||http://purl.uniprot.org/uniprot/Q8C650 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ G1 motif|||G3 motif|||G4 motif|||In isoform 2.|||Phosphoserine|||Septin-10|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173539|||http://purl.uniprot.org/annotation/VSP_014093 http://togogenome.org/gene/10090:Ankrd33b ^@ http://purl.uniprot.org/uniprot/Q3U0L2 ^@ 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 ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 33B|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000328770|||http://purl.uniprot.org/annotation/VSP_032778|||http://purl.uniprot.org/annotation/VSP_032779|||http://purl.uniprot.org/annotation/VSP_032780|||http://purl.uniprot.org/annotation/VSP_032781|||http://purl.uniprot.org/annotation/VSP_032782 http://togogenome.org/gene/10090:Itga9 ^@ http://purl.uniprot.org/uniprot/B8JK39|||http://purl.uniprot.org/uniprot/E9QAP0|||http://purl.uniprot.org/uniprot/Q3UT74 ^@ 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|||Site|||Topological Domain|||Transmembrane ^@ Cleavage|||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-2|||Integrin alpha-9|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000431914 http://togogenome.org/gene/10090:H2bc21 ^@ http://purl.uniprot.org/uniprot/Q64524 ^@ 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 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-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_0000244836 http://togogenome.org/gene/10090:Mterf1a ^@ http://purl.uniprot.org/uniprot/Q8CHZ9 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Chain|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Interaction with DNA|||Mitochondrion|||Transcription termination factor 1a, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000021780 http://togogenome.org/gene/10090:Gria1 ^@ http://purl.uniprot.org/uniprot/F6YNQ1|||http://purl.uniprot.org/uniprot/P23818|||http://purl.uniprot.org/uniprot/Q7TNB5 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Almost abolishes interaction with SHANK3.|||Cytoplasmic|||Disordered|||Extracellular|||Glutamate receptor|||Glutamate receptor 1|||Helical|||Helical; Name=M4|||Helical; Pore-forming|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000011530|||http://purl.uniprot.org/annotation/PRO_5015098855 http://togogenome.org/gene/10090:Shc2 ^@ http://purl.uniprot.org/uniprot/Q8BMC3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ CH1|||PID|||Phosphotyrosine|||SH2|||SHC-transforming protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000097733 http://togogenome.org/gene/10090:Vmn1r226 ^@ http://purl.uniprot.org/uniprot/Q8R2A8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sorbs2 ^@ http://purl.uniprot.org/uniprot/A0A0S3CWK3|||http://purl.uniprot.org/uniprot/B2RXQ9|||http://purl.uniprot.org/uniprot/B7ZWM6|||http://purl.uniprot.org/uniprot/B9EKP8|||http://purl.uniprot.org/uniprot/D3Z080|||http://purl.uniprot.org/uniprot/Q3UTJ2 ^@ 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, isoform 3, isoform 5 and isoform 6.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||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_0000344478|||http://purl.uniprot.org/annotation/VSP_034800|||http://purl.uniprot.org/annotation/VSP_034801|||http://purl.uniprot.org/annotation/VSP_034802|||http://purl.uniprot.org/annotation/VSP_034803|||http://purl.uniprot.org/annotation/VSP_034804|||http://purl.uniprot.org/annotation/VSP_034805|||http://purl.uniprot.org/annotation/VSP_034806|||http://purl.uniprot.org/annotation/VSP_034807|||http://purl.uniprot.org/annotation/VSP_034808|||http://purl.uniprot.org/annotation/VSP_034809|||http://purl.uniprot.org/annotation/VSP_034810|||http://purl.uniprot.org/annotation/VSP_034811 http://togogenome.org/gene/10090:Map3k14 ^@ http://purl.uniprot.org/uniprot/Q544K4|||http://purl.uniprot.org/uniprot/Q9WUL6 ^@ 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 residues|||Disordered|||In ALY; no binding to IKKA.|||Interaction with ZFP91|||Mitogen-activated protein kinase kinase kinase 14|||Phosphothreonine|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086267 http://togogenome.org/gene/10090:Prmt6 ^@ http://purl.uniprot.org/uniprot/Q6NZB1 ^@ Active Site|||Binding 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|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Asymmetric dimethylarginine; by autocatalysis|||Basic and acidic residues|||Disordered|||Protein arginine N-methyltransferase 6|||SAM-dependent MTase PRMT-type ^@ http://purl.uniprot.org/annotation/PRO_0000212333 http://togogenome.org/gene/10090:Ube2n ^@ http://purl.uniprot.org/uniprot/A2RTT4|||http://purl.uniprot.org/uniprot/P61089 ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Glycyl thioester intermediate|||N6-acetyllysine|||UBC core|||Ubiquitin-conjugating enzyme E2 N ^@ http://purl.uniprot.org/annotation/PRO_0000082504 http://togogenome.org/gene/10090:Dennd4c ^@ http://purl.uniprot.org/uniprot/A6H8H2 ^@ 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|||DENN domain-containing protein 4C|||Disordered|||In isoform 2.|||MABP|||PPR|||Phosphoserine|||Phosphothreonine|||Polar residues|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000420446|||http://purl.uniprot.org/annotation/VSP_044491 http://togogenome.org/gene/10090:Fam117b ^@ http://purl.uniprot.org/uniprot/Q3U3E2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Pro residues|||Protein FAM117B ^@ http://purl.uniprot.org/annotation/PRO_0000299534 http://togogenome.org/gene/10090:Polr3e ^@ http://purl.uniprot.org/uniprot/Q3TWE8|||http://purl.uniprot.org/uniprot/Q9CZT4 ^@ 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 ^@ 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.|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000073971|||http://purl.uniprot.org/annotation/VSP_007066 http://togogenome.org/gene/10090:Mbl2 ^@ http://purl.uniprot.org/uniprot/P41317|||http://purl.uniprot.org/uniprot/Q3UEK1 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 4-hydroxyproline|||C-type lectin|||C-type lectin domain-containing protein|||Collagen-like|||Disordered|||Interchain|||Mannose-binding protein C|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017405|||http://purl.uniprot.org/annotation/PRO_5014309205 http://togogenome.org/gene/10090:Or5h22 ^@ http://purl.uniprot.org/uniprot/K7N5T5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ppme1 ^@ http://purl.uniprot.org/uniprot/Q8BVQ5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Omega-N-methylarginine; alternate|||Phosphoserine|||Protein phosphatase methylesterase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000090391 http://togogenome.org/gene/10090:Fam210a ^@ http://purl.uniprot.org/uniprot/Q8BGY7 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ DUF1279|||Disordered|||Helical|||Protein FAM210A ^@ http://purl.uniprot.org/annotation/PRO_0000274425 http://togogenome.org/gene/10090:Btla ^@ http://purl.uniprot.org/uniprot/A0A0R4J1A0|||http://purl.uniprot.org/uniprot/E9QNY6|||http://purl.uniprot.org/uniprot/Q32MV8|||http://purl.uniprot.org/uniprot/Q7TSA3 ^@ 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|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ B- and T-lymphocyte attenuator|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In strain: 129/SvEv.|||In strain: 129/SvEv; requires 2 nucleotide substitutions.|||In strain: C57BL/6J.|||Loss of interaction with TNFRSF14.|||N-linked (GlcNAc...) asparagine|||No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-245 and/or F-274.|||No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-245 and/or F-299.|||No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-274 and/or F-299. ^@ http://purl.uniprot.org/annotation/PRO_0000014524|||http://purl.uniprot.org/annotation/PRO_5003243349|||http://purl.uniprot.org/annotation/PRO_5006451996|||http://purl.uniprot.org/annotation/PRO_5014309013|||http://purl.uniprot.org/annotation/VSP_014836|||http://purl.uniprot.org/annotation/VSP_014837 http://togogenome.org/gene/10090:Rbmx ^@ http://purl.uniprot.org/uniprot/Q9WV02 ^@ 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 and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||N-acetylvaline; in RNA-binding motif protein, X chromosome, N-terminally processed|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||RNA-binding motif protein, X chromosome|||RNA-binding motif protein, X chromosome, N-terminally processed|||RRM|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000414747|||http://purl.uniprot.org/annotation/PRO_0000414748|||http://purl.uniprot.org/annotation/VSP_042129 http://togogenome.org/gene/10090:Or7a41 ^@ http://purl.uniprot.org/uniprot/Q8VGU7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nckap5 ^@ http://purl.uniprot.org/uniprot/E9Q3G9|||http://purl.uniprot.org/uniprot/E9QAE1|||http://purl.uniprot.org/uniprot/Q6NZK2|||http://purl.uniprot.org/uniprot/Q8C6S8 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Nck-associated protein 5 C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Nudt11 ^@ http://purl.uniprot.org/uniprot/P0C027|||http://purl.uniprot.org/uniprot/P0C028 ^@ 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-alpha|||Diphosphoinositol polyphosphate phosphohydrolase 3-beta|||Disordered|||Nudix box|||Nudix hydrolase|||Polar residues|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000057063|||http://purl.uniprot.org/annotation/PRO_0000057066 http://togogenome.org/gene/10090:6030468B19Rik ^@ http://purl.uniprot.org/uniprot/Q9CX63 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Protein IL-40 ^@ http://purl.uniprot.org/annotation/PRO_0000272655 http://togogenome.org/gene/10090:Vmn1r48 ^@ http://purl.uniprot.org/uniprot/Q9EQ52 ^@ 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|||Vomeronasal type-1 receptor 48 ^@ http://purl.uniprot.org/annotation/PRO_0000239958 http://togogenome.org/gene/10090:Alg8 ^@ http://purl.uniprot.org/uniprot/Q6P8H8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000174163 http://togogenome.org/gene/10090:Vmn1r234 ^@ http://purl.uniprot.org/uniprot/Q8R298 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Man2a1 ^@ http://purl.uniprot.org/uniprot/P27046|||http://purl.uniprot.org/uniprot/Q8C4L1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||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_0000206903 http://togogenome.org/gene/10090:Tnfaip8 ^@ http://purl.uniprot.org/uniprot/D3YWJ5|||http://purl.uniprot.org/uniprot/D3Z325|||http://purl.uniprot.org/uniprot/Q921Z5 ^@ Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn ^@ Chain|||Coiled-Coil|||Helix|||Sequence Conflict|||Splice Variant|||Turn ^@ In isoform 2.|||Tumor necrosis factor alpha-induced protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000285719|||http://purl.uniprot.org/annotation/VSP_024900|||http://purl.uniprot.org/annotation/VSP_024901 http://togogenome.org/gene/10090:Car10 ^@ http://purl.uniprot.org/uniprot/P61215|||http://purl.uniprot.org/uniprot/Q3V1V7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Alpha-carbonic anhydrase|||Alpha-carbonic anhydrase domain-containing protein|||Carbonic anhydrase-related protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000077438|||http://purl.uniprot.org/annotation/PRO_5009970847 http://togogenome.org/gene/10090:Siglec1 ^@ http://purl.uniprot.org/uniprot/G3X8X6|||http://purl.uniprot.org/uniprot/Q62230 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 10-fold loss in affinity to sialic acid.|||Cell attachment site|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||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.|||Loss of sialic acid binding.|||N-linked (GlcNAc...) asparagine|||Sialoadhesin ^@ http://purl.uniprot.org/annotation/PRO_0000014969|||http://purl.uniprot.org/annotation/PRO_5015091844|||http://purl.uniprot.org/annotation/VSP_002573|||http://purl.uniprot.org/annotation/VSP_002574|||http://purl.uniprot.org/annotation/VSP_002575|||http://purl.uniprot.org/annotation/VSP_002576 http://togogenome.org/gene/10090:Chek1 ^@ http://purl.uniprot.org/uniprot/O35280 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Autoinhibitory region|||Disordered|||Enhances cell cycle arrest.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Interaction with CLSPN|||Phosphoserine|||Phosphoserine; by ATM and ATR|||Phosphoserine; by ATR|||Phosphoserine; by PKB/AKT1|||Polar residues|||Promotes mono and/or diubiquitination and nuclear exclusion. Reduces phosphorylation at S-345.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Chk1 ^@ http://purl.uniprot.org/annotation/PRO_0000085849|||http://purl.uniprot.org/annotation/VSP_015791|||http://purl.uniprot.org/annotation/VSP_015792 http://togogenome.org/gene/10090:Higd1a ^@ http://purl.uniprot.org/uniprot/Q1XG81|||http://purl.uniprot.org/uniprot/Q9JLR9 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Transmembrane ^@ HIG1|||HIG1 domain family member 1A, mitochondrial|||Helical|||N-acetylserine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000215771 http://togogenome.org/gene/10090:Fam227b ^@ http://purl.uniprot.org/uniprot/Q9D518 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Protein FAM227B ^@ http://purl.uniprot.org/annotation/PRO_0000244100 http://togogenome.org/gene/10090:2210408I21Rik ^@ http://purl.uniprot.org/uniprot/Q3TNF8|||http://purl.uniprot.org/uniprot/Q3UPC7 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Splice Variant ^@ Chain|||Non-terminal Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Uncharacterized protein KIAA0825 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000340690|||http://purl.uniprot.org/annotation/VSP_039419|||http://purl.uniprot.org/annotation/VSP_039420 http://togogenome.org/gene/10090:Skint4 ^@ http://purl.uniprot.org/uniprot/A7TZF3|||http://purl.uniprot.org/uniprot/E9QLU2 ^@ 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|||Ig-like C1-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Selection and upkeep of intraepithelial T-cells protein 4 ^@ http://purl.uniprot.org/annotation/PRO_5000270108|||http://purl.uniprot.org/annotation/VSP_034882 http://togogenome.org/gene/10090:Or7e166 ^@ http://purl.uniprot.org/uniprot/Q7TRF7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lrrd1 ^@ http://purl.uniprot.org/uniprot/Q8C0R9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ Death|||Disordered|||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|||Leucine-rich repeat and death domain-containing protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000325806 http://togogenome.org/gene/10090:Kif22 ^@ http://purl.uniprot.org/uniprot/Q3V300 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Kinesin motor|||Kinesin-like protein KIF22|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000262921 http://togogenome.org/gene/10090:Ifi27l2b ^@ http://purl.uniprot.org/uniprot/Q8VC49 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transit Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transit Peptide|||Transmembrane ^@ Disordered|||Helical|||Interferon alpha-inducible protein 27-like protein 2B|||Mitochondrion|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000416108 http://togogenome.org/gene/10090:Adora2b ^@ http://purl.uniprot.org/uniprot/Q60614 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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_0000069004 http://togogenome.org/gene/10090:AU022252 ^@ http://purl.uniprot.org/uniprot/Q5EBG8 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Uncharacterized protein C1orf50 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000251190 http://togogenome.org/gene/10090:Ano3 ^@ http://purl.uniprot.org/uniprot/A2AHL1 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Anoctamin-3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000353188|||http://purl.uniprot.org/annotation/VSP_052958|||http://purl.uniprot.org/annotation/VSP_052959 http://togogenome.org/gene/10090:Ssxb8 ^@ http://purl.uniprot.org/uniprot/B1AY40 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB|||KRAB-related ^@ http://togogenome.org/gene/10090:Slc25a48 ^@ http://purl.uniprot.org/uniprot/Q8BW66 ^@ 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 48 ^@ http://purl.uniprot.org/annotation/PRO_0000325769 http://togogenome.org/gene/10090:Lce3c ^@ http://purl.uniprot.org/uniprot/Q91V05 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Plekha6 ^@ http://purl.uniprot.org/uniprot/E9PX43|||http://purl.uniprot.org/uniprot/Q69ZU4|||http://purl.uniprot.org/uniprot/Q7TQG1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ 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_0000053885 http://togogenome.org/gene/10090:Pfkfb4 ^@ http://purl.uniprot.org/uniprot/C9VZF2|||http://purl.uniprot.org/uniprot/Q6DTY7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Site|||Splice Variant ^@ 6-phosphofructo-2-kinase|||6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4|||Fructose-2,6-bisphosphatase|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine; by PKC|||Phosphothreonine; by PKC|||Proton donor/acceptor|||Tele-phosphohistidine intermediate|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000268187|||http://purl.uniprot.org/annotation/VSP_021959|||http://purl.uniprot.org/annotation/VSP_021960|||http://purl.uniprot.org/annotation/VSP_021961|||http://purl.uniprot.org/annotation/VSP_021962|||http://purl.uniprot.org/annotation/VSP_021963|||http://purl.uniprot.org/annotation/VSP_021964 http://togogenome.org/gene/10090:Or8g17 ^@ http://purl.uniprot.org/uniprot/Q60884 ^@ 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|||Olfactory receptor 8G17 ^@ http://purl.uniprot.org/annotation/PRO_0000150823 http://togogenome.org/gene/10090:Gzmc ^@ http://purl.uniprot.org/uniprot/P08882|||http://purl.uniprot.org/uniprot/Q0VB76 ^@ 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 ^@ Charge relay system|||Granzyme C|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027403|||http://purl.uniprot.org/annotation/PRO_0000027404|||http://purl.uniprot.org/annotation/PRO_5014306860 http://togogenome.org/gene/10090:Enam ^@ http://purl.uniprot.org/uniprot/O55196|||http://purl.uniprot.org/uniprot/Q548P8 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Enamelin|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000021175 http://togogenome.org/gene/10090:Rnf13 ^@ http://purl.uniprot.org/uniprot/O54965|||http://purl.uniprot.org/uniprot/Q3UTG4|||http://purl.uniprot.org/uniprot/Q8C4F9|||http://purl.uniprot.org/uniprot/Q8CB78 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Acidic residues|||Cytoplasmic|||Disordered|||E3 ubiquitin-protein ligase RNF13|||Helical|||In isoform 2.|||Loss of E3 ligase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||PA|||Polar residues|||RING-type|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000056055|||http://purl.uniprot.org/annotation/VSP_005749|||http://purl.uniprot.org/annotation/VSP_005750 http://togogenome.org/gene/10090:Plce1 ^@ http://purl.uniprot.org/uniprot/Q8K4S1 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1|||Basic and acidic residues|||C2|||Disordered|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Polar residues|||Ras-GEF|||Ras-associating 1|||Ras-associating 2|||Required for activation by RHOA, RHOB, GNA12, GNA13 and G-beta gamma ^@ http://purl.uniprot.org/annotation/PRO_0000256239 http://togogenome.org/gene/10090:Vsir ^@ http://purl.uniprot.org/uniprot/A0A171EBK7|||http://purl.uniprot.org/uniprot/Q9D659 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||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_0000014766|||http://purl.uniprot.org/annotation/PRO_5015052207 http://togogenome.org/gene/10090:Atp6v1d ^@ http://purl.uniprot.org/uniprot/P57746 ^@ Chain|||Molecule Processing ^@ Chain ^@ V-type proton ATPase subunit D ^@ http://purl.uniprot.org/annotation/PRO_0000144232 http://togogenome.org/gene/10090:Clrn1 ^@ http://purl.uniprot.org/uniprot/B7ZNE8|||http://purl.uniprot.org/uniprot/Q8BYX9|||http://purl.uniprot.org/uniprot/Q8K444|||http://purl.uniprot.org/uniprot/Q8K445 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Clarin-1|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000274695|||http://purl.uniprot.org/annotation/PRO_5014300216|||http://purl.uniprot.org/annotation/PRO_5015099258|||http://purl.uniprot.org/annotation/VSP_022870 http://togogenome.org/gene/10090:Nr2e3 ^@ http://purl.uniprot.org/uniprot/Q543C7|||http://purl.uniprot.org/uniprot/Q9QXZ7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Mutagenesis Site|||Region|||Zinc Finger ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Greatly reduced levels of PIAS3-mediated sumoylation. Completely abolishes sumoylation; when associated with R-315 and R-322.|||Little change in sumoylation. Completely abolishes sumoylation; when associated with R-178 and R-315.|||Little change in sumoylation. Completely abolishes sumoylation; when associated with R-178 and R-322.|||NR C4-type|||NR LBD|||Nuclear receptor|||Photoreceptor-specific nuclear receptor|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053600 http://togogenome.org/gene/10090:Rapgef1 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPI9|||http://purl.uniprot.org/uniprot/Q3UGX8|||http://purl.uniprot.org/uniprot/Q3UHC1|||http://purl.uniprot.org/uniprot/Q8C5V7|||http://purl.uniprot.org/uniprot/Q91ZZ2 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||N-terminal Ras-GEF|||Polar residues|||Ras-GEF ^@ http://togogenome.org/gene/10090:Cnr1 ^@ http://purl.uniprot.org/uniprot/A0A385KNU8|||http://purl.uniprot.org/uniprot/P47746 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cannabinoid receptor 1|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Loss of mitochondrial localization. Loss of cannabinoid-induced reduction of respiration, mitochondrial mobility, synaptic transmission and memory formation. No effect on MAPK/ERK signaling, nor on G protein activation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Required for mitochondrial localization|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069316 http://togogenome.org/gene/10090:Myt1l ^@ http://purl.uniprot.org/uniprot/P97500|||http://purl.uniprot.org/uniprot/Q0VGN2 ^@ 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 2 and isoform 4.|||In isoform 3 and isoform 4.|||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_0000096674|||http://purl.uniprot.org/annotation/VSP_015726|||http://purl.uniprot.org/annotation/VSP_015727|||http://purl.uniprot.org/annotation/VSP_015728|||http://purl.uniprot.org/annotation/VSP_015729|||http://purl.uniprot.org/annotation/VSP_015730|||http://purl.uniprot.org/annotation/VSP_015731 http://togogenome.org/gene/10090:Ttc36 ^@ http://purl.uniprot.org/uniprot/Q8VBW8 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 36 ^@ http://purl.uniprot.org/annotation/PRO_0000332180 http://togogenome.org/gene/10090:Sohlh2 ^@ http://purl.uniprot.org/uniprot/Q9D489 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 2|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000315701 http://togogenome.org/gene/10090:Cep95 ^@ http://purl.uniprot.org/uniprot/Q14B65|||http://purl.uniprot.org/uniprot/Q8BVV7|||http://purl.uniprot.org/uniprot/Q8BWE9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Centrosomal protein of 95 kDa|||DUF5745|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000234506 http://togogenome.org/gene/10090:Ube4a ^@ http://purl.uniprot.org/uniprot/E9Q735|||http://purl.uniprot.org/uniprot/G3X9Y5|||http://purl.uniprot.org/uniprot/Q6A0C5 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ Disordered|||N6-acetyllysine|||U-box|||Ubiquitin conjugation factor E4 A ^@ http://purl.uniprot.org/annotation/PRO_0000430791 http://togogenome.org/gene/10090:Apoh ^@ http://purl.uniprot.org/uniprot/Q01339|||http://purl.uniprot.org/uniprot/Q9CY42 ^@ 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 ^@ Beta-2-glycoprotein 1|||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_0000002060|||http://purl.uniprot.org/annotation/PRO_5004327947 http://togogenome.org/gene/10090:Pced1a ^@ http://purl.uniprot.org/uniprot/Q6P1Z5 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ PC-esterase domain-containing protein 1A ^@ http://purl.uniprot.org/annotation/PRO_0000079447 http://togogenome.org/gene/10090:Cwf19l2 ^@ http://purl.uniprot.org/uniprot/Q8BG79 ^@ 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|||CWF19-like protein 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315649|||http://purl.uniprot.org/annotation/VSP_030594|||http://purl.uniprot.org/annotation/VSP_030595 http://togogenome.org/gene/10090:Tacr1 ^@ http://purl.uniprot.org/uniprot/P30548 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||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|||Substance-P receptor ^@ http://purl.uniprot.org/annotation/PRO_0000069887 http://togogenome.org/gene/10090:Or10p22 ^@ http://purl.uniprot.org/uniprot/Q14A42|||http://purl.uniprot.org/uniprot/Q60885 ^@ 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 10P22 ^@ http://purl.uniprot.org/annotation/PRO_0000150808 http://togogenome.org/gene/10090:Capza3 ^@ http://purl.uniprot.org/uniprot/P70190 ^@ 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_0000208632 http://togogenome.org/gene/10090:Rap2a ^@ http://purl.uniprot.org/uniprot/Q80ZJ1 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Splice Variant ^@ Cysteine methyl ester|||Effector region|||In isoform 2.|||Loss of affinity for GTP and loss of interaction with RUNDC3A.|||Loss of association with membranes.|||Loss of association with the recycling endosome membranes and loss of TNIK activation; when associated with C-176.|||Loss of association with the recycling endosome membranes and loss of TNIK activation; when associated with C-177.|||Loss of interaction with RUNDC3A.|||Ras-related protein Rap-2a|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000082688|||http://purl.uniprot.org/annotation/PRO_0000281337|||http://purl.uniprot.org/annotation/VSP_013381 http://togogenome.org/gene/10090:Yif1b ^@ http://purl.uniprot.org/uniprot/Q9CX30 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Protein YIF1B ^@ http://purl.uniprot.org/annotation/PRO_0000307259|||http://purl.uniprot.org/annotation/VSP_028656 http://togogenome.org/gene/10090:Foxf1 ^@ http://purl.uniprot.org/uniprot/Q61080 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Region|||Sequence Conflict ^@ Disordered|||Fork-head|||Forkhead box protein F1 ^@ http://purl.uniprot.org/annotation/PRO_0000091833 http://togogenome.org/gene/10090:Klf15 ^@ http://purl.uniprot.org/uniprot/Q9EPW2 ^@ Chain|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Motif|||Region|||Zinc Finger ^@ 9aaTAD|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 15 ^@ http://purl.uniprot.org/annotation/PRO_0000047188 http://togogenome.org/gene/10090:Arpp19 ^@ http://purl.uniprot.org/uniprot/E9Q827|||http://purl.uniprot.org/uniprot/P56212 ^@ 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|||Phosphoserine; by PKA|||Removed|||cAMP-regulated phosphoprotein 19 ^@ http://purl.uniprot.org/annotation/PRO_0000146762|||http://purl.uniprot.org/annotation/VSP_018556 http://togogenome.org/gene/10090:Amz2 ^@ http://purl.uniprot.org/uniprot/Q400C8 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Splice Variant ^@ Archaemetzincin-2|||In isoform 2.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000159619|||http://purl.uniprot.org/annotation/VSP_016984|||http://purl.uniprot.org/annotation/VSP_016985 http://togogenome.org/gene/10090:Spryd7 ^@ http://purl.uniprot.org/uniprot/Q3TFQ1|||http://purl.uniprot.org/uniprot/Q3UBW1 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ B30.2/SPRY|||Helical|||N-acetylalanine|||Removed|||SPRY domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000243926 http://togogenome.org/gene/10090:Tex52 ^@ http://purl.uniprot.org/uniprot/Q3TTI8 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Testis-expressed protein 52 ^@ http://purl.uniprot.org/annotation/PRO_0000346160|||http://purl.uniprot.org/annotation/VSP_034982|||http://purl.uniprot.org/annotation/VSP_034983 http://togogenome.org/gene/10090:Ppp4r1 ^@ http://purl.uniprot.org/uniprot/E9PX53|||http://purl.uniprot.org/uniprot/E9QPR5|||http://purl.uniprot.org/uniprot/Q3TLM9|||http://purl.uniprot.org/uniprot/Q8K2V1 ^@ 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|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In isoform 2.|||Phosphoserine|||Polar residues|||Serine/threonine-protein phosphatase 4 regulatory subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000071528|||http://purl.uniprot.org/annotation/VSP_009470 http://togogenome.org/gene/10090:Psmc3 ^@ http://purl.uniprot.org/uniprot/O88685|||http://purl.uniprot.org/uniprot/Q3TKG4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict ^@ 26S proteasome regulatory subunit 6A|||AAA+ ATPase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000084699 http://togogenome.org/gene/10090:Samd12 ^@ http://purl.uniprot.org/uniprot/Q0VE29 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||SAM|||Sterile alpha motif domain-containing protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000279503 http://togogenome.org/gene/10090:Or6c3b ^@ http://purl.uniprot.org/uniprot/Q8VFI3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tlx3 ^@ http://purl.uniprot.org/uniprot/O55144 ^@ 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_0000049339 http://togogenome.org/gene/10090:Etaa1 ^@ http://purl.uniprot.org/uniprot/Q5SVT3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ ATR-activation domain (AAD)|||Basic and acidic residues|||Disordered|||Ewing's tumor-associated antigen 1 homolog|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||RBM1 motif|||RBM2 motif ^@ http://purl.uniprot.org/annotation/PRO_0000280100|||http://purl.uniprot.org/annotation/VSP_023537|||http://purl.uniprot.org/annotation/VSP_023538 http://togogenome.org/gene/10090:Glis2 ^@ http://purl.uniprot.org/uniprot/Q8VDL9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Abolishes interaction with CTNNB1. No effect on nuclear localization.|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Cleavage|||Disordered|||Impairs C-terminus cleavage.|||Impairs DNA-binding.|||Interaction with CTNND1|||No effect on C-terminus cleavage.|||Polar residues|||Transcription activation|||Transcription repression|||Zinc finger protein GLIS2 ^@ http://purl.uniprot.org/annotation/PRO_0000286984 http://togogenome.org/gene/10090:Tjp1 ^@ http://purl.uniprot.org/uniprot/B9EHJ3|||http://purl.uniprot.org/uniprot/P39447 ^@ 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 ^@ Acidic residues|||Actin-binding region (ABR)|||Basic and acidic residues|||Disordered|||Guanylate kinase-like|||Occludin (OCLN)-binding region|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH3|||Tight junction protein ZO-1|||ZU5 ^@ http://purl.uniprot.org/annotation/PRO_0000094541 http://togogenome.org/gene/10090:Xcr1 ^@ http://purl.uniprot.org/uniprot/Q544D8|||http://purl.uniprot.org/uniprot/S4R1K3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dop1b ^@ http://purl.uniprot.org/uniprot/Q3UHQ6|||http://purl.uniprot.org/uniprot/Q6PGE1|||http://purl.uniprot.org/uniprot/Q9DCG4 ^@ 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|||Dopey N-terminal|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein dopey-2 ^@ http://purl.uniprot.org/annotation/PRO_0000297949|||http://purl.uniprot.org/annotation/VSP_027430 http://togogenome.org/gene/10090:Paqr3 ^@ http://purl.uniprot.org/uniprot/Q0VAZ2|||http://purl.uniprot.org/uniprot/Q6TCG8 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Golgi targeting|||Helical|||Lumenal|||Progestin and adipoQ receptor family member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000218847 http://togogenome.org/gene/10090:Ghr ^@ http://purl.uniprot.org/uniprot/P16882|||http://purl.uniprot.org/uniprot/Q3UNY8|||http://purl.uniprot.org/uniprot/Q3UP14 ^@ Chain|||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 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Growth hormone receptor|||Growth hormone-binding protein|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Required for JAK2 binding|||Required for endocytosis and down-regulation|||UbE motif|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010961|||http://purl.uniprot.org/annotation/PRO_0000010962|||http://purl.uniprot.org/annotation/PRO_5004230217|||http://purl.uniprot.org/annotation/PRO_5015097486|||http://purl.uniprot.org/annotation/VSP_001716|||http://purl.uniprot.org/annotation/VSP_001717 http://togogenome.org/gene/10090:Rhox2e ^@ http://purl.uniprot.org/uniprot/G3UYY0|||http://purl.uniprot.org/uniprot/Q9D4Y3 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Nop53 ^@ http://purl.uniprot.org/uniprot/Q8BK35 ^@ 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 and acidic residues|||Disordered|||Mediates interaction with CDKN2A/isoform tumor suppressor ARF|||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_0000440968 http://togogenome.org/gene/10090:Vmn2r60 ^@ http://purl.uniprot.org/uniprot/A0A3B2WBC8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5017441655 http://togogenome.org/gene/10090:Niban3 ^@ http://purl.uniprot.org/uniprot/D3YZB0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ PH ^@ http://togogenome.org/gene/10090:Mrpl18 ^@ http://purl.uniprot.org/uniprot/Q9CQL5 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein uL18m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000030557 http://togogenome.org/gene/10090:ATP8 ^@ http://purl.uniprot.org/uniprot/P03930|||http://purl.uniprot.org/uniprot/Q7JCZ0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Transmembrane ^@ ATP synthase protein 8|||Helical|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000195551 http://togogenome.org/gene/10090:Batf3 ^@ http://purl.uniprot.org/uniprot/Q9D275 ^@ 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 3|||Basic motif|||Disordered|||Leucine-zipper|||Phosphoserine|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000326107 http://togogenome.org/gene/10090:Zfp607a ^@ http://purl.uniprot.org/uniprot/Q3TQG9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Arhgef1 ^@ http://purl.uniprot.org/uniprot/E9PUF7|||http://purl.uniprot.org/uniprot/Q61210 ^@ 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|||DH|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by JAK2|||Polar residues|||Pro residues|||RGSL|||Rho guanine nucleotide exchange factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000080907|||http://purl.uniprot.org/annotation/VSP_008126|||http://purl.uniprot.org/annotation/VSP_008127|||http://purl.uniprot.org/annotation/VSP_008128|||http://purl.uniprot.org/annotation/VSP_008129|||http://purl.uniprot.org/annotation/VSP_008130|||http://purl.uniprot.org/annotation/VSP_026131 http://togogenome.org/gene/10090:H2-M1 ^@ http://purl.uniprot.org/uniprot/F7CXU4|||http://purl.uniprot.org/uniprot/Q31200|||http://purl.uniprot.org/uniprot/Q85ZX2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Non-terminal Residue|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5004219702|||http://purl.uniprot.org/annotation/PRO_5004300028|||http://purl.uniprot.org/annotation/PRO_5015091178 http://togogenome.org/gene/10090:Clhc1 ^@ http://purl.uniprot.org/uniprot/B7ZMV8|||http://purl.uniprot.org/uniprot/Q5M6W3 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict ^@ Clathrin heavy chain linker domain-containing protein 1|||Translin-associated factor X-interacting protein 1 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000325872 http://togogenome.org/gene/10090:A3galt2 ^@ http://purl.uniprot.org/uniprot/Q3V1N9 ^@ 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|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Alpha-1,3-galactosyltransferase 2|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In strain: NOD.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000314871|||http://purl.uniprot.org/annotation/VSP_054297 http://togogenome.org/gene/10090:Sgtb ^@ http://purl.uniprot.org/uniprot/Q8VD33 ^@ 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_0000106369 http://togogenome.org/gene/10090:Haus2 ^@ http://purl.uniprot.org/uniprot/Q9CQS9 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant ^@ HAUS augmin-like complex subunit 2|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000089485|||http://purl.uniprot.org/annotation/VSP_012224 http://togogenome.org/gene/10090:Zfp957 ^@ http://purl.uniprot.org/uniprot/Q3UT76 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||PHD-type|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Irs3 ^@ http://purl.uniprot.org/uniprot/O54718 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||IRS-type PTB|||PH|||Pro residues ^@ http://togogenome.org/gene/10090:Eif3g ^@ http://purl.uniprot.org/uniprot/Q544H0|||http://purl.uniprot.org/uniprot/Q9Z1D1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Eukaryotic translation initiation factor 3 subunit G|||Phosphoserine|||Phosphothreonine|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000123511 http://togogenome.org/gene/10090:Defb22 ^@ http://purl.uniprot.org/uniprot/Q8BVC1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Signal Peptide ^@ Beta-defensin 22|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5007953120 http://togogenome.org/gene/10090:Or4s2b ^@ http://purl.uniprot.org/uniprot/A2AV13 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kcnk4 ^@ http://purl.uniprot.org/uniprot/O88454|||http://purl.uniprot.org/uniprot/Q0VD85 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||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|||INTRAMEM|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Pore helix 1|||Helical; Name=Pore helix 2|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine|||Potassium channel|||Potassium channel subfamily K member 4|||Pro residues|||Selectivity filter 1|||Selectivity filter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000101748|||http://purl.uniprot.org/annotation/PRO_5015097001|||http://purl.uniprot.org/annotation/VSP_006690|||http://purl.uniprot.org/annotation/VSP_006691 http://togogenome.org/gene/10090:Tbc1d31 ^@ http://purl.uniprot.org/uniprot/Q6NXY1 ^@ 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 ^@ In isoform 2.|||Mediates direct interaction with PJA2|||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_0000051421|||http://purl.uniprot.org/annotation/VSP_016185|||http://purl.uniprot.org/annotation/VSP_016186|||http://purl.uniprot.org/annotation/VSP_016187 http://togogenome.org/gene/10090:Exosc2 ^@ http://purl.uniprot.org/uniprot/Q3TKQ3|||http://purl.uniprot.org/uniprot/Q8VBV3 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Exosome complex component N-terminal|||Exosome complex component RRP4|||K Homology|||Phosphoserine|||S1 motif ^@ http://purl.uniprot.org/annotation/PRO_0000087130 http://togogenome.org/gene/10090:Tnfrsf9 ^@ http://purl.uniprot.org/uniprot/P20334|||http://purl.uniprot.org/uniprot/Q3U3R1|||http://purl.uniprot.org/uniprot/Q8R037 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||TNFR-Cys|||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_0000034578|||http://purl.uniprot.org/annotation/PRO_5010843375|||http://purl.uniprot.org/annotation/PRO_5015099330 http://togogenome.org/gene/10090:Rrh ^@ http://purl.uniprot.org/uniprot/O35214|||http://purl.uniprot.org/uniprot/Q543W9|||http://purl.uniprot.org/uniprot/Q80XL3|||http://purl.uniprot.org/uniprot/Q9D1T9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||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|||N6-(retinylidene)lysine|||Visual pigment-like receptor peropsin ^@ http://purl.uniprot.org/annotation/PRO_0000197820 http://togogenome.org/gene/10090:Evx2 ^@ http://purl.uniprot.org/uniprot/P49749|||http://purl.uniprot.org/uniprot/Q6P7W9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Homeobox even-skipped homolog protein 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048873 http://togogenome.org/gene/10090:Arhgap42 ^@ http://purl.uniprot.org/uniprot/B2RQE8 ^@ 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 ^@ BAR|||Disordered|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Rho GTPase-activating protein 42|||Rho-GAP|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000399498 http://togogenome.org/gene/10090:Fndc1 ^@ http://purl.uniprot.org/uniprot/E9Q043 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Fibronectin type-III|||Polar residues ^@ http://togogenome.org/gene/10090:Trim38 ^@ http://purl.uniprot.org/uniprot/Q5SZ99 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Zinc Finger ^@ Abolished E3 ubiquitin-protein activity and ability to inhibit type I interferon IFN-beta production.|||Abolished E3 ubiquitin-protein activity and ability to ubiquitinate TICAM1. Abolished E3 SUMO-protein activity and ability to sumoylate CGAS.|||B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM38|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000454476 http://togogenome.org/gene/10090:Gm1604b ^@ http://purl.uniprot.org/uniprot/Q3TRG0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rtl8a ^@ http://purl.uniprot.org/uniprot/Q9D1F0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ DUF4939 ^@ http://togogenome.org/gene/10090:Vmn1r132 ^@ http://purl.uniprot.org/uniprot/E9Q8L6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc26a5 ^@ http://purl.uniprot.org/uniprot/Q32MT6|||http://purl.uniprot.org/uniprot/Q32MT7|||http://purl.uniprot.org/uniprot/Q99NH7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Contributes to anion binding|||Controls the electromotile activity|||Cytoplasmic|||Disordered|||Extended region for STAS domain|||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=5a|||Helical; Name=5b|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Involved in motor function|||N-linked (GlcNAc...) asparagine|||Polar residues|||Prestin|||STAS ^@ http://purl.uniprot.org/annotation/PRO_0000080169 http://togogenome.org/gene/10090:Ubxn11 ^@ http://purl.uniprot.org/uniprot/Q9D572 ^@ 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|||Polar residues|||SEP|||UBX|||UBX domain-containing protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000284922|||http://purl.uniprot.org/annotation/VSP_024778|||http://purl.uniprot.org/annotation/VSP_024779 http://togogenome.org/gene/10090:Sestd1 ^@ http://purl.uniprot.org/uniprot/Q80UK0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ CRAL-TRIO|||SEC14 domain and spectrin repeat-containing protein 1|||Spectrin 1|||Spectrin 2|||Spectrin 3 ^@ http://purl.uniprot.org/annotation/PRO_0000309480 http://togogenome.org/gene/10090:Map4k1 ^@ http://purl.uniprot.org/uniprot/P70218 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||CNH|||Disordered|||Loss of kinase activity and ability to activate JNK family. Inhibits the ability of CLNK to up-regulate CD3-triggered activation of the IL2 promoter.|||Mitogen-activated protein kinase kinase kinase kinase 1|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086274 http://togogenome.org/gene/10090:Camk2d ^@ http://purl.uniprot.org/uniprot/A0A0G2JGS4|||http://purl.uniprot.org/uniprot/E9Q1T1|||http://purl.uniprot.org/uniprot/E9Q1W0|||http://purl.uniprot.org/uniprot/Q6PHZ2|||http://purl.uniprot.org/uniprot/Q8CCM0 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase type II subunit delta|||Calmodulin-binding|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000277817|||http://purl.uniprot.org/annotation/VSP_023100|||http://purl.uniprot.org/annotation/VSP_023101|||http://purl.uniprot.org/annotation/VSP_023102|||http://purl.uniprot.org/annotation/VSP_023103 http://togogenome.org/gene/10090:Grik5 ^@ http://purl.uniprot.org/uniprot/Q61626|||http://purl.uniprot.org/uniprot/Q80WU3 ^@ 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|||Glutamate receptor|||Glutamate receptor ionotropic, kainate 5|||Helical|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000011553|||http://purl.uniprot.org/annotation/PRO_5027134822 http://togogenome.org/gene/10090:Pgd ^@ http://purl.uniprot.org/uniprot/Q9DCD0 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ 6-phosphogluconate dehydrogenase, decarboxylating|||N6-acetyllysine|||Phosphoserine|||Proton acceptor|||Proton donor|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000090064 http://togogenome.org/gene/10090:Gpc3 ^@ http://purl.uniprot.org/uniprot/Q3TWB2|||http://purl.uniprot.org/uniprot/Q8CFZ4 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||GPI-anchor amidated serine|||Glypican-3 alpha subunit|||Glypican-3 beta subunit|||Interchain (between alpha and beta chains)|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Phosphoserine|||Pyrrolidone carboxylic acid|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000012312|||http://purl.uniprot.org/annotation/PRO_0000445412|||http://purl.uniprot.org/annotation/PRO_0000445413|||http://purl.uniprot.org/annotation/PRO_5014309150 http://togogenome.org/gene/10090:Ubr1 ^@ http://purl.uniprot.org/uniprot/O70481 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase UBR1|||N-acetylalanine|||Phosphoserine|||RING-type; atypical|||Removed|||UBR-type ^@ http://purl.uniprot.org/annotation/PRO_0000056137 http://togogenome.org/gene/10090:Cygb ^@ http://purl.uniprot.org/uniprot/Q546K1|||http://purl.uniprot.org/uniprot/Q9CX80 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region ^@ Cytoglobin|||Disordered|||Globin|||Globin family profile|||distal binding residue|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000053385 http://togogenome.org/gene/10090:Or2d2 ^@ http://purl.uniprot.org/uniprot/Q8VG49 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:V1rd19 ^@ http://purl.uniprot.org/uniprot/Q3KNP5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cbr3 ^@ http://purl.uniprot.org/uniprot/Q8K354 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ Carbonyl reductase [NADPH] 3|||N-acetylserine|||Phosphoserine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000415806 http://togogenome.org/gene/10090:Dram2 ^@ http://purl.uniprot.org/uniprot/Q9CR48|||http://purl.uniprot.org/uniprot/Q9D835 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ DNA damage-regulated autophagy modulator protein 2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000254103 http://togogenome.org/gene/10090:Zmym4 ^@ http://purl.uniprot.org/uniprot/A2A791 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||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 isoform 2.|||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|||Removed|||Zinc finger MYM-type protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000299018|||http://purl.uniprot.org/annotation/VSP_027515 http://togogenome.org/gene/10090:Atp8b4 ^@ http://purl.uniprot.org/uniprot/A1L3S5|||http://purl.uniprot.org/uniprot/A2ANX3|||http://purl.uniprot.org/uniprot/Q69Z59 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Basic residues|||Disordered|||Helical|||P-type ATPase C-terminal|||P-type ATPase N-terminal ^@ http://togogenome.org/gene/10090:Sun5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J084|||http://purl.uniprot.org/uniprot/Q9DA32 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Corresponds to C-356 variant associated with SPGF16 in human. Impairs nuclear inner membrane location and decreases interaction with DNAJB13.|||Corresponds to I-348 variant associated with SPGF16 in human. Impairs nuclear inner membrane location and increases interaction with DNAJB13.|||Corresponds to M-261 variant associated with SPGF16 in human. Decreases protein solubility, impairs nuclear inner membrane location and decreases interaction with DNAJB13.|||Corresponds to M-275 variant associated with SPGF16 in human. Impairs nuclear inner membrane location and decreases interaction with DNAJB13.|||Corresponds to R-114 variant associated with SPGF16 in human. Impairs nuclear inner membrane location, expressed in the cytosol with some protein aggregation near the nuclear envelope.|||Corresponds to variant K-162 associated with SPGF16 in human. Increases interaction with DNAJB13. Impairs nuclear inner membrane location, expressed in the cytosol with some protein aggregation near the nuclear envelope.|||Helical|||In isoform 2.|||Nuclear|||Perinuclear space|||SUN|||SUN domain-containing protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000218920|||http://purl.uniprot.org/annotation/VSP_046528 http://togogenome.org/gene/10090:Psma6 ^@ http://purl.uniprot.org/uniprot/Q9QUM9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphotyrosine|||Proteasome subunit alpha type-6 ^@ http://purl.uniprot.org/annotation/PRO_0000124131 http://togogenome.org/gene/10090:Mrps9 ^@ http://purl.uniprot.org/uniprot/Q9D7N3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||Mitochondrion|||Small ribosomal subunit protein uS9m ^@ http://purl.uniprot.org/annotation/PRO_0000030656 http://togogenome.org/gene/10090:Pim2 ^@ http://purl.uniprot.org/uniprot/Q62070|||http://purl.uniprot.org/uniprot/Q8R1Z0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase pim-2 ^@ http://purl.uniprot.org/annotation/PRO_0000024366|||http://purl.uniprot.org/annotation/VSP_018854|||http://purl.uniprot.org/annotation/VSP_018855|||http://purl.uniprot.org/annotation/VSP_018856 http://togogenome.org/gene/10090:Eea1 ^@ http://purl.uniprot.org/uniprot/Q8BL66 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ C2H2-type|||Disordered|||Early endosome antigen 1|||FYVE-type|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000098707 http://togogenome.org/gene/10090:Fbxo17 ^@ http://purl.uniprot.org/uniprot/Q3V064|||http://purl.uniprot.org/uniprot/Q9QZM8 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ F-box|||F-box only protein 17|||FBA|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000119899|||http://purl.uniprot.org/annotation/VSP_012981|||http://purl.uniprot.org/annotation/VSP_012982 http://togogenome.org/gene/10090:Ccnf ^@ http://purl.uniprot.org/uniprot/P51944 ^@ 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 ^@ Cyclin N-terminal|||Cyclin-F|||D box 1|||D box 2|||D box 3|||D box 4|||Disordered|||F-box|||In isoform 2.|||In isoform 3.|||Nuclear localization signal 1|||Nuclear localization signal 2|||PEST|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080464|||http://purl.uniprot.org/annotation/VSP_001257|||http://purl.uniprot.org/annotation/VSP_039778 http://togogenome.org/gene/10090:Mgam ^@ http://purl.uniprot.org/uniprot/A0A571BF69|||http://purl.uniprot.org/uniprot/B5THE2 ^@ Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Disulfide Bond|||Domain Extent|||Transmembrane ^@ Helical|||P-type ^@ http://togogenome.org/gene/10090:Pank2 ^@ http://purl.uniprot.org/uniprot/Q7M753 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Region ^@ Disordered|||Nuclear export signal|||Pantothenate kinase 2, mitochondrial|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000452677 http://togogenome.org/gene/10090:Htr1a ^@ http://purl.uniprot.org/uniprot/Q64264 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane ^@ 5-hydroxytryptamine receptor 1A|||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|||In strain: C3H/An.|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000068904 http://togogenome.org/gene/10090:Kctd12 ^@ http://purl.uniprot.org/uniprot/A0A0R4J2B2|||http://purl.uniprot.org/uniprot/Q69ZA6|||http://purl.uniprot.org/uniprot/Q6WVG3|||http://purl.uniprot.org/uniprot/Q8C2V2 ^@ 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 KCTD12|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000191296 http://togogenome.org/gene/10090:Ntrk3 ^@ http://purl.uniprot.org/uniprot/A0A0A6YWF9|||http://purl.uniprot.org/uniprot/Q3TNY3|||http://purl.uniprot.org/uniprot/Q6VNS1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||In isoform 3.|||Interaction with PLC-gamma-1|||Interaction with PLCG1|||Interaction with SHC1|||LRR 1|||LRR 2|||LRRCT|||N-linked (GlcNAc...) asparagine|||NT-3 growth factor receptor|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase receptor ^@ http://purl.uniprot.org/annotation/PRO_0000260434|||http://purl.uniprot.org/annotation/PRO_5002035481|||http://purl.uniprot.org/annotation/VSP_021596|||http://purl.uniprot.org/annotation/VSP_021597|||http://purl.uniprot.org/annotation/VSP_021598|||http://purl.uniprot.org/annotation/VSP_021599 http://togogenome.org/gene/10090:Trpm2 ^@ http://purl.uniprot.org/uniprot/Q3UYE9|||http://purl.uniprot.org/uniprot/Q91YD4 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Abolishes lowering of temperature threshold for activation in response to reactive oxygen species.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ion transport|||Nudix box|||Nudix hydrolase|||Pore-forming|||Transient receptor potential cation channel subfamily M member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000215327 http://togogenome.org/gene/10090:Cd209b ^@ http://purl.uniprot.org/uniprot/Q3UTX5|||http://purl.uniprot.org/uniprot/Q8CJ85|||http://purl.uniprot.org/uniprot/Q8CJ91 ^@ 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|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||CD209 antigen-like protein B|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046605|||http://purl.uniprot.org/annotation/VSP_010068|||http://purl.uniprot.org/annotation/VSP_010069|||http://purl.uniprot.org/annotation/VSP_010070 http://togogenome.org/gene/10090:Niban2 ^@ http://purl.uniprot.org/uniprot/Q8R1F1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-myristoyl glycine|||PH|||Phosphoserine|||Polar residues|||Protein Niban 2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213122 http://togogenome.org/gene/10090:Xpo7 ^@ http://purl.uniprot.org/uniprot/Q9EPK7 ^@ 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 ^@ Exportin-7|||Importin N-terminal|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000204714|||http://purl.uniprot.org/annotation/VSP_018600 http://togogenome.org/gene/10090:Cfap57 ^@ http://purl.uniprot.org/uniprot/Q9D180 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Repeat ^@ Cilia- and flagella-associated protein 57|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8 ^@ http://purl.uniprot.org/annotation/PRO_0000346432 http://togogenome.org/gene/10090:Plau ^@ http://purl.uniprot.org/uniprot/P06869|||http://purl.uniprot.org/uniprot/Q0VBA8 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Signal Peptide|||Strand|||Turn ^@ Binds urokinase plasminogen activator surface receptor|||Charge relay system|||Connecting peptide|||EGF-like|||Interchain (between A and B chains)|||Kringle|||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/PRO_0000028322|||http://purl.uniprot.org/annotation/PRO_0000028323|||http://purl.uniprot.org/annotation/PRO_0000028324|||http://purl.uniprot.org/annotation/PRO_0000028325|||http://purl.uniprot.org/annotation/PRO_5014306862 http://togogenome.org/gene/10090:Gm3636 ^@ http://purl.uniprot.org/uniprot/A6NAV4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Crispld1 ^@ http://purl.uniprot.org/uniprot/Q8CGD2 ^@ 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 ^@ Cysteine-rich secretory protein LCCL domain-containing 1|||Disordered|||LCCL 1|||LCCL 2|||SCP ^@ http://purl.uniprot.org/annotation/PRO_0000248147 http://togogenome.org/gene/10090:Entpd3 ^@ http://purl.uniprot.org/uniprot/Q8BFW6 ^@ 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|||Ectonucleoside triphosphate diphosphohydrolase 3|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000455156 http://togogenome.org/gene/10090:Htr2c ^@ http://purl.uniprot.org/uniprot/P34968|||http://purl.uniprot.org/uniprot/Q8BZI5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 5-hydroxytryptamine receptor 2C|||Basic and acidic residues|||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|||PDZ-binding ^@ http://purl.uniprot.org/annotation/PRO_0000068959 http://togogenome.org/gene/10090:Adamtsl1 ^@ http://purl.uniprot.org/uniprot/E9PWW5|||http://purl.uniprot.org/uniprot/Q8BLI0|||http://purl.uniprot.org/uniprot/Q9CX59 ^@ 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 ^@ ADAMTS-like protein 1|||ADAMTS/ADAMTS-like cysteine-rich|||ADAMTS/ADAMTS-like cysteine-rich domain-containing protein|||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 2.|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc...) serine|||O-linked (Fuc...) threonine|||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|||TSP type-1 8|||TSP type-1 9 ^@ http://purl.uniprot.org/annotation/PRO_0000035861|||http://purl.uniprot.org/annotation/PRO_5003245465|||http://purl.uniprot.org/annotation/PRO_5004325008|||http://purl.uniprot.org/annotation/VSP_039332|||http://purl.uniprot.org/annotation/VSP_039333 http://togogenome.org/gene/10090:Mfsd13b ^@ http://purl.uniprot.org/uniprot/A0A1L1SUA2|||http://purl.uniprot.org/uniprot/Q9D3Y2 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Gm5916 ^@ http://purl.uniprot.org/uniprot/G5E8W5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015091954 http://togogenome.org/gene/10090:Casp6 ^@ http://purl.uniprot.org/uniprot/O08738|||http://purl.uniprot.org/uniprot/Q3TPJ9 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region ^@ 130's region|||Caspase family p10|||Caspase family p20|||Caspase-6 subunit p11|||Caspase-6 subunit p18|||Does not affect ability to promote ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis).|||Phosphoserine|||S-palmitoyl cysteine|||Tri-arginine exosite ^@ http://purl.uniprot.org/annotation/PRO_0000004612|||http://purl.uniprot.org/annotation/PRO_0000004613|||http://purl.uniprot.org/annotation/PRO_0000004614|||http://purl.uniprot.org/annotation/PRO_0000004615 http://togogenome.org/gene/10090:Smr2l ^@ http://purl.uniprot.org/uniprot/E9Q079 ^@ 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_5003245571 http://togogenome.org/gene/10090:Rnase2a ^@ http://purl.uniprot.org/uniprot/Q8K196 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_5015020126 http://togogenome.org/gene/10090:Tceal6 ^@ http://purl.uniprot.org/uniprot/Q9DB24 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Nhlrc1 ^@ http://purl.uniprot.org/uniprot/Q0VF71|||http://purl.uniprot.org/uniprot/Q8BR37 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Zinc Finger ^@ Chain|||Domain Extent|||Repeat|||Zinc Finger ^@ E3 ubiquitin-protein ligase NHLRC1|||NHL|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||NHL 6|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055981 http://togogenome.org/gene/10090:Fth1 ^@ http://purl.uniprot.org/uniprot/P09528 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Turn ^@ Ferritin heavy chain|||Ferritin heavy chain, N-terminally processed|||Ferritin-like diiron|||N-acetylmethionine|||N-acetylthreonine; in Ferritin heavy chain, N-terminally processed|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000201049|||http://purl.uniprot.org/annotation/PRO_0000424473 http://togogenome.org/gene/10090:Eif4h ^@ http://purl.uniprot.org/uniprot/Q3TG58|||http://purl.uniprot.org/uniprot/Q564E5|||http://purl.uniprot.org/uniprot/Q9WUK2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 4H|||In isoform Short.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||RRM|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000081620|||http://purl.uniprot.org/annotation/VSP_005800 http://togogenome.org/gene/10090:Phf3 ^@ http://purl.uniprot.org/uniprot/B2RQG2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PHD-type|||Polar residues|||Pro residues|||TFIIS central ^@ http://togogenome.org/gene/10090:Lrr1 ^@ http://purl.uniprot.org/uniprot/D3YY91 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Leucine-rich repeat protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000456676 http://togogenome.org/gene/10090:Gfy ^@ http://purl.uniprot.org/uniprot/J3KML8 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Golgi-associated olfactory signaling regulator|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000424824 http://togogenome.org/gene/10090:Or2y17 ^@ http://purl.uniprot.org/uniprot/Q8VGW9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ptger3 ^@ http://purl.uniprot.org/uniprot/Q6PDF2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mis18a ^@ http://purl.uniprot.org/uniprot/Q9CZJ6 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Mis18|||Phosphoserine|||Protein Mis18-alpha ^@ http://purl.uniprot.org/annotation/PRO_0000278473 http://togogenome.org/gene/10090:Ms4a10 ^@ http://purl.uniprot.org/uniprot/B2RWS0|||http://purl.uniprot.org/uniprot/Q99N03 ^@ 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.|||Membrane-spanning 4-domains subfamily A member 10 ^@ http://purl.uniprot.org/annotation/PRO_0000158647|||http://purl.uniprot.org/annotation/VSP_007387 http://togogenome.org/gene/10090:Tiparp ^@ http://purl.uniprot.org/uniprot/Q8C1B2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ ADP-ribosylcysteine|||C3H1-type|||Disordered|||Nuclear localization signal|||PARP catalytic|||Protein mono-ADP-ribosyltransferase TIPARP|||WWE ^@ http://purl.uniprot.org/annotation/PRO_0000247836 http://togogenome.org/gene/10090:Psme4 ^@ http://purl.uniprot.org/uniprot/Q5SSW2 ^@ 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 ^@ Bromodomain-like (BRDL)|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||In isoform 2.|||Phosphoserine|||Proteasome activator complex subunit 4 ^@ http://purl.uniprot.org/annotation/PRO_0000280719|||http://purl.uniprot.org/annotation/VSP_023880 http://togogenome.org/gene/10090:Lcn3 ^@ http://purl.uniprot.org/uniprot/Q14AJ3|||http://purl.uniprot.org/uniprot/Q62471 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding|||N-linked (GlcNAc...) asparagine|||Vomeronasal secretory protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000017978|||http://purl.uniprot.org/annotation/PRO_5015097032 http://togogenome.org/gene/10090:Prm2 ^@ http://purl.uniprot.org/uniprot/P07978|||http://purl.uniprot.org/uniprot/Q545M0 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Basic residues|||Disordered|||PP2-A|||PP2-B|||PP2-C|||PP2-D|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000025790|||http://purl.uniprot.org/annotation/PRO_0000025791|||http://purl.uniprot.org/annotation/PRO_0000025792|||http://purl.uniprot.org/annotation/PRO_0000025793 http://togogenome.org/gene/10090:Psg21 ^@ http://purl.uniprot.org/uniprot/Q9DAV5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Zfp423 ^@ http://purl.uniprot.org/uniprot/G3UW89|||http://purl.uniprot.org/uniprot/Q3V017|||http://purl.uniprot.org/uniprot/Q80TS5 ^@ 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 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 isoform 2.|||Phosphoserine|||Polar residues|||Zinc finger protein 423 ^@ http://purl.uniprot.org/annotation/PRO_0000308596|||http://purl.uniprot.org/annotation/VSP_029008 http://togogenome.org/gene/10090:Ccdc150 ^@ http://purl.uniprot.org/uniprot/A0A571BEL4|||http://purl.uniprot.org/uniprot/Q8CDI7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Sequence Conflict ^@ Coiled-coil domain-containing protein 150 ^@ http://purl.uniprot.org/annotation/PRO_0000328985 http://togogenome.org/gene/10090:Ring1 ^@ http://purl.uniprot.org/uniprot/O35730 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RING1|||In isoform 2.|||In isoform 3.|||Necessary for interaction with CBX2|||Necessary for transcriptional repression|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056386|||http://purl.uniprot.org/annotation/VSP_017695|||http://purl.uniprot.org/annotation/VSP_017696|||http://purl.uniprot.org/annotation/VSP_017697 http://togogenome.org/gene/10090:Mak ^@ http://purl.uniprot.org/uniprot/A0A286YD80|||http://purl.uniprot.org/uniprot/Q04859 ^@ 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 ^@ Disordered|||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_0000086285|||http://purl.uniprot.org/annotation/VSP_042472|||http://purl.uniprot.org/annotation/VSP_042473|||http://purl.uniprot.org/annotation/VSP_042474 http://togogenome.org/gene/10090:Nusap1 ^@ http://purl.uniprot.org/uniprot/Q9ERH4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Interaction with microtubules|||KEN box|||Nucleolar and spindle-associated protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000302035|||http://purl.uniprot.org/annotation/VSP_027913 http://togogenome.org/gene/10090:Ipo9 ^@ http://purl.uniprot.org/uniprot/E9QKZ2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Importin N-terminal ^@ http://togogenome.org/gene/10090:Apof ^@ http://purl.uniprot.org/uniprot/A0A0R4J0M4|||http://purl.uniprot.org/uniprot/Q91V80 ^@ Chain|||Molecule Processing|||Propeptide|||Signal Peptide ^@ Chain|||Propeptide|||Signal Peptide ^@ Apolipoprotein F ^@ http://purl.uniprot.org/annotation/PRO_0000002053|||http://purl.uniprot.org/annotation/PRO_0000002054|||http://purl.uniprot.org/annotation/PRO_5015044312 http://togogenome.org/gene/10090:Nln ^@ http://purl.uniprot.org/uniprot/Q91YP2 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||N6-acetyllysine|||Neurolysin, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000319046 http://togogenome.org/gene/10090:Vmn2r28 ^@ http://purl.uniprot.org/uniprot/L7N203 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982448 http://togogenome.org/gene/10090:Cry2 ^@ http://purl.uniprot.org/uniprot/Q9R194 ^@ 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolishes binding of FBXL3 and SKP1. Strongly decreases CRY2 degradation.|||Basic and acidic residues|||Cryptochrome-2|||Decreases FBXL3 binding. Strongly decreases CRY2 degradation.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs protein folding. Abolishes binding of BMAL1, PER1 and FBXL3. Strongly reduces SKP1 binding.|||Inhibits interaction with PER2. Does not suppress its nuclear localization. Inhibits its repression activity on CLOCK|NPAS2-BMAL1-driven transcription.|||Loss of ability to inhibit CLOCK-BMAL1-mediated transcriptional activity. No loss of ability to inhibit NR1I2 transcriptional activity.|||Phosphoserine|||Phosphoserine; by DYRK1A and MAPK|||Phosphoserine; by GSK3-beta|||Phosphoserine; by MAPK|||Photolyase/cryptochrome alpha/beta|||Polar residues|||Reduced in vitro MAPK-catalyzed phosphorylation. No effect on inhibition of CLOCK-BMAL1-mediated transcriptional activity. Very little in vitro MAPK-catalyzed phosphorylation; when associated with A-265. Shorter circadian rhythm; when associated with A-553.|||Reduced in vitro MAPK-catalyzed phosphorylation. No effect on inhibition of CLOCK-BMAL1-mediated transcriptional activity. Very little in vitro MAPK-catalyzed phosphorylation; when associated with A-557.|||Reduced inhibition of CLOCK-BMAL1-mediated transcriptional activity. No effect on nuclear localization nor on protein stability.|||Reduced interaction with NR1I2 and NR1I3. Significant decrease in interaction with NR1I2 and NR1I3; when associated with E-394 and K-397.|||Reduced interaction with NR1I2 and NR1I3. Significant decrease in interaction with NR1I2 and NR1I3; when associated with E-394 and M-396.|||Reduced interaction with NR1I2 and NR1I3. Significant decrease in interaction with NR1I2 and NR1I3; when associated with M-396 and K-397.|||Required for inhibition of CLOCK-BMAL1-mediated transcription|||Shorter circadian rhythm; when associated with A-557.|||Strongly reduces PER1 binding. ^@ http://purl.uniprot.org/annotation/PRO_0000261149 http://togogenome.org/gene/10090:Adgrf4 ^@ http://purl.uniprot.org/uniprot/A0A0D9SEG9|||http://purl.uniprot.org/uniprot/Q9D2L6 ^@ 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 ^@ Adhesion G protein-coupled receptor F4|||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_0000012895|||http://purl.uniprot.org/annotation/PRO_5015036490 http://togogenome.org/gene/10090:Acot6 ^@ http://purl.uniprot.org/uniprot/B2RTE4|||http://purl.uniprot.org/uniprot/Q32Q92 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Motif|||Splice Variant ^@ Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase|||Acyl-coenzyme A thioesterase 6|||BAAT/Acyl-CoA thioester hydrolase C-terminal|||Charge relay system|||In isoform 2.|||Peroxisome targeting signal ^@ http://purl.uniprot.org/annotation/PRO_0000305099|||http://purl.uniprot.org/annotation/VSP_028234|||http://purl.uniprot.org/annotation/VSP_028235 http://togogenome.org/gene/10090:Trpc5 ^@ http://purl.uniprot.org/uniprot/Q2KHN9|||http://purl.uniprot.org/uniprot/Q8C8A8|||http://purl.uniprot.org/uniprot/Q9QX29 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Repeat|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cytoplasmic|||Disordered|||Essential for binding to NHERF1 PDZ domain|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Short transient receptor potential channel 5|||Transient receptor ion channel ^@ http://purl.uniprot.org/annotation/PRO_0000215319 http://togogenome.org/gene/10090:Hoga1 ^@ http://purl.uniprot.org/uniprot/Q9DCU9 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Site|||Transit Peptide ^@ 4-hydroxy-2-oxoglutarate aldolase, mitochondrial|||Involved in proton transfer during cleavage|||Mitochondrion|||Schiff-base intermediate with substrate ^@ http://purl.uniprot.org/annotation/PRO_0000273347 http://togogenome.org/gene/10090:Gm9602 ^@ http://purl.uniprot.org/uniprot/L7N276 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:Vmn1r10 ^@ http://purl.uniprot.org/uniprot/W4VSP8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc22a23 ^@ http://purl.uniprot.org/uniprot/Q3UHH2 ^@ 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|||Solute carrier family 22 member 23 ^@ http://purl.uniprot.org/annotation/PRO_0000308316|||http://purl.uniprot.org/annotation/VSP_028957|||http://purl.uniprot.org/annotation/VSP_028958 http://togogenome.org/gene/10090:H2al1k ^@ http://purl.uniprot.org/uniprot/J3QP08 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Histone H2A/H2B/H3 ^@ http://togogenome.org/gene/10090:Pdik1l ^@ http://purl.uniprot.org/uniprot/Q8QZR7 ^@ 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 PDIK1L ^@ http://purl.uniprot.org/annotation/PRO_0000086495 http://togogenome.org/gene/10090:Mlec ^@ http://purl.uniprot.org/uniprot/Q6ZQI3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Malectin|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000013983 http://togogenome.org/gene/10090:Or52m2 ^@ http://purl.uniprot.org/uniprot/Q7TRS6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or1b1 ^@ http://purl.uniprot.org/uniprot/Q8VGV7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cpxm1 ^@ http://purl.uniprot.org/uniprot/Q3V190|||http://purl.uniprot.org/uniprot/Q9Z100 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||F5/8 type C|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Probable carboxypeptidase X1 ^@ http://purl.uniprot.org/annotation/PRO_0000004408 http://togogenome.org/gene/10090:Stk39 ^@ http://purl.uniprot.org/uniprot/A2AQL0|||http://purl.uniprot.org/uniprot/Q9Z1W9 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Abolished ability to activate SLC12A2/NKCC1.|||Basic and acidic residues|||Caspase cleavage related site|||Disordered|||Impaired phosphorylation by WNK4 and activation. Abolished ability to activate SLC12A2/NKCC1. Knockin mice are unable to activate SLC12A3/NCC.|||Increased kinase activity and autophosphorylation.|||Interaction with RELT|||Loss of kinase activity but no loss of interaction with RELT.|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PKC/PRKCQ|||Phosphothreonine|||Phosphothreonine; by WNK4|||Pro residues|||Protein kinase|||Proton acceptor|||STE20/SPS1-related proline-alanine-rich protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000086723 http://togogenome.org/gene/10090:Prpf3 ^@ http://purl.uniprot.org/uniprot/Q922U1 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Mediates interaction with SART3|||PWI|||Phosphoserine|||U4/U6 small nuclear ribonucleoprotein Prp3 ^@ http://purl.uniprot.org/annotation/PRO_0000097045 http://togogenome.org/gene/10090:Sowahd ^@ http://purl.uniprot.org/uniprot/Q8BY98 ^@ 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 SOWAHD|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315706 http://togogenome.org/gene/10090:Nkain1 ^@ http://purl.uniprot.org/uniprot/Q9D035 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000263644 http://togogenome.org/gene/10090:Srp14 ^@ http://purl.uniprot.org/uniprot/P16254 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Helix|||Modified Residue|||Region|||Strand ^@ Disordered|||Phosphoserine|||Signal recognition particle 14 kDa protein ^@ http://purl.uniprot.org/annotation/PRO_0000135191 http://togogenome.org/gene/10090:1810062G17Rik ^@ http://purl.uniprot.org/uniprot/G3X8Y2|||http://purl.uniprot.org/uniprot/Q9D8K9 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Upb1 ^@ http://purl.uniprot.org/uniprot/Q3UEK4|||http://purl.uniprot.org/uniprot/Q8VC97 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue ^@ Beta-ureidopropionase|||CN hydrolase|||Nucleophile|||Phosphoserine|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000204052 http://togogenome.org/gene/10090:Wrn ^@ http://purl.uniprot.org/uniprot/O09053|||http://purl.uniprot.org/uniprot/Q3TB25|||http://purl.uniprot.org/uniprot/Q8BWH5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Strand ^@ 3'-5' exonuclease|||Basic and acidic residues|||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|||Interaction with DNA|||Interaction with WRNIP1|||KBM 1|||KBM 2|||Loss of exonuclease activity.|||Phosphoserine|||Polar residues|||Strongly reduced exonuclease activity.|||XLM ^@ http://purl.uniprot.org/annotation/PRO_0000205046 http://togogenome.org/gene/10090:Tsga8 ^@ http://purl.uniprot.org/uniprot/Q9JJL0 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1-1|||1-2|||1-3|||1-4|||2-1|||2-2|||2-3|||2-4|||4 X 15 AA tandem repeats of A-A-A-A-A-P-E-A-A-A-S-[PL]-E-S-S|||4 X 6 AA repeats of P-A-A-P-E-A|||Disordered|||Testis-specific gene A8 protein ^@ http://purl.uniprot.org/annotation/PRO_0000439814 http://togogenome.org/gene/10090:Prrg3 ^@ http://purl.uniprot.org/uniprot/Q6PAQ9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Propeptide|||Region|||Topological Domain|||Transmembrane ^@ 4-carboxyglutamate|||Cytoplasmic|||Disordered|||Extracellular|||Gla|||Helical|||Polar residues|||Transmembrane gamma-carboxyglutamic acid protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000022549|||http://purl.uniprot.org/annotation/PRO_0000022550 http://togogenome.org/gene/10090:Flcn ^@ http://purl.uniprot.org/uniprot/Q8QZS3 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Disordered|||Essential for GTPase activation (GAP) activity|||Folliculin|||Phosphoserine|||cDENN FLCN/SMCR8-type|||dDENN FLCN/SMCR8-type|||uDENN FLCN/SMCR8-type ^@ http://purl.uniprot.org/annotation/PRO_0000223941 http://togogenome.org/gene/10090:Hsbp1 ^@ http://purl.uniprot.org/uniprot/Q9CQZ1 ^@ Chain|||Molecule Processing ^@ Chain ^@ Heat shock factor-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000124806 http://togogenome.org/gene/10090:Mpl ^@ http://purl.uniprot.org/uniprot/A2A9D4|||http://purl.uniprot.org/uniprot/Q08351 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Box 1 motif|||Cytoplasmic|||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 isoform Mpl-tr.|||N-linked (GlcNAc...) asparagine|||Thrombopoietin receptor|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010988|||http://purl.uniprot.org/annotation/PRO_5009682416|||http://purl.uniprot.org/annotation/VSP_059621|||http://purl.uniprot.org/annotation/VSP_059622 http://togogenome.org/gene/10090:Or9k2 ^@ http://purl.uniprot.org/uniprot/Q8VFU7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nisch ^@ http://purl.uniprot.org/uniprot/Q80TM9|||http://purl.uniprot.org/uniprot/Q8CF63 ^@ 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 ^@ 1|||10|||10 X 6 AA tandem repeat of A-E-A-P-A-A|||2|||3|||4|||5|||6|||7|||8|||9|||Acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with ITGA5|||Interaction with LIMK|||Interaction with PAK1|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||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|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000348266|||http://purl.uniprot.org/annotation/VSP_035136|||http://purl.uniprot.org/annotation/VSP_035137|||http://purl.uniprot.org/annotation/VSP_035138|||http://purl.uniprot.org/annotation/VSP_035139|||http://purl.uniprot.org/annotation/VSP_035140|||http://purl.uniprot.org/annotation/VSP_035141|||http://purl.uniprot.org/annotation/VSP_035142|||http://purl.uniprot.org/annotation/VSP_035143|||http://purl.uniprot.org/annotation/VSP_035144|||http://purl.uniprot.org/annotation/VSP_035145 http://togogenome.org/gene/10090:Rpp30 ^@ http://purl.uniprot.org/uniprot/O88796|||http://purl.uniprot.org/uniprot/Q3TF81 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue ^@ Chain|||Initiator Methionine|||Modified Residue|||Non-terminal Residue ^@ N-acetylalanine|||Phosphoserine|||Removed|||Ribonuclease P protein subunit p30 ^@ http://purl.uniprot.org/annotation/PRO_0000140032 http://togogenome.org/gene/10090:Ccdc184 ^@ http://purl.uniprot.org/uniprot/Q8BMK5 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Splice Variant ^@ Coiled-coil domain-containing protein 184|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000335682|||http://purl.uniprot.org/annotation/VSP_033768 http://togogenome.org/gene/10090:Ccdc7b ^@ http://purl.uniprot.org/uniprot/B9EJU4|||http://purl.uniprot.org/uniprot/E9Q9Y3|||http://purl.uniprot.org/uniprot/Q9DAK5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Romo1 ^@ http://purl.uniprot.org/uniprot/P60603 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Helical|||Reactive oxygen species modulator 1|||Sufficient for antibacterial activity ^@ http://purl.uniprot.org/annotation/PRO_0000079434 http://togogenome.org/gene/10090:Nrde2 ^@ http://purl.uniprot.org/uniprot/Q80XC6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||HAT 1|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||MID/MTR4-interacting domain|||N-acetylalanine|||Nuclear exosome regulator NRDE2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089908 http://togogenome.org/gene/10090:Cd164 ^@ http://purl.uniprot.org/uniprot/Q9R0L9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Increased targeting to the endosomal/lysosomal compartment and reduced myotube formation.|||Inefficient targeting to the endosomal/lysosomal compartment and enhanced myotube formation.|||N-linked (GlcNAc...) asparagine|||Required for endosomal and lysosomal localization|||Sialomucin core protein 24 ^@ http://purl.uniprot.org/annotation/PRO_0000383341 http://togogenome.org/gene/10090:Bcor ^@ http://purl.uniprot.org/uniprot/Q8CGN4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||BCL-6 corepressor|||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.|||Interaction with BCL6|||N6-acetyllysine|||Necessary and sufficient for interaction with PCGF1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000066979|||http://purl.uniprot.org/annotation/VSP_012558|||http://purl.uniprot.org/annotation/VSP_012559 http://togogenome.org/gene/10090:Themis2 ^@ http://purl.uniprot.org/uniprot/Q91YX0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region ^@ CABIT 1|||CABIT 2|||Disordered|||Drastic decrease in GRB2-binding, but no effect on VAV-binding; when associated with A-552. Partial loss of enhancement of LPS-induced TNF production; when associated with A-552.|||Drastic decrease in GRB2-binding, but no effect on VAV-binding; when associated with A-555. Partial loss of enhancement of LPS-induced TNF production; when associated with A-555.|||Loss of phosphorylation. Loss of LYN-binding. Slight decrease in GRB2-binding. No effect on VAV-binding. Partial loss of enhancement of LPS-induced TNF production.|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein THEMIS2 ^@ http://purl.uniprot.org/annotation/PRO_0000084144 http://togogenome.org/gene/10090:Pgam2 ^@ http://purl.uniprot.org/uniprot/O70250|||http://purl.uniprot.org/uniprot/Q5NCI4 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Site ^@ Phosphoglycerate mutase 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton donor/acceptor|||Tele-phosphohistidine intermediate|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000179830 http://togogenome.org/gene/10090:Cops7b ^@ http://purl.uniprot.org/uniprot/Q8BV13 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||COP9 signalosome complex subunit 7b|||Disordered|||N-acetylalanine|||PCI|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000121000 http://togogenome.org/gene/10090:2310011J03Rik ^@ http://purl.uniprot.org/uniprot/Q9D7E4 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Region ^@ Disordered|||Phosphotyrosine|||UPF0449 protein C19orf25 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000252421 http://togogenome.org/gene/10090:Il33 ^@ http://purl.uniprot.org/uniprot/Q8BVZ5 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Chain|||Helix|||Propeptide|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ Cleavage; by CTSG and ELANE|||Cleavage; by ELANE|||Homeodomain-like HTH domain|||Interaction with RELA|||Interleukin-33|||Interleukin-33(102-266)|||Interleukin-33(109-266) ^@ http://purl.uniprot.org/annotation/PRO_0000096791|||http://purl.uniprot.org/annotation/PRO_0000430087|||http://purl.uniprot.org/annotation/PRO_0000430088|||http://purl.uniprot.org/annotation/PRO_0000430089 http://togogenome.org/gene/10090:Gck ^@ http://purl.uniprot.org/uniprot/P52792|||http://purl.uniprot.org/uniprot/Q5SVI5|||http://purl.uniprot.org/uniprot/Q5SVI6 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Hexokinase|||Hexokinase C-terminal|||Hexokinase N-terminal|||Hexokinase large subdomain|||Hexokinase small subdomain|||Hexokinase-4|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000197594|||http://purl.uniprot.org/annotation/VSP_002076 http://togogenome.org/gene/10090:Rabl6 ^@ http://purl.uniprot.org/uniprot/Q5U3K5 ^@ 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|||Interaction with CDKN2A|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rab-like protein 6|||Small GTPase-like ^@ http://purl.uniprot.org/annotation/PRO_0000274224 http://togogenome.org/gene/10090:Actr3 ^@ http://purl.uniprot.org/uniprot/Q99JY9 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Actin-related protein 3|||N-acetylalanine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089080 http://togogenome.org/gene/10090:Slx4ip ^@ http://purl.uniprot.org/uniprot/Q9D7Y9 ^@ 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 ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphothreonine|||Polar residues|||Protein SLX4IP ^@ http://purl.uniprot.org/annotation/PRO_0000306120|||http://purl.uniprot.org/annotation/VSP_028421|||http://purl.uniprot.org/annotation/VSP_028422|||http://purl.uniprot.org/annotation/VSP_028423 http://togogenome.org/gene/10090:Magee1 ^@ http://purl.uniprot.org/uniprot/Q6PCZ4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Interaction with DTNA|||MAGE 1|||MAGE 2|||Melanoma-associated antigen E1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000404299 http://togogenome.org/gene/10090:Thumpd1 ^@ http://purl.uniprot.org/uniprot/Q99J36 ^@ 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 ^@ Basic and acidic residues|||Disordered|||N-acetylalanine|||Phosphoserine|||Removed|||THUMP|||THUMP domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072531 http://togogenome.org/gene/10090:Pkd2l2 ^@ http://purl.uniprot.org/uniprot/Q3V056|||http://purl.uniprot.org/uniprot/Q9JLG4 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polycystin|||Polycystin cation channel PKD1/PKD2|||Polycystin-2-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000164362 http://togogenome.org/gene/10090:Smad3 ^@ http://purl.uniprot.org/uniprot/Q8BUN5 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Linker|||MH1|||MH2|||Mothers against decapentaplegic homolog 3|||N-acetylserine|||N6-acetyllysine|||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|||Removed|||Required for interaction with DNA and JUN and for functional cooperation with JUN|||Required for trimerization|||Sufficient for interaction with XPO4 ^@ http://purl.uniprot.org/annotation/PRO_0000090857 http://togogenome.org/gene/10090:Or5b94 ^@ http://purl.uniprot.org/uniprot/Q0VEV7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lig1 ^@ http://purl.uniprot.org/uniprot/P37913|||http://purl.uniprot.org/uniprot/Q3TSU8|||http://purl.uniprot.org/uniprot/Q3U4X8|||http://purl.uniprot.org/uniprot/Q8R055 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Site ^@ ATP-dependent DNA ligase family profile|||Basic and acidic residues|||DNA ligase 1|||Disordered|||Interaction with target DNA|||N6-AMP-lysine intermediate|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000059571 http://togogenome.org/gene/10090:Tbce ^@ http://purl.uniprot.org/uniprot/Q8CIV8 ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant|||Strand|||Turn ^@ CAP-Gly|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000083539 http://togogenome.org/gene/10090:Or4k2 ^@ http://purl.uniprot.org/uniprot/E9Q8M3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Snrpd3 ^@ http://purl.uniprot.org/uniprot/P62320 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat ^@ 1|||2|||3|||4|||5|||5 X 2 AA tandem repeats of [RM]-G|||N-acetylserine|||Removed|||Sm|||Small nuclear ribonucleoprotein Sm D3 ^@ http://purl.uniprot.org/annotation/PRO_0000122215 http://togogenome.org/gene/10090:Atad5 ^@ http://purl.uniprot.org/uniprot/Q4QY64|||http://purl.uniprot.org/uniprot/Z4YKQ9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ AAA+ ATPase|||ATPase family AAA domain-containing protein 5|||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|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317619|||http://purl.uniprot.org/annotation/VSP_031098|||http://purl.uniprot.org/annotation/VSP_031099 http://togogenome.org/gene/10090:Tarbp2 ^@ http://purl.uniprot.org/uniprot/P97473|||http://purl.uniprot.org/uniprot/Q3UNH9 ^@ 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 ^@ DRBM|||DRBM 1|||DRBM 2|||DRBM 3|||Disordered|||Phosphoserine|||Polar residues|||RISC-loading complex subunit TARBP2|||Sufficient for interaction with DICER1|||Sufficient for interaction with PRKRA ^@ http://purl.uniprot.org/annotation/PRO_0000065623 http://togogenome.org/gene/10090:E2f6 ^@ http://purl.uniprot.org/uniprot/O54917|||http://purl.uniprot.org/uniprot/Q8VHT4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Binding to corepressors|||DEF box|||Dimerization|||Disordered|||E2F/DP family winged-helix DNA-binding|||Leucine-zipper|||Polar residues|||Transcription factor E2F6|||Transcription repression ^@ http://purl.uniprot.org/annotation/PRO_0000219473 http://togogenome.org/gene/10090:Ttc12 ^@ http://purl.uniprot.org/uniprot/Q8BW49 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ Phosphothreonine|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000106397 http://togogenome.org/gene/10090:Gm614 ^@ http://purl.uniprot.org/uniprot/Q3V2K1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Uncharacterized protein CXorf65 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000346435 http://togogenome.org/gene/10090:Ddx17 ^@ http://purl.uniprot.org/uniprot/Q3U741|||http://purl.uniprot.org/uniprot/Q501J6|||http://purl.uniprot.org/uniprot/Q8K392 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||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.|||Interaction with YAP1|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphothreonine|||Polar residues|||Pro residues|||Probable ATP-dependent RNA helicase DDX17|||Q motif|||Transactivation domain ^@ http://purl.uniprot.org/annotation/PRO_0000054994|||http://purl.uniprot.org/annotation/VSP_015780|||http://purl.uniprot.org/annotation/VSP_015781 http://togogenome.org/gene/10090:Or2ak4 ^@ http://purl.uniprot.org/uniprot/A0A0N4SVP2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp414 ^@ http://purl.uniprot.org/uniprot/Q14A93|||http://purl.uniprot.org/uniprot/Q9DCK4 ^@ 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 ^@ C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; degenerate|||Disordered|||In isoform 2.|||Polar residues|||Pro residues|||Zinc finger protein 414 ^@ http://purl.uniprot.org/annotation/PRO_0000242164|||http://purl.uniprot.org/annotation/VSP_019454 http://togogenome.org/gene/10090:Rab7b ^@ http://purl.uniprot.org/uniprot/Q8VEA8 ^@ 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 ^@ Effector region|||In isoform 2.|||Phosphoserine|||Ras-related protein Rab-7b|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121126|||http://purl.uniprot.org/annotation/VSP_011108 http://togogenome.org/gene/10090:Dkk4 ^@ http://purl.uniprot.org/uniprot/Q8VEJ3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Signal Peptide ^@ DKK-type Cys-1|||DKK-type Cys-2|||Dickkopf-related protein 4|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000007227 http://togogenome.org/gene/10090:Myc ^@ http://purl.uniprot.org/uniprot/P01108 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ 9aaTAD|||Basic and acidic residues|||Disordered|||Does not affect interaction with TRIM6.|||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.|||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|||Phosphoserine|||Phosphoserine; by DYRK2, GSK3 and CDK2|||Phosphoserine; by PIM2; in vitro|||Phosphothreonine|||Phosphothreonine; by GSK3; alternate|||Polar residues|||Reduces phosphorylation by PIM2 by 60%, and decreases the transcriptional activity of MYC.|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127296|||http://purl.uniprot.org/annotation/VSP_061781|||http://purl.uniprot.org/annotation/VSP_061782 http://togogenome.org/gene/10090:Tat ^@ http://purl.uniprot.org/uniprot/Q8QZR1 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ N-acetylmethionine|||N6-(pyridoxal phosphate)lysine|||Phosphoserine|||Tyrosine aminotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000123888 http://togogenome.org/gene/10090:Dpyd ^@ http://purl.uniprot.org/uniprot/Q8CHR6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ 4Fe-4S ferredoxin-type 1|||4Fe-4S ferredoxin-type 2|||4Fe-4S ferredoxin-type 3|||Dihydropyrimidine dehydrogenase [NADP(+)]|||N6-acetyllysine|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000327501 http://togogenome.org/gene/10090:Smarca4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J170|||http://purl.uniprot.org/uniprot/Q3TKT4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ 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 isoform 2.|||N6-acetyllysine|||Necessary for interaction with SS18L1/CREST|||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_0000391343|||http://purl.uniprot.org/annotation/VSP_038696 http://togogenome.org/gene/10090:Hsd11b1 ^@ http://purl.uniprot.org/uniprot/P50172|||http://purl.uniprot.org/uniprot/Q4JHD9 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 11-beta-hydroxysteroid dehydrogenase 1|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054621 http://togogenome.org/gene/10090:Pknox1 ^@ http://purl.uniprot.org/uniprot/O70477 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Homeobox protein PKNOX1|||Homeobox; TALE-type|||MEIS N-terminal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000049249 http://togogenome.org/gene/10090:Ceacam10 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0G1|||http://purl.uniprot.org/uniprot/Q61400 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site ^@ Carcinoembryonic antigen-related cell adhesion molecule 10|||Ig-like V-type 1|||Ig-like V-type 2|||Immunoglobulin V-set|||N-linked (GlcNAc...) asparagine|||Not glycosylated ^@ http://purl.uniprot.org/annotation/PRO_0000014574|||http://purl.uniprot.org/annotation/PRO_5006451945 http://togogenome.org/gene/10090:Sbk2 ^@ http://purl.uniprot.org/uniprot/P0C5K1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase SBK2 ^@ http://purl.uniprot.org/annotation/PRO_0000308264 http://togogenome.org/gene/10090:Or4k5 ^@ http://purl.uniprot.org/uniprot/Q8VET4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp114 ^@ http://purl.uniprot.org/uniprot/Q3UGQ0|||http://purl.uniprot.org/uniprot/Q3UTF4 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Cpb1 ^@ http://purl.uniprot.org/uniprot/B2RS76 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase M14 carboxypeptidase A ^@ http://purl.uniprot.org/annotation/PRO_5015087148 http://togogenome.org/gene/10090:Efcab15 ^@ http://purl.uniprot.org/uniprot/A2AB62 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||EF-hand|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Cabp1 ^@ http://purl.uniprot.org/uniprot/D3Z1M4|||http://purl.uniprot.org/uniprot/Q9JLK7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Calcium-binding protein 1|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform S-CaBP1.|||N-myristoyl glycine|||Phosphoserine|||Pro residues|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000073514|||http://purl.uniprot.org/annotation/VSP_000733 http://togogenome.org/gene/10090:Mageb16 ^@ http://purl.uniprot.org/uniprot/Q9CWV4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||MAGE|||Melanoma-associated antigen B16 ^@ http://purl.uniprot.org/annotation/PRO_0000311929 http://togogenome.org/gene/10090:Cul5 ^@ http://purl.uniprot.org/uniprot/E9Q6Z0|||http://purl.uniprot.org/uniprot/G3X914|||http://purl.uniprot.org/uniprot/Q2M4H5|||http://purl.uniprot.org/uniprot/Q9D5V5 ^@ 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|||Region|||Sequence Conflict|||Turn ^@ Cullin family profile|||Cullin-5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000119798 http://togogenome.org/gene/10090:Nsun4 ^@ http://purl.uniprot.org/uniprot/Q9CZ57 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Splice Variant|||Transit Peptide ^@ 5-methylcytosine rRNA methyltransferase NSUN4|||In isoform 2.|||Mitochondrion|||Nucleophile|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000289235|||http://purl.uniprot.org/annotation/VSP_025974|||http://purl.uniprot.org/annotation/VSP_025975 http://togogenome.org/gene/10090:Arl8b ^@ http://purl.uniprot.org/uniprot/Q9CQW2 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||INTRAMEM|||Sequence Conflict ^@ ADP-ribosylation factor-like protein 8B|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Note=Mediates targeting to membranes ^@ http://purl.uniprot.org/annotation/PRO_0000232923 http://togogenome.org/gene/10090:Timm17a ^@ http://purl.uniprot.org/uniprot/Q545U2|||http://purl.uniprot.org/uniprot/Q9Z0V8 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Disulfide Bond|||Region|||Transmembrane ^@ Disordered|||Helical|||Mitochondrial import inner membrane translocase subunit Tim17-A ^@ http://purl.uniprot.org/annotation/PRO_0000210285 http://togogenome.org/gene/10090:Rgl1 ^@ http://purl.uniprot.org/uniprot/E9Q8M9|||http://purl.uniprot.org/uniprot/E9Q8N0|||http://purl.uniprot.org/uniprot/Q60695 ^@ 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 ^@ Disordered|||N-terminal Ras-GEF|||Phosphoserine|||Polar residues|||Ral guanine nucleotide dissociation stimulator-like 1|||Ras-GEF|||Ras-associating ^@ http://purl.uniprot.org/annotation/PRO_0000068886 http://togogenome.org/gene/10090:Myh3 ^@ http://purl.uniprot.org/uniprot/P13541 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Actin-binding|||Disordered|||IQ|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-3|||N6,N6,N6-trimethyllysine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000123395 http://togogenome.org/gene/10090:Cidea ^@ http://purl.uniprot.org/uniprot/O70302 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolished lipid transferase activity.|||Abolished localization to lipid droplets.|||Amphipathic helix|||CIDE-N|||Does not affect localization to lipid droplets but prevents lipid droplet fusion.|||Does not affect localization to lipid droplets or ability to mediate lipid droplet fusion.|||Increased nuclear localization.|||Lipid transferase CIDEA|||Sustantial reduction in nuclear localization and loss of XDH induction; when associated with A-23.|||Sustantial reduction in nuclear localization and loss of XDH induction; when associated with A-24. ^@ http://purl.uniprot.org/annotation/PRO_0000144719 http://togogenome.org/gene/10090:Aldh3a2 ^@ http://purl.uniprot.org/uniprot/B1AV77|||http://purl.uniprot.org/uniprot/P47740 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Aldehyde dehydrogenase|||Aldehyde dehydrogenase family 3 member A2|||Cytoplasmic|||Helical|||Phosphoserine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000056475 http://togogenome.org/gene/10090:Tmem200a ^@ http://purl.uniprot.org/uniprot/B2RUN2|||http://purl.uniprot.org/uniprot/Q8C817 ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Transmembrane protein 200A ^@ http://purl.uniprot.org/annotation/PRO_0000294341 http://togogenome.org/gene/10090:Cecr2 ^@ http://purl.uniprot.org/uniprot/E9Q2Z1 ^@ 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|||Basic and acidic residues|||Bromo|||Chromatin remodeling regulator CECR2|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000441775|||http://purl.uniprot.org/annotation/VSP_059110 http://togogenome.org/gene/10090:U2af2 ^@ http://purl.uniprot.org/uniprot/P26369|||http://purl.uniprot.org/uniprot/Q80XR5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn ^@ 5-hydroxylysine; by JMJD6|||5-hydroxylysine; by JMJD6; alternate|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylserine|||N6-acetyllysine; alternate|||Necessary and sufficient to stimulate pre-mRNAs 3'-end cleavage in a CFIm complex-dependent manner|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||RRM 3|||Removed|||Required for interaction with PRPF19|||Splicing factor U2AF 65 kDa subunit ^@ http://purl.uniprot.org/annotation/PRO_0000081989 http://togogenome.org/gene/10090:Serpinh1 ^@ http://purl.uniprot.org/uniprot/P19324 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide|||Site ^@ N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Prevents secretion from ER|||Reactive bond homolog|||Serpin H1 ^@ http://purl.uniprot.org/annotation/PRO_0000032517 http://togogenome.org/gene/10090:Sike1 ^@ http://purl.uniprot.org/uniprot/Q9CPR7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Sequence Conflict ^@ Suppressor of IKBKE 1 ^@ http://purl.uniprot.org/annotation/PRO_0000299051 http://togogenome.org/gene/10090:Hoxd13 ^@ http://purl.uniprot.org/uniprot/P70217 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Changes the function in transcription regulation.|||Changes the specificity for binding motifs in promoters. Recognizes the PITX1 consensus DNA-binding sites and triggers the expression of a gene pattern similar to PITX1.|||Disordered|||Homeobox|||Homeobox protein Hox-D13 ^@ http://purl.uniprot.org/annotation/PRO_0000200245 http://togogenome.org/gene/10090:Lipo1 ^@ http://purl.uniprot.org/uniprot/F6WYC8 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Signal Peptide ^@ AB hydrolase-1|||Charge relay system|||Lipase|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_5017191142 http://togogenome.org/gene/10090:Bcl2l15 ^@ http://purl.uniprot.org/uniprot/Q08ED0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Bcl-2-like protein 15 ^@ http://purl.uniprot.org/annotation/PRO_0000283004 http://togogenome.org/gene/10090:Sgip1 ^@ http://purl.uniprot.org/uniprot/Q3UGH4|||http://purl.uniprot.org/uniprot/Q8VD37 ^@ 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, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 6 and isoform 7.|||In isoform 5.|||In isoform 6.|||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_0000248396|||http://purl.uniprot.org/annotation/VSP_020279|||http://purl.uniprot.org/annotation/VSP_020280|||http://purl.uniprot.org/annotation/VSP_020281|||http://purl.uniprot.org/annotation/VSP_020282|||http://purl.uniprot.org/annotation/VSP_020283|||http://purl.uniprot.org/annotation/VSP_020284|||http://purl.uniprot.org/annotation/VSP_020285|||http://purl.uniprot.org/annotation/VSP_043987 http://togogenome.org/gene/10090:P2ry10 ^@ http://purl.uniprot.org/uniprot/Q8BFU7 ^@ 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|||Putative P2Y purinoceptor 10 ^@ http://purl.uniprot.org/annotation/PRO_0000303885 http://togogenome.org/gene/10090:Memo1 ^@ http://purl.uniprot.org/uniprot/Q91VH6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Phosphotyrosine|||Protein MEMO1 ^@ http://purl.uniprot.org/annotation/PRO_0000134395 http://togogenome.org/gene/10090:Slc6a2 ^@ http://purl.uniprot.org/uniprot/O55192|||http://purl.uniprot.org/uniprot/Q8R2I2 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||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-dependent noradrenaline transporter ^@ http://purl.uniprot.org/annotation/PRO_0000214749 http://togogenome.org/gene/10090:Ugt2b34 ^@ http://purl.uniprot.org/uniprot/Q8K154 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||UDP-glucuronosyltransferase ^@ http://purl.uniprot.org/annotation/PRO_5015020123 http://togogenome.org/gene/10090:Defa32 ^@ http://purl.uniprot.org/uniprot/Q45VN2 ^@ Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Alpha-defensin 20|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000300066|||http://purl.uniprot.org/annotation/PRO_0000300067 http://togogenome.org/gene/10090:Alg10b ^@ http://purl.uniprot.org/uniprot/Q3UGP8 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase|||Significant hearing impairment, associated with loss or degeneration of cochlear outer hair cells. ^@ http://purl.uniprot.org/annotation/PRO_0000320064 http://togogenome.org/gene/10090:Ppih ^@ http://purl.uniprot.org/uniprot/Q3UWH9|||http://purl.uniprot.org/uniprot/Q4G0C5|||http://purl.uniprot.org/uniprot/Q9D868 ^@ 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|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase H|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000064163|||http://purl.uniprot.org/annotation/VSP_008325 http://togogenome.org/gene/10090:Lbx1 ^@ http://purl.uniprot.org/uniprot/P52955 ^@ 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_0000049167 http://togogenome.org/gene/10090:Jsrp1 ^@ http://purl.uniprot.org/uniprot/M0QW57 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Gp6 ^@ http://purl.uniprot.org/uniprot/P0C191 ^@ 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|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Platelet glycoprotein VI ^@ http://purl.uniprot.org/annotation/PRO_0000232384 http://togogenome.org/gene/10090:Or5p81 ^@ http://purl.uniprot.org/uniprot/Q8VEW6 ^@ 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 5P81 ^@ http://purl.uniprot.org/annotation/PRO_0000150856 http://togogenome.org/gene/10090:Dlx1 ^@ http://purl.uniprot.org/uniprot/Q64317 ^@ 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 DLX-1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049021 http://togogenome.org/gene/10090:Eri2 ^@ http://purl.uniprot.org/uniprot/Q5BKS4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||ERI1 exoribonuclease 2|||Exonuclease|||GRF-type|||Polar residues|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000338974 http://togogenome.org/gene/10090:Gabrg3 ^@ http://purl.uniprot.org/uniprot/P27681 ^@ 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|||Gamma-aminobutyric acid receptor subunit gamma-3|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000000482 http://togogenome.org/gene/10090:Lgr5 ^@ http://purl.uniprot.org/uniprot/Q9Z1P4 ^@ 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|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||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_0000012795 http://togogenome.org/gene/10090:Tent5c ^@ http://purl.uniprot.org/uniprot/Q5SSF7 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn ^@ Does not affect polynucleotide adenylyltransferase activity. Increases cell apoptosis.|||Increases polynucleotide adenylyltransferase activity.|||Loss of polynucleotide adenylyltransferase activity.|||Significantly increases polynucleotide adenylyltransferase activity.|||Significantly reduces polynucleotide adenylyltransferase activity.|||Terminal nucleotidyltransferase 5C ^@ http://purl.uniprot.org/annotation/PRO_0000259935 http://togogenome.org/gene/10090:Defb13 ^@ http://purl.uniprot.org/uniprot/Q8R2I4 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 13 ^@ http://purl.uniprot.org/annotation/PRO_0000006941 http://togogenome.org/gene/10090:Calcr ^@ http://purl.uniprot.org/uniprot/Q60755 ^@ 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|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000012807|||http://purl.uniprot.org/annotation/VSP_053294 http://togogenome.org/gene/10090:Neurl1b ^@ http://purl.uniprot.org/uniprot/Q0MW30 ^@ 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|||E3 ubiquitin-protein ligase NEURL1B|||NHR 1|||NHR 2|||Phosphothreonine|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000349383 http://togogenome.org/gene/10090:Vmn2r14 ^@ http://purl.uniprot.org/uniprot/E9Q759 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5040102365 http://togogenome.org/gene/10090:Msh2 ^@ http://purl.uniprot.org/uniprot/P43247|||http://purl.uniprot.org/uniprot/Q3TZI5 ^@ 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|||Region|||Sequence Conflict ^@ DNA mismatch repair protein Msh2|||DNA mismatch repair proteins mutS family|||Interaction with EXO1|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000115184 http://togogenome.org/gene/10090:Ror2 ^@ http://purl.uniprot.org/uniprot/Q8C3W2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Acidic residues|||Disordered|||FZ|||Helical|||Ig-like|||Kringle|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_5014312029 http://togogenome.org/gene/10090:Cldn10 ^@ http://purl.uniprot.org/uniprot/Q9Z0S6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Claudin-10|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3, isoform 5 and isoform 6.|||In isoform 4 and isoform 5. ^@ http://purl.uniprot.org/annotation/PRO_0000144758|||http://purl.uniprot.org/annotation/VSP_053551|||http://purl.uniprot.org/annotation/VSP_053552|||http://purl.uniprot.org/annotation/VSP_053553 http://togogenome.org/gene/10090:4930544D05Rik ^@ http://purl.uniprot.org/uniprot/J3QK56 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ttc38 ^@ http://purl.uniprot.org/uniprot/A3KMP2 ^@ 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 38 ^@ http://purl.uniprot.org/annotation/PRO_0000321531|||http://purl.uniprot.org/annotation/VSP_031791 http://togogenome.org/gene/10090:Abca1 ^@ http://purl.uniprot.org/uniprot/P41233|||http://purl.uniprot.org/uniprot/Q8BPY1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ABC transporter|||ABC transporter 1|||ABC transporter 2|||Annulus domain 1|||Annulus domain 2|||Basic and acidic residues|||Disordered|||Extracellular|||Gateway domain|||Helical|||N-linked (GlcNAc...) asparagine|||Phospholipid-transporting ATPase ABCA1|||Phosphoserine|||Phosphoserine; by PKA|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000093289 http://togogenome.org/gene/10090:Selenot ^@ http://purl.uniprot.org/uniprot/P62342 ^@ Chain|||Crosslink|||Modification|||Molecule Processing|||Non standard residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Crosslink|||Non standard residue|||Signal Peptide|||Transmembrane ^@ Cysteinyl-selenocysteine (Cys-Sec)|||Helical|||Selenocysteine|||Thioredoxin reductase-like selenoprotein T ^@ http://purl.uniprot.org/annotation/PRO_0000032291 http://togogenome.org/gene/10090:Slc26a3 ^@ http://purl.uniprot.org/uniprot/Q9WVC8 ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Topological Domain|||Transmembrane ^@ Chloride anion exchanger|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||STAS ^@ http://purl.uniprot.org/annotation/PRO_0000080162 http://togogenome.org/gene/10090:Igsf11 ^@ http://purl.uniprot.org/uniprot/D3Z6S7|||http://purl.uniprot.org/uniprot/P0C673 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||Immunoglobulin superfamily member 11|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000317371 http://togogenome.org/gene/10090:Areg ^@ http://purl.uniprot.org/uniprot/P31955|||http://purl.uniprot.org/uniprot/Q4FJT2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Transmembrane ^@ Amphiregulin|||Basic and acidic residues|||Basic residues|||Disordered|||EGF-like|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000007476|||http://purl.uniprot.org/annotation/PRO_0000007477|||http://purl.uniprot.org/annotation/PRO_5014309361 http://togogenome.org/gene/10090:Ppp2r1a ^@ http://purl.uniprot.org/uniprot/Q76MZ3 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Strand|||Turn ^@ 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|||N-acetylalanine|||N6-acetyllysine|||Removed|||Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform ^@ http://purl.uniprot.org/annotation/PRO_0000071401 http://togogenome.org/gene/10090:Egr1 ^@ http://purl.uniprot.org/uniprot/P08046|||http://purl.uniprot.org/uniprot/Q544D6|||http://purl.uniprot.org/uniprot/Q8CAT6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Region|||Sequence Conflict|||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_0000047110 http://togogenome.org/gene/10090:Apool ^@ http://purl.uniprot.org/uniprot/B1AV14|||http://purl.uniprot.org/uniprot/Q78IK4 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000042054 http://togogenome.org/gene/10090:Wdr38 ^@ http://purl.uniprot.org/uniprot/Q9D994 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ 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_0000294441 http://togogenome.org/gene/10090:Fkbp10 ^@ http://purl.uniprot.org/uniprot/Q3UNJ3|||http://purl.uniprot.org/uniprot/Q61576 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 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_0000025518|||http://purl.uniprot.org/annotation/PRO_5004230236 http://togogenome.org/gene/10090:Cyp4f39 ^@ http://purl.uniprot.org/uniprot/Q8BGU0 ^@ Binding Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Podxl2 ^@ http://purl.uniprot.org/uniprot/D3YW47|||http://purl.uniprot.org/uniprot/G3X9D3|||http://purl.uniprot.org/uniprot/Q8CAE9 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Podocalyxin-like protein 2|||Polar residues|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000252130|||http://purl.uniprot.org/annotation/PRO_5005908492|||http://purl.uniprot.org/annotation/VSP_020877|||http://purl.uniprot.org/annotation/VSP_020878|||http://purl.uniprot.org/annotation/VSP_020879 http://togogenome.org/gene/10090:Ppp2r1b ^@ http://purl.uniprot.org/uniprot/G3UWS4|||http://purl.uniprot.org/uniprot/Q3TTF6|||http://purl.uniprot.org/uniprot/Q7TNP2|||http://purl.uniprot.org/uniprot/Q8BIX1 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||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|||N-acetylalanine|||Removed|||Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform ^@ http://purl.uniprot.org/annotation/PRO_0000071404 http://togogenome.org/gene/10090:Klb ^@ http://purl.uniprot.org/uniprot/Q99N32 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Beta-klotho|||Cytoplasmic|||Extracellular|||Glycosyl hydrolase-1 1|||Glycosyl hydrolase-1 2|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000063906|||http://purl.uniprot.org/annotation/VSP_015830|||http://purl.uniprot.org/annotation/VSP_015831 http://togogenome.org/gene/10090:Or5ap2 ^@ http://purl.uniprot.org/uniprot/Q8VFK7 ^@ 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 5AP2 ^@ http://purl.uniprot.org/annotation/PRO_0000150861 http://togogenome.org/gene/10090:Or6c210 ^@ http://purl.uniprot.org/uniprot/Q8VFH7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Eno1 ^@ http://purl.uniprot.org/uniprot/P17182|||http://purl.uniprot.org/uniprot/Q5FW97 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Alpha-enolase|||Enolase C-terminal TIM barrel|||Enolase N-terminal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000134098 http://togogenome.org/gene/10090:Nfkbia ^@ http://purl.uniprot.org/uniprot/Q9Z1E3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ (3S)-3-hydroxyasparagine; by HIF1AN|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||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|||NF-kappa-B inhibitor alpha|||Nuclear export signal|||Nuclear import signal|||Phosphoserine; by CK2|||Phosphoserine; by IKKA, IKKB, IKKE and TBK1|||Phosphoserine; by IKKB|||Phosphothreonine|||Phosphothreonine; by CK2|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000067000 http://togogenome.org/gene/10090:Btbd35f15 ^@ http://purl.uniprot.org/uniprot/A0A087WR44 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Rbm11 ^@ http://purl.uniprot.org/uniprot/Q80YT9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||RRM|||Splicing regulator RBM11 ^@ http://purl.uniprot.org/annotation/PRO_0000416116 http://togogenome.org/gene/10090:Tnp2 ^@ http://purl.uniprot.org/uniprot/P11378 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic residues|||Disordered|||Nuclear localization signal|||Nuclear transition protein 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000191428 http://togogenome.org/gene/10090:Pak4 ^@ http://purl.uniprot.org/uniprot/Q8BTW9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||CRIB|||Disordered|||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_0000086475 http://togogenome.org/gene/10090:Ak7 ^@ http://purl.uniprot.org/uniprot/F8WIC0|||http://purl.uniprot.org/uniprot/Q9D2H2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant ^@ Acidic residues|||Adenylate kinase|||Adenylate kinase 7|||DPY-30|||Disordered|||In isoform 2.|||LID|||NMP ^@ http://purl.uniprot.org/annotation/PRO_0000158954|||http://purl.uniprot.org/annotation/VSP_008474|||http://purl.uniprot.org/annotation/VSP_008475|||http://purl.uniprot.org/annotation/VSP_008476 http://togogenome.org/gene/10090:Pcdha4 ^@ http://purl.uniprot.org/uniprot/O88689 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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|||O-linked (Man) serine|||O-linked (Man) threonine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||PXXP 6|||Protocadherin alpha-4|||Required for interaction with FYN ^@ http://purl.uniprot.org/annotation/PRO_0000240663|||http://purl.uniprot.org/annotation/VSP_019413|||http://purl.uniprot.org/annotation/VSP_019414|||http://purl.uniprot.org/annotation/VSP_019415 http://togogenome.org/gene/10090:Omt2b ^@ http://purl.uniprot.org/uniprot/D3YX29 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Mtif3 ^@ http://purl.uniprot.org/uniprot/A4QMQ0|||http://purl.uniprot.org/uniprot/Q9CZD5 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Chain|||Domain Extent|||Helix|||Propeptide|||Region|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Disordered|||Mitochondrion|||Removed in mature form|||Translation initiation factor 3 C-terminal|||Translation initiation factor 3 N-terminal|||Translation initiation factor IF-3, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000280038|||http://purl.uniprot.org/annotation/PRO_0000280039 http://togogenome.org/gene/10090:Zfp775 ^@ http://purl.uniprot.org/uniprot/Q8BI73 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||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|||Polar residues|||Zinc finger protein 775 ^@ http://purl.uniprot.org/annotation/PRO_0000280442 http://togogenome.org/gene/10090:Ankrd13d ^@ http://purl.uniprot.org/uniprot/Q6PD24 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Ankyrin repeat domain-containing protein 13D|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||UIM 1|||UIM 2|||UIM 3|||UIM 4 ^@ http://purl.uniprot.org/annotation/PRO_0000240652 http://togogenome.org/gene/10090:Or11g27 ^@ http://purl.uniprot.org/uniprot/L7N1Y2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp146 ^@ http://purl.uniprot.org/uniprot/Q8BQN6 ^@ Chain|||Crosslink|||Modification|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Crosslink|||Region|||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)|||Interaction with TERF2IP|||Zinc finger protein OZF ^@ http://purl.uniprot.org/annotation/PRO_0000047277 http://togogenome.org/gene/10090:St8sia2 ^@ http://purl.uniprot.org/uniprot/O35696 ^@ 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|||Sequence Conflict|||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_0000149286 http://togogenome.org/gene/10090:Chil1 ^@ http://purl.uniprot.org/uniprot/Q61362 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Chitinase-3-like protein 1|||GH18|||Important for AKT1 activation and IL8 production|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||No effect on chiting-binding. No restoration of chitinase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000011966|||http://purl.uniprot.org/annotation/VSP_054523|||http://purl.uniprot.org/annotation/VSP_054524 http://togogenome.org/gene/10090:Uqcc6 ^@ http://purl.uniprot.org/uniprot/Q8BTC1 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||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_0000340274 http://togogenome.org/gene/10090:Bmp5 ^@ http://purl.uniprot.org/uniprot/P49003|||http://purl.uniprot.org/uniprot/Q3UXE6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||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_0000033868|||http://purl.uniprot.org/annotation/PRO_0000033869|||http://purl.uniprot.org/annotation/VSP_044321 http://togogenome.org/gene/10090:1700016H13Rik ^@ http://purl.uniprot.org/uniprot/Q9DAA3 ^@ Chain|||Molecule Processing ^@ Chain ^@ Uncharacterized protein C4orf36 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000268821 http://togogenome.org/gene/10090:Sv2a ^@ http://purl.uniprot.org/uniprot/Q9JIS5 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with SYT1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Synaptic vesicle glycoprotein 2A ^@ http://purl.uniprot.org/annotation/PRO_0000239766 http://togogenome.org/gene/10090:Hoxb7 ^@ http://purl.uniprot.org/uniprot/P09024 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Motif|||Region|||Sequence Conflict ^@ Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-B7 ^@ http://purl.uniprot.org/annotation/PRO_0000200143 http://togogenome.org/gene/10090:Il7r ^@ http://purl.uniprot.org/uniprot/P16872|||http://purl.uniprot.org/uniprot/Q5FW78|||http://purl.uniprot.org/uniprot/Q8C9W4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Interleukin-7 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Phosphothreonine; by PKC|||Polar residues|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010910|||http://purl.uniprot.org/annotation/PRO_5004255941|||http://purl.uniprot.org/annotation/PRO_5004307369 http://togogenome.org/gene/10090:Dhrs1 ^@ http://purl.uniprot.org/uniprot/Q99L04 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Dehydrogenase/reductase SDR family member 1|||Omega-N-methylarginine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054641 http://togogenome.org/gene/10090:Gng7 ^@ http://purl.uniprot.org/uniprot/Q3UGN1|||http://purl.uniprot.org/uniprot/Q61016 ^@ Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide ^@ Cysteine methyl ester|||G protein gamma|||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_0000012637|||http://purl.uniprot.org/annotation/PRO_0000012638 http://togogenome.org/gene/10090:Septin4 ^@ http://purl.uniprot.org/uniprot/A0A5F8MP96|||http://purl.uniprot.org/uniprot/P28661 ^@ 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 ^@ Basic and acidic residues|||Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Septin-4|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173520|||http://purl.uniprot.org/annotation/VSP_038307|||http://purl.uniprot.org/annotation/VSP_038308|||http://purl.uniprot.org/annotation/VSP_038309|||http://purl.uniprot.org/annotation/VSP_038310|||http://purl.uniprot.org/annotation/VSP_038311|||http://purl.uniprot.org/annotation/VSP_038312|||http://purl.uniprot.org/annotation/VSP_038313|||http://purl.uniprot.org/annotation/VSP_038314|||http://purl.uniprot.org/annotation/VSP_061408 http://togogenome.org/gene/10090:Rnase4 ^@ http://purl.uniprot.org/uniprot/Q8C7E4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_5015020118 http://togogenome.org/gene/10090:Daxx ^@ http://purl.uniprot.org/uniprot/O35613|||http://purl.uniprot.org/uniprot/Q3UKR0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Daxx N-terminal Rassf1C-interacting|||Death domain-associated protein 6|||Diminishes phosphorylation by HIPK1.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with SPOP|||Interaction with histone H3.3|||Necessary for interaction with USP7|||Necessary for interaction with USP7 and ATRX|||No effect on phosphorylation by HIPK1.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by HIPK1|||Phosphothreonine|||Polar residues|||Sumo interaction motif (SIM) ^@ http://purl.uniprot.org/annotation/PRO_0000151259 http://togogenome.org/gene/10090:H3c10 ^@ http://purl.uniprot.org/uniprot/P68433 ^@ Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||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|||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; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoarginine|||Phosphoarginine; 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|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000221249 http://togogenome.org/gene/10090:Itgav ^@ http://purl.uniprot.org/uniprot/P43406 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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-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_0000016304|||http://purl.uniprot.org/annotation/PRO_0000016305|||http://purl.uniprot.org/annotation/PRO_0000016306 http://togogenome.org/gene/10090:Or9i1 ^@ http://purl.uniprot.org/uniprot/Q8VG66 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rnf17 ^@ http://purl.uniprot.org/uniprot/Q99MV7 ^@ 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|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||RING finger protein 17|||RING-type|||Tudor 1|||Tudor 2|||Tudor 3|||Tudor 4 ^@ http://purl.uniprot.org/annotation/PRO_0000056060|||http://purl.uniprot.org/annotation/VSP_033077|||http://purl.uniprot.org/annotation/VSP_033078|||http://purl.uniprot.org/annotation/VSP_033079|||http://purl.uniprot.org/annotation/VSP_033080|||http://purl.uniprot.org/annotation/VSP_033081 http://togogenome.org/gene/10090:Cavin4 ^@ http://purl.uniprot.org/uniprot/A2AMM0 ^@ 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_0000325764 http://togogenome.org/gene/10090:Sos2 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ87|||http://purl.uniprot.org/uniprot/Q02384 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||DH|||Disordered|||N-terminal Ras-GEF|||PH|||Polar residues|||Pro residues|||Ras-GEF|||Son of sevenless homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000068897 http://togogenome.org/gene/10090:Prr12 ^@ http://purl.uniprot.org/uniprot/E9PYL2|||http://purl.uniprot.org/uniprot/Q6PDJ2 ^@ 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 ^@ Basic and acidic residues|||DUF4211|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proline-rich protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000435433 http://togogenome.org/gene/10090:Coasy ^@ http://purl.uniprot.org/uniprot/Q9DBL7 ^@ 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|||Region|||Strand|||Turn ^@ Bifunctional coenzyme A synthase|||DPCK|||N6-succinyllysine|||Phosphopantetheine adenylyltransferase|||Phosphopantetheine adenylyltransferase activity abolished.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000173040 http://togogenome.org/gene/10090:Vmn1r95 ^@ http://purl.uniprot.org/uniprot/E9PUW9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sirt4 ^@ http://purl.uniprot.org/uniprot/Q8R216 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide ^@ Deacetylase sirtuin-type|||Mitochondrion|||NAD-dependent protein lipoamidase sirtuin-4, mitochondrial|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000110265 http://togogenome.org/gene/10090:Syde1 ^@ http://purl.uniprot.org/uniprot/G3X960 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||C2|||Disordered|||Polar residues|||Rho-GAP ^@ http://togogenome.org/gene/10090:Pom121l2 ^@ http://purl.uniprot.org/uniprot/Q3V0N0|||http://purl.uniprot.org/uniprot/Q5SW25 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||POM121-like protein 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000292040 http://togogenome.org/gene/10090:Fam124a ^@ http://purl.uniprot.org/uniprot/D3Z5V4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||FAM124|||Polar residues ^@ http://togogenome.org/gene/10090:Fastk ^@ http://purl.uniprot.org/uniprot/Q8C725|||http://purl.uniprot.org/uniprot/Q91WQ6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||RAP ^@ http://togogenome.org/gene/10090:Mboat2 ^@ http://purl.uniprot.org/uniprot/Q8BN01|||http://purl.uniprot.org/uniprot/Q8R3I2 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Chain|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Lysophospholipid acyltransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000273021|||http://purl.uniprot.org/annotation/VSP_022457|||http://purl.uniprot.org/annotation/VSP_022458|||http://purl.uniprot.org/annotation/VSP_022459 http://togogenome.org/gene/10090:Gm16451 ^@ http://purl.uniprot.org/uniprot/D3YZG3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or5k1 ^@ http://purl.uniprot.org/uniprot/E9QAT7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ppp1r1a ^@ http://purl.uniprot.org/uniprot/Q9ERT9 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Essential for activity|||Interaction with PPP1R15A|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein phosphatase 1 regulatory subunit 1A ^@ http://purl.uniprot.org/annotation/PRO_0000071478 http://togogenome.org/gene/10090:Rbpms ^@ http://purl.uniprot.org/uniprot/Q8C586|||http://purl.uniprot.org/uniprot/Q9WVB0|||http://purl.uniprot.org/uniprot/T1ECW4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Interaction with RNA|||N-acetylmethionine|||Phosphothreonine|||RNA-binding protein with multiple splicing|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081794|||http://purl.uniprot.org/annotation/VSP_045747 http://togogenome.org/gene/10090:Ncoa3 ^@ http://purl.uniprot.org/uniprot/A5D6Q2|||http://purl.uniprot.org/uniprot/Q05BA5 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ BHLH|||Basic and acidic residues|||Disordered|||PAS|||Polar residues ^@ http://togogenome.org/gene/10090:Amer1 ^@ http://purl.uniprot.org/uniprot/Q7TS75 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ APC membrane recruitment protein 1|||Acidic residues|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000281888 http://togogenome.org/gene/10090:Vmn1r26 ^@ http://purl.uniprot.org/uniprot/Q8R2D7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp821 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLE5|||http://purl.uniprot.org/uniprot/Q6PD05 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||Disordered|||Polar residues|||Zinc finger protein 821 ^@ http://purl.uniprot.org/annotation/PRO_0000317290 http://togogenome.org/gene/10090:Dmp1 ^@ http://purl.uniprot.org/uniprot/O55188 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Cell attachment site|||Dentin matrix acidic phosphoprotein 1|||Disordered|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000021111 http://togogenome.org/gene/10090:Foxi2 ^@ http://purl.uniprot.org/uniprot/A2RTG9|||http://purl.uniprot.org/uniprot/Q3I5G5 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Fork-head|||Forkhead box protein I2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000091848 http://togogenome.org/gene/10090:Taar7b ^@ http://purl.uniprot.org/uniprot/Q5QD11 ^@ 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|||Trace amine-associated receptor 7b ^@ http://purl.uniprot.org/annotation/PRO_0000070164 http://togogenome.org/gene/10090:Arvcf ^@ http://purl.uniprot.org/uniprot/P98203 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||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 2 and isoform 4.|||In isoform 4 and isoform 5.|||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_0000064295|||http://purl.uniprot.org/annotation/VSP_014922|||http://purl.uniprot.org/annotation/VSP_014923 http://togogenome.org/gene/10090:Mcm9 ^@ http://purl.uniprot.org/uniprot/Q2KHI9 ^@ 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 ^@ Basic and acidic residues|||DNA helicase MCM9|||Disordered|||In isoform 2.|||In isoform 3.|||MCM|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000304144|||http://purl.uniprot.org/annotation/VSP_028015|||http://purl.uniprot.org/annotation/VSP_028016|||http://purl.uniprot.org/annotation/VSP_028017 http://togogenome.org/gene/10090:Ndufb8 ^@ http://purl.uniprot.org/uniprot/Q3V406|||http://purl.uniprot.org/uniprot/Q9D6J5 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Transmembrane|||Turn ^@ Chain|||Helix|||Sequence Conflict|||Strand|||Transit Peptide|||Transmembrane|||Turn ^@ Helical|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000020047 http://togogenome.org/gene/10090:Cntn4 ^@ http://purl.uniprot.org/uniprot/Q69Z26 ^@ 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|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ 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 isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000014713|||http://purl.uniprot.org/annotation/PRO_0000014714|||http://purl.uniprot.org/annotation/VSP_011963|||http://purl.uniprot.org/annotation/VSP_011964|||http://purl.uniprot.org/annotation/VSP_011965|||http://purl.uniprot.org/annotation/VSP_011966 http://togogenome.org/gene/10090:Six2 ^@ http://purl.uniprot.org/uniprot/Q62232 ^@ 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 SIX2|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000049298 http://togogenome.org/gene/10090:Hinfp ^@ http://purl.uniprot.org/uniprot/Q8K1K9 ^@ 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; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Histone H4 transcription factor|||Interaction with NPAT|||Required for activation of histone H4 transcription and contributes to DNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000047219 http://togogenome.org/gene/10090:Fam32a ^@ http://purl.uniprot.org/uniprot/Q9CR80 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Protein FAM32A ^@ http://purl.uniprot.org/annotation/PRO_0000223251 http://togogenome.org/gene/10090:Kbtbd6 ^@ http://purl.uniprot.org/uniprot/A0A2I3BQ98|||http://purl.uniprot.org/uniprot/Q3TWH9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BTB|||Disordered ^@ http://togogenome.org/gene/10090:Fam151b ^@ http://purl.uniprot.org/uniprot/D3YUE4 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein FAM151B ^@ http://purl.uniprot.org/annotation/PRO_0000458941 http://togogenome.org/gene/10090:Cbx5 ^@ http://purl.uniprot.org/uniprot/Q61686 ^@ 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 ^@ Chromo 1|||Chromo 2; shadow subtype|||Chromobox protein homolog 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000080209 http://togogenome.org/gene/10090:2310061I04Rik ^@ http://purl.uniprot.org/uniprot/B8JJ69 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Or8b38 ^@ http://purl.uniprot.org/uniprot/Q7TRE0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rhox4e ^@ http://purl.uniprot.org/uniprot/Q504P9 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Tmem212 ^@ http://purl.uniprot.org/uniprot/Q8C6V3 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 212 ^@ http://purl.uniprot.org/annotation/PRO_0000341208 http://togogenome.org/gene/10090:Lyrm7 ^@ http://purl.uniprot.org/uniprot/Q9DA03 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Complex III assembly factor LYRM7|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000251180 http://togogenome.org/gene/10090:Il17f ^@ http://purl.uniprot.org/uniprot/Q7TNI7 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Interchain (with C-135)|||Interchain (with C-45)|||Interleukin-17F|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000378104|||http://purl.uniprot.org/annotation/VSP_037499 http://togogenome.org/gene/10090:Safb ^@ http://purl.uniprot.org/uniprot/D3YXK2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ 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|||Interaction with POLR2A; SFRS1; SFRS9 and SFRS10|||Interaction with SAFB2|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||Removed|||SAP|||Scaffold attachment factor B1 ^@ http://purl.uniprot.org/annotation/PRO_0000413022 http://togogenome.org/gene/10090:Ano8 ^@ http://purl.uniprot.org/uniprot/Q6PB70 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Acidic residues|||Anoctamin-8|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000249004 http://togogenome.org/gene/10090:St3gal5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1J3|||http://purl.uniprot.org/uniprot/O88829 ^@ 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|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lactosylceramide alpha-2,3-sialyltransferase|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149303|||http://purl.uniprot.org/annotation/VSP_033689 http://togogenome.org/gene/10090:Foxl2 ^@ http://purl.uniprot.org/uniprot/O88470|||http://purl.uniprot.org/uniprot/Q2TVT7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Fork-head|||Forkhead box protein L2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000091862 http://togogenome.org/gene/10090:Slc30a8 ^@ http://purl.uniprot.org/uniprot/Q8BGG0 ^@ Binding Site|||Chain|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Motif|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||HCH Motif; seals regulatory zinc-binding pocket|||Helical|||Lumenal, vesicle|||Proton-coupled zinc antiporter SLC30A8|||in chain A|||in chain B ^@ http://purl.uniprot.org/annotation/PRO_0000281741 http://togogenome.org/gene/10090:Ctag2l2 ^@ http://purl.uniprot.org/uniprot/A2BG94 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Nr3c2 ^@ http://purl.uniprot.org/uniprot/A3KN90 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||NR LBD|||Nuclear receptor|||Pro residues ^@ http://togogenome.org/gene/10090:Tnfrsf10b ^@ http://purl.uniprot.org/uniprot/Q9QZM4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ (Microbial infection) N-beta-linked (GlcNAc) arginine|||Cytoplasmic|||Death|||Disordered|||Extracellular|||Helical|||Polar residues|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 10B ^@ http://purl.uniprot.org/annotation/PRO_0000034581 http://togogenome.org/gene/10090:H1f2 ^@ http://purl.uniprot.org/uniprot/P15864|||http://purl.uniprot.org/uniprot/Q5SZA3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region ^@ ADP-ribosylserine|||Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.2|||Mimics the charge change that accompanies citrullination, resulting in impaired nucleosome-binding.|||N-acetylserine|||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|||Retains the positive charge, resulting in slightly decreased nucleosome-binding. ^@ http://purl.uniprot.org/annotation/PRO_0000195915 http://togogenome.org/gene/10090:Gm3696 ^@ http://purl.uniprot.org/uniprot/K7N751 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Bbln ^@ http://purl.uniprot.org/uniprot/P58686 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Region ^@ Bublin coiled-coil protein|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000195162 http://togogenome.org/gene/10090:Slamf7 ^@ http://purl.uniprot.org/uniprot/A0A0A6YW73|||http://purl.uniprot.org/uniprot/A0A0R4J2D6|||http://purl.uniprot.org/uniprot/A0A0R4J2D8|||http://purl.uniprot.org/uniprot/Q8BHK6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disrupts interaction with SH2D1B, abolishes NK cell activation in presence of SH2D1B, no effect on NK cell inhibition in absence of SH2D1B.|||Extracellular|||Helical|||ITSM|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Interaction with FYN when phosphorylated at Tyr-282|||N-linked (GlcNAc...) asparagine|||No effect on interaction with SH2D1, no effect on NK cell activation in presence of SH2D1B, no effect on NK cell inhibition in absence of SH2D1B.|||No effect on interaction with SH2D1B, increases NK cell activation in presence of SH2D1B, abolishes NK cell inhibition in absence of SH2D1B.|||Phosphotyrosine|||SLAM family member 7 ^@ http://purl.uniprot.org/annotation/PRO_0000014964|||http://purl.uniprot.org/annotation/PRO_5006452032|||http://purl.uniprot.org/annotation/PRO_5015032929|||http://purl.uniprot.org/annotation/PRO_5015044309|||http://purl.uniprot.org/annotation/VSP_013783|||http://purl.uniprot.org/annotation/VSP_013784 http://togogenome.org/gene/10090:Gucy2g ^@ http://purl.uniprot.org/uniprot/Q6TL19 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Does not affect guanylate cyclase activity; when associated with S-458.|||Does not affect guanylate cyclase activity; when associated with S-465.|||Extracellular|||Guanylate cyclase|||Guanylate cyclase 2G|||Helical|||N-linked (GlcNAc...) asparagine|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000042178 http://togogenome.org/gene/10090:Pcnx4 ^@ http://purl.uniprot.org/uniprot/E9QN69|||http://purl.uniprot.org/uniprot/Q3UVY5 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Pecanex C-terminal|||Pecanex-like protein 4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000339367|||http://purl.uniprot.org/annotation/VSP_034161 http://togogenome.org/gene/10090:Mael ^@ http://purl.uniprot.org/uniprot/Q8BVN9 ^@ Chain|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||DNA Binding ^@ HMG box|||Protein maelstrom homolog ^@ http://purl.uniprot.org/annotation/PRO_0000232503 http://togogenome.org/gene/10090:Eola1 ^@ http://purl.uniprot.org/uniprot/Q9D1F3 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Turn ^@ ASCH|||Protein EOLA1 ^@ http://purl.uniprot.org/annotation/PRO_0000079734 http://togogenome.org/gene/10090:Rnf144a ^@ http://purl.uniprot.org/uniprot/Q925F3 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Region|||Transmembrane|||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_0000056299 http://togogenome.org/gene/10090:Xpr1 ^@ http://purl.uniprot.org/uniprot/Q9Z0U0 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||EXS|||Extracellular|||Gives susceptibility to xenotropic murine leukemia retroviruses infection.|||Helical|||Important for inositol polyphosphate binding|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||SPX|||Solute carrier family 53 member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000315854|||http://purl.uniprot.org/annotation/VSP_030749 http://togogenome.org/gene/10090:Or12e1 ^@ http://purl.uniprot.org/uniprot/A2ATA0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cndp1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0V0|||http://purl.uniprot.org/uniprot/Q3TSF8|||http://purl.uniprot.org/uniprot/Q8BUG2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Site ^@ Beta-Ala-His dipeptidase|||Important for catalytic activity|||Peptidase M20 dimerisation|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000250530 http://togogenome.org/gene/10090:Dzip1 ^@ http://purl.uniprot.org/uniprot/Q8BMD2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type|||Changed cilium assembly. Adult animals develop myxomatous mitral valves and functional mitral valve prolapse.|||Cilium assembly protein DZIP1|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of interaction with PCM1.|||Loss of phosphorylation by GSK3-beta. Decreased interaction with GDI2.|||Loss of phosphorylation by PLK1. Increased interaction with PCM1.|||Mediates interaction with GDI2 and RAB8A|||Mediates interaction with GLI3 and localization to the cilium basal body|||Mediates interaction with PCM1|||Phosphorylation mimicking mutant. Increased interaction with GDI2.|||Phosphoserine; by GSK3-beta|||Phosphoserine; by PLK1|||Polar residues|||Required for interaction with DAZ1 ^@ http://purl.uniprot.org/annotation/PRO_0000047107|||http://purl.uniprot.org/annotation/VSP_010966|||http://purl.uniprot.org/annotation/VSP_010967|||http://purl.uniprot.org/annotation/VSP_010968|||http://purl.uniprot.org/annotation/VSP_010969 http://togogenome.org/gene/10090:Hebp1 ^@ http://purl.uniprot.org/uniprot/Q9R257 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Helix|||Sequence Conflict|||Strand ^@ Heme-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000116898 http://togogenome.org/gene/10090:Lgi4 ^@ http://purl.uniprot.org/uniprot/Q8K1S1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide ^@ EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||EAR 7|||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_0000017713 http://togogenome.org/gene/10090:Bach2 ^@ http://purl.uniprot.org/uniprot/P97303 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ BTB|||Basic and acidic residues|||Basic motif|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interchain; redox-active|||Leucine-zipper|||Nuclear export signal|||Phosphoserine|||Polar residues|||Transcription regulator protein BACH2|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076457|||http://purl.uniprot.org/annotation/VSP_047933 http://togogenome.org/gene/10090:Ndp ^@ http://purl.uniprot.org/uniprot/P48744 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ CTCK|||Interchain|||Interchain (with C-91)|||Interchain (with C-93)|||Norrin ^@ http://purl.uniprot.org/annotation/PRO_0000021796 http://togogenome.org/gene/10090:Taf9b ^@ http://purl.uniprot.org/uniprot/A2AP82|||http://purl.uniprot.org/uniprot/Q6NZA9 ^@ 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|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription initiation factor TFIID subunit 9B ^@ http://purl.uniprot.org/annotation/PRO_0000118892 http://togogenome.org/gene/10090:Fgf17 ^@ http://purl.uniprot.org/uniprot/P63075|||http://purl.uniprot.org/uniprot/Q0VF19 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||Fibroblast growth factor|||Fibroblast growth factor 17|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000008986|||http://purl.uniprot.org/annotation/PRO_5014205723 http://togogenome.org/gene/10090:Proca1 ^@ http://purl.uniprot.org/uniprot/B0QZF6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Mmp21 ^@ http://purl.uniprot.org/uniprot/Q3KP73|||http://purl.uniprot.org/uniprot/Q3KP74|||http://purl.uniprot.org/uniprot/Q8K3F2 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Repeat|||Signal Peptide ^@ Cysteine switch|||Embryos have congenital heart defects with transposition of the great artery, 61% exhibiting situs inversus or heterotaxy and 39% exhibiting situs solitus. This mutation corresponds to the pathological variant 'T-226' identified in humans.|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Koli mutant, animals exhibit visceral heterotaxy, with heart defects commonly associated with heterotaxy.|||Matrix metalloproteinase-21|||Miri mutant, animals exhibit visceral heterotaxy, with heart defects commonly associated with heterotaxy.|||N-linked (GlcNAc...) asparagine|||Peptidase metallopeptidase|||Phosphotyrosine; by PKDCC|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028841|||http://purl.uniprot.org/annotation/PRO_0000437089|||http://purl.uniprot.org/annotation/PRO_5014309084|||http://purl.uniprot.org/annotation/PRO_5015097411 http://togogenome.org/gene/10090:1700102P08Rik ^@ http://purl.uniprot.org/uniprot/Q9D9C7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Uncharacterized protein C3orf62 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000239306 http://togogenome.org/gene/10090:Or8g37 ^@ http://purl.uniprot.org/uniprot/Q8VFN3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pcsk2 ^@ http://purl.uniprot.org/uniprot/P21661|||http://purl.uniprot.org/uniprot/Q547J8 ^@ Active Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Signal Peptide ^@ Charge relay system|||N-linked (GlcNAc...) asparagine|||Neuroendocrine convertase 2|||P/Homo B|||Peptidase S8 ^@ http://purl.uniprot.org/annotation/PRO_0000027067|||http://purl.uniprot.org/annotation/PRO_0000027068|||http://purl.uniprot.org/annotation/PRO_5014309589 http://togogenome.org/gene/10090:Tmprss3 ^@ http://purl.uniprot.org/uniprot/Q3TZ06|||http://purl.uniprot.org/uniprot/Q8K1T0 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Charge relay system|||Cleavage|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||LDL-receptor class A|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SRCR|||Transmembrane protease serine 3 ^@ http://purl.uniprot.org/annotation/PRO_0000088691|||http://purl.uniprot.org/annotation/VSP_041581 http://togogenome.org/gene/10090:Traip ^@ http://purl.uniprot.org/uniprot/Q8VIG6 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ E3 ubiquitin-protein ligase TRAIP|||Fails to autoubiquitinate.|||In isoform 2.|||Interaction with CYLD|||PIP-box|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000056192|||http://purl.uniprot.org/annotation/VSP_007406|||http://purl.uniprot.org/annotation/VSP_007407 http://togogenome.org/gene/10090:Ccdc158 ^@ http://purl.uniprot.org/uniprot/Q8CDI6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant ^@ Coiled-coil domain-containing protein 158|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000325761|||http://purl.uniprot.org/annotation/VSP_032393|||http://purl.uniprot.org/annotation/VSP_032394 http://togogenome.org/gene/10090:Or11g1 ^@ http://purl.uniprot.org/uniprot/L7N1X7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rasl11a ^@ http://purl.uniprot.org/uniprot/Q6IMB1 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Region|||Splice Variant ^@ In isoform 2.|||Ras-like protein family member 11A|||Small GTPase-like ^@ http://purl.uniprot.org/annotation/PRO_0000308361|||http://purl.uniprot.org/annotation/VSP_052584 http://togogenome.org/gene/10090:Arrdc4 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1F4 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Motif|||Mutagenesis Site|||Splice Variant ^@ Arrestin domain-containing protein 4|||In isoform 2.|||Loss of localization to the cell membrane.|||PPxY motif 1|||PPxY motif 2 ^@ http://purl.uniprot.org/annotation/PRO_0000435031|||http://purl.uniprot.org/annotation/VSP_058000|||http://purl.uniprot.org/annotation/VSP_058001 http://togogenome.org/gene/10090:Rhox7a ^@ http://purl.uniprot.org/uniprot/A2A4F1 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Timm8b ^@ http://purl.uniprot.org/uniprot/P62077 ^@ Chain|||Disulfide Bond|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Initiator Methionine|||Modified Residue|||Motif ^@ Mitochondrial import inner membrane translocase subunit Tim8 B|||N-acetylalanine|||Removed|||Twin CX3C motif ^@ http://purl.uniprot.org/annotation/PRO_0000193588 http://togogenome.org/gene/10090:Igsf23 ^@ http://purl.uniprot.org/uniprot/B2RTN2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Ig-like|||Immunoglobulin superfamily member 23|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000457624 http://togogenome.org/gene/10090:Tgds ^@ http://purl.uniprot.org/uniprot/Q3TMF9|||http://purl.uniprot.org/uniprot/Q8VDR7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ NAD(P)-binding|||Proton acceptor|||Proton donor|||dTDP-D-glucose 4,6-dehydratase ^@ http://purl.uniprot.org/annotation/PRO_0000183251 http://togogenome.org/gene/10090:Zfp273 ^@ http://purl.uniprot.org/uniprot/Q7M6W8|||http://purl.uniprot.org/uniprot/Q8BIF3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ascl1 ^@ http://purl.uniprot.org/uniprot/Q02067 ^@ 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 ^@ Achaete-scute homolog 1|||Disordered|||N6-acetyllysine|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127127 http://togogenome.org/gene/10090:Slc7a15 ^@ http://purl.uniprot.org/uniprot/Q50E62|||http://purl.uniprot.org/uniprot/Q8BZV2|||http://purl.uniprot.org/uniprot/Q9D8H4 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Ces1d ^@ http://purl.uniprot.org/uniprot/Q8VCT4 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide ^@ Acyl-ester intermediate|||Carboxylesterase 1D|||Charge relay system|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000008583 http://togogenome.org/gene/10090:Acer2 ^@ http://purl.uniprot.org/uniprot/Q8VD53 ^@ 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 ^@ Alkaline ceramidase 2|||Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000247749|||http://purl.uniprot.org/annotation/VSP_020036 http://togogenome.org/gene/10090:Tmbim1 ^@ http://purl.uniprot.org/uniprot/Q3U717|||http://purl.uniprot.org/uniprot/Q8BJZ3 ^@ 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|||Pro residues|||Protein lifeguard 3 ^@ http://purl.uniprot.org/annotation/PRO_0000179091|||http://purl.uniprot.org/annotation/VSP_008995|||http://purl.uniprot.org/annotation/VSP_008996 http://togogenome.org/gene/10090:Pigv ^@ http://purl.uniprot.org/uniprot/Q7TPN3 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||GPI mannosyltransferase 2|||Helical|||In isoform 2.|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000246235|||http://purl.uniprot.org/annotation/VSP_019840 http://togogenome.org/gene/10090:Glrx5 ^@ http://purl.uniprot.org/uniprot/Q80Y14 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Glutaredoxin|||Glutaredoxin-related protein 5, mitochondrial|||Mitochondrion|||N6-succinyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000141651 http://togogenome.org/gene/10090:Or2b4 ^@ http://purl.uniprot.org/uniprot/Q8VGW6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or4c111 ^@ http://purl.uniprot.org/uniprot/Q7TR05 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Magea8 ^@ http://purl.uniprot.org/uniprot/O89012 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Grip2 ^@ http://purl.uniprot.org/uniprot/G3XA20 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PDZ|||Polar residues ^@ http://togogenome.org/gene/10090:Dpf1 ^@ http://purl.uniprot.org/uniprot/Q6GTK4|||http://purl.uniprot.org/uniprot/Q9QX66 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger ^@ C2H2-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||PHD-type|||PHD-type 1|||PHD-type 2|||Zinc finger protein neuro-d4 ^@ http://purl.uniprot.org/annotation/PRO_0000168146|||http://purl.uniprot.org/annotation/VSP_005608|||http://purl.uniprot.org/annotation/VSP_005609 http://togogenome.org/gene/10090:Pard3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Y4|||http://purl.uniprot.org/uniprot/A5D6P2|||http://purl.uniprot.org/uniprot/B7ZNY3|||http://purl.uniprot.org/uniprot/E9PYJ2|||http://purl.uniprot.org/uniprot/G3XA13|||http://purl.uniprot.org/uniprot/Q99NH2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||Inhibits Schwann cell peripheral myelination; when associated with A-831; A-848 and A-1327.|||Inhibits Schwann cell peripheral myelination; when associated with A-831; A-848 and A-881.|||Inhibits Schwann cell peripheral myelination; when associated with A-831; A-881 and A-1327.|||Inhibits Schwann cell peripheral myelination; when associated with A-848; A-881 and A-1327.|||Interaction with FRMD4A|||Interaction with PRKCI and PRKCZ|||N6-acetyllysine|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Partitioning defective 3 homolog|||Phosphoserine|||Phosphoserine; by AURKA|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Strongly reduces phosphorylation by PRKCZ and abolishes interaction with PKRCI. ^@ http://purl.uniprot.org/annotation/PRO_0000185070|||http://purl.uniprot.org/annotation/VSP_007472|||http://purl.uniprot.org/annotation/VSP_007473|||http://purl.uniprot.org/annotation/VSP_007474|||http://purl.uniprot.org/annotation/VSP_035895|||http://purl.uniprot.org/annotation/VSP_035896|||http://purl.uniprot.org/annotation/VSP_035897|||http://purl.uniprot.org/annotation/VSP_035898|||http://purl.uniprot.org/annotation/VSP_035899 http://togogenome.org/gene/10090:Nup43 ^@ http://purl.uniprot.org/uniprot/P59235 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ N-acetylmethionine|||Nucleoporin Nup43|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000051112 http://togogenome.org/gene/10090:Pira13 ^@ http://purl.uniprot.org/uniprot/D3Z678|||http://purl.uniprot.org/uniprot/F6PZL4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5006722401|||http://purl.uniprot.org/annotation/PRO_5006725618 http://togogenome.org/gene/10090:Mrpl32 ^@ http://purl.uniprot.org/uniprot/Q9DCI9 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein bL32m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000030514 http://togogenome.org/gene/10090:Zfp619 ^@ http://purl.uniprot.org/uniprot/G3X9T2|||http://purl.uniprot.org/uniprot/Q66JZ1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Arhgef15 ^@ http://purl.uniprot.org/uniprot/Q5FWH6 ^@ 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 ^@ Abolishes phosphorylation by EPHB2.|||Basic and acidic residues|||DH|||Disordered|||Impairs RHOA activation; when associated with 566-A-A-567.|||Impairs RHOA activation; when associated with A-562.|||In isoform 2.|||No effect on RHOA activation; when associated with 547-A-A-548.|||No effect on RHOA activation; when associated with 554-A-A-555.|||Phosphoserine|||Phosphotyrosine; by EPHB2|||Polar residues|||Pro residues|||Rho guanine nucleotide exchange factor 15 ^@ http://purl.uniprot.org/annotation/PRO_0000360997|||http://purl.uniprot.org/annotation/VSP_036209|||http://purl.uniprot.org/annotation/VSP_036210 http://togogenome.org/gene/10090:H2-M10.6 ^@ http://purl.uniprot.org/uniprot/Q85ZW5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015099004 http://togogenome.org/gene/10090:Slc26a7 ^@ http://purl.uniprot.org/uniprot/Q8R2Z3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Anion exchange transporter|||Cytoplasmic|||Extracellular|||Helical|||Membrane targeting|||STAS ^@ http://purl.uniprot.org/annotation/PRO_0000320682 http://togogenome.org/gene/10090:Itga4 ^@ http://purl.uniprot.org/uniprot/Q00651|||http://purl.uniprot.org/uniprot/Q792F9|||http://purl.uniprot.org/uniprot/Q8BQ25 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Non-terminal Residue|||Repeat|||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|||Integrin alpha-2|||Integrin alpha-2 domain-containing protein|||Integrin alpha-4|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||SG1 ^@ http://purl.uniprot.org/annotation/PRO_0000016245|||http://purl.uniprot.org/annotation/PRO_5001426214|||http://purl.uniprot.org/annotation/PRO_5015020096 http://togogenome.org/gene/10090:C330018D20Rik ^@ http://purl.uniprot.org/uniprot/Q9CWB7 ^@ Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Strand ^@ Chain|||Disulfide Bond|||Helix|||Strand ^@ Glutaredoxin-like protein C5orf63 homolog|||Redox-active ^@ http://purl.uniprot.org/annotation/PRO_0000328757 http://togogenome.org/gene/10090:Cdh7 ^@ http://purl.uniprot.org/uniprot/Q8BM92 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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_0000320090|||http://purl.uniprot.org/annotation/PRO_0000320091 http://togogenome.org/gene/10090:Mgll ^@ http://purl.uniprot.org/uniprot/E9Q3B9|||http://purl.uniprot.org/uniprot/O35678|||http://purl.uniprot.org/uniprot/Q3UFN1 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ 3'-nitrotyrosine|||Abolishes activity.|||Charge relay system|||Disordered|||In isoform 2.|||Monoglyceride lipase|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Reduces activity.|||Serine aminopeptidase S33|||Slightly reduces activity. ^@ http://purl.uniprot.org/annotation/PRO_0000191266|||http://purl.uniprot.org/annotation/VSP_010315 http://togogenome.org/gene/10090:Cep192 ^@ http://purl.uniprot.org/uniprot/E9Q4Y4|||http://purl.uniprot.org/uniprot/Q8C769 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tnip1 ^@ http://purl.uniprot.org/uniprot/D3Z2W0|||http://purl.uniprot.org/uniprot/E9QM75|||http://purl.uniprot.org/uniprot/Q9WUU8 ^@ 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 ^@ Abolishes interaction with polyubiquitinated IRAK1.|||Abolishes ubiquitin binding; loss of inhibitory activity on NF-kappa-B activation.|||Abolishes ubiquitin binding; loss of inhibitory activity on TNF-induced NF-kappa-B activation; no effect on interaction with TNFAIP3.|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with Nef|||Loss of inhibitory activity on TNF-induced NF-kappa-B activation; no effect on interaction with TNFAIP3.|||Nuclear localization signal|||Omega-N-methylarginine; alternate|||Phosphoserine|||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_0000096692|||http://purl.uniprot.org/annotation/VSP_003914|||http://purl.uniprot.org/annotation/VSP_003915 http://togogenome.org/gene/10090:Rrp7a ^@ http://purl.uniprot.org/uniprot/Q9D1C9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||RRM|||Ribosomal RNA-processing protein 7 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000082009 http://togogenome.org/gene/10090:Nkapd1 ^@ http://purl.uniprot.org/uniprot/E9PUQ3|||http://purl.uniprot.org/uniprot/Q6NX79 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Psmd3 ^@ http://purl.uniprot.org/uniprot/P14685 ^@ 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 ^@ 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|||PCI|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000173817 http://togogenome.org/gene/10090:Lnpep ^@ http://purl.uniprot.org/uniprot/Q8C129 ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dileucine internalization motif|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Leucyl-cystinyl aminopeptidase|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Tankyrase binding|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000278198 http://togogenome.org/gene/10090:Olig1 ^@ http://purl.uniprot.org/uniprot/Q3UN59|||http://purl.uniprot.org/uniprot/Q9JKN5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Basic and acidic residues|||Disordered|||Oligodendrocyte transcription factor 1|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127412 http://togogenome.org/gene/10090:Vmn1r142 ^@ http://purl.uniprot.org/uniprot/K7N6U0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdh6 ^@ http://purl.uniprot.org/uniprot/P97326|||http://purl.uniprot.org/uniprot/Q3UYK5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000003763|||http://purl.uniprot.org/annotation/PRO_0000003764 http://togogenome.org/gene/10090:Slc27a6 ^@ http://purl.uniprot.org/uniprot/E9Q9W4 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Helical|||Long-chain fatty acid transport protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000449573 http://togogenome.org/gene/10090:Ufsp1 ^@ http://purl.uniprot.org/uniprot/Q9CZP0 ^@ Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Helix|||Mutagenesis Site|||Strand|||Turn ^@ Does not affect proteolysis activity.|||Loss of function.|||Ufm1-specific protease 1 ^@ http://purl.uniprot.org/annotation/PRO_0000280361 http://togogenome.org/gene/10090:Kifc2 ^@ http://purl.uniprot.org/uniprot/G3X8Q6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Kinesin motor|||Kinesin-like protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015091837 http://togogenome.org/gene/10090:Slc35f3 ^@ http://purl.uniprot.org/uniprot/Q1LZI2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Solute carrier family 35 member F3 ^@ http://purl.uniprot.org/annotation/PRO_0000307880 http://togogenome.org/gene/10090:Selenbp2 ^@ http://purl.uniprot.org/uniprot/Q63836 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Selenium-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000174635 http://togogenome.org/gene/10090:Pglyrp4 ^@ http://purl.uniprot.org/uniprot/B7ZMZ4|||http://purl.uniprot.org/uniprot/Q0VB07 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide ^@ Interaction with murein|||N-acetylmuramoyl-L-alanine amidase|||N-acetylmuramoyl-L-alanine amidase 1|||N-acetylmuramoyl-L-alanine amidase 2|||N-linked (GlcNAc...) asparagine|||Peptidoglycan recognition protein 4|||Peptidoglycan recognition protein family ^@ http://purl.uniprot.org/annotation/PRO_0000295275|||http://purl.uniprot.org/annotation/PRO_5015087438 http://togogenome.org/gene/10090:Gpr137b ^@ http://purl.uniprot.org/uniprot/A0A0R4J022|||http://purl.uniprot.org/uniprot/A0A1Y7VLJ5|||http://purl.uniprot.org/uniprot/Q8BNQ3 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||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 GPR137B|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000304801 http://togogenome.org/gene/10090:Prkd2 ^@ http://purl.uniprot.org/uniprot/Q8BZ03 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Important for ABL1-mediated Tyr-718 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|||Serine/threonine-protein kinase D2|||Strong decrease in catalytic activity; when associated with A-707.|||Strong decrease in catalytic activity; when associated with A-711. ^@ http://purl.uniprot.org/annotation/PRO_0000260436 http://togogenome.org/gene/10090:Slc36a2 ^@ http://purl.uniprot.org/uniprot/Q8BHK3 ^@ 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.|||Polar residues|||Proton-coupled amino acid transporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000324820|||http://purl.uniprot.org/annotation/VSP_032374|||http://purl.uniprot.org/annotation/VSP_032375 http://togogenome.org/gene/10090:Or2k2 ^@ http://purl.uniprot.org/uniprot/A2AM35 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r180 ^@ http://purl.uniprot.org/uniprot/B9EK86 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or8b56 ^@ http://purl.uniprot.org/uniprot/Q7TRB9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zmynd12 ^@ http://purl.uniprot.org/uniprot/A2BGJ5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ MYND-type ^@ http://togogenome.org/gene/10090:Drd2 ^@ http://purl.uniprot.org/uniprot/P61168 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||D(2) 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|||Important for receptor activation|||In isoform 2.|||Interaction with PPP1R9B|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069388|||http://purl.uniprot.org/annotation/VSP_010241 http://togogenome.org/gene/10090:Cyth4 ^@ http://purl.uniprot.org/uniprot/Q3U0C0|||http://purl.uniprot.org/uniprot/Q3U6Y6|||http://purl.uniprot.org/uniprot/Q3U8A6|||http://purl.uniprot.org/uniprot/Q80YW0 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region ^@ C-terminal autoinhibitory region|||Cytohesin-4|||PH|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000120204 http://togogenome.org/gene/10090:Surf1 ^@ http://purl.uniprot.org/uniprot/I6L9E0|||http://purl.uniprot.org/uniprot/P09925 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Surfeit locus protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000215653 http://togogenome.org/gene/10090:Atpsckmt ^@ http://purl.uniprot.org/uniprot/Q9D1Z3 ^@ 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 ^@ ATP synthase subunit C lysine N-methyltransferase|||Disordered|||Helical|||N-acetylmethionine|||Polar residues|||Required for mitochondrial location ^@ http://purl.uniprot.org/annotation/PRO_0000321537 http://togogenome.org/gene/10090:Psmc6 ^@ http://purl.uniprot.org/uniprot/P62334|||http://purl.uniprot.org/uniprot/Q14AQ1 ^@ 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_0000084733 http://togogenome.org/gene/10090:Sh2d1b1 ^@ http://purl.uniprot.org/uniprot/Q149T1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ SH2 ^@ http://togogenome.org/gene/10090:Ms4a4c ^@ http://purl.uniprot.org/uniprot/Q9D3F6 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Plekha5 ^@ http://purl.uniprot.org/uniprot/E9Q6H8|||http://purl.uniprot.org/uniprot/Q6ZPK1 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||PH|||Polar residues|||WW ^@ http://togogenome.org/gene/10090:Fbxo3 ^@ http://purl.uniprot.org/uniprot/Q8CDU1|||http://purl.uniprot.org/uniprot/Q9CVV6|||http://purl.uniprot.org/uniprot/Q9DC63 ^@ 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 ^@ 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_0000119878|||http://purl.uniprot.org/annotation/VSP_039615|||http://purl.uniprot.org/annotation/VSP_039616|||http://purl.uniprot.org/annotation/VSP_039617 http://togogenome.org/gene/10090:Insl6 ^@ http://purl.uniprot.org/uniprot/Q545M1|||http://purl.uniprot.org/uniprot/Q9QY05 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Propeptide|||Signal Peptide ^@ Connecting peptide|||Insulin-like|||Insulin-like peptide INSL6|||Insulin-like peptide INSL6 A chain|||Insulin-like peptide INSL6 B chain ^@ http://purl.uniprot.org/annotation/PRO_0000016177|||http://purl.uniprot.org/annotation/PRO_0000016178|||http://purl.uniprot.org/annotation/PRO_0000016179|||http://purl.uniprot.org/annotation/PRO_0000016180|||http://purl.uniprot.org/annotation/PRO_5014212506 http://togogenome.org/gene/10090:Ms4a18 ^@ http://purl.uniprot.org/uniprot/J3QN01 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Ccno ^@ http://purl.uniprot.org/uniprot/B2RWG0|||http://purl.uniprot.org/uniprot/P0C242 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Cyclin C-terminal|||Cyclin-O|||Cyclin-like|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000261156 http://togogenome.org/gene/10090:Npcd ^@ http://purl.uniprot.org/uniprot/F8VQB8|||http://purl.uniprot.org/uniprot/H3BLN6|||http://purl.uniprot.org/uniprot/Q6TLW0|||http://purl.uniprot.org/uniprot/Q6TLW1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Chromo|||Disordered ^@ http://togogenome.org/gene/10090:Vwde ^@ http://purl.uniprot.org/uniprot/Q6DFV8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ VWFD|||von Willebrand factor D and EGF domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000329442 http://togogenome.org/gene/10090:Snca ^@ http://purl.uniprot.org/uniprot/O55042 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 1|||2|||3; approximate|||4|||4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)|||Alpha-synuclein|||Disordered|||In isoform 2.|||Interaction with SERF1A|||N-acetylmethionine|||Phosphoserine; by PLK2|||Phosphotyrosine; by FYN ^@ http://purl.uniprot.org/annotation/PRO_0000184026|||http://purl.uniprot.org/annotation/VSP_025018|||http://purl.uniprot.org/annotation/VSP_025019 http://togogenome.org/gene/10090:Phax ^@ http://purl.uniprot.org/uniprot/G5E8V8|||http://purl.uniprot.org/uniprot/Q9JJT9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Does not inhibit URNA-binding.|||N-acetylalanine|||Necessary for interaction with CBP80|||Necessary for poly U RNA-binding and snRNA export|||Nuclear export signal|||Nuclear localization signal|||Partially inhibits URNA-binding.|||Partially reduces its import in the nucleus.|||Phosphorylated adapter RNA export protein|||Phosphorylated adapter RNA export protein RNA-binding|||Phosphoserine|||Phosphothreonine|||Reduces U snRNA export. Strongly abolishes the U snRNA export complex formation. Does not abolish the pre-complex formation.|||Removed|||Strongly inhibits URNA-binding.|||Strongly reduces its import in the nucleus. Abolishes its import in the nucleus, does not change its export to the cytoplasm and the export of U snRNA complex; when associated with 190-AA-191.|||Strongly reduces its import in the nucleus. Abolishes its import in the nucleus, does not change its export to the cytoplasm and the export of the U snRNA complex; when associated with 71-ARAA-74.|||Sufficient for poly U RNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000239776 http://togogenome.org/gene/10090:Nxph1 ^@ http://purl.uniprot.org/uniprot/Q61200 ^@ 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-1|||V (Cys-rich) ^@ http://purl.uniprot.org/annotation/PRO_0000020060 http://togogenome.org/gene/10090:Trpv2 ^@ http://purl.uniprot.org/uniprot/Q9WTR1 ^@ Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||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_0000215343 http://togogenome.org/gene/10090:Cd2ap ^@ http://purl.uniprot.org/uniprot/Q9JLQ0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||CD2-associated protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with ANLN and localization to the midbody|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3 1; truncated|||SH3 2|||SH3 3|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000089436 http://togogenome.org/gene/10090:Nudt18 ^@ http://purl.uniprot.org/uniprot/Q3U2V3 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Splice Variant ^@ 8-oxo-dGDP phosphatase NUDT18|||In isoform 2.|||In isoform 3.|||Nudix box|||Nudix hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000324568|||http://purl.uniprot.org/annotation/VSP_032278|||http://purl.uniprot.org/annotation/VSP_032279 http://togogenome.org/gene/10090:Xrn1 ^@ http://purl.uniprot.org/uniprot/A0A087WQN7|||http://purl.uniprot.org/uniprot/F8VQ87 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ 5'-3' exoribonuclease 1 D1|||5'-3' exoribonuclease 1 SH3-like|||Basic and acidic residues|||Disordered|||Polar residues|||Xrn1 N-terminal|||Xrn1 helical ^@ http://togogenome.org/gene/10090:Abhd4 ^@ http://purl.uniprot.org/uniprot/Q3U7M5|||http://purl.uniprot.org/uniprot/Q8C0M2|||http://purl.uniprot.org/uniprot/Q8VD66 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ (Lyso)-N-acylphosphatidylethanolamine lipase|||AB hydrolase-1 ^@ http://purl.uniprot.org/annotation/PRO_0000080865 http://togogenome.org/gene/10090:Cfp ^@ http://purl.uniprot.org/uniprot/A2AE15|||http://purl.uniprot.org/uniprot/P11680 ^@ 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 ^@ C-linked (Man) tryptophan|||Interaction with Complement C3 beta chain|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc...) serine|||O-linked (Fuc...) threonine|||Properdin|||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_0000043369|||http://purl.uniprot.org/annotation/PRO_5014296785 http://togogenome.org/gene/10090:Fosl1 ^@ http://purl.uniprot.org/uniprot/P48755|||http://purl.uniprot.org/uniprot/Q3UMK5 ^@ 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 ^@ BZIP|||Basic and acidic residues|||Basic motif|||Disordered|||Fos-related antigen 1|||Leucine-zipper|||Phosphoserine|||Polar residues|||Pro residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076480 http://togogenome.org/gene/10090:Zp2 ^@ http://purl.uniprot.org/uniprot/P20239|||http://purl.uniprot.org/uniprot/Q3UX44 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes proteolytic cleavage of the propeptide.|||Cleavage|||Cleavage; by ASTL|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||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_0000041693|||http://purl.uniprot.org/annotation/PRO_0000041694|||http://purl.uniprot.org/annotation/PRO_0000304561|||http://purl.uniprot.org/annotation/PRO_5015097511 http://togogenome.org/gene/10090:Adgre4 ^@ http://purl.uniprot.org/uniprot/Q91ZE5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Adhesion G protein-coupled receptor E4|||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_0000012878 http://togogenome.org/gene/10090:Tcn2 ^@ http://purl.uniprot.org/uniprot/O88968 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ In strain: NZB.|||Transcobalamin-2|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000005565 http://togogenome.org/gene/10090:Poc1a ^@ http://purl.uniprot.org/uniprot/Q8JZX3 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2 and isoform 3.|||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_0000231523|||http://purl.uniprot.org/annotation/VSP_017840|||http://purl.uniprot.org/annotation/VSP_017841 http://togogenome.org/gene/10090:Crlf2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JGP1|||http://purl.uniprot.org/uniprot/A0A0R4J0F5|||http://purl.uniprot.org/uniprot/Q8CII9 ^@ 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.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000011042|||http://purl.uniprot.org/annotation/PRO_5006451951|||http://purl.uniprot.org/annotation/VSP_008788|||http://purl.uniprot.org/annotation/VSP_008789|||http://purl.uniprot.org/annotation/VSP_008790|||http://purl.uniprot.org/annotation/VSP_018990|||http://purl.uniprot.org/annotation/VSP_018991 http://togogenome.org/gene/10090:Adarb1 ^@ http://purl.uniprot.org/uniprot/Q91ZS8 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ A to I editase|||DRBM 1|||DRBM 2|||Disordered|||Double-stranded RNA-specific editase 1|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 6.|||Interaction with substrate RNA|||Phosphoserine|||Polar residues|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000171780|||http://purl.uniprot.org/annotation/VSP_013709|||http://purl.uniprot.org/annotation/VSP_013710|||http://purl.uniprot.org/annotation/VSP_013711|||http://purl.uniprot.org/annotation/VSP_041423 http://togogenome.org/gene/10090:Htra3 ^@ http://purl.uniprot.org/uniprot/Q9D236 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Abolishes protease activity. No inhibition of BMP4-mediated signaling.|||Charge relay system|||IGFBP N-terminal|||In isoform 2.|||In isoform 3.|||Kazal-like|||PDZ|||Serine protease|||Serine protease HTRA3 ^@ http://purl.uniprot.org/annotation/PRO_0000026950|||http://purl.uniprot.org/annotation/VSP_018127|||http://purl.uniprot.org/annotation/VSP_018128|||http://purl.uniprot.org/annotation/VSP_018129 http://togogenome.org/gene/10090:Epm2aip1 ^@ http://purl.uniprot.org/uniprot/Q8VEH5 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ EPM2A-interacting protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000086993 http://togogenome.org/gene/10090:Ldah ^@ http://purl.uniprot.org/uniprot/Q8BVA5 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Mutagenesis Site|||Sequence Conflict|||Splice Variant ^@ Abolishes active hydrolase probe binding in serine hydrolase assays.|||Charge relay system|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Lipid droplet-associated hydrolase|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000300125|||http://purl.uniprot.org/annotation/VSP_027796|||http://purl.uniprot.org/annotation/VSP_027797|||http://purl.uniprot.org/annotation/VSP_027798|||http://purl.uniprot.org/annotation/VSP_027799 http://togogenome.org/gene/10090:Tek ^@ http://purl.uniprot.org/uniprot/B1AWS8|||http://purl.uniprot.org/uniprot/Q02858|||http://purl.uniprot.org/uniprot/Q80YS4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Loss of kinase activity.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduced levels of autophosphorylation.|||Reduced levels of autophosphorylation. Abolishes interaction with GRB2 and GRB7. Abolishes phosphorylation of GRB7 and PIK3R1.|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000024475|||http://purl.uniprot.org/annotation/PRO_5015087035|||http://purl.uniprot.org/annotation/PRO_5015098927 http://togogenome.org/gene/10090:Rassf6 ^@ http://purl.uniprot.org/uniprot/Q80UQ2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Splice Variant ^@ In isoform 2.|||Phosphoserine|||Ras association domain-containing protein 6|||Ras-associating|||SARAH ^@ http://purl.uniprot.org/annotation/PRO_0000240405|||http://purl.uniprot.org/annotation/VSP_019373 http://togogenome.org/gene/10090:Cbl ^@ http://purl.uniprot.org/uniprot/A0A0X1KG61|||http://purl.uniprot.org/uniprot/P22682 ^@ 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|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Turn|||Zinc Finger ^@ 4H|||Abolishes interaction with ZAP70, but does not affect interaction with SLA.|||Cbl-PTB|||Disordered|||E3 ubiquitin-protein ligase CBL|||EF-hand-like|||In oncogenic variant 70Z/3.|||Interaction with CD2AP|||Linker|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Phosphotyrosine; by SRC|||Polar residues|||Pro residues|||RING-type|||Required for ubiquitination of SPRED2|||SH2-like|||Sufficient for interaction with EPHB1|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000055859 http://togogenome.org/gene/10090:Semp2l2b ^@ http://purl.uniprot.org/uniprot/D3Z741 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Ubiquitin-like protease family profile ^@ http://togogenome.org/gene/10090:Vmn1r189 ^@ http://purl.uniprot.org/uniprot/Q8K3N3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nkx6-2 ^@ http://purl.uniprot.org/uniprot/D3Z4R4 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Fyn ^@ http://purl.uniprot.org/uniprot/P39688 ^@ 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 Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Abolishes myristoylation and palmitoylation.|||Abolishes palmitoylation and plasma membrane association; when associated with A-3.|||Abolishes palmitoylation and plasma membrane association; when associated with A-6.|||Abolishes palmitoylation and plasma membrane association; when associated with S-3.|||Abolishes palmitoylation and plasma membrane association; when associated with S-6. Abolishes plasma membrane association.|||Disordered|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||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_0000088100|||http://purl.uniprot.org/annotation/VSP_024111|||http://purl.uniprot.org/annotation/VSP_024112 http://togogenome.org/gene/10090:Cfap58 ^@ http://purl.uniprot.org/uniprot/B2RW38 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Cilia- and flagella-associated protein 58|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000432111 http://togogenome.org/gene/10090:Tsc1 ^@ http://purl.uniprot.org/uniprot/Q9EP53 ^@ 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|||Hamartin|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Mediates interaction with WDR45B|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000379922|||http://purl.uniprot.org/annotation/VSP_037747|||http://purl.uniprot.org/annotation/VSP_037748|||http://purl.uniprot.org/annotation/VSP_037749 http://togogenome.org/gene/10090:Scube1 ^@ http://purl.uniprot.org/uniprot/Q68EF9|||http://purl.uniprot.org/uniprot/Q6NZL8 ^@ 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 ^@ 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|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Signal peptide, CUB and EGF-like domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000254649|||http://purl.uniprot.org/annotation/PRO_5015098144|||http://purl.uniprot.org/annotation/VSP_021271|||http://purl.uniprot.org/annotation/VSP_021272|||http://purl.uniprot.org/annotation/VSP_021273 http://togogenome.org/gene/10090:Sgf29 ^@ http://purl.uniprot.org/uniprot/Q9DA08 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Histone H3K4me3 N-terminus binding|||Histone H3K4me3 binding|||N6-acetyllysine|||SAGA-associated factor 29|||SGF29 C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000274269 http://togogenome.org/gene/10090:Elapor2 ^@ http://purl.uniprot.org/uniprot/B9EHI9|||http://purl.uniprot.org/uniprot/Q3UZV7 ^@ 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|||Endosome/lysosome-associated apoptosis and autophagy regulator family member 2|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||MRH|||MRH domain-containing protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000333799|||http://purl.uniprot.org/annotation/PRO_5014300274|||http://purl.uniprot.org/annotation/VSP_033531|||http://purl.uniprot.org/annotation/VSP_033532|||http://purl.uniprot.org/annotation/VSP_033533|||http://purl.uniprot.org/annotation/VSP_033534|||http://purl.uniprot.org/annotation/VSP_033535|||http://purl.uniprot.org/annotation/VSP_033536|||http://purl.uniprot.org/annotation/VSP_033537|||http://purl.uniprot.org/annotation/VSP_033538|||http://purl.uniprot.org/annotation/VSP_033539 http://togogenome.org/gene/10090:Ggnbp2 ^@ http://purl.uniprot.org/uniprot/Q5SV77 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Gametogenetin-binding protein 2|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000239349|||http://purl.uniprot.org/annotation/VSP_019179|||http://purl.uniprot.org/annotation/VSP_019180 http://togogenome.org/gene/10090:Or2z2 ^@ http://purl.uniprot.org/uniprot/Q8VGD8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cyria ^@ http://purl.uniprot.org/uniprot/Q8BHZ0 ^@ Chain|||Molecule Processing ^@ Chain ^@ CYFIP-related Rac1 interactor A ^@ http://purl.uniprot.org/annotation/PRO_0000187059 http://togogenome.org/gene/10090:Or5an1b ^@ http://purl.uniprot.org/uniprot/Q7TQR7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ptgr3 ^@ http://purl.uniprot.org/uniprot/Q14AZ9|||http://purl.uniprot.org/uniprot/Q8BGC4 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Enoyl reductase (ER)|||N6-acetyllysine|||Phosphoserine|||Prostaglandin reductase-3 ^@ http://purl.uniprot.org/annotation/PRO_0000223466 http://togogenome.org/gene/10090:Gltpd2 ^@ http://purl.uniprot.org/uniprot/Q8K0R6 ^@ Chain|||Molecule Processing ^@ Chain ^@ Glycolipid transfer protein domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000317163 http://togogenome.org/gene/10090:Tmem117 ^@ http://purl.uniprot.org/uniprot/Q8BH18 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Transmembrane protein 117 ^@ http://purl.uniprot.org/annotation/PRO_0000251205 http://togogenome.org/gene/10090:Zfhx3 ^@ http://purl.uniprot.org/uniprot/E9QMD3 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||C2H2-type|||Disordered|||Homeobox|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Zc3hav1 ^@ http://purl.uniprot.org/uniprot/D3Z5I1|||http://purl.uniprot.org/uniprot/Q3UPF5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Basic residues|||Binding to EXOSC5|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||In isoform 2.|||N-terminal domain|||Nuclear export signal|||Nuclear localization signal|||PARP catalytic|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||WWE|||Zinc finger CCCH-type antiviral protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000331461|||http://purl.uniprot.org/annotation/VSP_033213|||http://purl.uniprot.org/annotation/VSP_033214 http://togogenome.org/gene/10090:Dab2ip ^@ http://purl.uniprot.org/uniprot/A2AUX3|||http://purl.uniprot.org/uniprot/A2AUX5|||http://purl.uniprot.org/uniprot/B7ZD29|||http://purl.uniprot.org/uniprot/Q3UHC7|||http://purl.uniprot.org/uniprot/Q52KF5 ^@ 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 ^@ Basic and acidic residues|||C2|||Disabled homolog 2-interacting protein|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Necessary for interaction with AKT1|||PH|||Phosphoserine|||Phosphoserine; by MAP3K5 and RIPK1|||Polar residues|||Pro residues|||Ras-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000252408|||http://purl.uniprot.org/annotation/VSP_020956|||http://purl.uniprot.org/annotation/VSP_020957|||http://purl.uniprot.org/annotation/VSP_046519|||http://purl.uniprot.org/annotation/VSP_046520 http://togogenome.org/gene/10090:Ptov1 ^@ http://purl.uniprot.org/uniprot/Q91VU8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Interaction with FLOT1|||Phosphoserine|||Prostate tumor-overexpressed gene 1 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000304966 http://togogenome.org/gene/10090:Cst9 ^@ http://purl.uniprot.org/uniprot/Q9Z0H6 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Cystatin-9|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000006657 http://togogenome.org/gene/10090:Srr ^@ http://purl.uniprot.org/uniprot/Q9QZX7 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant ^@ Abolishes S-nitrosylation.|||Impairs ATP-binding inducing a 80% decrease in enzyme activity.|||In isoform 2.|||In isoform 3.|||N6-(pyridoxal phosphate)lysine|||Phosphothreonine|||Proton acceptor|||S-nitrosocysteine|||Serine racemase ^@ http://purl.uniprot.org/annotation/PRO_0000185651|||http://purl.uniprot.org/annotation/VSP_025013|||http://purl.uniprot.org/annotation/VSP_025014 http://togogenome.org/gene/10090:Coa6 ^@ http://purl.uniprot.org/uniprot/Q8BGD8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Domain Extent|||Motif ^@ CHCH|||Cx10C motif|||Cx9C motif|||Cytochrome c oxidase assembly factor 6 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000420734 http://togogenome.org/gene/10090:Ankrd17 ^@ http://purl.uniprot.org/uniprot/A0A0G2JDZ9|||http://purl.uniprot.org/uniprot/E9Q804|||http://purl.uniprot.org/uniprot/E9QKG6|||http://purl.uniprot.org/uniprot/Q99NH0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||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 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 isoform 2.|||In isoform 3.|||K Homology|||KH|||N-acetylmethionine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000307918|||http://purl.uniprot.org/annotation/VSP_028866|||http://purl.uniprot.org/annotation/VSP_028867|||http://purl.uniprot.org/annotation/VSP_028868|||http://purl.uniprot.org/annotation/VSP_028869|||http://purl.uniprot.org/annotation/VSP_028870|||http://purl.uniprot.org/annotation/VSP_028871 http://togogenome.org/gene/10090:Plpp5 ^@ http://purl.uniprot.org/uniprot/Q3UMZ3|||http://purl.uniprot.org/uniprot/Q6P6K4 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||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_0000286946|||http://purl.uniprot.org/annotation/VSP_025243|||http://purl.uniprot.org/annotation/VSP_025244 http://togogenome.org/gene/10090:Prop1 ^@ http://purl.uniprot.org/uniprot/P97458 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Mutagenesis Site|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein prophet of Pit-1|||Pro residues|||Shows no significant DNA binding to a Prop1 response element in gel shift assays; transcriptional activation of a luciferase reporter gene is reduced to approximately 34% compared with that of wild-type Prop1 in transiently transfected human embryonic kidney cells.|||Shows very weak DNA binding to a Prop1 response element in gel shift assays; transcriptional activation of a luciferase reporter gene is reduced to 43% compared with that of wild-type Prop1 in transiently transfected human embryonic kidney cells. ^@ http://purl.uniprot.org/annotation/PRO_0000049272 http://togogenome.org/gene/10090:Itm2c ^@ http://purl.uniprot.org/uniprot/Q91VK4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Peptide|||Sequence Conflict|||Site|||Transmembrane ^@ BRICHOS|||CT-BRI3|||Cleavage; by furin|||Helical; Signal-anchor for type II membrane protein|||Integral membrane protein 2C|||N-linked (GlcNAc...) asparagine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000154827|||http://purl.uniprot.org/annotation/PRO_0000232646 http://togogenome.org/gene/10090:Or52h2 ^@ http://purl.uniprot.org/uniprot/Q8VGW1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Elfn2 ^@ http://purl.uniprot.org/uniprot/Q68FM6 ^@ 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_0000256139 http://togogenome.org/gene/10090:Bpnt1 ^@ http://purl.uniprot.org/uniprot/Q9Z0S1 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ 3'(2'),5'-bisphosphate nucleotidase 1|||N-acetylalanine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000142528 http://togogenome.org/gene/10090:Nxf3 ^@ http://purl.uniprot.org/uniprot/Q4ZGD9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||NTF2|||TAP-C ^@ http://togogenome.org/gene/10090:Iqce ^@ http://purl.uniprot.org/uniprot/Q6PCQ0 ^@ 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|||IQ 1|||IQ 2|||IQ domain-containing protein E|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000284111|||http://purl.uniprot.org/annotation/VSP_024436|||http://purl.uniprot.org/annotation/VSP_024437|||http://purl.uniprot.org/annotation/VSP_024438|||http://purl.uniprot.org/annotation/VSP_024439 http://togogenome.org/gene/10090:Itpr1 ^@ http://purl.uniprot.org/uniprot/P11881|||http://purl.uniprot.org/uniprot/Q3UVA1|||http://purl.uniprot.org/uniprot/Q8BQN0|||http://purl.uniprot.org/uniprot/Q8C7X9|||http://purl.uniprot.org/uniprot/Q8C8N0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes inositol 1,4,5-triphosphate binding.|||Basic and acidic residues|||Complete loss of channel activity. Significant decrease of interaction with ERP44.|||Cytoplasmic|||Decreases interaction with AHCYL1; when associated with A-1588.|||Decreases interaction with AHCYL1; when associated with A-1755.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2, isoform 4, isoform 6 and isoform 8.|||In isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 7 and isoform 8.|||Increases interaction with AHCYL1; when associated with A-1588.|||Increases interaction with AHCYL1; when associated with A-1755.|||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|||Nearly abolishes calcium flux.|||No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Polar residues|||Reduces calcium flux by about 50%.|||S-palmitoyl cysteine|||Strongly reduced palmitoylation; when associated with A-56 and A-2215.|||Strongly reduced palmitoylation; when associated with A-56 and A-849.|||Strongly reduced palmitoylation; when associated with A-849 and A-2215. ^@ http://purl.uniprot.org/annotation/PRO_0000153921|||http://purl.uniprot.org/annotation/VSP_002691|||http://purl.uniprot.org/annotation/VSP_002692|||http://purl.uniprot.org/annotation/VSP_002693|||http://purl.uniprot.org/annotation/VSP_002694 http://togogenome.org/gene/10090:Tmem127 ^@ http://purl.uniprot.org/uniprot/Q8BGP5 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||N-acetylmethionine|||Phosphoserine|||Transmembrane protein 127 ^@ http://purl.uniprot.org/annotation/PRO_0000251719 http://togogenome.org/gene/10090:Arl6ip4 ^@ http://purl.uniprot.org/uniprot/Q9JM93 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ ADP-ribosylation factor-like protein 6-interacting protein 4|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000312271 http://togogenome.org/gene/10090:Zc3h12a ^@ http://purl.uniprot.org/uniprot/Q5D1E7 ^@ 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|||C3H1-type|||Disordered|||Endoribonuclease ZC3H12A|||Increases ICOS surface expression.|||Loss of MALT1-dependent cleavage and degradation in T-cells.|||Loss of RNase activity and no loss of protein deubiquitination; when associated with A-226.|||Loss of RNase activity, no loss of protein deubiquitination and ability to inhibit stress granule (SG) formation under stress; when associated with A-226.|||Loss of RNase activity. Loss of mRNAs and miRNAs degradation. Loss of protein deubiquitination and suppression of inhibition on JNK and NF-kappa-B signaling pathway activation. Inhibits induction of angiogenesis and macrophage M2 polarization. Mislocalized in stress granule (SG). Loss of the ability to inhibit SG formation under stress. Does not inhibit binding to IL6 mRNA. Increases ICOS surface expression.|||Loss of inhibition on JNK and NF-kappa-B signaling pathway activation; when associated with A-278.|||Loss of inhibition on JNK and NF-kappa-B signaling pathway activation; when associated with A-279.|||Loss of protein deubiquitination and suppression of inhibition on JNK and NF-kappa-B signaling pathway activation. Loss of the ability to inhibit stress granule (SG) formation. No loss of RNase activity. No effect on ICOS surface expression.|||Loss of protein deubiquitination and suppression of inhibition on JNK and NF-kappa-B signaling pathway activations. No loss of RNase activity.|||Necessary for interaction with TANK|||Necessary for interaction with ZC3H12D|||Phosphoserine|||Polar residues|||Pro residues|||RNA binding|||RNase|||RNase NYN|||Reduces MALT1-dependent cleavage and degradation in T-cells.|||Reduces its phosphorylation status, does not interact with IKBKB/IKKB and BTRC, inhibits IL6 mRNA instability and IKK-mediated degradation of ZC3H12A; when associated with A-435.|||Reduces its phosphorylation status, does not interact with IKBKB/IKKB and BTRC, inhibits IL6 mRNA instability and IKK-mediated degradation of ZC3H12A; when associated with A-439.|||Ubiquitin association domain ^@ http://purl.uniprot.org/annotation/PRO_0000341513 http://togogenome.org/gene/10090:Adprm ^@ http://purl.uniprot.org/uniprot/Q99KS6 ^@ 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 ^@ In isoform 2.|||Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000286568|||http://purl.uniprot.org/annotation/VSP_025094|||http://purl.uniprot.org/annotation/VSP_025095 http://togogenome.org/gene/10090:Crygs ^@ http://purl.uniprot.org/uniprot/O35486|||http://purl.uniprot.org/uniprot/Q3UPY3 ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||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|||N-acetylserine|||N-terminal arm|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057566 http://togogenome.org/gene/10090:Adgrg5 ^@ http://purl.uniprot.org/uniprot/Q3V3Z3 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Adhesion G-protein coupled receptor G5|||Cleavage; by autolysis|||Cytoplasmic|||Drastic decrease in basal cAMP production.|||Drastic reduction in basal cAMP production.|||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|||No effect on basal cAMP production.|||Small reduction in basal cAMP production. ^@ http://purl.uniprot.org/annotation/PRO_0000288638|||http://purl.uniprot.org/annotation/VSP_058541 http://togogenome.org/gene/10090:Clvs2 ^@ http://purl.uniprot.org/uniprot/Q8BG92 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Splice Variant ^@ CRAL-TRIO|||Clavesin-2|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000297653|||http://purl.uniprot.org/annotation/VSP_027326|||http://purl.uniprot.org/annotation/VSP_027327 http://togogenome.org/gene/10090:Ufc1 ^@ http://purl.uniprot.org/uniprot/Q9CR09 ^@ Active Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Chain ^@ Glycyl thioester intermediate|||Ubiquitin-fold modifier-conjugating enzyme 1 ^@ http://purl.uniprot.org/annotation/PRO_0000082614 http://togogenome.org/gene/10090:Vmn1r25 ^@ http://purl.uniprot.org/uniprot/H3BLP0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Smc1a ^@ http://purl.uniprot.org/uniprot/Q9CU62 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||N6-acetyllysine|||Phosphoserine|||Polar residues|||SMC hinge|||Structural maintenance of chromosomes protein 1A ^@ http://purl.uniprot.org/annotation/PRO_0000118990 http://togogenome.org/gene/10090:Scamp3 ^@ http://purl.uniprot.org/uniprot/E9Q855|||http://purl.uniprot.org/uniprot/O35609|||http://purl.uniprot.org/uniprot/Q3UXS0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Secretory carrier-associated membrane protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000191258 http://togogenome.org/gene/10090:Sec31b ^@ http://purl.uniprot.org/uniprot/Q3TZ89 ^@ 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 ^@ Disordered|||In isoform 2.|||Polar 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_0000295154|||http://purl.uniprot.org/annotation/VSP_026764 http://togogenome.org/gene/10090:Creld2 ^@ http://purl.uniprot.org/uniprot/Q9CYA0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Repeat|||Signal Peptide ^@ CXXC|||Does not act as a substrate-trapping mutant.|||EGF-like 1|||EGF-like 2; calcium-binding|||FU 1|||FU 2|||N-linked (GlcNAc...) asparagine|||Protein disulfide isomerase Creld2|||Redox-active|||Substrate-trapping mutant. ^@ http://purl.uniprot.org/annotation/PRO_0000256246 http://togogenome.org/gene/10090:Grwd1 ^@ http://purl.uniprot.org/uniprot/Q5XJZ3|||http://purl.uniprot.org/uniprot/Q810D6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Acidic residues|||Disordered|||Glutamate-rich WD repeat-containing protein 1|||Histone-binding protein RBBP4 N-terminal|||Phosphoserine|||Phosphothreonine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000051012 http://togogenome.org/gene/10090:Sstr4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1D6|||http://purl.uniprot.org/uniprot/P49660 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Somatostatin receptor type 4 ^@ http://purl.uniprot.org/annotation/PRO_0000070128 http://togogenome.org/gene/10090:Cxxc4 ^@ http://purl.uniprot.org/uniprot/M0QWU0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ CXXC-type|||Disordered ^@ http://togogenome.org/gene/10090:Wwp1 ^@ http://purl.uniprot.org/uniprot/Q05CE4|||http://purl.uniprot.org/uniprot/Q3UV52|||http://purl.uniprot.org/uniprot/Q8BZZ3 ^@ 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|||Site ^@ Basic and acidic residues|||C2|||Disordered|||Glycyl thioester intermediate|||HECT|||Interaction with ERBB4|||Loss of catalytic activity. No effect on RNF11-binding. No effect on KLF2 ubiquitination. Abolishes ubiquitination of KLF5.|||NEDD4-like E3 ubiquitin-protein ligase WWP1|||Polar residues|||Required for ubiquitin-thioester formation|||WW|||WW 1|||WW 2|||WW 3|||WW 4 ^@ http://purl.uniprot.org/annotation/PRO_0000120337 http://togogenome.org/gene/10090:Fdxr ^@ http://purl.uniprot.org/uniprot/Q61578 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||NADPH:adrenodoxin oxidoreductase, mitochondrial|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000019421 http://togogenome.org/gene/10090:Tspan13 ^@ http://purl.uniprot.org/uniprot/Q9D8C2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Tetraspanin-13 ^@ http://purl.uniprot.org/annotation/PRO_0000219259 http://togogenome.org/gene/10090:Hsfy2 ^@ http://purl.uniprot.org/uniprot/Q80Y37 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||HSF-type DNA-binding|||Polar residues ^@ http://togogenome.org/gene/10090:Ccdc66 ^@ http://purl.uniprot.org/uniprot/Q6NS45 ^@ 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|||Coiled-coil domain-containing protein 66|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000320038|||http://purl.uniprot.org/annotation/VSP_031588|||http://purl.uniprot.org/annotation/VSP_031589|||http://purl.uniprot.org/annotation/VSP_031590 http://togogenome.org/gene/10090:Exosc1 ^@ http://purl.uniprot.org/uniprot/Q9DAA6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Splice Variant ^@ Exosome complex component CSL4|||In isoform 2.|||Phosphoserine|||S1 motif ^@ http://purl.uniprot.org/annotation/PRO_0000087128|||http://purl.uniprot.org/annotation/VSP_004176 http://togogenome.org/gene/10090:Pnldc1 ^@ http://purl.uniprot.org/uniprot/B2RXZ1 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Helical|||Poly(A)-specific ribonuclease PNLDC1 ^@ http://purl.uniprot.org/annotation/PRO_0000439351 http://togogenome.org/gene/10090:Marchf2 ^@ http://purl.uniprot.org/uniprot/Q8CA25|||http://purl.uniprot.org/uniprot/Q99M02 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Region|||Transmembrane|||Zinc Finger ^@ E3 ubiquitin-protein ligase MARCHF2|||Helical|||RING-CH-type|||RING-type|||Required for interaction with IKBKG ^@ http://purl.uniprot.org/annotation/PRO_0000055926 http://togogenome.org/gene/10090:Or56b35 ^@ http://purl.uniprot.org/uniprot/Q8VG18 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Snx4 ^@ http://purl.uniprot.org/uniprot/Q91YJ2 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||PX|||Sorting nexin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000236197 http://togogenome.org/gene/10090:Bsph1 ^@ http://purl.uniprot.org/uniprot/B7ZWD1|||http://purl.uniprot.org/uniprot/Q3UW26 ^@ 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|||Fibronectin type-II 1|||Fibronectin type-II 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000326157|||http://purl.uniprot.org/annotation/PRO_5015087459 http://togogenome.org/gene/10090:Thoc2 ^@ http://purl.uniprot.org/uniprot/B1AZI6|||http://purl.uniprot.org/uniprot/Q3US09|||http://purl.uniprot.org/uniprot/Q3UUT9|||http://purl.uniprot.org/uniprot/Q8CCY8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||THO complex subunit 2|||THO complex subunit 2 N-terminal|||THO complex subunitTHOC2 C-terminal|||THO complex subunitTHOC2 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000384399 http://togogenome.org/gene/10090:Bdnf ^@ http://purl.uniprot.org/uniprot/P21237|||http://purl.uniprot.org/uniprot/Q541P3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ BDNF precursor form|||Brain-derived neurotrophic factor|||Cleavage; by MBTPS1|||Forms homodimers processed at L-112 that seem more stable than the wild-type.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nerve growth factor-related|||Reduced hippocampal volume, dendritic complexity and context-dependent memory. Decreased density of dendritic mushroom spines and synapses. Impaired fear extinction. Increased anxiety-related behaviors. ^@ http://purl.uniprot.org/annotation/PRO_0000019635|||http://purl.uniprot.org/annotation/PRO_0000019636|||http://purl.uniprot.org/annotation/PRO_0000447536|||http://purl.uniprot.org/annotation/PRO_5014205862|||http://purl.uniprot.org/annotation/VSP_060202 http://togogenome.org/gene/10090:Mcm4 ^@ http://purl.uniprot.org/uniprot/P49717|||http://purl.uniprot.org/uniprot/Q3UA65|||http://purl.uniprot.org/uniprot/Q542F4 ^@ 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Arginine finger|||Basic and acidic residues|||DNA replication licensing factor MCM4|||Decreased MCM complex DNA helicase activity. Reduced ssDNA binding. No effect on MCM complex formation. No effect on MCM complex ATP binding and ATPase activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||MCM|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Results in unstable hexamers. Increased MCM complex DNA helicase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000194102 http://togogenome.org/gene/10090:Nmu ^@ http://purl.uniprot.org/uniprot/Q059S5|||http://purl.uniprot.org/uniprot/Q9QXK8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide ^@ Asparagine amide|||Methionine sulfoxide; partial|||Neuromedin U C-terminal|||Neuromedin precursor-related peptide 33|||Neuromedin precursor-related peptide 36|||Neuromedin-U-23 ^@ http://purl.uniprot.org/annotation/PRO_0000019775|||http://purl.uniprot.org/annotation/PRO_0000019776|||http://purl.uniprot.org/annotation/PRO_0000019777|||http://purl.uniprot.org/annotation/PRO_0000445767|||http://purl.uniprot.org/annotation/PRO_0000445768|||http://purl.uniprot.org/annotation/PRO_5014306676 http://togogenome.org/gene/10090:2310057M21Rik ^@ http://purl.uniprot.org/uniprot/Q9D2Q3 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ ATPase PAAT|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000260086 http://togogenome.org/gene/10090:Gcnt7 ^@ http://purl.uniprot.org/uniprot/F8WK01|||http://purl.uniprot.org/uniprot/Q3V3K7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000299039|||http://purl.uniprot.org/annotation/VSP_027537 http://togogenome.org/gene/10090:Serf1 ^@ http://purl.uniprot.org/uniprot/O88892 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Small EDRK-rich factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000050711 http://togogenome.org/gene/10090:Spink11 ^@ http://purl.uniprot.org/uniprot/A0A0R4J158|||http://purl.uniprot.org/uniprot/Q09TK7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Site|||Transmembrane ^@ Helical|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Serine protease inhibitor Kazal-type 11 ^@ http://purl.uniprot.org/annotation/PRO_0000302142 http://togogenome.org/gene/10090:Tcstv3 ^@ http://purl.uniprot.org/uniprot/O70518 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Trim61 ^@ http://purl.uniprot.org/uniprot/Q6P242|||http://purl.uniprot.org/uniprot/Q8JZK6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ B30.2/SPRY|||RING-type ^@ http://togogenome.org/gene/10090:1110032F04Rik ^@ http://purl.uniprot.org/uniprot/E9Q0B3 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Uncharacterized membrane protein C3orf80 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000413692 http://togogenome.org/gene/10090:Snx1 ^@ http://purl.uniprot.org/uniprot/Q6NZD2|||http://purl.uniprot.org/uniprot/Q9WV80 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ BAR|||Disordered|||Membrane-binding amphipathic helix|||N6-acetyllysine|||PX|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sorting nexin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000213836 http://togogenome.org/gene/10090:Ebna1bp2 ^@ http://purl.uniprot.org/uniprot/Q9D903 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable rRNA-processing protein EBP2 ^@ http://purl.uniprot.org/annotation/PRO_0000119994 http://togogenome.org/gene/10090:Phgdh ^@ http://purl.uniprot.org/uniprot/Q61753 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ 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|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000076014 http://togogenome.org/gene/10090:Or2d3 ^@ http://purl.uniprot.org/uniprot/K7N662 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ddx31 ^@ http://purl.uniprot.org/uniprot/Q6NZQ2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Probable ATP-dependent RNA helicase DDX31|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000434575 http://togogenome.org/gene/10090:Zfp579 ^@ http://purl.uniprot.org/uniprot/Q80VM4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||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_0000047670 http://togogenome.org/gene/10090:Nomo1 ^@ http://purl.uniprot.org/uniprot/Q6GQT9 ^@ 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 ^@ BOS complex subunit NOMO1|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000396822 http://togogenome.org/gene/10090:Dnajc17 ^@ http://purl.uniprot.org/uniprot/Q91WT4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||DnaJ homolog subfamily C member 17|||J|||N6-methyllysine|||Phosphoserine|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000247119 http://togogenome.org/gene/10090:Dstyk ^@ http://purl.uniprot.org/uniprot/Q6XUX1 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Dual serine/threonine and tyrosine protein kinase|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000233119|||http://purl.uniprot.org/annotation/VSP_018035|||http://purl.uniprot.org/annotation/VSP_018036|||http://purl.uniprot.org/annotation/VSP_018037|||http://purl.uniprot.org/annotation/VSP_018038|||http://purl.uniprot.org/annotation/VSP_018039 http://togogenome.org/gene/10090:Smarcd1 ^@ http://purl.uniprot.org/uniprot/Q61466|||http://purl.uniprot.org/uniprot/Q68FH8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine|||DM2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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|||Polar residues|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1|||SWIB/MDM2 ^@ http://purl.uniprot.org/annotation/PRO_0000071984 http://togogenome.org/gene/10090:Hsd3b3 ^@ http://purl.uniprot.org/uniprot/E9PXG7|||http://purl.uniprot.org/uniprot/P26150 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Transmembrane ^@ 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 3|||3-beta hydroxysteroid dehydrogenase/isomerase|||Helical|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000087782 http://togogenome.org/gene/10090:Pla2g10 ^@ http://purl.uniprot.org/uniprot/Q8C5Y6|||http://purl.uniprot.org/uniprot/Q8K130|||http://purl.uniprot.org/uniprot/Q9QXX3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Group 10 secretory phospholipase A2|||Impaired acrosome reaction.|||Phospholipase A2 ^@ http://purl.uniprot.org/annotation/PRO_0000022766|||http://purl.uniprot.org/annotation/PRO_0000022767|||http://purl.uniprot.org/annotation/PRO_5015020125 http://togogenome.org/gene/10090:Orai1 ^@ http://purl.uniprot.org/uniprot/A3KCG1|||http://purl.uniprot.org/uniprot/Q8BWG9 ^@ 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 ^@ Calcium release-activated calcium channel protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with STIM1|||N-linked (GlcNAc...) asparagine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000234382 http://togogenome.org/gene/10090:Lce1c ^@ http://purl.uniprot.org/uniprot/Q9D1C5 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Or4m1 ^@ http://purl.uniprot.org/uniprot/Q8VFT4 ^@ 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 ^@ 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 4M1|||Reduced affinity for Asprosin. ^@ http://purl.uniprot.org/annotation/PRO_0000453783 http://togogenome.org/gene/10090:Vgll3 ^@ http://purl.uniprot.org/uniprot/E9Q1Y1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Cldn34b4 ^@ http://purl.uniprot.org/uniprot/Q3V0X2 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Acap2 ^@ http://purl.uniprot.org/uniprot/A0A338P6P6|||http://purl.uniprot.org/uniprot/D4AFX6|||http://purl.uniprot.org/uniprot/Q6ZQK5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ANK|||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|||In isoform 2.|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000306385|||http://purl.uniprot.org/annotation/VSP_052554 http://togogenome.org/gene/10090:Efemp2 ^@ http://purl.uniprot.org/uniprot/G5E8D6|||http://purl.uniprot.org/uniprot/Q542X5|||http://purl.uniprot.org/uniprot/Q9WVJ9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage|||Cleavage; by ELANE|||Cleavage; by MMP2, MMP3, MMP7, MMP9, MMP12|||Disordered|||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|||EGF-like domain-containing protein|||Knockin mutant mice are viable and survive into adulthood. Mice display abnormalities in multiple organ systems, including loose skin, bent forelimb, aortic aneurysm, tortuous artery, and pulmonary emphysema. In addition to elastic fiber abnormalities in the skin and large arteries, collagen fibrils are irregularly shaped, with many large fibrils in the dermis. Mice have large artery stiffness and systolic hypertension. Reduces protein secretion.|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000007576|||http://purl.uniprot.org/annotation/PRO_5014309555|||http://purl.uniprot.org/annotation/PRO_5015091905 http://togogenome.org/gene/10090:Lalba ^@ http://purl.uniprot.org/uniprot/A0A077S9Z6|||http://purl.uniprot.org/uniprot/P29752 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Signal Peptide|||Strand|||Turn ^@ Alpha-lactalbumin|||C-type lysozyme|||Glycosyl hydrolases family 22 (GH22)|||Lactose synthase B protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000018446|||http://purl.uniprot.org/annotation/PRO_5009743845 http://togogenome.org/gene/10090:Maged2 ^@ http://purl.uniprot.org/uniprot/Q99PB4|||http://purl.uniprot.org/uniprot/Q9ER67 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Eef1akmt1 ^@ http://purl.uniprot.org/uniprot/Q9CY45 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ EEF1A lysine methyltransferase 1|||N-acetylserine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000311295 http://togogenome.org/gene/10090:Cacna1a ^@ http://purl.uniprot.org/uniprot/A0A571BET0|||http://purl.uniprot.org/uniprot/E9Q1R5|||http://purl.uniprot.org/uniprot/P97445|||http://purl.uniprot.org/uniprot/Q3UHA5|||http://purl.uniprot.org/uniprot/Q3UHN4|||http://purl.uniprot.org/uniprot/Q8R5M6|||http://purl.uniprot.org/uniprot/Q8R5M7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Basic residues|||Binding to the beta subunit|||Binds to omega-Aga-IVA|||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|||IV|||In tg.|||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_0000053917 http://togogenome.org/gene/10090:Pgm1 ^@ http://purl.uniprot.org/uniprot/Q3U6X6|||http://purl.uniprot.org/uniprot/Q9D0F9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Alpha-D-phosphohexomutase alpha/beta/alpha|||N-acetylmethionine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoglucomutase-1|||Phosphoserine|||Phosphoserine intermediate|||Phosphothreonine|||Phosphothreonine; by PAK1|||Phosphotyrosine|||via phosphate group ^@ http://purl.uniprot.org/annotation/PRO_0000147778 http://togogenome.org/gene/10090:Arpc3 ^@ http://purl.uniprot.org/uniprot/Q9JM76 ^@ Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue ^@ 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_0000124043 http://togogenome.org/gene/10090:Gpr87 ^@ http://purl.uniprot.org/uniprot/Q99MT7 ^@ 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|||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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069596 http://togogenome.org/gene/10090:Zfp36l2 ^@ http://purl.uniprot.org/uniprot/P23949 ^@ 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 ^@ Basic and acidic residues|||C3H1-type 1|||C3H1-type 2|||Disordered|||Inhibits RNA-binding.|||Phosphoserine|||Phosphoserine; by RPS6KA1|||Polar residues|||Pro residues|||RNA-binding|||mRNA decay activator protein ZFP36L2 ^@ http://purl.uniprot.org/annotation/PRO_0000089171 http://togogenome.org/gene/10090:Timp1 ^@ http://purl.uniprot.org/uniprot/P12032 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Involved in metalloproteinase-binding|||Metalloproteinase inhibitor 1|||N-linked (GlcNAc...) asparagine|||NTR|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000034325 http://togogenome.org/gene/10090:Rad18 ^@ http://purl.uniprot.org/uniprot/E9Q392|||http://purl.uniprot.org/uniprot/Q8CDH2|||http://purl.uniprot.org/uniprot/Q8CED3|||http://purl.uniprot.org/uniprot/Q9QXK2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RAD18|||LR motif|||N-acetylmethionine|||Phosphoserine|||Polar residues|||RING-type|||SAP|||UBZ4-type ^@ http://purl.uniprot.org/annotation/PRO_0000056150 http://togogenome.org/gene/10090:Or8k25 ^@ http://purl.uniprot.org/uniprot/Q7TR72 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Myl10 ^@ http://purl.uniprot.org/uniprot/A0A0G2JDZ4|||http://purl.uniprot.org/uniprot/E9QNY3|||http://purl.uniprot.org/uniprot/Q62082 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Region|||Splice Variant ^@ Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2.|||In isoform 3.|||Myosin regulatory light chain 10 ^@ http://purl.uniprot.org/annotation/PRO_0000322131|||http://purl.uniprot.org/annotation/VSP_031873|||http://purl.uniprot.org/annotation/VSP_031874 http://togogenome.org/gene/10090:Tmc6 ^@ http://purl.uniprot.org/uniprot/B1ATB3|||http://purl.uniprot.org/uniprot/Q7TN60 ^@ 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|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||TMC|||Transmembrane channel-like protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000185385|||http://purl.uniprot.org/annotation/VSP_016443|||http://purl.uniprot.org/annotation/VSP_016444|||http://purl.uniprot.org/annotation/VSP_016445|||http://purl.uniprot.org/annotation/VSP_016446|||http://purl.uniprot.org/annotation/VSP_016447 http://togogenome.org/gene/10090:Stx7 ^@ http://purl.uniprot.org/uniprot/Q8BH40 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||T-SNARE coiled-coil homology ^@ http://togogenome.org/gene/10090:Mrm2 ^@ http://purl.uniprot.org/uniprot/Q9CPY0 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Transit Peptide ^@ Mitochondrion|||Proton acceptor|||rRNA methyltransferase 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000391771 http://togogenome.org/gene/10090:Uap1l1 ^@ http://purl.uniprot.org/uniprot/Q3TW96 ^@ Binding Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Motif|||Splice Variant ^@ In isoform 2.|||Substrate binding|||UDP-N-acetylhexosamine pyrophosphorylase-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000324581|||http://purl.uniprot.org/annotation/VSP_032281 http://togogenome.org/gene/10090:Celf4 ^@ http://purl.uniprot.org/uniprot/Q7TSY6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ CUGBP Elav-like family member 4|||Disordered|||In isoform 2 and isoform 5.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6.|||In isoform 7.|||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_0000295223|||http://purl.uniprot.org/annotation/VSP_026833|||http://purl.uniprot.org/annotation/VSP_026834|||http://purl.uniprot.org/annotation/VSP_026835|||http://purl.uniprot.org/annotation/VSP_026836|||http://purl.uniprot.org/annotation/VSP_026837|||http://purl.uniprot.org/annotation/VSP_026838|||http://purl.uniprot.org/annotation/VSP_026839|||http://purl.uniprot.org/annotation/VSP_026840 http://togogenome.org/gene/10090:Alox8 ^@ http://purl.uniprot.org/uniprot/O35936 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant ^@ Changes the stereoselectivity of the oxygenation reaction to produce (15S)-HPETE instead of (8S)-HPETE. Completely changes the stereoselectivity; when associated with D-603.|||Changes the stereoselectivity of the oxygenation reaction to produce (15S)-HPETE instead of (8S)-HPETE. Completely changes the stereoselectivity; when associated with V-604.|||In clone G2.|||In clone K12.|||In clone K7.|||In clones G2, G5 and G11.|||In clones G2, G5, G11 and K1.|||Lipoxygenase|||Loss of enzymatic activity.|||PLAT|||Polyunsaturated fatty acid lipoxygenase ALOX8|||Retains catalytic activity indicating it is not required for iron ligand-binding. ^@ http://purl.uniprot.org/annotation/PRO_0000220701 http://togogenome.org/gene/10090:Iqschfp ^@ http://purl.uniprot.org/uniprot/A0A088MLT8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant ^@ Acidic residues|||Disordered|||IQ|||IQCJ-SCHIP1 readthrough transcript protein|||In isoform Iqcj-schip1-2.|||Loss of interaction with calmodulin.|||Polar residues|||Required for interaction with ankyrins ^@ http://purl.uniprot.org/annotation/PRO_0000442333|||http://purl.uniprot.org/annotation/VSP_059226 http://togogenome.org/gene/10090:Fancg ^@ http://purl.uniprot.org/uniprot/Q9EQR6 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ Fanconi anemia group G protein homolog|||TPR 1|||TPR 2|||TPR 3|||TPR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000106293 http://togogenome.org/gene/10090:Tmem29 ^@ http://purl.uniprot.org/uniprot/A2ANF5|||http://purl.uniprot.org/uniprot/E9PZH0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Sgms2 ^@ http://purl.uniprot.org/uniprot/Q9D4B1 ^@ Active Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Phosphatidylcholine:ceramide cholinephosphotransferase 2|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000221073 http://togogenome.org/gene/10090:Pycard ^@ http://purl.uniprot.org/uniprot/Q54AA2|||http://purl.uniprot.org/uniprot/Q9EPB4 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Apoptosis-associated speck-like protein containing a CARD|||CARD|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000064693 http://togogenome.org/gene/10090:P3h1 ^@ http://purl.uniprot.org/uniprot/A2A7Q5|||http://purl.uniprot.org/uniprot/A6PW84|||http://purl.uniprot.org/uniprot/Q3V1T4 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||Fe2OG dioxygenase|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Prolyl 3-hydroxylase 1|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||procollagen-proline 3-dioxygenase ^@ http://purl.uniprot.org/annotation/PRO_0000240353|||http://purl.uniprot.org/annotation/PRO_5002642435|||http://purl.uniprot.org/annotation/PRO_5002698090|||http://purl.uniprot.org/annotation/VSP_019349|||http://purl.uniprot.org/annotation/VSP_019350|||http://purl.uniprot.org/annotation/VSP_019351 http://togogenome.org/gene/10090:Mfsd4b1 ^@ http://purl.uniprot.org/uniprot/Q8VCV9 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Sodium-dependent glucose transporter 1A ^@ http://purl.uniprot.org/annotation/PRO_0000294511 http://togogenome.org/gene/10090:Lrch3 ^@ http://purl.uniprot.org/uniprot/B2RXP1|||http://purl.uniprot.org/uniprot/B7ZWM8|||http://purl.uniprot.org/uniprot/E9QAU9|||http://purl.uniprot.org/uniprot/Q8BVU0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Calponin-homology (CH)|||DISP complex protein LRCH3|||Disordered|||Helical|||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_0000253485 http://togogenome.org/gene/10090:Plk2 ^@ http://purl.uniprot.org/uniprot/P53351|||http://purl.uniprot.org/uniprot/Q3TV29|||http://purl.uniprot.org/uniprot/Q548A9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Does not significantly affect kinase activity.|||In DN mutant; Loss of kinase activity; leading to disrupted Ras and Rap protein signaling, altered spine morphology and aberrant memory formation in mice.|||Mimicks phosphorylation state, leading to increased 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_0000086562 http://togogenome.org/gene/10090:Gm13278 ^@ http://purl.uniprot.org/uniprot/Q8CD73 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099103 http://togogenome.org/gene/10090:Rgs22 ^@ http://purl.uniprot.org/uniprot/G3UYX5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||RGS 1|||RGS 2|||Regulator of G-protein signaling 22 ^@ http://purl.uniprot.org/annotation/PRO_0000428676 http://togogenome.org/gene/10090:Mvp ^@ http://purl.uniprot.org/uniprot/E9Q3X0|||http://purl.uniprot.org/uniprot/Q3U7S9|||http://purl.uniprot.org/uniprot/Q9EQK5 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ 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_0000158981 http://togogenome.org/gene/10090:Defa37 ^@ http://purl.uniprot.org/uniprot/K9J724 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Mammalian defensins ^@ http://purl.uniprot.org/annotation/PRO_5015096006 http://togogenome.org/gene/10090:Rad54l2 ^@ http://purl.uniprot.org/uniprot/E9QKL0|||http://purl.uniprot.org/uniprot/Q99NG0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes ATP-binding.|||Abolishes ATPase activity.|||Acidic residues|||Basic and acidic residues|||DEAH box|||Decreased sumoylation; when associated with E-361; E-573; E-664; E-935 and E-1013.|||Decreased sumoylation; when associated with E-361; E-573; E-664; E-935 and E-961.|||Decreased sumoylation; when associated with E-361; E-573; E-664; E-961 and E-1013.|||Decreased sumoylation; when associated with E-361; E-573; E-935; E-961 and E-1013.|||Decreased sumoylation; when associated with E-361; E-664; E-935; E-961 and E-1013.|||Decreased sumoylation; when associated with E-573; E-664; E-935; E-961 and E-1013.|||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_0000315782 http://togogenome.org/gene/10090:Alg6 ^@ http://purl.uniprot.org/uniprot/Q3TAE8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000284132 http://togogenome.org/gene/10090:Sphk2 ^@ http://purl.uniprot.org/uniprot/Q3U912|||http://purl.uniprot.org/uniprot/Q58E38|||http://purl.uniprot.org/uniprot/Q9JIA7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes sphingosine kinase activity. Decreases apoptosis induction. Abolishes sphingosine kinase activity. No effect on endoplasmic reticulum location increase upon serum starvation. Abolishes sphingosine kinase activity and decreases apoptosis induction; when associated with A-219.|||DAGKc|||Disordered|||Loss of nuclear location. Loss of DNA synthesis inhibition.|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Proton donor/acceptor|||Required for binding to sulfatide and phosphoinositides and for membrane localization|||Sphingosine kinase 2|||Strongly decreases sphingosine kinase activity. Decreases apoptosis induction. No effect on endoplasmic reticulum location increase upon serum starvation. Abolishes sphingosine kinase activity and decreases apoptosis induction; when associated with E-213. ^@ http://purl.uniprot.org/annotation/PRO_0000181359 http://togogenome.org/gene/10090:Cdx4 ^@ http://purl.uniprot.org/uniprot/Q07424|||http://purl.uniprot.org/uniprot/Q78Z64 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Homeobox protein CDX-4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048853 http://togogenome.org/gene/10090:Ppip5k2 ^@ http://purl.uniprot.org/uniprot/Q6ZQB6|||http://purl.uniprot.org/uniprot/Q8BWK5 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2|||Phosphoserine|||Polar residues|||Polyphosphoinositide-binding domain ^@ http://purl.uniprot.org/annotation/PRO_0000315693|||http://purl.uniprot.org/annotation/VSP_030637|||http://purl.uniprot.org/annotation/VSP_030638|||http://purl.uniprot.org/annotation/VSP_041618 http://togogenome.org/gene/10090:Rln3 ^@ http://purl.uniprot.org/uniprot/Q8CHK2 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Signal Peptide ^@ Connecting peptide|||Interchain (between B and A chains)|||Relaxin-3 A chain|||Relaxin-3 B chain ^@ http://purl.uniprot.org/annotation/PRO_0000016085|||http://purl.uniprot.org/annotation/PRO_0000016086|||http://purl.uniprot.org/annotation/PRO_0000016087 http://togogenome.org/gene/10090:Or5w1 ^@ http://purl.uniprot.org/uniprot/Q7TR43 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cplx2 ^@ http://purl.uniprot.org/uniprot/P84086 ^@ 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_0000144876 http://togogenome.org/gene/10090:Wdr27 ^@ http://purl.uniprot.org/uniprot/A0A338P6H6|||http://purl.uniprot.org/uniprot/Q8C5V5 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ 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 27 ^@ http://purl.uniprot.org/annotation/PRO_0000306832 http://togogenome.org/gene/10090:Tex19.2 ^@ http://purl.uniprot.org/uniprot/B2RUP5|||http://purl.uniprot.org/uniprot/Q9D5S1 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Important for interaction with piRNA|||Testis-expressed protein 19.2 ^@ http://purl.uniprot.org/annotation/PRO_0000325964 http://togogenome.org/gene/10090:Erich6b ^@ http://purl.uniprot.org/uniprot/Q9D4S6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Gar1 ^@ http://purl.uniprot.org/uniprot/Q9CY66 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H/ACA ribonucleoprotein complex subunit 1|||In isoform 2 and isoform 3.|||In isoform 3.|||RGG-box 1|||RGG-box 2 ^@ http://purl.uniprot.org/annotation/PRO_0000208553|||http://purl.uniprot.org/annotation/VSP_011426|||http://purl.uniprot.org/annotation/VSP_011427 http://togogenome.org/gene/10090:Or6c215 ^@ http://purl.uniprot.org/uniprot/Q8VFI1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r123 ^@ http://purl.uniprot.org/uniprot/L7N270 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Naip2 ^@ http://purl.uniprot.org/uniprot/Q8CGT0|||http://purl.uniprot.org/uniprot/Q9QUK4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ BIR 1|||BIR 2|||BIR 3|||Baculoviral IAP repeat-containing protein 1b|||NACHT ^@ http://purl.uniprot.org/annotation/PRO_0000122343 http://togogenome.org/gene/10090:Actr5 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ89 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Dnajc28 ^@ http://purl.uniprot.org/uniprot/E9Q1L7|||http://purl.uniprot.org/uniprot/Q8C4S9|||http://purl.uniprot.org/uniprot/Q8VCE1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent ^@ DnaJ homolog subfamily C member 28|||J ^@ http://purl.uniprot.org/annotation/PRO_0000071140 http://togogenome.org/gene/10090:Lilra6 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1F3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015034605 http://togogenome.org/gene/10090:Rgs10 ^@ http://purl.uniprot.org/uniprot/Q32MD7|||http://purl.uniprot.org/uniprot/Q9CQE5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||RGS|||Regulator of G-protein signaling 10|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000204208 http://togogenome.org/gene/10090:Mllt6 ^@ http://purl.uniprot.org/uniprot/B1AR09|||http://purl.uniprot.org/uniprot/B1AR10|||http://purl.uniprot.org/uniprot/Q3UPK1 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||PHD-type|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Vmn2r19 ^@ http://purl.uniprot.org/uniprot/G5E8G4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015091898 http://togogenome.org/gene/10090:Nexn ^@ http://purl.uniprot.org/uniprot/A0A0G2JEX1|||http://purl.uniprot.org/uniprot/Q7TPW1 ^@ 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|||Ig-like|||Nexilin|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000302086 http://togogenome.org/gene/10090:Zfp456 ^@ http://purl.uniprot.org/uniprot/B2RUK9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Arf1 ^@ http://purl.uniprot.org/uniprot/P84078 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ ADP-ribosylation factor 1|||Important for the stable binding to the membranes|||N-acetylglycine; alternate|||N-myristoyl glycine; alternate|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207380 http://togogenome.org/gene/10090:Comtd1 ^@ http://purl.uniprot.org/uniprot/Q8BIG7 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Catechol O-methyltransferase domain-containing protein 1|||Helical; Signal-anchor for type II membrane protein ^@ http://purl.uniprot.org/annotation/PRO_0000233290 http://togogenome.org/gene/10090:Gm2a ^@ http://purl.uniprot.org/uniprot/Q5F1Z8|||http://purl.uniprot.org/uniprot/Q60648 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Abolishes phospholipid binding.|||Ganglioside GM2 activator|||MD-2-related lipid-recognition|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000031643|||http://purl.uniprot.org/annotation/PRO_5014309797 http://togogenome.org/gene/10090:Gpkow ^@ http://purl.uniprot.org/uniprot/Q56A08 ^@ 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 ^@ Basic and acidic residues|||Disordered|||G-patch|||G-patch domain and KOW motifs-containing protein|||KOW 1|||KOW 2|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by PKA|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000280563 http://togogenome.org/gene/10090:Rpl13a ^@ http://purl.uniprot.org/uniprot/P19253 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant ^@ Citrulline|||In allele TUM-.|||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_0000133770 http://togogenome.org/gene/10090:Cldn2 ^@ http://purl.uniprot.org/uniprot/O88552 ^@ Chain|||Crosslink|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Disulfide Bond|||Modified Residue|||Region|||Strand|||Topological Domain|||Transmembrane ^@ Claudin-2|||Cytoplasmic|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||Interactions with TJP1, TJP2 and TJP3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000144735 http://togogenome.org/gene/10090:H2al1b ^@ http://purl.uniprot.org/uniprot/A0A087WP11 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Histone H2A/H2B/H3 ^@ http://togogenome.org/gene/10090:Kctd9 ^@ http://purl.uniprot.org/uniprot/E9PUA6|||http://purl.uniprot.org/uniprot/Q80UN1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ BTB|||BTB/POZ domain-containing protein KCTD9|||KHA|||Pentapeptide repeat 1|||Pentapeptide repeat 2|||Pentapeptide repeat 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000191294 http://togogenome.org/gene/10090:Sult4a1 ^@ http://purl.uniprot.org/uniprot/P63046 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Phosphothreonine|||Sulfotransferase 4A1 ^@ http://purl.uniprot.org/annotation/PRO_0000085168|||http://purl.uniprot.org/annotation/VSP_006305 http://togogenome.org/gene/10090:Psenen ^@ http://purl.uniprot.org/uniprot/Q9CQR7 ^@ Chain|||INTRAMEM|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Gamma-secretase subunit PEN-2|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000190901 http://togogenome.org/gene/10090:Tas2r110 ^@ http://purl.uniprot.org/uniprot/Q7M712 ^@ 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 110 ^@ http://purl.uniprot.org/annotation/PRO_0000247660 http://togogenome.org/gene/10090:Abcc1 ^@ http://purl.uniprot.org/uniprot/A5D6P3|||http://purl.uniprot.org/uniprot/O35379 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ ABC transmembrane type-1|||ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter|||ABC transporter 1|||ABC transporter 2|||Cytoplasmic|||Disordered|||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|||Multidrug resistance-associated protein 1|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000093353 http://togogenome.org/gene/10090:Peds1 ^@ http://purl.uniprot.org/uniprot/Q99LQ7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Site|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Essential for catalytic activity|||Helical|||Histidine box-1|||Histidine box-2|||Loss of plasmanylethanolamine desaturase activity. Does not affect endoplasmic reticulum membrane localization.|||Plasmanylethanolamine desaturase 1|||Strongly reduces plasmanylethanolamine desaturase activity. Does not affect endoplasmic reticulum membrane localization. ^@ http://purl.uniprot.org/annotation/PRO_0000319994 http://togogenome.org/gene/10090:Fbxl19 ^@ http://purl.uniprot.org/uniprot/Q6PB97 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||CXXC-type|||Disordered|||F-box|||F-box/LRR-repeat protein 19|||In isoform 2 and isoform 3.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||PHD-type|||Polar residues|||Pro residues|||Strongly inhibits the recognition of non-methylated CpGs. ^@ http://purl.uniprot.org/annotation/PRO_0000119869|||http://purl.uniprot.org/annotation/VSP_013016|||http://purl.uniprot.org/annotation/VSP_013017 http://togogenome.org/gene/10090:Tmem91 ^@ http://purl.uniprot.org/uniprot/D3Z7E7|||http://purl.uniprot.org/uniprot/D3Z7E8|||http://purl.uniprot.org/uniprot/Q8C581 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Transmembrane protein 91 ^@ http://purl.uniprot.org/annotation/PRO_0000135700 http://togogenome.org/gene/10090:Pramel1 ^@ http://purl.uniprot.org/uniprot/Q99MW3 ^@ 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|||Preferentially expressed antigen in melanoma-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000438837 http://togogenome.org/gene/10090:Eif3a ^@ http://purl.uniprot.org/uniprot/P23116|||http://purl.uniprot.org/uniprot/Q3TRH1|||http://purl.uniprot.org/uniprot/Q3UM46 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ 10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||1; truncated|||2|||20|||21 X 10 AA approximate tandem repeats of [DA]-[DE]-[ED]-R-[PLIGFSV]-[RPS]-[RW]-[RL]-[GNIHT]-[DGLPTAM]|||21; approximate|||3; approximate|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 3 subunit A|||Interaction with EIF3B|||N6-acetyllysine|||PCI|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000123538 http://togogenome.org/gene/10090:Aqp7 ^@ http://purl.uniprot.org/uniprot/O54794|||http://purl.uniprot.org/uniprot/Q5DX24 ^@ Chain|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Modified Residue|||Motif|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Aquaporin-7|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||Important for permeability to glycerol|||NPA 1|||NPA 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000063959 http://togogenome.org/gene/10090:Fkbp1b ^@ http://purl.uniprot.org/uniprot/A9E3L2|||http://purl.uniprot.org/uniprot/Q810R7|||http://purl.uniprot.org/uniprot/Q9Z2I2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP1B ^@ http://purl.uniprot.org/annotation/PRO_0000075296 http://togogenome.org/gene/10090:Gm14391 ^@ http://purl.uniprot.org/uniprot/A2ART0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Aarsd1 ^@ http://purl.uniprot.org/uniprot/Q3THG9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Alanyl-tRNA editing protein Aarsd1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000277466 http://togogenome.org/gene/10090:St8sia5 ^@ http://purl.uniprot.org/uniprot/P70126|||http://purl.uniprot.org/uniprot/Q3TRR3 ^@ 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 V-M.|||In isoform V-S.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000149297|||http://purl.uniprot.org/annotation/VSP_001789|||http://purl.uniprot.org/annotation/VSP_001790 http://togogenome.org/gene/10090:Creb5 ^@ http://purl.uniprot.org/uniprot/A0A0N4SUK5|||http://purl.uniprot.org/uniprot/A0A0N4SV71|||http://purl.uniprot.org/uniprot/Q8K1L0 ^@ 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 ^@ BZIP|||Basic and acidic residues|||Basic motif|||Basic residues|||C2H2-type|||Cyclic AMP-responsive element-binding protein 5|||Disordered|||In isoform 2.|||Leucine-zipper|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076605|||http://purl.uniprot.org/annotation/VSP_022061|||http://purl.uniprot.org/annotation/VSP_022062|||http://purl.uniprot.org/annotation/VSP_022063 http://togogenome.org/gene/10090:Adamts14 ^@ http://purl.uniprot.org/uniprot/B2RXX5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||PLAC|||Peptidase M12B|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015087172 http://togogenome.org/gene/10090:Slc25a42 ^@ http://purl.uniprot.org/uniprot/Q8R0Y8 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Repeat|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial coenzyme A transporter SLC25A42|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000291818 http://togogenome.org/gene/10090:Peg10 ^@ http://purl.uniprot.org/uniprot/Q7TN75 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||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.|||Necessary for interaction with ACVRL1|||Omega-N-methylarginine|||Phosphoserine|||Pro residues|||Retrotransposon-derived protein PEG10 ^@ http://purl.uniprot.org/annotation/PRO_0000323027|||http://purl.uniprot.org/annotation/VSP_032009|||http://purl.uniprot.org/annotation/VSP_032010 http://togogenome.org/gene/10090:Nhlh1 ^@ http://purl.uniprot.org/uniprot/Q02576 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Helix-loop-helix protein 1|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127198 http://togogenome.org/gene/10090:Tpbpa ^@ http://purl.uniprot.org/uniprot/Q9CPR0 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Region|||Signal Peptide ^@ Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015099659 http://togogenome.org/gene/10090:Or1l8 ^@ http://purl.uniprot.org/uniprot/Q8VFP6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dock7 ^@ http://purl.uniprot.org/uniprot/A0A0U1RNK7|||http://purl.uniprot.org/uniprot/A2A9M5|||http://purl.uniprot.org/uniprot/E9PX48 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Zfp994 ^@ http://purl.uniprot.org/uniprot/J3QM38 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Atp13a2 ^@ http://purl.uniprot.org/uniprot/E9Q2A4|||http://purl.uniprot.org/uniprot/Q9CTG6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||P5B-type ATPase N-terminal|||Polyamine-transporting ATPase 13A2 ^@ http://purl.uniprot.org/annotation/PRO_0000046424 http://togogenome.org/gene/10090:Or10ak11 ^@ http://purl.uniprot.org/uniprot/Q7TQV7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or12e13 ^@ http://purl.uniprot.org/uniprot/Q7TR35 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp182 ^@ http://purl.uniprot.org/uniprot/A2AE18|||http://purl.uniprot.org/uniprot/Q6P560 ^@ 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 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 182 ^@ http://purl.uniprot.org/annotation/PRO_0000047346 http://togogenome.org/gene/10090:Gpr65 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Y2|||http://purl.uniprot.org/uniprot/Q3UQ35|||http://purl.uniprot.org/uniprot/Q3UZ41|||http://purl.uniprot.org/uniprot/Q61038 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||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|||Psychosine receptor ^@ http://purl.uniprot.org/annotation/PRO_0000070088 http://togogenome.org/gene/10090:Stag2 ^@ http://purl.uniprot.org/uniprot/A2AFF6|||http://purl.uniprot.org/uniprot/O35638|||http://purl.uniprot.org/uniprot/Q3TG33 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Cohesin subunit SA-2|||Disordered|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SCD ^@ http://purl.uniprot.org/annotation/PRO_0000120186 http://togogenome.org/gene/10090:Akr1c19 ^@ http://purl.uniprot.org/uniprot/G3X9Y6 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Site ^@ Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor ^@ http://togogenome.org/gene/10090:Ilk ^@ http://purl.uniprot.org/uniprot/O55222 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||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_0000086022 http://togogenome.org/gene/10090:Hoxc13 ^@ http://purl.uniprot.org/uniprot/P50207 ^@ Chain|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Region ^@ Disordered|||Homeobox|||Homeobox protein Hox-C13 ^@ http://purl.uniprot.org/annotation/PRO_0000200198 http://togogenome.org/gene/10090:Tpmt ^@ http://purl.uniprot.org/uniprot/A0A0R4J018|||http://purl.uniprot.org/uniprot/O55060 ^@ 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 ^@ In strain: C57BL/6J.|||N6-acetyllysine|||Phosphoserine|||Thiopurine S-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000220105 http://togogenome.org/gene/10090:Nkx2-5 ^@ http://purl.uniprot.org/uniprot/P42582|||http://purl.uniprot.org/uniprot/Q3UQU2 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Helix|||Sequence Conflict ^@ Homeobox|||Homeobox protein Nkx-2.5 ^@ http://purl.uniprot.org/annotation/PRO_0000048938 http://togogenome.org/gene/10090:Ccm2l ^@ http://purl.uniprot.org/uniprot/Q8VCC6 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Region|||Splice Variant ^@ Cerebral cavernous malformations 2 protein-like|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000079477|||http://purl.uniprot.org/annotation/VSP_044624|||http://purl.uniprot.org/annotation/VSP_044625 http://togogenome.org/gene/10090:Rnf113a2 ^@ http://purl.uniprot.org/uniprot/Q14B01|||http://purl.uniprot.org/uniprot/Q9D7A3 ^@ Domain Extent|||Region|||Zinc Finger ^@ Domain Extent|||Region|||Zinc Finger ^@ C3H1-type|||Disordered|||RING-type ^@ http://togogenome.org/gene/10090:Tmem219 ^@ http://purl.uniprot.org/uniprot/Q9D123 ^@ 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.|||Insulin-like growth factor-binding protein 3 receptor|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000329050|||http://purl.uniprot.org/annotation/VSP_032932|||http://purl.uniprot.org/annotation/VSP_032933|||http://purl.uniprot.org/annotation/VSP_032934 http://togogenome.org/gene/10090:Rnf185 ^@ http://purl.uniprot.org/uniprot/Q91YT2 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Region|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||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_0000247521|||http://purl.uniprot.org/annotation/VSP_020005 http://togogenome.org/gene/10090:Or11h4b ^@ http://purl.uniprot.org/uniprot/E9PXH6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vax2 ^@ http://purl.uniprot.org/uniprot/Q14B19|||http://purl.uniprot.org/uniprot/Q9WTP9 ^@ 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|||Polar residues|||Ventral anterior homeobox 2 ^@ http://purl.uniprot.org/annotation/PRO_0000049352 http://togogenome.org/gene/10090:Uso1 ^@ http://purl.uniprot.org/uniprot/Q9Z1Z0 ^@ 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 10|||ARM 11|||ARM 12|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Acidic residues|||Disordered|||General vesicular transport factor p115|||Globular head|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000065775|||http://purl.uniprot.org/annotation/VSP_016978|||http://purl.uniprot.org/annotation/VSP_016979|||http://purl.uniprot.org/annotation/VSP_016980|||http://purl.uniprot.org/annotation/VSP_016981 http://togogenome.org/gene/10090:Cog4 ^@ http://purl.uniprot.org/uniprot/Q7TSQ9|||http://purl.uniprot.org/uniprot/Q8R1U1 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Conserved oligomeric Golgi complex subunit 4|||D domain|||Disordered|||E domain; essential for proper cell surface glycosylation|||Interaction with SCFD1|||Interaction with STX5|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213505 http://togogenome.org/gene/10090:Bst1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J190|||http://purl.uniprot.org/uniprot/Q64277 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase|||ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000004034|||http://purl.uniprot.org/annotation/PRO_0000004035|||http://purl.uniprot.org/annotation/PRO_5006452006 http://togogenome.org/gene/10090:Six4 ^@ http://purl.uniprot.org/uniprot/Q61321 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein SIX4|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Removed|||Transactivation domain ^@ http://purl.uniprot.org/annotation/PRO_0000049304|||http://purl.uniprot.org/annotation/VSP_002293|||http://purl.uniprot.org/annotation/VSP_002294|||http://purl.uniprot.org/annotation/VSP_002295|||http://purl.uniprot.org/annotation/VSP_002296 http://togogenome.org/gene/10090:Pcdhb22 ^@ http://purl.uniprot.org/uniprot/Q8C8Z3|||http://purl.uniprot.org/uniprot/Q91XZ8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Cadherin domain-containing protein|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5004306233|||http://purl.uniprot.org/annotation/PRO_5015099504 http://togogenome.org/gene/10090:Syt10 ^@ http://purl.uniprot.org/uniprot/Q059J3|||http://purl.uniprot.org/uniprot/Q9R0N4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ C2|||C2 1|||C2 2|||Cysteine motif|||Cytoplasmic|||Helical|||Loss of function; when associated with A-268; A-320; A-322; A-400 and A-454.|||Loss of function; when associated with A-268; A-320; A-322; A-400 and A-456.|||Loss of function; when associated with A-268; A-320; A-322; A-454 and A-456.|||Loss of function; when associated with A-268; A-320; A-400; A-454 and A-456.|||Loss of function; when associated with A-268; A-322; A-400; A-454 and A-456.|||Loss of function; when associated with A-320; A-322; A-400; A-454 and A-456.|||Phosphothreonine|||Synaptotagmin-10|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000183966 http://togogenome.org/gene/10090:Fbxl8 ^@ http://purl.uniprot.org/uniprot/Q3TD55|||http://purl.uniprot.org/uniprot/Q8CIG9 ^@ 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_0000119851 http://togogenome.org/gene/10090:1700028K03Rik ^@ http://purl.uniprot.org/uniprot/Q3KQP7 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||Protein SPO16 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000299021|||http://purl.uniprot.org/annotation/VSP_027516|||http://purl.uniprot.org/annotation/VSP_027517 http://togogenome.org/gene/10090:Dixdc1 ^@ http://purl.uniprot.org/uniprot/Q80Y83 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||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|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Actin-binding|||Calponin-homology (CH)|||DIX|||Disordered|||Dixin|||In isoform 11 and isoform 12.|||In isoform 13 and isoform 14.|||In isoform 15.|||In isoform 16.|||In isoform 2, isoform 4, isoform 6, isoform 8, isoform 10, isoform 12 and isoform 14.|||In isoform 3, isoform 4, isoform 7, isoform 8 and isoform 16.|||In isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 9 and isoform 10.|||N-myristoyl glycine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000287224|||http://purl.uniprot.org/annotation/VSP_025383|||http://purl.uniprot.org/annotation/VSP_025384|||http://purl.uniprot.org/annotation/VSP_025385|||http://purl.uniprot.org/annotation/VSP_025386|||http://purl.uniprot.org/annotation/VSP_025387|||http://purl.uniprot.org/annotation/VSP_025388|||http://purl.uniprot.org/annotation/VSP_025389|||http://purl.uniprot.org/annotation/VSP_025390|||http://purl.uniprot.org/annotation/VSP_025391|||http://purl.uniprot.org/annotation/VSP_025392|||http://purl.uniprot.org/annotation/VSP_025393|||http://purl.uniprot.org/annotation/VSP_025394|||http://purl.uniprot.org/annotation/VSP_025395|||http://purl.uniprot.org/annotation/VSP_025396 http://togogenome.org/gene/10090:Ppp1r14a ^@ http://purl.uniprot.org/uniprot/Q91VC7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Inhibitory|||Phosphoserine|||Phosphothreonine; by PKC|||Protein phosphatase 1 regulatory subunit 14A ^@ http://purl.uniprot.org/annotation/PRO_0000071487 http://togogenome.org/gene/10090:Med23 ^@ http://purl.uniprot.org/uniprot/E9QNV2|||http://purl.uniprot.org/uniprot/F8WJB0|||http://purl.uniprot.org/uniprot/Q80YQ2 ^@ 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.|||Mediator of RNA polymerase II transcription subunit 23|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000305931|||http://purl.uniprot.org/annotation/VSP_028382|||http://purl.uniprot.org/annotation/VSP_041583|||http://purl.uniprot.org/annotation/VSP_041584 http://togogenome.org/gene/10090:Trcg1 ^@ http://purl.uniprot.org/uniprot/F8VPJ5|||http://purl.uniprot.org/uniprot/Q58Y74 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||Taste receptor cell protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000309591|||http://purl.uniprot.org/annotation/PRO_5003385282|||http://purl.uniprot.org/annotation/VSP_029241|||http://purl.uniprot.org/annotation/VSP_029242|||http://purl.uniprot.org/annotation/VSP_029243 http://togogenome.org/gene/10090:Dmrtc1c2 ^@ http://purl.uniprot.org/uniprot/Q14AJ8|||http://purl.uniprot.org/uniprot/Q9D410 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Doublesex- and mab-3-related transcription factor C1/C2 C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Zfp85 ^@ http://purl.uniprot.org/uniprot/Q7TMC9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Igf1r ^@ http://purl.uniprot.org/uniprot/E9QNX9|||http://purl.uniprot.org/uniprot/Q3U1L4|||http://purl.uniprot.org/uniprot/Q60751 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Acidic residues|||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|||Insulin-like growth factor 1 receptor alpha chain|||Insulin-like growth factor 1 receptor beta chain|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Proton donor/acceptor|||Tyrosine-protein kinase receptor ^@ http://purl.uniprot.org/annotation/PRO_0000016683|||http://purl.uniprot.org/annotation/PRO_0000016684|||http://purl.uniprot.org/annotation/PRO_5003244826 http://togogenome.org/gene/10090:Taar8b ^@ http://purl.uniprot.org/uniprot/Q5QD06 ^@ 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|||Trace amine-associated receptor 8b ^@ http://purl.uniprot.org/annotation/PRO_0000070177 http://togogenome.org/gene/10090:Fpr-rs6 ^@ http://purl.uniprot.org/uniprot/Q3SXG2 ^@ 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|||Formyl peptide receptor-related sequence 6|||Helical; 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_0000382025 http://togogenome.org/gene/10090:Asb1 ^@ http://purl.uniprot.org/uniprot/G3X9J5|||http://purl.uniprot.org/uniprot/Q3U5A0|||http://purl.uniprot.org/uniprot/Q9WV74 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ ANK|||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_0000066924 http://togogenome.org/gene/10090:Mecr ^@ http://purl.uniprot.org/uniprot/Q9DCS3 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Enoyl-[acyl-carrier-protein] reductase, mitochondrial|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000000889 http://togogenome.org/gene/10090:As3mt ^@ http://purl.uniprot.org/uniprot/Q91WU5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Arsenite methyltransferase|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000204448 http://togogenome.org/gene/10090:Kcna6 ^@ http://purl.uniprot.org/uniprot/Q61923 ^@ Chain|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Region|||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|||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_0000053991 http://togogenome.org/gene/10090:Yaf2 ^@ http://purl.uniprot.org/uniprot/Q99LW6 ^@ 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.|||Phosphoserine|||Polar residues|||RanBP2-type|||YY1-associated factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000066114|||http://purl.uniprot.org/annotation/VSP_050619|||http://purl.uniprot.org/annotation/VSP_050620 http://togogenome.org/gene/10090:Fam168a ^@ http://purl.uniprot.org/uniprot/Q8BGZ2 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||N-acetylmethionine|||Protein FAM168A ^@ http://purl.uniprot.org/annotation/PRO_0000050743|||http://purl.uniprot.org/annotation/VSP_010096 http://togogenome.org/gene/10090:Pou3f1 ^@ http://purl.uniprot.org/uniprot/P21952|||http://purl.uniprot.org/uniprot/Q3UTH6 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic residues|||Disordered|||Homeobox|||POU domain, class 3, transcription factor 1|||POU-specific ^@ http://purl.uniprot.org/annotation/PRO_0000100721 http://togogenome.org/gene/10090:Homer2 ^@ http://purl.uniprot.org/uniprot/E9Q4F9|||http://purl.uniprot.org/uniprot/Q9QWW1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Homer protein homolog 2|||In isoform 2.|||Polar residues|||WH1 ^@ http://purl.uniprot.org/annotation/PRO_0000191009|||http://purl.uniprot.org/annotation/VSP_009071 http://togogenome.org/gene/10090:Slc9a3 ^@ http://purl.uniprot.org/uniprot/G3X939 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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|||Interaction with AHCYL1|||Interaction with EZR|||Interaction with NHERF4|||Phosphoserine|||Phosphoserine; by SGK1|||Sodium/hydrogen exchanger 3 ^@ http://purl.uniprot.org/annotation/PRO_0000433355 http://togogenome.org/gene/10090:Muc1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0H1|||http://purl.uniprot.org/uniprot/Q02496 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ 1|||10; approximate|||11|||12|||13|||14|||15|||16|||16 X 20 AA approximate tandem repeats|||2|||3|||4; approximate|||5; approximate|||6; approximate|||7|||8|||9; approximate|||Cleavage; by autolysis|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with GRB2|||Interaction with P53|||Interaction with SRC and ESR1|||Mucin-1|||Mucin-1 subunit alpha|||Mucin-1 subunit beta|||N-linked (GlcNAc...) asparagine|||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|||Required for interaction with AP1S2|||Required for interaction with GSK3B|||Required for interaction with beta- and gamma-catenins|||S-palmitoyl cysteine|||SEA ^@ http://purl.uniprot.org/annotation/PRO_0000019280|||http://purl.uniprot.org/annotation/PRO_0000317452|||http://purl.uniprot.org/annotation/PRO_0000317453|||http://purl.uniprot.org/annotation/PRO_5015044289 http://togogenome.org/gene/10090:Trappc12 ^@ http://purl.uniprot.org/uniprot/Q3UGE1|||http://purl.uniprot.org/uniprot/Q8C0C3|||http://purl.uniprot.org/uniprot/Q8K2L8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||Trafficking protein particle complex subunit 12 ^@ http://purl.uniprot.org/annotation/PRO_0000106402 http://togogenome.org/gene/10090:Lyzl4 ^@ http://purl.uniprot.org/uniprot/Q78ID0|||http://purl.uniprot.org/uniprot/Q9D925 ^@ 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_0000240639|||http://purl.uniprot.org/annotation/PRO_5014310807 http://togogenome.org/gene/10090:Sall3 ^@ http://purl.uniprot.org/uniprot/Q62255 ^@ 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|||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 isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Sal-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000047025|||http://purl.uniprot.org/annotation/VSP_006834 http://togogenome.org/gene/10090:4933421I07Rik ^@ http://purl.uniprot.org/uniprot/Q9D420 ^@ Domain Extent|||Region ^@ Domain Extent ^@ N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:E4f1 ^@ http://purl.uniprot.org/uniprot/Q8CCE9 ^@ 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; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||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_0000324308|||http://purl.uniprot.org/annotation/VSP_032192|||http://purl.uniprot.org/annotation/VSP_032193|||http://purl.uniprot.org/annotation/VSP_032194|||http://purl.uniprot.org/annotation/VSP_032195|||http://purl.uniprot.org/annotation/VSP_032196|||http://purl.uniprot.org/annotation/VSP_032197 http://togogenome.org/gene/10090:Zfp874b ^@ http://purl.uniprot.org/uniprot/Q7M6X2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Tacc3 ^@ http://purl.uniprot.org/uniprot/Q6NV52|||http://purl.uniprot.org/uniprot/Q99LH8 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disordered|||Transforming acidic coiled-coil-containing protein C-terminal ^@ http://togogenome.org/gene/10090:Ndufb10 ^@ http://purl.uniprot.org/uniprot/Q9DCS9 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Disordered|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000118831 http://togogenome.org/gene/10090:Vmn2r102 ^@ http://purl.uniprot.org/uniprot/L7N279 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982270 http://togogenome.org/gene/10090:Nr5a2 ^@ http://purl.uniprot.org/uniprot/A0A0A6YY04|||http://purl.uniprot.org/uniprot/P45448|||http://purl.uniprot.org/uniprot/Q1WLP7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Motif|||Region|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||FTZ-F1 box|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 5 group A member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000053736 http://togogenome.org/gene/10090:Ctcf ^@ http://purl.uniprot.org/uniprot/Q61164 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||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|||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|||N-acetylmethionine|||No sumoylation.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Transcriptional repressor CTCF ^@ http://purl.uniprot.org/annotation/PRO_0000047229 http://togogenome.org/gene/10090:Col3a1 ^@ http://purl.uniprot.org/uniprot/P08121|||http://purl.uniprot.org/uniprot/Q3TVI5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Signal Peptide ^@ 5-hydroxylysine|||5-hydroxylysine; alternate|||C-terminal propeptide|||Collagen alpha-1(III) chain|||Disordered|||Fibrillar collagen NC1|||Interchain|||Interchain (with C-1266)|||Interchain (with C-1283)|||N-terminal propeptide|||Nonhelical region (N-terminal)|||O-linked (Gal...) hydroxylysine; alternate|||Polar residues|||Pro residues|||Triple-helical region|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000005743|||http://purl.uniprot.org/annotation/PRO_0000005744|||http://purl.uniprot.org/annotation/PRO_0000005745|||http://purl.uniprot.org/annotation/PRO_5014309114 http://togogenome.org/gene/10090:Abi3 ^@ http://purl.uniprot.org/uniprot/Q8BYZ1 ^@ 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 ^@ ABI gene family member 3|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000191793|||http://purl.uniprot.org/annotation/VSP_010773 http://togogenome.org/gene/10090:Tnr ^@ http://purl.uniprot.org/uniprot/Q8BYI9 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||Fibrinogen C-terminal|||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 isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Tenascin-R ^@ http://purl.uniprot.org/annotation/PRO_0000007748|||http://purl.uniprot.org/annotation/VSP_012994 http://togogenome.org/gene/10090:H2al1m ^@ http://purl.uniprot.org/uniprot/Q9DAD9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Histone H2A/H2B/H3 ^@ http://togogenome.org/gene/10090:Ints5 ^@ http://purl.uniprot.org/uniprot/Q8CHT3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Integrator complex subunit 5|||N-acetylserine|||Phosphoserine|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000259542 http://togogenome.org/gene/10090:Blmh ^@ http://purl.uniprot.org/uniprot/Q8R016 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Bleomycin hydrolase|||N-acetylmethionine|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000050551 http://togogenome.org/gene/10090:Slc10a7 ^@ http://purl.uniprot.org/uniprot/Q5PT53 ^@ 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.|||In isoform 3.|||Sodium/bile acid cotransporter 7 ^@ http://purl.uniprot.org/annotation/PRO_0000278251|||http://purl.uniprot.org/annotation/VSP_023225|||http://purl.uniprot.org/annotation/VSP_023226 http://togogenome.org/gene/10090:Gvin2 ^@ http://purl.uniprot.org/uniprot/Q80SU7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Interferon-induced very large GTPase 1|||VLIG-type G ^@ http://purl.uniprot.org/annotation/PRO_0000324579 http://togogenome.org/gene/10090:Pctp ^@ http://purl.uniprot.org/uniprot/Q5SV41 ^@ Domain Extent|||Region ^@ Domain Extent ^@ START ^@ http://togogenome.org/gene/10090:Mamstr ^@ http://purl.uniprot.org/uniprot/Q0ZCJ7 ^@ 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.|||MEF2-activating motif and SAP domain-containing transcriptional regulator|||MEF2-binding|||Polar residues|||Pro residues|||SAP|||Transcription activation ^@ http://purl.uniprot.org/annotation/PRO_0000319982|||http://purl.uniprot.org/annotation/VSP_031556|||http://purl.uniprot.org/annotation/VSP_031557 http://togogenome.org/gene/10090:Or12j3 ^@ http://purl.uniprot.org/uniprot/Q8VFE8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tubd1 ^@ http://purl.uniprot.org/uniprot/Q5SWF8|||http://purl.uniprot.org/uniprot/Q8CDD3|||http://purl.uniprot.org/uniprot/Q9R1K7 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Tubulin delta chain|||Tubulin/FtsZ GTPase ^@ http://purl.uniprot.org/annotation/PRO_0000048485 http://togogenome.org/gene/10090:Cdk13 ^@ http://purl.uniprot.org/uniprot/Q69ZA1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||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|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||Cyclin-dependent kinase 13|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085712|||http://purl.uniprot.org/annotation/VSP_013580 http://togogenome.org/gene/10090:Rnf182 ^@ http://purl.uniprot.org/uniprot/Q8C432 ^@ Chain|||Molecule Processing|||Region|||Transmembrane|||Zinc Finger ^@ Chain|||Transmembrane|||Zinc Finger ^@ E3 ubiquitin-protein ligase RNF182|||Helical|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000261621 http://togogenome.org/gene/10090:E130308A19Rik ^@ http://purl.uniprot.org/uniprot/Q0P6E2|||http://purl.uniprot.org/uniprot/Q8C4P0 ^@ 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 ^@ DUF3504|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Uncharacterized protein KIAA1958 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000050812|||http://purl.uniprot.org/annotation/VSP_015147 http://togogenome.org/gene/10090:Cntnap1 ^@ http://purl.uniprot.org/uniprot/O54991 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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|||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_0000019504 http://togogenome.org/gene/10090:Lhfpl7 ^@ http://purl.uniprot.org/uniprot/Q3UUA0 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||LHFPL tetraspan subfamily member 7 protein ^@ http://purl.uniprot.org/annotation/PRO_0000337009 http://togogenome.org/gene/10090:Bahcc1 ^@ http://purl.uniprot.org/uniprot/Q3UHR0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Acidic residues|||BAH|||BAH and coiled-coil domain-containing protein 1|||Basic and acidic residues|||Disordered|||N6-acetyllysine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000312119 http://togogenome.org/gene/10090:Heyl ^@ http://purl.uniprot.org/uniprot/Q9DBX7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ 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_0000286430 http://togogenome.org/gene/10090:Ndufa3 ^@ http://purl.uniprot.org/uniprot/Q9CQ91 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Transmembrane|||Turn ^@ Disordered|||Helical|||N-acetylalanine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118794 http://togogenome.org/gene/10090:Metap1d ^@ http://purl.uniprot.org/uniprot/Q9CPW9 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Methionine aminopeptidase 1D, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000314127|||http://purl.uniprot.org/annotation/VSP_030210 http://togogenome.org/gene/10090:Gm21637 ^@ http://purl.uniprot.org/uniprot/E9PWJ8 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Ctla4 ^@ http://purl.uniprot.org/uniprot/P09793|||http://purl.uniprot.org/uniprot/Q5SSM0|||http://purl.uniprot.org/uniprot/Q6GTR6 ^@ 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 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Cytotoxic T-lymphocyte protein 4|||Extracellular|||Helical|||Homodimerization|||Ig-like|||Ig-like V-type|||Important for interaction with CD80 and CD86|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by TXK and JAK2 ^@ http://purl.uniprot.org/annotation/PRO_0000014735|||http://purl.uniprot.org/annotation/PRO_5015098018|||http://purl.uniprot.org/annotation/PRO_5015098282 http://togogenome.org/gene/10090:Wdr76 ^@ http://purl.uniprot.org/uniprot/A6PWY4 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||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_0000351092|||http://purl.uniprot.org/annotation/VSP_035463|||http://purl.uniprot.org/annotation/VSP_035464|||http://purl.uniprot.org/annotation/VSP_035465|||http://purl.uniprot.org/annotation/VSP_035466 http://togogenome.org/gene/10090:Fgfr1 ^@ http://purl.uniprot.org/uniprot/P16092|||http://purl.uniprot.org/uniprot/Q8CBY7|||http://purl.uniprot.org/uniprot/Q8CIM9 ^@ 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 Conflict|||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|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Acidic residues|||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 isoform 2, isoform 4 and isoform 5.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 5.|||Mediates interaction with PLCG1 and SHB|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000016781|||http://purl.uniprot.org/annotation/PRO_5004306372|||http://purl.uniprot.org/annotation/VSP_002961|||http://purl.uniprot.org/annotation/VSP_002962|||http://purl.uniprot.org/annotation/VSP_002963|||http://purl.uniprot.org/annotation/VSP_041919|||http://purl.uniprot.org/annotation/VSP_041920|||http://purl.uniprot.org/annotation/VSP_041921|||http://purl.uniprot.org/annotation/VSP_041922 http://togogenome.org/gene/10090:Prom1 ^@ http://purl.uniprot.org/uniprot/A0A0G2JDH9|||http://purl.uniprot.org/uniprot/A0A0G2JE50|||http://purl.uniprot.org/uniprot/A0A0R4J0B0|||http://purl.uniprot.org/uniprot/G3X9J8|||http://purl.uniprot.org/uniprot/G5E8G5|||http://purl.uniprot.org/uniprot/O54990|||http://purl.uniprot.org/uniprot/Q8CDK8|||http://purl.uniprot.org/uniprot/Q8R056 ^@ Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2, isoform 3, isoform 5 and isoform 6.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine|||Prominin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000025814|||http://purl.uniprot.org/annotation/PRO_5002545879|||http://purl.uniprot.org/annotation/PRO_5006451959|||http://purl.uniprot.org/annotation/PRO_5015039209|||http://purl.uniprot.org/annotation/PRO_5015091842|||http://purl.uniprot.org/annotation/PRO_5015091899|||http://purl.uniprot.org/annotation/PRO_5015099032|||http://purl.uniprot.org/annotation/PRO_5015099335|||http://purl.uniprot.org/annotation/VSP_040005|||http://purl.uniprot.org/annotation/VSP_040006|||http://purl.uniprot.org/annotation/VSP_040007|||http://purl.uniprot.org/annotation/VSP_040008|||http://purl.uniprot.org/annotation/VSP_040009|||http://purl.uniprot.org/annotation/VSP_040010|||http://purl.uniprot.org/annotation/VSP_040011 http://togogenome.org/gene/10090:Mmp7 ^@ http://purl.uniprot.org/uniprot/Q3UN27 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Motif|||Signal Peptide ^@ Cysteine switch|||Peptidase metallopeptidase|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_5015020016 http://togogenome.org/gene/10090:Or8g55 ^@ http://purl.uniprot.org/uniprot/Q9EQA2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wnk1 ^@ http://purl.uniprot.org/uniprot/P83741|||http://purl.uniprot.org/uniprot/Q7TPR2 ^@ 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|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Amphipathic alpha-helix|||Autoinhibitory domain|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with KLHL3|||No effect on inhibition of SLC4A4.|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000086820|||http://purl.uniprot.org/annotation/PRO_5004294889|||http://purl.uniprot.org/annotation/VSP_040271|||http://purl.uniprot.org/annotation/VSP_040272|||http://purl.uniprot.org/annotation/VSP_040273|||http://purl.uniprot.org/annotation/VSP_040274|||http://purl.uniprot.org/annotation/VSP_040275|||http://purl.uniprot.org/annotation/VSP_040276|||http://purl.uniprot.org/annotation/VSP_040277|||http://purl.uniprot.org/annotation/VSP_058592|||http://purl.uniprot.org/annotation/VSP_058593 http://togogenome.org/gene/10090:Nfatc4 ^@ http://purl.uniprot.org/uniprot/Q8K120 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 2 approximate SP repeats|||Calcineurin-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||IPT/TIG|||In isoform 2.|||Nuclear factor of activated T-cells, cytoplasmic 4|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by MAPK7 and MAPK14|||Phosphoserine; by MAPK8 and MAPK9|||Phosphoserine; by RPS6KA3|||Polar residues|||Pro residues|||RHD|||SP 1|||SP 2; approximate ^@ http://purl.uniprot.org/annotation/PRO_0000367433|||http://purl.uniprot.org/annotation/VSP_053054|||http://purl.uniprot.org/annotation/VSP_053055 http://togogenome.org/gene/10090:Bora ^@ http://purl.uniprot.org/uniprot/Q8BS90 ^@ 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.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Protein aurora borealis ^@ http://purl.uniprot.org/annotation/PRO_0000273206|||http://purl.uniprot.org/annotation/VSP_022496|||http://purl.uniprot.org/annotation/VSP_022497 http://togogenome.org/gene/10090:Spast ^@ http://purl.uniprot.org/uniprot/A0A286YE25|||http://purl.uniprot.org/uniprot/Q9QYY8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ AAA+ ATPase|||Cytoplasmic|||Decreased microtubule severing activity.|||Disordered|||Helical|||In isoform 2.|||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_0000084764|||http://purl.uniprot.org/annotation/VSP_058335 http://togogenome.org/gene/10090:Akain1 ^@ http://purl.uniprot.org/uniprot/G3UWD5 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ A-kinase anchor protein inhibitor 1|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000432849 http://togogenome.org/gene/10090:Ccdc166 ^@ http://purl.uniprot.org/uniprot/Q0P5Z5|||http://purl.uniprot.org/uniprot/S4R181 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||DUF4515|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Pde6g ^@ http://purl.uniprot.org/uniprot/P09174|||http://purl.uniprot.org/uniprot/Q542R6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma ^@ http://purl.uniprot.org/annotation/PRO_0000166118 http://togogenome.org/gene/10090:Hrh3 ^@ http://purl.uniprot.org/uniprot/P58406|||http://purl.uniprot.org/uniprot/Q3USH0|||http://purl.uniprot.org/uniprot/Q540P3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||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|||Histamine H3 receptor|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000069691 http://togogenome.org/gene/10090:Epg5 ^@ http://purl.uniprot.org/uniprot/Q80TA9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Ectopic P granules protein 5 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000306256 http://togogenome.org/gene/10090:Barhl2 ^@ http://purl.uniprot.org/uniprot/Q7TNS3|||http://purl.uniprot.org/uniprot/Q8VIB5 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region ^@ BarH-like 2 homeobox protein|||Basic and acidic residues|||Disordered|||Homeobox|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000048830 http://togogenome.org/gene/10090:Tex54 ^@ http://purl.uniprot.org/uniprot/G3UW99 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Testis-expressed protein 54 ^@ http://purl.uniprot.org/annotation/PRO_0000443094 http://togogenome.org/gene/10090:Pcp4l1 ^@ http://purl.uniprot.org/uniprot/Q6W8Q3 ^@ 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|||IQ|||Phosphothreonine|||Purkinje cell protein 4-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000331433 http://togogenome.org/gene/10090:Tll1 ^@ http://purl.uniprot.org/uniprot/G3X9F5 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Site ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region ^@ Basic and acidic residues|||CUB|||Disordered|||EGF-like|||Peptidase M12A ^@ http://togogenome.org/gene/10090:Ihh ^@ http://purl.uniprot.org/uniprot/P97812|||http://purl.uniprot.org/uniprot/Q80XI9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Cholesterol glycine ester|||Cleavage; by autolysis|||Disordered|||Essential for auto-cleavage|||Hint|||Indian hedgehog protein|||Indian hedgehog protein N-product|||Involved in auto-cleavage|||Involved in cholesterol transfer|||N-linked (GlcNAc...) asparagine|||N-palmitoyl cysteine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000013232|||http://purl.uniprot.org/annotation/PRO_0000013233 http://togogenome.org/gene/10090:Myh8 ^@ http://purl.uniprot.org/uniprot/P13542 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Actin-binding|||Basic and acidic residues|||Disordered|||IQ|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-8|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pros-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000123414 http://togogenome.org/gene/10090:Kmt2d ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ73 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||FYR C-terminal|||FYR N-terminal|||PHD-type|||Polar residues|||Post-SET|||Pro residues|||RING-type|||SET ^@ http://togogenome.org/gene/10090:Galnt9 ^@ http://purl.uniprot.org/uniprot/G3X942|||http://purl.uniprot.org/uniprot/Q3TB05 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Ricin B lectin ^@ http://togogenome.org/gene/10090:R3hdml ^@ http://purl.uniprot.org/uniprot/A2A5I3 ^@ 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 R3HDML|||SCP ^@ http://purl.uniprot.org/annotation/PRO_0000287637|||http://purl.uniprot.org/annotation/PRO_0000287638 http://togogenome.org/gene/10090:Atm ^@ http://purl.uniprot.org/uniprot/B9EHX4|||http://purl.uniprot.org/uniprot/Q62388 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Activation loop|||Catalytic loop|||Disordered|||FAT|||FATC|||G-loop|||Interaction with ABL1|||Microbody targeting signal; atypical|||N-acetylserine|||N6-acetyllysine|||PI3K/PI4K catalytic|||Phosphoserine|||Phosphoserine; by autocatalysis|||Polar residues|||Removed|||Retains genomic stability and cell cycle checkpoint correction and kinase activity towards downstream targets; when associated with A-1987. Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-1899 and A-1987.|||Retains genomic stability and cell cycle checkpoint correction and kinase activity towards downstream targets; when associated with A-367. Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-367 and A-1987.|||Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-367 and A-1987.|||Serine-protein kinase ATM ^@ http://purl.uniprot.org/annotation/PRO_0000088841 http://togogenome.org/gene/10090:Slc7a6os ^@ http://purl.uniprot.org/uniprot/Q7TPE5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Probable RNA polymerase II nuclear localization protein SLC7A6OS ^@ http://purl.uniprot.org/annotation/PRO_0000289170 http://togogenome.org/gene/10090:Clic1 ^@ http://purl.uniprot.org/uniprot/Q542F1|||http://purl.uniprot.org/uniprot/Q9Z1Q5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Transmembrane ^@ Chloride intracellular channel protein 1|||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_0000144202 http://togogenome.org/gene/10090:Ackr3 ^@ http://purl.uniprot.org/uniprot/P56485 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Atypical chemokine receptor 3|||C-terminal cytoplasmic tail|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000070102 http://togogenome.org/gene/10090:Smap2 ^@ http://purl.uniprot.org/uniprot/Q7TN29 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Arf-GAP|||C4-type|||Disordered|||In isoform 2.|||Interaction with PICALM|||Interaction with clathrin heavy chains|||Loss of GTPase activation.|||Loss of interaction with clathrin heavy chains; when associated with 187-AAAAA-191.|||Loss of interaction with clathrin heavy chains; when associated with 212-AAA-214.|||Phosphoserine|||Stromal membrane-associated protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000235842|||http://purl.uniprot.org/annotation/VSP_018505|||http://purl.uniprot.org/annotation/VSP_018506 http://togogenome.org/gene/10090:Pik3c2b ^@ http://purl.uniprot.org/uniprot/E9QAN8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2|||C2 PI3K-type|||Disordered|||PI3K-RBD|||PI3K/PI4K catalytic|||PIK helical|||PX|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Or2h2 ^@ http://purl.uniprot.org/uniprot/Q0VEL5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gatb ^@ http://purl.uniprot.org/uniprot/Q99JT1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial|||Mitochondrion|||N6-succinyllysine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000010711 http://togogenome.org/gene/10090:Stfa2l1 ^@ http://purl.uniprot.org/uniprot/Q8BWM3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Cystatin ^@ http://togogenome.org/gene/10090:Chsy3 ^@ http://purl.uniprot.org/uniprot/Q5DTK1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chondroitin sulfate synthase 3|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000320145 http://togogenome.org/gene/10090:Maged1 ^@ http://purl.uniprot.org/uniprot/Q9QYH6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ 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|||MAGE|||Melanoma-associated antigen D1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000156724 http://togogenome.org/gene/10090:Or4c116 ^@ http://purl.uniprot.org/uniprot/L7MU53 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rb1 ^@ http://purl.uniprot.org/uniprot/P13405 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes the interaction with many chromatin regulators but not that with KMT5B and KMT5C; when associated with A-746 and A-750.|||Abolishes the interaction with many chromatin regulators but not that with KMT5B and KMT5C; when associated with A-746 and A-754.|||Abolishes the interaction with many chromatin regulators but not that with KMT5B and KMT5C; when associated with A-750 and A-754.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Domain A|||Domain B|||Domain; mediates interaction with E4F1|||Interaction with LIMD1|||Loss of exclusive nuclear localization and loss of growth inhibition, when transfected in Saos-2 cells. No effect on the interaction with SV40 large T antigen.|||Loss of exclusive nuclear localization, no effect on the interaction with SV40 large T antigen, adenovirus E1a, nor E2F1. Decreased growth inhibition activity, when transfected in Saos-2 cells. Complete loss of nuclear localization, loss of growth inhibition, when transfected in Saos-2 cells and loss of interaction with SV40 large T antigen, adenovirus E1a and E2F1; when associated with 733-K--P-769.|||Loss of exclusive nuclear localization. Complete loss of nuclear localization, loss of growth inhibition, when transfected in Saos-2 cells and loss of interaction with SV40 large T antigen, adenovirus E1a and E2F1; when associated with 866-N--Q-869.|||Loss of exclusive nuclear localization. Decreased growth inhibition activity, when transfected in Saos-2 cells. No effect on the interaction with SV40 large T antigen, adenovirus E1a, nor E2F1.|||N,N-dimethylproline; by NTM1|||N6-acetyllysine; by PCAF|||N6-methyllysine; by SMYD2|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphothreonine|||Pocket; binds T and E1A|||Pro residues|||Removed|||Retinoblastoma-associated protein|||Spacer ^@ http://purl.uniprot.org/annotation/PRO_0000167837 http://togogenome.org/gene/10090:Slc7a8 ^@ http://purl.uniprot.org/uniprot/Q9QXW9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Region|||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|||Important for substrate specificity|||Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.|||Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake. Increases the export of both L-leucine and L-phenylalanine.|||Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.|||Interchain (with C-103 in SLC3A2)|||Large neutral amino acids transporter small subunit 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000054274 http://togogenome.org/gene/10090:Dnajc15 ^@ http://purl.uniprot.org/uniprot/Q78YY6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Topological Domain|||Transmembrane ^@ DnaJ homolog subfamily C member 15|||Helical|||J|||Mitochondrial intermembrane|||Mitochondrial matrix|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000247140 http://togogenome.org/gene/10090:Dclk2 ^@ http://purl.uniprot.org/uniprot/A0A0A6YX33|||http://purl.uniprot.org/uniprot/Q6PGN3 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Doublecortin|||Doublecortin 1|||Doublecortin 2|||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.|||Loss of kinase activity. No effect on colocalization with microtubules.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase DCLK2 ^@ http://purl.uniprot.org/annotation/PRO_0000085923|||http://purl.uniprot.org/annotation/VSP_012797|||http://purl.uniprot.org/annotation/VSP_038892|||http://purl.uniprot.org/annotation/VSP_038893|||http://purl.uniprot.org/annotation/VSP_038894|||http://purl.uniprot.org/annotation/VSP_038895|||http://purl.uniprot.org/annotation/VSP_038896 http://togogenome.org/gene/10090:Or10d5j ^@ http://purl.uniprot.org/uniprot/Q8VF15 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cmtr2 ^@ http://purl.uniprot.org/uniprot/Q8BWQ4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Adrift-type SAM-dependent 2'-O-MTase|||Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000326181 http://togogenome.org/gene/10090:Slc51a ^@ http://purl.uniprot.org/uniprot/Q8R000 ^@ 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|||Organic solute transporter subunit alpha|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000331544 http://togogenome.org/gene/10090:Vps53 ^@ http://purl.uniprot.org/uniprot/Q8CCB4 ^@ 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.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Vacuolar protein sorting-associated protein 53 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000215190|||http://purl.uniprot.org/annotation/VSP_016239 http://togogenome.org/gene/10090:Dlx6 ^@ http://purl.uniprot.org/uniprot/P70397 ^@ 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. ^@ http://purl.uniprot.org/annotation/PRO_0000049035|||http://purl.uniprot.org/annotation/VSP_040733 http://togogenome.org/gene/10090:Dhrs11 ^@ http://purl.uniprot.org/uniprot/Q3U0B3 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Signal Peptide ^@ Dehydrogenase/reductase SDR family member 11|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000045491 http://togogenome.org/gene/10090:Cacng3 ^@ http://purl.uniprot.org/uniprot/Q9JJV5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Decreased interaction with AP4M1. Has no effect on interaction with GRIA1. Dominant negative mutant which alters AMPARs localization to the somatodendritic compartment.|||Disordered|||Helical|||Phosphoserine|||Voltage-dependent calcium channel gamma-3 subunit ^@ http://purl.uniprot.org/annotation/PRO_0000164676 http://togogenome.org/gene/10090:Ap5b1 ^@ http://purl.uniprot.org/uniprot/Q3TAP4 ^@ Chain|||Molecule Processing ^@ Chain ^@ AP-5 complex subunit beta-1 ^@ http://purl.uniprot.org/annotation/PRO_0000405405 http://togogenome.org/gene/10090:Urb1 ^@ http://purl.uniprot.org/uniprot/E9PU96|||http://purl.uniprot.org/uniprot/Q571H0 ^@ 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.|||Nucleolar pre-ribosomal-associated protein 1|||Nucleolar pre-ribosomal-associated protein 1 C-terminal|||Nucleolar pre-ribosomal-associated protein 1 N-terminal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000307935|||http://purl.uniprot.org/annotation/VSP_028877|||http://purl.uniprot.org/annotation/VSP_028878 http://togogenome.org/gene/10090:Golph3 ^@ http://purl.uniprot.org/uniprot/Q9CRA5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Beta-hairpin required for oligomerization|||Disordered|||Golgi phosphoprotein 3|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000123820|||http://purl.uniprot.org/annotation/VSP_037833|||http://purl.uniprot.org/annotation/VSP_037834 http://togogenome.org/gene/10090:Hfe ^@ http://purl.uniprot.org/uniprot/P70387|||http://purl.uniprot.org/uniprot/Q5SZ87 ^@ 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 ^@ Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Extracellular|||Helical|||Hereditary hemochromatosis protein homolog|||Ig-like|||Ig-like C1-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000018894|||http://purl.uniprot.org/annotation/PRO_5015098026 http://togogenome.org/gene/10090:Klk1b22 ^@ http://purl.uniprot.org/uniprot/P15948|||http://purl.uniprot.org/uniprot/Q540N3 ^@ 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|||Kallikrein 1-related peptidase b22|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027989|||http://purl.uniprot.org/annotation/PRO_0000027990|||http://purl.uniprot.org/annotation/PRO_5014309525 http://togogenome.org/gene/10090:Lypd1 ^@ http://purl.uniprot.org/uniprot/Q8BLC3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ GPI-anchor amidated glycine|||Ly6/PLAUR domain-containing protein 1|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000226743|||http://purl.uniprot.org/annotation/PRO_0000226744 http://togogenome.org/gene/10090:Btrc ^@ http://purl.uniprot.org/uniprot/A0A286YDT6|||http://purl.uniprot.org/uniprot/Q3ULA2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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_0000393571|||http://purl.uniprot.org/annotation/VSP_053208 http://togogenome.org/gene/10090:Lrig3 ^@ http://purl.uniprot.org/uniprot/Q6P1C6 ^@ 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|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Basic and acidic residues|||Disordered|||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 3|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014832 http://togogenome.org/gene/10090:Tgm7 ^@ http://purl.uniprot.org/uniprot/A2ART8 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent ^@ Transglutaminase-like ^@ http://togogenome.org/gene/10090:Reg3d ^@ http://purl.uniprot.org/uniprot/G3UWG6|||http://purl.uniprot.org/uniprot/Q9QUS9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ C-type lectin ^@ http://purl.uniprot.org/annotation/PRO_5015091565|||http://purl.uniprot.org/annotation/PRO_5015099933 http://togogenome.org/gene/10090:Or10a4 ^@ http://purl.uniprot.org/uniprot/Q7TRM9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdk5 ^@ http://purl.uniprot.org/uniprot/P49615|||http://purl.uniprot.org/uniprot/Q543F6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site ^@ Cyclin-dependent kinase 5|||Loss of tyrosine phosphorylations by CABLES1 and ABL1; decreased activity.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by ABL1, EPHA4 and FYN|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085785 http://togogenome.org/gene/10090:Vmn1r87 ^@ http://purl.uniprot.org/uniprot/Q8R255 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical|||Vomeronasal type-1 receptor ^@ http://purl.uniprot.org/annotation/PRO_5015099331 http://togogenome.org/gene/10090:Rnf225 ^@ http://purl.uniprot.org/uniprot/Q9D7D1 ^@ 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_0000431310 http://togogenome.org/gene/10090:Kiss1 ^@ http://purl.uniprot.org/uniprot/I0J0X7|||http://purl.uniprot.org/uniprot/Q6Y4S4 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Modified Residue|||Peptide|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||Essential for receptor binding and receptor activation|||In isoform 2.|||Kisspeptin-10|||Metastasis-suppressor KiSS-1|||Metastin|||Phosphotyrosine|||Tyrosine amide ^@ http://purl.uniprot.org/annotation/PRO_0000021552|||http://purl.uniprot.org/annotation/PRO_0000021553|||http://purl.uniprot.org/annotation/PRO_0000021554|||http://purl.uniprot.org/annotation/PRO_5003629519|||http://purl.uniprot.org/annotation/VSP_012957 http://togogenome.org/gene/10090:Sema3d ^@ http://purl.uniprot.org/uniprot/Q8BH34 ^@ 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 ^@ Basic residues|||Disordered|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||PSI|||Sema|||Semaphorin-3D ^@ http://purl.uniprot.org/annotation/PRO_0000042161 http://togogenome.org/gene/10090:Prl ^@ http://purl.uniprot.org/uniprot/Q3TT66|||http://purl.uniprot.org/uniprot/Q9CPQ2 ^@ Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Signal Peptide ^@ Prolactin ^@ http://purl.uniprot.org/annotation/PRO_5010843320|||http://purl.uniprot.org/annotation/PRO_5015099698 http://togogenome.org/gene/10090:Slc41a1 ^@ http://purl.uniprot.org/uniprot/Q8BJA2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Solute carrier family 41 member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000295112 http://togogenome.org/gene/10090:Or8c15 ^@ http://purl.uniprot.org/uniprot/K7N678 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dbil5 ^@ http://purl.uniprot.org/uniprot/O09035|||http://purl.uniprot.org/uniprot/Q545L5 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ ACB|||Diazepam-binding inhibitor-like 5 ^@ http://purl.uniprot.org/annotation/PRO_0000214024 http://togogenome.org/gene/10090:Krtap19-4 ^@ http://purl.uniprot.org/uniprot/Q925H7 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ 24 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 19-4 ^@ http://purl.uniprot.org/annotation/PRO_0000356214 http://togogenome.org/gene/10090:Shmt1 ^@ http://purl.uniprot.org/uniprot/P50431 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ N6-(pyridoxal phosphate)lysine|||Serine hydroxymethyltransferase, cytosolic ^@ http://purl.uniprot.org/annotation/PRO_0000113505 http://togogenome.org/gene/10090:Hacd2 ^@ http://purl.uniprot.org/uniprot/Q9D3B1 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Removed|||Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000349320 http://togogenome.org/gene/10090:Cystm1 ^@ http://purl.uniprot.org/uniprot/D3YWV2 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Ddhd2 ^@ http://purl.uniprot.org/uniprot/Q80Y98 ^@ 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 ^@ Basic and acidic residues|||DDHD|||Disordered|||In isoform 2.|||In isoform 3.|||Phospholipase DDHD2|||Phosphoserine|||SAM|||WWE ^@ http://purl.uniprot.org/annotation/PRO_0000309331|||http://purl.uniprot.org/annotation/VSP_029141|||http://purl.uniprot.org/annotation/VSP_029142|||http://purl.uniprot.org/annotation/VSP_029143|||http://purl.uniprot.org/annotation/VSP_029144 http://togogenome.org/gene/10090:Ints12 ^@ http://purl.uniprot.org/uniprot/Q9D168 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Strand|||Turn|||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_0000059314 http://togogenome.org/gene/10090:Nphp4 ^@ http://purl.uniprot.org/uniprot/P59240 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Nephrocystin-4|||Phosphoserine|||Polar residues|||Sufficient for basal bodies localization ^@ http://purl.uniprot.org/annotation/PRO_0000159770 http://togogenome.org/gene/10090:Wasf1 ^@ http://purl.uniprot.org/uniprot/Q8R5H6 ^@ 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 ^@ Actin-binding protein WASF1|||Asymmetric dimethylarginine; alternate|||Disordered|||Omega-N-methylarginine; alternate|||Phosphoserine|||Pro residues|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000188993 http://togogenome.org/gene/10090:Ednra ^@ http://purl.uniprot.org/uniprot/Q61614 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000012722 http://togogenome.org/gene/10090:Snorc ^@ http://purl.uniprot.org/uniprot/A0A0A7EP66|||http://purl.uniprot.org/uniprot/Q9CXL7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues|||Protein SNORC ^@ http://purl.uniprot.org/annotation/PRO_0000317642|||http://purl.uniprot.org/annotation/PRO_5035987127 http://togogenome.org/gene/10090:Ap1s3 ^@ http://purl.uniprot.org/uniprot/Q7TN05 ^@ Chain|||Molecule Processing ^@ Chain ^@ AP-1 complex subunit sigma-3 ^@ http://purl.uniprot.org/annotation/PRO_0000193802 http://togogenome.org/gene/10090:Eif3j2 ^@ http://purl.uniprot.org/uniprot/Q66JS6 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 3 subunit J-B|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Promotes stable association with the 40S ribosome|||Removed|||Sufficient for interaction with EIF3B ^@ http://purl.uniprot.org/annotation/PRO_0000123507 http://togogenome.org/gene/10090:Pheta2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Z2|||http://purl.uniprot.org/uniprot/Q14B98 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||F&H|||PH|||Sesquipedalian-2 ^@ http://purl.uniprot.org/annotation/PRO_0000254134 http://togogenome.org/gene/10090:Or2t45 ^@ http://purl.uniprot.org/uniprot/Q8VFG7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tph2 ^@ http://purl.uniprot.org/uniprot/Q8CGV2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ ACT|||Basic and acidic residues|||Disordered|||Phosphoserine|||Tryptophan 5-hydroxylase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000205575 http://togogenome.org/gene/10090:1600014C23Rik ^@ http://purl.uniprot.org/uniprot/Q9DAX4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Stimate ^@ http://purl.uniprot.org/uniprot/Q3UF25 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||GXXXG motif|||Helical|||Required for localization in the endoplasmic reticulum|||Store-operated calcium entry regulator STIMATE ^@ http://purl.uniprot.org/annotation/PRO_0000243916 http://togogenome.org/gene/10090:Zranb1 ^@ http://purl.uniprot.org/uniprot/Q7M760 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Zinc Finger ^@ ANK 1|||ANK 2|||Disordered|||Nucleophile|||OTU|||Polar residues|||Proton acceptor|||RanBP2-type 1|||RanBP2-type 2|||RanBP2-type 3|||Ubiquitin thioesterase Zranb1 ^@ http://purl.uniprot.org/annotation/PRO_0000361554 http://togogenome.org/gene/10090:Krt6a ^@ http://purl.uniprot.org/uniprot/P50446 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type II cytoskeletal 6A|||Linker 1|||Linker 12|||Polar residues|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063736 http://togogenome.org/gene/10090:Tcta ^@ http://purl.uniprot.org/uniprot/A0A0A6YXI4|||http://purl.uniprot.org/uniprot/Q8VEA7 ^@ Chain|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Removed|||T-cell leukemia translocation-altered gene protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000301679 http://togogenome.org/gene/10090:Mob2 ^@ http://purl.uniprot.org/uniprot/Q3TYF8|||http://purl.uniprot.org/uniprot/Q8VI63 ^@ 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.|||MOB kinase activator 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000193569|||http://purl.uniprot.org/annotation/VSP_012300 http://togogenome.org/gene/10090:Gm960 ^@ http://purl.uniprot.org/uniprot/A0A182DWE7 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Cldn9 ^@ http://purl.uniprot.org/uniprot/Q9Z0S7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Claudin-9|||Cytoplasmic|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000144756 http://togogenome.org/gene/10090:Tektip1 ^@ http://purl.uniprot.org/uniprot/A6H6Q4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Tektin bundle-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000332197 http://togogenome.org/gene/10090:Ldha ^@ http://purl.uniprot.org/uniprot/A0A1B0GSX0|||http://purl.uniprot.org/uniprot/P06151|||http://purl.uniprot.org/uniprot/Q564E2 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||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|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000168414 http://togogenome.org/gene/10090:Rbck1 ^@ http://purl.uniprot.org/uniprot/Q9WUB0 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Disordered|||IBR-type|||Interaction with IRF3|||Interaction with RNF31|||Interaction with TAB2|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine|||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_0000056296 http://togogenome.org/gene/10090:Samd8 ^@ http://purl.uniprot.org/uniprot/Q14AQ4|||http://purl.uniprot.org/uniprot/Q9DA37 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||SAM|||Sphingomyelin synthase-related protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000221081 http://togogenome.org/gene/10090:Vmn1r195 ^@ http://purl.uniprot.org/uniprot/Q5SVD6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fbxl2 ^@ http://purl.uniprot.org/uniprot/Q4VA21|||http://purl.uniprot.org/uniprot/Q8BH16 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Abolished phosphorylation by GSK3B, preventing ubiquitination by the SCF(FBXO3) complex.|||CAAX motif|||F-box|||F-box/LRR-repeat protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||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|||Phosphothreonine; by GSK3-beta|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000119841 http://togogenome.org/gene/10090:G3bp1 ^@ http://purl.uniprot.org/uniprot/P97855 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ Acidic disordered region|||Acidic residues|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Dimethylated arginine; alternate|||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|||N6-acetyllysine; alternate|||NTF2|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||RG-rich region|||RRM|||Ras GTPase-activating protein-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000194799 http://togogenome.org/gene/10090:Maea ^@ http://purl.uniprot.org/uniprot/Q4VC33 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ CTLH|||E3 ubiquitin-protein transferase MAEA|||Essential for ubiquitin ligase activity|||Extracellular and involved in cell to cell contact|||In isoform 2.|||LisH|||Phosphothreonine|||RING-Gid-type ^@ http://purl.uniprot.org/annotation/PRO_0000284938|||http://purl.uniprot.org/annotation/VSP_024797 http://togogenome.org/gene/10090:Tsen2 ^@ http://purl.uniprot.org/uniprot/Q6P7W5 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||tRNA-splicing endonuclease subunit Sen2 ^@ http://purl.uniprot.org/annotation/PRO_0000109453 http://togogenome.org/gene/10090:Sdcbp ^@ http://purl.uniprot.org/uniprot/O08992|||http://purl.uniprot.org/uniprot/Q3TMX0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Transmembrane ^@ Helical|||Interaction with PDCD6IP|||LYPX(n)L motif 1|||LYPX(n)L motif 2|||LYPX(n)L motif 3|||N-acetylserine|||No loss of interaction with PDCD6IP. Loss of interaction with PDCD6IP; when associated with 4-A--A-5 and 47-A--A-48.|||No loss of interaction with PDCD6IP. Loss of interaction with PDCD6IP; when associated with 4-A--A-5 and 51-A--A-52.|||No loss of interaction with PDCD6IP. Loss of interaction with PDCD6IP; when associated with 46-A--A-47 and 50-A--A-51.|||PDZ|||PDZ 1|||PDZ 2|||Phosphoserine|||Phosphotyrosine|||Removed|||Syntenin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000184002 http://togogenome.org/gene/10090:Sh3bgr ^@ http://purl.uniprot.org/uniprot/Q9WUZ7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Motif|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||SH3 domain-binding glutamic acid-rich protein|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000220744 http://togogenome.org/gene/10090:Ezh2 ^@ http://purl.uniprot.org/uniprot/Q3TZH6|||http://purl.uniprot.org/uniprot/Q571L5|||http://purl.uniprot.org/uniprot/Q61188|||http://purl.uniprot.org/uniprot/Q6AXH7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Abrogates interaction with EED.|||Acidic residues|||Basic and acidic residues|||CXC|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase EZH2|||In isoform ENX-1B.|||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|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000213993|||http://purl.uniprot.org/annotation/VSP_001501 http://togogenome.org/gene/10090:Gm38667 ^@ http://purl.uniprot.org/uniprot/Q8K490 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Cadherin C-terminal catenin-binding|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Polr2i ^@ http://purl.uniprot.org/uniprot/P60898 ^@ 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_0000121468 http://togogenome.org/gene/10090:Pim1 ^@ http://purl.uniprot.org/uniprot/P06803 ^@ 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|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Loss of autophosphorylation and kinase activity.|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase pim-1 ^@ http://purl.uniprot.org/annotation/PRO_0000043351|||http://purl.uniprot.org/annotation/VSP_059830 http://togogenome.org/gene/10090:Gpr37l1 ^@ http://purl.uniprot.org/uniprot/A1L151|||http://purl.uniprot.org/uniprot/Q99JG2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 37-like 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-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000012797 http://togogenome.org/gene/10090:Tmem14a ^@ http://purl.uniprot.org/uniprot/D3YV08|||http://purl.uniprot.org/uniprot/P56983|||http://purl.uniprot.org/uniprot/Q9CYF4 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 14A ^@ http://purl.uniprot.org/annotation/PRO_0000221170 http://togogenome.org/gene/10090:Lsp1 ^@ http://purl.uniprot.org/uniprot/A0A1B0GRF5|||http://purl.uniprot.org/uniprot/A2A6J4|||http://purl.uniprot.org/uniprot/A2A6J7|||http://purl.uniprot.org/uniprot/P19973 ^@ 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 ^@ Basic and acidic residues|||Complete loss of phosphorylation by MAPKAPK2, partial loss of phosphorylation by PKA, no effect on phosphorylation by PKC and CaMK2.|||Disordered|||In isoform 2.|||Lymphocyte-specific protein 1|||N6-acetyllysine|||No effect on phosphorylation by PKC, PKA, MAPKAPK2 and CaMK2.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by MAPKAPK2|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084504|||http://purl.uniprot.org/annotation/VSP_004313 http://togogenome.org/gene/10090:Zfp35 ^@ http://purl.uniprot.org/uniprot/P15620|||http://purl.uniprot.org/uniprot/Q3V142 ^@ 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 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|||Zinc finger protein 271 ^@ http://purl.uniprot.org/annotation/PRO_0000047497 http://togogenome.org/gene/10090:Zcchc17 ^@ http://purl.uniprot.org/uniprot/Q3TG23|||http://purl.uniprot.org/uniprot/Q9ESX4 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||CCHC-type|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||S1 motif|||Zinc finger CCHC domain-containing protein 17 ^@ http://purl.uniprot.org/annotation/PRO_0000096904|||http://purl.uniprot.org/annotation/VSP_015309 http://togogenome.org/gene/10090:Dad1 ^@ http://purl.uniprot.org/uniprot/P61804 ^@ 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|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1|||Helical|||Lumenal|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000124011 http://togogenome.org/gene/10090:Or4c124 ^@ http://purl.uniprot.org/uniprot/Q8VEX7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Commd2 ^@ http://purl.uniprot.org/uniprot/Q497T6|||http://purl.uniprot.org/uniprot/Q8BXC6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ COMM|||COMM domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000077387 http://togogenome.org/gene/10090:Srrm4 ^@ http://purl.uniprot.org/uniprot/J9QHX6|||http://purl.uniprot.org/uniprot/Q8BKA3 ^@ 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|||Basic residues|||Disordered|||In isoform 2.|||Polar residues|||Serine/arginine repetitive matrix protein 4|||Serine/arginine repetitive matrix protein C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000311912|||http://purl.uniprot.org/annotation/VSP_029639 http://togogenome.org/gene/10090:Ankrd28 ^@ http://purl.uniprot.org/uniprot/Q505D1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ 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|||Phosphoserine|||Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A ^@ http://purl.uniprot.org/annotation/PRO_0000244571 http://togogenome.org/gene/10090:Pls1 ^@ http://purl.uniprot.org/uniprot/Q3V0K9|||http://purl.uniprot.org/uniprot/Q3V3X1 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ 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 1|||EF-hand 2|||N-acetylmethionine|||Plastin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000364188 http://togogenome.org/gene/10090:Jakmip3 ^@ http://purl.uniprot.org/uniprot/Q5DTN8 ^@ 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 and isoform 3.|||In isoform 2.|||In isoform 3.|||Janus kinase and microtubule-interacting protein 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000323012|||http://purl.uniprot.org/annotation/VSP_032000|||http://purl.uniprot.org/annotation/VSP_032001|||http://purl.uniprot.org/annotation/VSP_032002|||http://purl.uniprot.org/annotation/VSP_032003 http://togogenome.org/gene/10090:Pwwp2a ^@ http://purl.uniprot.org/uniprot/Q69Z61 ^@ 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.|||Interaction with HDAC1 and MTA1|||Interaction with the H2A.Z/H2AZ1|||PWWP|||PWWP domain-containing protein 2A|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000311364|||http://purl.uniprot.org/annotation/VSP_029549|||http://purl.uniprot.org/annotation/VSP_029550|||http://purl.uniprot.org/annotation/VSP_029551 http://togogenome.org/gene/10090:Or52m1 ^@ http://purl.uniprot.org/uniprot/E9Q546 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Umad1 ^@ http://purl.uniprot.org/uniprot/E0CX23|||http://purl.uniprot.org/uniprot/E0CXP6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||UMA ^@ http://togogenome.org/gene/10090:Tmem190 ^@ http://purl.uniprot.org/uniprot/Q9D2E9 ^@ 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|||P-type|||Polar residues|||Transmembrane protein 190 ^@ http://purl.uniprot.org/annotation/PRO_0000312283 http://togogenome.org/gene/10090:Elmod2 ^@ http://purl.uniprot.org/uniprot/Q8BGF6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ ELMO|||ELMO domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000225018 http://togogenome.org/gene/10090:Myoc ^@ http://purl.uniprot.org/uniprot/O70624|||http://purl.uniprot.org/uniprot/Q05AC1 ^@ Binding Site|||Chain|||Coiled-Coil|||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 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn ^@ Cleavage; by CAPN2|||Disordered|||In strain: BALB/cJ.|||Myocilin|||Myocilin, C-terminal fragment|||Myocilin, N-terminal fragment|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000020086|||http://purl.uniprot.org/annotation/PRO_0000428743|||http://purl.uniprot.org/annotation/PRO_0000428744|||http://purl.uniprot.org/annotation/PRO_5014306678 http://togogenome.org/gene/10090:Brcc3 ^@ http://purl.uniprot.org/uniprot/P46737 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||JAMM motif|||Lys-63-specific deubiquitinase BRCC36|||MPN|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213968|||http://purl.uniprot.org/annotation/VSP_037260 http://togogenome.org/gene/10090:Mup10 ^@ http://purl.uniprot.org/uniprot/A2BIN1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5015086049 http://togogenome.org/gene/10090:Gsta5 ^@ http://purl.uniprot.org/uniprot/E9Q6L7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ GST C-terminal|||GST N-terminal ^@ http://togogenome.org/gene/10090:Sipa1l3 ^@ http://purl.uniprot.org/uniprot/G3X9J0 ^@ 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|||N6-acetyllysine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rap-GAP|||Signal-induced proliferation-associated 1-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000435476 http://togogenome.org/gene/10090:Btbd18 ^@ http://purl.uniprot.org/uniprot/A0A0A6YY25 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ BTB|||BTB/POZ domain-containing protein 18|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000441744 http://togogenome.org/gene/10090:Jpt1 ^@ http://purl.uniprot.org/uniprot/P97825 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||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_0000054919|||http://purl.uniprot.org/annotation/PRO_0000424488 http://togogenome.org/gene/10090:Dyrk4 ^@ http://purl.uniprot.org/uniprot/Q8BI55 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Dual specificity tyrosine-phosphorylation-regulated kinase 4|||In isoform 2.|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000291539|||http://purl.uniprot.org/annotation/VSP_052456|||http://purl.uniprot.org/annotation/VSP_052457 http://togogenome.org/gene/10090:Zcchc3 ^@ http://purl.uniprot.org/uniprot/Q8BPK2 ^@ 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|||CCHC-type 1|||CCHC-type 2|||Disordered|||Phosphotyrosine|||Zinc finger CCHC domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000446169 http://togogenome.org/gene/10090:Zdhhc1 ^@ http://purl.uniprot.org/uniprot/Q8R0N9 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Disordered|||Helical|||Lumenal|||Mediates interaction with STING1|||Palmitoyltransferase ZDHHC1|||Polar residues|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212858 http://togogenome.org/gene/10090:Zg16 ^@ http://purl.uniprot.org/uniprot/Q8K0C5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Jacalin-type lectin|||Zymogen granule membrane protein 16 ^@ http://purl.uniprot.org/annotation/PRO_0000017571 http://togogenome.org/gene/10090:Psma2 ^@ http://purl.uniprot.org/uniprot/P49722 ^@ 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-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Proteasome subunit alpha type-2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000124078 http://togogenome.org/gene/10090:Ugt2a2 ^@ http://purl.uniprot.org/uniprot/Q6PDD0 ^@ 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|||UDP-glucuronosyltransferase 2A2 ^@ http://purl.uniprot.org/annotation/PRO_0000299144 http://togogenome.org/gene/10090:Cfap73 ^@ http://purl.uniprot.org/uniprot/J3QPZ5 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Cilia- and flagella-associated protein 73 ^@ http://purl.uniprot.org/annotation/PRO_0000437481 http://togogenome.org/gene/10090:Cd276 ^@ http://purl.uniprot.org/uniprot/A6MDC5|||http://purl.uniprot.org/uniprot/Q8VE98 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||CD276 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000045802|||http://purl.uniprot.org/annotation/PRO_5009946539 http://togogenome.org/gene/10090:Fibcd1 ^@ http://purl.uniprot.org/uniprot/A2AV25 ^@ 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|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000294317|||http://purl.uniprot.org/annotation/VSP_026621 http://togogenome.org/gene/10090:Ikzf5 ^@ http://purl.uniprot.org/uniprot/Q8BU00 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 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.|||In isoform 3.|||Polar residues|||Zinc finger protein Pegasus ^@ http://purl.uniprot.org/annotation/PRO_0000299472|||http://purl.uniprot.org/annotation/VSP_027692|||http://purl.uniprot.org/annotation/VSP_027693|||http://purl.uniprot.org/annotation/VSP_027694 http://togogenome.org/gene/10090:Agxt2 ^@ http://purl.uniprot.org/uniprot/Q3UEG6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ Alanine--glyoxylate aminotransferase 2, mitochondrial|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000283753 http://togogenome.org/gene/10090:Fcamr ^@ http://purl.uniprot.org/uniprot/Q2TB54 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||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 V-type|||In isoform 2.|||Mediates immunoglobulin Fc fragment-binding|||N-linked (GlcNAc...) asparagine|||Polar residues|||Prevents receptor internalization. ^@ http://purl.uniprot.org/annotation/PRO_0000331484|||http://purl.uniprot.org/annotation/VSP_033233 http://togogenome.org/gene/10090:Prkar2b ^@ http://purl.uniprot.org/uniprot/P31324 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Dimerization and phosphorylation|||Phosphoserine|||cAMP-dependent protein kinase type II-beta regulatory subunit ^@ http://purl.uniprot.org/annotation/PRO_0000205391 http://togogenome.org/gene/10090:Gm9 ^@ http://purl.uniprot.org/uniprot/Q3UKW5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Secisbp2 ^@ http://purl.uniprot.org/uniprot/Q3TGQ4|||http://purl.uniprot.org/uniprot/Q3U1C4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Ribosomal protein eL8/eL30/eS12/Gadd45 ^@ http://togogenome.org/gene/10090:Or8b44 ^@ http://purl.uniprot.org/uniprot/Q7TRC7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Retnla ^@ http://purl.uniprot.org/uniprot/Q8JZM3|||http://purl.uniprot.org/uniprot/Q9EP95 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Resistin-like alpha ^@ http://purl.uniprot.org/annotation/PRO_0000030343|||http://purl.uniprot.org/annotation/PRO_5014312164 http://togogenome.org/gene/10090:Gtsf2 ^@ http://purl.uniprot.org/uniprot/Q80Y74 ^@ Domain Extent|||Region ^@ Domain Extent ^@ CHHC U11-48K-type ^@ http://togogenome.org/gene/10090:Or4d10c ^@ http://purl.uniprot.org/uniprot/Q8VG74 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Top3b ^@ http://purl.uniprot.org/uniprot/Q3UJF5|||http://purl.uniprot.org/uniprot/Q9Z321 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic residues|||DNA topoisomerase 3-beta-1|||Disordered|||O-(5'-phospho-DNA)-tyrosine intermediate|||Toprim ^@ http://purl.uniprot.org/annotation/PRO_0000145193 http://togogenome.org/gene/10090:Cbfa2t3 ^@ http://purl.uniprot.org/uniprot/B7ZP57|||http://purl.uniprot.org/uniprot/E9QM80|||http://purl.uniprot.org/uniprot/O54972 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with HIF1A|||Interaction with ZBTB33|||MYND-type|||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|||Pro residues|||Protein CBFA2T3|||TAFH ^@ http://purl.uniprot.org/annotation/PRO_0000307174|||http://purl.uniprot.org/annotation/VSP_028626|||http://purl.uniprot.org/annotation/VSP_028627 http://togogenome.org/gene/10090:Rlf ^@ http://purl.uniprot.org/uniprot/A2A7F4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Bysl ^@ http://purl.uniprot.org/uniprot/O54825 ^@ 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|||Bystin|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000186115 http://togogenome.org/gene/10090:Ctsd ^@ http://purl.uniprot.org/uniprot/P18242|||http://purl.uniprot.org/uniprot/Q3UCD9 ^@ 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|||Cathepsin D|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Peptidase A1 ^@ http://purl.uniprot.org/annotation/PRO_0000025953|||http://purl.uniprot.org/annotation/PRO_0000025954|||http://purl.uniprot.org/annotation/PRO_5014309144 http://togogenome.org/gene/10090:Gm10352 ^@ http://purl.uniprot.org/uniprot/B2RWR6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||RRM ^@ http://togogenome.org/gene/10090:Tcap ^@ http://purl.uniprot.org/uniprot/O70548|||http://purl.uniprot.org/uniprot/Q545G3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Telethonin ^@ http://purl.uniprot.org/annotation/PRO_0000072484 http://togogenome.org/gene/10090:Vmn1r224 ^@ http://purl.uniprot.org/uniprot/E9PWK2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnfn ^@ http://purl.uniprot.org/uniprot/Q6PCW6 ^@ Chain|||Molecule Processing ^@ Chain ^@ Cornifelin ^@ http://purl.uniprot.org/annotation/PRO_0000261196 http://togogenome.org/gene/10090:Ext2 ^@ http://purl.uniprot.org/uniprot/P70428|||http://purl.uniprot.org/uniprot/Q3UDB5 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Exostosin GT47|||Exostosin-2|||Glycosyl transferase 64|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149652 http://togogenome.org/gene/10090:Pnoc ^@ http://purl.uniprot.org/uniprot/B7ZMX9|||http://purl.uniprot.org/uniprot/Q543U6|||http://purl.uniprot.org/uniprot/Q64387 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Peptide|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 1|||2|||3|||3 X 6 AA tandem repeats of D-A-E-P-G-A|||Disordered|||In isoform Long.|||Nociceptin|||Nocistatin|||Orphanin FQ2 ^@ http://purl.uniprot.org/annotation/PRO_0000008330|||http://purl.uniprot.org/annotation/PRO_0000008331|||http://purl.uniprot.org/annotation/PRO_0000008332|||http://purl.uniprot.org/annotation/PRO_0000008333|||http://purl.uniprot.org/annotation/PRO_0000008334|||http://purl.uniprot.org/annotation/PRO_5014300204|||http://purl.uniprot.org/annotation/PRO_5014309603|||http://purl.uniprot.org/annotation/VSP_001446 http://togogenome.org/gene/10090:Tgs1 ^@ http://purl.uniprot.org/uniprot/Q923W1 ^@ 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|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Trimethylguanosine synthase ^@ http://purl.uniprot.org/annotation/PRO_0000204469 http://togogenome.org/gene/10090:Or5ac24 ^@ http://purl.uniprot.org/uniprot/Q8VGP9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Angpt2 ^@ http://purl.uniprot.org/uniprot/B9EHQ4|||http://purl.uniprot.org/uniprot/O35608 ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Angiopoietin-2|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009114|||http://purl.uniprot.org/annotation/PRO_5014300275 http://togogenome.org/gene/10090:Abcg8 ^@ http://purl.uniprot.org/uniprot/E9Q0P2|||http://purl.uniprot.org/uniprot/Q7TSR6|||http://purl.uniprot.org/uniprot/Q9DBM0 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ ABC transmembrane type-2|||ABC transporter|||ATP-binding cassette sub-family G member 8|||Abolishes N-glycosylation.|||Abolishes cholesterol transport activity, and nearly abolishes plant sterol transport.|||Abolishes expression at the apical cell membrane. Strongly decreases cholesterol secretion into bile.|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||Mildly decreases cholesterol transport. No effect on plant sterol transport.|||N-linked (GlcNAc...) asparagine|||No effect on ATP-binding and on expression of both ABCG5 and ABCG8. No effect on sterol transport.|||No effect on sterol transport.|||No effect on sterol transport; when associated with I-214.|||No effect on sterol transport; when associated with S-216. ^@ http://purl.uniprot.org/annotation/PRO_0000093397|||http://purl.uniprot.org/annotation/VSP_000053 http://togogenome.org/gene/10090:Mcpt9 ^@ http://purl.uniprot.org/uniprot/O35164 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Mast cell protease 9|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027459|||http://purl.uniprot.org/annotation/PRO_0000027460 http://togogenome.org/gene/10090:Gtse1 ^@ http://purl.uniprot.org/uniprot/Q542Q3|||http://purl.uniprot.org/uniprot/Q8R080 ^@ 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|||G2 and S phase-expressed protein 1|||G2 and S phase-expressed protein 1 N-terminal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000083876 http://togogenome.org/gene/10090:Diaph1 ^@ http://purl.uniprot.org/uniprot/E9PV41|||http://purl.uniprot.org/uniprot/F6XC54|||http://purl.uniprot.org/uniprot/O08808 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Basic and acidic residues|||DAD|||Disordered|||FH1|||FH2|||GBD/FH3|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein diaphanous homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000194894 http://togogenome.org/gene/10090:Zfp697 ^@ http://purl.uniprot.org/uniprot/G5E8C0|||http://purl.uniprot.org/uniprot/Q569E7 ^@ 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 ^@ Acidic residues|||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|||Zinc finger protein 697 ^@ http://purl.uniprot.org/annotation/PRO_0000305139 http://togogenome.org/gene/10090:Arl14epl ^@ http://purl.uniprot.org/uniprot/Q3UKZ7 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ ARL14 effector protein-like|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000419647 http://togogenome.org/gene/10090:Syncrip ^@ http://purl.uniprot.org/uniprot/A0A0R4J259|||http://purl.uniprot.org/uniprot/G3UZ48|||http://purl.uniprot.org/uniprot/Q3TRV3|||http://purl.uniprot.org/uniprot/Q7TMK9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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; alternate|||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.|||Interaction with APOBEC1|||Interaction with SMN|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine; alternate|||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_0000081868|||http://purl.uniprot.org/annotation/VSP_009585|||http://purl.uniprot.org/annotation/VSP_009586 http://togogenome.org/gene/10090:Serpina1e ^@ http://purl.uniprot.org/uniprot/Q00898 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide|||Site ^@ Alpha-1-antitrypsin 1-5|||N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000032392 http://togogenome.org/gene/10090:Ints9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0J5|||http://purl.uniprot.org/uniprot/Q8K114 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Crosslink|||Domain Extent|||Region|||Splice Variant ^@ Beta-Casp|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Integrator complex subunit 9 ^@ http://purl.uniprot.org/annotation/PRO_0000259559|||http://purl.uniprot.org/annotation/VSP_021470|||http://purl.uniprot.org/annotation/VSP_021471 http://togogenome.org/gene/10090:Spink6 ^@ http://purl.uniprot.org/uniprot/Q8BT20 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Signal Peptide|||Site ^@ Kazal-like|||Pyrrolidone carboxylic acid|||Reactive bond|||Serine protease inhibitor Kazal-type 6 ^@ http://purl.uniprot.org/annotation/PRO_0000016576 http://togogenome.org/gene/10090:Jakmip2 ^@ http://purl.uniprot.org/uniprot/D3YXK0 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Janus kinase and microtubule-interacting protein C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Alyref ^@ http://purl.uniprot.org/uniprot/O08583 ^@ 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 ^@ Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Citrulline|||Dimethylated arginine; alternate|||Disordered|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-methyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||RRM|||Removed|||Sufficient for RNA-binding, interaction with NXF1-NXT1 heterodimer|||THO complex subunit 4 ^@ http://purl.uniprot.org/annotation/PRO_0000081975|||http://purl.uniprot.org/annotation/VSP_008597 http://togogenome.org/gene/10090:Esco1 ^@ http://purl.uniprot.org/uniprot/Q3UKT9|||http://purl.uniprot.org/uniprot/Q69Z69 ^@ Binding Site|||Chain|||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|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||CCHH-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetyltransferase ESCO acetyl-transferase|||N-acetyltransferase ESCO zinc-finger|||N-acetyltransferase ESCO1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000074540|||http://purl.uniprot.org/annotation/VSP_014031|||http://purl.uniprot.org/annotation/VSP_014032|||http://purl.uniprot.org/annotation/VSP_014033|||http://purl.uniprot.org/annotation/VSP_014034 http://togogenome.org/gene/10090:Mesp2 ^@ http://purl.uniprot.org/uniprot/A6H5V4|||http://purl.uniprot.org/uniprot/O08574 ^@ 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 ^@ BHLH|||Disordered|||Localizes in nucleus and cytoplasm. Localizes mainly in cytoplasm; when associated with 145-A--A-150.|||Localizes in nucleus and cytoplasm. Localizes mainly in cytoplasm; when associated with 70-A--A-73.|||May contain a degradation domain|||Mesoderm posterior protein 2|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000296302 http://togogenome.org/gene/10090:Rab26 ^@ http://purl.uniprot.org/uniprot/Q148R0|||http://purl.uniprot.org/uniprot/Q504M8 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Motif|||Region ^@ Disordered|||Effector region|||Ras-related protein Rab-26|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121219 http://togogenome.org/gene/10090:Rubcn ^@ http://purl.uniprot.org/uniprot/Q80U62 ^@ 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 4.|||In isoform 3 and isoform 4.|||In isoform 4.|||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_0000050737|||http://purl.uniprot.org/annotation/VSP_017110|||http://purl.uniprot.org/annotation/VSP_017111|||http://purl.uniprot.org/annotation/VSP_039474 http://togogenome.org/gene/10090:Pias1 ^@ http://purl.uniprot.org/uniprot/O88907|||http://purl.uniprot.org/uniprot/Q2M4G9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ 1|||2|||3; approximate|||4 X 4 AA repeats of N-T-S-L|||4; approximate|||Disordered|||E3 SUMO-protein ligase PIAS1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||LXXLL motif|||Loss of promotion of EKLF sumoylation.|||Loss of promotion of EKLF sumoylation; when associated with G-346 and A-356.|||Loss of promotion of EKLF sumoylation; when associated with G-346 and G-351.|||Loss of promotion of EKLF sumoylation; when associated with G-351 and A-356.|||Loss of promotion of NCOA2 sumoylation. No effect on interaction with MSX1 or localization of either protein at the nuclear periphery.|||N-acetylalanine|||No effect on interaction with MSX1 or localization of either protein at the nuclear periphery.|||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_0000218975 http://togogenome.org/gene/10090:Fgf10 ^@ http://purl.uniprot.org/uniprot/O35565 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ Fibroblast growth factor 10|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000008982 http://togogenome.org/gene/10090:Sptbn2 ^@ http://purl.uniprot.org/uniprot/Q68FG2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Npas4 ^@ http://purl.uniprot.org/uniprot/Q8BGD7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic motif; degenerate|||Disordered|||Helix-loop-helix motif|||Neuronal PAS domain-containing protein 4|||PAC|||PAS 1|||PAS 2|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000248223 http://togogenome.org/gene/10090:Csf2rb ^@ http://purl.uniprot.org/uniprot/P26955 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Box 1 motif|||Cytokine receptor common subunit beta|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010863 http://togogenome.org/gene/10090:Nova1 ^@ http://purl.uniprot.org/uniprot/Q9JKN6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||KH 1|||KH 2|||KH 3|||Phosphoserine|||RNA-binding protein Nova-1|||Required for RNA binding|||Strongly decreases RNA-binding. ^@ http://purl.uniprot.org/annotation/PRO_0000050117 http://togogenome.org/gene/10090:Dctpp1 ^@ http://purl.uniprot.org/uniprot/Q9QY93 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand ^@ Disordered|||Loss of activity.|||N-acetylserine|||Phosphoserine|||Reduces affinity for substrate and catalytic activity by about 50%.|||Removed|||dCTP pyrophosphatase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000291770 http://togogenome.org/gene/10090:Thbs3 ^@ http://purl.uniprot.org/uniprot/Q05895 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||Disordered|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3|||Interchain|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||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|||Thrombospondin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000035850 http://togogenome.org/gene/10090:Vipas39 ^@ http://purl.uniprot.org/uniprot/Q8BGQ1 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Spermatogenesis-defective protein 39 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089936|||http://purl.uniprot.org/annotation/VSP_009285 http://togogenome.org/gene/10090:Cldn6 ^@ http://purl.uniprot.org/uniprot/Q0GH64|||http://purl.uniprot.org/uniprot/Q9Z262 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Claudin|||Claudin-6|||Cytoplasmic|||Extracellular|||Helical|||Interactions with TJP1, TJP2 and TJP3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000144749|||http://purl.uniprot.org/annotation/PRO_5014306734 http://togogenome.org/gene/10090:Arhgap35 ^@ http://purl.uniprot.org/uniprot/B2RTN5|||http://purl.uniprot.org/uniprot/Q3UVZ8|||http://purl.uniprot.org/uniprot/Q8CCL8|||http://purl.uniprot.org/uniprot/Q91YM2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region ^@ Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. Affects polarized cell migration. Increases RhoGAP catalytic activity.|||Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. No effect on polarized cell migration.|||Basic and acidic residues|||Basic residues|||Disordered|||FF|||FF 1|||FF 2|||FF 3|||FF 4|||Has GTPase activity, required for proper localization|||In ENU mutant Arhgap35-D34; mutant animals show hypodysplastic kidneys and neural tube closure defects; the number of ciliated cells and cilia average length are drastically reduced in the proximal tubules. Results in loss of activation of GTP hydrolysis.|||PG1 pseudoGTPase|||PG2 pseudoGTPase|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ABL2 and PTK6|||Polar residues|||Pro residues|||Reduces phosphorylation by GSK3B by 50%. No effect on polarized cell migration.|||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_0000056731 http://togogenome.org/gene/10090:Acp6 ^@ http://purl.uniprot.org/uniprot/Q8BP40 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Chain|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Lysophosphatidic acid phosphatase type 6|||Mitochondrion|||Nucleophile|||Proton donor|||Substrate binding ^@ http://purl.uniprot.org/annotation/PRO_0000023966|||http://purl.uniprot.org/annotation/VSP_014123|||http://purl.uniprot.org/annotation/VSP_014124 http://togogenome.org/gene/10090:Ccr1 ^@ http://purl.uniprot.org/uniprot/P51675|||http://purl.uniprot.org/uniprot/Q8BMH9|||http://purl.uniprot.org/uniprot/Q8BVW4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000069231 http://togogenome.org/gene/10090:Eef2kmt ^@ http://purl.uniprot.org/uniprot/Q3UZW7 ^@ 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 ^@ In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Protein-lysine N-methyltransferase EEF2KMT ^@ http://purl.uniprot.org/annotation/PRO_0000076219|||http://purl.uniprot.org/annotation/VSP_033329|||http://purl.uniprot.org/annotation/VSP_033330 http://togogenome.org/gene/10090:Vdr ^@ http://purl.uniprot.org/uniprot/P48281 ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ 9aaTAD|||Disordered|||Hinge|||Interaction with coactivator LXXLL motif|||NR C4-type|||NR LBD|||Nuclear receptor|||Polar residues|||Vitamin D3 receptor ^@ http://purl.uniprot.org/annotation/PRO_0000053543 http://togogenome.org/gene/10090:Msh5 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZY8|||http://purl.uniprot.org/uniprot/Q9QUM7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict ^@ DNA mismatch repair proteins mutS family|||Disordered|||Mice carrying this mutation show atrophic ovaries without oocytes, but no other visible phenotype.|||MutS protein homolog 5|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000115203 http://togogenome.org/gene/10090:Dus4l ^@ http://purl.uniprot.org/uniprot/A0A0R4J016|||http://purl.uniprot.org/uniprot/Q32M08 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ DUS-like FMN-binding|||Proton donor|||tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]-like ^@ http://purl.uniprot.org/annotation/PRO_0000247348 http://togogenome.org/gene/10090:Zfp384 ^@ http://purl.uniprot.org/uniprot/E9Q1A5|||http://purl.uniprot.org/uniprot/E9QAR1|||http://purl.uniprot.org/uniprot/E9QAR4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:H2-Oa ^@ http://purl.uniprot.org/uniprot/B2RST7|||http://purl.uniprot.org/uniprot/Q9QWV1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5014298334|||http://purl.uniprot.org/annotation/PRO_5015099939 http://togogenome.org/gene/10090:B3galnt1 ^@ http://purl.uniprot.org/uniprot/Q920V1 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In strain: CAST/Ei.|||In strain: NJL/Msf, BLG2/Msf, MSM/Msf and SWN/Msf.|||In strain: SWN/Msf.|||Lumenal|||N-linked (GlcNAc...) asparagine|||UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000219154 http://togogenome.org/gene/10090:Plac9 ^@ http://purl.uniprot.org/uniprot/Q8K262 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Region|||Signal Peptide ^@ Disordered|||Placenta-specific protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000261406 http://togogenome.org/gene/10090:Nup188 ^@ http://purl.uniprot.org/uniprot/Q6ZQH8 ^@ 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 ^@ Disordered|||N-acetylalanine|||Nucleoporin NUP188|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000299173 http://togogenome.org/gene/10090:Efhb ^@ http://purl.uniprot.org/uniprot/Q8CDU5 ^@ 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 ^@ Disordered|||EF-hand 1|||EF-hand 2|||EF-hand domain-containing family member B|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000252095 http://togogenome.org/gene/10090:Stxbp5l ^@ http://purl.uniprot.org/uniprot/Q5DQR4 ^@ 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|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Results in attenuation of insulin secretion; increased protein stability.|||Syntaxin-binding protein 5-like|||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_0000051248|||http://purl.uniprot.org/annotation/VSP_016295|||http://purl.uniprot.org/annotation/VSP_016296|||http://purl.uniprot.org/annotation/VSP_016297|||http://purl.uniprot.org/annotation/VSP_016298|||http://purl.uniprot.org/annotation/VSP_016299|||http://purl.uniprot.org/annotation/VSP_016300 http://togogenome.org/gene/10090:Hcn2 ^@ http://purl.uniprot.org/uniprot/O88703 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes pH-sensitivity.|||Abolishes surface expression and channel activity.|||Cytoplasmic|||Decreases current amplitude.|||Disordered|||Disrupts channel closure.|||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|||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|||Reduces surface expression and abolishes channel activity.|||Reduces surface expression and decreases current amplitude.|||Reduces surface expression and disrupts channel closure.|||Shifts channel activation to more negative voltage, slows channel opening and speeds up channel closure. Reduces sensitivity to activation by cAMP.|||Shifts voltage dependence of activation to more negative values.|||Shifts voltage dependence of activation to more positive values and abolishes pH-sensitivity. ^@ http://purl.uniprot.org/annotation/PRO_0000054112 http://togogenome.org/gene/10090:Mrpl13 ^@ http://purl.uniprot.org/uniprot/Q9D1P0 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Large ribosomal subunit protein uL13m|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000133794 http://togogenome.org/gene/10090:Tmco2 ^@ http://purl.uniprot.org/uniprot/J3JS82 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Irak1 ^@ http://purl.uniprot.org/uniprot/B1AUW6|||http://purl.uniprot.org/uniprot/Q540G0|||http://purl.uniprot.org/uniprot/Q62406|||http://purl.uniprot.org/uniprot/Q8BR10 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes dimerization.|||Death|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Interleukin-1 receptor-associated kinase 1|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by IRAK4|||Phosphothreonine; by PKC/PRKCI|||Polar residues|||ProST region|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086031|||http://purl.uniprot.org/annotation/VSP_011852 http://togogenome.org/gene/10090:Far2 ^@ http://purl.uniprot.org/uniprot/Q7TNT2 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Fatty acyl-CoA reductase 2|||Helical|||In isoform 2.|||Peroxisomal ^@ http://purl.uniprot.org/annotation/PRO_0000261402|||http://purl.uniprot.org/annotation/VSP_021682 http://togogenome.org/gene/10090:Orc5 ^@ http://purl.uniprot.org/uniprot/Q9WUV0 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Origin recognition complex subunit 5 ^@ http://purl.uniprot.org/annotation/PRO_0000127093 http://togogenome.org/gene/10090:Tmem39b ^@ http://purl.uniprot.org/uniprot/Q810L4 ^@ 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 39B ^@ http://purl.uniprot.org/annotation/PRO_0000279233 http://togogenome.org/gene/10090:Pyurf ^@ http://purl.uniprot.org/uniprot/Q9D1C3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Transit Peptide ^@ Mitochondrion|||Protein preY, mitochondrial|||TRM112 ^@ http://purl.uniprot.org/annotation/PRO_0000246316 http://togogenome.org/gene/10090:Adck5 ^@ http://purl.uniprot.org/uniprot/E9PUK2|||http://purl.uniprot.org/uniprot/Q80V03 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ ABC1 atypical kinase-like|||Helical|||In isoform 2.|||Protein kinase|||Uncharacterized aarF domain-containing protein kinase 5 ^@ http://purl.uniprot.org/annotation/PRO_0000271801|||http://purl.uniprot.org/annotation/VSP_022358 http://togogenome.org/gene/10090:Tas2r116 ^@ http://purl.uniprot.org/uniprot/Q7M713 ^@ 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 116 ^@ http://purl.uniprot.org/annotation/PRO_0000248475 http://togogenome.org/gene/10090:Pms1 ^@ http://purl.uniprot.org/uniprot/Q8K119 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||HMG box|||Polar residues ^@ http://togogenome.org/gene/10090:Lrguk ^@ http://purl.uniprot.org/uniprot/Q9D5S7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ 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_0000326409 http://togogenome.org/gene/10090:Gm13287 ^@ http://purl.uniprot.org/uniprot/B1AYI3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015087047 http://togogenome.org/gene/10090:Rgs8 ^@ http://purl.uniprot.org/uniprot/D3Z289|||http://purl.uniprot.org/uniprot/Q8BXT1 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Phosphoserine|||RGS|||Regulator of G-protein signaling 8 ^@ http://purl.uniprot.org/annotation/PRO_0000204200 http://togogenome.org/gene/10090:Nphs2 ^@ http://purl.uniprot.org/uniprot/C0LL94|||http://purl.uniprot.org/uniprot/Q91X05 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Band 7|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Podocin|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000094036 http://togogenome.org/gene/10090:Shld2 ^@ http://purl.uniprot.org/uniprot/Q3UEN2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Mediates interaction with SHLD1|||Polar residues|||Shieldin complex subunit 2|||Sufficient for interaction with SHLD3 and MAD2L2 ^@ http://purl.uniprot.org/annotation/PRO_0000087162 http://togogenome.org/gene/10090:Zfyve21 ^@ http://purl.uniprot.org/uniprot/Q8VCM3 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Region|||Sequence Conflict|||Zinc Finger ^@ FYVE-type|||PH-like|||Zinc finger FYVE domain-containing protein 21 ^@ http://purl.uniprot.org/annotation/PRO_0000098721 http://togogenome.org/gene/10090:F8a ^@ http://purl.uniprot.org/uniprot/Q00558 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 40-kDa huntingtin-associated protein|||Disordered|||N-acetylalanine|||Not detected in nucleus. Redistributed in cytoplasm.|||Nuclear localization signal|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087160 http://togogenome.org/gene/10090:Gm14434 ^@ http://purl.uniprot.org/uniprot/A2ART4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Wfdc21 ^@ http://purl.uniprot.org/uniprot/Q8BTE6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Protein Wfdc21|||WAP; atypical ^@ http://purl.uniprot.org/annotation/PRO_5005940237 http://togogenome.org/gene/10090:Cpne8 ^@ http://purl.uniprot.org/uniprot/Q9DC53 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ C2 1|||C2 2|||Copine-8|||Phosphoserine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000144850 http://togogenome.org/gene/10090:Sprr2i ^@ http://purl.uniprot.org/uniprot/O70560 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1|||2|||3|||3 X 9 AA approximate tandem repeats|||Disordered|||Small proline-rich protein 2I ^@ http://purl.uniprot.org/annotation/PRO_0000150021 http://togogenome.org/gene/10090:Tex44 ^@ http://purl.uniprot.org/uniprot/Q9DA60 ^@ 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|||Pro residues|||Testis-expressed protein 44 ^@ http://purl.uniprot.org/annotation/PRO_0000309183 http://togogenome.org/gene/10090:Or5m12 ^@ http://purl.uniprot.org/uniprot/A2ASU7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Deup1 ^@ http://purl.uniprot.org/uniprot/Q7M6Y5|||http://purl.uniprot.org/uniprot/U5KUF9 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Centrosomal protein Cep63/Deup1 N-terminal|||Deuterosome assembly protein 1|||Disordered|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000297831|||http://purl.uniprot.org/annotation/VSP_041617 http://togogenome.org/gene/10090:Gatm ^@ http://purl.uniprot.org/uniprot/Q9D964 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Amidino-cysteine intermediate|||Glycine amidinotransferase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000001207 http://togogenome.org/gene/10090:Haus3 ^@ http://purl.uniprot.org/uniprot/Q8QZX2 ^@ 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 ^@ HAUS augmin-like complex subunit 3|||In isoform 2.|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000301952|||http://purl.uniprot.org/annotation/VSP_027887 http://togogenome.org/gene/10090:Vmn1r128 ^@ http://purl.uniprot.org/uniprot/L7N2B4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nans ^@ http://purl.uniprot.org/uniprot/Q99J77 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ AFP-like|||N6-acetyllysine|||Phosphoserine|||Sialic acid synthase ^@ http://purl.uniprot.org/annotation/PRO_0000438681 http://togogenome.org/gene/10090:Lrrc69 ^@ http://purl.uniprot.org/uniprot/Q9D9Q0 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 69 ^@ http://purl.uniprot.org/annotation/PRO_0000336073 http://togogenome.org/gene/10090:Adamts12 ^@ http://purl.uniprot.org/uniprot/Q3UXR3|||http://purl.uniprot.org/uniprot/Q811B3|||http://purl.uniprot.org/uniprot/Q8BMS3 ^@ 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|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ A disintegrin and metalloproteinase with thrombospondin motifs 12|||Cysteine switch|||Disintegrin|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Peptidase M12B propeptide|||Peptidase M12B propeptide domain-containing protein|||Polar 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_0000029188|||http://purl.uniprot.org/annotation/PRO_0000029189|||http://purl.uniprot.org/annotation/PRO_5004230388|||http://purl.uniprot.org/annotation/VSP_013149|||http://purl.uniprot.org/annotation/VSP_013150 http://togogenome.org/gene/10090:Gprc5b ^@ http://purl.uniprot.org/uniprot/D2DFA9|||http://purl.uniprot.org/uniprot/Q923Z0 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000012966 http://togogenome.org/gene/10090:Dnajc6 ^@ http://purl.uniprot.org/uniprot/Q80TZ3 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 1|||2|||3|||3 X 4 AA approximate tandem repeats|||C2 tensin-type|||Disordered|||In isoform 2.|||In isoform 3.|||J|||Phosphatase tensin-type|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Putative tyrosine-protein phosphatase auxilin|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000244517|||http://purl.uniprot.org/annotation/VSP_019582|||http://purl.uniprot.org/annotation/VSP_019583 http://togogenome.org/gene/10090:Pacs1 ^@ http://purl.uniprot.org/uniprot/Q8K212 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In mouse mutant chicory (ccy); reduced proportion of B cells in peripheral blood.|||In mouse mutant endive (en); reduced proportion of B cells in peripheral blood.|||N-acetylalanine|||Phosphofurin acidic cluster sorting protein 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000058172 http://togogenome.org/gene/10090:Ms4a3 ^@ http://purl.uniprot.org/uniprot/Q3TYT4|||http://purl.uniprot.org/uniprot/Q53ZU3|||http://purl.uniprot.org/uniprot/Q920C4 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Membrane-spanning 4-domains subfamily A member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000158633 http://togogenome.org/gene/10090:Trmt61a ^@ http://purl.uniprot.org/uniprot/Q80XC2 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ N-acetylserine|||Phosphoserine|||Removed|||Substrate|||tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A ^@ http://purl.uniprot.org/annotation/PRO_0000233095 http://togogenome.org/gene/10090:Sdhaf4 ^@ http://purl.uniprot.org/uniprot/Q8BTE0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||Mitochondrion|||Succinate dehydrogenase assembly factor 4, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000244341 http://togogenome.org/gene/10090:Zfp469 ^@ http://purl.uniprot.org/uniprot/A0A571BEL3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||C2H2-type|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Gpr141b ^@ http://purl.uniprot.org/uniprot/B9EKH0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Arfgap3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0T8|||http://purl.uniprot.org/uniprot/Q9D8S3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ ADP-ribosylation factor GTPase-activating protein 3|||Arf-GAP|||Basic and acidic residues|||C4-type|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000074194 http://togogenome.org/gene/10090:Gna15 ^@ http://purl.uniprot.org/uniprot/P30678 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region ^@ 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_0000203756 http://togogenome.org/gene/10090:Carnmt1 ^@ http://purl.uniprot.org/uniprot/Q80UY1 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Region|||Sequence Conflict ^@ Carnosine N-methyltransferase|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000089686 http://togogenome.org/gene/10090:Marveld2 ^@ http://purl.uniprot.org/uniprot/A1BQX3|||http://purl.uniprot.org/uniprot/E9Q1T5|||http://purl.uniprot.org/uniprot/Q3UZP0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||MARVEL|||MARVEL domain-containing protein 2|||OCEL|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000271527 http://togogenome.org/gene/10090:Gm3404 ^@ http://purl.uniprot.org/uniprot/Q9D506 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Vmn2r75 ^@ http://purl.uniprot.org/uniprot/G5E8Z7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015091957 http://togogenome.org/gene/10090:Bex2 ^@ http://purl.uniprot.org/uniprot/Q9WTZ8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||His cluster|||Omega-N-methylarginine|||Protein BEX2 ^@ http://purl.uniprot.org/annotation/PRO_0000229778 http://togogenome.org/gene/10090:Sumo3 ^@ http://purl.uniprot.org/uniprot/G3UWX9|||http://purl.uniprot.org/uniprot/G3UZA7|||http://purl.uniprot.org/uniprot/Q9Z172 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Propeptide|||Region|||Splice Variant ^@ Disordered|||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|||In isoform 2.|||Polar residues|||Small ubiquitin-related modifier 3|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000035959|||http://purl.uniprot.org/annotation/PRO_0000035960|||http://purl.uniprot.org/annotation/VSP_021948 http://togogenome.org/gene/10090:Kdm2b ^@ http://purl.uniprot.org/uniprot/Q6P1G2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 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.|||JmjC|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Lysine-specific demethylase 2B|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000119854|||http://purl.uniprot.org/annotation/VSP_011342|||http://purl.uniprot.org/annotation/VSP_011343|||http://purl.uniprot.org/annotation/VSP_017477|||http://purl.uniprot.org/annotation/VSP_017478|||http://purl.uniprot.org/annotation/VSP_019003 http://togogenome.org/gene/10090:Twsg1 ^@ http://purl.uniprot.org/uniprot/Q9EP52 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Twisted gastrulation protein homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000278809 http://togogenome.org/gene/10090:Psg27 ^@ http://purl.uniprot.org/uniprot/Q497W2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Mettl18 ^@ http://purl.uniprot.org/uniprot/Q9CZ09 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Histidine protein methyltransferase 1 homolog|||Nuclear localization signal|||Phosphoserine|||Tele-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000247200 http://togogenome.org/gene/10090:Pgs1 ^@ http://purl.uniprot.org/uniprot/B9EKS7|||http://purl.uniprot.org/uniprot/Q8BHF7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial|||Mitochondrion|||PLD phosphodiesterase|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000337107 http://togogenome.org/gene/10090:Nat8 ^@ http://purl.uniprot.org/uniprot/Q9JIY7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-acetyltransferase|||N-acetyltransferase 8 ^@ http://purl.uniprot.org/annotation/PRO_0000284692 http://togogenome.org/gene/10090:Cep295 ^@ http://purl.uniprot.org/uniprot/A0A1N9NPH8|||http://purl.uniprot.org/uniprot/E9QPW4|||http://purl.uniprot.org/uniprot/Q8BQ48 ^@ 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 ^@ ALMS motif|||Basic and acidic residues|||Centrosomal protein of 295 kDa|||Disordered|||In isoform 2.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||Necessary for centriole targeting and microtubule association|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000324596|||http://purl.uniprot.org/annotation/VSP_032292|||http://purl.uniprot.org/annotation/VSP_032293|||http://purl.uniprot.org/annotation/VSP_032294|||http://purl.uniprot.org/annotation/VSP_032295|||http://purl.uniprot.org/annotation/VSP_032296|||http://purl.uniprot.org/annotation/VSP_032297|||http://purl.uniprot.org/annotation/VSP_032298 http://togogenome.org/gene/10090:Hck ^@ http://purl.uniprot.org/uniprot/P08103 ^@ 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|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Reduced autophosphorylation.|||Removed|||S-palmitoyl cysteine|||SH2|||SH3|||Tyrosine-protein kinase HCK ^@ http://purl.uniprot.org/annotation/PRO_0000024435|||http://purl.uniprot.org/annotation/VSP_018859 http://togogenome.org/gene/10090:Immp1l ^@ http://purl.uniprot.org/uniprot/Q9CQU8 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Sequence Conflict ^@ Mitochondrial inner membrane protease subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000259574 http://togogenome.org/gene/10090:Tmigd3 ^@ http://purl.uniprot.org/uniprot/G3X8R9|||http://purl.uniprot.org/uniprot/Q497R5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical|||Polar residues|||Transmembrane domain-containing protein TMIGD3 ^@ http://purl.uniprot.org/annotation/PRO_0000441841 http://togogenome.org/gene/10090:Rpl38 ^@ http://purl.uniprot.org/uniprot/Q9JJI8 ^@ 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_0000215436 http://togogenome.org/gene/10090:Hephl1 ^@ http://purl.uniprot.org/uniprot/Q3V1H3 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Ferroxidase HEPHL1|||Helical|||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_0000346772 http://togogenome.org/gene/10090:Eif1ad4 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VLT7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||S1-like ^@ http://togogenome.org/gene/10090:Klhdc7a ^@ http://purl.uniprot.org/uniprot/A2APT9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch domain-containing protein 7A|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000285086 http://togogenome.org/gene/10090:Nsa2 ^@ http://purl.uniprot.org/uniprot/Q9CR47 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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_0000122260 http://togogenome.org/gene/10090:Pax4 ^@ http://purl.uniprot.org/uniprot/A2RRY5|||http://purl.uniprot.org/uniprot/B7ZNC8|||http://purl.uniprot.org/uniprot/P32115 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||DNA Binding|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Homeobox|||In isoform 2.|||In isoform 3.|||Loss of transactivation function.|||PAI subdomain|||Paired|||Paired box protein Pax-4|||RED subdomain|||Transcription repression ^@ http://purl.uniprot.org/annotation/PRO_0000050181|||http://purl.uniprot.org/annotation/VSP_002361|||http://purl.uniprot.org/annotation/VSP_002362 http://togogenome.org/gene/10090:Lgsn ^@ http://purl.uniprot.org/uniprot/Q8CIX8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||GS beta-grasp|||GS catalytic|||Lengsin|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000153283 http://togogenome.org/gene/10090:Kdm6b ^@ http://purl.uniprot.org/uniprot/Q5NCY0 ^@ 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||JmjC|||Lysine-specific demethylase 6B|||No loss of its ability to regulate TBX21-dependent gene expression or its ability to interact with SMARCA4; when associated with A-1388 and A-1390.|||No loss of its ability to regulate TBX21-dependent gene expression or its ability to interact with SMARCA4; when associated with A-1388 and A-1468.|||No loss of its ability to regulate TBX21-dependent gene expression or its ability to interact with SMARCA4; when associated with A-1390 and A-1468.|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000292008 http://togogenome.org/gene/10090:Foxg1 ^@ http://purl.uniprot.org/uniprot/Q3V1Q8|||http://purl.uniprot.org/uniprot/Q60987 ^@ 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 residues|||Disordered|||Fork-head|||Forkhead box protein G1|||Interaction with KDM5B|||Pro residues|||Required for interaction with TLE6 ^@ http://purl.uniprot.org/annotation/PRO_0000091837 http://togogenome.org/gene/10090:Or10ag60 ^@ http://purl.uniprot.org/uniprot/A0A1L1SQT2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc25a47 ^@ http://purl.uniprot.org/uniprot/Q6IS41 ^@ 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 47 ^@ http://purl.uniprot.org/annotation/PRO_0000291780 http://togogenome.org/gene/10090:Pepd ^@ http://purl.uniprot.org/uniprot/A2RS23|||http://purl.uniprot.org/uniprot/Q11136 ^@ 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 ^@ Aminopeptidase P N-terminal|||N-acetylalanine|||Phosphoserine|||Removed|||Xaa-Pro dipeptidase ^@ http://purl.uniprot.org/annotation/PRO_0000185088 http://togogenome.org/gene/10090:Prdm13 ^@ http://purl.uniprot.org/uniprot/E9PZZ1 ^@ 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 ^@ Basic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In isoform 2.|||PR domain zinc finger protein 13|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000416115|||http://purl.uniprot.org/annotation/VSP_042506 http://togogenome.org/gene/10090:Ppp1r15a ^@ http://purl.uniprot.org/uniprot/B2RRL7|||http://purl.uniprot.org/uniprot/P17564 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain ^@ 1|||2|||3|||4|||4.5 X approximate repeats|||5; truncated|||Abolishes interaction with PP1.|||Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Interaction with KMT2A/MLL1|||Interaction with SMAD7|||Interaction with SMARCB1|||Phosphotyrosine|||Polar residues|||Protein phosphatase 1 regulatory subunit 15A|||Protein phosphatase 1 regulatory subunit 15A/B C-terminal|||Required for localization in the endoplasmic reticulum ^@ http://purl.uniprot.org/annotation/PRO_0000096665|||http://purl.uniprot.org/annotation/VSP_031651 http://togogenome.org/gene/10090:Ube2q2l ^@ http://purl.uniprot.org/uniprot/Q8BW45 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||UBC core ^@ http://togogenome.org/gene/10090:Shq1 ^@ http://purl.uniprot.org/uniprot/Q7TMX5 ^@ 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 ^@ CS|||Disordered|||In isoform 2.|||Polar residues|||Protein SHQ1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000302823|||http://purl.uniprot.org/annotation/VSP_027961 http://togogenome.org/gene/10090:L3hypdh ^@ http://purl.uniprot.org/uniprot/Q9CXA2 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Proton acceptor|||Trans-L-3-hydroxyproline dehydratase ^@ http://purl.uniprot.org/annotation/PRO_0000288950 http://togogenome.org/gene/10090:Or1q1 ^@ http://purl.uniprot.org/uniprot/Q8VFP4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or7g16 ^@ http://purl.uniprot.org/uniprot/Q8VFM8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfpl1 ^@ http://purl.uniprot.org/uniprot/Q9DB43 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane|||Zinc Finger ^@ B box-type; degenerate|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Polar residues|||RING-type; degenerate|||Zinc finger protein-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000056319 http://togogenome.org/gene/10090:Dok6 ^@ http://purl.uniprot.org/uniprot/Q2MHE5 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Motif|||Region ^@ DKFBH motif|||Disordered|||Docking protein 6|||IRS-type PTB|||PH ^@ http://purl.uniprot.org/annotation/PRO_0000322637 http://togogenome.org/gene/10090:Ctsf ^@ http://purl.uniprot.org/uniprot/Q9R013 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cathepsin F|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000026204|||http://purl.uniprot.org/annotation/PRO_0000026205 http://togogenome.org/gene/10090:Atp1b3 ^@ http://purl.uniprot.org/uniprot/P97370|||http://purl.uniprot.org/uniprot/Q544Q7 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Sodium/potassium-transporting ATPase subunit beta-3|||immunoglobulin-like ^@ http://purl.uniprot.org/annotation/PRO_0000219109 http://togogenome.org/gene/10090:Mindy3 ^@ http://purl.uniprot.org/uniprot/Q9CV28 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Active Site|||Chain|||Modified Residue|||Splice Variant ^@ In isoform 2.|||Nucleophile|||Phosphoserine|||Proton acceptor|||Ubiquitin carboxyl-terminal hydrolase MINDY-3 ^@ http://purl.uniprot.org/annotation/PRO_0000317562|||http://purl.uniprot.org/annotation/VSP_031041 http://togogenome.org/gene/10090:Sco1 ^@ http://purl.uniprot.org/uniprot/Q5SUC9 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Mutagenesis Site|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Disordered|||Helical|||Important for dimerization|||Knockin mice hearts exhibit a severe combined COX and copper deficiency and a mislocalization of copper transporter protein CTR1 to the cytoplasm.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Protein SCO1 homolog, mitochondrial|||Redox-active ^@ http://purl.uniprot.org/annotation/PRO_0000354066 http://togogenome.org/gene/10090:Grem2 ^@ http://purl.uniprot.org/uniprot/O88273|||http://purl.uniprot.org/uniprot/Q3TST1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand ^@ CTCK|||Gremlin|||Gremlin-2|||N-linked (GlcNAc...) asparagine|||No effect on dimerization. No effect on inhibition of BMP signaling.|||Reduces affinity for BMP2 and BMP4. Reduces inhibition of BMP2 signaling.|||Reduces affinity for BMP2 and BMP4. Strongly reduces inhibition of BMP2 signaling.|||Slightly reduces affinity for BMP2 and BMP4. No effect on inhibition of BMP2 signaling.|||Strongly reduces affinity for BMP2 and BMP4. Reduces inhibition of BMP2 signaling.|||Strongly reduces affinity for BMP2 and BMP4. Strongly reduces inhibition of BMP2 signaling. ^@ http://purl.uniprot.org/annotation/PRO_0000006721|||http://purl.uniprot.org/annotation/PRO_5014212503 http://togogenome.org/gene/10090:Nme7 ^@ http://purl.uniprot.org/uniprot/Q3UMG6|||http://purl.uniprot.org/uniprot/Q8BUH2 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent ^@ DM10|||Pros-phosphohistidine intermediate ^@ http://togogenome.org/gene/10090:Vps13d ^@ http://purl.uniprot.org/uniprot/B1ART2|||http://purl.uniprot.org/uniprot/Q6A066 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||UBA ^@ http://togogenome.org/gene/10090:Asb9 ^@ http://purl.uniprot.org/uniprot/Q91ZT8 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Site ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 9|||Disordered|||Essential for binding to CKB|||N-acetylmethionine|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066941 http://togogenome.org/gene/10090:Smim33 ^@ http://purl.uniprot.org/uniprot/Q3TS39 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Small integral membrane protein 33 ^@ http://purl.uniprot.org/annotation/PRO_0000443400 http://togogenome.org/gene/10090:Trap1 ^@ http://purl.uniprot.org/uniprot/Q9CQN1 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Transit Peptide ^@ Heat shock protein 75 kDa, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000013605 http://togogenome.org/gene/10090:Nmbr ^@ http://purl.uniprot.org/uniprot/O54799|||http://purl.uniprot.org/uniprot/Q0VEH1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||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|||Neuromedin-B receptor|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069904 http://togogenome.org/gene/10090:Ccnd1 ^@ http://purl.uniprot.org/uniprot/P25322|||http://purl.uniprot.org/uniprot/Q790L7 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Constitutively nuclear. Strongly reduced interaction with FBXO4. Strongly reduced ubiquitination.|||Cyclin N-terminal|||Disordered|||G1/S-specific cyclin-D1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphothreonine|||Promotes location to the nucleus. Reduces proteasomal degradation, but does not prevent ubiquitination. ^@ http://purl.uniprot.org/annotation/PRO_0000080431 http://togogenome.org/gene/10090:Aadacl4fm4 ^@ http://purl.uniprot.org/uniprot/B1AVU6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Alpha/beta hydrolase fold-3 ^@ http://togogenome.org/gene/10090:Ifi213 ^@ http://purl.uniprot.org/uniprot/D3Z5G0|||http://purl.uniprot.org/uniprot/Q3UPZ5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pyrin ^@ http://togogenome.org/gene/10090:Esp8 ^@ http://purl.uniprot.org/uniprot/F7AMQ8 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5003347888 http://togogenome.org/gene/10090:Or52d1 ^@ http://purl.uniprot.org/uniprot/Q8VGW2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or1a1 ^@ http://purl.uniprot.org/uniprot/Q7TRX2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Il25 ^@ http://purl.uniprot.org/uniprot/Q8VHH8 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||Interleukin-25|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_5015099440 http://togogenome.org/gene/10090:Ifi209 ^@ http://purl.uniprot.org/uniprot/Q8BV49 ^@ 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|||HIN-200|||Polar residues|||Pyrin|||Pyrin and HIN domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000334525 http://togogenome.org/gene/10090:Tcf7 ^@ http://purl.uniprot.org/uniprot/Q00417|||http://purl.uniprot.org/uniprot/Q80UF1 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Splice Variant ^@ Basic and acidic residues|||CTNNB1-binding|||Disordered|||HMG box|||In isoform 1.|||Nuclear localization signal|||Polar residues|||Pro residues|||Transcription factor 7 ^@ http://purl.uniprot.org/annotation/PRO_0000048613|||http://purl.uniprot.org/annotation/VSP_014963 http://togogenome.org/gene/10090:Lama5 ^@ http://purl.uniprot.org/uniprot/Q3TZ05|||http://purl.uniprot.org/uniprot/Q61001 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Cell attachment site|||Disordered|||Domain II and I|||Domain IV 1 (domain IV B)|||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|||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|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000017063 http://togogenome.org/gene/10090:Ranbp17 ^@ http://purl.uniprot.org/uniprot/Q99NF8 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ N-acetylalanine|||Phosphoserine|||Ran-binding protein 17|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000204719 http://togogenome.org/gene/10090:Ndufb7 ^@ http://purl.uniprot.org/uniprot/Q9CR61 ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Strand|||Turn ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||N-myristoyl glycine|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118812 http://togogenome.org/gene/10090:Bub1b ^@ http://purl.uniprot.org/uniprot/Q3UZD6|||http://purl.uniprot.org/uniprot/Q9Z1S0 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ BUB1 N-terminal|||Cleavage; by caspase-3|||D-box|||Disordered|||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; by PLK1|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085674 http://togogenome.org/gene/10090:Pcdhb7 ^@ http://purl.uniprot.org/uniprot/Q8CDY9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Cadherin|||Helical ^@ http://togogenome.org/gene/10090:Trib1 ^@ http://purl.uniprot.org/uniprot/Q8K4K4 ^@ 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 ^@ COP1-binding|||Disordered|||In isoform 2.|||Pro residues|||Protein kinase|||Tribbles homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000131860|||http://purl.uniprot.org/annotation/VSP_051888 http://togogenome.org/gene/10090:Frrs1l ^@ http://purl.uniprot.org/uniprot/B1AXV0|||http://purl.uniprot.org/uniprot/Q8BVG0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ DOMON|||DOMON domain-containing protein FRRS1L|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000420688 http://togogenome.org/gene/10090:Cep350 ^@ http://purl.uniprot.org/uniprot/E9Q309 ^@ 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|||CAP-Gly|||Centrosome-associated protein 350|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000440628 http://togogenome.org/gene/10090:Ryr1 ^@ http://purl.uniprot.org/uniprot/E9PZQ0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 1|||2|||3; truncated|||4; truncated|||5|||6|||6 X approximate repeats|||Acidic residues|||B30.2/SPRY 1|||B30.2/SPRY 2|||B30.2/SPRY 3|||Basic and acidic residues|||Causes paralysis and perinatal death in homozygous mice, apparently due to asphyxia. Mutant mice have greatly reduced and amorphous skeletal muscle.|||Cytoplasmic|||Disordered|||EF-hand|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Increased channel activity, leading to permanently increased cytoplasmic Ca(2+) levels. Increased activation by calcium, and increased ryanodine binding.|||Interaction with CALM|||Interaction with FKBP1A|||Lumenal|||MIR 1|||MIR 2|||MIR 3|||MIR 4|||MIR 5|||Phosphoserine|||Phosphoserine; by PKA and PKG|||Phosphothreonine|||Phosphotyrosine|||Pore-forming|||Pro residues|||Ryanodine receptor 1|||S-nitrosocysteine|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000415566 http://togogenome.org/gene/10090:Rp9 ^@ http://purl.uniprot.org/uniprot/P97762|||http://purl.uniprot.org/uniprot/Q3TH81 ^@ 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|||CCHC-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||PIM1-binding|||Phosphoserine; by PIM1; in vitro|||Retinitis pigmentosa 9 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000097429 http://togogenome.org/gene/10090:Ppp1r1b ^@ http://purl.uniprot.org/uniprot/Q60829 ^@ 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|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKA|||Polar residues|||Protein phosphatase 1 regulatory subunit 1B ^@ http://purl.uniprot.org/annotation/PRO_0000071474|||http://purl.uniprot.org/annotation/VSP_025058 http://togogenome.org/gene/10090:Med7 ^@ http://purl.uniprot.org/uniprot/Q9CZB6 ^@ 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 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_0000079409 http://togogenome.org/gene/10090:Trem2 ^@ http://purl.uniprot.org/uniprot/Q99NH8 ^@ 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|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cleavage of ectodomain|||Cytoplasmic|||Decreases myeloid cell immune response. Reduces expression levels.|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||In strain: FVB/N.|||Macrophages exhibit increased apoptosis, reduced proliferation, and reduced phagocytosis. Macrophages also exhibit increased inflammatory cytokine secretion. Microglia demonstrate reduced immune activity. Also decreases cerebral blood flow and reduces cerebral glucose metabolism.|||N-linked (GlcNAc...) asparagine|||Triggering receptor expressed on myeloid cells 2 ^@ http://purl.uniprot.org/annotation/PRO_0000014988|||http://purl.uniprot.org/annotation/VSP_010794 http://togogenome.org/gene/10090:Or6b3 ^@ http://purl.uniprot.org/uniprot/Q8VGU5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or4k1 ^@ http://purl.uniprot.org/uniprot/Q7TRM6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cacnb4 ^@ http://purl.uniprot.org/uniprot/A2ATZ8|||http://purl.uniprot.org/uniprot/Q3TYI5|||http://purl.uniprot.org/uniprot/Q8R0S4 ^@ 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 1.|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3|||Voltage-dependent L-type calcium channel subunit beta-4 ^@ http://purl.uniprot.org/annotation/PRO_0000144061|||http://purl.uniprot.org/annotation/VSP_010737|||http://purl.uniprot.org/annotation/VSP_022599 http://togogenome.org/gene/10090:Gda ^@ http://purl.uniprot.org/uniprot/D3YU09|||http://purl.uniprot.org/uniprot/Q548F2|||http://purl.uniprot.org/uniprot/Q9R111 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Amidohydrolase-related|||Guanine deaminase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000122299 http://togogenome.org/gene/10090:Eppk1 ^@ http://purl.uniprot.org/uniprot/Q8R0W0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||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 66|||Plectin 67|||Plectin 68|||Plectin 69|||Plectin 7|||Plectin 70|||Plectin 71|||Plectin 72|||Plectin 73|||Plectin 74|||Plectin 75|||Plectin 76|||Plectin 8|||Plectin 9|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000078146 http://togogenome.org/gene/10090:Vmn1r51 ^@ http://purl.uniprot.org/uniprot/A0A0R4J266|||http://purl.uniprot.org/uniprot/Q78GE8|||http://purl.uniprot.org/uniprot/Q8VIC6 ^@ 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|||Vomeronasal type-1 receptor 51 ^@ http://purl.uniprot.org/annotation/PRO_0000239955 http://togogenome.org/gene/10090:Cyp4f16 ^@ http://purl.uniprot.org/uniprot/Q99N17 ^@ Binding Site|||Site ^@ Binding Site ^@ ^@ http://togogenome.org/gene/10090:Cort ^@ http://purl.uniprot.org/uniprot/P56469 ^@ Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Cortistatin-14|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000033157|||http://purl.uniprot.org/annotation/PRO_0000033158 http://togogenome.org/gene/10090:Amph ^@ http://purl.uniprot.org/uniprot/A0A0G2JEG8|||http://purl.uniprot.org/uniprot/Q7TQF7 ^@ 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 ^@ Amphiphysin|||BAR|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Pro residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000192948 http://togogenome.org/gene/10090:Yipf7 ^@ http://purl.uniprot.org/uniprot/Q9JIM5 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Protein YIPF7 ^@ http://purl.uniprot.org/annotation/PRO_0000333008 http://togogenome.org/gene/10090:Ppia ^@ http://purl.uniprot.org/uniprot/P17742|||http://purl.uniprot.org/uniprot/Q5SVY2 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||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|||N-acetylmethionine|||N-acetylvaline; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||N6-acetyllysine; alternate|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase A|||Peptidyl-prolyl cis-trans isomerase A, N-terminally processed|||Phosphoserine|||Phosphothreonine|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000064117|||http://purl.uniprot.org/annotation/PRO_0000423245 http://togogenome.org/gene/10090:Tas2r106 ^@ http://purl.uniprot.org/uniprot/Q7M724 ^@ 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 106 ^@ http://purl.uniprot.org/annotation/PRO_0000248250 http://togogenome.org/gene/10090:Nfib ^@ http://purl.uniprot.org/uniprot/P97863|||http://purl.uniprot.org/uniprot/Q6GSP7 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant ^@ 9aaTAD|||Asymmetric dimethylarginine|||CTF/NF-I|||Disordered|||In isoform 2.|||In isoform 3.|||In strain: NIHSwiss.|||Nuclear factor 1 B-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000100197|||http://purl.uniprot.org/annotation/VSP_003547|||http://purl.uniprot.org/annotation/VSP_003548|||http://purl.uniprot.org/annotation/VSP_003549 http://togogenome.org/gene/10090:Hormad1 ^@ http://purl.uniprot.org/uniprot/Q9D5T7 ^@ 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 ^@ Disordered|||HORMA|||HORMA domain-containing protein 1|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284666|||http://purl.uniprot.org/annotation/VSP_024604 http://togogenome.org/gene/10090:Slc9b2 ^@ http://purl.uniprot.org/uniprot/Q5BKR2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and 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=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.|||Phosphoserine|||Polar residues|||Sodium/hydrogen exchanger 9B2 ^@ http://purl.uniprot.org/annotation/PRO_0000331271|||http://purl.uniprot.org/annotation/VSP_033154|||http://purl.uniprot.org/annotation/VSP_033155 http://togogenome.org/gene/10090:4933434E20Rik ^@ http://purl.uniprot.org/uniprot/Q05D39|||http://purl.uniprot.org/uniprot/Q8R092 ^@ 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.|||Polar residues|||Protein C1orf43 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089257|||http://purl.uniprot.org/annotation/VSP_014422|||http://purl.uniprot.org/annotation/VSP_014423|||http://purl.uniprot.org/annotation/VSP_014424 http://togogenome.org/gene/10090:Ebf1 ^@ http://purl.uniprot.org/uniprot/Q07802|||http://purl.uniprot.org/uniprot/Q3UTW6|||http://purl.uniprot.org/uniprot/Q5SWK4|||http://purl.uniprot.org/uniprot/Q5SWK5|||http://purl.uniprot.org/uniprot/Q8CBL7 ^@ 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|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||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|||In isoform Short.|||Interaction with DNA|||N-acetylmethionine|||Polar residues|||Reduced interaction with DNA.|||Strongly reduced interaction with DNA.|||Transcription factor COE1 ^@ http://purl.uniprot.org/annotation/PRO_0000107826|||http://purl.uniprot.org/annotation/VSP_001112 http://togogenome.org/gene/10090:Zfp93 ^@ http://purl.uniprot.org/uniprot/Q61116 ^@ 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 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 235 ^@ http://purl.uniprot.org/annotation/PRO_0000047475 http://togogenome.org/gene/10090:Oxgr1 ^@ http://purl.uniprot.org/uniprot/Q6IYF8 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ 2-oxoglutarate 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_0000069995 http://togogenome.org/gene/10090:Il18rap ^@ http://purl.uniprot.org/uniprot/Q0VBK3|||http://purl.uniprot.org/uniprot/Q3TTU1|||http://purl.uniprot.org/uniprot/Q9Z2B1 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Interleukin-18 receptor accessory protein|||N-linked (GlcNAc...) asparagine|||TIR ^@ http://purl.uniprot.org/annotation/PRO_0000042186|||http://purl.uniprot.org/annotation/PRO_5014306834 http://togogenome.org/gene/10090:Taf11 ^@ http://purl.uniprot.org/uniprot/Q99JX1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||N-acetylmethionine|||Transcription initiation factor TFIID subunit 11 ^@ http://purl.uniprot.org/annotation/PRO_0000118903 http://togogenome.org/gene/10090:Pdcd5 ^@ http://purl.uniprot.org/uniprot/P56812|||http://purl.uniprot.org/uniprot/Q564F6 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Programmed cell death protein 5|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000121546 http://togogenome.org/gene/10090:Col5a2 ^@ http://purl.uniprot.org/uniprot/Q3U962 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ 4-hydroxyproline|||Basic and acidic residues|||C-terminal propeptide|||Cell attachment site|||Collagen alpha-2(V) chain|||Disordered|||Fibrillar collagen NC1|||N-linked (GlcNAc...) asparagine|||Pro residues|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000283768|||http://purl.uniprot.org/annotation/PRO_0000283769 http://togogenome.org/gene/10090:S100g ^@ http://purl.uniprot.org/uniprot/P97816|||http://purl.uniprot.org/uniprot/Q5VM59 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ EF-hand|||EF-hand 1|||EF-hand 2|||Phosphoserine|||Protein S100-G ^@ http://purl.uniprot.org/annotation/PRO_0000144028 http://togogenome.org/gene/10090:Iqcg ^@ http://purl.uniprot.org/uniprot/Q80W32 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Dynein regulatory complex protein 9|||IQ ^@ http://purl.uniprot.org/annotation/PRO_0000282563 http://togogenome.org/gene/10090:Kcng4 ^@ http://purl.uniprot.org/uniprot/Q80XM3 ^@ 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 G member 4|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000320142 http://togogenome.org/gene/10090:Fhod3 ^@ http://purl.uniprot.org/uniprot/Q76LL6 ^@ 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|||DAD|||Disordered|||FH1|||FH1/FH2 domain-containing protein 3|||FH2|||GBD/FH3|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000283792|||http://purl.uniprot.org/annotation/VSP_024399|||http://purl.uniprot.org/annotation/VSP_024400|||http://purl.uniprot.org/annotation/VSP_024401 http://togogenome.org/gene/10090:Rab13 ^@ http://purl.uniprot.org/uniprot/D3YUS4|||http://purl.uniprot.org/uniprot/Q9DD03 ^@ 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|||Disordered|||Effector region|||Phosphoserine|||Ras-related protein Rab-13|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121183|||http://purl.uniprot.org/annotation/PRO_0000370758 http://togogenome.org/gene/10090:Rps10 ^@ http://purl.uniprot.org/uniprot/P63325|||http://purl.uniprot.org/uniprot/Q5M9K7 ^@ 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 ubiquitin)|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Plectin/eS10 N-terminal|||Small ribosomal subunit protein eS10|||Symmetric dimethylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000116361 http://togogenome.org/gene/10090:Snapc2 ^@ http://purl.uniprot.org/uniprot/Q91XA5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||snRNA-activating protein complex subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000072021 http://togogenome.org/gene/10090:Ntaq1 ^@ http://purl.uniprot.org/uniprot/A0A2I3BQY8|||http://purl.uniprot.org/uniprot/Q80WB5|||http://purl.uniprot.org/uniprot/Q9CWD7 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site ^@ Does not strongly affect N-terminal glutamine amidohydrolase activity.|||Impaired N-terminal glutamine amidohydrolase activity.|||Loss of N-terminal glutamine amidohydrolase activity.|||Protein N-terminal glutamine amidohydrolase|||Protein N-terminal glutamine amidohydrolase alpha beta roll ^@ http://purl.uniprot.org/annotation/PRO_0000279410 http://togogenome.org/gene/10090:Slc2a5 ^@ http://purl.uniprot.org/uniprot/Q9WV38 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||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-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Solute carrier family 2, facilitated glucose transporter member 5 ^@ http://purl.uniprot.org/annotation/PRO_0000050370 http://togogenome.org/gene/10090:Dmrt3 ^@ http://purl.uniprot.org/uniprot/Q80WT2 ^@ 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 ^@ DM|||DMA|||Disordered|||Doublesex- and mab-3-related transcription factor 3|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000277795 http://togogenome.org/gene/10090:Rnf31 ^@ http://purl.uniprot.org/uniprot/Q924T7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Turn|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Site|||Splice Variant|||Turn|||Zinc Finger ^@ Cleavage; by caspase|||Disordered|||E3 ubiquitin-protein ligase RNF31|||IBR-type|||In isoform 2.|||Interaction with RBCK1|||LDD domain|||PUB|||Phosphoserine|||Polar residues|||Polyubiquitin-binding|||RING-type 1|||RING-type 2; atypical|||RanBP2-type 1|||RanBP2-type 2|||RanBP2-type 3|||TRIAD supradomain|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000056070|||http://purl.uniprot.org/annotation/VSP_009649 http://togogenome.org/gene/10090:Tufm ^@ http://purl.uniprot.org/uniprot/Q8BFR5 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Transit Peptide ^@ Elongation factor Tu, mitochondrial|||G1|||G2|||G3|||G4|||G5|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000007463|||http://purl.uniprot.org/annotation/VSP_013942 http://togogenome.org/gene/10090:Cdk4 ^@ http://purl.uniprot.org/uniprot/P30285|||http://purl.uniprot.org/uniprot/Q545C3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Cyclin-dependent kinase 4|||N-acetylalanine|||Phosphoserine|||Phosphothreonine; by CAK|||Protein kinase|||Proton acceptor|||Removed|||Required for binding D-type cyclins ^@ http://purl.uniprot.org/annotation/PRO_0000085779 http://togogenome.org/gene/10090:Selp ^@ http://purl.uniprot.org/uniprot/Q01102 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||EGF-like|||Endocytosis signal|||Extracellular|||Helical|||Interaction with SNX17|||N-linked (GlcNAc...) asparagine|||P-selectin|||S-palmitoyl cysteine; alternate|||S-stearoyl cysteine; alternate|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8 ^@ http://purl.uniprot.org/annotation/PRO_0000017499 http://togogenome.org/gene/10090:Samt2 ^@ http://purl.uniprot.org/uniprot/Q497M0 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Cpt1c ^@ http://purl.uniprot.org/uniprot/Q8BGD5 ^@ 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 ^@ Carnitine O-palmitoyltransferase 1, brain isoform|||Cytoplasmic|||Helical|||Mitochondrial intermembrane|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000210167 http://togogenome.org/gene/10090:Coil ^@ http://purl.uniprot.org/uniprot/E9Q284 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Coilin N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ifrd2 ^@ http://purl.uniprot.org/uniprot/Q9D8U0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Interferon-related developmental regulator 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000458235 http://togogenome.org/gene/10090:Gm21693 ^@ http://purl.uniprot.org/uniprot/J3QK27 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||RRM ^@ http://togogenome.org/gene/10090:Ctnnd1 ^@ http://purl.uniprot.org/uniprot/E9Q8Z5|||http://purl.uniprot.org/uniprot/E9Q8Z6|||http://purl.uniprot.org/uniprot/E9Q8Z8|||http://purl.uniprot.org/uniprot/E9Q905|||http://purl.uniprot.org/uniprot/E9Q986|||http://purl.uniprot.org/uniprot/P30999 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ ARM|||ARM 1|||ARM 10|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Abolishes nuclear localization.|||Basic and acidic residues|||Catenin delta-1|||Disordered|||Essential for interaction with cadherins|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 2.|||N-acetylmethionine|||Necessary and sufficient for interaction with CCDC85B|||Nuclear localization signal (NLS)|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FYN|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064297|||http://purl.uniprot.org/annotation/VSP_030567|||http://purl.uniprot.org/annotation/VSP_030568 http://togogenome.org/gene/10090:Wdr91 ^@ http://purl.uniprot.org/uniprot/Q7TMQ7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||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_0000295747 http://togogenome.org/gene/10090:Erbb3 ^@ http://purl.uniprot.org/uniprot/Q61526 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Receptor tyrosine-protein kinase erbB-3 ^@ http://purl.uniprot.org/annotation/PRO_0000042231 http://togogenome.org/gene/10090:Pex11g ^@ http://purl.uniprot.org/uniprot/Q6P6M5 ^@ 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.|||Lumenal|||Peroxisomal membrane protein 11C ^@ http://purl.uniprot.org/annotation/PRO_0000105971|||http://purl.uniprot.org/annotation/VSP_013540|||http://purl.uniprot.org/annotation/VSP_013541 http://togogenome.org/gene/10090:Lmbr1l ^@ http://purl.uniprot.org/uniprot/Q9D1E5 ^@ 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|||Extracellular|||Helical|||In isoform 2.|||In st (strawberry phenotype); affected mice exhibit severe lymphopenia, failure of lymphocyte development, reduced natural killer (NK) cell function and impaired B-cell development.|||Interaction with LGB|||LCN1-binding|||Protein LMBR1L ^@ http://purl.uniprot.org/annotation/PRO_0000053912|||http://purl.uniprot.org/annotation/VSP_016897 http://togogenome.org/gene/10090:Or2a52 ^@ http://purl.uniprot.org/uniprot/Q8VEV1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wnt5b ^@ http://purl.uniprot.org/uniprot/P22726 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-5b ^@ http://purl.uniprot.org/annotation/PRO_0000041435 http://togogenome.org/gene/10090:Brcc3dc ^@ http://purl.uniprot.org/uniprot/Q7M757 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif ^@ JAMM motif|||Lys-63-specific deubiquitinase BRCC36-like|||MPN ^@ http://purl.uniprot.org/annotation/PRO_0000373951 http://togogenome.org/gene/10090:Spata22 ^@ http://purl.uniprot.org/uniprot/B2KFD7|||http://purl.uniprot.org/uniprot/Q5SV06 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Spermatogenesis-associated protein 22 ^@ http://purl.uniprot.org/annotation/PRO_0000251607 http://togogenome.org/gene/10090:Akap17b ^@ http://purl.uniprot.org/uniprot/A2A3V1 ^@ 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 ^@ A-kinase anchor protein 17B|||Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000343419 http://togogenome.org/gene/10090:Celsr1 ^@ http://purl.uniprot.org/uniprot/O35161 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||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|||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|||Laminin EGF-like|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000012915 http://togogenome.org/gene/10090:Atp2c1 ^@ http://purl.uniprot.org/uniprot/Q3UZR5|||http://purl.uniprot.org/uniprot/Q69ZL4|||http://purl.uniprot.org/uniprot/Q80XR2|||http://purl.uniprot.org/uniprot/Q8BMS7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Calcium-transporting ATPase type 2C member 1|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000046224 http://togogenome.org/gene/10090:Tbl2 ^@ http://purl.uniprot.org/uniprot/Q9R099 ^@ 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)|||Phosphothreonine|||Transducin beta-like protein 2|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051271 http://togogenome.org/gene/10090:Usp9y ^@ http://purl.uniprot.org/uniprot/F8VPU6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||USP ^@ http://togogenome.org/gene/10090:Tvp23a ^@ http://purl.uniprot.org/uniprot/Q6NVH0 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Hs3st6 ^@ http://purl.uniprot.org/uniprot/A2RTI7|||http://purl.uniprot.org/uniprot/Q3UIC7|||http://purl.uniprot.org/uniprot/Q5GFD5 ^@ 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|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||For sulfotransferase activity|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate glucosamine 3-O-sulfotransferase 6|||Lumenal|||N-linked (GlcNAc...) asparagine|||Sulfotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000085225 http://togogenome.org/gene/10090:Tbc1d20 ^@ http://purl.uniprot.org/uniprot/Q0P648|||http://purl.uniprot.org/uniprot/Q9D9I4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane ^@ Arginine finger|||Basic and acidic residues|||Disordered|||Glutamine finger|||Helical|||In bs.|||Rab-GAP TBC|||TBC1 domain family member 20 ^@ http://purl.uniprot.org/annotation/PRO_0000208049 http://togogenome.org/gene/10090:Ephb1 ^@ http://purl.uniprot.org/uniprot/Q8CA63|||http://purl.uniprot.org/uniprot/Q8CBF3 ^@ Active Site|||Binding Site|||Chain|||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 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Eph LBD|||Ephrin type-B receptor 1|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000260317|||http://purl.uniprot.org/annotation/PRO_5015099081|||http://purl.uniprot.org/annotation/VSP_021595 http://togogenome.org/gene/10090:Mab21l1 ^@ http://purl.uniprot.org/uniprot/O70299 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Putative nucleotidyltransferase MAB21L1 ^@ http://purl.uniprot.org/annotation/PRO_0000312782 http://togogenome.org/gene/10090:Tfap2d ^@ http://purl.uniprot.org/uniprot/Q91ZK0 ^@ 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|||H-S-H (helix-span-helix), dimerization|||Phosphoserine; by PKA|||Transcription factor AP-2-delta ^@ http://purl.uniprot.org/annotation/PRO_0000309514 http://togogenome.org/gene/10090:Myo1g ^@ http://purl.uniprot.org/uniprot/Q5SUA5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes localization to phagocytic cups; when associated with A-883.|||Abolishes localization to phagocytic cups; when associated with A-893.|||Actin-binding|||Disordered|||Does not affect localization to the plasma membrane.|||IQ|||Myosin motor|||Polar residues|||TH1|||Unconventional myosin-Ig ^@ http://purl.uniprot.org/annotation/PRO_0000340318 http://togogenome.org/gene/10090:Kng1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J038|||http://purl.uniprot.org/uniprot/D3YTY9|||http://purl.uniprot.org/uniprot/O08677 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||Bradykinin|||Cleavage; by ACE|||Cystatin kininogen-type|||Cystatin kininogen-type 1|||Cystatin kininogen-type 2|||Cystatin kininogen-type 3|||Disordered|||In isoform 3.|||In isoform LMW.|||Interchain (between heavy and light chains)|||Kininogen-1|||Kininogen-1 heavy chain|||Kininogen-1 light chain|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000006691|||http://purl.uniprot.org/annotation/PRO_0000006692|||http://purl.uniprot.org/annotation/PRO_0000006693|||http://purl.uniprot.org/annotation/PRO_0000006694|||http://purl.uniprot.org/annotation/PRO_5003053051|||http://purl.uniprot.org/annotation/PRO_5006451928|||http://purl.uniprot.org/annotation/VSP_001263|||http://purl.uniprot.org/annotation/VSP_001264|||http://purl.uniprot.org/annotation/VSP_037159 http://togogenome.org/gene/10090:Gapdh ^@ http://purl.uniprot.org/uniprot/A0A0A0MQF6|||http://purl.uniprot.org/uniprot/D2KHZ9|||http://purl.uniprot.org/uniprot/P16858 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||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|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited form|||Abolishes sulfhydration and induces impaired enzyme activity.|||Activates thiol group during catalysis|||Cysteine persulfide|||Deamidated asparagine|||Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding|||Glyceraldehyde-3-phosphate dehydrogenase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with WARS1|||N6,N6-dimethyllysine|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||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_0000145490 http://togogenome.org/gene/10090:Scgb2b18 ^@ http://purl.uniprot.org/uniprot/A0A087WPA9 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015029574 http://togogenome.org/gene/10090:Wfdc12 ^@ http://purl.uniprot.org/uniprot/Q3V469|||http://purl.uniprot.org/uniprot/Q9JHY3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ WAP|||WAP domain-containing protein|||WAP four-disulfide core domain protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000041391|||http://purl.uniprot.org/annotation/PRO_5009970848 http://togogenome.org/gene/10090:Zfp322a ^@ http://purl.uniprot.org/uniprot/Q8BZ89 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Modified Residue|||Sequence Conflict|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 10; 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; degenerate|||Phosphoserine|||Zinc finger protein 322 ^@ http://purl.uniprot.org/annotation/PRO_0000047531 http://togogenome.org/gene/10090:Gcfc2 ^@ http://purl.uniprot.org/uniprot/Q8BKT3 ^@ 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.|||Intron Large complex component GCFC2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000262647|||http://purl.uniprot.org/annotation/VSP_021799|||http://purl.uniprot.org/annotation/VSP_021800 http://togogenome.org/gene/10090:Spata5l1 ^@ http://purl.uniprot.org/uniprot/A0A7N9VSG0|||http://purl.uniprot.org/uniprot/Q3TER3 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ AAA+ ATPase|||ATPase family gene 2 protein homolog B|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000456283 http://togogenome.org/gene/10090:Gbp4 ^@ http://purl.uniprot.org/uniprot/A4UUI3 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ GB1/RHD3-type G|||Guanylate-binding protein 4|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000457892|||http://purl.uniprot.org/annotation/VSP_061850 http://togogenome.org/gene/10090:Rbp2 ^@ http://purl.uniprot.org/uniprot/Q059R7|||http://purl.uniprot.org/uniprot/Q08652 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Cytosolic fatty-acid binding proteins|||Retinol-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000067396 http://togogenome.org/gene/10090:Stradb ^@ http://purl.uniprot.org/uniprot/Q8K4T3 ^@ 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 ^@ In isoform 2.|||Protein kinase|||STE20-related kinase adapter protein beta ^@ http://purl.uniprot.org/annotation/PRO_0000085618|||http://purl.uniprot.org/annotation/VSP_016626|||http://purl.uniprot.org/annotation/VSP_016627 http://togogenome.org/gene/10090:Ciart ^@ http://purl.uniprot.org/uniprot/A2RTE4|||http://purl.uniprot.org/uniprot/Q3TQ03 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Circadian-associated transcriptional repressor|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000251194 http://togogenome.org/gene/10090:Serac1 ^@ http://purl.uniprot.org/uniprot/Q3U213 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane ^@ Chain|||Sequence Variant|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||In isoform 3.|||In strain: BALB/cByJ and C57BL/6J; requires 2 nucleotide substitutions.|||In strain: C57BL/6J.|||Protein SERAC1 ^@ http://purl.uniprot.org/annotation/PRO_0000274673|||http://purl.uniprot.org/annotation/VSP_022864|||http://purl.uniprot.org/annotation/VSP_022865|||http://purl.uniprot.org/annotation/VSP_022866 http://togogenome.org/gene/10090:Cyp2c23 ^@ http://purl.uniprot.org/uniprot/E9Q5K4|||http://purl.uniprot.org/uniprot/Q3UEM4 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Cytochrome P450|||Cytochrome P450 2C44|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_5003244448|||http://purl.uniprot.org/annotation/PRO_5004230066|||http://purl.uniprot.org/annotation/VSP_060520|||http://purl.uniprot.org/annotation/VSP_060521 http://togogenome.org/gene/10090:Adam17 ^@ http://purl.uniprot.org/uniprot/E9PXU2|||http://purl.uniprot.org/uniprot/Q9Z0F8 ^@ Active Site|||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|||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 Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Crambin-like|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 17|||Disordered|||Extracellular|||Helical|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphoserine|||Phosphothreonine|||SH3-binding|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029090|||http://purl.uniprot.org/annotation/PRO_0000029091|||http://purl.uniprot.org/annotation/PRO_5003243020|||http://purl.uniprot.org/annotation/VSP_005479|||http://purl.uniprot.org/annotation/VSP_005480 http://togogenome.org/gene/10090:Epn2 ^@ http://purl.uniprot.org/uniprot/J3QNT7|||http://purl.uniprot.org/uniprot/Q5NCM7|||http://purl.uniprot.org/uniprot/Q8CHU3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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|||Basic and acidic residues|||Disordered|||ENTH|||Epsin-2|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||UIM 1|||UIM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000074517|||http://purl.uniprot.org/annotation/VSP_009157 http://togogenome.org/gene/10090:Gm5458 ^@ http://purl.uniprot.org/uniprot/L7N219 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Dcp1a ^@ http://purl.uniprot.org/uniprot/Q91YD3 ^@ 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|||In strain: C57BL/6J.|||Phosphoserine|||Phosphothreonine|||Polar residues|||mRNA-decapping enzyme 1A ^@ http://purl.uniprot.org/annotation/PRO_0000189633 http://togogenome.org/gene/10090:Or10u4 ^@ http://purl.uniprot.org/uniprot/K7N727 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Plcxd2 ^@ http://purl.uniprot.org/uniprot/B2RXA1 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ PI-PLC X domain-containing protein 2|||PI-PLC X-box ^@ http://purl.uniprot.org/annotation/PRO_0000437755 http://togogenome.org/gene/10090:Coq8b ^@ http://purl.uniprot.org/uniprot/E9QLB8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ ABC1 atypical kinase-like ^@ http://togogenome.org/gene/10090:Tmem265 ^@ http://purl.uniprot.org/uniprot/E9Q8G3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:ND2 ^@ http://purl.uniprot.org/uniprot/P03893|||http://purl.uniprot.org/uniprot/Q9MD59 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ Helical|||NADH dehydrogenase subunit 2 C-terminal|||NADH-ubiquinone oxidoreductase chain 2|||NADH:quinone oxidoreductase/Mrp antiporter membrane subunit ^@ http://purl.uniprot.org/annotation/PRO_0000117607 http://togogenome.org/gene/10090:Or51f1e ^@ http://purl.uniprot.org/uniprot/E9PXW4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dhx37 ^@ http://purl.uniprot.org/uniprot/Q6NZL1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Pro residues ^@ http://togogenome.org/gene/10090:Dnajc3 ^@ http://purl.uniprot.org/uniprot/Q3UFV9|||http://purl.uniprot.org/uniprot/Q91YW3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Disordered|||DnaJ homolog subfamily C member 3|||Doesn't affect binding of misfolded proteins.|||Flexible linker|||J|||J domain-containing protein|||Phosphoserine|||Reduces binding affinity for misfolded proteins by 40%.|||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_0000071046|||http://purl.uniprot.org/annotation/PRO_5014309225 http://togogenome.org/gene/10090:Bin3 ^@ http://purl.uniprot.org/uniprot/Q9JI08 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ BAR|||Basic and acidic residues|||Bridging integrator 3|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000192956 http://togogenome.org/gene/10090:Lpin1 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VLN4|||http://purl.uniprot.org/uniprot/A0A5F8MQ53|||http://purl.uniprot.org/uniprot/E9QKQ5|||http://purl.uniprot.org/uniprot/Q8CD95|||http://purl.uniprot.org/uniprot/Q91ZP3 ^@ 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 phosphatidate phosphatase activity but does not prevent membrane association.|||Abolishes phosphatidate phosphatase activity. No effect on interaction or coactivation with PPARA.|||Abolishes phosphorylation in response to insulin but has no effect on cellular location.|||C-LIP|||DXDXT motif|||Diminishes significantly the interaction and coactivation OFPPARA; when associated with F-726.|||Diminishes significantly the interaction and coactivation OFPPARA; when associated with F-727.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In allele FLD2J; causes the fatty liver dystrophy phenotype (fld), characterized by neonatal fatty liver and hypertriglyceridemia that resolve at weaning and neuropathy affecting peripheral nerve in adulthood.|||In isoform 2.|||LNS2/PITP|||LXXIL motif|||N-LIP|||N6-acetyllysine|||Nuclear localization signal|||Phosphatidate phosphatase LPIN1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces sumoylation. Abolishes sumoylation and nuclear localization; when associated with R-599.|||Reduces sumoylation. Abolishes sumoylation and nuclear localization; when associated with R-629. ^@ http://purl.uniprot.org/annotation/PRO_0000209880|||http://purl.uniprot.org/annotation/VSP_003134 http://togogenome.org/gene/10090:Ier5 ^@ http://purl.uniprot.org/uniprot/O89113|||http://purl.uniprot.org/uniprot/Q3UJ54 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Immediate early response gene 5 protein|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000190439 http://togogenome.org/gene/10090:Cilk1 ^@ http://purl.uniprot.org/uniprot/Q69ZV0|||http://purl.uniprot.org/uniprot/Q9JKV2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Complete loss of kinase activity and of nuclear localization.|||Complete loss of kinase activity and of nuclear localization. Complete loss of kinase activity and of nuclear localization; when associated with A-270 and A-272.|||Disordered|||Loss of kinase activity and of autophosphorylation; loss of phosphorylation by CDK7; no effect on nuclear subcellular location.|||Loss of kinase activity and of autophosphorylation; no effect on phosphorylation by CDK7.|||Loss of kinase activity; loss of phosphorylation by CDK7; no effect on autophosphorylation.|||Loss of kinase activity; no effect on nuclear subcellular location.|||No effect on cilium length.|||Partial loss of autocatalytic kinase activity. Complete loss of kinase activity and of nuclear localization; when associated with A-271 and A-272.|||Partial loss of kinase activity. Complete loss of kinase activity and of nuclear localization; when associated with A-270 and A-272.|||Phosphoserine|||Phosphothreonine; by CDK7|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase ICK ^@ http://purl.uniprot.org/annotation/PRO_0000086008 http://togogenome.org/gene/10090:Usp47 ^@ http://purl.uniprot.org/uniprot/Q8BY87 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 47 ^@ http://purl.uniprot.org/annotation/PRO_0000080677|||http://purl.uniprot.org/annotation/VSP_014416 http://togogenome.org/gene/10090:4931406B18Rik ^@ http://purl.uniprot.org/uniprot/A2RSL7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015086072 http://togogenome.org/gene/10090:Klk1b5 ^@ http://purl.uniprot.org/uniprot/P15945 ^@ 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|||Kallikrein 1-related peptidase b5|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027973|||http://purl.uniprot.org/annotation/PRO_0000027974 http://togogenome.org/gene/10090:Lypd8 ^@ http://purl.uniprot.org/uniprot/Q9D7S0 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated serine|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-105; D-115; D-128; D-154; D-169; D-179; D-200 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-179 and D-200.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-179 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-200 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-179; D-200 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-169; D-179; D-200 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-154; D-169; D-179; D-200 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-128; D-154; D-169; D-179; D-200 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-115; D-128; D-154; D-169; D-179; D-200 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-76; D-105; D-115; D-128; D-154; D-169; D-179; D-200 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-179; D-200 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-179; D-200 and D-210.|||In mutant N-D: Abolished N-glycosylation; when associated with D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-179; D-200 and D-210.|||Ly6/PLAUR domain-containing protein 8|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000317741|||http://purl.uniprot.org/annotation/PRO_0000317742 http://togogenome.org/gene/10090:C130026I21Rik ^@ http://purl.uniprot.org/uniprot/Q3KNJ6|||http://purl.uniprot.org/uniprot/Q3TQS4|||http://purl.uniprot.org/uniprot/Q8C898 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||HSR|||Polar residues ^@ http://togogenome.org/gene/10090:Vwc2 ^@ http://purl.uniprot.org/uniprot/Q8C8N3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Signal Peptide ^@ Basic and acidic residues|||Brorin|||Disordered|||Mediates cell adhesion|||VWFC 1|||VWFC 2 ^@ http://purl.uniprot.org/annotation/PRO_0000307160 http://togogenome.org/gene/10090:Mrpl30 ^@ http://purl.uniprot.org/uniprot/Q9D7N6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||Large ribosomal subunit protein uL30m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000273241 http://togogenome.org/gene/10090:Gpcpd1 ^@ http://purl.uniprot.org/uniprot/Q8C0L9 ^@ 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 ^@ CBM20|||GP-PDE|||Glycerophosphocholine phosphodiesterase GPCPD1|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000251947|||http://purl.uniprot.org/annotation/VSP_020819|||http://purl.uniprot.org/annotation/VSP_020820 http://togogenome.org/gene/10090:Slc1a2 ^@ http://purl.uniprot.org/uniprot/A2APL7|||http://purl.uniprot.org/uniprot/A2APL8|||http://purl.uniprot.org/uniprot/P43006|||http://purl.uniprot.org/uniprot/Q3UYK6 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Discontinuously helical|||Disordered|||Excitatory amino acid transporter 2|||Helical|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||In isoform Glt-1A and isoform Glt-1B.|||In isoform Glt-1B.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||S-palmitoyl cysteine|||Severely impairs glutamate uptake activity. ^@ http://purl.uniprot.org/annotation/PRO_0000202062|||http://purl.uniprot.org/annotation/VSP_006264|||http://purl.uniprot.org/annotation/VSP_006265 http://togogenome.org/gene/10090:Thbs1 ^@ http://purl.uniprot.org/uniprot/Q3TR40|||http://purl.uniprot.org/uniprot/Q80YQ1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||EGF-like|||TSP C-terminal|||TSP type-3|||Thrombospondin-1|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_5004229565|||http://purl.uniprot.org/annotation/PRO_5015098949 http://togogenome.org/gene/10090:Gpr52 ^@ http://purl.uniprot.org/uniprot/P0C5J4 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||G-protein coupled receptor 52|||Helical; 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_0000307680 http://togogenome.org/gene/10090:Dnajb6 ^@ http://purl.uniprot.org/uniprot/G3X8S5|||http://purl.uniprot.org/uniprot/O54946 ^@ 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 ^@ Acidic residues|||Disordered|||DnaJ homolog subfamily B member 6|||In isoform B.|||Interaction with HSP70|||Interaction with KRT18|||J|||Omega-N-methylarginine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000071026|||http://purl.uniprot.org/annotation/VSP_026212|||http://purl.uniprot.org/annotation/VSP_026213 http://togogenome.org/gene/10090:Stk26 ^@ http://purl.uniprot.org/uniprot/A2AD85|||http://purl.uniprot.org/uniprot/Q99JT2 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase 26 ^@ http://purl.uniprot.org/annotation/PRO_0000086405 http://togogenome.org/gene/10090:Mgat4d ^@ http://purl.uniprot.org/uniprot/Q9D4R2 ^@ 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 ^@ Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000311677|||http://purl.uniprot.org/annotation/VSP_058925 http://togogenome.org/gene/10090:Gmip ^@ http://purl.uniprot.org/uniprot/Q6PGG2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||F-BAR|||GEM-interacting protein|||In isoform 2.|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000056726|||http://purl.uniprot.org/annotation/VSP_013190|||http://purl.uniprot.org/annotation/VSP_013191 http://togogenome.org/gene/10090:Insc ^@ http://purl.uniprot.org/uniprot/D3Z267|||http://purl.uniprot.org/uniprot/Q3HNM7 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes interaction with GPSM2.|||Important for interaction with GPSM2|||In isoform 2.|||PDZ-binding|||Protein inscuteable homolog|||Protein inscuteable homologue C-terminal|||Protein inscuteable homologue LGN-binding ^@ http://purl.uniprot.org/annotation/PRO_0000252406|||http://purl.uniprot.org/annotation/VSP_020951 http://togogenome.org/gene/10090:Fam222b ^@ http://purl.uniprot.org/uniprot/E9PXL0|||http://purl.uniprot.org/uniprot/Q3V2W6|||http://purl.uniprot.org/uniprot/Q6P539 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Pro residues|||Protein FAM222B ^@ http://purl.uniprot.org/annotation/PRO_0000274246 http://togogenome.org/gene/10090:Pcdhga4 ^@ http://purl.uniprot.org/uniprot/Q91XY4 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin gamma-A4 ^@ http://purl.uniprot.org/annotation/PRO_0000423520 http://togogenome.org/gene/10090:Slc6a16 ^@ http://purl.uniprot.org/uniprot/A0A1L1SR47 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Pcyt1b ^@ http://purl.uniprot.org/uniprot/Q811Q9 ^@ 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 2.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247762|||http://purl.uniprot.org/annotation/VSP_020041|||http://purl.uniprot.org/annotation/VSP_020042 http://togogenome.org/gene/10090:Hapln2 ^@ http://purl.uniprot.org/uniprot/B2RRU7|||http://purl.uniprot.org/uniprot/Q9ESM3 ^@ 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|||Ig-like V-type|||Link|||Link 1|||Link 2 ^@ http://purl.uniprot.org/annotation/PRO_0000013188|||http://purl.uniprot.org/annotation/PRO_5014298303 http://togogenome.org/gene/10090:Ncf2 ^@ http://purl.uniprot.org/uniprot/O70145 ^@ 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 ^@ Disordered|||Neutrophil cytosol factor 2|||PB1|||Phosphoserine|||Phosphothreonine|||Pro residues|||SH3 1|||SH3 2|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000312227 http://togogenome.org/gene/10090:Asb15 ^@ http://purl.uniprot.org/uniprot/Q3UQ60|||http://purl.uniprot.org/uniprot/Q8C565|||http://purl.uniprot.org/uniprot/Q8VHS6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Non-terminal Residue|||Repeat|||Sequence Conflict ^@ 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 SOCS box protein 15|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066955 http://togogenome.org/gene/10090:Pde10a ^@ http://purl.uniprot.org/uniprot/A0A384DV92|||http://purl.uniprot.org/uniprot/Q7TPG2|||http://purl.uniprot.org/uniprot/Q8CA95 ^@ 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 ^@ Decreased protein abundance; decreased 3',5'-cyclic-nucleotide phosphodiesterase activity.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PDEase|||Polar residues|||Proton donor|||cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A ^@ http://purl.uniprot.org/annotation/PRO_0000355558|||http://purl.uniprot.org/annotation/VSP_035915|||http://purl.uniprot.org/annotation/VSP_035916|||http://purl.uniprot.org/annotation/VSP_035917|||http://purl.uniprot.org/annotation/VSP_035918 http://togogenome.org/gene/10090:Leo1 ^@ http://purl.uniprot.org/uniprot/Q5XJE5 ^@ 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 ^@ Acidic residues|||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_0000247820|||http://purl.uniprot.org/annotation/VSP_020054|||http://purl.uniprot.org/annotation/VSP_020055 http://togogenome.org/gene/10090:Nat8f5 ^@ http://purl.uniprot.org/uniprot/Q9QXS8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ Helical|||N-acetyltransferase|||Probable N-acetyltransferase CML5 ^@ http://purl.uniprot.org/annotation/PRO_0000284694 http://togogenome.org/gene/10090:Comt ^@ http://purl.uniprot.org/uniprot/O88587 ^@ Binding Site|||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 ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Catechol O-methyltransferase|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform Soluble.|||Phosphoserine|||Reduces methyltransferase activity against norepinephrine. ^@ http://purl.uniprot.org/annotation/PRO_0000020973|||http://purl.uniprot.org/annotation/VSP_018779 http://togogenome.org/gene/10090:Smpd1 ^@ http://purl.uniprot.org/uniprot/Q04519 ^@ 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|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Cleavage; by CASP7|||Complete loss of activity.|||Knockin mice are fertile and healthy but show increased burdens in response to bacterial infection. Cleavage by Casp7 is abolished, ceramide synthesis is decreased, leading to increased burdens in response to bacterial infection.|||N-linked (GlcNAc...) asparagine|||No activity with sphingomyelin as substrate; retains 70% of wild-type activity with bis(p-nitrophenyl) phosphate as substrate.|||Phosphoserine|||Retains 10% of wild-type activity with sphingomyelin as substrate; retains 70% of wild-type activity with bis(p-nitrophenyl) phosphate as substrate.|||Retains 10% of wild-type activity.|||Retains 20% of wild-type activity with sphingomyelin as substrate; retains 50% of wild-type activity with bis(p-nitrophenyl) phosphate as substrate.|||Retains 20% of wild-type activity with sphingomyelin as substrate; retains 70% of wild-type activity with bis(p-nitrophenyl) phosphate as substrate.|||Saposin B-type|||Sphingomyelin phosphodiesterase|||Sphingomyelin phosphodiesterase, processed form ^@ http://purl.uniprot.org/annotation/PRO_0000002324|||http://purl.uniprot.org/annotation/PRO_0000456685 http://togogenome.org/gene/10090:Efna4 ^@ http://purl.uniprot.org/uniprot/O08542|||http://purl.uniprot.org/uniprot/Q3UQB5|||http://purl.uniprot.org/uniprot/Q9CZS8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Cell attachment site|||Disordered|||Ephrin RBD|||Ephrin RBD domain-containing protein|||Ephrin-A4|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000008375|||http://purl.uniprot.org/annotation/PRO_0000008376|||http://purl.uniprot.org/annotation/PRO_5004325846|||http://purl.uniprot.org/annotation/PRO_5010843466 http://togogenome.org/gene/10090:Myom1 ^@ http://purl.uniprot.org/uniprot/Q62234 ^@ 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|||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_0000072685|||http://purl.uniprot.org/annotation/VSP_035664 http://togogenome.org/gene/10090:Vdac3 ^@ http://purl.uniprot.org/uniprot/Q60931 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||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|||N-acetylcysteine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||Voltage-dependent anion-selective channel protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000050513 http://togogenome.org/gene/10090:Unc13b ^@ http://purl.uniprot.org/uniprot/A0A140LHX5|||http://purl.uniprot.org/uniprot/E9Q263|||http://purl.uniprot.org/uniprot/Q9Z1N9 ^@ 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 ^@ Basic and acidic residues|||C2|||C2 1|||C2 2|||C2 3|||Disordered|||In isoform 2.|||In isoform 3.|||MHD1|||MHD2|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Protein unc-13 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000188576|||http://purl.uniprot.org/annotation/VSP_039197|||http://purl.uniprot.org/annotation/VSP_039198 http://togogenome.org/gene/10090:Barx2 ^@ http://purl.uniprot.org/uniprot/O08686 ^@ 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 BarH-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000048839 http://togogenome.org/gene/10090:1700003F12Rik ^@ http://purl.uniprot.org/uniprot/A2AKE5|||http://purl.uniprot.org/uniprot/Q9DAQ3 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Stk32b ^@ http://purl.uniprot.org/uniprot/Q9JJX8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 32B ^@ http://purl.uniprot.org/annotation/PRO_0000232414 http://togogenome.org/gene/10090:Cdca7l ^@ http://purl.uniprot.org/uniprot/Q922M5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Cell division cycle-associated 7-like protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Integrase domain-binding motif 1 (IBM1)|||Integrase domain-binding motif 2 (IBM2)|||MYC-binding|||PSIP1-binding|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000249314 http://togogenome.org/gene/10090:Mok ^@ http://purl.uniprot.org/uniprot/Q9WVS4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of activity; when associated with A-159.|||Loss of activity; when associated with F-161.|||MAPK/MAK/MRK overlapping kinase|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086342|||http://purl.uniprot.org/annotation/VSP_009147|||http://purl.uniprot.org/annotation/VSP_009148|||http://purl.uniprot.org/annotation/VSP_009149|||http://purl.uniprot.org/annotation/VSP_009150 http://togogenome.org/gene/10090:Gata6 ^@ http://purl.uniprot.org/uniprot/Q61169 ^@ 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 ^@ Disordered|||GATA-type 1|||GATA-type 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Transcription factor GATA-6 ^@ http://purl.uniprot.org/annotation/PRO_0000083424|||http://purl.uniprot.org/annotation/VSP_035779 http://togogenome.org/gene/10090:Clic3 ^@ http://purl.uniprot.org/uniprot/Q9D7P7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Transmembrane ^@ 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_0000144208 http://togogenome.org/gene/10090:Gm21650 ^@ http://purl.uniprot.org/uniprot/J3QNI1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Fbxo42 ^@ http://purl.uniprot.org/uniprot/Q6PDJ6 ^@ 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 ^@ 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_0000119943 http://togogenome.org/gene/10090:Kcnj3 ^@ http://purl.uniprot.org/uniprot/B1AYE4|||http://purl.uniprot.org/uniprot/P63250|||http://purl.uniprot.org/uniprot/Q3ZAT1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Region|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||G protein-activated inward rectifier potassium channel 1|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||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_0000154939 http://togogenome.org/gene/10090:Magea3 ^@ http://purl.uniprot.org/uniprot/Q6T340 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Or9a2 ^@ http://purl.uniprot.org/uniprot/Q924H8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pdhb ^@ http://purl.uniprot.org/uniprot/Q9D051 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ Important for interaction with DLAT|||Mitochondrion|||N6-acetyllysine|||Phosphotyrosine|||Pyruvate dehydrogenase E1 component subunit beta, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000020458 http://togogenome.org/gene/10090:Ap4m1 ^@ http://purl.uniprot.org/uniprot/Q9JKC7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ AP-4 complex subunit mu-1|||MHD ^@ http://purl.uniprot.org/annotation/PRO_0000193788 http://togogenome.org/gene/10090:F8 ^@ http://purl.uniprot.org/uniprot/B2RRC9|||http://purl.uniprot.org/uniprot/B7ZNH8|||http://purl.uniprot.org/uniprot/Q06194|||http://purl.uniprot.org/uniprot/Q8BQ43 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ B|||Basic and acidic residues|||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|||F5/8 type C 1|||F5/8 type C 2|||N-linked (GlcNAc...) asparagine|||Plastocyanin-like|||Plastocyanin-like 1|||Plastocyanin-like 2|||Plastocyanin-like 3|||Plastocyanin-like 4|||Plastocyanin-like 5|||Plastocyanin-like 6|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000002972|||http://purl.uniprot.org/annotation/PRO_5002866996|||http://purl.uniprot.org/annotation/PRO_5004303807|||http://purl.uniprot.org/annotation/PRO_5015087144 http://togogenome.org/gene/10090:Pitx1 ^@ http://purl.uniprot.org/uniprot/P70314|||http://purl.uniprot.org/uniprot/Q3UQH0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Homeobox|||Interaction with PIT-1|||N-acetylmethionine|||Nuclear localization signal|||OAR|||Phosphoserine|||Pituitary homeobox 1 ^@ http://purl.uniprot.org/annotation/PRO_0000049219 http://togogenome.org/gene/10090:Or12d17 ^@ http://purl.uniprot.org/uniprot/Q8VG96 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Polr3h ^@ http://purl.uniprot.org/uniprot/Q9D2C6 ^@ Chain|||Molecule Processing ^@ Chain ^@ DNA-directed RNA polymerase III subunit RPC8 ^@ http://purl.uniprot.org/annotation/PRO_0000073995 http://togogenome.org/gene/10090:Pinlyp ^@ http://purl.uniprot.org/uniprot/B2RSX2|||http://purl.uniprot.org/uniprot/Q9CQD7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ Phospholipase A2 inhibitor N-terminal|||Phospholipase A2 inhibitor and Ly6/PLAUR domain-containing protein|||UPAR/Ly6|||phospholipase A2 inhibitor and Ly6/PLAUR domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000332738|||http://purl.uniprot.org/annotation/PRO_5014298335 http://togogenome.org/gene/10090:Dkkl1 ^@ http://purl.uniprot.org/uniprot/A0A1B0GRV4|||http://purl.uniprot.org/uniprot/Q3V2N2|||http://purl.uniprot.org/uniprot/Q9QZL9 ^@ 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|||Dickkopf-like protein 1|||Disordered|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000007229|||http://purl.uniprot.org/annotation/PRO_5004230525 http://togogenome.org/gene/10090:Ltbp2 ^@ http://purl.uniprot.org/uniprot/O08999|||http://purl.uniprot.org/uniprot/Q0VD84 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ C-terminal domain|||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; 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|||Heparin-binding|||Latent-transforming growth factor beta-binding protein 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues|||TB|||TB 1|||TB 2|||TB 3|||TB 4 ^@ http://purl.uniprot.org/annotation/PRO_0000007644 http://togogenome.org/gene/10090:Or5a3 ^@ http://purl.uniprot.org/uniprot/Q8VFV3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gls2 ^@ http://purl.uniprot.org/uniprot/Q571F8 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ ANK 1|||ANK 2|||Disordered|||Glutaminase liver isoform, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000011626 http://togogenome.org/gene/10090:Or4c29 ^@ http://purl.uniprot.org/uniprot/Q3SXJ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp738 ^@ http://purl.uniprot.org/uniprot/B8JJX8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dpt ^@ http://purl.uniprot.org/uniprot/Q9QZZ6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ 1-1|||1-2|||2 X 53-55 AA tandem repeats|||2-1|||2-2|||2-3|||3 X 6 AA tandem repeats of D-R-[EQ]-W-[NQK]-[FY]|||Dermatopontin|||Or C-106 with C-132|||Or C-90 with C-133|||Pyrrolidone carboxylic acid|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000007369 http://togogenome.org/gene/10090:Pwwp4c ^@ http://purl.uniprot.org/uniprot/A3KG49 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Traf3ip3 ^@ http://purl.uniprot.org/uniprot/B2RPU5|||http://purl.uniprot.org/uniprot/G3X949|||http://purl.uniprot.org/uniprot/Q8C0G2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Anchor for type IV membrane protein|||Polar residues|||TRAF3-interacting JNK-activating modulator ^@ http://purl.uniprot.org/annotation/PRO_0000072404 http://togogenome.org/gene/10090:Vmn1r243 ^@ http://purl.uniprot.org/uniprot/K9J7G6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sox9 ^@ http://purl.uniprot.org/uniprot/Q04887 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 9aaTAD 1|||9aaTAD 2|||9aaTAD 3|||Abolished phosphorylation by PKA, leading to deacreased ability to activate transcription of target genes; does not affect subcellular localization; when associated with A-211.|||Abolished phosphorylation by PKA, leading to deacreased ability to activate transcription of target genes; does not affect subcellular localization; when associated with A-64.|||Basic and acidic residues|||Dimerization (DIM)|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HMG box|||Increased stability.|||PQA|||Phosphoserine; by PKA|||Polar residues|||Pro residues|||Transactivation domain (TAC)|||Transactivation domain (TAM)|||Transcription factor SOX-9 ^@ http://purl.uniprot.org/annotation/PRO_0000048741 http://togogenome.org/gene/10090:Sgcz ^@ http://purl.uniprot.org/uniprot/Q8BX51 ^@ 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; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Zeta-sarcoglycan ^@ http://purl.uniprot.org/annotation/PRO_0000031679|||http://purl.uniprot.org/annotation/VSP_018885 http://togogenome.org/gene/10090:Dctn2 ^@ http://purl.uniprot.org/uniprot/Q3TPZ5|||http://purl.uniprot.org/uniprot/Q99KJ8 ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Dynactin subunit 2|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000079822 http://togogenome.org/gene/10090:Aoc1l2 ^@ http://purl.uniprot.org/uniprot/E9Q745 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Signal Peptide ^@ 2',4',5'-topaquinone|||Amine oxidase|||Copper amine oxidase N2-terminal|||Copper amine oxidase N3-terminal|||Copper amine oxidase catalytic|||Proton acceptor|||Schiff-base intermediate with substrate; via topaquinone ^@ http://purl.uniprot.org/annotation/PRO_5003243115 http://togogenome.org/gene/10090:Jrkl ^@ http://purl.uniprot.org/uniprot/B2RRL2 ^@ 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_0000379975 http://togogenome.org/gene/10090:Klra1 ^@ http://purl.uniprot.org/uniprot/Q8MHR8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Gm21466 ^@ http://purl.uniprot.org/uniprot/A0A571BDE3 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Mup15 ^@ http://purl.uniprot.org/uniprot/A9R9W0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5002742409 http://togogenome.org/gene/10090:Gstm7 ^@ http://purl.uniprot.org/uniprot/Q80W21 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Turn ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 7 ^@ http://purl.uniprot.org/annotation/PRO_0000333228 http://togogenome.org/gene/10090:Sirpd ^@ http://purl.uniprot.org/uniprot/Q1AN91 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097053 http://togogenome.org/gene/10090:Rassf4 ^@ http://purl.uniprot.org/uniprot/Q8CB96 ^@ 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.|||In isoform 3.|||Phosphoserine|||Ras association domain-containing protein 4|||Ras-associating|||SARAH ^@ http://purl.uniprot.org/annotation/PRO_0000240399|||http://purl.uniprot.org/annotation/VSP_019360|||http://purl.uniprot.org/annotation/VSP_019361|||http://purl.uniprot.org/annotation/VSP_019362 http://togogenome.org/gene/10090:Omd ^@ http://purl.uniprot.org/uniprot/O35103 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide ^@ 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_0000032755 http://togogenome.org/gene/10090:Zdhhc2 ^@ http://purl.uniprot.org/uniprot/P59267 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Decreased localization to the plasma membrane.|||Disordered|||Helical|||Increased localization to the plasma membrane.|||Loss of localization to the plasma membrane.|||Loss of protein-cysteine S-palmitoyltransferase activity. Loss of autopalmitoylation.|||Lumenal|||Mediates localization to plasma membrane and recycling endosomes|||NPxY-like endocytic signal|||No effect on subcellular localization.|||Non-canonical dileucine endocytic signal|||Palmitoyltransferase ZDHHC2|||Polar residues|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212860 http://togogenome.org/gene/10090:Gjb4 ^@ http://purl.uniprot.org/uniprot/A0A654ICD1|||http://purl.uniprot.org/uniprot/Q02738|||http://purl.uniprot.org/uniprot/Q8C677 ^@ Chain|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Topological Domain|||Transmembrane ^@ Connexin N-terminal|||Cytoplasmic|||Extracellular|||Gap junction beta-4 protein|||Gap junction protein cysteine-rich|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000057866 http://togogenome.org/gene/10090:Ssbp3 ^@ http://purl.uniprot.org/uniprot/Q3U5B9|||http://purl.uniprot.org/uniprot/Q9D032 ^@ 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|||Disordered|||In isoform 2.|||LisH|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Single-stranded DNA-binding protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000123829|||http://purl.uniprot.org/annotation/VSP_006262 http://togogenome.org/gene/10090:Cdcp1 ^@ http://purl.uniprot.org/uniprot/Q5U462 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ CUB|||CUB domain-containing protein 1|||Cleavage; by ST14/MT-SP1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000226250 http://togogenome.org/gene/10090:Prss32 ^@ http://purl.uniprot.org/uniprot/E9Q409 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5003243072 http://togogenome.org/gene/10090:Ahi1 ^@ http://purl.uniprot.org/uniprot/E9Q552|||http://purl.uniprot.org/uniprot/E9QP54 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||SH3|||WD ^@ http://togogenome.org/gene/10090:Il11ra2 ^@ http://purl.uniprot.org/uniprot/P70225 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like C2-type|||Interleukin-11 receptor subunit alpha-2|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010915 http://togogenome.org/gene/10090:Tmem37 ^@ http://purl.uniprot.org/uniprot/Q9JJV3 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Voltage-dependent calcium channel gamma-like subunit ^@ http://purl.uniprot.org/annotation/PRO_0000164693 http://togogenome.org/gene/10090:Prkcq ^@ http://purl.uniprot.org/uniprot/A6H667|||http://purl.uniprot.org/uniprot/Q02111 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn|||Zinc Finger ^@ AGC-kinase C-terminal|||C2|||Disordered|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by PDPK1|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by LCK|||Protein kinase|||Protein kinase C theta type|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000055709 http://togogenome.org/gene/10090:Fcgr3 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1M6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5002091802 http://togogenome.org/gene/10090:Resf1 ^@ http://purl.uniprot.org/uniprot/B2KFD2|||http://purl.uniprot.org/uniprot/Q5DTW7 ^@ 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|||Polar residues|||Retroelement silencing factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000295243|||http://purl.uniprot.org/annotation/VSP_026863 http://togogenome.org/gene/10090:Or8b51 ^@ http://purl.uniprot.org/uniprot/Q8VG53 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nedd9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J212|||http://purl.uniprot.org/uniprot/O35177 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Caspase cleavage related site|||Disordered|||Divergent helix-loop-helix motif|||Enhancer of filamentation 1|||Interacts with CTTN|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Required for interaction with PLK1|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000089329 http://togogenome.org/gene/10090:Rfc5 ^@ http://purl.uniprot.org/uniprot/Q5HZI8|||http://purl.uniprot.org/uniprot/Q9D0F6 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ AAA+ ATPase|||Replication factor C subunit 5 ^@ http://purl.uniprot.org/annotation/PRO_0000121752 http://togogenome.org/gene/10090:Asic4 ^@ http://purl.uniprot.org/uniprot/Q7TNS7 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Acid-sensing ion channel 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000181305 http://togogenome.org/gene/10090:Gtf2f1 ^@ http://purl.uniprot.org/uniprot/Q3THK3 ^@ 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|||General transcription factor IIF subunit 1|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000260322 http://togogenome.org/gene/10090:Zbtb6 ^@ http://purl.uniprot.org/uniprot/Q8K088 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger ^@ BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Phosphoserine|||Zinc finger and BTB domain-containing protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000047609 http://togogenome.org/gene/10090:Cbln2 ^@ http://purl.uniprot.org/uniprot/Q8BGU2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Signal Peptide ^@ C1q|||Cerebellin-2|||Interchain|||N-linked (GlcNAc...) asparagine|||No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with NRXN1 and NRXN3. Total loss of N-glycosylation; when associated with Q-110.|||No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with NRXN1. Total loss of N-glycosylation; when associated with Q-53. ^@ http://purl.uniprot.org/annotation/PRO_0000003552 http://togogenome.org/gene/10090:Tmem151b ^@ http://purl.uniprot.org/uniprot/Q68FE7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Transmembrane protein 151B ^@ http://purl.uniprot.org/annotation/PRO_0000307221 http://togogenome.org/gene/10090:Rab5b ^@ http://purl.uniprot.org/uniprot/B2RPS1|||http://purl.uniprot.org/uniprot/P61021 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Effector region|||N-acetylthreonine|||Phosphoserine|||Polar residues|||Ras-related protein Rab-5B|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121108 http://togogenome.org/gene/10090:Rmi2 ^@ http://purl.uniprot.org/uniprot/Q3UPE3 ^@ Chain|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||DNA Binding|||Modified Residue|||Splice Variant ^@ In isoform 2.|||OB|||Phosphoserine|||RecQ-mediated genome instability protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000297578|||http://purl.uniprot.org/annotation/VSP_027288 http://togogenome.org/gene/10090:C1qtnf2 ^@ http://purl.uniprot.org/uniprot/Q9D8U4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 2|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000320083 http://togogenome.org/gene/10090:Serpina16 ^@ http://purl.uniprot.org/uniprot/D3Z660 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Serpin ^@ http://purl.uniprot.org/annotation/PRO_5015088527 http://togogenome.org/gene/10090:Or9g20 ^@ http://purl.uniprot.org/uniprot/A2ASV2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H4c3 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Foxi1 ^@ http://purl.uniprot.org/uniprot/Q922I5 ^@ 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 I1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000091847 http://togogenome.org/gene/10090:Gm10406 ^@ http://purl.uniprot.org/uniprot/A6NAS4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tubb4a ^@ http://purl.uniprot.org/uniprot/Q9D6F9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict ^@ 5-glutamyl polyglutamate|||MREI motif|||Phosphoserine; by CDK1|||Tubulin beta-4A chain ^@ http://purl.uniprot.org/annotation/PRO_0000048254 http://togogenome.org/gene/10090:Kcnj14 ^@ http://purl.uniprot.org/uniprot/Q8JZN3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ATP-sensitive inward rectifier potassium channel 14|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Polar residues|||Pore-forming|||S-nitrosocysteine|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000154969 http://togogenome.org/gene/10090:Tcl1b2 ^@ http://purl.uniprot.org/uniprot/P56841 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein TCL1B2 ^@ http://purl.uniprot.org/annotation/PRO_0000184492 http://togogenome.org/gene/10090:Cnih1 ^@ http://purl.uniprot.org/uniprot/O35372 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Protein cornichon homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000122223 http://togogenome.org/gene/10090:Otol1 ^@ http://purl.uniprot.org/uniprot/Q4ZJM7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 5-hydroxylysine|||Basic and acidic residues|||C1q|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Disordered|||Hydroxyproline|||O-linked (Gal...) hydroxylysine|||Otolin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000332216 http://togogenome.org/gene/10090:Klhl25 ^@ http://purl.uniprot.org/uniprot/Q8R2P1 ^@ 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 25 ^@ http://purl.uniprot.org/annotation/PRO_0000272309 http://togogenome.org/gene/10090:Lmcd1 ^@ http://purl.uniprot.org/uniprot/Q3TVW6|||http://purl.uniprot.org/uniprot/Q8BVZ6|||http://purl.uniprot.org/uniprot/Q8VEE1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||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_0000075816 http://togogenome.org/gene/10090:Ankfy1 ^@ http://purl.uniprot.org/uniprot/Q810B6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 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|||FYVE-type|||In isoform 2.|||Interaction with RHOD and RAB5A|||N-acetylalanine|||NPF|||Phosphoserine|||Rabankyrin-5|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000066891|||http://purl.uniprot.org/annotation/VSP_007917|||http://purl.uniprot.org/annotation/VSP_007918 http://togogenome.org/gene/10090:Abhd13 ^@ http://purl.uniprot.org/uniprot/Q80UX8 ^@ Active Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Transmembrane ^@ Charge relay system|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Protein ABHD13 ^@ http://purl.uniprot.org/annotation/PRO_0000281077 http://togogenome.org/gene/10090:Apip ^@ http://purl.uniprot.org/uniprot/Q9WVQ5 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Methylthioribulose-1-phosphate dehydratase|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000239023 http://togogenome.org/gene/10090:Potefam3e ^@ http://purl.uniprot.org/uniprot/D3Z1P8 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ ANK|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Sntn ^@ http://purl.uniprot.org/uniprot/Q8C9X1 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Sentan ^@ http://purl.uniprot.org/annotation/PRO_0000342517 http://togogenome.org/gene/10090:Tpgs2 ^@ http://purl.uniprot.org/uniprot/E9PUD7|||http://purl.uniprot.org/uniprot/E9QLP0|||http://purl.uniprot.org/uniprot/Q66JT5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Knr4/Smi1-like|||Pro residues|||Tubulin polyglutamylase complex subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000079305 http://togogenome.org/gene/10090:Mcm5 ^@ http://purl.uniprot.org/uniprot/P49718|||http://purl.uniprot.org/uniprot/Q8BQ03 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif ^@ Arginine finger|||DNA replication licensing factor MCM5|||MCM|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194108 http://togogenome.org/gene/10090:Or5m5 ^@ http://purl.uniprot.org/uniprot/A0PK66|||http://purl.uniprot.org/uniprot/Q8VFL5 ^@ 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 5M5 ^@ http://purl.uniprot.org/annotation/PRO_0000150862 http://togogenome.org/gene/10090:Zfp710 ^@ http://purl.uniprot.org/uniprot/Q3U288 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Crosslink|||Region|||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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Zinc finger protein 710 ^@ http://purl.uniprot.org/annotation/PRO_0000233709|||http://purl.uniprot.org/annotation/VSP_018152|||http://purl.uniprot.org/annotation/VSP_026943 http://togogenome.org/gene/10090:Dip2c ^@ http://purl.uniprot.org/uniprot/B2RQ71 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DMAP1-binding|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Fhl4 ^@ http://purl.uniprot.org/uniprot/Q8CDC8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ LIM zinc-binding ^@ http://togogenome.org/gene/10090:Syne3 ^@ http://purl.uniprot.org/uniprot/Q4FZC9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Interchain (C-577 in SUN2); alternate|||Interchain (with C-759 in SUN1)|||KASH|||Nesprin-3|||Perinuclear space|||Spectrin 1|||Spectrin 2 ^@ http://purl.uniprot.org/annotation/PRO_0000281121|||http://purl.uniprot.org/annotation/VSP_023979|||http://purl.uniprot.org/annotation/VSP_023980 http://togogenome.org/gene/10090:Armc1 ^@ http://purl.uniprot.org/uniprot/Q9D7A8 ^@ 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 ^@ ARM|||Armadillo repeat-containing protein 1|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000240883 http://togogenome.org/gene/10090:C1qtnf7 ^@ http://purl.uniprot.org/uniprot/E9PVG1|||http://purl.uniprot.org/uniprot/Q5BKS0|||http://purl.uniprot.org/uniprot/Q8BVD7 ^@ 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 ^@ Basic and acidic residues|||C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 7|||Disordered|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000003540|||http://purl.uniprot.org/annotation/PRO_5009953751|||http://purl.uniprot.org/annotation/PRO_5014309726 http://togogenome.org/gene/10090:Gm4567 ^@ http://purl.uniprot.org/uniprot/Q3UTA8 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Jdp2 ^@ http://purl.uniprot.org/uniprot/P97875 ^@ 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 ^@ Basic and acidic residues|||Basic motif|||Blocks phosphorylation by MAPK8.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Jun dimerization protein 2|||Leucine-zipper|||Phosphothreonine; by MAPK8|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000331131 http://togogenome.org/gene/10090:Vwa5b1 ^@ http://purl.uniprot.org/uniprot/A9Z1V5|||http://purl.uniprot.org/uniprot/B1AZ81 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||VIT|||VWFA|||von Willebrand factor A domain-containing protein 5B1 ^@ http://purl.uniprot.org/annotation/PRO_0000326174 http://togogenome.org/gene/10090:Rnh1 ^@ http://purl.uniprot.org/uniprot/Q91VI7 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Strand ^@ 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|||Phosphoserine|||Ribonuclease inhibitor ^@ http://purl.uniprot.org/annotation/PRO_0000097344 http://togogenome.org/gene/10090:Cxcl17 ^@ http://purl.uniprot.org/uniprot/Q5UW37 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Signal Peptide|||Site ^@ 4-Cys CXCL17|||Basic residues|||C-X-C motif chemokine 17|||Cleavage|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000438488|||http://purl.uniprot.org/annotation/PRO_5000000292 http://togogenome.org/gene/10090:Slc4a4 ^@ http://purl.uniprot.org/uniprot/A2VDF7|||http://purl.uniprot.org/uniprot/A7E1Z5|||http://purl.uniprot.org/uniprot/E9Q8N8|||http://purl.uniprot.org/uniprot/O88343 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Band 3 cytoplasmic|||Basic and acidic residues|||Basic residues|||Bicarbonate transporter-like transmembrane|||CA2-binding|||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.|||Interaction with CA4|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Required for basolateral targeting|||Required for interaction with AHCYL1 ^@ http://purl.uniprot.org/annotation/PRO_0000079228|||http://purl.uniprot.org/annotation/VSP_016709|||http://purl.uniprot.org/annotation/VSP_016710|||http://purl.uniprot.org/annotation/VSP_016711|||http://purl.uniprot.org/annotation/VSP_016712 http://togogenome.org/gene/10090:Hmces ^@ http://purl.uniprot.org/uniprot/Q8R1M0 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site ^@ Abasic site processing protein HMCES|||Accumulation of uncleaved form with the N-terminal methionine.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nucleophile|||PIP-box|||Phosphoserine|||Removed|||Required for sensing abasic sites|||Required to stabilize abasic sites|||Stimulates cleavage of the N-terminal methionine.|||Thiazolidine linkage to a ring-opened DNA abasic site ^@ http://purl.uniprot.org/annotation/PRO_0000164395 http://togogenome.org/gene/10090:Mip ^@ http://purl.uniprot.org/uniprot/P51180 ^@ Chain|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Important for formation of cell junction|||Important for water channel gating|||In LOP.|||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_0000063913 http://togogenome.org/gene/10090:Tor2a ^@ http://purl.uniprot.org/uniprot/Q8R1J9 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Localizes in the nuclear envelope.|||N-linked (GlcNAc...) asparagine|||Torsin-2A ^@ http://purl.uniprot.org/annotation/PRO_0000228830|||http://purl.uniprot.org/annotation/VSP_017705 http://togogenome.org/gene/10090:Srf ^@ http://purl.uniprot.org/uniprot/Q9JM73 ^@ Chain|||DNA Binding|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region ^@ Disordered|||Involved in dimerization|||MADS-box|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphoserine; by dsDNA kinase|||Serum response factor ^@ http://purl.uniprot.org/annotation/PRO_0000245225 http://togogenome.org/gene/10090:Dvl3 ^@ http://purl.uniprot.org/uniprot/E9Q967|||http://purl.uniprot.org/uniprot/Q61062 ^@ 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 ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Basic and acidic residues|||Basic residues|||DEP|||DIX|||Dimethylated arginine; alternate|||Disordered|||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_0000145750 http://togogenome.org/gene/10090:Csk ^@ http://purl.uniprot.org/uniprot/P41241 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Interaction with PTPN22|||N-acetylserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||SH2|||SH3|||Tyrosine-protein kinase CSK ^@ http://purl.uniprot.org/annotation/PRO_0000088071 http://togogenome.org/gene/10090:Pde9a ^@ http://purl.uniprot.org/uniprot/O70628|||http://purl.uniprot.org/uniprot/Q8BSU4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A|||PDEase|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000198842 http://togogenome.org/gene/10090:Hrob ^@ http://purl.uniprot.org/uniprot/Q32P12 ^@ 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|||Homologous recombination OB-fold protein|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288093|||http://purl.uniprot.org/annotation/VSP_025656 http://togogenome.org/gene/10090:Ddr2 ^@ http://purl.uniprot.org/uniprot/Q62371 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Abolishes kinase activity. Reduces tyrosine phosphorylation by 90%; when associated with F-471.|||Cytoplasmic|||Discoidin domain-containing receptor 2|||Disordered|||Extracellular|||F5/8 type C|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC and autocatalysis|||Protein kinase|||Proton acceptor|||Reduces tyrosine phosphorylation by 90%; when associated with E-608. ^@ http://purl.uniprot.org/annotation/PRO_0000016747 http://togogenome.org/gene/10090:Or14j1 ^@ http://purl.uniprot.org/uniprot/Q14AJ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tie1 ^@ http://purl.uniprot.org/uniprot/Q06806 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase receptor Tie-1 ^@ http://purl.uniprot.org/annotation/PRO_0000024472 http://togogenome.org/gene/10090:Ccr4 ^@ http://purl.uniprot.org/uniprot/P51680 ^@ 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 ^@ C-C chemokine receptor type 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_0000069246 http://togogenome.org/gene/10090:Aspscr1 ^@ http://purl.uniprot.org/uniprot/Q8VBT9 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with GLUT4|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Tether containing UBX domain for GLUT4|||UBX ^@ http://purl.uniprot.org/annotation/PRO_0000249886|||http://purl.uniprot.org/annotation/VSP_020579|||http://purl.uniprot.org/annotation/VSP_020580 http://togogenome.org/gene/10090:Klrc2 ^@ http://purl.uniprot.org/uniprot/Q9WTJ9|||http://purl.uniprot.org/uniprot/Q9WVJ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ C-type lectin|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Pabpc2 ^@ http://purl.uniprot.org/uniprot/Q62029 ^@ Domain Extent|||Region ^@ Domain Extent ^@ PABC|||RRM ^@ http://togogenome.org/gene/10090:Cdc34 ^@ http://purl.uniprot.org/uniprot/Q8CFI2 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Glycyl thioester intermediate|||Phosphoserine; by CK2|||Phosphothreonine; by CK2|||SCF-binding|||UBC core|||Ubiquitin-conjugating enzyme E2 R1 ^@ http://purl.uniprot.org/annotation/PRO_0000082452 http://togogenome.org/gene/10090:H2-T3 ^@ http://purl.uniprot.org/uniprot/Q05A75|||http://purl.uniprot.org/uniprot/Q8HWB4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like|||Ig-like domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5004308107|||http://purl.uniprot.org/annotation/PRO_5015096888 http://togogenome.org/gene/10090:Tmem101 ^@ http://purl.uniprot.org/uniprot/Q91VP7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 101 ^@ http://purl.uniprot.org/annotation/PRO_0000240865 http://togogenome.org/gene/10090:Mapk8ip1 ^@ http://purl.uniprot.org/uniprot/Q3UI81|||http://purl.uniprot.org/uniprot/Q6GQW8|||http://purl.uniprot.org/uniprot/Q9WVI9 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||C-Jun-amino-terminal kinase-interacting protein 1|||D-box 1|||D-box 2|||Disordered|||In isoform JIP-1a.|||In isoform JIP-1c and isoform JIP-1d.|||In isoform JIP-1d.|||In isoform JIP-1e.|||In strain: ILS.|||Interaction with MAP3K7|||Interaction with VRK2|||JNK-binding domain (JBD)|||Minimal inhibitory domain (MID)|||PID|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK8, MAPK9 and MAPK10|||Polar residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000220629|||http://purl.uniprot.org/annotation/VSP_002763|||http://purl.uniprot.org/annotation/VSP_002764|||http://purl.uniprot.org/annotation/VSP_002765|||http://purl.uniprot.org/annotation/VSP_002766 http://togogenome.org/gene/10090:Med10 ^@ http://purl.uniprot.org/uniprot/Q9CXU0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Mediator of RNA polymerase II transcription subunit 10 ^@ http://purl.uniprot.org/annotation/PRO_0000303153 http://togogenome.org/gene/10090:Hdac3 ^@ http://purl.uniprot.org/uniprot/O88895|||http://purl.uniprot.org/uniprot/Q9JM08 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Basic and acidic residues|||Deacetylase-dead mutant. No effect on its interaction with BMAL1, CRY1 and FBXL3 or its ability to regulate the circadian clock.|||Disordered|||Histone deacetylase|||Histone deacetylase 3|||In isoform Short.|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000114697|||http://purl.uniprot.org/annotation/VSP_002080 http://togogenome.org/gene/10090:Tmed2 ^@ http://purl.uniprot.org/uniprot/A2RS53|||http://purl.uniprot.org/uniprot/Q9R0Q3 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||Embryonic lethal.|||GOLD|||Helical|||Interaction with F2RL1|||Lumenal|||Required for TMED10 and TMED2 cis-Golgi network localization|||Transmembrane emp24 domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000010382|||http://purl.uniprot.org/annotation/PRO_5014296811 http://togogenome.org/gene/10090:Wdr48 ^@ http://purl.uniprot.org/uniprot/Q8BH57 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphothreonine|||Phosphotyrosine|||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_0000051401|||http://purl.uniprot.org/annotation/VSP_016778|||http://purl.uniprot.org/annotation/VSP_016779|||http://purl.uniprot.org/annotation/VSP_016780 http://togogenome.org/gene/10090:Cd2 ^@ http://purl.uniprot.org/uniprot/P08920|||http://purl.uniprot.org/uniprot/Q549Q4 ^@ 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 ^@ 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|||N-linked (GlcNAc...) asparagine|||Pro residues|||T-cell surface antigen CD2 ^@ http://purl.uniprot.org/annotation/PRO_0000014602|||http://purl.uniprot.org/annotation/PRO_5014309638 http://togogenome.org/gene/10090:Socs2 ^@ http://purl.uniprot.org/uniprot/O35717|||http://purl.uniprot.org/uniprot/Q548Q7 ^@ 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 ubiquitin)|||Interaction with AREL1|||Phosphoserine|||Phosphoserine; by PKC|||SH2|||SOCS box|||Suppressor of cytokine signaling 2 ^@ http://purl.uniprot.org/annotation/PRO_0000181239 http://togogenome.org/gene/10090:Actr8 ^@ http://purl.uniprot.org/uniprot/Q8R2S9 ^@ 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 ^@ Actin-related protein 8|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000089124 http://togogenome.org/gene/10090:Ago1 ^@ http://purl.uniprot.org/uniprot/A0A6I8MX18|||http://purl.uniprot.org/uniprot/Q8BJP2|||http://purl.uniprot.org/uniprot/Q8CJG1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Impairs access of bound RNA to the active site|||Interaction with guide RNA|||PAZ|||Piwi|||Protein argonaute-1 ^@ http://purl.uniprot.org/annotation/PRO_0000194056 http://togogenome.org/gene/10090:Otp ^@ http://purl.uniprot.org/uniprot/O09113 ^@ 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_0000049204 http://togogenome.org/gene/10090:Mtfp1 ^@ http://purl.uniprot.org/uniprot/Q9CRB8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Mitochondrial fission process protein 1|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000212412 http://togogenome.org/gene/10090:Ifna6 ^@ http://purl.uniprot.org/uniprot/Q810G5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015098932 http://togogenome.org/gene/10090:Adgrg7 ^@ http://purl.uniprot.org/uniprot/Q8BM96 ^@ 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 ^@ Adhesion G-protein coupled receptor G7|||Cytoplasmic|||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_0000012904 http://togogenome.org/gene/10090:Hnrnph2 ^@ http://purl.uniprot.org/uniprot/P70333 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat ^@ 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|||N-acetylmethionine|||N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||RRM 1|||RRM 2|||RRM 3|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000081860|||http://purl.uniprot.org/annotation/PRO_0000434386 http://togogenome.org/gene/10090:Emp1 ^@ http://purl.uniprot.org/uniprot/P47801|||http://purl.uniprot.org/uniprot/Q05BR0|||http://purl.uniprot.org/uniprot/Q4FK43 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Epithelial membrane protein 1|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000164654 http://togogenome.org/gene/10090:Tas2r117 ^@ http://purl.uniprot.org/uniprot/Q7M715 ^@ 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 117 ^@ http://purl.uniprot.org/annotation/PRO_0000248477 http://togogenome.org/gene/10090:Kifc5b ^@ http://purl.uniprot.org/uniprot/E9PUA5|||http://purl.uniprot.org/uniprot/Q9JKY9|||http://purl.uniprot.org/uniprot/Q9QWT9 ^@ 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|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Kinesin motor|||Kinesin-like protein KIFC1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000302089|||http://purl.uniprot.org/annotation/VSP_052526|||http://purl.uniprot.org/annotation/VSP_052527 http://togogenome.org/gene/10090:Shox2 ^@ http://purl.uniprot.org/uniprot/A0A140T8S9|||http://purl.uniprot.org/uniprot/P70390 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Homeobox|||In isoform 2.|||OAR|||Short stature homeobox protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000049293|||http://purl.uniprot.org/annotation/VSP_002289 http://togogenome.org/gene/10090:Zglp1 ^@ http://purl.uniprot.org/uniprot/Q1WG82 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Zinc Finger ^@ Disordered|||GATA-type|||GATA-type zinc finger protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317558 http://togogenome.org/gene/10090:Klf2 ^@ http://purl.uniprot.org/uniprot/Q3V293|||http://purl.uniprot.org/uniprot/Q60843 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ 9aaTAD|||Abolishes polyubiquitination; when associated with R-121.|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Greatly impairs polyubiquitination. Abolishes polyubiquitination; when associated with R-146.|||Interaction with WWP1|||Krueppel-like factor 2|||Phosphoserine|||Phosphothreonine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000047163 http://togogenome.org/gene/10090:Mia3 ^@ http://purl.uniprot.org/uniprot/Q8BI84 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Mediates interaction with MIA2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||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_0000288999|||http://purl.uniprot.org/annotation/VSP_025865|||http://purl.uniprot.org/annotation/VSP_025866|||http://purl.uniprot.org/annotation/VSP_025867|||http://purl.uniprot.org/annotation/VSP_025868 http://togogenome.org/gene/10090:Fads3 ^@ http://purl.uniprot.org/uniprot/Q3T9H9|||http://purl.uniprot.org/uniprot/Q9JJE7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict|||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_0000307109 http://togogenome.org/gene/10090:Dgka ^@ http://purl.uniprot.org/uniprot/O88673 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger ^@ DAGKc|||Diacylglycerol kinase alpha|||EF-hand 1|||EF-hand 2|||N6-acetyllysine|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000218454 http://togogenome.org/gene/10090:Or5p63 ^@ http://purl.uniprot.org/uniprot/Q7TRU9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Chmp2b ^@ http://purl.uniprot.org/uniprot/Q8BJF9 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Charged multivesicular body protein 2b|||Disordered|||MIT-interacting motif|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000211470 http://togogenome.org/gene/10090:Ptgis ^@ http://purl.uniprot.org/uniprot/O35074 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Helical|||Prostacyclin synthase|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051911 http://togogenome.org/gene/10090:Lrwd1 ^@ http://purl.uniprot.org/uniprot/Q8BUI3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Region|||Repeat ^@ Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||Leucine-rich repeat and WD repeat-containing protein 1|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000310995 http://togogenome.org/gene/10090:Heatr1 ^@ http://purl.uniprot.org/uniprot/G3X9B1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BP28 C-terminal ^@ http://togogenome.org/gene/10090:Pml ^@ http://purl.uniprot.org/uniprot/A0A068EW80|||http://purl.uniprot.org/uniprot/D3Z3A6|||http://purl.uniprot.org/uniprot/Q60953|||http://purl.uniprot.org/uniprot/Q8BSJ6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ B box-type|||B box-type 1|||B box-type 2|||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 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.|||Interaction with PER2|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nuclear localization signal|||PML-like coiled-coil|||Phosphoserine|||Phosphoserine; by CDK1 and CDK2|||Phosphoserine; by CK2|||Phosphoserine; by HIPK2|||Phosphoserine; by HIPK2 and MAPK1|||Phosphoserine; by MAPK1|||Phosphothreonine|||Polar residues|||Protein PML|||RING-type|||Sumo interaction motif (SIM) ^@ http://purl.uniprot.org/annotation/PRO_0000056002|||http://purl.uniprot.org/annotation/VSP_026028 http://togogenome.org/gene/10090:Ppm1k ^@ http://purl.uniprot.org/uniprot/B9EHW0|||http://purl.uniprot.org/uniprot/Q8BXN7 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||PPM-type phosphatase|||Phosphoserine|||Protein phosphatase 1K, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000278209 http://togogenome.org/gene/10090:Troap ^@ http://purl.uniprot.org/uniprot/B7ZNG4 ^@ 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|||Tastin ^@ http://purl.uniprot.org/annotation/PRO_0000394294 http://togogenome.org/gene/10090:Ranbp1 ^@ http://purl.uniprot.org/uniprot/P34022 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||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_0000213668 http://togogenome.org/gene/10090:Sec13 ^@ http://purl.uniprot.org/uniprot/Q9D1M0 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ N-acetylvaline|||Phosphoserine|||Protein SEC13 homolog|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000051204 http://togogenome.org/gene/10090:Vmn1r252 ^@ http://purl.uniprot.org/uniprot/K9J7G4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc38a6 ^@ http://purl.uniprot.org/uniprot/G3UVW3 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||N-acetylmethionine|||Phosphoserine|||Solute carrier family 38 member 6 ^@ http://purl.uniprot.org/annotation/PRO_0000434577 http://togogenome.org/gene/10090:Casd1 ^@ http://purl.uniprot.org/uniprot/Q7TN73 ^@ Active Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Acyl-ester intermediate|||Cytoplasmic|||Helical|||Lumenal|||N-acetylneuraminate 9-O-acetyltransferase|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000307231 http://togogenome.org/gene/10090:Mat2a ^@ http://purl.uniprot.org/uniprot/Q3THS6|||http://purl.uniprot.org/uniprot/Q99J57 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Flexible loop|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000174437 http://togogenome.org/gene/10090:Fam174c ^@ http://purl.uniprot.org/uniprot/Q9DAZ5 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein FAM174C ^@ http://purl.uniprot.org/annotation/PRO_0000393874 http://togogenome.org/gene/10090:Crabp1 ^@ http://purl.uniprot.org/uniprot/P62965 ^@ Binding Site|||Chain|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand ^@ Binding Site|||Chain|||Helix|||Motif|||Strand ^@ Cellular retinoic acid-binding protein 1|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000067407 http://togogenome.org/gene/10090:Vmn2r8 ^@ http://purl.uniprot.org/uniprot/L7N472 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982456 http://togogenome.org/gene/10090:Bloc1s2 ^@ http://purl.uniprot.org/uniprot/Q9CWG9 ^@ 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|||Biogenesis of lysosome-related organelles complex 1 subunit 2|||Disordered|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000234545 http://togogenome.org/gene/10090:Cyp2f2 ^@ http://purl.uniprot.org/uniprot/P33267 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Cytochrome P450 2F2|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051760 http://togogenome.org/gene/10090:Txnl1 ^@ http://purl.uniprot.org/uniprot/Q8CDN6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ PITH|||Phosphoserine|||Redox-active|||Thioredoxin|||Thioredoxin-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000120017 http://togogenome.org/gene/10090:Nat8l ^@ http://purl.uniprot.org/uniprot/A0A0R4J0R4|||http://purl.uniprot.org/uniprot/Q3UGX3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||N-acetylaspartate synthetase|||N-acetyltransferase|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000305230 http://togogenome.org/gene/10090:Cfap100 ^@ http://purl.uniprot.org/uniprot/Q80VN0 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict ^@ Cilia- and flagella-associated protein 100|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000234489 http://togogenome.org/gene/10090:Hdac10 ^@ http://purl.uniprot.org/uniprot/Q6P3E7 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Region|||Sequence Conflict ^@ Histone deacetylase|||Polyamine deacetylase HDAC10 ^@ http://purl.uniprot.org/annotation/PRO_0000114713 http://togogenome.org/gene/10090:Armcx3 ^@ http://purl.uniprot.org/uniprot/Q8BHS6 ^@ 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_0000191368 http://togogenome.org/gene/10090:Synpo2 ^@ http://purl.uniprot.org/uniprot/E9Q1U2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PDZ|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Ptpn21 ^@ http://purl.uniprot.org/uniprot/G5E8J4|||http://purl.uniprot.org/uniprot/Q4KML9 ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||FERM|||Phosphocysteine intermediate|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://togogenome.org/gene/10090:Naa16 ^@ http://purl.uniprot.org/uniprot/Q9DBB4 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ Disordered|||N-alpha-acetyltransferase 16, NatA auxiliary subunit|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7 ^@ http://purl.uniprot.org/annotation/PRO_0000106298 http://togogenome.org/gene/10090:Aamp ^@ http://purl.uniprot.org/uniprot/J3QN89|||http://purl.uniprot.org/uniprot/Q3TJ22 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ Acidic residues|||Disordered|||WD ^@ http://togogenome.org/gene/10090:Hes1 ^@ http://purl.uniprot.org/uniprot/P35428|||http://purl.uniprot.org/uniprot/Q3UZZ2 ^@ 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|||Polar residues|||Pro residues|||Transcription factor HES-1|||WRPW motif|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127203 http://togogenome.org/gene/10090:Rasa1 ^@ http://purl.uniprot.org/uniprot/E9PYG6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2|||Disordered|||PH|||Ras-GAP|||SH2|||SH3 ^@ http://togogenome.org/gene/10090:Eif2ak3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Y1|||http://purl.uniprot.org/uniprot/E9QQ30|||http://purl.uniprot.org/uniprot/Q7TQC8|||http://purl.uniprot.org/uniprot/Q9Z2B5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||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|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Eukaryotic translation initiation factor 2-alpha kinase 3|||Helical|||Loss of activity and autophosphorylation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000024323|||http://purl.uniprot.org/annotation/PRO_5003246318|||http://purl.uniprot.org/annotation/PRO_5004291774|||http://purl.uniprot.org/annotation/PRO_5006452045 http://togogenome.org/gene/10090:Klhl38 ^@ http://purl.uniprot.org/uniprot/Q8BSF5 ^@ 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 38 ^@ http://purl.uniprot.org/annotation/PRO_0000325810 http://togogenome.org/gene/10090:Fcrl6 ^@ http://purl.uniprot.org/uniprot/A1YIY0 ^@ 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|||Fc receptor-like protein 6|||Helical|||Ig-like C2-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000280214|||http://purl.uniprot.org/annotation/VSP_053295|||http://purl.uniprot.org/annotation/VSP_053296 http://togogenome.org/gene/10090:Ntn4 ^@ http://purl.uniprot.org/uniprot/Q0VEM1|||http://purl.uniprot.org/uniprot/Q9JI33 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ 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_0000042117|||http://purl.uniprot.org/annotation/PRO_5014306871 http://togogenome.org/gene/10090:Rhcg ^@ http://purl.uniprot.org/uniprot/Q9QXP0 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Ammonium transporter Rh type C|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000283579 http://togogenome.org/gene/10090:Pbld2 ^@ http://purl.uniprot.org/uniprot/Q9CXN7 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Sequence Conflict ^@ Phenazine biosynthesis-like domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000162384 http://togogenome.org/gene/10090:Liat1 ^@ http://purl.uniprot.org/uniprot/Q810M6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ 1|||Acidic residues|||Basic and acidic residues|||Disordered|||Interaction with ATE1|||Lysine-rich domain|||Protein LIAT1 ^@ http://purl.uniprot.org/annotation/PRO_0000340234 http://togogenome.org/gene/10090:Khdc1b ^@ http://purl.uniprot.org/uniprot/P0C7A0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ KH|||KH homology domain-containing protein 1B ^@ http://purl.uniprot.org/annotation/PRO_0000328819 http://togogenome.org/gene/10090:Foxn1 ^@ http://purl.uniprot.org/uniprot/Q32MU3|||http://purl.uniprot.org/uniprot/Q5SYK1|||http://purl.uniprot.org/uniprot/Q61575 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Fork-head|||Forkhead box protein N1|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000091867 http://togogenome.org/gene/10090:Or10d1 ^@ http://purl.uniprot.org/uniprot/Q9EQ86 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Oasl1 ^@ http://purl.uniprot.org/uniprot/Q8VI94 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ 2'-5'-oligoadenylate synthase-like protein 1|||Ubiquitin-like 1|||Ubiquitin-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000418632 http://togogenome.org/gene/10090:Zbtb3 ^@ http://purl.uniprot.org/uniprot/Q91X45 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000047711 http://togogenome.org/gene/10090:Chtf18 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0I4|||http://purl.uniprot.org/uniprot/E9PVJ3|||http://purl.uniprot.org/uniprot/Q8BIW9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ AAA+ ATPase|||Chromosome transmission fidelity protein 18 homolog|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000340082 http://togogenome.org/gene/10090:Clca1 ^@ http://purl.uniprot.org/uniprot/Q9D7Z6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Calcium-activated chloride channel regulator 1|||Cleavage; by autolysis|||Metalloprotease domain|||N-linked (GlcNAc...) asparagine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000333692 http://togogenome.org/gene/10090:Prdm4 ^@ http://purl.uniprot.org/uniprot/A0A1X7SB67|||http://purl.uniprot.org/uniprot/Q80V63 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; degenerate|||Disordered|||PR domain zinc finger protein 4|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000230792 http://togogenome.org/gene/10090:BC005624 ^@ http://purl.uniprot.org/uniprot/Q3TQI7 ^@ 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|||Interaction with SNRNP200|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Splicing factor C9orf78 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000227524 http://togogenome.org/gene/10090:Cep57l1 ^@ http://purl.uniprot.org/uniprot/B2RR53|||http://purl.uniprot.org/uniprot/G5E828|||http://purl.uniprot.org/uniprot/Q8VDS7 ^@ 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|||Centrosomal protein CEP57L1|||Cep57 centrosome localisation|||Cep57 centrosome microtubule-binding|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000189535|||http://purl.uniprot.org/annotation/VSP_013897|||http://purl.uniprot.org/annotation/VSP_013898|||http://purl.uniprot.org/annotation/VSP_013899|||http://purl.uniprot.org/annotation/VSP_013900 http://togogenome.org/gene/10090:Prap1 ^@ http://purl.uniprot.org/uniprot/Q80XD8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Impairs its ability to form a complex with triglycerides and MTTP, as well as its ability to facilitate MTTP-mediated lipid transfer and MTTP-mediated apoB lipoprotein assembly and secretion.|||Proline-rich acidic protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000299417 http://togogenome.org/gene/10090:Slc10a4 ^@ http://purl.uniprot.org/uniprot/A2RTJ6|||http://purl.uniprot.org/uniprot/Q3UEZ8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cleavage; by thrombin|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sodium/bile acid cotransporter 4 ^@ http://purl.uniprot.org/annotation/PRO_0000263743 http://togogenome.org/gene/10090:Or7g25 ^@ http://purl.uniprot.org/uniprot/Q7TRG4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Csnk1e ^@ http://purl.uniprot.org/uniprot/Q3TYE1|||http://purl.uniprot.org/uniprot/Q9JMK2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Casein kinase I isoform epsilon|||Decreases PER1 phosphorylation.|||Disordered|||Increases PER1 nuclear import.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Shortens circadian rhythm. Accelerates PER2 degradation. ^@ http://purl.uniprot.org/annotation/PRO_0000192838 http://togogenome.org/gene/10090:Adora2a ^@ http://purl.uniprot.org/uniprot/Q60613|||http://purl.uniprot.org/uniprot/Q8CAU3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||Interaction with GAS2L2|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069000 http://togogenome.org/gene/10090:Ifitm7 ^@ http://purl.uniprot.org/uniprot/Q8BVR2 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Cul7 ^@ http://purl.uniprot.org/uniprot/A9C491|||http://purl.uniprot.org/uniprot/Q8VE73 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Cullin family profile|||Cullin-7|||DOC|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||In isoform 2.|||Interaction with TP53 ^@ http://purl.uniprot.org/annotation/PRO_0000119803|||http://purl.uniprot.org/annotation/VSP_038331 http://togogenome.org/gene/10090:Grk5 ^@ http://purl.uniprot.org/uniprot/Q3TST4|||http://purl.uniprot.org/uniprot/Q8VEB1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ AGC-kinase C-terminal|||Disordered|||G protein-coupled receptor kinase 5|||Interaction with calmodulin|||N-terminal|||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_0000085972 http://togogenome.org/gene/10090:Misp3 ^@ http://purl.uniprot.org/uniprot/A0A087WQ89|||http://purl.uniprot.org/uniprot/Q9CVC4 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ A-kinase anchor protein 2 C-terminal|||Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Cyp2c66 ^@ http://purl.uniprot.org/uniprot/Q5GLZ0 ^@ Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015097892 http://togogenome.org/gene/10090:Dtl ^@ http://purl.uniprot.org/uniprot/Q3TLR7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ DDB1-binding motif|||Denticleless protein homolog|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1 and CDK2|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000274868|||http://purl.uniprot.org/annotation/VSP_022884|||http://purl.uniprot.org/annotation/VSP_022885|||http://purl.uniprot.org/annotation/VSP_022886 http://togogenome.org/gene/10090:Pcdh1 ^@ http://purl.uniprot.org/uniprot/Q8CFX3 ^@ 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|||Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099089 http://togogenome.org/gene/10090:Opn5 ^@ http://purl.uniprot.org/uniprot/Q6VZZ7 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||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|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||Opsin-5|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000197818|||http://purl.uniprot.org/annotation/VSP_014041|||http://purl.uniprot.org/annotation/VSP_014042 http://togogenome.org/gene/10090:Lars2 ^@ http://purl.uniprot.org/uniprot/Q8VDC0 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Transit Peptide ^@ 'HIGH' region|||'KMSKS' region|||Mitochondrion|||N6-acetyllysine|||Probable leucine--tRNA ligase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000035807 http://togogenome.org/gene/10090:Or10g6 ^@ http://purl.uniprot.org/uniprot/Q8VEU2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vps29 ^@ http://purl.uniprot.org/uniprot/Q9QZ88 ^@ 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 interaction with VPS35.|||Disrupts interaction with ANKRD27.|||Disrupts interaction with VPS35.|||In isoform 2.|||N6-acetyllysine|||Vacuolar protein sorting-associated protein 29 ^@ http://purl.uniprot.org/annotation/PRO_0000065895|||http://purl.uniprot.org/annotation/VSP_004074 http://togogenome.org/gene/10090:Nmnat2 ^@ http://purl.uniprot.org/uniprot/Q5HZI3|||http://purl.uniprot.org/uniprot/Q8BNJ3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Mutagenesis Site ^@ Abolished palmitoylation and membrane association in neurons.|||Cytidyltransferase-like|||Impaired membrane association in neurons; when associated with A-151; A-155; A-162 and A-167.|||Impaired membrane association in neurons; when associated with A-151; A-155; A-162 and A-172.|||Impaired membrane association in neurons; when associated with A-151; A-155; A-167 and A-172.|||Impaired membrane association in neurons; when associated with A-151; A-162; A-167 and A-172.|||Impaired membrane association in neurons; when associated with A-155; A-162; A-167 and A-172.|||Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2|||S-palmitoyl cysteine|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000135015 http://togogenome.org/gene/10090:Cox7a2 ^@ http://purl.uniprot.org/uniprot/P48771 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||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_0000006146 http://togogenome.org/gene/10090:B4galnt1 ^@ http://purl.uniprot.org/uniprot/A0A1Z4EAV4|||http://purl.uniprot.org/uniprot/Q09200|||http://purl.uniprot.org/uniprot/Q3UN35 ^@ 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 ^@ Beta-1,4 N-acetylgalactosaminyltransferase 1|||Cytoplasmic|||Disordered|||Glycosyltransferase 2-like|||Helical|||Helical; Signal-anchor for type II membrane protein|||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_0000059101 http://togogenome.org/gene/10090:Glipr1l2 ^@ http://purl.uniprot.org/uniprot/Q9CQ35 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Transmembrane ^@ Acidic residues|||Disordered|||GLIPR1-like protein 2|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||SCP ^@ http://purl.uniprot.org/annotation/PRO_0000324388|||http://purl.uniprot.org/annotation/VSP_032247|||http://purl.uniprot.org/annotation/VSP_032248 http://togogenome.org/gene/10090:Tmem198 ^@ http://purl.uniprot.org/uniprot/Q8BG75 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Pro residues|||Transmembrane protein 198 ^@ http://purl.uniprot.org/annotation/PRO_0000326031 http://togogenome.org/gene/10090:Pabir1 ^@ http://purl.uniprot.org/uniprot/Q9DB52 ^@ 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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||P2R1A-PPP2R2A-interacting phosphatase regulator 1|||Phosphoserine|||Phosphoserine; by CHEK1|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089690 http://togogenome.org/gene/10090:Ifna2 ^@ http://purl.uniprot.org/uniprot/B1AYH7 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015087039 http://togogenome.org/gene/10090:Pum2 ^@ http://purl.uniprot.org/uniprot/Q3TQ29|||http://purl.uniprot.org/uniprot/Q3UR91|||http://purl.uniprot.org/uniprot/Q80U58 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Turn ^@ Adenine-nucleotide binding in RNA target|||Basic and acidic residues|||Disordered|||Guanine-nucleotide binding in RNA target|||In isoform 2 and isoform 3.|||In isoform 3.|||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_0000075920|||http://purl.uniprot.org/annotation/VSP_009321|||http://purl.uniprot.org/annotation/VSP_009322|||http://purl.uniprot.org/annotation/VSP_009323 http://togogenome.org/gene/10090:Lnx2 ^@ http://purl.uniprot.org/uniprot/Q91XL2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Abolishes binding to NUMB protein.|||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_0000055916 http://togogenome.org/gene/10090:Mks1 ^@ http://purl.uniprot.org/uniprot/Q5SW45 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ C2 B9-type|||Tectonic-like complex member MKS1 ^@ http://purl.uniprot.org/annotation/PRO_0000225687 http://togogenome.org/gene/10090:Cd37 ^@ http://purl.uniprot.org/uniprot/Q3U429|||http://purl.uniprot.org/uniprot/Q4FK35|||http://purl.uniprot.org/uniprot/Q61470 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Leukocyte antigen CD37|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219210 http://togogenome.org/gene/10090:Tnn ^@ http://purl.uniprot.org/uniprot/Q80Z71 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Fibrinogen C-terminal|||Fibronectin type-III 1|||Fibronectin type-III 10|||Fibronectin type-III 11|||Fibronectin type-III 12|||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 isoform 2.|||N-linked (GlcNAc...) asparagine|||Tenascin-N ^@ http://purl.uniprot.org/annotation/PRO_0000007746|||http://purl.uniprot.org/annotation/VSP_058850 http://togogenome.org/gene/10090:Scaf8 ^@ http://purl.uniprot.org/uniprot/Q6DID3 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||CID|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||SR-related and CTD-associated factor 8 ^@ http://purl.uniprot.org/annotation/PRO_0000394194 http://togogenome.org/gene/10090:Lamp5 ^@ http://purl.uniprot.org/uniprot/Q9D387 ^@ 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 ^@ Cell surface localization.|||Cytoplasmic|||Extracellular|||Helical|||Lysosome-associated membrane glycoprotein 5|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000021032 http://togogenome.org/gene/10090:Tcirg1 ^@ http://purl.uniprot.org/uniprot/Q9JHF5 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Rap1gap ^@ http://purl.uniprot.org/uniprot/A2ALS4|||http://purl.uniprot.org/uniprot/A2ALS5 ^@ 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|||GoLoco|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rap-GAP|||Rap1 GTPase-activating protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000424956|||http://purl.uniprot.org/annotation/VSP_053560|||http://purl.uniprot.org/annotation/VSP_053561|||http://purl.uniprot.org/annotation/VSP_053562 http://togogenome.org/gene/10090:Rwdd2a ^@ http://purl.uniprot.org/uniprot/Q14BN8|||http://purl.uniprot.org/uniprot/Q9D9S3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ RWD|||RWD domain-containing protein 2A ^@ http://purl.uniprot.org/annotation/PRO_0000097544 http://togogenome.org/gene/10090:Trpm8 ^@ http://purl.uniprot.org/uniprot/Q8R4D5 ^@ Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes glycosylation. Shifts threshold of temperature activation from 26.5 to 24 degrees Celsius. Reduced cell surface expression, association with lipid rafts and response to cold.|||Abolishes ion channel activity. No effect on cell surface expression. Reduced glycosylation.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||N-linked (GlcNAc...) (complex) asparagine|||No effect on glycosylation or ability to form functional channels.|||Reduced ion channel sensitivity to cold stimuli or menthol plus cold stimuli.|||Slighty reduced ion channel sensitivity to cold stimuli. No significant effect on ion channel sensitivity to menthol plus cold stimuli.|||Transient receptor potential cation channel subfamily M member 8 ^@ http://purl.uniprot.org/annotation/PRO_0000215334 http://togogenome.org/gene/10090:Zfp599 ^@ http://purl.uniprot.org/uniprot/E9PWP1|||http://purl.uniprot.org/uniprot/Q810J2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Depdc1b ^@ http://purl.uniprot.org/uniprot/Q8BH88 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ DEP|||DEP domain-containing protein 1B|||Phosphoserine|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000284792 http://togogenome.org/gene/10090:Rab32 ^@ http://purl.uniprot.org/uniprot/Q9CZE3 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disrupts interaction with ANKRD27.|||Effector region|||Inhibits the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes.|||N-acetylalanine|||PKA-RII subunit binding domain|||Phosphoserine|||Ras-related protein Rab-32|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121236 http://togogenome.org/gene/10090:Cdc42ep5 ^@ http://purl.uniprot.org/uniprot/Q9Z0X0 ^@ 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 ^@ Basic and acidic residues|||CRIB|||Cdc42 effector protein 5|||Disordered|||No binding with CDC42.|||Omega-N-methylarginine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000212654 http://togogenome.org/gene/10090:Exoc6b ^@ http://purl.uniprot.org/uniprot/A6H5Z3 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Splice Variant ^@ Disordered|||Exocyst complex component 6B|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000406778|||http://purl.uniprot.org/annotation/VSP_040840|||http://purl.uniprot.org/annotation/VSP_040841 http://togogenome.org/gene/10090:Gm20814 ^@ http://purl.uniprot.org/uniprot/A0A087WRK1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Fscn3 ^@ http://purl.uniprot.org/uniprot/Q9QXW4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Fascin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000219384 http://togogenome.org/gene/10090:S1pr1 ^@ http://purl.uniprot.org/uniprot/O08530 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||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-acetylvaline|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||S-palmitoyl cysteine|||Sphingosine 1-phosphate receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000069413 http://togogenome.org/gene/10090:Lrp5 ^@ http://purl.uniprot.org/uniprot/Q91VN0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Extracellular|||Helical|||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 5|||N-linked (GlcNAc...) asparagine|||PPPSP motif A|||PPPSP motif B|||PPPSP motif C|||PPPSP motif D|||PPPSP motif E|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000017329 http://togogenome.org/gene/10090:Ogfrl1 ^@ http://purl.uniprot.org/uniprot/Q8VE52 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Opioid growth factor receptor-like protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314143 http://togogenome.org/gene/10090:Itga5 ^@ http://purl.uniprot.org/uniprot/P11688|||http://purl.uniprot.org/uniprot/Q80YP5 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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_0000016252|||http://purl.uniprot.org/annotation/PRO_0000016253|||http://purl.uniprot.org/annotation/PRO_0000016254 http://togogenome.org/gene/10090:Etnppl ^@ http://purl.uniprot.org/uniprot/Q8BWU8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Ethanolamine-phosphate phospho-lyase|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_0000287664 http://togogenome.org/gene/10090:Ccar2 ^@ http://purl.uniprot.org/uniprot/Q8VDP4 ^@ 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|||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|||Interaction with MCC|||Interaction with NR1D1|||N6-acetyllysine; by KAT8|||N6-methyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000050814 http://togogenome.org/gene/10090:Pi4ka ^@ http://purl.uniprot.org/uniprot/A0A140T8I9|||http://purl.uniprot.org/uniprot/E9Q3L2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Activation loop|||Catalytic loop|||Disordered|||G-loop|||PI3K/PI4K catalytic|||PIK helical|||Phosphatidylinositol 4-kinase alpha|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000435632 http://togogenome.org/gene/10090:Map3k1 ^@ http://purl.uniprot.org/uniprot/F8VQ72 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Protein kinase|||RING-type|||SWIM-type ^@ http://togogenome.org/gene/10090:Tma16 ^@ http://purl.uniprot.org/uniprot/Q9CR02 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Translation machinery-associated protein 16 ^@ http://purl.uniprot.org/annotation/PRO_0000321560|||http://purl.uniprot.org/annotation/VSP_031803 http://togogenome.org/gene/10090:Lrrc4c ^@ http://purl.uniprot.org/uniprot/Q8C031 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||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|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 4C|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000015109 http://togogenome.org/gene/10090:Gdpd3 ^@ http://purl.uniprot.org/uniprot/Q99LY2 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||GP-PDE|||Helical|||Lysophospholipase D GDPD3 ^@ http://purl.uniprot.org/annotation/PRO_0000251937 http://togogenome.org/gene/10090:Etfa ^@ http://purl.uniprot.org/uniprot/Q99LC5 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Domain I|||Domain II|||Electron transfer flavoprotein subunit alpha, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000008652 http://togogenome.org/gene/10090:Vps26c ^@ http://purl.uniprot.org/uniprot/O35075 ^@ Chain|||Molecule Processing ^@ Chain ^@ Vacuolar protein sorting-associated protein 26C ^@ http://purl.uniprot.org/annotation/PRO_0000073017 http://togogenome.org/gene/10090:Cyp7b1 ^@ http://purl.uniprot.org/uniprot/Q3USU4|||http://purl.uniprot.org/uniprot/Q60991 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Cytochrome P450 7B1|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051907 http://togogenome.org/gene/10090:Or4a69 ^@ http://purl.uniprot.org/uniprot/Q8VF91 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Amy2a3 ^@ http://purl.uniprot.org/uniprot/P00688 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ In A1 and B(C).|||In A1, B(A) and B(C).|||In A1, B(A) and B(C); requires 2 nucleotide substitutions.|||In A1, B(C) and AMY-2.2Y.|||In AMY-2.2Y.|||In B(A).|||In B(C).|||In B1.|||Nucleophile|||Pancreatic alpha-amylase 2a5|||Proton donor|||Pyrrolidone carboxylic acid|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000001398 http://togogenome.org/gene/10090:Esyt1 ^@ http://purl.uniprot.org/uniprot/Q3U7R1 ^@ 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|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolished phosphorylation by CDK5.|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||Cytoplasmic|||Disordered|||Extended synaptotagmin-1|||Helical|||In isoform 2.|||Lumenal|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphotyrosine|||Polar residues|||Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane|||SMP-LTD ^@ http://purl.uniprot.org/annotation/PRO_0000234345|||http://purl.uniprot.org/annotation/VSP_018278|||http://purl.uniprot.org/annotation/VSP_018279 http://togogenome.org/gene/10090:Lsm10 ^@ http://purl.uniprot.org/uniprot/Q3UPL7|||http://purl.uniprot.org/uniprot/Q8QZX5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Sm|||U7 snRNA-associated Sm-like protein LSm10 ^@ http://purl.uniprot.org/annotation/PRO_0000125586 http://togogenome.org/gene/10090:Scarb2 ^@ http://purl.uniprot.org/uniprot/O35114 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Abolishes interaction with GBA1. No effect on normal location in lysosomes.|||Cytoplasmic|||Helical|||Important for interaction with GBA1|||Loss of glycosylation site. Causes retention in the endoplasmic reticulum and abolishes normal location in lysosomes.|||Loss of glycosylation site. No effect on normal location in lysosomes.|||Lumenal|||Lysosome membrane protein 2|||N-linked (GlcNAc...) asparagine|||Slightly increased GBA1 binding. No effect on normal location in lysosomes. ^@ http://purl.uniprot.org/annotation/PRO_0000144156 http://togogenome.org/gene/10090:Sulf2 ^@ http://purl.uniprot.org/uniprot/Q8CFG0 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ 3-oxoalanine (Cys)|||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|||N-linked (GlcNAc...) asparagine|||Nucleophile|||O-linked (Xyl...) (chondroitin sulfate) serine|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000033441|||http://purl.uniprot.org/annotation/PRO_0000457760 http://togogenome.org/gene/10090:Tafa1 ^@ http://purl.uniprot.org/uniprot/Q7TPG8 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Chemokine-like protein TAFA-1 ^@ http://purl.uniprot.org/annotation/PRO_0000042722 http://togogenome.org/gene/10090:Mtfr1 ^@ http://purl.uniprot.org/uniprot/Q3TTQ5|||http://purl.uniprot.org/uniprot/Q99MB2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Transit Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Signal Peptide|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||Mitochondrial fission regulator|||Mitochondrial fission regulator 1|||Mitochondrion|||Necessary and sufficient to promote mitochondrial fission|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000096623|||http://purl.uniprot.org/annotation/PRO_5014309113 http://togogenome.org/gene/10090:Grid2ip ^@ http://purl.uniprot.org/uniprot/Q0QWG9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Delphilin|||Disordered|||FH2|||In isoform 2.|||In isoform 3.|||PDZ 1|||PDZ 2|||Phosphoserine|||Polar residues|||Pro residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000331625|||http://purl.uniprot.org/annotation/VSP_033275|||http://purl.uniprot.org/annotation/VSP_033276|||http://purl.uniprot.org/annotation/VSP_033277|||http://purl.uniprot.org/annotation/VSP_033278 http://togogenome.org/gene/10090:Shisa3 ^@ http://purl.uniprot.org/uniprot/Q3UPR0 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Protein shisa-3 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000330026 http://togogenome.org/gene/10090:Vmn1r230 ^@ http://purl.uniprot.org/uniprot/Q8R2A2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Il2rb ^@ http://purl.uniprot.org/uniprot/P16297 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Interleukin-2 receptor subunit beta|||N-linked (GlcNAc...) asparagine|||Polar residues|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010879 http://togogenome.org/gene/10090:Ube2g1 ^@ http://purl.uniprot.org/uniprot/P62254|||http://purl.uniprot.org/uniprot/Q5F239 ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ 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_0000082481|||http://purl.uniprot.org/annotation/PRO_0000424516 http://togogenome.org/gene/10090:Ighmbp2 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1E3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ AN1-type|||Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||R3H ^@ http://togogenome.org/gene/10090:Samt3 ^@ http://purl.uniprot.org/uniprot/A2ARK7|||http://purl.uniprot.org/uniprot/Q9D9H1 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Zcchc8 ^@ http://purl.uniprot.org/uniprot/Q9CYA6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ CCHC-type|||Disordered|||MTREX binding|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RBM7 binding|||Removed|||Zinc finger CCHC domain-containing protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000150961 http://togogenome.org/gene/10090:Rps23rg1 ^@ http://purl.uniprot.org/uniprot/Q8C7T0 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Ntmt2 ^@ http://purl.uniprot.org/uniprot/B2RXM4 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ N-terminal Xaa-Pro-Lys N-methyltransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000399779 http://togogenome.org/gene/10090:Dna2 ^@ http://purl.uniprot.org/uniprot/Q6ZQJ5 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ DNA replication ATP-dependent helicase/nuclease DNA2|||Helicase activity|||In isoform 2.|||Nuclease activity ^@ http://purl.uniprot.org/annotation/PRO_0000263604|||http://purl.uniprot.org/annotation/VSP_021872|||http://purl.uniprot.org/annotation/VSP_021873 http://togogenome.org/gene/10090:Fam43a ^@ http://purl.uniprot.org/uniprot/Q8BUP8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Acidic residues|||Disordered|||Polar residues|||Protein FAM43A ^@ http://purl.uniprot.org/annotation/PRO_0000187025 http://togogenome.org/gene/10090:Fbxo10 ^@ http://purl.uniprot.org/uniprot/Q7TQF2 ^@ 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 ^@ Disordered|||F-box|||F-box only protein 10|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000307718 http://togogenome.org/gene/10090:Or7e168 ^@ http://purl.uniprot.org/uniprot/Q7TRF5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nudt21 ^@ http://purl.uniprot.org/uniprot/Q9CQF3 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ 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|||Nudix box|||Nudix hydrolase|||Omega-N-methylarginine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057151 http://togogenome.org/gene/10090:Vps37a ^@ http://purl.uniprot.org/uniprot/Q3UV99|||http://purl.uniprot.org/uniprot/Q8CHS8 ^@ 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.|||Phosphoserine|||VPS37 C-terminal|||Vacuolar protein sorting-associated protein 37A ^@ http://purl.uniprot.org/annotation/PRO_0000287199|||http://purl.uniprot.org/annotation/VSP_025370|||http://purl.uniprot.org/annotation/VSP_025371|||http://purl.uniprot.org/annotation/VSP_025372 http://togogenome.org/gene/10090:9430038I01Rik ^@ http://purl.uniprot.org/uniprot/Q9CX25 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Uncharacterized protein C10orf143 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000442934 http://togogenome.org/gene/10090:Ift46 ^@ http://purl.uniprot.org/uniprot/Q9DB07 ^@ 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|||Intraflagellar transport protein 46 homolog|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000085517 http://togogenome.org/gene/10090:Nsmaf ^@ http://purl.uniprot.org/uniprot/O35242 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ BEACH|||BEACH-type PH|||GRAM|||Protein FAN|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000050976 http://togogenome.org/gene/10090:Car7 ^@ http://purl.uniprot.org/uniprot/G3XA26|||http://purl.uniprot.org/uniprot/Q3UND9|||http://purl.uniprot.org/uniprot/Q9ERQ8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase 7|||Disordered|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000077432 http://togogenome.org/gene/10090:Pex3 ^@ http://purl.uniprot.org/uniprot/Q9QXY9 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Interaction with PEX19|||Peroxisomal|||Peroxisomal biogenesis factor 3|||Targeting to peroxisomes ^@ http://purl.uniprot.org/annotation/PRO_0000208739 http://togogenome.org/gene/10090:Lmnb2 ^@ http://purl.uniprot.org/uniprot/P21619|||http://purl.uniprot.org/uniprot/Q3V159 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||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 isoform B3.|||LTD|||Lamin-B2|||Linker 1|||Linker 2|||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_0000063821|||http://purl.uniprot.org/annotation/PRO_0000403471|||http://purl.uniprot.org/annotation/VSP_017070 http://togogenome.org/gene/10090:Or2aa1 ^@ http://purl.uniprot.org/uniprot/Q8VF69 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Stc2 ^@ http://purl.uniprot.org/uniprot/O88452|||http://purl.uniprot.org/uniprot/Q5SS12 ^@ 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|||Polar residues|||Stanniocalcin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000033305|||http://purl.uniprot.org/annotation/PRO_5014309954 http://togogenome.org/gene/10090:Atp5g3 ^@ http://purl.uniprot.org/uniprot/P56384|||http://purl.uniprot.org/uniprot/Q14BC2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Site|||Transit Peptide|||Transmembrane ^@ ATP synthase F(0) complex subunit C3, mitochondrial|||Helical|||Mitochondrion|||N6,N6,N6-trimethyllysine|||Reversibly protonated during proton transport|||V-ATPase proteolipid subunit C-like ^@ http://purl.uniprot.org/annotation/PRO_0000002568 http://togogenome.org/gene/10090:Tbx10 ^@ http://purl.uniprot.org/uniprot/Q810F8 ^@ 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.|||T-box|||T-box transcription factor TBX10 ^@ http://purl.uniprot.org/annotation/PRO_0000184442|||http://purl.uniprot.org/annotation/VSP_011305 http://togogenome.org/gene/10090:Prss55 ^@ http://purl.uniprot.org/uniprot/Q14BX2 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Disordered|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Removed in mature form|||Serine protease 55 ^@ http://purl.uniprot.org/annotation/PRO_0000328816|||http://purl.uniprot.org/annotation/PRO_0000449399 http://togogenome.org/gene/10090:Uvrag ^@ http://purl.uniprot.org/uniprot/Q8K245 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict ^@ C2|||Disordered|||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 protein ^@ http://purl.uniprot.org/annotation/PRO_0000433403 http://togogenome.org/gene/10090:Txlna ^@ http://purl.uniprot.org/uniprot/Q3UD58|||http://purl.uniprot.org/uniprot/Q6PAM1 ^@ 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 ^@ Alpha-taxilin|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000189422|||http://purl.uniprot.org/annotation/VSP_011833|||http://purl.uniprot.org/annotation/VSP_011834 http://togogenome.org/gene/10090:Mre11a ^@ http://purl.uniprot.org/uniprot/Q3TU24|||http://purl.uniprot.org/uniprot/Q3URU4|||http://purl.uniprot.org/uniprot/Q61216|||http://purl.uniprot.org/uniprot/Q8BRV3 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Double-strand break repair protein MRE11|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Mre11 DNA-binding|||N-acetylserine|||Phosphoserine|||Polar residues|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000138674|||http://purl.uniprot.org/annotation/VSP_003263 http://togogenome.org/gene/10090:Adra2c ^@ http://purl.uniprot.org/uniprot/Q01337 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Alpha-2C adrenergic receptor|||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|||Implicated in catechol agonist binding and receptor activation|||Implicated in ligand binding|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069106 http://togogenome.org/gene/10090:Tbrg1 ^@ http://purl.uniprot.org/uniprot/Q3UB74 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||FYR C-terminal|||FYR N-terminal|||N-acetylserine|||Phosphothreonine|||Removed|||Transforming growth factor beta regulator 1 ^@ http://purl.uniprot.org/annotation/PRO_0000274219 http://togogenome.org/gene/10090:Mageb3 ^@ http://purl.uniprot.org/uniprot/Q9D2H4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic residues|||Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Lelp1 ^@ http://purl.uniprot.org/uniprot/Q9DAE3 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Late cornified envelope-like proline-rich protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000271605 http://togogenome.org/gene/10090:Gpn2 ^@ http://purl.uniprot.org/uniprot/Q8VEJ1 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||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_0000247831 http://togogenome.org/gene/10090:Ica1l ^@ http://purl.uniprot.org/uniprot/Q3TY65 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ AH|||Disordered|||Islet cell autoantigen 1-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000076176 http://togogenome.org/gene/10090:Smn1 ^@ http://purl.uniprot.org/uniprot/P97801|||http://purl.uniprot.org/uniprot/Q549F9 ^@ 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 ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Loss of interaction with SYNCRIP.|||P1 (binding site for GEMIN2)|||P2 (binding site for SNRPB)|||Phosphoserine|||Phosphothreonine|||Pro residues|||Required for interaction with RPP20/POP7|||Required for interaction with SYNCRIP|||Survival motor neuron protein|||Tudor ^@ http://purl.uniprot.org/annotation/PRO_0000218904 http://togogenome.org/gene/10090:Plekhd1 ^@ http://purl.uniprot.org/uniprot/B2RPU2 ^@ 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 ^@ Disordered|||Omega-N-methylarginine|||PH|||Pleckstrin homology domain-containing family D member 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000415810 http://togogenome.org/gene/10090:Phf12 ^@ http://purl.uniprot.org/uniprot/Q3U2C9|||http://purl.uniprot.org/uniprot/Q5SPL2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||FHA|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||PHD finger protein 12|||PHD-type|||PHD-type 1|||PHD-type 2; atypical|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000059303|||http://purl.uniprot.org/annotation/VSP_051773|||http://purl.uniprot.org/annotation/VSP_051774 http://togogenome.org/gene/10090:Scgb2b3 ^@ http://purl.uniprot.org/uniprot/D2XZ38 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Signal Peptide ^@ Chain|||Non-terminal Residue|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015088470 http://togogenome.org/gene/10090:Or51l4 ^@ http://purl.uniprot.org/uniprot/Q9EQQ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp354a ^@ http://purl.uniprot.org/uniprot/B1ATG3|||http://purl.uniprot.org/uniprot/Q5PPR4|||http://purl.uniprot.org/uniprot/Q61751 ^@ 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|||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 354A ^@ http://purl.uniprot.org/annotation/PRO_0000047239 http://togogenome.org/gene/10090:Spats1 ^@ http://purl.uniprot.org/uniprot/A2RRY8 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Spermatogenesis-associated serine-rich protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000307695|||http://purl.uniprot.org/annotation/VSP_028788|||http://purl.uniprot.org/annotation/VSP_028789 http://togogenome.org/gene/10090:Plekhf1 ^@ http://purl.uniprot.org/uniprot/Q3TB82 ^@ 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_0000251598 http://togogenome.org/gene/10090:Atp8b3 ^@ http://purl.uniprot.org/uniprot/Q6UQ17 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cytoplasmic|||Disordered|||Exoplasmic loop|||Helical|||Phospholipid-transporting ATPase IK|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000429839 http://togogenome.org/gene/10090:Adam28 ^@ http://purl.uniprot.org/uniprot/Q9JLN6 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes prodomain removal.|||Basic and acidic residues|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 28|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Pro residues|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029132|||http://purl.uniprot.org/annotation/PRO_0000029133|||http://purl.uniprot.org/annotation/VSP_005488|||http://purl.uniprot.org/annotation/VSP_005489|||http://purl.uniprot.org/annotation/VSP_005490 http://togogenome.org/gene/10090:Eps15 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0A0|||http://purl.uniprot.org/uniprot/H3BK65|||http://purl.uniprot.org/uniprot/P42567|||http://purl.uniprot.org/uniprot/Q80ZL3 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Strand|||Turn ^@ 1|||10|||11|||12|||13|||13 X 3 AA repeats of D-P-F|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EH|||EH 1|||EH 2|||EH 3|||Epidermal growth factor receptor substrate 15|||In isoform 2.|||Inefficient EGFR internalization.|||Interaction with DAB2|||Loss of interaction with UBQLN1; when associated with A-863 and A-864.|||Loss of interaction with UBQLN1; when associated with A-863 and A-865.|||Loss of interaction with UBQLN1; when associated with A-864 and A-865.|||Loss of ubiquitination and interaction with UBQLN1; when associated with A-883.|||Loss of ubiquitination and interaction with UBQLN1; when associated with A-885.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by EGFR|||Polar residues|||Pro residues|||Removed|||UIM 1|||UIM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000146117|||http://purl.uniprot.org/annotation/VSP_036170|||http://purl.uniprot.org/annotation/VSP_036171 http://togogenome.org/gene/10090:Gigyf1 ^@ http://purl.uniprot.org/uniprot/Q99MR1 ^@ 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 ^@ Abolishes binding to GRB10.|||Acidic residues|||Basic and acidic residues|||Decreases binding to GRB10.|||Disordered|||GRB10-interacting GYF protein 1|||GYF|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000058315 http://togogenome.org/gene/10090:Rapgef6 ^@ http://purl.uniprot.org/uniprot/B2RUJ6|||http://purl.uniprot.org/uniprot/Q3TKC6|||http://purl.uniprot.org/uniprot/Q3TPI6|||http://purl.uniprot.org/uniprot/Q3UPQ2|||http://purl.uniprot.org/uniprot/Q5DTR1|||http://purl.uniprot.org/uniprot/Q5NCJ0|||http://purl.uniprot.org/uniprot/Q5NCJ1|||http://purl.uniprot.org/uniprot/Q8BLC8 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Cyclic nucleotide-binding|||Disordered|||N-terminal Ras-GEF|||PDZ|||Polar residues|||Ras-GEF|||Ras-associating ^@ http://togogenome.org/gene/10090:N4bp2l2 ^@ http://purl.uniprot.org/uniprot/Q8BYP6|||http://purl.uniprot.org/uniprot/Q8JZS6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||NEDD4-binding protein 2-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000299027|||http://purl.uniprot.org/annotation/VSP_027519|||http://purl.uniprot.org/annotation/VSP_027520 http://togogenome.org/gene/10090:Tymp ^@ http://purl.uniprot.org/uniprot/Q99N42 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region ^@ Disordered|||Phosphothreonine|||Thymidine phosphorylase ^@ http://purl.uniprot.org/annotation/PRO_0000059047 http://togogenome.org/gene/10090:Pld6 ^@ http://purl.uniprot.org/uniprot/Q5SWZ9 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger ^@ Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger ^@ C3H1-type; atypical|||Cytoplasmic|||Helical|||In isoform 2.|||Loss of nuclease activity.|||Mitochondrial cardiolipin hydrolase|||Mitochondrial intermembrane|||PLD phosphodiesterase|||Required for mitochondrial localization ^@ http://purl.uniprot.org/annotation/PRO_0000325911|||http://purl.uniprot.org/annotation/VSP_032474|||http://purl.uniprot.org/annotation/VSP_032475 http://togogenome.org/gene/10090:Sostdc1 ^@ http://purl.uniprot.org/uniprot/Q9CQN4 ^@ 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 ^@ Basic residues|||CTCK|||Disordered|||N-linked (GlcNAc...) asparagine|||Sclerostin domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000033181 http://togogenome.org/gene/10090:ND6 ^@ http://purl.uniprot.org/uniprot/P03925|||http://purl.uniprot.org/uniprot/Q7JCY4 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Chain|||Helix|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Helical|||NADH-ubiquinone oxidoreductase chain 6 ^@ http://purl.uniprot.org/annotation/PRO_0000118304|||http://purl.uniprot.org/annotation/PRO_5010845655 http://togogenome.org/gene/10090:Or51g1 ^@ http://purl.uniprot.org/uniprot/Q8VH17 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ubl7 ^@ http://purl.uniprot.org/uniprot/Q91W67 ^@ 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 ^@ Disordered|||Phosphoserine|||Polar residues|||UBA|||Ubiquitin-like|||Ubiquitin-like protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000211022 http://togogenome.org/gene/10090:Cers3 ^@ http://purl.uniprot.org/uniprot/Q1A3B0 ^@ 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 ^@ Acidic residues|||Ceramide synthase 3|||Cytoplasmic|||Disordered|||Helical|||Homeobox-like|||In isoform 2.|||Phosphoserine|||TLC ^@ http://purl.uniprot.org/annotation/PRO_0000423433|||http://purl.uniprot.org/annotation/VSP_047870 http://togogenome.org/gene/10090:Or2y12 ^@ http://purl.uniprot.org/uniprot/Q7TQT3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cxcr3 ^@ http://purl.uniprot.org/uniprot/O88410 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-X-C chemokine receptor type 3|||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|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000069347 http://togogenome.org/gene/10090:Lratd2 ^@ http://purl.uniprot.org/uniprot/D3YXJ5 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||LRAT ^@ http://togogenome.org/gene/10090:Bivm ^@ http://purl.uniprot.org/uniprot/Q8CBX9 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Basic immunoglobulin-like variable motif-containing protein|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000328956 http://togogenome.org/gene/10090:Tap2 ^@ http://purl.uniprot.org/uniprot/P36371|||http://purl.uniprot.org/uniprot/Q792S7 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||ABC-type antigen peptide transporter|||Antigen peptide transporter 2|||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|||Inter-subunit salt bridge with TAPBP|||Lumenal|||Part of the peptide-binding site ^@ http://purl.uniprot.org/annotation/PRO_0000093330|||http://purl.uniprot.org/annotation/PRO_5010143262 http://togogenome.org/gene/10090:Usp54 ^@ http://purl.uniprot.org/uniprot/Q8BL06 ^@ 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 and isoform 3.|||In isoform 2.|||Inactive ubiquitin carboxyl-terminal hydrolase 54|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||USP ^@ http://purl.uniprot.org/annotation/PRO_0000249531|||http://purl.uniprot.org/annotation/VSP_020488|||http://purl.uniprot.org/annotation/VSP_035679|||http://purl.uniprot.org/annotation/VSP_035680 http://togogenome.org/gene/10090:Cisd3 ^@ http://purl.uniprot.org/uniprot/B1AR13 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Transit Peptide ^@ CDGSH iron-sulfur domain-containing protein 3, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000341406 http://togogenome.org/gene/10090:Car8 ^@ http://purl.uniprot.org/uniprot/P28651 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Acidic residues|||Alpha-carbonic anhydrase|||Ancestral zinc ligand|||Carbonic anhydrase-related protein|||Disordered|||Phosphoserine|||Proton donor/acceptor|||Restores zinc-binding and activity. ^@ http://purl.uniprot.org/annotation/PRO_0000077434 http://togogenome.org/gene/10090:4933436I01Rik ^@ http://purl.uniprot.org/uniprot/Q9D3T1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic residues|||Disordered ^@ http://togogenome.org/gene/10090:Yju2b ^@ http://purl.uniprot.org/uniprot/Q9D516 ^@ 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 ^@ Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Probable splicing factor YJU2B ^@ http://purl.uniprot.org/annotation/PRO_0000280046|||http://purl.uniprot.org/annotation/VSP_023900|||http://purl.uniprot.org/annotation/VSP_023901 http://togogenome.org/gene/10090:Kcnmb4 ^@ http://purl.uniprot.org/uniprot/Q9JIN6 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Calcium-activated potassium channel subunit beta-4|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000187056 http://togogenome.org/gene/10090:Wdr11 ^@ http://purl.uniprot.org/uniprot/Q8K1X1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ 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_0000309846 http://togogenome.org/gene/10090:Mrpl44 ^@ http://purl.uniprot.org/uniprot/Q9CY73 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ DRBM|||Disordered|||In isoform 2.|||Large ribosomal subunit protein mL44|||Mitochondrion|||RNase III ^@ http://purl.uniprot.org/annotation/PRO_0000030822|||http://purl.uniprot.org/annotation/VSP_014126|||http://purl.uniprot.org/annotation/VSP_014127 http://togogenome.org/gene/10090:Anapc5 ^@ http://purl.uniprot.org/uniprot/A0A0G2JDE8|||http://purl.uniprot.org/uniprot/A0A0G2JDM7|||http://purl.uniprot.org/uniprot/A0A0G2JE03|||http://purl.uniprot.org/uniprot/Q3TWF7|||http://purl.uniprot.org/uniprot/Q3U5Y4|||http://purl.uniprot.org/uniprot/Q3U981|||http://purl.uniprot.org/uniprot/Q3UFC2|||http://purl.uniprot.org/uniprot/Q8BTZ4 ^@ 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 ^@ Anaphase-promoting complex subunit 5|||In isoform 2.|||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_0000064598|||http://purl.uniprot.org/annotation/VSP_008472 http://togogenome.org/gene/10090:Sptbn4 ^@ http://purl.uniprot.org/uniprot/E9PX29|||http://purl.uniprot.org/uniprot/E9PZC2|||http://purl.uniprot.org/uniprot/Q8VIE5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||PH|||Pro residues ^@ http://togogenome.org/gene/10090:Ppp6r2 ^@ http://purl.uniprot.org/uniprot/A0A5F8MQ25|||http://purl.uniprot.org/uniprot/G3X9K4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Sc5d ^@ http://purl.uniprot.org/uniprot/O88822 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Fatty acid hydroxylase|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Lathosterol oxidase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000117029 http://togogenome.org/gene/10090:Maml1 ^@ http://purl.uniprot.org/uniprot/Q6T264 ^@ 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|||Mastermind-like protein 1|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Required for interaction with NOTCH proteins ^@ http://purl.uniprot.org/annotation/PRO_0000129494 http://togogenome.org/gene/10090:Gpr68 ^@ http://purl.uniprot.org/uniprot/Q8BFQ3 ^@ 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|||Ovarian cancer G-protein coupled receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000070114 http://togogenome.org/gene/10090:Or6c69b ^@ http://purl.uniprot.org/uniprot/Q8VFH9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dnajc19 ^@ http://purl.uniprot.org/uniprot/D3Z5K6|||http://purl.uniprot.org/uniprot/Q9CQV7 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Helical|||In isoform 2.|||In isoform 3.|||Inhibits cell growth. No effect on interaction with PHB2.|||J|||Mitochondrial import inner membrane translocase subunit TIM14|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000071101|||http://purl.uniprot.org/annotation/VSP_016390|||http://purl.uniprot.org/annotation/VSP_016391 http://togogenome.org/gene/10090:Stk35 ^@ http://purl.uniprot.org/uniprot/E9PXA2|||http://purl.uniprot.org/uniprot/Q80ZW0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 35 ^@ http://purl.uniprot.org/annotation/PRO_0000277618 http://togogenome.org/gene/10090:Bmal2 ^@ http://purl.uniprot.org/uniprot/E9Q993|||http://purl.uniprot.org/uniprot/E9Q994|||http://purl.uniprot.org/uniprot/Q1A3C9|||http://purl.uniprot.org/uniprot/Q1A532|||http://purl.uniprot.org/uniprot/Q2VPD4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ BHLH|||Basic and acidic residues|||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.|||Interaction with PER2|||Nuclear export signal 1|||Nuclear export signal 2|||Nuclear localization signal|||PAC|||PAS|||PAS 1|||PAS 2|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000273632|||http://purl.uniprot.org/annotation/VSP_022586|||http://purl.uniprot.org/annotation/VSP_022587 http://togogenome.org/gene/10090:Tktl2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J2A3|||http://purl.uniprot.org/uniprot/Q9D4D4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Site ^@ Important for catalytic activity|||Proton donor|||Transketolase-like protein 2|||Transketolase-like pyrimidine-binding ^@ http://purl.uniprot.org/annotation/PRO_0000285201 http://togogenome.org/gene/10090:Insyn2b ^@ http://purl.uniprot.org/uniprot/Q6GQV1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||INSYN2B protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000349184 http://togogenome.org/gene/10090:Fam234b ^@ http://purl.uniprot.org/uniprot/Q8BYI8 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Protein FAM234B ^@ http://purl.uniprot.org/annotation/PRO_0000288914|||http://purl.uniprot.org/annotation/VSP_025825 http://togogenome.org/gene/10090:Rhox3e ^@ http://purl.uniprot.org/uniprot/Q4TU90 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Nipa2 ^@ http://purl.uniprot.org/uniprot/Q9JJC8 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Magnesium transporter NIPA2 ^@ http://purl.uniprot.org/annotation/PRO_0000191744 http://togogenome.org/gene/10090:Vmn2r66 ^@ http://purl.uniprot.org/uniprot/K7N6R9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908930 http://togogenome.org/gene/10090:Pcdhga9 ^@ http://purl.uniprot.org/uniprot/Q91XX9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (Man...) serine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099537 http://togogenome.org/gene/10090:Aadacl4fm1 ^@ http://purl.uniprot.org/uniprot/Q8BM81 ^@ 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 family member 1|||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_0000265938 http://togogenome.org/gene/10090:Pdpr ^@ http://purl.uniprot.org/uniprot/Q7TSQ8 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000328741 http://togogenome.org/gene/10090:Ndst2 ^@ http://purl.uniprot.org/uniprot/P52850 ^@ 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 ^@ Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2|||Cytoplasmic|||Disordered|||For sulfotransferase activity|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate N-deacetylase 2|||Heparan sulfate N-sulfotransferase 2|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000085213 http://togogenome.org/gene/10090:Baz2a ^@ http://purl.uniprot.org/uniprot/E9Q374|||http://purl.uniprot.org/uniprot/F8VPM0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Bromo|||DDT|||Disordered|||MBD|||PHD-type|||Polar residues ^@ http://togogenome.org/gene/10090:Clip4 ^@ http://purl.uniprot.org/uniprot/A0A2R8VJW4|||http://purl.uniprot.org/uniprot/Q3TTL7|||http://purl.uniprot.org/uniprot/Q8CI96 ^@ 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 ^@ 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.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000083530|||http://purl.uniprot.org/annotation/VSP_012973|||http://purl.uniprot.org/annotation/VSP_012974|||http://purl.uniprot.org/annotation/VSP_012975|||http://purl.uniprot.org/annotation/VSP_012976 http://togogenome.org/gene/10090:Sh2d1b2 ^@ http://purl.uniprot.org/uniprot/Q45HK4 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant ^@ Chain|||Domain Extent|||Sequence Variant ^@ In strain: 129Sv.|||SH2|||SH2 domain-containing protein 1B2 ^@ http://purl.uniprot.org/annotation/PRO_0000435288 http://togogenome.org/gene/10090:Zfp963 ^@ http://purl.uniprot.org/uniprot/D3Z2T8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Elob ^@ http://purl.uniprot.org/uniprot/P62869 ^@ Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Disordered|||Elongin-B|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000114915 http://togogenome.org/gene/10090:Dmrt1 ^@ http://purl.uniprot.org/uniprot/Q9QZ59 ^@ 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 ^@ DM|||Disordered|||Doublesex- and mab-3-related transcription factor 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000207043|||http://purl.uniprot.org/annotation/VSP_042963|||http://purl.uniprot.org/annotation/VSP_042964|||http://purl.uniprot.org/annotation/VSP_042965 http://togogenome.org/gene/10090:Gm13272 ^@ http://purl.uniprot.org/uniprot/B1AYI3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015087047 http://togogenome.org/gene/10090:Snai3 ^@ http://purl.uniprot.org/uniprot/Q9QY31 ^@ 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; degenerate|||SNAG domain|||Zinc finger protein SNAI3 ^@ http://purl.uniprot.org/annotation/PRO_0000330038 http://togogenome.org/gene/10090:Cops3 ^@ http://purl.uniprot.org/uniprot/O88543|||http://purl.uniprot.org/uniprot/Q3UQL2 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ COP9 signalosome complex subunit 3|||Disordered|||N-acetylalanine|||PCI|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000120979 http://togogenome.org/gene/10090:Defb29 ^@ http://purl.uniprot.org/uniprot/A3KGR0|||http://purl.uniprot.org/uniprot/Q8BGW9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Beta-defensin|||Beta-defensin 29|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000006945 http://togogenome.org/gene/10090:Or51f1 ^@ http://purl.uniprot.org/uniprot/Q7TRS5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tbc1d8 ^@ http://purl.uniprot.org/uniprot/Q9Z1A9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Site ^@ Arginine finger|||Basic and acidic residues|||Disordered|||GRAM 1|||GRAM 2|||Glutamine finger|||Rab-GAP TBC|||TBC1 domain family member 8 ^@ http://purl.uniprot.org/annotation/PRO_0000208034 http://togogenome.org/gene/10090:Fam3c ^@ http://purl.uniprot.org/uniprot/Q91VU0 ^@ 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 ^@ GG-type lectin|||Protein FAM3C ^@ http://purl.uniprot.org/annotation/PRO_0000008753 http://togogenome.org/gene/10090:Myoz2 ^@ http://purl.uniprot.org/uniprot/Q9JJW5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Myozenin-2|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000111100 http://togogenome.org/gene/10090:A630001G21Rik ^@ http://purl.uniprot.org/uniprot/Q3UTB2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||HSR|||Polar residues ^@ http://togogenome.org/gene/10090:Bcl10 ^@ http://purl.uniprot.org/uniprot/B7ZWE5|||http://purl.uniprot.org/uniprot/Q9Z0H7 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Site ^@ B-cell lymphoma/leukemia 10|||CARD|||Cleavage; by MALT1|||Decreased interaction with CARD11.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000144075 http://togogenome.org/gene/10090:F2r ^@ http://purl.uniprot.org/uniprot/P30558 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ 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|||Removed for receptor activation ^@ http://purl.uniprot.org/annotation/PRO_0000012742|||http://purl.uniprot.org/annotation/PRO_0000012743 http://togogenome.org/gene/10090:Arhgap8 ^@ http://purl.uniprot.org/uniprot/Q9CXP4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ CRAL-TRIO|||Disordered|||Pro residues|||Rho GTPase-activating protein 8|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000056711 http://togogenome.org/gene/10090:Fndc7 ^@ http://purl.uniprot.org/uniprot/A2AED3 ^@ 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 ^@ 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|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000284678|||http://purl.uniprot.org/annotation/VSP_024610|||http://purl.uniprot.org/annotation/VSP_024611|||http://purl.uniprot.org/annotation/VSP_024612|||http://purl.uniprot.org/annotation/VSP_024613 http://togogenome.org/gene/10090:Trim43c ^@ http://purl.uniprot.org/uniprot/P86449 ^@ 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 43C ^@ http://purl.uniprot.org/annotation/PRO_0000392436 http://togogenome.org/gene/10090:Gcg ^@ http://purl.uniprot.org/uniprot/P55095 ^@ Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide|||Site ^@ Compositionally Biased Region|||Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide|||Site ^@ Arginine amide|||Basic and acidic residues|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000011273|||http://purl.uniprot.org/annotation/PRO_0000011274|||http://purl.uniprot.org/annotation/PRO_0000011275|||http://purl.uniprot.org/annotation/PRO_0000011276|||http://purl.uniprot.org/annotation/PRO_0000011277|||http://purl.uniprot.org/annotation/PRO_0000011278|||http://purl.uniprot.org/annotation/PRO_0000011279|||http://purl.uniprot.org/annotation/PRO_0000011280|||http://purl.uniprot.org/annotation/PRO_0000011281|||http://purl.uniprot.org/annotation/PRO_0000011282 http://togogenome.org/gene/10090:Camkv ^@ http://purl.uniprot.org/uniprot/Q3UHL1 ^@ 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 ^@ CaM kinase-like vesicle-associated protein|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000250095 http://togogenome.org/gene/10090:Map7 ^@ http://purl.uniprot.org/uniprot/D3YWN7|||http://purl.uniprot.org/uniprot/E9QMU3|||http://purl.uniprot.org/uniprot/O88735 ^@ 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 and acidic residues|||Disordered|||Ensconsin|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000255950|||http://purl.uniprot.org/annotation/VSP_021318 http://togogenome.org/gene/10090:Tgfa ^@ http://purl.uniprot.org/uniprot/P48030|||http://purl.uniprot.org/uniprot/Q545E4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EGF-like|||Extracellular|||Helical|||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_0000007758|||http://purl.uniprot.org/annotation/PRO_0000007759|||http://purl.uniprot.org/annotation/PRO_0000007760|||http://purl.uniprot.org/annotation/PRO_0000302746|||http://purl.uniprot.org/annotation/PRO_5014309574 http://togogenome.org/gene/10090:Rdh12 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1M3|||http://purl.uniprot.org/uniprot/Q8BYK4 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Signal Peptide ^@ Proton acceptor|||Retinol dehydrogenase 12 ^@ http://purl.uniprot.org/annotation/PRO_0000054767|||http://purl.uniprot.org/annotation/PRO_5006452036 http://togogenome.org/gene/10090:Ugcg ^@ http://purl.uniprot.org/uniprot/O88693 ^@ 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_0000059177 http://togogenome.org/gene/10090:Pdlim4 ^@ http://purl.uniprot.org/uniprot/P70271|||http://purl.uniprot.org/uniprot/Q5SWV3 ^@ 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 ^@ Disordered|||Interaction with TRIP6.|||LIM zinc-binding|||No loss of interaction with PTPN13 (via PDZ domains).|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-261.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-263.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-264.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-265.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-266.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-267.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-272.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-274.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-276.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-277.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-286.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-288.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-291.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-292.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-294.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-295.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-299.|||No loss of interaction with PTPN13 (via PDZ domains); when associated with A-301.|||PDZ|||PDZ and LIM domain protein 4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000075874 http://togogenome.org/gene/10090:Ccdc14 ^@ http://purl.uniprot.org/uniprot/Q8K2J4 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Coiled-coil domain-containing protein 14|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000333044 http://togogenome.org/gene/10090:Pla2g2e ^@ http://purl.uniprot.org/uniprot/Q3UG05|||http://purl.uniprot.org/uniprot/Q9QUL3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Group IIE secretory phospholipase A2|||Phospholipase A2 ^@ http://purl.uniprot.org/annotation/PRO_0000022758|||http://purl.uniprot.org/annotation/PRO_5014205832 http://togogenome.org/gene/10090:Metap2 ^@ http://purl.uniprot.org/uniprot/O08663|||http://purl.uniprot.org/uniprot/Q58E65 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Methionine aminopeptidase 2|||N-acetylalanine|||O-linked (GlcNAc) serine; alternate|||Peptidase M24|||Phosphoserine; alternate|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000148983 http://togogenome.org/gene/10090:Acot1 ^@ http://purl.uniprot.org/uniprot/O55137 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Site ^@ Active Site|||Chain|||Modified Residue|||Mutagenesis Site ^@ Abolishes activity.|||Acyl-coenzyme A thioesterase 1|||Charge relay system|||Phosphoserine|||Retains 2% of the initial activity; deacylation of the acyl-enzyme intermediate becomes rate-limiting. ^@ http://purl.uniprot.org/annotation/PRO_0000202156 http://togogenome.org/gene/10090:Hbb-bh2 ^@ http://purl.uniprot.org/uniprot/B2RVB7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Globin family profile ^@ http://togogenome.org/gene/10090:Slc46a1 ^@ http://purl.uniprot.org/uniprot/Q6PEM8 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Proton-coupled folate transporter|||reversibly protonated residue during proton transport ^@ http://purl.uniprot.org/annotation/PRO_0000084852 http://togogenome.org/gene/10090:Eefsec ^@ http://purl.uniprot.org/uniprot/Q3UGH6|||http://purl.uniprot.org/uniprot/Q9JHW4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||G1|||G2|||G3|||G4|||G5|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Selenocysteine-specific elongation factor|||Tr-type G|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000091479 http://togogenome.org/gene/10090:Orc4 ^@ http://purl.uniprot.org/uniprot/O88708|||http://purl.uniprot.org/uniprot/Q8C693|||http://purl.uniprot.org/uniprot/Q9CZF7 ^@ 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 ^@ AAA+ ATPase|||N6-methyllysine|||Orc1-like AAA ATPase|||Origin recognition complex subunit 4 ^@ http://purl.uniprot.org/annotation/PRO_0000127088 http://togogenome.org/gene/10090:Zfp760 ^@ http://purl.uniprot.org/uniprot/E9QAF5|||http://purl.uniprot.org/uniprot/Q5U4A6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Papola ^@ http://purl.uniprot.org/uniprot/E9PZR3|||http://purl.uniprot.org/uniprot/Q3V141|||http://purl.uniprot.org/uniprot/Q61183 ^@ 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|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Eliminates MAPK-mediated phosphorylation.|||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.|||In isoform 3.|||In isoform 4.|||Interaction with RNA|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nuclear localization signal 1|||Nuclear localization signal 2|||Phosphoserine|||Phosphoserine; by MAPK|||Polar residues|||Poly(A) polymerase RNA-binding|||Poly(A) polymerase alpha|||Poly(A) polymerase central|||Polymerase nucleotidyl transferase|||Required for interaction with NUDT21|||Ser/Thr-rich|||Some loss of sumoylation. No change in nuclear localization.|||Some loss of sumoylation; Largely localized to the cytoplasm. ^@ http://purl.uniprot.org/annotation/PRO_0000051613|||http://purl.uniprot.org/annotation/VSP_004527|||http://purl.uniprot.org/annotation/VSP_004528|||http://purl.uniprot.org/annotation/VSP_004529|||http://purl.uniprot.org/annotation/VSP_004530|||http://purl.uniprot.org/annotation/VSP_004531|||http://purl.uniprot.org/annotation/VSP_004532 http://togogenome.org/gene/10090:Dscam ^@ http://purl.uniprot.org/uniprot/Q9ERC8 ^@ 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 ^@ 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|||N-linked (GlcNAc...) asparagine|||Polar residues|||Required for netrin-mediated axon repulsion of neuronal growth cones ^@ http://purl.uniprot.org/annotation/PRO_0000392478 http://togogenome.org/gene/10090:Htt ^@ http://purl.uniprot.org/uniprot/G3X9H5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Kctd8 ^@ http://purl.uniprot.org/uniprot/Q50H33 ^@ 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 ^@ BTB|||BTB/POZ domain-containing protein KCTD8|||Basic and acidic residues|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000251482|||http://purl.uniprot.org/annotation/VSP_020761|||http://purl.uniprot.org/annotation/VSP_020762 http://togogenome.org/gene/10090:Nobox ^@ http://purl.uniprot.org/uniprot/Q8VIH1 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes DNA-binding.|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein NOBOX|||No effect on DNA-binding.|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000268866 http://togogenome.org/gene/10090:Klhdc4 ^@ http://purl.uniprot.org/uniprot/G3X961 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Dcun1d2 ^@ http://purl.uniprot.org/uniprot/G5E8Q5|||http://purl.uniprot.org/uniprot/G5E8Q6|||http://purl.uniprot.org/uniprot/Q3TSY8|||http://purl.uniprot.org/uniprot/Q8BZJ7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Splice Variant ^@ DCN1-like protein 2|||DCUN1|||In isoform 2.|||In isoform 3.|||Phosphoserine|||UBA-like ^@ http://purl.uniprot.org/annotation/PRO_0000129502|||http://purl.uniprot.org/annotation/VSP_015318|||http://purl.uniprot.org/annotation/VSP_027370 http://togogenome.org/gene/10090:Ap1g1 ^@ http://purl.uniprot.org/uniprot/P22892|||http://purl.uniprot.org/uniprot/Q8CBB7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Mutagenesis Site|||Region|||Strand|||Turn ^@ AP-1 complex subunit gamma-1|||Disordered|||GAE|||Polar residues|||Reduces interaction with EPS15 and SYNRG.|||Removed|||Strongly reduces interaction with EPS15 and SYNRG. ^@ http://purl.uniprot.org/annotation/PRO_0000193759 http://togogenome.org/gene/10090:Kansl1 ^@ http://purl.uniprot.org/uniprot/A2A5Y4|||http://purl.uniprot.org/uniprot/Q80TG1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||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 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||KAT8 regulatory NSL complex subunit 1|||N6-acetyllysine|||PEHE|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for activation of KAT8 histone acetyltransferase activity|||Sufficient for interaction with KAT8 ^@ http://purl.uniprot.org/annotation/PRO_0000234566|||http://purl.uniprot.org/annotation/VSP_018360|||http://purl.uniprot.org/annotation/VSP_018361|||http://purl.uniprot.org/annotation/VSP_018362|||http://purl.uniprot.org/annotation/VSP_018363|||http://purl.uniprot.org/annotation/VSP_018364|||http://purl.uniprot.org/annotation/VSP_018365 http://togogenome.org/gene/10090:Plk1 ^@ http://purl.uniprot.org/uniprot/Q07832|||http://purl.uniprot.org/uniprot/Q3TPZ2 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||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|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolishes activity.|||Abolishes interaction with NEDD9; when associated with A-538.|||Abolishes interaction with NEDD9; when associated with M-540.|||Activation loop|||D-box that targets the protein for proteasomal degradation in anaphase|||Decreases activity three-fold.|||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|||Increases activity four-fold.|||Linker|||No change in activity.|||POLO box|||POLO box 1|||POLO box 2|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by AURKA|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PLK1 ^@ http://purl.uniprot.org/annotation/PRO_0000086557 http://togogenome.org/gene/10090:Rbm45 ^@ http://purl.uniprot.org/uniprot/Q3US38|||http://purl.uniprot.org/uniprot/Q8BHN5 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||RNA-binding protein 45|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000081573 http://togogenome.org/gene/10090:Gli3 ^@ http://purl.uniprot.org/uniprot/B2RUG4|||http://purl.uniprot.org/uniprot/Q3TYX7|||http://purl.uniprot.org/uniprot/Q61602 ^@ 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 ^@ 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|||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_0000047203|||http://purl.uniprot.org/annotation/PRO_0000406138 http://togogenome.org/gene/10090:Slc16a10 ^@ http://purl.uniprot.org/uniprot/Q3U9N9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||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.|||Monocarboxylate transporter 10|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000314254|||http://purl.uniprot.org/annotation/VSP_030252|||http://purl.uniprot.org/annotation/VSP_030253 http://togogenome.org/gene/10090:Tcim ^@ http://purl.uniprot.org/uniprot/Q9D915 ^@ Chain|||Molecule Processing ^@ Chain ^@ Transcriptional and immune response regulator ^@ http://purl.uniprot.org/annotation/PRO_0000089606 http://togogenome.org/gene/10090:Zscan20 ^@ http://purl.uniprot.org/uniprot/B2KFW1 ^@ 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 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|||Disordered|||In isoform 2.|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 20 ^@ http://purl.uniprot.org/annotation/PRO_0000367588|||http://purl.uniprot.org/annotation/VSP_036740 http://togogenome.org/gene/10090:Prxl2b ^@ http://purl.uniprot.org/uniprot/Q9DB60 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Modified Residue|||Mutagenesis Site ^@ Almost abolishes enzyme activity.|||Decreased enzyme activity to retain 63% of wild type activity.|||Phosphotyrosine|||Prostamide/prostaglandin F synthase ^@ http://purl.uniprot.org/annotation/PRO_0000284638 http://togogenome.org/gene/10090:Apom ^@ http://purl.uniprot.org/uniprot/Q9Z1R3 ^@ Binding Site|||Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Site|||Strand ^@ Binding Site|||Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Strand ^@ Apolipoprotein M|||Not cleaved ^@ http://purl.uniprot.org/annotation/PRO_0000223279 http://togogenome.org/gene/10090:Tmem59 ^@ http://purl.uniprot.org/uniprot/Q9QY73 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ ATG16L1-binding motif|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Transmembrane protein 59 ^@ http://purl.uniprot.org/annotation/PRO_0000003004 http://togogenome.org/gene/10090:Retreg3 ^@ http://purl.uniprot.org/uniprot/Q9CQV4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes interaction with ATG8 family proteins.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||LIR motif|||Lumenal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reticulophagy regulator 3 ^@ http://purl.uniprot.org/annotation/PRO_0000288470|||http://purl.uniprot.org/annotation/VSP_025689 http://togogenome.org/gene/10090:Musk ^@ http://purl.uniprot.org/uniprot/E9PVV8|||http://purl.uniprot.org/uniprot/Q1XD56|||http://purl.uniprot.org/uniprot/Q32S49|||http://purl.uniprot.org/uniprot/Q32S50|||http://purl.uniprot.org/uniprot/Q32SD3|||http://purl.uniprot.org/uniprot/Q497X0|||http://purl.uniprot.org/uniprot/Q61006 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||FZ|||Helical|||Ig-like|||Ig-like 1|||Ig-like 2|||Ig-like 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of interaction with DOK7.|||Muscle, skeletal receptor tyrosine-protein kinase|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by CK2|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000024447|||http://purl.uniprot.org/annotation/PRO_5003245416|||http://purl.uniprot.org/annotation/PRO_5004197438|||http://purl.uniprot.org/annotation/PRO_5004221087|||http://purl.uniprot.org/annotation/PRO_5004221250|||http://purl.uniprot.org/annotation/PRO_5004221295|||http://purl.uniprot.org/annotation/PRO_5015097585|||http://purl.uniprot.org/annotation/VSP_010784|||http://purl.uniprot.org/annotation/VSP_010785|||http://purl.uniprot.org/annotation/VSP_010786 http://togogenome.org/gene/10090:Atl1 ^@ http://purl.uniprot.org/uniprot/Q8BH66 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Atlastin-1|||Cytoplasmic|||Disordered|||GB1/RHD3-type G|||Helical|||Lumenal|||N6-acetyllysine|||Phosphoserine|||Sufficient for membrane association ^@ http://purl.uniprot.org/annotation/PRO_0000190973 http://togogenome.org/gene/10090:Gtf2h5 ^@ http://purl.uniprot.org/uniprot/Q8K2X8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ General transcription factor IIH subunit 5|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000119257 http://togogenome.org/gene/10090:Zdhhc5 ^@ http://purl.uniprot.org/uniprot/Q8VDZ4 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Loss of palmitoyltransferase activity.|||Omega-N-methylarginine|||Palmitoyltransferase ZDHHC5|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212869|||http://purl.uniprot.org/annotation/VSP_006936|||http://purl.uniprot.org/annotation/VSP_006937 http://togogenome.org/gene/10090:Gldn ^@ http://purl.uniprot.org/uniprot/Q8BMF8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes BMP1-mediated cleavage of ectodomain release of olfactomedin-like domain.|||Abolishes furin-mediated cleavage and shedding of ectodomain.|||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|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000246322|||http://purl.uniprot.org/annotation/PRO_0000434266 http://togogenome.org/gene/10090:Prpf40b ^@ http://purl.uniprot.org/uniprot/A0A0R4J1S2|||http://purl.uniprot.org/uniprot/E9QP07|||http://purl.uniprot.org/uniprot/Q80W14 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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.|||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_0000309283|||http://purl.uniprot.org/annotation/VSP_029122|||http://purl.uniprot.org/annotation/VSP_029123|||http://purl.uniprot.org/annotation/VSP_029124|||http://purl.uniprot.org/annotation/VSP_029125 http://togogenome.org/gene/10090:Mmachc ^@ http://purl.uniprot.org/uniprot/Q9CZD0 ^@ 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 ^@ Cyanocobalamin reductase / alkylcobalamin dealkylase|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000076259 http://togogenome.org/gene/10090:Serpina3g ^@ http://purl.uniprot.org/uniprot/Q3U0Y1|||http://purl.uniprot.org/uniprot/Q5I2A0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Site ^@ RCL|||Reactive bond|||Serine protease inhibitor A3G|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_0000094098 http://togogenome.org/gene/10090:Or8k24 ^@ http://purl.uniprot.org/uniprot/Q7TR74 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Frat1 ^@ http://purl.uniprot.org/uniprot/B2RU64|||http://purl.uniprot.org/uniprot/P70339 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Involved in GSK-3 binding|||Phosphoserine|||Proto-oncogene FRAT1 ^@ http://purl.uniprot.org/annotation/PRO_0000087333 http://togogenome.org/gene/10090:Hace1 ^@ http://purl.uniprot.org/uniprot/Q3U0D9 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||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 isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4. ^@ http://purl.uniprot.org/annotation/PRO_0000280623|||http://purl.uniprot.org/annotation/VSP_023832|||http://purl.uniprot.org/annotation/VSP_023833|||http://purl.uniprot.org/annotation/VSP_023834|||http://purl.uniprot.org/annotation/VSP_042379 http://togogenome.org/gene/10090:Fam50b ^@ http://purl.uniprot.org/uniprot/Q9WTJ8 ^@ 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 and acidic residues|||Disordered|||N-acetylalanine|||Protein FAM50B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000068287 http://togogenome.org/gene/10090:Nacc1 ^@ http://purl.uniprot.org/uniprot/Q7TSZ8 ^@ 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 ^@ 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|||Nucleus accumbens-associated protein 1|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000274042 http://togogenome.org/gene/10090:Psmd6 ^@ http://purl.uniprot.org/uniprot/Q99JI4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ 26S proteasome non-ATPase regulatory subunit 6|||PCI ^@ http://purl.uniprot.org/annotation/PRO_0000173839 http://togogenome.org/gene/10090:Otud4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J260|||http://purl.uniprot.org/uniprot/B2RRE7 ^@ 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 ^@ Abolishes 'Lys-48'- and 'Lys-63'-specific deubiquitinase activity. Impairs 'Lys-63'-specific deubiquitination of TRAF6 substrate.|||Basic and acidic residues|||Cys-loop|||Disordered|||His-loop|||N-acetylmethionine|||Nucleophile|||OTU|||OTU domain-containing protein 4|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Variable-loop ^@ http://purl.uniprot.org/annotation/PRO_0000394458 http://togogenome.org/gene/10090:Ccdc182 ^@ http://purl.uniprot.org/uniprot/Q9D9C6 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Coiled-coil domain-containing protein 182 ^@ http://purl.uniprot.org/annotation/PRO_0000329035 http://togogenome.org/gene/10090:Klhl33 ^@ http://purl.uniprot.org/uniprot/G3UW92 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BACK ^@ http://togogenome.org/gene/10090:Rnf11 ^@ http://purl.uniprot.org/uniprot/Q9QYK7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ Abolishes interaction with NEDD4.|||Disordered|||N-myristoyl glycine|||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_0000056051 http://togogenome.org/gene/10090:Lrrc3 ^@ http://purl.uniprot.org/uniprot/P59034|||http://purl.uniprot.org/uniprot/Q543Z4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Repeat|||Signal Peptide|||Transmembrane ^@ Helical|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000021619|||http://purl.uniprot.org/annotation/PRO_5014309568 http://togogenome.org/gene/10090:Cd209g ^@ http://purl.uniprot.org/uniprot/D3Z5D4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C-type lectin ^@ http://togogenome.org/gene/10090:Apoa5 ^@ http://purl.uniprot.org/uniprot/Q8C7G5 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Apolipoprotein A-V|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000001982 http://togogenome.org/gene/10090:Pou2f1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Z4|||http://purl.uniprot.org/uniprot/E9Q6Z8|||http://purl.uniprot.org/uniprot/F8VQL7|||http://purl.uniprot.org/uniprot/P25425 ^@ 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 ^@ Disordered|||Homeobox|||In isoform 10.|||In isoform 12.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3 and isoform 8.|||In isoform 4 and isoform 11.|||In isoform 4, isoform 5 and isoform 11.|||In isoform 4.|||In isoform 6 and isoform 8.|||In isoform 7.|||In isoform 9.|||POU domain, class 2, transcription factor 1|||POU-specific|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000100708|||http://purl.uniprot.org/annotation/VSP_002321|||http://purl.uniprot.org/annotation/VSP_002322|||http://purl.uniprot.org/annotation/VSP_002323|||http://purl.uniprot.org/annotation/VSP_007271|||http://purl.uniprot.org/annotation/VSP_007272|||http://purl.uniprot.org/annotation/VSP_007273|||http://purl.uniprot.org/annotation/VSP_007274|||http://purl.uniprot.org/annotation/VSP_007275|||http://purl.uniprot.org/annotation/VSP_007276|||http://purl.uniprot.org/annotation/VSP_007277|||http://purl.uniprot.org/annotation/VSP_007278|||http://purl.uniprot.org/annotation/VSP_013403|||http://purl.uniprot.org/annotation/VSP_013404|||http://purl.uniprot.org/annotation/VSP_013405 http://togogenome.org/gene/10090:Sobp ^@ http://purl.uniprot.org/uniprot/Q0P5V2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||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_0000312233 http://togogenome.org/gene/10090:Tpm3 ^@ http://purl.uniprot.org/uniprot/D3Z6I8|||http://purl.uniprot.org/uniprot/E9Q5J9|||http://purl.uniprot.org/uniprot/P21107|||http://purl.uniprot.org/uniprot/Q58E70|||http://purl.uniprot.org/uniprot/Q8C7C3|||http://purl.uniprot.org/uniprot/Q8K0Z5 ^@ 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|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||N-acetylalanine|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Tropomyosin alpha-3 chain ^@ http://purl.uniprot.org/annotation/PRO_0000205633|||http://purl.uniprot.org/annotation/VSP_006608|||http://purl.uniprot.org/annotation/VSP_006609|||http://purl.uniprot.org/annotation/VSP_006610 http://togogenome.org/gene/10090:Mcrip1 ^@ http://purl.uniprot.org/uniprot/Q3UGS4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Modified Residue|||Motif|||Region ^@ Disordered|||Mapk-regulated corepressor-interacting protein 1|||N6-acetyllysine|||PXDLS motif|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000393955 http://togogenome.org/gene/10090:Or5p52 ^@ http://purl.uniprot.org/uniprot/A6H654|||http://purl.uniprot.org/uniprot/Q8VG43 ^@ 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 5P52 ^@ http://purl.uniprot.org/annotation/PRO_0000150832 http://togogenome.org/gene/10090:Vmn2r32 ^@ http://purl.uniprot.org/uniprot/K7N686 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003910726 http://togogenome.org/gene/10090:Acox2 ^@ http://purl.uniprot.org/uniprot/Q9QXD1 ^@ 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|||Microbody targeting signal|||N6-succinyllysine|||Peroxisomal acyl-coenzyme A oxidase 2|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000204682 http://togogenome.org/gene/10090:Trub1 ^@ http://purl.uniprot.org/uniprot/Q8C0D0 ^@ Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||N-acetylalanine|||Nucleophile|||Pseudouridylate synthase TRUB1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000252088|||http://purl.uniprot.org/annotation/VSP_020860|||http://purl.uniprot.org/annotation/VSP_020861 http://togogenome.org/gene/10090:Fuca1 ^@ http://purl.uniprot.org/uniprot/Q99LJ1 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site ^@ May be important for catalysis|||N-linked (GlcNAc...) asparagine|||Tissue alpha-L-fucosidase ^@ http://purl.uniprot.org/annotation/PRO_0000010310 http://togogenome.org/gene/10090:Med16 ^@ http://purl.uniprot.org/uniprot/E9QP84|||http://purl.uniprot.org/uniprot/G3UW74|||http://purl.uniprot.org/uniprot/Q3UET8 ^@ Region|||Repeat ^@ Region|||Repeat ^@ Disordered|||WD ^@ http://togogenome.org/gene/10090:C2cd4a ^@ http://purl.uniprot.org/uniprot/E9Q861 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:H2az1 ^@ http://purl.uniprot.org/uniprot/P0C0S6|||http://purl.uniprot.org/uniprot/Q3UA95 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Histone H2A C-terminal|||Histone H2A.Z|||Histone H2A/H2B/H3|||M6 cassette|||N6-acetyllysine; alternate|||N6-lactoyllysine|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||Removed|||Required for interaction with INCENP|||Required for interaction with PWWP2A ^@ http://purl.uniprot.org/annotation/PRO_0000055298 http://togogenome.org/gene/10090:Slc22a4 ^@ http://purl.uniprot.org/uniprot/Q9Z306 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||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 4 ^@ http://purl.uniprot.org/annotation/PRO_0000220498 http://togogenome.org/gene/10090:Wbp11 ^@ http://purl.uniprot.org/uniprot/Q923D5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs interaction with PP1; when associated with A-219.|||Impairs interaction with PP1; when associated with A-221.|||Impairs interaction with PP1; when associated with A-308.|||Impairs interaction with PP1; when associated with A-310.|||Interaction with PP1|||N6-acetyllysine|||Omega-N-methylarginine|||PGR|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||Required for nuclear export|||Required for nuclear import|||WW domain-binding protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000065946 http://togogenome.org/gene/10090:Mob3a ^@ http://purl.uniprot.org/uniprot/Q8BSU7 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ MOB kinase activator 3A ^@ http://purl.uniprot.org/annotation/PRO_0000193571 http://togogenome.org/gene/10090:Klk1 ^@ http://purl.uniprot.org/uniprot/A0A0B6VSQ6|||http://purl.uniprot.org/uniprot/P15947 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Kallikrein-1|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027975|||http://purl.uniprot.org/annotation/PRO_0000027976|||http://purl.uniprot.org/annotation/PRO_5014221785 http://togogenome.org/gene/10090:Robo1 ^@ http://purl.uniprot.org/uniprot/G5E843|||http://purl.uniprot.org/uniprot/O89026|||http://purl.uniprot.org/uniprot/Q3UQ03|||http://purl.uniprot.org/uniprot/Q3UXH3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Loss of expression in the kidney of homozygous mice. Mutant mice have severe urogenital defects, congenital heart defects and craniofacial abnormalities.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Roundabout homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000031034 http://togogenome.org/gene/10090:Or5b116 ^@ http://purl.uniprot.org/uniprot/F6QVZ8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nek3 ^@ http://purl.uniprot.org/uniprot/F8WGD4|||http://purl.uniprot.org/uniprot/Q9R0A5 ^@ 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|||Region|||Sequence Conflict ^@ Disordered|||Distorted neuronal morphology with disturbed polarity and deacetylation of microtubules.|||Interaction with VAV2|||N-acetylmethionine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek3 ^@ http://purl.uniprot.org/annotation/PRO_0000086424 http://togogenome.org/gene/10090:Cyp2r1 ^@ http://purl.uniprot.org/uniprot/Q32MW1|||http://purl.uniprot.org/uniprot/Q6VVW9 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Helical|||Vitamin D 25-hydroxylase|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051779 http://togogenome.org/gene/10090:Slc50a1 ^@ http://purl.uniprot.org/uniprot/Q9CXK4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Mediates interaction with TRPV2|||MtN3/slv 1|||MtN3/slv 2|||Sugar transporter SWEET1 ^@ http://purl.uniprot.org/annotation/PRO_0000345117 http://togogenome.org/gene/10090:Hmga1b ^@ http://purl.uniprot.org/uniprot/P17095|||http://purl.uniprot.org/uniprot/Q3TVP0|||http://purl.uniprot.org/uniprot/Q566K0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||High mobility group protein HMG-I/HMG-Y|||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 HIPK2 and CDC2|||Phosphothreonine|||Phosphothreonine; by HIPK2 and CDC2|||Polar residues|||Removed|||Symmetric dimethylarginine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000206709|||http://purl.uniprot.org/annotation/VSP_012406 http://togogenome.org/gene/10090:Nkrf ^@ http://purl.uniprot.org/uniprot/Q8BY02 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Active repression domain|||Disordered|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||NF-kappa-B-repressing factor|||Nuclear localization signal|||Phosphoserine|||Polar residues|||R3H ^@ http://purl.uniprot.org/annotation/PRO_0000096870 http://togogenome.org/gene/10090:Spata21 ^@ http://purl.uniprot.org/uniprot/Q8BHW6 ^@ 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|||Polar residues|||Spermatogenesis-associated protein 21 ^@ http://purl.uniprot.org/annotation/PRO_0000330688 http://togogenome.org/gene/10090:4833439L19Rik ^@ http://purl.uniprot.org/uniprot/D3Z1F7|||http://purl.uniprot.org/uniprot/Q9DBN4 ^@ 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_0000307731|||http://purl.uniprot.org/annotation/VSP_028802|||http://purl.uniprot.org/annotation/VSP_028803|||http://purl.uniprot.org/annotation/VSP_028804|||http://purl.uniprot.org/annotation/VSP_028805 http://togogenome.org/gene/10090:2200002J24Rik ^@ http://purl.uniprot.org/uniprot/Q9D807 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Dync1i1 ^@ http://purl.uniprot.org/uniprot/D6Q0F3|||http://purl.uniprot.org/uniprot/D6Q0F4|||http://purl.uniprot.org/uniprot/O88485|||http://purl.uniprot.org/uniprot/Q3TYJ3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Abolishes interaction with DYNLL2.|||Basic and acidic residues|||Cytoplasmic dynein 1 intermediate chain 1|||Disordered|||Impairs interaction with DYNLL2.|||In isoform 1B.|||Interaction with DYNLT1|||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_0000114653|||http://purl.uniprot.org/annotation/VSP_001334 http://togogenome.org/gene/10090:Flnb ^@ http://purl.uniprot.org/uniprot/Q80X90 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Actin-binding|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||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|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Self-association site, tail ^@ http://purl.uniprot.org/annotation/PRO_0000087299 http://togogenome.org/gene/10090:Prrx1 ^@ http://purl.uniprot.org/uniprot/G3UZ44|||http://purl.uniprot.org/uniprot/P63013 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Disordered|||Homeobox|||In isoform 2.|||N6-acetyllysine|||OAR|||Paired mesoderm homeobox protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049252|||http://purl.uniprot.org/annotation/VSP_002279 http://togogenome.org/gene/10090:Mppe1 ^@ http://purl.uniprot.org/uniprot/Q80XL7 ^@ 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.|||Metallophosphoesterase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000315729|||http://purl.uniprot.org/annotation/VSP_030684|||http://purl.uniprot.org/annotation/VSP_030685|||http://purl.uniprot.org/annotation/VSP_030686 http://togogenome.org/gene/10090:Or9m2 ^@ http://purl.uniprot.org/uniprot/A2BHP7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rps23 ^@ http://purl.uniprot.org/uniprot/P62267 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ 3-hydroxyproline|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||N6-succinyllysine|||Small ribosomal subunit protein uS12 ^@ http://purl.uniprot.org/annotation/PRO_0000146458 http://togogenome.org/gene/10090:Hus1b ^@ http://purl.uniprot.org/uniprot/Q8K572 ^@ Chain|||Molecule Processing ^@ Chain ^@ Checkpoint protein HUS1B ^@ http://purl.uniprot.org/annotation/PRO_0000226246 http://togogenome.org/gene/10090:Pus7 ^@ http://purl.uniprot.org/uniprot/Q3ULP8|||http://purl.uniprot.org/uniprot/Q91VU7 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Nucleophile|||Phosphoserine|||Pseudouridylate synthase 7 homolog|||TRUD ^@ http://purl.uniprot.org/annotation/PRO_0000444609|||http://purl.uniprot.org/annotation/VSP_059623 http://togogenome.org/gene/10090:Or1ad1 ^@ http://purl.uniprot.org/uniprot/Q8VGH1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccdc85c ^@ http://purl.uniprot.org/uniprot/A0A217FL83|||http://purl.uniprot.org/uniprot/E9Q6B2 ^@ 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_0000415925 http://togogenome.org/gene/10090:Rorc ^@ http://purl.uniprot.org/uniprot/A0A0G2JGZ6|||http://purl.uniprot.org/uniprot/A0A0R4J096|||http://purl.uniprot.org/uniprot/P51450 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ AF-2|||Abolishes DNA-binding. No effect neither on interaction with NCOA1 and NCOA2 nor on inhibition of NFATC1 expression.|||Abolishes interaction with NCOA1 and NCOA2.|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of adipogenesis inhibition, when associated with A-31.|||Loss of adipogenesis inhibition, when associated with A-48.|||Loss of transactivation function.|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor ROR-gamma|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053518|||http://purl.uniprot.org/annotation/VSP_003659|||http://purl.uniprot.org/annotation/VSP_003660|||http://purl.uniprot.org/annotation/VSP_056787|||http://purl.uniprot.org/annotation/VSP_056788 http://togogenome.org/gene/10090:Sde2 ^@ http://purl.uniprot.org/uniprot/Q8K1J5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Site ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Propeptide|||Region|||Site ^@ Basic and acidic residues|||Cleavage|||Disordered|||PIP-box|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAP|||Splicing regulator SDE2|||UBL ^@ http://purl.uniprot.org/annotation/PRO_0000286085|||http://purl.uniprot.org/annotation/PRO_0000442522 http://togogenome.org/gene/10090:Nrg3 ^@ http://purl.uniprot.org/uniprot/E9Q396|||http://purl.uniprot.org/uniprot/G3V023|||http://purl.uniprot.org/uniprot/O35181 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||Helical; Note=Internal signal sequence|||Neuregulin-3|||Polar residues|||Pro-neuregulin-3, membrane-bound isoform ^@ http://purl.uniprot.org/annotation/PRO_0000019483|||http://purl.uniprot.org/annotation/PRO_0000019484 http://togogenome.org/gene/10090:Asxl2 ^@ http://purl.uniprot.org/uniprot/B2RUG8|||http://purl.uniprot.org/uniprot/D6REV1|||http://purl.uniprot.org/uniprot/Q8BJR0|||http://purl.uniprot.org/uniprot/Q8BZ32 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||DEUBAD|||Disordered|||HTH HARE-type|||LXXLL motif|||Nuclear localization signal|||PHD-type; atypical|||Phosphoserine|||Polar residues|||Putative Polycomb group protein ASXL2 ^@ http://purl.uniprot.org/annotation/PRO_0000313827 http://togogenome.org/gene/10090:D930020B18Rik ^@ http://purl.uniprot.org/uniprot/D3Z3G0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Pafah1b1 ^@ http://purl.uniprot.org/uniprot/P63005|||http://purl.uniprot.org/uniprot/Q5SW18 ^@ Chain|||Coiled-Coil|||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|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Strand|||Turn ^@ Abrogates interaction with NDEL1, PAFAH1B3 and RSN. Also impairs localization to centrosomes and microtubule plus ends. Reduces protein stability.|||Abrogates interaction with NDEL1.|||Abrogates interaction with NDLE1, NUDC, PAFAH1B3 and RSN. Also impairs localization to centrosomes and microtubule plus ends. Reduces protein stability.|||Abrogates interaction with PAFAH1B2.|||Abrogates interaction with PAFAH1B3 and RSN. Also impairs localization to centrosomes and microtubule plus ends. Reduces protein stability.|||Abrogates self-association and interaction with DAB1, dynein, NDEL1, PAFAH1B3 and RSN. Also impairs localization to centrosomes and microtubule plus ends. Reduces protein stability.|||Impairs self-association and reduces protein stability.|||Impairs self-association, reduces protein stability and promotes localization to actin fibers.|||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|||Removed|||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_0000051063|||http://purl.uniprot.org/annotation/VSP_006778 http://togogenome.org/gene/10090:Ttc23 ^@ http://purl.uniprot.org/uniprot/Q8CHY7 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Repeat|||Splice Variant ^@ In isoform 2.|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||Tetratricopeptide repeat protein 23 ^@ http://purl.uniprot.org/annotation/PRO_0000289549|||http://purl.uniprot.org/annotation/VSP_026019|||http://purl.uniprot.org/annotation/VSP_026020 http://togogenome.org/gene/10090:Cdc42bpg ^@ http://purl.uniprot.org/uniprot/Q80UW5 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ AGC-kinase C-terminal|||CNH|||CRIB|||Disordered|||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_0000086398 http://togogenome.org/gene/10090:Trim28 ^@ http://purl.uniprot.org/uniprot/Q5EBP9|||http://purl.uniprot.org/uniprot/Q62318 ^@ 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|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ B box-type|||B box-type 1|||B box-type 2|||Bromo|||Citrulline|||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|||HP1 box|||In chatwo; hypomorphic mutation with reduced protein stability and impaired transcriptional corepression activity. Embryonic development arrests prior to stage E9, with pronounced convergent extention defects and defective morphogenesis of extra-embryonic tissues. The anterior-posterior axis is shortened and embryos fail to undergo gut closure. No effect on interaction with ZFP568.|||In isoform 2.|||Interaction with MAGEC2|||Involved in binding PPP1CA|||Leucine zipper alpha helical coiled-coil region|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||PHD-type|||Phosphoserine|||Phosphoserine; by ATM and ATR and dsDNA kinase|||Phosphothreonine|||Phosphotyrosine|||PxVxL motif|||RING-type|||Removed|||Transcription intermediary factor 1-beta ^@ http://purl.uniprot.org/annotation/PRO_0000056393|||http://purl.uniprot.org/annotation/VSP_010899|||http://purl.uniprot.org/annotation/VSP_010900 http://togogenome.org/gene/10090:Nt5c1a ^@ http://purl.uniprot.org/uniprot/A3KFX0 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Region ^@ Cytosolic 5'-nucleotidase 1A|||Disordered|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000304930 http://togogenome.org/gene/10090:Coq3 ^@ http://purl.uniprot.org/uniprot/Q8BMS4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||N6-acetyllysine|||Polar residues|||Ubiquinone biosynthesis O-methyltransferase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000035927 http://togogenome.org/gene/10090:Il4ra ^@ http://purl.uniprot.org/uniprot/P16382|||http://purl.uniprot.org/uniprot/Q3U905 ^@ 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 ^@ Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||ITIM motif|||In isoform 2.|||In isoform 3.|||In strain: BALB/c, AKR/J and SJL/J.|||In strain: BALB/c, AKR/J and SJL/J; reduced IL4-neutralizing capacity of soluble form.|||Interleukin-4 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||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_0000010889|||http://purl.uniprot.org/annotation/PRO_0000010890|||http://purl.uniprot.org/annotation/PRO_5014309132|||http://purl.uniprot.org/annotation/VSP_001675|||http://purl.uniprot.org/annotation/VSP_001676|||http://purl.uniprot.org/annotation/VSP_001677 http://togogenome.org/gene/10090:Hs1bp3 ^@ http://purl.uniprot.org/uniprot/Q3TC93|||http://purl.uniprot.org/uniprot/Q8C910 ^@ 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 ^@ Basic and acidic residues|||Disordered|||HCLS1-binding protein 3|||N-acetylmethionine|||N6-acetyllysine|||PX|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000313803 http://togogenome.org/gene/10090:Bdkrb1 ^@ http://purl.uniprot.org/uniprot/Q0VBD7|||http://purl.uniprot.org/uniprot/Q61125 ^@ 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 ^@ B1 bradykinin 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 ^@ http://purl.uniprot.org/annotation/PRO_0000069184 http://togogenome.org/gene/10090:Smagp ^@ http://purl.uniprot.org/uniprot/A0A2R8W734|||http://purl.uniprot.org/uniprot/Q99KC7 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||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_0000328796 http://togogenome.org/gene/10090:Mrpl27 ^@ http://purl.uniprot.org/uniprot/Q99N92 ^@ Chain|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Region|||Transit Peptide ^@ Disordered|||Large ribosomal subunit protein bL27m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000181230 http://togogenome.org/gene/10090:Acvr2b ^@ http://purl.uniprot.org/uniprot/P27040 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Activin receptor type-2B|||Cytoplasmic|||Extracellular|||Helical|||In isoform ActR-IIB2 and isoform ActR-IIB4.|||In isoform ActR-IIB3 and isoform ActR-IIB4.|||Interaction with DYNLT1|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000024405|||http://purl.uniprot.org/annotation/VSP_004951|||http://purl.uniprot.org/annotation/VSP_004952 http://togogenome.org/gene/10090:Pdlim5 ^@ http://purl.uniprot.org/uniprot/D9J2Z9|||http://purl.uniprot.org/uniprot/D9J300|||http://purl.uniprot.org/uniprot/D9J301|||http://purl.uniprot.org/uniprot/D9J302|||http://purl.uniprot.org/uniprot/D9J303|||http://purl.uniprot.org/uniprot/E9Q8P5|||http://purl.uniprot.org/uniprot/Q8CI51|||http://purl.uniprot.org/uniprot/Q9CRA2 ^@ 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); alternate|||In isoform 2 and isoform 3.|||In isoform 3.|||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_0000075878|||http://purl.uniprot.org/annotation/VSP_010467|||http://purl.uniprot.org/annotation/VSP_010468|||http://purl.uniprot.org/annotation/VSP_010469|||http://purl.uniprot.org/annotation/VSP_010470 http://togogenome.org/gene/10090:Or5b99 ^@ http://purl.uniprot.org/uniprot/Q8VFX5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lilrb4b ^@ http://purl.uniprot.org/uniprot/A0A1W2P7F3|||http://purl.uniprot.org/uniprot/Q61450 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Abolishes mast cell activation and homodimerization.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Leukocyte immunoglobulin-like receptor subfamily B member 4B|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014767|||http://purl.uniprot.org/annotation/PRO_5015071734 http://togogenome.org/gene/10090:Or1e21 ^@ http://purl.uniprot.org/uniprot/Q8VGT3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cd3e ^@ http://purl.uniprot.org/uniprot/A6H6M1|||http://purl.uniprot.org/uniprot/P22646 ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITAM|||Ig-like|||Phosphotyrosine|||T-cell surface glycoprotein CD3 epsilon chain ^@ http://purl.uniprot.org/annotation/PRO_0000014609|||http://purl.uniprot.org/annotation/PRO_5014297004 http://togogenome.org/gene/10090:Agt ^@ http://purl.uniprot.org/uniprot/Q3UTR7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Atf4 ^@ http://purl.uniprot.org/uniprot/Q06507|||http://purl.uniprot.org/uniprot/Q8CF69 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 4-hydroxyproline|||Abolished phosphorylation by RPS6KA3/RSK2.|||BZIP|||Basic motif|||BetaTrCP degron motif|||Cyclic AMP-dependent transcription factor ATF-4|||Disordered|||Does not affect phosphorylation by RPS6KA3/RSK2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with GABBR1|||Leucine-zipper|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by RPS6KA3|||Phosphothreonine|||Polar residues|||Promotes stabilization due to impaired ubiquitination.|||Promotes stabilization due to impaired ubiquitination; when associated with A-212; A-223; A-230 and A-234. Does not affect phosphorylation by RPS6KA3/RSK2.|||Promotes stabilization due to impaired ubiquitination; when associated with A-212; A-223; A-230 and A-247.|||Promotes stabilization due to impaired ubiquitination; when associated with A-212; A-223; A-234 and A-247.|||Promotes stabilization due to impaired ubiquitination; when associated with A-212; A-230; A-234 and A-247.|||Promotes stabilization due to impaired ubiquitination; when associated with A-223; A-230; A-234 and A-247.|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076585 http://togogenome.org/gene/10090:Tas2r137 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0T3|||http://purl.uniprot.org/uniprot/Q7TQA7 ^@ 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|||Taste receptor type 2 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000082202 http://togogenome.org/gene/10090:Ttc34 ^@ http://purl.uniprot.org/uniprot/Q8C0Q3 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ 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_0000341279 http://togogenome.org/gene/10090:Mtres1 ^@ http://purl.uniprot.org/uniprot/Q9CQF4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Transit Peptide ^@ Acidic residues|||Disordered|||Mitochondrial transcription rescue factor 1|||Mitochondrion|||Phosphoserine|||S4 RNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000089560 http://togogenome.org/gene/10090:Krt72 ^@ http://purl.uniprot.org/uniprot/Q6IME9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type II cytoskeletal 72|||Linker 1|||Linker 12|||Polar residues|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000314878 http://togogenome.org/gene/10090:Hnrnpr ^@ http://purl.uniprot.org/uniprot/F7B5B5|||http://purl.uniprot.org/uniprot/Q3U8W9|||http://purl.uniprot.org/uniprot/Q3UKV5|||http://purl.uniprot.org/uniprot/Q3UZI0|||http://purl.uniprot.org/uniprot/Q8VHM5 ^@ 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 ^@ Disordered|||Polar residues|||RRM|||RRM domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5004230204|||http://purl.uniprot.org/annotation/PRO_5004230460 http://togogenome.org/gene/10090:Endou ^@ http://purl.uniprot.org/uniprot/Q3V188 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Splice Variant ^@ Alternate|||EndoU|||In isoform 2.|||SMB 1|||SMB 2|||Uridylate-specific endoribonuclease ^@ http://purl.uniprot.org/annotation/PRO_0000394222|||http://purl.uniprot.org/annotation/VSP_039224 http://togogenome.org/gene/10090:Rabgef1 ^@ http://purl.uniprot.org/uniprot/Q9JM13 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ A20-type|||Disordered|||Interaction with ubiquitinated proteins|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Rab5 GDP/GTP exchange factor|||VPS9 ^@ http://purl.uniprot.org/annotation/PRO_0000191316 http://togogenome.org/gene/10090:Lmod1 ^@ http://purl.uniprot.org/uniprot/F8VPR1|||http://purl.uniprot.org/uniprot/Q8BVA4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ 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|||Leiomodin-1|||Phosphoserine|||Polar residues|||Pro residues|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000354070 http://togogenome.org/gene/10090:Tcaf2 ^@ http://purl.uniprot.org/uniprot/Q921K8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Peptidase M60|||TRPM8 channel-associated factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000320188 http://togogenome.org/gene/10090:Klk1b1 ^@ http://purl.uniprot.org/uniprot/A0A1R3UCH6|||http://purl.uniprot.org/uniprot/P00755|||http://purl.uniprot.org/uniprot/Q8C232 ^@ 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|||Kallikrein 1-related peptidase b1|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Peptidase S1 domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000027966|||http://purl.uniprot.org/annotation/PRO_0000027967|||http://purl.uniprot.org/annotation/PRO_5004307283|||http://purl.uniprot.org/annotation/PRO_5014274084 http://togogenome.org/gene/10090:Cebpa ^@ http://purl.uniprot.org/uniprot/P53566 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Basic motif|||CCAAT/enhancer-binding protein alpha|||Decreases phosphorylated form. Deregulation of hepatic glucose metabolism.|||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 2.|||In isoform 3.|||In isoform 4.|||Interaction with FOXO1|||Leucine-zipper|||N6-acetyllysine; alternate|||No effect on DNA-binding or interaction with CDK2 and CDK4. No effect on cell cycle inhibition.|||No effect on DNA-binding, no effect on repression of E2F1:TFDP1-mediated transcription and no effect on adipogenesis and granulopoiesis; when associated with A-288.|||No effect on DNA-binding, no effect on repression of E2F1:TFDP1-mediated transcription and no effect on adipogenesis and granulopoiesis; when associated with A-291.|||No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia.|||No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia; when associated with A-295.|||No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia; when associated with A-298.|||No effect on DNA-binding. Loss of interaction with CDK2 and CDK4 as well as cell cycle inhibition.|||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_0000076614|||http://purl.uniprot.org/annotation/VSP_057549|||http://purl.uniprot.org/annotation/VSP_057550|||http://purl.uniprot.org/annotation/VSP_057608 http://togogenome.org/gene/10090:Sbpl ^@ http://purl.uniprot.org/uniprot/Q3TUY3|||http://purl.uniprot.org/uniprot/Q9CPP2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Jacalin-type lectin|||Jacalin-type lectin domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5010847688|||http://purl.uniprot.org/annotation/PRO_5015097462 http://togogenome.org/gene/10090:Rhox5 ^@ http://purl.uniprot.org/uniprot/Q3UJH4|||http://purl.uniprot.org/uniprot/Q4TU88 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Zfp14 ^@ http://purl.uniprot.org/uniprot/P10755|||http://purl.uniprot.org/uniprot/Q8BR51 ^@ 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 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 ^@ http://purl.uniprot.org/annotation/PRO_0000047286 http://togogenome.org/gene/10090:Chp1 ^@ http://purl.uniprot.org/uniprot/P61022 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Motif ^@ Calcineurin B homologous protein 1|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||N-myristoyl glycine|||Necessary for association with microtubule and interaction with GAPDH|||Nuclear export signal 1|||Nuclear export signal 2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073844 http://togogenome.org/gene/10090:Fndc10 ^@ http://purl.uniprot.org/uniprot/A2A9Q0|||http://purl.uniprot.org/uniprot/Q8BX63|||http://purl.uniprot.org/uniprot/Q9JJ92 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Basic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type III domain-containing protein 10|||Fibronectin type-III|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000416239|||http://purl.uniprot.org/annotation/PRO_5004331897 http://togogenome.org/gene/10090:Ptpn1 ^@ http://purl.uniprot.org/uniprot/P35821|||http://purl.uniprot.org/uniprot/Q3TZW9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Cysteine persulfide|||Disordered|||Helical|||N-acetylmethionine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphoserine; by CLK1 and CLK2|||Phosphoserine; by CLK1, CLK2 and PKB/AKT1 or PKB/AKT2|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by EGFR|||S-nitrosocysteine; in reversibly inhibited form|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 1 ^@ http://purl.uniprot.org/annotation/PRO_0000094749 http://togogenome.org/gene/10090:Rnf112 ^@ http://purl.uniprot.org/uniprot/Q96DY5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ GB1/RHD3-type G|||Helical|||In isoform 2.|||In isoform 3.|||Interaction with ZBTB16|||Loss of endosomal localization.|||RING finger protein 112|||RING-type|||Reduced GTP-hydrolysis. ^@ http://purl.uniprot.org/annotation/PRO_0000415817|||http://purl.uniprot.org/annotation/VSP_042392|||http://purl.uniprot.org/annotation/VSP_042393 http://togogenome.org/gene/10090:Cux2 ^@ http://purl.uniprot.org/uniprot/P70298 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||CUT 1|||CUT 2|||CUT 3|||Disordered|||Homeobox|||Homeobox protein cut-like 2|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000202397 http://togogenome.org/gene/10090:Nol4 ^@ http://purl.uniprot.org/uniprot/E9Q947|||http://purl.uniprot.org/uniprot/G3UW35|||http://purl.uniprot.org/uniprot/P60954|||http://purl.uniprot.org/uniprot/Q8C0U4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Nucleolar protein 4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096936|||http://purl.uniprot.org/annotation/VSP_040778|||http://purl.uniprot.org/annotation/VSP_040779|||http://purl.uniprot.org/annotation/VSP_040780 http://togogenome.org/gene/10090:Tmem126a ^@ http://purl.uniprot.org/uniprot/Q9D8Y1 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Transmembrane protein 126A ^@ http://purl.uniprot.org/annotation/PRO_0000271000 http://togogenome.org/gene/10090:Rasgrf2 ^@ http://purl.uniprot.org/uniprot/P70392 ^@ 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 ^@ DH|||Disordered|||IQ|||Loss of interaction with Ras. Loss of Ras activation. Loss of ubiquitination.|||N-terminal Ras-GEF|||PH 1|||PH 2|||Partial loss of interaction with Ras. Partial loss of Ras activation. Partial loss of ubiquitination.|||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_0000312864 http://togogenome.org/gene/10090:Vmn1r257 ^@ http://purl.uniprot.org/uniprot/E9PW18 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clca3a1 ^@ http://purl.uniprot.org/uniprot/Q9QX15 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Calcium-activated chloride channel regulator 3A-1|||Cleavage; by autolysis|||Metalloprotease domain|||N-linked (GlcNAc...) asparagine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5010510991 http://togogenome.org/gene/10090:Abca8b ^@ http://purl.uniprot.org/uniprot/A2AM56|||http://purl.uniprot.org/uniprot/Q8K440 ^@ 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 ^@ ABC transporter|||ABC transporter 1|||ABC transporter 2|||ABC-type organic anion transporter ABCA8B|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000250679|||http://purl.uniprot.org/annotation/VSP_020704 http://togogenome.org/gene/10090:Pklr ^@ http://purl.uniprot.org/uniprot/E9Q509|||http://purl.uniprot.org/uniprot/G3X925|||http://purl.uniprot.org/uniprot/Q3UEH4|||http://purl.uniprot.org/uniprot/Q3UEI4 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ Pyruvate kinase C-terminal|||Pyruvate kinase barrel ^@ http://togogenome.org/gene/10090:Fam187a ^@ http://purl.uniprot.org/uniprot/Q9D3R5 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||Ig-like V-type domain-containing protein FAM187A|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000340655 http://togogenome.org/gene/10090:Tmem205 ^@ http://purl.uniprot.org/uniprot/Q91XE8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 205 ^@ http://purl.uniprot.org/annotation/PRO_0000317502 http://togogenome.org/gene/10090:Or4k45 ^@ http://purl.uniprot.org/uniprot/Q8VF48 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cyp3a16 ^@ http://purl.uniprot.org/uniprot/Q2KHL4|||http://purl.uniprot.org/uniprot/Q64481 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Cytochrome P450 3A16|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051799 http://togogenome.org/gene/10090:Skida1 ^@ http://purl.uniprot.org/uniprot/G3X9M2|||http://purl.uniprot.org/uniprot/Q80YR3 ^@ 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|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||SKI/DACH domain-containing protein 1|||SKI/SNO/DAC ^@ http://purl.uniprot.org/annotation/PRO_0000328530 http://togogenome.org/gene/10090:Hpgd ^@ http://purl.uniprot.org/uniprot/Q8VCC1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ 15-hydroxyprostaglandin dehydrogenase [NAD(+)]|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000253626 http://togogenome.org/gene/10090:Bclaf1 ^@ http://purl.uniprot.org/uniprot/A0A087WQA0|||http://purl.uniprot.org/uniprot/F8WI22|||http://purl.uniprot.org/uniprot/Q8K019 ^@ 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|||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.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064889|||http://purl.uniprot.org/annotation/VSP_010372|||http://purl.uniprot.org/annotation/VSP_010373|||http://purl.uniprot.org/annotation/VSP_010374 http://togogenome.org/gene/10090:Gm11437 ^@ http://purl.uniprot.org/uniprot/Q5QR91 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Uncharacterized protein C17orf78 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000300631 http://togogenome.org/gene/10090:Syt14 ^@ http://purl.uniprot.org/uniprot/A0A1L1SVE7|||http://purl.uniprot.org/uniprot/B7ZP31|||http://purl.uniprot.org/uniprot/Q7TN84|||http://purl.uniprot.org/uniprot/Q8BL96 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||C2|||C2 1|||C2 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||Polar residues|||Synaptotagmin-14 ^@ http://purl.uniprot.org/annotation/PRO_0000183979 http://togogenome.org/gene/10090:Ptpn6 ^@ http://purl.uniprot.org/uniprot/P29351|||http://purl.uniprot.org/uniprot/Q3UB72|||http://purl.uniprot.org/uniprot/Q3UCJ0 ^@ 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 binding to phosphorylated Lilrb4a.|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In motheaten (me).|||Mice display a low bone mass density and are associated with osteopenia and elevated inflammatory cytokines.|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by LYN|||SH2|||SH2 1|||SH2 2|||Slight reduction in binding to phosphorylated Lilrb4a.|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 6 ^@ http://purl.uniprot.org/annotation/PRO_0000094759|||http://purl.uniprot.org/annotation/VSP_005131|||http://purl.uniprot.org/annotation/VSP_005132|||http://purl.uniprot.org/annotation/VSP_005133 http://togogenome.org/gene/10090:Slco1a1 ^@ http://purl.uniprot.org/uniprot/Q53ZW9|||http://purl.uniprot.org/uniprot/Q9QXZ6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Essential for pH-sensitivity of estrone 3-sulfate 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|||Kazal-like|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier organic anion transporter family member 1A1 ^@ http://purl.uniprot.org/annotation/PRO_0000191040 http://togogenome.org/gene/10090:Tmem252 ^@ http://purl.uniprot.org/uniprot/Q8C353 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 252 ^@ http://purl.uniprot.org/annotation/PRO_0000089708 http://togogenome.org/gene/10090:Rdh10 ^@ http://purl.uniprot.org/uniprot/Q8VCH7 ^@ 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_0000307683 http://togogenome.org/gene/10090:Wdr6 ^@ http://purl.uniprot.org/uniprot/Q99ME2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ N-acetylmethionine|||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_0000393460 http://togogenome.org/gene/10090:Fdx1 ^@ http://purl.uniprot.org/uniprot/A0A1L1STP5|||http://purl.uniprot.org/uniprot/P46656|||http://purl.uniprot.org/uniprot/Q3UG56|||http://purl.uniprot.org/uniprot/Q545P3 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ 2Fe-2S ferredoxin-type|||Adrenodoxin, mitochondrial|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000000989 http://togogenome.org/gene/10090:Kcna4 ^@ http://purl.uniprot.org/uniprot/Q61423 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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|||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_0000053982 http://togogenome.org/gene/10090:Tollip ^@ http://purl.uniprot.org/uniprot/F7AT44|||http://purl.uniprot.org/uniprot/Q9QZ06 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif ^@ AIM1|||AIM2|||C2|||CUE|||N-acetylalanine|||Phosphoserine|||Removed|||Toll-interacting protein ^@ http://purl.uniprot.org/annotation/PRO_0000072626 http://togogenome.org/gene/10090:Pigb ^@ http://purl.uniprot.org/uniprot/Q9JJQ0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Disordered|||GPI mannosyltransferase 3|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000246252 http://togogenome.org/gene/10090:Rxylt1 ^@ http://purl.uniprot.org/uniprot/Q8VDX6 ^@ 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; Signal-anchor for type II membrane protein|||Ribitol-5-phosphate xylosyltransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072588 http://togogenome.org/gene/10090:Or5p57 ^@ http://purl.uniprot.org/uniprot/Q8VEZ0 ^@ 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 5p57 ^@ http://purl.uniprot.org/annotation/PRO_0000150838 http://togogenome.org/gene/10090:Zbtb4 ^@ http://purl.uniprot.org/uniprot/Q5F293 ^@ 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 ^@ Acidic residues|||BTB|||Basic and acidic residues|||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)|||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_0000434408 http://togogenome.org/gene/10090:Obp1b ^@ http://purl.uniprot.org/uniprot/A2AEP0 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Odorant-binding protein 1b ^@ http://purl.uniprot.org/annotation/PRO_5002642467 http://togogenome.org/gene/10090:Gadd45b ^@ http://purl.uniprot.org/uniprot/P22339 ^@ Chain|||Molecule Processing ^@ Chain ^@ Growth arrest and DNA damage-inducible protein GADD45 beta ^@ http://purl.uniprot.org/annotation/PRO_0000148335 http://togogenome.org/gene/10090:Cldn17 ^@ http://purl.uniprot.org/uniprot/Q8BXA6 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Claudin-17|||Cytoplasmic|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000144778 http://togogenome.org/gene/10090:Cldn15 ^@ http://purl.uniprot.org/uniprot/Q9Z0S5 ^@ Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes formation of tight-junction strand-like structures.|||Abolishes palmitoylation; when associated with 183-A--A-185.|||Abolishes palmitoylation; when associated with A-102.|||Claudin-15|||Cytoplasmic|||Extracellular|||Helical|||Important for Na(+)-selective paracellular ion transport|||Important for the formation of tight-junction strand-like structures|||No effect on formation of tight-junction strand-like structures.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000144772 http://togogenome.org/gene/10090:Mcmdc2 ^@ http://purl.uniprot.org/uniprot/E9Q956 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Splice Variant ^@ In isoform 2.|||MCM|||Minichromosome maintenance domain-containing protein 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000415824|||http://purl.uniprot.org/annotation/VSP_042394|||http://purl.uniprot.org/annotation/VSP_042395|||http://purl.uniprot.org/annotation/VSP_042396 http://togogenome.org/gene/10090:Bloc1s5 ^@ http://purl.uniprot.org/uniprot/Q8R015 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant ^@ Biogenesis of lysosome-related organelles complex 1 subunit 5|||Disordered|||In isoform 2.|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000096653|||http://purl.uniprot.org/annotation/VSP_008196 http://togogenome.org/gene/10090:Adtrp ^@ http://purl.uniprot.org/uniprot/A0A0R4J0W3|||http://purl.uniprot.org/uniprot/Q8C138 ^@ Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Site|||Topological Domain|||Transmembrane ^@ Androgen-dependent TFPI-regulating protein|||Cytoplasmic|||Extracellular|||Helical|||Important for catalytic activity ^@ http://purl.uniprot.org/annotation/PRO_0000190102 http://togogenome.org/gene/10090:Slc39a12 ^@ http://purl.uniprot.org/uniprot/Q5FWH7 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||XEXPHE-motif|||Zinc transporter ZIP12 ^@ http://purl.uniprot.org/annotation/PRO_0000312499|||http://purl.uniprot.org/annotation/VSP_029851 http://togogenome.org/gene/10090:Ift25 ^@ http://purl.uniprot.org/uniprot/Q8VDG4|||http://purl.uniprot.org/uniprot/Q9D6H2 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Intraflagellar transport protein 25 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000058532 http://togogenome.org/gene/10090:Msx2 ^@ http://purl.uniprot.org/uniprot/Q03358|||http://purl.uniprot.org/uniprot/Q3UZH5 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Homeobox|||Homeobox protein MSX-2 ^@ http://purl.uniprot.org/annotation/PRO_0000049100 http://togogenome.org/gene/10090:Gsdma ^@ http://purl.uniprot.org/uniprot/Q9EST1 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Mutagenesis Site|||Region|||Site|||Transmembrane ^@ (Microbial infection) Cleavage; by bacterial effector protein SpeB|||Abolished cleavage by bacterial effector protein SpeB, preventing pyroptosis.|||Beta stranded|||Gasdermin-A|||Gasdermin-A, C-terminal|||Gasdermin-A, N-terminal|||Triggers pyroptosis ^@ http://purl.uniprot.org/annotation/PRO_0000148174|||http://purl.uniprot.org/annotation/PRO_0000451666|||http://purl.uniprot.org/annotation/PRO_0000451667 http://togogenome.org/gene/10090:Dtx1 ^@ http://purl.uniprot.org/uniprot/Q61010 ^@ 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 ^@ Disordered|||E3 ubiquitin-protein ligase DTX1|||In isoform 2.|||In isoform 3.|||Polar residues|||Pro residues|||RING-type|||SH3-binding|||WWE 1|||WWE 2 ^@ http://purl.uniprot.org/annotation/PRO_0000219081|||http://purl.uniprot.org/annotation/VSP_008348|||http://purl.uniprot.org/annotation/VSP_008349 http://togogenome.org/gene/10090:Pcdh18 ^@ http://purl.uniprot.org/uniprot/Q8VHR0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||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|||Interaction with DAB1|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin 18 ^@ http://purl.uniprot.org/annotation/PRO_5000061325 http://togogenome.org/gene/10090:Lbhd2 ^@ http://purl.uniprot.org/uniprot/G3UW55 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||LBH ^@ http://togogenome.org/gene/10090:Tmcc1 ^@ http://purl.uniprot.org/uniprot/A0A0N4SWB9|||http://purl.uniprot.org/uniprot/Q69ZZ6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Transmembrane and coiled-coil domains protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000184596|||http://purl.uniprot.org/annotation/VSP_019589|||http://purl.uniprot.org/annotation/VSP_019590|||http://purl.uniprot.org/annotation/VSP_019591 http://togogenome.org/gene/10090:Or10j27 ^@ http://purl.uniprot.org/uniprot/Q8VG32 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ttc6 ^@ http://purl.uniprot.org/uniprot/G3UYY4 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||TPR ^@ http://togogenome.org/gene/10090:Sema3g ^@ http://purl.uniprot.org/uniprot/Q4LFA9 ^@ 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 ^@ Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3G ^@ http://purl.uniprot.org/annotation/PRO_0000257792 http://togogenome.org/gene/10090:B9d1 ^@ http://purl.uniprot.org/uniprot/Q9R1S0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ B9 domain-containing protein 1|||C2 B9-type ^@ http://purl.uniprot.org/annotation/PRO_0000307668 http://togogenome.org/gene/10090:Glod4 ^@ http://purl.uniprot.org/uniprot/Q9CPV4 ^@ 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 ^@ Glyoxalase domain-containing protein 4|||In isoform 2.|||In isoform 3.|||N6-succinyllysine|||Phosphoserine|||VOC 1|||VOC 2 ^@ http://purl.uniprot.org/annotation/PRO_0000280392|||http://purl.uniprot.org/annotation/VSP_023649|||http://purl.uniprot.org/annotation/VSP_023650|||http://purl.uniprot.org/annotation/VSP_023651 http://togogenome.org/gene/10090:Ubqln4 ^@ http://purl.uniprot.org/uniprot/Q99NB8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Turn ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||STI1 1|||STI1 2|||STI1 3|||STI1 4|||UBA|||Ubiquilin-4|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000211016 http://togogenome.org/gene/10090:Arg2 ^@ http://purl.uniprot.org/uniprot/O08691 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Mutagenesis Site|||Transit Peptide ^@ Arginase-2, mitochondrial|||Catalytically inactive; defective in promoting NOS3/eNOS-uncoupling in endothelial cells.|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000002085 http://togogenome.org/gene/10090:Spp2 ^@ http://purl.uniprot.org/uniprot/Q8K1I3 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Phosphoserine|||Secreted phosphoprotein 24 ^@ http://purl.uniprot.org/annotation/PRO_0000022404 http://togogenome.org/gene/10090:Snx13 ^@ http://purl.uniprot.org/uniprot/E9QNG6|||http://purl.uniprot.org/uniprot/Q6PHS6|||http://purl.uniprot.org/uniprot/Q80TT7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Transmembrane ^@ Helical|||PX|||PXA|||RGS|||Sorting nexin-13 ^@ http://purl.uniprot.org/annotation/PRO_0000236200 http://togogenome.org/gene/10090:Cd55b ^@ http://purl.uniprot.org/uniprot/E9Q731|||http://purl.uniprot.org/uniprot/E9QAP4|||http://purl.uniprot.org/uniprot/Q61476 ^@ 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 ^@ Complement decay-accelerating factor transmembrane isoform|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4 ^@ http://purl.uniprot.org/annotation/PRO_0000006006|||http://purl.uniprot.org/annotation/PRO_5003243145|||http://purl.uniprot.org/annotation/PRO_5003244473 http://togogenome.org/gene/10090:Mlh3 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VMP7|||http://purl.uniprot.org/uniprot/Q3V1X3|||http://purl.uniprot.org/uniprot/Q68FG1|||http://purl.uniprot.org/uniprot/Q8BZC3 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ DNA mismatch repair protein S5|||Disordered|||MutL C-terminal dimerisation|||Polar residues ^@ http://togogenome.org/gene/10090:Tonsl ^@ http://purl.uniprot.org/uniprot/G3UW83|||http://purl.uniprot.org/uniprot/Q6NZL6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||Acidic residues|||Basic and acidic residues|||Disordered|||Homozygous mice are not viable. Embryos show early lethality along with fetal growth restriction and lack of visible blood vessels in yolk sacs.|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Omega-N-methylarginine|||Polar residues|||Pro 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_0000326635 http://togogenome.org/gene/10090:Sp140 ^@ http://purl.uniprot.org/uniprot/Q6NSQ5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic residues|||Bromo|||Disordered|||HSR|||PHD-type|||Polar residues|||SAND ^@ http://togogenome.org/gene/10090:Pold2 ^@ http://purl.uniprot.org/uniprot/O35654 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ DNA polymerase delta subunit 2|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000096167 http://togogenome.org/gene/10090:Klhl24 ^@ http://purl.uniprot.org/uniprot/Q8BRG6 ^@ 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 24 ^@ http://purl.uniprot.org/annotation/PRO_0000261595 http://togogenome.org/gene/10090:Or5ar1 ^@ http://purl.uniprot.org/uniprot/Q149M3|||http://purl.uniprot.org/uniprot/Q8VGS3 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreased receptor activity in response to MTMT binding, even in the presence of copper.|||Extracellular|||G-protein coupled receptors family 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 receptor activity in response to MTMT binding, even in the presence of copper.|||Olfactory receptor 5AR1 ^@ http://purl.uniprot.org/annotation/PRO_0000150860 http://togogenome.org/gene/10090:Derl3 ^@ http://purl.uniprot.org/uniprot/Q14C34|||http://purl.uniprot.org/uniprot/Q9D8K3 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Derlin-3|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In isoform 2.|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000219049|||http://purl.uniprot.org/annotation/VSP_011090 http://togogenome.org/gene/10090:Fa2h ^@ http://purl.uniprot.org/uniprot/Q5MPP0 ^@ 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 ^@ Cytochrome b5 heme-binding|||Fatty acid 2-hydroxylase|||Fatty acid hydroxylase|||Helical|||In isoform 2.|||In isoform 3.|||In strain: C57BL/6J.|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000312351|||http://purl.uniprot.org/annotation/VSP_029837|||http://purl.uniprot.org/annotation/VSP_029838 http://togogenome.org/gene/10090:Enox1 ^@ http://purl.uniprot.org/uniprot/Q8BHR2 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Splice Variant ^@ Ecto-NOX disulfide-thiol exchanger 1|||In isoform 2.|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000295901|||http://purl.uniprot.org/annotation/VSP_027122 http://togogenome.org/gene/10090:Lrrc28 ^@ http://purl.uniprot.org/uniprot/Q3TX51 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ 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_0000272299 http://togogenome.org/gene/10090:Tescl ^@ http://purl.uniprot.org/uniprot/Q9DAJ7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ EF-hand ^@ http://togogenome.org/gene/10090:Btbd35f20 ^@ http://purl.uniprot.org/uniprot/A2CG71 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Rbm20 ^@ http://purl.uniprot.org/uniprot/Q3UQS8 ^@ 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|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Abolished localization to the nucleus, leading to impaired ability to regulate alternative splicing of Ttn (Titin) mRNAs.|||Basic and acidic residues|||Decreased localization to the nucleus, leading to impaired ability to regulate alternative splicing of Ttn (Titin) mRNAs.|||Disordered|||Does not affect pre-mRNA-binding.|||Impaired ability to regulate alternative splicing of Ttn (Titin) mRNAs.|||In isoform 2.|||Knockin mice show severe cardiac phenotypes, characterized by dilated cardiomyopathy and atrial fibrillation. Decreased localization to the nucleus, leading to impaired ability to regulate alternative splicing of Ttn (Titin) mRNAs.|||Knockin mice show severe cardiac phenotypes, characterized by dilated cardiomyopathy, leading to premature death. Decreased localization to the nucleus associated with an increased localization to cytoplasmic ribonucleoprotein granules.|||Matrin-type|||Phosphoserine|||Polar residues|||Pro residues|||RNA-binding protein 20|||RRM|||RS|||Slightly reduced pre-mRNA-binding.|||Strongly reduced pre-mRNA-binding.|||U1-type ^@ http://purl.uniprot.org/annotation/PRO_0000328825|||http://purl.uniprot.org/annotation/VSP_044393 http://togogenome.org/gene/10090:Panx1 ^@ http://purl.uniprot.org/uniprot/Q9JIP4 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Abolishes S-nitrosylation; when associated with Ala-346.|||Abolishes S-nitrosylation; when associated with Ala-40.|||Cytoplasmic|||Extracellular|||Helical|||Impairs glycosylation.|||N-linked (GlcNAc...) asparagine|||No effect on S-nitrosylation.|||Pannexin-1|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000208485 http://togogenome.org/gene/10090:Olfm2 ^@ http://purl.uniprot.org/uniprot/Q8BM13 ^@ 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 ^@ N-linked (GlcNAc...) asparagine|||Noelin-2|||Olfactomedin-like ^@ http://purl.uniprot.org/annotation/PRO_0000020079 http://togogenome.org/gene/10090:Fastkd1 ^@ http://purl.uniprot.org/uniprot/Q6DI86 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ FAST kinase domain-containing protein 1, mitochondrial|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||N6-acetyllysine|||RAP ^@ http://purl.uniprot.org/annotation/PRO_0000284711|||http://purl.uniprot.org/annotation/VSP_024618|||http://purl.uniprot.org/annotation/VSP_024619|||http://purl.uniprot.org/annotation/VSP_024620|||http://purl.uniprot.org/annotation/VSP_024621 http://togogenome.org/gene/10090:Itgad ^@ http://purl.uniprot.org/uniprot/E9PXZ7|||http://purl.uniprot.org/uniprot/H3BKX8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Disordered|||FG-GAP|||Helical|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5001424274|||http://purl.uniprot.org/annotation/PRO_5001424946 http://togogenome.org/gene/10090:Akirin1 ^@ http://purl.uniprot.org/uniprot/Q99LF1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region ^@ Akirin-1|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Pro residues|||SYVS motif ^@ http://purl.uniprot.org/annotation/PRO_0000274319 http://togogenome.org/gene/10090:Vmn1r212 ^@ http://purl.uniprot.org/uniprot/Q8R268 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Etv4 ^@ http://purl.uniprot.org/uniprot/A2A5C2|||http://purl.uniprot.org/uniprot/A2A5C3|||http://purl.uniprot.org/uniprot/A6MDC6|||http://purl.uniprot.org/uniprot/P28322 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ 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.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204117|||http://purl.uniprot.org/annotation/VSP_047943|||http://purl.uniprot.org/annotation/VSP_047944|||http://purl.uniprot.org/annotation/VSP_047945 http://togogenome.org/gene/10090:Cd209a ^@ http://purl.uniprot.org/uniprot/Q91ZX1 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-type lectin|||CD209 antigen-like protein A|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046604|||http://purl.uniprot.org/annotation/VSP_010067 http://togogenome.org/gene/10090:Gabra6 ^@ http://purl.uniprot.org/uniprot/P16305 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit alpha-6|||Helical|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000000448|||http://purl.uniprot.org/annotation/VSP_000085|||http://purl.uniprot.org/annotation/VSP_000086 http://togogenome.org/gene/10090:Cfi ^@ http://purl.uniprot.org/uniprot/Q61129 ^@ 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|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Complement factor I|||Complement factor I heavy chain|||Complement factor I light chain|||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...) asparagine|||Peptidase S1|||SRCR ^@ http://purl.uniprot.org/annotation/PRO_0000027571|||http://purl.uniprot.org/annotation/PRO_0000027572|||http://purl.uniprot.org/annotation/PRO_0000027573 http://togogenome.org/gene/10090:Mtmr14 ^@ http://purl.uniprot.org/uniprot/Q8VEL2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region ^@ Disordered|||Myotubularin-related protein 14|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000260215 http://togogenome.org/gene/10090:Ankrd53 ^@ http://purl.uniprot.org/uniprot/Q3V0J4|||http://purl.uniprot.org/uniprot/Q9CUG5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat domain-containing protein 53|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000320070 http://togogenome.org/gene/10090:Picalm ^@ http://purl.uniprot.org/uniprot/Q3TD51|||http://purl.uniprot.org/uniprot/Q570Z8|||http://purl.uniprot.org/uniprot/Q7M6Y3 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||ENTH|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 6.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2, isoform 3 and isoform 5.|||Interaction with PIMREG|||N-acetylserine|||Phosphatidylinositol-binding clathrin assembly protein|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000187063|||http://purl.uniprot.org/annotation/VSP_050684|||http://purl.uniprot.org/annotation/VSP_050685|||http://purl.uniprot.org/annotation/VSP_050686 http://togogenome.org/gene/10090:Or10h28 ^@ http://purl.uniprot.org/uniprot/A0PK62|||http://purl.uniprot.org/uniprot/Q8VBW9 ^@ 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 10H28 ^@ http://purl.uniprot.org/annotation/PRO_0000150815 http://togogenome.org/gene/10090:Map3k7 ^@ http://purl.uniprot.org/uniprot/Q543B5|||http://purl.uniprot.org/uniprot/Q62073|||http://purl.uniprot.org/uniprot/Q923A8 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolishes ubiquitination. Abolishes ubiquitination and induction of phosphorylation; when associated with R-209.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with MAPK8IP1|||Mitogen-activated protein kinase kinase kinase 7|||No effect on ubiquitination. No effect on induction of phosphorylation; when associated with R-34.|||No effect on ubiquitination. No effect on induction of phosphorylation; when associated with R-562.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Strongly decreases ubiquitination. Abolishes ubiquitination and induction of phosphorylation; when associated with R-158. ^@ http://purl.uniprot.org/annotation/PRO_0000086253 http://togogenome.org/gene/10090:Or4a74 ^@ http://purl.uniprot.org/uniprot/A2AT78 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Urb2 ^@ http://purl.uniprot.org/uniprot/E9Q7L1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Nucleolar 27S pre-rRNA processing Urb2/Npa2 C-terminal ^@ http://togogenome.org/gene/10090:Chmp2a ^@ http://purl.uniprot.org/uniprot/Q9DB34 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Motif|||Region ^@ Charged multivesicular body protein 2a|||Disordered|||Interaction with VPS4B|||Interaction with VTA1|||MIT-interacting motif|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000211463 http://togogenome.org/gene/10090:1700019N19Rik ^@ http://purl.uniprot.org/uniprot/A0A0R4J076|||http://purl.uniprot.org/uniprot/Q9CQT6 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Sperm-associated microtubule inner protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000358916 http://togogenome.org/gene/10090:Zfp638 ^@ http://purl.uniprot.org/uniprot/A0A0N4SV80|||http://purl.uniprot.org/uniprot/E9QML5|||http://purl.uniprot.org/uniprot/Q61464 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||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 5.|||In isoform 6.|||Involved in localization to nuclear speckles|||Matrin-type|||Phosphoserine|||Polar residues|||Pro residues|||RRM|||RRM 1|||RRM 2|||Zinc finger protein 638 ^@ http://purl.uniprot.org/annotation/PRO_0000082012|||http://purl.uniprot.org/annotation/VSP_014807|||http://purl.uniprot.org/annotation/VSP_014808|||http://purl.uniprot.org/annotation/VSP_014809|||http://purl.uniprot.org/annotation/VSP_014810|||http://purl.uniprot.org/annotation/VSP_014811|||http://purl.uniprot.org/annotation/VSP_014812|||http://purl.uniprot.org/annotation/VSP_014813|||http://purl.uniprot.org/annotation/VSP_014814 http://togogenome.org/gene/10090:Dhx40 ^@ http://purl.uniprot.org/uniprot/Q6PE54 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Probable ATP-dependent RNA helicase DHX40 ^@ http://purl.uniprot.org/annotation/PRO_0000252396 http://togogenome.org/gene/10090:Scnn1g ^@ http://purl.uniprot.org/uniprot/Q9WU39 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Amiloride-sensitive sodium channel subunit gamma|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000181277 http://togogenome.org/gene/10090:Vmn1r135 ^@ http://purl.uniprot.org/uniprot/K9J7G0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gnpda2 ^@ http://purl.uniprot.org/uniprot/Q9CRC9 ^@ Active Site|||Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ For ring-opening step|||Glucosamine-6-phosphate isomerase 2|||In isoform 2.|||Phosphothreonine|||Proton acceptor; for enolization step|||Proton acceptor; for ring-opening step ^@ http://purl.uniprot.org/annotation/PRO_0000343206|||http://purl.uniprot.org/annotation/VSP_034581 http://togogenome.org/gene/10090:Dbn1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1E3|||http://purl.uniprot.org/uniprot/Q3TRK3|||http://purl.uniprot.org/uniprot/Q9QXS6 ^@ 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 ^@ ADF-H|||Basic and acidic residues|||Disordered|||Drebrin|||In isoform A2.|||In isoform E2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000080009|||http://purl.uniprot.org/annotation/VSP_004198|||http://purl.uniprot.org/annotation/VSP_004199|||http://purl.uniprot.org/annotation/VSP_004200 http://togogenome.org/gene/10090:H3c3 ^@ http://purl.uniprot.org/uniprot/B9EI85|||http://purl.uniprot.org/uniprot/P84228 ^@ Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||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 H2A/H2B/H3|||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; 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_0000221250 http://togogenome.org/gene/10090:Itgb5 ^@ http://purl.uniprot.org/uniprot/G5E8F8|||http://purl.uniprot.org/uniprot/O70309|||http://purl.uniprot.org/uniprot/Q6PE70 ^@ Binding Site|||Chain|||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 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||In isoform Beta-5B.|||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_0000016349|||http://purl.uniprot.org/annotation/PRO_5015091933|||http://purl.uniprot.org/annotation/PRO_5015098432|||http://purl.uniprot.org/annotation/VSP_002752 http://togogenome.org/gene/10090:Ankrd49 ^@ http://purl.uniprot.org/uniprot/Q8VE42 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 49|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000244586 http://togogenome.org/gene/10090:Mthfs ^@ http://purl.uniprot.org/uniprot/Q9D110 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ 5-formyltetrahydrofolate cyclo-ligase|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000200276 http://togogenome.org/gene/10090:Grin1 ^@ http://purl.uniprot.org/uniprot/A2AI16|||http://purl.uniprot.org/uniprot/P35438 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||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|||INTRAMEM|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Glutamate receptor|||Glutamate receptor ionotropic, NMDA 1|||Helical|||In isoform 2.|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKC|||Pore-forming ^@ http://purl.uniprot.org/annotation/PRO_0000011588|||http://purl.uniprot.org/annotation/PRO_5027165666|||http://purl.uniprot.org/annotation/VSP_014222|||http://purl.uniprot.org/annotation/VSP_014223 http://togogenome.org/gene/10090:Shisa9 ^@ http://purl.uniprot.org/uniprot/E9QN38|||http://purl.uniprot.org/uniprot/Q9CZN4 ^@ 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 and isoform 4.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein shisa-9 ^@ http://purl.uniprot.org/annotation/PRO_0000394254|||http://purl.uniprot.org/annotation/PRO_5003246423|||http://purl.uniprot.org/annotation/VSP_039229|||http://purl.uniprot.org/annotation/VSP_039230|||http://purl.uniprot.org/annotation/VSP_039231|||http://purl.uniprot.org/annotation/VSP_039232 http://togogenome.org/gene/10090:Dck ^@ http://purl.uniprot.org/uniprot/P43346|||http://purl.uniprot.org/uniprot/Q545E8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Deoxycytidine kinase|||Deoxynucleoside kinase|||Phosphoserine|||Phosphoserine; by CK1|||Phosphothreonine; by CK1|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000175091 http://togogenome.org/gene/10090:St6galnac4 ^@ http://purl.uniprot.org/uniprot/Q9R2B6 ^@ 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 ^@ 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|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149279|||http://purl.uniprot.org/annotation/VSP_001787|||http://purl.uniprot.org/annotation/VSP_001788 http://togogenome.org/gene/10090:Ubiad1 ^@ http://purl.uniprot.org/uniprot/Q9DC60 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||N-acetylalanine|||Removed|||UbiA prenyltransferase domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000242628 http://togogenome.org/gene/10090:Prss34 ^@ http://purl.uniprot.org/uniprot/Q80UR4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015098924 http://togogenome.org/gene/10090:Il17b ^@ http://purl.uniprot.org/uniprot/Q9QXT6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Interleukin-17B|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015428 http://togogenome.org/gene/10090:Fam136a ^@ http://purl.uniprot.org/uniprot/Q9CR98 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||Phosphothreonine|||Protein FAM136A|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000296951 http://togogenome.org/gene/10090:Pon3 ^@ http://purl.uniprot.org/uniprot/Q62087 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Not cleaved|||Phosphoserine|||Proton acceptor|||Serum paraoxonase/lactonase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000223291 http://togogenome.org/gene/10090:Mc2r ^@ http://purl.uniprot.org/uniprot/Q544P9|||http://purl.uniprot.org/uniprot/Q64326 ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Topological Domain|||Transmembrane ^@ Adrenocorticotropic hormone 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_0000069056 http://togogenome.org/gene/10090:Ppp1r3g ^@ http://purl.uniprot.org/uniprot/Q9CW07 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ CBM21|||Disordered|||Phosphoserine|||Polar residues|||Protein phosphatase 1 regulatory subunit 3G ^@ http://purl.uniprot.org/annotation/PRO_0000394966 http://togogenome.org/gene/10090:Or5k3 ^@ http://purl.uniprot.org/uniprot/Q8VGQ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fbxo2 ^@ http://purl.uniprot.org/uniprot/Q3USR5|||http://purl.uniprot.org/uniprot/Q80UW2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn ^@ Abolishes binding of glycoprotein targets.|||Abolishes binding of glycoprotein targets. Strongly reduced ubiquitination of glycoprotein targets.|||Acidic residues|||Basic and acidic residues|||Disordered|||F-box|||F-box only protein 2|||FBA|||Important for carbohydrate binding|||No effect on carbohydrate binding.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000119876 http://togogenome.org/gene/10090:Rcan3 ^@ http://purl.uniprot.org/uniprot/Q9JKK0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Calcineurin-binding|||Calcipressin-3|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000211421 http://togogenome.org/gene/10090:Nup210 ^@ http://purl.uniprot.org/uniprot/Q8BPS7|||http://purl.uniprot.org/uniprot/Q9QY81 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ BIG2|||Cytoplasmic|||Helical|||N-linked (GlcNAc...) asparagine|||Nuclear pore membrane glycoprotein 210|||Perinuclear space|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000236047|||http://purl.uniprot.org/annotation/PRO_5004303797 http://togogenome.org/gene/10090:Ncor2 ^@ http://purl.uniprot.org/uniprot/E9PY55|||http://purl.uniprot.org/uniprot/E9Q9V3|||http://purl.uniprot.org/uniprot/F8VQL9|||http://purl.uniprot.org/uniprot/Q80ZV7|||http://purl.uniprot.org/uniprot/Q9WU42 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||CORNR box of ID1|||CORNR box of ID2|||Disordered|||HTH myb-type|||In isoform Beta.|||Interaction with SIN3A/B|||Myb-like|||N6-acetyllysine|||Nuclear receptor corepressor 2|||Omega-N-methylarginine|||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_0000055623|||http://purl.uniprot.org/annotation/VSP_003414 http://togogenome.org/gene/10090:Or7e175 ^@ http://purl.uniprot.org/uniprot/A0A2I3BRV7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp867 ^@ http://purl.uniprot.org/uniprot/E9Q2M4|||http://purl.uniprot.org/uniprot/Q3V232 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Aatf ^@ http://purl.uniprot.org/uniprot/Q9JKX4 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Binds POLR2J|||Binds RB1|||Binds RB1 and SP1|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Protein AATF|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056617|||http://purl.uniprot.org/annotation/VSP_014897|||http://purl.uniprot.org/annotation/VSP_014898|||http://purl.uniprot.org/annotation/VSP_014899|||http://purl.uniprot.org/annotation/VSP_014900 http://togogenome.org/gene/10090:Ang4 ^@ http://purl.uniprot.org/uniprot/Q3TMQ6|||http://purl.uniprot.org/uniprot/W0UUX7 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Angiogenin-4|||Loss of angiogenic activity. Increased ribonuclease activity.|||Loss of angiogenic activity. No effect on ribonuclease activity.|||Loss of ribonuclease activity. Loss of angiogenic activity.|||Nucleolar localization signal|||Proton acceptor|||Proton donor|||Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_0000415440|||http://purl.uniprot.org/annotation/PRO_5007751481 http://togogenome.org/gene/10090:Vmn1r33 ^@ http://purl.uniprot.org/uniprot/Q8R2E0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nubp1 ^@ http://purl.uniprot.org/uniprot/Q9R060 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Cytosolic Fe-S cluster assembly factor NUBP1|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000184944 http://togogenome.org/gene/10090:Slc10a2 ^@ http://purl.uniprot.org/uniprot/P70172|||http://purl.uniprot.org/uniprot/Q0VBB8 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ileal sodium/bile acid cotransporter|||In strain: NZB/BlNJ and C57BL/6.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000052340 http://togogenome.org/gene/10090:Cntnap5a ^@ http://purl.uniprot.org/uniprot/Q0V8T9 ^@ 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 ^@ Contactin-associated protein like 5-1|||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_0000317378 http://togogenome.org/gene/10090:Znhit3 ^@ http://purl.uniprot.org/uniprot/Q9CQK1 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Modified Residue|||Region|||Zinc Finger ^@ Disordered|||HIT-type|||Phosphoserine|||Zinc finger HIT domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000173552 http://togogenome.org/gene/10090:Cstf2t ^@ http://purl.uniprot.org/uniprot/Q8C7E9 ^@ 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; approximate|||1-2; approximate|||1-3; approximate|||1-4; approximate|||1-5; approximate|||1-6|||1-7; approximate|||1-8; approximate|||12 X 5 AA tandem repeats of G-[AT]-G-[MI]-Q|||2-10; approximate|||2-11; approximate|||2-12|||2-1; approximate|||2-2|||2-3; approximate|||2-4|||2-5; approximate|||2-6|||2-7; approximate|||2-8|||2-9; approximate|||8 X 5 AA tandem repeats of M-E-T-R-[AG]|||Basic and acidic residues|||Cleavage stimulation factor subunit 2 tau variant|||Disordered|||Phosphoserine|||Polar residues|||Pro residues|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081535 http://togogenome.org/gene/10090:Gm46608 ^@ http://purl.uniprot.org/uniprot/Q8K4Y1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Stxbp3 ^@ http://purl.uniprot.org/uniprot/Q60770 ^@ 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 ^@ In isoform 2.|||Mediates interaction with DOC2B|||Syntaxin-binding protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000206286|||http://purl.uniprot.org/annotation/VSP_037061|||http://purl.uniprot.org/annotation/VSP_037062 http://togogenome.org/gene/10090:2610008E11Rik ^@ http://purl.uniprot.org/uniprot/G3X964|||http://purl.uniprot.org/uniprot/Q3UFT9 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Or8g32 ^@ http://purl.uniprot.org/uniprot/Q9EQ94 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kif7 ^@ http://purl.uniprot.org/uniprot/E9QMU1|||http://purl.uniprot.org/uniprot/J3QNW9 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Kinesin motor ^@ http://togogenome.org/gene/10090:Imp3 ^@ http://purl.uniprot.org/uniprot/Q921Y2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ S4 RNA-binding|||U3 small nucleolar ribonucleoprotein protein IMP3 ^@ http://purl.uniprot.org/annotation/PRO_0000132710 http://togogenome.org/gene/10090:Adss ^@ http://purl.uniprot.org/uniprot/B9EIE9|||http://purl.uniprot.org/uniprot/P46664 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict ^@ Adenylosuccinate synthetase isozyme 2|||Disordered|||Proton acceptor|||Proton donor|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000095131 http://togogenome.org/gene/10090:Pmaip1 ^@ http://purl.uniprot.org/uniprot/Q9JM54 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure ^@ Chain|||Helix|||Motif|||Mutagenesis Site|||Region ^@ BH3 1|||BH3 2|||Loss of pro-apoptotic activity and of targeting to mitochondria; when associated with A-27.|||Loss of pro-apoptotic activity and of targeting to mitochondria; when associated with A-78.|||Phorbol-12-myristate-13-acetate-induced protein 1|||Required for mitochondrial location ^@ http://purl.uniprot.org/annotation/PRO_0000333230 http://togogenome.org/gene/10090:Ypel4 ^@ http://purl.uniprot.org/uniprot/Q0VEE5|||http://purl.uniprot.org/uniprot/Q65Z93 ^@ 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_0000212393 http://togogenome.org/gene/10090:Fpr-rs3 ^@ http://purl.uniprot.org/uniprot/O88537 ^@ 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|||Formyl peptide receptor-related sequence 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 ^@ http://purl.uniprot.org/annotation/PRO_0000382023 http://togogenome.org/gene/10090:Anxa2 ^@ http://purl.uniprot.org/uniprot/P07356 ^@ Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn ^@ Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Strand|||Turn ^@ Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A2|||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-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphoserine; by PKC|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Removed|||S100A10-binding site ^@ http://purl.uniprot.org/annotation/PRO_0000067471 http://togogenome.org/gene/10090:Amer2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J030|||http://purl.uniprot.org/uniprot/Q8CCJ4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant ^@ APC membrane recruitment protein 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000281886|||http://purl.uniprot.org/annotation/VSP_024090 http://togogenome.org/gene/10090:Lgals2 ^@ http://purl.uniprot.org/uniprot/Q9CQW5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Galectin|||Galectin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000076925 http://togogenome.org/gene/10090:Slc35f1 ^@ http://purl.uniprot.org/uniprot/Q8BGK5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Solute carrier family 35 member F1 ^@ http://purl.uniprot.org/annotation/PRO_0000307308 http://togogenome.org/gene/10090:Idh3b ^@ http://purl.uniprot.org/uniprot/Q91VA7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Isopropylmalate dehydrogenase-like ^@ http://togogenome.org/gene/10090:Smok3b ^@ http://purl.uniprot.org/uniprot/C0HKC8|||http://purl.uniprot.org/uniprot/C0HKC9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Protein kinase|||Proton acceptor|||Sperm motility kinase 3A|||Sperm motility kinase 3B|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000307871|||http://purl.uniprot.org/annotation/PRO_0000439229 http://togogenome.org/gene/10090:Plekhg5 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQC2|||http://purl.uniprot.org/uniprot/A0A2X0SG37|||http://purl.uniprot.org/uniprot/A0A5F8MPI8|||http://purl.uniprot.org/uniprot/Q66T02 ^@ 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 ^@ Acidic residues|||DH|||Disordered|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology domain-containing family G member 5|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000307135|||http://purl.uniprot.org/annotation/VSP_028587 http://togogenome.org/gene/10090:Pi4k2a ^@ http://purl.uniprot.org/uniprot/Q2TBE6 ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region ^@ Activation loop|||Catalytic loop|||Disordered|||G-loop|||Important for interaction with membranes|||Important for substrate binding|||N-acetylmethionine|||PI3K/PI4K catalytic|||Phosphatidylinositol 4-kinase type 2-alpha|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000285159 http://togogenome.org/gene/10090:Gm382 ^@ http://purl.uniprot.org/uniprot/Q3V0S4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||K Homology|||Polar residues ^@ http://togogenome.org/gene/10090:Or51t4 ^@ http://purl.uniprot.org/uniprot/F8VQ18 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Elovl6 ^@ http://purl.uniprot.org/uniprot/Q920L5 ^@ 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_0000282846 http://togogenome.org/gene/10090:Eral1 ^@ http://purl.uniprot.org/uniprot/Q9CZU4|||http://purl.uniprot.org/uniprot/Q9ESC5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Era-type G|||G1|||G2|||G3|||G4|||G5|||GTPase Era, mitochondrial|||KH type-2|||Mitochondrion|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000180082 http://togogenome.org/gene/10090:Ywhah ^@ http://purl.uniprot.org/uniprot/P68510 ^@ Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site|||Turn ^@ 14-3-3 protein eta|||Interaction with phosphoserine on interacting protein|||N-acetylglycine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000058624 http://togogenome.org/gene/10090:Pllp ^@ http://purl.uniprot.org/uniprot/Q9DCU2 ^@ 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_0000156814 http://togogenome.org/gene/10090:Auh ^@ http://purl.uniprot.org/uniprot/A0A0R4J023|||http://purl.uniprot.org/uniprot/E9QMT1|||http://purl.uniprot.org/uniprot/Q9JLZ3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transit Peptide ^@ Disordered|||In isoform 2.|||In isoform 3.|||Methylglutaconyl-CoA hydratase, mitochondrial|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||RNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000007416|||http://purl.uniprot.org/annotation/PRO_5003243343|||http://purl.uniprot.org/annotation/PRO_5006451925|||http://purl.uniprot.org/annotation/VSP_008337|||http://purl.uniprot.org/annotation/VSP_008338|||http://purl.uniprot.org/annotation/VSP_008339|||http://purl.uniprot.org/annotation/VSP_008340 http://togogenome.org/gene/10090:Zfp534 ^@ http://purl.uniprot.org/uniprot/A2A7A1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Gimd1 ^@ http://purl.uniprot.org/uniprot/E9PW74 ^@ 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_0000419200 http://togogenome.org/gene/10090:Rarg ^@ http://purl.uniprot.org/uniprot/P18911 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Hinge|||In isoform 2.|||In isoform 3.|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Omega-N-methylarginine|||Polar residues|||Retinoic acid receptor gamma ^@ http://purl.uniprot.org/annotation/PRO_0000053474|||http://purl.uniprot.org/annotation/VSP_031081|||http://purl.uniprot.org/annotation/VSP_031082 http://togogenome.org/gene/10090:Ubfd1 ^@ http://purl.uniprot.org/uniprot/Q78JW9 ^@ 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|||Ubiquitin domain-containing protein UBFD1|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000283076 http://togogenome.org/gene/10090:Spaca7b ^@ http://purl.uniprot.org/uniprot/Q9DAA5 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099687 http://togogenome.org/gene/10090:Ces1e ^@ http://purl.uniprot.org/uniprot/Q3UN14|||http://purl.uniprot.org/uniprot/Q64176 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Signal Peptide ^@ Acyl-ester intermediate|||Carboxylesterase 1E|||Carboxylesterase type B|||Carboxylic ester hydrolase|||Charge relay system|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000008576|||http://purl.uniprot.org/annotation/PRO_5008452076 http://togogenome.org/gene/10090:Scn1b ^@ http://purl.uniprot.org/uniprot/P97952 ^@ 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|||Helical|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||Sodium channel subunit beta-1 ^@ http://purl.uniprot.org/annotation/PRO_0000014927 http://togogenome.org/gene/10090:Or4a78 ^@ http://purl.uniprot.org/uniprot/Q7TQZ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cybrd1 ^@ http://purl.uniprot.org/uniprot/Q925G2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytochrome b561|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Plasma membrane ascorbate-dependent reductase CYBRD1|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000314831|||http://purl.uniprot.org/annotation/VSP_030396|||http://purl.uniprot.org/annotation/VSP_030397 http://togogenome.org/gene/10090:Gm7876 ^@ http://purl.uniprot.org/uniprot/K7N6V6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Tbx3 ^@ http://purl.uniprot.org/uniprot/P70324|||http://purl.uniprot.org/uniprot/Q3ULL3|||http://purl.uniprot.org/uniprot/Q4VA43 ^@ 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|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||T-box|||T-box transcription factor TBX3|||T-box; first part|||T-box; second part ^@ http://purl.uniprot.org/annotation/PRO_0000184429|||http://purl.uniprot.org/annotation/VSP_013377 http://togogenome.org/gene/10090:Tmsb10 ^@ http://purl.uniprot.org/uniprot/A6H6H4|||http://purl.uniprot.org/uniprot/Q6ZWY8 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Thymosin beta-10 ^@ http://purl.uniprot.org/annotation/PRO_0000045932 http://togogenome.org/gene/10090:Rbbp7 ^@ http://purl.uniprot.org/uniprot/Q60973|||http://purl.uniprot.org/uniprot/Q8C5H3 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat ^@ 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|||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_0000051196 http://togogenome.org/gene/10090:Cyp2w1 ^@ http://purl.uniprot.org/uniprot/E9Q816 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Glycosylation Site|||Signal Peptide ^@ Cytochrome P450 2W1|||N-linked (GlcNAc...) asparagine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000431705 http://togogenome.org/gene/10090:B4galt3 ^@ http://purl.uniprot.org/uniprot/Q3U260|||http://purl.uniprot.org/uniprot/Q91YY2 ^@ 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 ^@ Beta-1,4-galactosyltransferase 3|||Cytoplasmic|||Disordered|||Galactosyltransferase C-terminal|||Galactosyltransferase N-terminal|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000080538 http://togogenome.org/gene/10090:Kcnq2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFQ2|||http://purl.uniprot.org/uniprot/B7ZBV4|||http://purl.uniprot.org/uniprot/B7ZBV5|||http://purl.uniprot.org/uniprot/B7ZBV6|||http://purl.uniprot.org/uniprot/B7ZBV7|||http://purl.uniprot.org/uniprot/B7ZBV8|||http://purl.uniprot.org/uniprot/B7ZBV9|||http://purl.uniprot.org/uniprot/B7ZBW1|||http://purl.uniprot.org/uniprot/B7ZBW2|||http://purl.uniprot.org/uniprot/Q3UY10|||http://purl.uniprot.org/uniprot/Q9Z351 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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 10.|||In isoform 11.|||In isoform 12 and isoform 13.|||In isoform 12.|||In isoform 13.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 12.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 7, isoform 12 and isoform 13.|||In isoform 9.|||Ion transport|||Loss of interaction with calmodulin.|||Loss of interaction with calmodulin; when associated with E-525.|||Loss of interaction with calmodulin; when associated with E-526.|||Mediates interaction with SLC5A3|||Mediates interaction with calmodulin|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium channel voltage dependent KCNQ C-terminal|||Potassium voltage-gated channel subfamily KQT member 2|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054031|||http://purl.uniprot.org/annotation/VSP_000991|||http://purl.uniprot.org/annotation/VSP_000992|||http://purl.uniprot.org/annotation/VSP_000993|||http://purl.uniprot.org/annotation/VSP_000994|||http://purl.uniprot.org/annotation/VSP_000995|||http://purl.uniprot.org/annotation/VSP_000996|||http://purl.uniprot.org/annotation/VSP_000997|||http://purl.uniprot.org/annotation/VSP_000998|||http://purl.uniprot.org/annotation/VSP_000999|||http://purl.uniprot.org/annotation/VSP_001000|||http://purl.uniprot.org/annotation/VSP_001001|||http://purl.uniprot.org/annotation/VSP_001002|||http://purl.uniprot.org/annotation/VSP_001003|||http://purl.uniprot.org/annotation/VSP_001004|||http://purl.uniprot.org/annotation/VSP_001005|||http://purl.uniprot.org/annotation/VSP_001006|||http://purl.uniprot.org/annotation/VSP_012365|||http://purl.uniprot.org/annotation/VSP_012366|||http://purl.uniprot.org/annotation/VSP_022637 http://togogenome.org/gene/10090:Lrrc75a ^@ http://purl.uniprot.org/uniprot/Q7TSF4 ^@ 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 ^@ Disordered|||In isoform 2.|||LRR 1|||LRR 2|||Leucine-rich repeat-containing protein 75A|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000286625|||http://purl.uniprot.org/annotation/VSP_025136 http://togogenome.org/gene/10090:Gm14743 ^@ http://purl.uniprot.org/uniprot/A2BHD2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5002642227 http://togogenome.org/gene/10090:Ric8b ^@ http://purl.uniprot.org/uniprot/Q80XE1 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Splice Variant|||Strand|||Turn ^@ In isoform 1.|||Phosphoserine|||Phosphothreonine|||Synembryn-B ^@ http://purl.uniprot.org/annotation/PRO_0000235900|||http://purl.uniprot.org/annotation/VSP_039867 http://togogenome.org/gene/10090:Angptl7 ^@ http://purl.uniprot.org/uniprot/Q8R1Q3 ^@ 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 7|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009132 http://togogenome.org/gene/10090:Sqor ^@ http://purl.uniprot.org/uniprot/Q9R112 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Cysteine persulfide intermediate|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Sulfide:quinone oxidoreductase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000022409 http://togogenome.org/gene/10090:Thap7 ^@ http://purl.uniprot.org/uniprot/Q8VCZ3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Modified Residue|||Motif|||Region|||Zinc Finger ^@ Disordered|||HCFC1-binding motif (HBM)|||Phosphoserine|||THAP domain-containing protein 7|||THAP-type ^@ http://purl.uniprot.org/annotation/PRO_0000068649 http://togogenome.org/gene/10090:Pradc1 ^@ http://purl.uniprot.org/uniprot/Q14C45|||http://purl.uniprot.org/uniprot/Q9D9N8 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||PA|||Protease-associated domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000022002|||http://purl.uniprot.org/annotation/PRO_5015097033 http://togogenome.org/gene/10090:Scgb2b24 ^@ http://purl.uniprot.org/uniprot/D2XZ39|||http://purl.uniprot.org/uniprot/Q7M747 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Signal Peptide ^@ Chain|||Non-terminal Residue|||Signal Peptide ^@ Secretoglobin family 2B member 24 ^@ http://purl.uniprot.org/annotation/PRO_0000342376|||http://purl.uniprot.org/annotation/PRO_5015088472 http://togogenome.org/gene/10090:Manea ^@ http://purl.uniprot.org/uniprot/Q6NXH2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Catalytic|||Cytoplasmic|||Glycoprotein endo-alpha-1,2-mannosidase|||Helical; Signal-anchor for type II membrane protein|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000282316 http://togogenome.org/gene/10090:Zfp317 ^@ http://purl.uniprot.org/uniprot/Q0P5V5|||http://purl.uniprot.org/uniprot/Q8BLF0|||http://purl.uniprot.org/uniprot/Q8C0Q5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Or6c8 ^@ http://purl.uniprot.org/uniprot/Q8VG33 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Loxl2 ^@ http://purl.uniprot.org/uniprot/P58022 ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 2',4',5'-topaquinone|||Abolishes oxidase activity and secretion but does not affect binding to the CDH1 promoter, repression of CDH1 transcription, interaction with SNAI1, binding to the CDH1 promoter, repression of CDH1 transcription or ability to induce EMT.|||In isoform 2.|||Lysine tyrosylquinone (Lys-Tyr)|||Lysyl oxidase homolog 2|||Lysyl-oxidase like|||N-linked (GlcNAc...) asparagine|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000042854|||http://purl.uniprot.org/annotation/VSP_016231|||http://purl.uniprot.org/annotation/VSP_016232 http://togogenome.org/gene/10090:Tmco6 ^@ http://purl.uniprot.org/uniprot/Q8BQX5 ^@ 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 6 ^@ http://purl.uniprot.org/annotation/PRO_0000305158|||http://purl.uniprot.org/annotation/VSP_059937|||http://purl.uniprot.org/annotation/VSP_059938 http://togogenome.org/gene/10090:Bmp4 ^@ http://purl.uniprot.org/uniprot/P21275|||http://purl.uniprot.org/uniprot/Q3ULR1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic residues|||Bone morphogenetic protein 4|||Disordered|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033858|||http://purl.uniprot.org/annotation/PRO_0000033859|||http://purl.uniprot.org/annotation/PRO_5014309211 http://togogenome.org/gene/10090:Tlcd4 ^@ http://purl.uniprot.org/uniprot/Q8CGF5 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||N6-acetyllysine|||TLC|||TLC domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000286702|||http://purl.uniprot.org/annotation/VSP_025144|||http://purl.uniprot.org/annotation/VSP_025145 http://togogenome.org/gene/10090:Gmfb ^@ http://purl.uniprot.org/uniprot/Q9CQI3 ^@ 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 ^@ ADF-H|||Glia maturation factor beta|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000214944 http://togogenome.org/gene/10090:Grk6 ^@ http://purl.uniprot.org/uniprot/A0A286YDA5|||http://purl.uniprot.org/uniprot/A0A286YDZ5|||http://purl.uniprot.org/uniprot/A0A286YE10|||http://purl.uniprot.org/uniprot/O70293|||http://purl.uniprot.org/uniprot/Q9EP84 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ AGC-kinase C-terminal|||Disordered|||G protein-coupled receptor kinase 6|||In isoform GRK6B.|||N-terminal|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||RGS|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000085975|||http://purl.uniprot.org/annotation/VSP_004939 http://togogenome.org/gene/10090:Dph6 ^@ http://purl.uniprot.org/uniprot/Q9CQ28 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ Diphthine--ammonia ligase|||In isoform 2.|||In isoform 3.|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000282398|||http://purl.uniprot.org/annotation/VSP_024125|||http://purl.uniprot.org/annotation/VSP_024126 http://togogenome.org/gene/10090:Parn ^@ http://purl.uniprot.org/uniprot/A0A0R4J0P6|||http://purl.uniprot.org/uniprot/Q8VDG3 ^@ 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|||Site|||Strand|||Turn ^@ Disordered|||Interaction with poly(A)|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Poly(A)-specific ribonuclease PARN|||R3H ^@ http://purl.uniprot.org/annotation/PRO_0000212852 http://togogenome.org/gene/10090:Rhox4c ^@ http://purl.uniprot.org/uniprot/Q2MDG1 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:4930433I11Rik ^@ http://purl.uniprot.org/uniprot/B2RX47 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF4629|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Nit1 ^@ http://purl.uniprot.org/uniprot/Q8VDK1 ^@ 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 2.|||Mitochondrion|||Nucleophile|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000213252|||http://purl.uniprot.org/annotation/VSP_011548 http://togogenome.org/gene/10090:Mrpl45 ^@ http://purl.uniprot.org/uniprot/Q9D0Q7 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein mL45|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000030564 http://togogenome.org/gene/10090:Oas1f ^@ http://purl.uniprot.org/uniprot/Q14AZ4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ 2'-5'-oligoadenylate synthetase 1 ^@ http://togogenome.org/gene/10090:Abca5 ^@ http://purl.uniprot.org/uniprot/Q8K448 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ ABC transporter 1|||ABC transporter 2|||Cholesterol transporter ABCA5|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000250670 http://togogenome.org/gene/10090:H2ac12 ^@ http://purl.uniprot.org/uniprot/A3KPD0|||http://purl.uniprot.org/uniprot/Q8CGP6 ^@ 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 ^@ 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; 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_0000227504 http://togogenome.org/gene/10090:Srek1ip1 ^@ http://purl.uniprot.org/uniprot/Q4V9W2 ^@ 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|||Basic residues|||CCHC-type|||Disordered|||In isoform 2.|||Phosphoserine|||Protein SREK1IP1 ^@ http://purl.uniprot.org/annotation/PRO_0000311923|||http://purl.uniprot.org/annotation/VSP_029642 http://togogenome.org/gene/10090:Clmn ^@ http://purl.uniprot.org/uniprot/Q8C5W0 ^@ 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 ^@ Acidic residues|||Actin-binding|||Basic and acidic residues|||Calmin|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089855|||http://purl.uniprot.org/annotation/VSP_007766|||http://purl.uniprot.org/annotation/VSP_007767|||http://purl.uniprot.org/annotation/VSP_007768|||http://purl.uniprot.org/annotation/VSP_007769|||http://purl.uniprot.org/annotation/VSP_007770 http://togogenome.org/gene/10090:Sh2d6 ^@ http://purl.uniprot.org/uniprot/A0A3Q4ECA8|||http://purl.uniprot.org/uniprot/E0CYY5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Pro residues|||SH2 ^@ http://togogenome.org/gene/10090:Endod1 ^@ http://purl.uniprot.org/uniprot/Q3UQH3|||http://purl.uniprot.org/uniprot/Q69ZY2|||http://purl.uniprot.org/uniprot/Q8C522 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Disordered|||Endonuclease domain-containing 1 protein|||Extracellular Endonuclease subunit A|||Helical|||N6-acetyllysine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000019925 http://togogenome.org/gene/10090:Itih2 ^@ http://purl.uniprot.org/uniprot/G3X977|||http://purl.uniprot.org/uniprot/Q61703 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ 4-carboxyglutamate|||Aspartate 1-(chondroitin 4-sulfate)-ester|||Inter-alpha-trypsin inhibitor heavy chain H2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||VIT|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000016520|||http://purl.uniprot.org/annotation/PRO_0000016521|||http://purl.uniprot.org/annotation/PRO_0000016522|||http://purl.uniprot.org/annotation/PRO_5015091835 http://togogenome.org/gene/10090:Ccr6 ^@ http://purl.uniprot.org/uniprot/O54689|||http://purl.uniprot.org/uniprot/Q542B6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ C-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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069287 http://togogenome.org/gene/10090:Mgst2 ^@ http://purl.uniprot.org/uniprot/A0A0A6YWX7|||http://purl.uniprot.org/uniprot/A2RST1 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Microsomal glutathione S-transferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000449878 http://togogenome.org/gene/10090:Defb42 ^@ http://purl.uniprot.org/uniprot/Q8BVB5 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 42 ^@ http://purl.uniprot.org/annotation/PRO_0000434510 http://togogenome.org/gene/10090:Or52ab7 ^@ http://purl.uniprot.org/uniprot/Q7TRR2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cep72 ^@ http://purl.uniprot.org/uniprot/Q9D3R3 ^@ 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|||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_0000089500|||http://purl.uniprot.org/annotation/VSP_012748|||http://purl.uniprot.org/annotation/VSP_012749 http://togogenome.org/gene/10090:Farp2 ^@ http://purl.uniprot.org/uniprot/Q91VS8 ^@ 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|||DH|||Disordered|||FERM|||FERM, ARHGEF and pleckstrin domain-containing protein 2|||Increases guanyl-nucleotide exchange factor activity with RAC1; when associated with Q-733.|||Increases guanyl-nucleotide exchange factor activity with RAC1; when associated with R-730.|||PH 1|||PH 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000232756 http://togogenome.org/gene/10090:Tnni1 ^@ http://purl.uniprot.org/uniprot/Q9WUZ5 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ 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_0000186140 http://togogenome.org/gene/10090:Nkx2-1 ^@ http://purl.uniprot.org/uniprot/P50220|||http://purl.uniprot.org/uniprot/Q6PFE0 ^@ Chain|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Homeobox|||Homeobox protein Nkx-2.1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000049344 http://togogenome.org/gene/10090:F5 ^@ http://purl.uniprot.org/uniprot/O88783 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Signal Peptide|||Site ^@ 1 X 17 AA tandem repeats|||1-1|||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|||2-4|||2-5|||2-6|||2-7|||2-8|||2-9|||32 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-T|||Activation peptide (connecting region)|||B|||Basic residues|||Cleavage; by activated protein C|||Cleavage; by thrombin|||Coagulation factor V|||Coagulation factor V heavy chain|||Coagulation factor V light chain|||Disordered|||Does not affect pro-coagulant function. Partially resistant to inactivation by activated protein C.|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||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_0000358718|||http://purl.uniprot.org/annotation/PRO_0000358719|||http://purl.uniprot.org/annotation/PRO_0000358720|||http://purl.uniprot.org/annotation/PRO_0000358721 http://togogenome.org/gene/10090:Arhgef10 ^@ http://purl.uniprot.org/uniprot/Q3UGZ6|||http://purl.uniprot.org/uniprot/Q8C033 ^@ 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|||DH|||Disordered|||In isoform 2.|||N5-methylglutamine|||Phosphoserine|||Polar residues|||Rho guanine nucleotide exchange factor 10 ^@ http://purl.uniprot.org/annotation/PRO_0000080927|||http://purl.uniprot.org/annotation/VSP_010707 http://togogenome.org/gene/10090:Folr1 ^@ http://purl.uniprot.org/uniprot/P35846 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Folate receptor alpha|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000008804|||http://purl.uniprot.org/annotation/PRO_0000008805 http://togogenome.org/gene/10090:Trim50 ^@ http://purl.uniprot.org/uniprot/E9PVV5|||http://purl.uniprot.org/uniprot/Q810I2 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Zinc Finger ^@ B box-type|||B30.2/SPRY|||Complete loss of acetylation.|||E3 ubiquitin-protein ligase TRIM50|||N6-acetyllysine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056275 http://togogenome.org/gene/10090:Clrn2 ^@ http://purl.uniprot.org/uniprot/B2RVW2 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Clarin-2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000454159 http://togogenome.org/gene/10090:Vmn1r155 ^@ http://purl.uniprot.org/uniprot/D3YTY1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:AB124611 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1G2|||http://purl.uniprot.org/uniprot/Q75VT8|||http://purl.uniprot.org/uniprot/Z4YNA9 ^@ 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 ^@ C19orf38 Ig|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein HIDE1 ^@ http://purl.uniprot.org/annotation/PRO_0000341218|||http://purl.uniprot.org/annotation/PRO_5002106984|||http://purl.uniprot.org/annotation/PRO_5004989818|||http://purl.uniprot.org/annotation/VSP_034226 http://togogenome.org/gene/10090:Slc2a13 ^@ http://purl.uniprot.org/uniprot/Q3UHK1 ^@ 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; 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_0000261317 http://togogenome.org/gene/10090:Ltf ^@ http://purl.uniprot.org/uniprot/P08071 ^@ 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|||Sequence Conflict|||Signal Peptide ^@ Lactotransferrin|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Transferrin-like 1|||Transferrin-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000035737 http://togogenome.org/gene/10090:Mapk10 ^@ http://purl.uniprot.org/uniprot/A0A5F8MP75|||http://purl.uniprot.org/uniprot/Q3TQZ7|||http://purl.uniprot.org/uniprot/Q61831|||http://purl.uniprot.org/uniprot/Q78GB8|||http://purl.uniprot.org/uniprot/Q80W80|||http://purl.uniprot.org/uniprot/Q80W81|||http://purl.uniprot.org/uniprot/Q80W82|||http://purl.uniprot.org/uniprot/Q8C9D4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform Alpha-1.|||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_0000186278|||http://purl.uniprot.org/annotation/VSP_004840 http://togogenome.org/gene/10090:Camta2 ^@ http://purl.uniprot.org/uniprot/B0QZH4|||http://purl.uniprot.org/uniprot/B0QZH6|||http://purl.uniprot.org/uniprot/Q80Y50 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Repeat|||Sequence Conflict|||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 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Nuclear localization signal|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000235822|||http://purl.uniprot.org/annotation/VSP_018494|||http://purl.uniprot.org/annotation/VSP_018495|||http://purl.uniprot.org/annotation/VSP_018496|||http://purl.uniprot.org/annotation/VSP_018497|||http://purl.uniprot.org/annotation/VSP_018498|||http://purl.uniprot.org/annotation/VSP_018499 http://togogenome.org/gene/10090:Slc37a1 ^@ http://purl.uniprot.org/uniprot/Q8R070 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Glucose-6-phosphate exchanger SLC37A1|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000436067 http://togogenome.org/gene/10090:Phactr2 ^@ http://purl.uniprot.org/uniprot/A1L3S9|||http://purl.uniprot.org/uniprot/B1AVN9|||http://purl.uniprot.org/uniprot/F7D4H5|||http://purl.uniprot.org/uniprot/Q3UQ19|||http://purl.uniprot.org/uniprot/Q3UTF8 ^@ 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|||Polar residues|||Pro residues|||RPEL ^@ http://togogenome.org/gene/10090:Wtip ^@ http://purl.uniprot.org/uniprot/Q7TQJ8 ^@ 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_0000328861 http://togogenome.org/gene/10090:Ulk2 ^@ http://purl.uniprot.org/uniprot/Q3UG39|||http://purl.uniprot.org/uniprot/Q9QY01 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||CTD-like region|||Decreased kinase activity.|||Disordered|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase ULK2 ^@ http://purl.uniprot.org/annotation/PRO_0000086783 http://togogenome.org/gene/10090:Or2m13 ^@ http://purl.uniprot.org/uniprot/Q8VFA2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccdc186 ^@ http://purl.uniprot.org/uniprot/Q8C9S4 ^@ 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 186|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089824 http://togogenome.org/gene/10090:Dsc1 ^@ http://purl.uniprot.org/uniprot/P55849|||http://purl.uniprot.org/uniprot/Q2VPA9|||http://purl.uniprot.org/uniprot/Q32ME9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cytoplasmic|||Desmocollin-1|||Extracellular|||Helical|||In isoform 1B.|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000003865|||http://purl.uniprot.org/annotation/PRO_0000003866|||http://purl.uniprot.org/annotation/PRO_5004217885|||http://purl.uniprot.org/annotation/PRO_5015097385|||http://purl.uniprot.org/annotation/VSP_000653|||http://purl.uniprot.org/annotation/VSP_000654 http://togogenome.org/gene/10090:Arhgef2 ^@ http://purl.uniprot.org/uniprot/H3BJ40|||http://purl.uniprot.org/uniprot/H3BJ45|||http://purl.uniprot.org/uniprot/Q60875 ^@ 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|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||Interaction with DYNLT1|||N6-acetyllysine|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by PAK4|||Phosphothreonine|||Phosphothreonine; by MAPK1 or MAPK3|||Phosphotyrosine|||Rho guanine nucleotide exchange factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000080910|||http://purl.uniprot.org/annotation/VSP_022640|||http://purl.uniprot.org/annotation/VSP_022641|||http://purl.uniprot.org/annotation/VSP_022642|||http://purl.uniprot.org/annotation/VSP_022643|||http://purl.uniprot.org/annotation/VSP_034962|||http://purl.uniprot.org/annotation/VSP_034963 http://togogenome.org/gene/10090:Susd5 ^@ http://purl.uniprot.org/uniprot/G3UW60 ^@ 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|||Link|||Polar residues|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_5015091559 http://togogenome.org/gene/10090:Psme2b ^@ http://purl.uniprot.org/uniprot/P97372|||http://purl.uniprot.org/uniprot/Q5SVP3 ^@ 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 ^@ Basic and acidic residues|||Disordered|||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_0000161786 http://togogenome.org/gene/10090:Msgn1 ^@ http://purl.uniprot.org/uniprot/Q9JK54 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Mesogenin-1|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000330029 http://togogenome.org/gene/10090:Mettl5 ^@ http://purl.uniprot.org/uniprot/Q3UZW4|||http://purl.uniprot.org/uniprot/Q8K1A0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site ^@ Abolished rRNAN6-adenosine-methyltransferase activity.|||Methyltransferase small|||rRNA N6-adenosine-methyltransferase METTL5 ^@ http://purl.uniprot.org/annotation/PRO_0000251920 http://togogenome.org/gene/10090:Acvr1b ^@ http://purl.uniprot.org/uniprot/Q3TZF1|||http://purl.uniprot.org/uniprot/Q61271 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Activin receptor type-1B|||Cytoplasmic|||Extracellular|||GS|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||receptor protein serine/threonine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000024418|||http://purl.uniprot.org/annotation/PRO_5014309160 http://togogenome.org/gene/10090:Hccs ^@ http://purl.uniprot.org/uniprot/P53702|||http://purl.uniprot.org/uniprot/Q8BP79 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||HRM 1|||HRM 2|||Holocytochrome c-type synthase|||N-myristoyl glycine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000121713 http://togogenome.org/gene/10090:Pot1a ^@ http://purl.uniprot.org/uniprot/Q91WC1 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||Protection of telomeres protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000121730|||http://purl.uniprot.org/annotation/VSP_010848|||http://purl.uniprot.org/annotation/VSP_010849 http://togogenome.org/gene/10090:Efcab3 ^@ http://purl.uniprot.org/uniprot/Q80X60 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||EF-hand 1|||EF-hand 2|||EF-hand calcium-binding domain-containing protein 3|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000253548 http://togogenome.org/gene/10090:Fbxo38 ^@ http://purl.uniprot.org/uniprot/Q8BMI0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Decreased cytoplasmic localization.|||Disordered|||F-box|||F-box only protein 38|||Impaired nuclear localization.|||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_0000119934 http://togogenome.org/gene/10090:Ms4a6c ^@ http://purl.uniprot.org/uniprot/Q6P6F8|||http://purl.uniprot.org/uniprot/Q99N08 ^@ 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.|||Membrane-spanning 4-domains subfamily A member 6C|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000158640|||http://purl.uniprot.org/annotation/VSP_007385|||http://purl.uniprot.org/annotation/VSP_007386 http://togogenome.org/gene/10090:Paqr5 ^@ http://purl.uniprot.org/uniprot/Q9DCU0 ^@ 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|||Membrane progestin receptor gamma ^@ http://purl.uniprot.org/annotation/PRO_0000218844 http://togogenome.org/gene/10090:Kif6 ^@ http://purl.uniprot.org/uniprot/E9PX57 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Kinesin motor|||Polar residues ^@ http://togogenome.org/gene/10090:Id2 ^@ http://purl.uniprot.org/uniprot/P41136|||http://purl.uniprot.org/uniprot/Q545T4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ BHLH|||DNA-binding protein inhibitor ID-2|||Interaction with IFI204|||Nuclear export signal|||Phosphoserine|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127242 http://togogenome.org/gene/10090:Oit3 ^@ http://purl.uniprot.org/uniprot/Q8R4V5 ^@ 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 ^@ EGF-like; calcium-binding|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Oncoprotein-induced transcript 3 protein|||ZP ^@ http://purl.uniprot.org/annotation/PRO_0000298932|||http://purl.uniprot.org/annotation/VSP_027484 http://togogenome.org/gene/10090:Cd300ld4 ^@ http://purl.uniprot.org/uniprot/A2A7W1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Immunoglobulin V-set ^@ http://purl.uniprot.org/annotation/PRO_5015086002 http://togogenome.org/gene/10090:Nr1d1 ^@ http://purl.uniprot.org/uniprot/Q3UV55 ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Crucial for activation of GJA1|||Disordered|||Loss of interaction with FBXW7 and loss of CDK1-mediated phosphorylation.|||Loss of interaction with FBXW7.|||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|||Pro residues|||Reduces interaction with PER2 by 60%.|||Required for phosphorylation by CSNK1E and cytoplasmic localization ^@ http://purl.uniprot.org/annotation/PRO_0000311182 http://togogenome.org/gene/10090:Nudt7 ^@ http://purl.uniprot.org/uniprot/Q99P30 ^@ 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|||Sequence Conflict|||Site|||Splice Variant ^@ 10-fold increase in Km for CoA.|||2- to 3-fold increase in Km for CoA.|||3-fold increase in Km for CoA.|||Important for coenzyme A binding|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of fatty acyl-coenzyme A diphosphatase activity.|||Microbody targeting signal|||N6-succinyllysine|||No significant effect on Km for CoA.|||Nudix box|||Nudix hydrolase|||Peroxisomal coenzyme A diphosphatase NUDT7 ^@ http://purl.uniprot.org/annotation/PRO_0000057141|||http://purl.uniprot.org/annotation/VSP_014271|||http://purl.uniprot.org/annotation/VSP_014272|||http://purl.uniprot.org/annotation/VSP_014273|||http://purl.uniprot.org/annotation/VSP_014274|||http://purl.uniprot.org/annotation/VSP_014275 http://togogenome.org/gene/10090:Ybx2 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQD2|||http://purl.uniprot.org/uniprot/B2RUF0|||http://purl.uniprot.org/uniprot/Q3TTC8|||http://purl.uniprot.org/uniprot/Q497N3 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||CSD|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Chchd2 ^@ http://purl.uniprot.org/uniprot/Q9D1L0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Motif|||Region ^@ CHCH|||Coiled-coil-helix-coiled-coil-helix domain-containing protein 2|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000129161 http://togogenome.org/gene/10090:Adprs ^@ http://purl.uniprot.org/uniprot/Q8CG72 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ ADP-ribosylhydrolase ARH3|||Glutamate flap|||In isoform 2.|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000277614|||http://purl.uniprot.org/annotation/VSP_023037 http://togogenome.org/gene/10090:Plxna1 ^@ http://purl.uniprot.org/uniprot/P70206 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||Loss of interaction with FARP2.|||N-linked (GlcNAc...) asparagine|||Plexin-A1|||Sema ^@ http://purl.uniprot.org/annotation/PRO_0000232746 http://togogenome.org/gene/10090:Or6s1 ^@ http://purl.uniprot.org/uniprot/E9Q0Z1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Crocc ^@ http://purl.uniprot.org/uniprot/Q8CJ40 ^@ 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.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||Rootletin ^@ http://purl.uniprot.org/annotation/PRO_0000239944|||http://purl.uniprot.org/annotation/VSP_052066|||http://purl.uniprot.org/annotation/VSP_052067|||http://purl.uniprot.org/annotation/VSP_052068 http://togogenome.org/gene/10090:Adcy10 ^@ http://purl.uniprot.org/uniprot/E9Q9T4|||http://purl.uniprot.org/uniprot/Q8C0T9 ^@ 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 ^@ Adenylate cyclase type 10|||Guanylate cyclase|||Guanylate cyclase 1|||Guanylate cyclase 2|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000317102|||http://purl.uniprot.org/annotation/VSP_030871|||http://purl.uniprot.org/annotation/VSP_030872 http://togogenome.org/gene/10090:Hyal2 ^@ http://purl.uniprot.org/uniprot/O35632|||http://purl.uniprot.org/uniprot/Q3UZE4 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ EGF-like|||GPI-anchor amidated asparagine; alternate|||Hyaluronidase|||Hyaluronidase-2|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; alternate|||Proton donor|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000012101|||http://purl.uniprot.org/annotation/PRO_0000012102|||http://purl.uniprot.org/annotation/PRO_5010843523 http://togogenome.org/gene/10090:Uxt ^@ http://purl.uniprot.org/uniprot/Q9WTZ0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Protein UXT ^@ http://purl.uniprot.org/annotation/PRO_0000065752 http://togogenome.org/gene/10090:Gm5926 ^@ http://purl.uniprot.org/uniprot/E9PWJ8 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Cbx8 ^@ http://purl.uniprot.org/uniprot/Q9QXV1 ^@ 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|||Chromo|||Chromobox protein homolog 8|||Disordered|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080216 http://togogenome.org/gene/10090:Slc16a5 ^@ http://purl.uniprot.org/uniprot/G5E8K6 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Monocarboxylate transporter 6 ^@ http://purl.uniprot.org/annotation/PRO_0000415804 http://togogenome.org/gene/10090:Slc5a5 ^@ http://purl.uniprot.org/uniprot/G3X8P5 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Tdo2 ^@ http://purl.uniprot.org/uniprot/P48776|||http://purl.uniprot.org/uniprot/Q8VCW3 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Tryptophan 2,3-dioxygenase|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000072400 http://togogenome.org/gene/10090:Nlrp9b ^@ http://purl.uniprot.org/uniprot/Q66X22 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Repeat|||Splice Variant ^@ In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||NACHT|||NACHT, LRR and PYD domains-containing protein 9B|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000286336|||http://purl.uniprot.org/annotation/VSP_025024|||http://purl.uniprot.org/annotation/VSP_025025|||http://purl.uniprot.org/annotation/VSP_025026 http://togogenome.org/gene/10090:Cldn4 ^@ http://purl.uniprot.org/uniprot/O35054|||http://purl.uniprot.org/uniprot/Q3UM35 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Abolishes ability to form paracellular chloride channel.|||Claudin-4|||Cytoplasmic|||Extracellular|||Helical|||Interaction with EPHA2|||Interactions with TJP1, TJP2 and TJP3|||No effect.|||Phosphotyrosine; by EPHA2 ^@ http://purl.uniprot.org/annotation/PRO_0000144744 http://togogenome.org/gene/10090:Rrs1 ^@ http://purl.uniprot.org/uniprot/Q9CYH6 ^@ 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 ^@ Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Ribosome biogenesis regulatory protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000185375 http://togogenome.org/gene/10090:Gstm5 ^@ http://purl.uniprot.org/uniprot/P48774 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 5|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000185829 http://togogenome.org/gene/10090:Atxn3 ^@ http://purl.uniprot.org/uniprot/E9Q717|||http://purl.uniprot.org/uniprot/Q546X9|||http://purl.uniprot.org/uniprot/Q5M8S1|||http://purl.uniprot.org/uniprot/Q810M8|||http://purl.uniprot.org/uniprot/Q9CVD2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region ^@ Abolishes deubiquitinating activity.|||Ataxin-3|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Josephin|||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_0000053832 http://togogenome.org/gene/10090:Ggt7 ^@ http://purl.uniprot.org/uniprot/Q99JP7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Glutathione hydrolase 7 heavy chain|||Glutathione hydrolase 7 light chain|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000011068|||http://purl.uniprot.org/annotation/PRO_0000011069 http://togogenome.org/gene/10090:Or5t17 ^@ http://purl.uniprot.org/uniprot/Q8VES2 ^@ 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 5T17 ^@ http://purl.uniprot.org/annotation/PRO_0000150868 http://togogenome.org/gene/10090:Glyat ^@ http://purl.uniprot.org/uniprot/Q91XE0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ Glycine N-acyltransferase|||In isoform 2.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000281870|||http://purl.uniprot.org/annotation/VSP_024075 http://togogenome.org/gene/10090:Prpsap1 ^@ http://purl.uniprot.org/uniprot/B1AT82|||http://purl.uniprot.org/uniprot/Q9D0M1 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ N-acetylmethionine|||Phosphoribosyl pyrophosphate synthase-associated protein 1|||Phosphoserine|||Ribose-phosphate pyrophosphokinase N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000141080 http://togogenome.org/gene/10090:Ptma ^@ http://purl.uniprot.org/uniprot/P26350|||http://purl.uniprot.org/uniprot/Q0VGU2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Turn ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000029866|||http://purl.uniprot.org/annotation/PRO_0000299251|||http://purl.uniprot.org/annotation/PRO_0000423256 http://togogenome.org/gene/10090:Tmem132c ^@ http://purl.uniprot.org/uniprot/E9QP73|||http://purl.uniprot.org/uniprot/Q8CEF9 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 132C|||Transmembrane protein TMEM132 C-terminal|||Transmembrane protein TMEM132 N-terminal|||Transmembrane protein family 132 middle ^@ http://purl.uniprot.org/annotation/PRO_0000287099 http://togogenome.org/gene/10090:Mob1b ^@ http://purl.uniprot.org/uniprot/Q8BPB0 ^@ 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 ^@ MOB kinase activator 1B|||N-acetylserine|||Phosphothreonine; by STK4/MST1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000193565 http://togogenome.org/gene/10090:Qars ^@ http://purl.uniprot.org/uniprot/Q8BML9 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Glutamine--tRNA ligase|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000441172 http://togogenome.org/gene/10090:Or8k33 ^@ http://purl.uniprot.org/uniprot/Q7TR67 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fam76b ^@ http://purl.uniprot.org/uniprot/Q80XP8 ^@ 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.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM76B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000245764|||http://purl.uniprot.org/annotation/VSP_019774|||http://purl.uniprot.org/annotation/VSP_019775|||http://purl.uniprot.org/annotation/VSP_019776|||http://purl.uniprot.org/annotation/VSP_019777 http://togogenome.org/gene/10090:Ccdc28a ^@ http://purl.uniprot.org/uniprot/Q3UFK1|||http://purl.uniprot.org/uniprot/Q8CEI3 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Prss12 ^@ http://purl.uniprot.org/uniprot/O08762 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Site|||Strand ^@ Charge relay system|||Disordered|||Kringle|||N-linked (GlcNAc...) asparagine|||Neurotrypsin|||Peptidase S1|||Reactive bond homolog|||SRCR 1|||SRCR 2|||SRCR 3|||Zymogen activation region ^@ http://purl.uniprot.org/annotation/PRO_0000027670 http://togogenome.org/gene/10090:Ptar1 ^@ http://purl.uniprot.org/uniprot/A0A494B9V8 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Defa42 ^@ http://purl.uniprot.org/uniprot/D3YX03 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Alpha-defensin N-terminal|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015088520 http://togogenome.org/gene/10090:Ccdc39 ^@ http://purl.uniprot.org/uniprot/Q3TQ36|||http://purl.uniprot.org/uniprot/Q9D5Y1 ^@ 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 ^@ Coiled-coil domain-containing protein 39|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000234494 http://togogenome.org/gene/10090:1700040F15Rik ^@ http://purl.uniprot.org/uniprot/A0A087WRK1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Ros1 ^@ http://purl.uniprot.org/uniprot/Q78DX7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Abrogates interaction with PTPN6.|||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|||Fibronectin type-III 9|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proto-oncogene tyrosine-protein kinase ROS|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000278115 http://togogenome.org/gene/10090:Cd86 ^@ http://purl.uniprot.org/uniprot/P42082|||http://purl.uniprot.org/uniprot/Q549Q9|||http://purl.uniprot.org/uniprot/Q61238 ^@ 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|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||T-lymphocyte activation antigen CD86 ^@ http://purl.uniprot.org/annotation/PRO_0000014551|||http://purl.uniprot.org/annotation/PRO_5010844061|||http://purl.uniprot.org/annotation/VSP_023125 http://togogenome.org/gene/10090:Ash1l ^@ http://purl.uniprot.org/uniprot/Q99MY8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ A.T hook 1|||A.T hook 2|||A.T hook 3|||AWS|||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|||N5-methylglutamine|||N6-acetyllysine|||PHD-type|||Phosphoserine|||Polar residues|||Post-SET|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000259517 http://togogenome.org/gene/10090:Tbc1d12 ^@ http://purl.uniprot.org/uniprot/E9QQ68|||http://purl.uniprot.org/uniprot/Q6A039 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Rab-GAP TBC|||TBC1 domain family member 12 ^@ http://purl.uniprot.org/annotation/PRO_0000327655 http://togogenome.org/gene/10090:Coro1b ^@ http://purl.uniprot.org/uniprot/A2RS22|||http://purl.uniprot.org/uniprot/Q9WUM3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Coronin-1B|||DUF1899|||Disordered|||Phosphoserine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000050923 http://togogenome.org/gene/10090:Vmn2r38 ^@ http://purl.uniprot.org/uniprot/G3UYA8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003457203 http://togogenome.org/gene/10090:4932414N04Rik ^@ http://purl.uniprot.org/uniprot/Q8CEQ9 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF3496|||Disordered ^@ http://togogenome.org/gene/10090:Acp5 ^@ http://purl.uniprot.org/uniprot/Q05117 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Tartrate-resistant acid phosphatase type 5 ^@ http://purl.uniprot.org/annotation/PRO_0000023982 http://togogenome.org/gene/10090:Csrp2 ^@ http://purl.uniprot.org/uniprot/P97314 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict ^@ Cysteine and glycine-rich protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000075722 http://togogenome.org/gene/10090:Tslp ^@ http://purl.uniprot.org/uniprot/Q9JIE6 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Signal Peptide|||Site ^@ Inserts into a conserved IL7R hydrophobic pocket, important for IL7R-binding|||N-linked (GlcNAc...) asparagine|||Thymic stromal lymphopoietin ^@ http://purl.uniprot.org/annotation/PRO_0000300874 http://togogenome.org/gene/10090:Lmx1b ^@ http://purl.uniprot.org/uniprot/A0A6I8MWW7|||http://purl.uniprot.org/uniprot/O88609 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Homeobox|||LIM homeobox transcription factor 1-beta|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2 ^@ http://purl.uniprot.org/annotation/PRO_0000075830 http://togogenome.org/gene/10090:Fxyd1 ^@ http://purl.uniprot.org/uniprot/Q9Z239 ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phospholemman|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||S-glutathionyl cysteine; alternate|||S-palmitoyl cysteine|||S-palmitoyl cysteine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000010360 http://togogenome.org/gene/10090:H2bc4 ^@ http://purl.uniprot.org/uniprot/Q6ZWY9 ^@ 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-C/E/G|||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-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_0000244831 http://togogenome.org/gene/10090:Slc24a1 ^@ http://purl.uniprot.org/uniprot/Q91WD8 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Acidic residues|||Alpha-1|||Alpha-2|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Not cleaved|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sodium/potassium/calcium exchanger 1 ^@ http://purl.uniprot.org/annotation/PRO_0000455293 http://togogenome.org/gene/10090:Smg8 ^@ http://purl.uniprot.org/uniprot/Q8VE18 ^@ 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|||Nonsense-mediated mRNA decay factor SMG8|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000304975 http://togogenome.org/gene/10090:Dnah9 ^@ http://purl.uniprot.org/uniprot/B1AR51 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disordered|||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|||Dynein heavy chain tail ^@ http://togogenome.org/gene/10090:Mpv17l2 ^@ http://purl.uniprot.org/uniprot/Q8VIK2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Mpv17-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000317622 http://togogenome.org/gene/10090:Klk8 ^@ http://purl.uniprot.org/uniprot/A0A0B6VRH9|||http://purl.uniprot.org/uniprot/Q61955 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Propeptide|||Signal Peptide|||Strand|||Turn ^@ Charge relay system|||Kallikrein-8|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027948|||http://purl.uniprot.org/annotation/PRO_0000027949|||http://purl.uniprot.org/annotation/PRO_5014221786 http://togogenome.org/gene/10090:Asic1 ^@ http://purl.uniprot.org/uniprot/Q6NXK8 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acid-sensing ion channel 1|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||Important for channel desensitizing|||Important for channel gating|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKA|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000181295|||http://purl.uniprot.org/annotation/VSP_015614|||http://purl.uniprot.org/annotation/VSP_015615 http://togogenome.org/gene/10090:Selenov ^@ http://purl.uniprot.org/uniprot/Q5FWB9 ^@ Compositionally Biased Region|||Modification|||Non standard residue|||Region ^@ Compositionally Biased Region|||Non standard residue|||Region ^@ Disordered|||Polar residues|||Selenocysteine ^@ http://togogenome.org/gene/10090:Scarb1 ^@ http://purl.uniprot.org/uniprot/Q61009 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Scavenger receptor class B member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000144161|||http://purl.uniprot.org/annotation/VSP_058986 http://togogenome.org/gene/10090:Cryl1 ^@ http://purl.uniprot.org/uniprot/A7VMV2|||http://purl.uniprot.org/uniprot/Q99KP3 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Site ^@ 3-hydroxyacyl-CoA dehydrogenase C-terminal|||3-hydroxyacyl-CoA dehydrogenase NAD binding|||Important for catalytic activity|||Lambda-crystallin homolog|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000109321 http://togogenome.org/gene/10090:Stpg1 ^@ http://purl.uniprot.org/uniprot/Q9D2F5 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ O(6)-methylguanine-induced apoptosis 2|||Phosphotyrosine|||STPGR 1|||STPGR 2|||STPGR 3|||STPGR 4|||STPGR 5|||STPGR 6|||STPGR 7 ^@ http://purl.uniprot.org/annotation/PRO_0000305171 http://togogenome.org/gene/10090:Nlrp4c ^@ http://purl.uniprot.org/uniprot/Q3TKR3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||NACHT|||NACHT, LRR and PYD domains-containing protein 4C|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000286331 http://togogenome.org/gene/10090:Spin4 ^@ http://purl.uniprot.org/uniprot/Q8K1L2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Region|||Sequence Conflict|||Site ^@ 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_0000313795 http://togogenome.org/gene/10090:Cyb561d2 ^@ http://purl.uniprot.org/uniprot/Q9WUE3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Cytochrome b561|||Cytoplasmic|||Helical|||Loss of heme binding.|||Lumenal|||Removed|||Transmembrane reductase CYB561D2|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000151037 http://togogenome.org/gene/10090:Tspan6 ^@ http://purl.uniprot.org/uniprot/Q99L96 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Prss38 ^@ http://purl.uniprot.org/uniprot/Q3UKY7 ^@ 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 38 ^@ http://purl.uniprot.org/annotation/PRO_0000328822|||http://purl.uniprot.org/annotation/PRO_0000328823 http://togogenome.org/gene/10090:Flt1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0A4|||http://purl.uniprot.org/uniprot/P35969 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||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|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Vascular endothelial growth factor receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000016769 http://togogenome.org/gene/10090:Hspb9 ^@ http://purl.uniprot.org/uniprot/G3UWB9|||http://purl.uniprot.org/uniprot/Q9DAM3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Heat shock protein beta-9|||Polar residues|||SHSP|||sHSP ^@ http://purl.uniprot.org/annotation/PRO_0000125951 http://togogenome.org/gene/10090:Mptx2 ^@ http://purl.uniprot.org/uniprot/D3YYJ7 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Pentraxin family member ^@ http://purl.uniprot.org/annotation/PRO_5015019507 http://togogenome.org/gene/10090:Gm4981 ^@ http://purl.uniprot.org/uniprot/Q3ULJ8 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Or9s18 ^@ http://purl.uniprot.org/uniprot/E9Q2B9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rps6ka4 ^@ http://purl.uniprot.org/uniprot/Q9Z2B9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ AGC-kinase C-terminal|||Disordered|||Phosphoserine|||Phosphoserine; by MAPK1, MAPK3 and MAPK14|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by MAPK1, MAPK3 and MAPK14|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Ribosomal protein S6 kinase alpha-4 ^@ http://purl.uniprot.org/annotation/PRO_0000086206 http://togogenome.org/gene/10090:Ccnb3 ^@ http://purl.uniprot.org/uniprot/A2AEP2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Cyclin C-terminal|||Cyclin-like|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rpap1 ^@ http://purl.uniprot.org/uniprot/Q80TE0 ^@ 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.|||Phosphothreonine|||Polar residues|||Pro residues|||RNA polymerase II-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000284842|||http://purl.uniprot.org/annotation/VSP_024682|||http://purl.uniprot.org/annotation/VSP_024683 http://togogenome.org/gene/10090:Nrn1l ^@ http://purl.uniprot.org/uniprot/Q8C4W3 ^@ Chain|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Signal Peptide|||Splice Variant ^@ Chain|||Lipid Binding|||Propeptide|||Signal Peptide|||Splice Variant ^@ GPI-anchor amidated alanine|||In isoform 2.|||Neuritin-like protein|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000319431|||http://purl.uniprot.org/annotation/PRO_0000319432|||http://purl.uniprot.org/annotation/VSP_031481 http://togogenome.org/gene/10090:Dbpht2 ^@ http://purl.uniprot.org/uniprot/Q8IWX3 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Efnb2 ^@ http://purl.uniprot.org/uniprot/P52800|||http://purl.uniprot.org/uniprot/Q4FJM3 ^@ 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|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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_0000008393 http://togogenome.org/gene/10090:Begain ^@ http://purl.uniprot.org/uniprot/F8WIG2|||http://purl.uniprot.org/uniprot/Q68EF6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Brain-enriched guanylate kinase-associated protein|||Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064905 http://togogenome.org/gene/10090:Thpo ^@ http://purl.uniprot.org/uniprot/P40226|||http://purl.uniprot.org/uniprot/Q543R9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Thrombopoietin ^@ http://purl.uniprot.org/annotation/PRO_0000008412|||http://purl.uniprot.org/annotation/PRO_5014309613|||http://purl.uniprot.org/annotation/VSP_001452 http://togogenome.org/gene/10090:Nol7 ^@ http://purl.uniprot.org/uniprot/A1L3B6|||http://purl.uniprot.org/uniprot/Q9D7Z3 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Nucleolar protein 7|||Nucleolar protein 7 C-terminal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000096938|||http://purl.uniprot.org/annotation/VSP_014793 http://togogenome.org/gene/10090:Nt5dc1 ^@ http://purl.uniprot.org/uniprot/Q8C5P5 ^@ 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 ^@ 5'-nucleotidase domain-containing protein 1|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000247223|||http://purl.uniprot.org/annotation/VSP_019948|||http://purl.uniprot.org/annotation/VSP_019949|||http://purl.uniprot.org/annotation/VSP_019950 http://togogenome.org/gene/10090:Cxadr ^@ http://purl.uniprot.org/uniprot/P97792 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||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|||Lipid Binding|||Modified Residue|||Motif|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||Coxsackievirus and adenovirus receptor homolog|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000014740|||http://purl.uniprot.org/annotation/VSP_014827|||http://purl.uniprot.org/annotation/VSP_014828|||http://purl.uniprot.org/annotation/VSP_014829 http://togogenome.org/gene/10090:Tssk1 ^@ http://purl.uniprot.org/uniprot/Q61241 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Testis-specific serine/threonine-protein kinase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000086767 http://togogenome.org/gene/10090:2410137M14Rik ^@ http://purl.uniprot.org/uniprot/Q9CWF0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Il9r ^@ http://purl.uniprot.org/uniprot/A2AVE0|||http://purl.uniprot.org/uniprot/Q01114|||http://purl.uniprot.org/uniprot/Q78PA5 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Interleukin-9 receptor|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010912 http://togogenome.org/gene/10090:Nipsnap2 ^@ http://purl.uniprot.org/uniprot/Q7TMG8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ NIPSNAP ^@ http://togogenome.org/gene/10090:Krtcap3 ^@ http://purl.uniprot.org/uniprot/Q8K177 ^@ 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_0000226986|||http://purl.uniprot.org/annotation/VSP_017531 http://togogenome.org/gene/10090:Ada ^@ http://purl.uniprot.org/uniprot/P03958|||http://purl.uniprot.org/uniprot/Q4FK28 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Strand|||Turn ^@ Adenosine deaminase|||Important for catalytic activity|||Important for interaction with adenosine receptors and increasing their affinity for agonists|||Increases affinity for adenosine 20-fold. Reduces enzyme activity 500-fold.|||Loss of activity.|||N-acetylalanine|||N6-acetyllysine|||Nearly abolishes enzyme activity.|||No effect on affinity for adenosine. Reduces enzyme activity 2750-fold.|||Proton donor|||Reduces affinity for adenosine 10-fold. Reduces enzyme activity 100-fold.|||Reduces affinity for adenosine 70-fold. Reduces enzyme activity 110000-fold.|||Reduces catalytic activity 3200-fold. No effect on affinity for adenosine.|||Reduces catalytic activity 4800-fold, and slightly increases affinity for substrate.|||Reduces catalytic activity 700-fold. No effect on affinity for adenosine.|||Reduces enzyme activity 1500-fold. No effect on affinity for adenosine.|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194353 http://togogenome.org/gene/10090:Smarcad1 ^@ http://purl.uniprot.org/uniprot/Q04692 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||CUE 1|||CUE 2|||DEAD box|||DEGH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||N-acetylmethionine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 ^@ http://purl.uniprot.org/annotation/PRO_0000074357|||http://purl.uniprot.org/annotation/VSP_007080 http://togogenome.org/gene/10090:Naa15 ^@ http://purl.uniprot.org/uniprot/G3X8Y3 ^@ Region|||Repeat ^@ Region|||Repeat ^@ Disordered|||TPR ^@ http://togogenome.org/gene/10090:Pdpn ^@ http://purl.uniprot.org/uniprot/A8Y5F6|||http://purl.uniprot.org/uniprot/Q62011 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 50% decrease of cell growth; when associated with A-167. 50% increase of cell migration; when associated with A-167.|||50% decrease of cell growth; when associated with A-171. 50% increase of cell migration; when associated with A-171.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not significantly increase cell motility; when associated with D-171. Does not significantly decrease cell growth; when associated with A-171.|||Eliminates platelet aggregation activity.|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Podoplanin|||Requires for dimerization and lipidd rafts association|||Requires for interaction with MSN and EZR ^@ http://purl.uniprot.org/annotation/PRO_0000021352|||http://purl.uniprot.org/annotation/PRO_5002734313 http://togogenome.org/gene/10090:Or9i14 ^@ http://purl.uniprot.org/uniprot/Q8VG65 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Limk1 ^@ http://purl.uniprot.org/uniprot/E9PVB6|||http://purl.uniprot.org/uniprot/P53668|||http://purl.uniprot.org/uniprot/Q3UR47 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abrogates kinase activity.|||Disordered|||LIM domain kinase 1|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||PDZ|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Phosphothreonine|||Phosphothreonine; by ROCK1|||Polar residues|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000075804 http://togogenome.org/gene/10090:Or1e30 ^@ http://purl.uniprot.org/uniprot/Q8VEZ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trim69 ^@ http://purl.uniprot.org/uniprot/Q80X56 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ B30.2/SPRY|||Disordered|||E3 ubiquitin-protein ligase TRIM69|||Necessary for nuclear localization|||Phosphoserine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000278237 http://togogenome.org/gene/10090:Mfap2 ^@ http://purl.uniprot.org/uniprot/P55002|||http://purl.uniprot.org/uniprot/Q99PM0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Signal Peptide ^@ Disordered|||Microfibrillar-associated protein 2|||Or 18|||Polar residues|||Pyrrolidone carboxylic acid|||ShKT|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000018683|||http://purl.uniprot.org/annotation/PRO_5015099617 http://togogenome.org/gene/10090:Tefm ^@ http://purl.uniprot.org/uniprot/Q5SSK3 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||Transcription elongation factor, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000406330 http://togogenome.org/gene/10090:Setd3 ^@ http://purl.uniprot.org/uniprot/Q91WC0 ^@ 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 ^@ Actin-histidine N-methyltransferase|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000254176|||http://purl.uniprot.org/annotation/VSP_021194|||http://purl.uniprot.org/annotation/VSP_021195|||http://purl.uniprot.org/annotation/VSP_021196|||http://purl.uniprot.org/annotation/VSP_021197|||http://purl.uniprot.org/annotation/VSP_021198 http://togogenome.org/gene/10090:Snx9 ^@ http://purl.uniprot.org/uniprot/Q3U1P2|||http://purl.uniprot.org/uniprot/Q91VH2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Strand|||Turn ^@ BAR|||Critical for tubulation activity|||Disordered|||N6-acetyllysine|||PX|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SH3|||Sorting nexin-9 ^@ http://purl.uniprot.org/annotation/PRO_0000213853 http://togogenome.org/gene/10090:Echdc3 ^@ http://purl.uniprot.org/uniprot/Q9D7J9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Enoyl-CoA hydratase domain-containing protein 3, mitochondrial|||Mitochondrion|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000333216 http://togogenome.org/gene/10090:Tasor ^@ http://purl.uniprot.org/uniprot/Q69ZR9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MommeD6; severe developmental delay leading to lethality before gastrulation. Mutants exhibit impaired primitive streak elongation, delayed epithelial-to-mesenchymal transition during gastrulation and an increase in p53/TP53-driven apoptosis. Epiblasts show an increased expression of p53 pathway genes as well as several pluripotency-associated long non-coding RNAs.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Protein TASOR|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000295729|||http://purl.uniprot.org/annotation/VSP_042114|||http://purl.uniprot.org/annotation/VSP_042115|||http://purl.uniprot.org/annotation/VSP_042116|||http://purl.uniprot.org/annotation/VSP_042117 http://togogenome.org/gene/10090:Atg101 ^@ http://purl.uniprot.org/uniprot/Q9D8Z6 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Autophagy-related protein 101|||Important for interaction with ATG13 ^@ http://purl.uniprot.org/annotation/PRO_0000294323 http://togogenome.org/gene/10090:Hsd17b1 ^@ http://purl.uniprot.org/uniprot/P51656|||http://purl.uniprot.org/uniprot/Q790P4 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ 17-beta-hydroxysteroid dehydrogenase type 1|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054568 http://togogenome.org/gene/10090:Txndc15 ^@ http://purl.uniprot.org/uniprot/Q6P6J9 ^@ 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|||N-linked (GlcNAc...) asparagine|||Thioredoxin|||Thioredoxin domain-containing protein 15 ^@ http://purl.uniprot.org/annotation/PRO_0000296095 http://togogenome.org/gene/10090:Ddx43 ^@ http://purl.uniprot.org/uniprot/D3Z6P9 ^@ Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ DEAD-box RNA helicase Q|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Polar residues|||Q motif ^@ http://togogenome.org/gene/10090:Or2h1b ^@ http://purl.uniprot.org/uniprot/Q6UAH1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp706 ^@ http://purl.uniprot.org/uniprot/B2RVQ7|||http://purl.uniprot.org/uniprot/Q9D115 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Zinc Finger ^@ C2H2-type|||Disordered|||Polar residues|||Small EDRK-rich factor-like N-terminal|||Unable to restore differentiation of embryonic stem cells (ESCs).|||Zinc finger protein 706 ^@ http://purl.uniprot.org/annotation/PRO_0000047704 http://togogenome.org/gene/10090:Dppa3 ^@ http://purl.uniprot.org/uniprot/Q8QZY3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure ^@ Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region ^@ Abolishes localization to the nucleus and ability to prevent DNA demethylation; when associated with A-44.|||Abolishes localization to the nucleus and ability to prevent DNA demethylation; when associated with A-46.|||Basic and acidic residues|||Developmental pluripotency-associated protein 3|||Disordered|||Required for H3K9me2-binding|||Required to exclude TET3 from the maternal pronucleus ^@ http://purl.uniprot.org/annotation/PRO_0000239266 http://togogenome.org/gene/10090:Krtap5-2 ^@ http://purl.uniprot.org/uniprot/Q9D5Z7 ^@ 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 5-2 ^@ http://purl.uniprot.org/annotation/PRO_0000361658 http://togogenome.org/gene/10090:Gnrhr ^@ http://purl.uniprot.org/uniprot/D3Z6P7|||http://purl.uniprot.org/uniprot/Q01776|||http://purl.uniprot.org/uniprot/Q6P8H4 ^@ 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|||Gonadotropin-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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069489 http://togogenome.org/gene/10090:Tm4sf4 ^@ http://purl.uniprot.org/uniprot/Q3TMT3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Dync2li1 ^@ http://purl.uniprot.org/uniprot/Q8K0T2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Cytoplasmic dynein 2 light intermediate chain 1|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000318751 http://togogenome.org/gene/10090:Smc5 ^@ http://purl.uniprot.org/uniprot/A0A286YDG5|||http://purl.uniprot.org/uniprot/Q8CG46 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Flexible hinge|||In isoform 2.|||Phosphoserine|||RecF/RecN/SMC N-terminal|||Structural maintenance of chromosomes protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000270952|||http://purl.uniprot.org/annotation/VSP_022251|||http://purl.uniprot.org/annotation/VSP_022252 http://togogenome.org/gene/10090:Hsdl1 ^@ http://purl.uniprot.org/uniprot/Q8BTX9 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Inactive hydroxysteroid dehydrogenase-like protein 1|||N-acetylalanine|||Removed|||Required for mitochondria translocation ^@ http://purl.uniprot.org/annotation/PRO_0000313672 http://togogenome.org/gene/10090:Pla2g2f ^@ http://purl.uniprot.org/uniprot/Q9QZT4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant ^@ Group IIF secretory phospholipase A2|||In isoform 2.|||Loss of catalytic activity.|||N-linked (GlcNAc...) asparagine|||No effect on lipase activity toward 1-palmitoyl-2-arachidonoyl-phosphatidylethanolamine (2-AA-PE).|||Required for localization on the plasma membrane ^@ http://purl.uniprot.org/annotation/PRO_0000022760|||http://purl.uniprot.org/annotation/VSP_037525 http://togogenome.org/gene/10090:Gtf3c2 ^@ http://purl.uniprot.org/uniprot/Q8BL74 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||General transcription factor 3C polypeptide 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000050986 http://togogenome.org/gene/10090:Ostm1 ^@ http://purl.uniprot.org/uniprot/Q8BGT0 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Osteopetrosis-associated transmembrane protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000021964 http://togogenome.org/gene/10090:Scaf4 ^@ http://purl.uniprot.org/uniprot/Q7TSH6|||http://purl.uniprot.org/uniprot/Q8BXA9 ^@ 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|||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_0000447631|||http://purl.uniprot.org/annotation/VSP_060218|||http://purl.uniprot.org/annotation/VSP_060219|||http://purl.uniprot.org/annotation/VSP_060220 http://togogenome.org/gene/10090:Or4p19 ^@ http://purl.uniprot.org/uniprot/Q0VB29 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp148 ^@ http://purl.uniprot.org/uniprot/A0A338P6K3|||http://purl.uniprot.org/uniprot/Q3UJ69|||http://purl.uniprot.org/uniprot/Q548L0|||http://purl.uniprot.org/uniprot/Q61624 ^@ 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 ^@ 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 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|||Phosphoserine|||Phosphothreonine|||Zinc finger protein 148 ^@ http://purl.uniprot.org/annotation/PRO_0000047428 http://togogenome.org/gene/10090:Foxk1 ^@ http://purl.uniprot.org/uniprot/P42128 ^@ Chain|||Compositionally Biased Region|||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|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand ^@ Abolishes DNA-binding. No effect on transcriptional repression.|||Decreased phosphorylation by GSK3A and interaction with 14-3-3 proteins.|||Decreases DNA-binding. No effect on transcriptional repression.|||Disordered|||FHA|||Fork-head|||Forkhead box protein K1|||Interaction with SIN3A and SIN3B|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Required for interaction with FOXO4 and MEF2C ^@ http://purl.uniprot.org/annotation/PRO_0000091857 http://togogenome.org/gene/10090:Ermardl1 ^@ http://purl.uniprot.org/uniprot/F6UWZ4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ DUF4209 ^@ http://togogenome.org/gene/10090:Lamc1 ^@ http://purl.uniprot.org/uniprot/F8VQJ3 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Laminin EGF-like|||Laminin IV type A|||Laminin N-terminal ^@ http://purl.uniprot.org/annotation/PRO_5003379251 http://togogenome.org/gene/10090:Magohb ^@ http://purl.uniprot.org/uniprot/Q9CQL1 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein mago nashi homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000174148 http://togogenome.org/gene/10090:Cacna1h ^@ http://purl.uniprot.org/uniprot/E9Q6P9|||http://purl.uniprot.org/uniprot/Q3UX23 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Ion transport|||Ion transport domain-containing protein|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5004230383 http://togogenome.org/gene/10090:Pgrmc1 ^@ http://purl.uniprot.org/uniprot/O55022|||http://purl.uniprot.org/uniprot/Q3TXU8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytochrome b5 heme-binding|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Membrane-associated progesterone receptor component 1|||Phosphoserine|||Phosphothreonine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000121740 http://togogenome.org/gene/10090:Art2b ^@ http://purl.uniprot.org/uniprot/O35975 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Changes thiol-independent NADase activity to thiol-dependent; when associated with C-201.|||Changes thiol-independent NADase activity to thiol-dependent; when associated with C-80.|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||T-cell ecto-ADP-ribosyltransferase 2|||TR mART core ^@ http://purl.uniprot.org/annotation/PRO_0000019321|||http://purl.uniprot.org/annotation/PRO_0000019322 http://togogenome.org/gene/10090:Tipin ^@ http://purl.uniprot.org/uniprot/Q91WA1 ^@ 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|||Interaction with TIMELESS|||Phosphoserine|||Phosphothreonine|||Polar residues|||TIMELESS-interacting protein ^@ http://purl.uniprot.org/annotation/PRO_0000305254 http://togogenome.org/gene/10090:Gdf15 ^@ http://purl.uniprot.org/uniprot/Q9Z0J7 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Growth/differentiation factor 15|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033994|||http://purl.uniprot.org/annotation/PRO_0000033995 http://togogenome.org/gene/10090:Rad51ap2 ^@ http://purl.uniprot.org/uniprot/G3UW63 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Pro residues|||RAD51 interacting motif ^@ http://togogenome.org/gene/10090:Myl6 ^@ http://purl.uniprot.org/uniprot/A0A1W2P7Q9|||http://purl.uniprot.org/uniprot/Q60605|||http://purl.uniprot.org/uniprot/Q642K0 ^@ 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 ^@ EF-hand|||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_0000198691|||http://purl.uniprot.org/annotation/VSP_009736 http://togogenome.org/gene/10090:Tmem143 ^@ http://purl.uniprot.org/uniprot/G3X9F4|||http://purl.uniprot.org/uniprot/Q8VD26 ^@ 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|||Transmembrane protein 143 ^@ http://purl.uniprot.org/annotation/PRO_0000285959|||http://purl.uniprot.org/annotation/VSP_024933|||http://purl.uniprot.org/annotation/VSP_024934|||http://purl.uniprot.org/annotation/VSP_024935|||http://purl.uniprot.org/annotation/VSP_024936|||http://purl.uniprot.org/annotation/VSP_024937 http://togogenome.org/gene/10090:Pknox2 ^@ http://purl.uniprot.org/uniprot/Q8BG99 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Homeobox|||Homeobox protein PKNOX2|||MEIS N-terminal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000249880 http://togogenome.org/gene/10090:Rpl3 ^@ http://purl.uniprot.org/uniprot/P27659 ^@ 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 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|||Phosphoserine|||Tele-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000077229 http://togogenome.org/gene/10090:Uba52 ^@ http://purl.uniprot.org/uniprot/P62984|||http://purl.uniprot.org/uniprot/Q5M9K3 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Site|||Strand ^@ ADP-ribosylglycine|||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|||N6,N6,N6-trimethyllysine|||Phosphoserine; by PINK1|||Ubiquitin|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000138752|||http://purl.uniprot.org/annotation/PRO_0000396435 http://togogenome.org/gene/10090:Cemip2 ^@ http://purl.uniprot.org/uniprot/Q5FWI3|||http://purl.uniprot.org/uniprot/Q8BS93 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cell surface hyaluronidase|||Cytoplasmic|||Disordered|||Does not affect hyaluronidase activity.|||Essential for hyaluronidase activity|||Extracellular|||G8|||GG-type lectin 1|||GG-type lectin 2|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||PbH1 1|||PbH1 2|||PbH1 3|||Phosphoserine|||Polar residues|||Slight suppression of hyaluronidase activity. Hyaluronidase activity is abolished; when associated with 248-N.|||Slight suppression of hyaluronidase activity. Hyaluronidase activity is abolished; when associated with 303-F.|||Slightly increases of hyaluronidase activity.|||Strongly decreased hyaluronidase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000289973 http://togogenome.org/gene/10090:Or4k51 ^@ http://purl.uniprot.org/uniprot/Q8VGE7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H2al1g ^@ http://purl.uniprot.org/uniprot/Q5M8Q2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Histone H2A-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000440627 http://togogenome.org/gene/10090:Slc13a2 ^@ http://purl.uniprot.org/uniprot/Q9ES88 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Solute carrier family 13 member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000172489 http://togogenome.org/gene/10090:Bcr ^@ http://purl.uniprot.org/uniprot/A2RRK7|||http://purl.uniprot.org/uniprot/Q6PAJ1 ^@ 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 ^@ Binding to ABL SH2-domain|||Breakpoint cluster region protein|||C2|||DH|||Disordered|||Kinase|||N-acetylmethionine|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FES|||Phosphotyrosine; by HCK|||Polar residues|||Pro residues|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000273731 http://togogenome.org/gene/10090:Llgl2 ^@ http://purl.uniprot.org/uniprot/J3QJU5|||http://purl.uniprot.org/uniprot/Q3TJ91|||http://purl.uniprot.org/uniprot/Q8BVC8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic residues|||Disordered|||LLGL scribble cell polarity complex component 2|||Lethal giant larvae homologue 2|||Phosphoserine|||Polar residues|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000232729 http://togogenome.org/gene/10090:Kcnc2 ^@ http://purl.uniprot.org/uniprot/A0A1W2P796|||http://purl.uniprot.org/uniprot/Q14B80 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Topological Domain|||Transmembrane ^@ BTB|||Cytoplasmic|||Disordered|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Potassium voltage-gated channel subfamily C member 2|||Pro residues|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000310417 http://togogenome.org/gene/10090:Vmn1r58 ^@ http://purl.uniprot.org/uniprot/G3X9U3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mgat5 ^@ http://purl.uniprot.org/uniprot/Q059T5|||http://purl.uniprot.org/uniprot/Q8R4G6 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A|||Sufficient for catalytic activity ^@ http://purl.uniprot.org/annotation/PRO_0000080523|||http://purl.uniprot.org/annotation/PRO_0000445693 http://togogenome.org/gene/10090:Alkbh3 ^@ http://purl.uniprot.org/uniprot/Q8K1E6 ^@ 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 ^@ (4R)-5-hydroxyleucine; alternate|||(4R)-5-oxoleucine; alternate|||Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3|||Disordered|||Fe2OG dioxygenase|||Loss of activity.|||Polar residues|||Reduced activity. ^@ http://purl.uniprot.org/annotation/PRO_0000239279 http://togogenome.org/gene/10090:Spin1 ^@ http://purl.uniprot.org/uniprot/Q3TLF7|||http://purl.uniprot.org/uniprot/Q61142 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Chain|||Crosslink|||Modified Residue|||Region|||Site|||Splice Variant ^@ 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|||In isoform 2.|||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_0000181368|||http://purl.uniprot.org/annotation/VSP_017942 http://togogenome.org/gene/10090:Wdr82 ^@ http://purl.uniprot.org/uniprot/B2RXQ8|||http://purl.uniprot.org/uniprot/Q8BFQ4 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 82 ^@ http://purl.uniprot.org/annotation/PRO_0000279686 http://togogenome.org/gene/10090:Ppp1r12a ^@ http://purl.uniprot.org/uniprot/Q9DBR7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Splice Variant ^@ (3S)-3-hydroxyasparagine; by HIF1AN|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with ROCK2|||KVKF motif|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000067026|||http://purl.uniprot.org/annotation/VSP_038478 http://togogenome.org/gene/10090:Rnf133 ^@ http://purl.uniprot.org/uniprot/Q14B02 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNF133|||Helical|||In isoform 2.|||PA|||Polar residues|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000380751|||http://purl.uniprot.org/annotation/VSP_037829 http://togogenome.org/gene/10090:Kcnk16 ^@ http://purl.uniprot.org/uniprot/G5E845 ^@ Domain Extent|||Glycosylation Site|||Modification|||Region|||Transmembrane ^@ Domain Extent|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Potassium channel ^@ http://togogenome.org/gene/10090:Or5w15 ^@ http://purl.uniprot.org/uniprot/Q8VFQ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hnf4a ^@ http://purl.uniprot.org/uniprot/B9VVT5|||http://purl.uniprot.org/uniprot/B9VVT6|||http://purl.uniprot.org/uniprot/P49698 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 9aaTAD|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hepatocyte nuclear factor 4-alpha|||In isoform Short.|||N6-acetyllysine|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000053559|||http://purl.uniprot.org/annotation/VSP_003676 http://togogenome.org/gene/10090:Emd ^@ http://purl.uniprot.org/uniprot/A2AM95|||http://purl.uniprot.org/uniprot/O08579 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Emerin|||Helical|||Interaction with CTNNB1|||Interaction with F-actin|||LEM|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000206141 http://togogenome.org/gene/10090:Pigl ^@ http://purl.uniprot.org/uniprot/Q5SX19 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase ^@ http://purl.uniprot.org/annotation/PRO_0000307824 http://togogenome.org/gene/10090:Ostf1 ^@ http://purl.uniprot.org/uniprot/Q62422 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat ^@ ANK 1|||ANK 2|||ANK 3|||Disordered|||N-acetylserine|||Osteoclast-stimulating factor 1|||Phosphoserine|||Phosphothreonine|||Removed|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000067036 http://togogenome.org/gene/10090:Or4c103 ^@ http://purl.uniprot.org/uniprot/Q8VG21 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:BC048679 ^@ http://purl.uniprot.org/uniprot/Q6XL63 ^@ Domain Extent|||Region ^@ Domain Extent ^@ NlpC/P60 ^@ http://togogenome.org/gene/10090:Med12l ^@ http://purl.uniprot.org/uniprot/A0A0G2JET8|||http://purl.uniprot.org/uniprot/Q8BQM9 ^@ 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.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Mediator complex subunit Med12|||Mediator of RNA polymerase II transcription subunit 12-like protein|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000313054|||http://purl.uniprot.org/annotation/VSP_029998|||http://purl.uniprot.org/annotation/VSP_029999|||http://purl.uniprot.org/annotation/VSP_030000|||http://purl.uniprot.org/annotation/VSP_030001|||http://purl.uniprot.org/annotation/VSP_030002|||http://purl.uniprot.org/annotation/VSP_030003 http://togogenome.org/gene/10090:Rgs18 ^@ http://purl.uniprot.org/uniprot/Q544K2|||http://purl.uniprot.org/uniprot/Q99PG4 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Phosphoserine|||RGS|||Regulator of G-protein signaling 18 ^@ http://purl.uniprot.org/annotation/PRO_0000204228 http://togogenome.org/gene/10090:Nfatc1 ^@ http://purl.uniprot.org/uniprot/B5B2N2|||http://purl.uniprot.org/uniprot/B5B2N4|||http://purl.uniprot.org/uniprot/B5B2N5|||http://purl.uniprot.org/uniprot/B5B2N7|||http://purl.uniprot.org/uniprot/Q6P7T9|||http://purl.uniprot.org/uniprot/Q9DBQ6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Pro residues|||RHD ^@ http://togogenome.org/gene/10090:Aldh18a1 ^@ http://purl.uniprot.org/uniprot/Q9Z110 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Delta-1-pyrroline-5-carboxylate synthase|||Gamma-glutamyl phosphate reductase|||Glutamate 5-kinase|||In isoform Short.|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000109770|||http://purl.uniprot.org/annotation/VSP_005216 http://togogenome.org/gene/10090:Coq2 ^@ http://purl.uniprot.org/uniprot/Q66JT7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ 4-hydroxybenzoate polyprenyltransferase, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000228624 http://togogenome.org/gene/10090:Mtf1 ^@ http://purl.uniprot.org/uniprot/Q07243|||http://purl.uniprot.org/uniprot/Q8BSY2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ C2H2-type|||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|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000047221 http://togogenome.org/gene/10090:Cldn34a ^@ http://purl.uniprot.org/uniprot/G3UW52 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Mtmr7 ^@ http://purl.uniprot.org/uniprot/Q9Z2C9 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Myotubularin phosphatase|||Myotubularin-related protein 7|||Phosphocysteine intermediate|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000094941 http://togogenome.org/gene/10090:4932429P05Rik ^@ http://purl.uniprot.org/uniprot/A2ADI4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Serine/threonine-protein phosphatase 4 regulatory subunit 3-like central ^@ http://togogenome.org/gene/10090:Ddx28 ^@ http://purl.uniprot.org/uniprot/Q9CWT6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict ^@ 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_0000055035 http://togogenome.org/gene/10090:Ttf2 ^@ http://purl.uniprot.org/uniprot/Q5NC05 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||DEAH box|||Disordered|||GRF-type|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Polar residues|||Transcription termination factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000074377 http://togogenome.org/gene/10090:Abcg1 ^@ http://purl.uniprot.org/uniprot/Q0VDW9|||http://purl.uniprot.org/uniprot/Q64343 ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Topological Domain|||Transmembrane ^@ ABC transmembrane type-2|||ABC transporter|||ATP-binding cassette sub-family G member 1|||Cytoplasmic|||Extracellular|||Helical|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000093385 http://togogenome.org/gene/10090:Sema4f ^@ http://purl.uniprot.org/uniprot/Q9Z123 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||In strain: BALB/c.|||Loss of interaction with DLG4.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||PSI|||Phosphoserine|||Sema|||Semaphorin-4F ^@ http://purl.uniprot.org/annotation/PRO_0000032331 http://togogenome.org/gene/10090:Smad1 ^@ http://purl.uniprot.org/uniprot/P70340 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Disordered|||L3 loop|||MH1|||MH2|||Mothers against decapentaplegic homolog 1|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine; by MINK1, TNIK and MAP4K4|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000090848 http://togogenome.org/gene/10090:Ascl2 ^@ http://purl.uniprot.org/uniprot/O35885|||http://purl.uniprot.org/uniprot/Q3TJR9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Achaete-scute homolog 2|||BHLH|||Disordered|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127131 http://togogenome.org/gene/10090:Prdm5 ^@ http://purl.uniprot.org/uniprot/E9Q707|||http://purl.uniprot.org/uniprot/Q9CXE0 ^@ 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; degenerate|||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|||PR domain zinc finger protein 5|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000230794 http://togogenome.org/gene/10090:Wdr20 ^@ http://purl.uniprot.org/uniprot/Q3UWE6 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ Disordered|||Polar residues|||WD ^@ http://togogenome.org/gene/10090:Elavl1 ^@ http://purl.uniprot.org/uniprot/P70372 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Asymmetric dimethylarginine; by CARM1; alternate|||ELAV-like protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylserine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||RRM 1|||RRM 2|||RRM 3|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000081578 http://togogenome.org/gene/10090:Snx21 ^@ http://purl.uniprot.org/uniprot/Q149Q9|||http://purl.uniprot.org/uniprot/Q3UR97 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Abolishes location on endosome membranes. Abolishes binding to membranes enriched in phosphatidylinositol 3-phosphate. No significant effect on binding to membranes enriched in phosphatidylinositol 4,5-bisphosphate.|||Acidic residues|||Disordered|||PX|||Sorting nexin-21 ^@ http://purl.uniprot.org/annotation/PRO_0000434600 http://togogenome.org/gene/10090:Arap1 ^@ http://purl.uniprot.org/uniprot/E9PUB0|||http://purl.uniprot.org/uniprot/Q4LDD4 ^@ 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 ^@ Arf-GAP|||Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1|||C4-type|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||PH|||PH 1|||PH 2|||PH 3|||PH 4|||Phosphoserine|||Phosphotyrosine|||Pro residues|||Ras-associating|||Rho-GAP|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000367029|||http://purl.uniprot.org/annotation/VSP_053047|||http://purl.uniprot.org/annotation/VSP_053048 http://togogenome.org/gene/10090:Sp7 ^@ http://purl.uniprot.org/uniprot/Q2KHK9|||http://purl.uniprot.org/uniprot/Q5RM08|||http://purl.uniprot.org/uniprot/Q8VI67 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ 9aaTAD|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Decreased propionylation, leading to increased transcription activator activity.|||Decreased propionylation.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N6-propionyllysine|||Transcription factor Sp7 ^@ http://purl.uniprot.org/annotation/PRO_0000047151 http://togogenome.org/gene/10090:Styx ^@ http://purl.uniprot.org/uniprot/Q60969 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Confers phosphatase activity.|||Disordered|||In isoform 2.|||Interaction with FBXW7|||Phosphoserine|||Serine/threonine/tyrosine-interacting protein|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094951|||http://purl.uniprot.org/annotation/VSP_005174 http://togogenome.org/gene/10090:Polh ^@ http://purl.uniprot.org/uniprot/Q9JJN0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Motif|||Region|||Zinc Finger ^@ DNA polymerase eta|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||PIP-box|||Polar residues|||UBZ3-type|||UmuC ^@ http://purl.uniprot.org/annotation/PRO_0000173987 http://togogenome.org/gene/10090:Klk1b27 ^@ http://purl.uniprot.org/uniprot/Q9JM71 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Kallikrein 1-related peptidase b27|||Loss of chymotryptic specificity and acquisition of trypsin-like cleavage specificity.|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027995|||http://purl.uniprot.org/annotation/PRO_0000027996 http://togogenome.org/gene/10090:Rab3d ^@ http://purl.uniprot.org/uniprot/P35276|||http://purl.uniprot.org/uniprot/Q543Q4 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region ^@ Cysteine methyl ester|||Disordered|||Effector region|||N-acetylalanine|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-3D|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121089 http://togogenome.org/gene/10090:Ubn2 ^@ http://purl.uniprot.org/uniprot/Q80WC1 ^@ 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.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Ubinuclein-2 ^@ http://purl.uniprot.org/annotation/PRO_0000295726|||http://purl.uniprot.org/annotation/VSP_027023|||http://purl.uniprot.org/annotation/VSP_027024|||http://purl.uniprot.org/annotation/VSP_027025|||http://purl.uniprot.org/annotation/VSP_027026|||http://purl.uniprot.org/annotation/VSP_027027|||http://purl.uniprot.org/annotation/VSP_027028|||http://purl.uniprot.org/annotation/VSP_027029 http://togogenome.org/gene/10090:Or5d35 ^@ http://purl.uniprot.org/uniprot/Q7TR29 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Enpp5 ^@ http://purl.uniprot.org/uniprot/Q5FWJ8|||http://purl.uniprot.org/uniprot/Q9EQG7 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Can hydrolyze nucleotides, with about fourfold higher rates for adenine versus uridine and no strong preference for diphosphates or triphosphates.|||Catalytically inactive.|||Ectonucleotide pyrophosphatase/phosphodiesterase family member 5|||Helical|||N-linked (GlcNAc...) asparagine|||No effect on its ability to hydrolyze NAD.|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000036402 http://togogenome.org/gene/10090:Fbxo5 ^@ http://purl.uniprot.org/uniprot/Q7TSG3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||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 phosphorylation by RPS6KA2.|||Does not affect phosphorylation by RPS6KA2.|||F-box|||F-box only protein 5|||Inhibits APC ubiquitin ligase activity|||Interaction with EVI5|||Phosphoserine|||Requires for efficient binding to CDC20|||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_0000258008 http://togogenome.org/gene/10090:Tet3 ^@ http://purl.uniprot.org/uniprot/A0A5K1VVP6|||http://purl.uniprot.org/uniprot/Q8BG87 ^@ 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Asymmetric dimethylarginine|||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 isoform 1.|||In isoform 2.|||Interaction with DNA|||Loss of enzyme activity; when associated with A-1087.|||Loss of enzyme activity; when associated with Y-1085.|||Methylcytosine dioxygenase TET1-3 oxygenase|||Methylcytosine dioxygenase TET3|||Polar residues|||Pro residues|||Strongly decreases ubiquitination, loss of DNA-binding and of 5-methylcytosine demethylase activity in vivo. Loss of nuclear localization, becomes mostly cytoplasmic. ^@ http://purl.uniprot.org/annotation/PRO_0000340228|||http://purl.uniprot.org/annotation/VSP_060404|||http://purl.uniprot.org/annotation/VSP_060405|||http://purl.uniprot.org/annotation/VSP_060406|||http://purl.uniprot.org/annotation/VSP_060407 http://togogenome.org/gene/10090:Btbd35f28 ^@ http://purl.uniprot.org/uniprot/A2CFD5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Rbm3 ^@ http://purl.uniprot.org/uniprot/O89086|||http://purl.uniprot.org/uniprot/Q545K5|||http://purl.uniprot.org/uniprot/Q5RJV3|||http://purl.uniprot.org/uniprot/Q8BG13 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||RNA-binding protein 3|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081753 http://togogenome.org/gene/10090:Park7 ^@ http://purl.uniprot.org/uniprot/Q99LX0 ^@ Active Site|||Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Site ^@ Cleavage; by CASP6|||Cysteine sulfinic acid (-SO2H); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||No sulfinic acid detected following treatment with hydrogen peroxide.|||Nucleophile|||Parkinson disease protein 7 homolog|||Phosphotyrosine|||Removed|||Removed in mature form|||S-palmitoyl cysteine|||S-palmitoyl cysteine; alternate|||Sulfinic acid detected following treatment with hydrogen peroxide. ^@ http://purl.uniprot.org/annotation/PRO_0000157850|||http://purl.uniprot.org/annotation/PRO_0000405560 http://togogenome.org/gene/10090:Tpt1 ^@ http://purl.uniprot.org/uniprot/P63028 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Phosphoserine|||Phosphoserine; by PLK1|||Required for reduction of TSC22D1 protein stability|||TCTP|||Translationally-controlled tumor protein ^@ http://purl.uniprot.org/annotation/PRO_0000211269 http://togogenome.org/gene/10090:Vmn1r217 ^@ http://purl.uniprot.org/uniprot/Q8R270 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gabrg2 ^@ http://purl.uniprot.org/uniprot/P22723 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit gamma-2|||Helical|||In isoform 2S.|||In strain: DBA/2J.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKC ^@ http://purl.uniprot.org/annotation/PRO_0000000478|||http://purl.uniprot.org/annotation/VSP_000091 http://togogenome.org/gene/10090:Man2c1 ^@ http://purl.uniprot.org/uniprot/Q91W89 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Alpha-mannosidase 2C1|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000206908 http://togogenome.org/gene/10090:Ndfip2 ^@ http://purl.uniprot.org/uniprot/M0QWK1|||http://purl.uniprot.org/uniprot/Q3V1V0 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Or10d1b ^@ http://purl.uniprot.org/uniprot/Q60888 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||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|||Olfactory receptor 10D1B ^@ http://purl.uniprot.org/annotation/PRO_0000150826 http://togogenome.org/gene/10090:Cgref1 ^@ http://purl.uniprot.org/uniprot/E9QPK1|||http://purl.uniprot.org/uniprot/Q8R1U2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Cell growth regulator with EF hand domain protein 1|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000073875|||http://purl.uniprot.org/annotation/PRO_5035299773 http://togogenome.org/gene/10090:Or14a256 ^@ http://purl.uniprot.org/uniprot/F7CWV4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp202 ^@ http://purl.uniprot.org/uniprot/Q8C879 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||Polar residues|||SCAN box ^@ http://togogenome.org/gene/10090:Stap1 ^@ http://purl.uniprot.org/uniprot/A0A0H2UKC0|||http://purl.uniprot.org/uniprot/Q9JM90 ^@ 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.|||PH|||Phosphotyrosine|||SH2|||Signal-transducing adaptor protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072238|||http://purl.uniprot.org/annotation/VSP_013399|||http://purl.uniprot.org/annotation/VSP_013400 http://togogenome.org/gene/10090:Cyp2d34 ^@ http://purl.uniprot.org/uniprot/L7N463 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Use1 ^@ http://purl.uniprot.org/uniprot/E9Q496|||http://purl.uniprot.org/uniprot/Q9CQ56 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Lumenal|||Vesicle transport protein USE1 ^@ http://purl.uniprot.org/annotation/PRO_0000215580|||http://purl.uniprot.org/annotation/VSP_012666|||http://purl.uniprot.org/annotation/VSP_012667 http://togogenome.org/gene/10090:Chodl ^@ http://purl.uniprot.org/uniprot/Q9CXM0 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000017416|||http://purl.uniprot.org/annotation/VSP_058918 http://togogenome.org/gene/10090:Rab20 ^@ http://purl.uniprot.org/uniprot/P35295|||http://purl.uniprot.org/uniprot/Q3TPA7 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Motif|||Region ^@ Disordered|||Effector region|||Ras-related protein Rab-20|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121203 http://togogenome.org/gene/10090:1700029H14Rik ^@ http://purl.uniprot.org/uniprot/G3X906|||http://purl.uniprot.org/uniprot/Q9D9Y4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or5w19 ^@ http://purl.uniprot.org/uniprot/Q7TR34 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp646 ^@ http://purl.uniprot.org/uniprot/Q6NV66 ^@ 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 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; degenerate|||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; degenerate|||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 646 ^@ http://purl.uniprot.org/annotation/PRO_0000447436 http://togogenome.org/gene/10090:Akt1s1 ^@ http://purl.uniprot.org/uniprot/E9QKI5|||http://purl.uniprot.org/uniprot/Q9D1F4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region ^@ Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Proline-rich AKT1 substrate 1|||TOS motif ^@ http://purl.uniprot.org/annotation/PRO_0000253447 http://togogenome.org/gene/10090:Dipk1a ^@ http://purl.uniprot.org/uniprot/Q9D6I7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Divergent protein kinase domain 1A|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000282424 http://togogenome.org/gene/10090:Hoxd1 ^@ http://purl.uniprot.org/uniprot/Q01822 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Motif|||Region|||Sequence Conflict ^@ Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-D1 ^@ http://purl.uniprot.org/annotation/PRO_0000200202 http://togogenome.org/gene/10090:Hhat ^@ http://purl.uniprot.org/uniprot/Q8BMT9 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||INTRAMEM|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||INTRAMEM|||Lipid Binding|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Essential for palmitoylation of SHH|||Helical|||In isoform 2.|||Lumenal|||Protein-cysteine N-palmitoyltransferase HHAT|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000213135|||http://purl.uniprot.org/annotation/VSP_016690|||http://purl.uniprot.org/annotation/VSP_016691 http://togogenome.org/gene/10090:Tmem181a ^@ http://purl.uniprot.org/uniprot/Q3U3W2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Wntless-like transmembrane ^@ http://togogenome.org/gene/10090:Rnf151 ^@ http://purl.uniprot.org/uniprot/Q9CQ29 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Zinc Finger ^@ RING finger protein 151|||RING-type|||TRAF-type ^@ http://purl.uniprot.org/annotation/PRO_0000255255 http://togogenome.org/gene/10090:Dbr1 ^@ http://purl.uniprot.org/uniprot/Q923B1 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Lariat debranching enzyme|||Lariat recognition loop|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000250359 http://togogenome.org/gene/10090:Ankrd60 ^@ http://purl.uniprot.org/uniprot/A2AMD2 ^@ Domain Extent|||Region|||Repeat ^@ Domain Extent|||Region|||Repeat ^@ ANK|||Disordered|||Ubiquitin-like ^@ http://togogenome.org/gene/10090:Itk ^@ http://purl.uniprot.org/uniprot/A1A560|||http://purl.uniprot.org/uniprot/Q03526|||http://purl.uniprot.org/uniprot/Q3U5G1|||http://purl.uniprot.org/uniprot/Q5STT7|||http://purl.uniprot.org/uniprot/Q5STT8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Btk-type|||Disordered|||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_0000088107 http://togogenome.org/gene/10090:H4c12 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Lzts2 ^@ http://purl.uniprot.org/uniprot/Q91YU6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||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_0000182975 http://togogenome.org/gene/10090:Tmem230 ^@ http://purl.uniprot.org/uniprot/Q8CIB6 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Phosphoserine|||Transmembrane protein 230 ^@ http://purl.uniprot.org/annotation/PRO_0000233893 http://togogenome.org/gene/10090:Rnf207 ^@ http://purl.uniprot.org/uniprot/Q3V3A7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Zinc Finger ^@ B box-type; atypical|||Basic and acidic residues|||Disordered|||Polar residues|||RING finger protein 207|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000300810 http://togogenome.org/gene/10090:Defa25 ^@ http://purl.uniprot.org/uniprot/Q5G864 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Alpha-defensin 25|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000300076|||http://purl.uniprot.org/annotation/PRO_0000300077 http://togogenome.org/gene/10090:St8sia4 ^@ http://purl.uniprot.org/uniprot/A0A087WRA0|||http://purl.uniprot.org/uniprot/Q53WR7|||http://purl.uniprot.org/uniprot/Q64692|||http://purl.uniprot.org/uniprot/Q6PAS1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000149294|||http://purl.uniprot.org/annotation/PRO_5001831838|||http://purl.uniprot.org/annotation/PRO_5004278350|||http://purl.uniprot.org/annotation/PRO_5010139245 http://togogenome.org/gene/10090:Prss45 ^@ http://purl.uniprot.org/uniprot/Q8K4I7 ^@ 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.|||Inactive serine protease 45|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000349308|||http://purl.uniprot.org/annotation/VSP_035356 http://togogenome.org/gene/10090:Col13a1 ^@ http://purl.uniprot.org/uniprot/D3Z7B8|||http://purl.uniprot.org/uniprot/Q9R1N9 ^@ 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|||Collagen alpha-1(XIII) chain|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||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_0000284680|||http://purl.uniprot.org/annotation/VSP_052388 http://togogenome.org/gene/10090:Usp14 ^@ http://purl.uniprot.org/uniprot/E9PYI8|||http://purl.uniprot.org/uniprot/Q9JMA1 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ N6-acetyllysine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 14|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000080637 http://togogenome.org/gene/10090:1700088E04Rik ^@ http://purl.uniprot.org/uniprot/B7ZMP0|||http://purl.uniprot.org/uniprot/Q4V9V4|||http://purl.uniprot.org/uniprot/Q9D9S1 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||UPF0193 protein EVG1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000221090 http://togogenome.org/gene/10090:Skic3 ^@ http://purl.uniprot.org/uniprot/F8VPK0 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat ^@ 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 21|||TPR 22|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9 ^@ http://purl.uniprot.org/annotation/PRO_0000458137 http://togogenome.org/gene/10090:Sytl3 ^@ http://purl.uniprot.org/uniprot/E9PUK9|||http://purl.uniprot.org/uniprot/Q0VF85|||http://purl.uniprot.org/uniprot/Q99N48 ^@ 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 ^@ Basic and acidic residues|||Binds phospholipids only in the absence of divalent cations.|||C2|||C2 1|||C2 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||RabBD|||Synaptotagmin-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000190215|||http://purl.uniprot.org/annotation/VSP_007895|||http://purl.uniprot.org/annotation/VSP_007896|||http://purl.uniprot.org/annotation/VSP_007897|||http://purl.uniprot.org/annotation/VSP_007898|||http://purl.uniprot.org/annotation/VSP_007899 http://togogenome.org/gene/10090:Pot1b ^@ http://purl.uniprot.org/uniprot/H7BX60 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Telomeric single stranded DNA binding POT1/Cdc13 ^@ http://togogenome.org/gene/10090:Fam161a ^@ http://purl.uniprot.org/uniprot/B1AVK0|||http://purl.uniprot.org/uniprot/Q8QZV6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Protein FAM161A|||Required for interaction with CFAP418 ^@ http://purl.uniprot.org/annotation/PRO_0000329053 http://togogenome.org/gene/10090:H2bl1 ^@ http://purl.uniprot.org/uniprot/Q9D9Z7 ^@ Chain|||Molecule Processing ^@ Chain ^@ Histone H2B variant L1 ^@ http://purl.uniprot.org/annotation/PRO_0000244839 http://togogenome.org/gene/10090:Or5m10b ^@ http://purl.uniprot.org/uniprot/L7MTT3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:2310022B05Rik ^@ http://purl.uniprot.org/uniprot/Q8C3W1 ^@ 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 and acidic residues|||Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Uncharacterized protein C1orf198 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000280343 http://togogenome.org/gene/10090:Golim4 ^@ http://purl.uniprot.org/uniprot/D3YVW2|||http://purl.uniprot.org/uniprot/Q8BXA1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||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|||Lumenal|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000285098 http://togogenome.org/gene/10090:Dlg1 ^@ http://purl.uniprot.org/uniprot/D3Z3B8|||http://purl.uniprot.org/uniprot/E9Q9H0|||http://purl.uniprot.org/uniprot/H7BWY4|||http://purl.uniprot.org/uniprot/Q3UP61|||http://purl.uniprot.org/uniprot/Q811D0 ^@ 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|||Disks large homolog 1|||Disordered|||Guanylate kinase-like|||In isoform 2.|||In isoform 3.|||Interaction with SH3 domains|||L27|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Required for interaction with MARCHF2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000094549|||http://purl.uniprot.org/annotation/VSP_012866|||http://purl.uniprot.org/annotation/VSP_012867|||http://purl.uniprot.org/annotation/VSP_012868 http://togogenome.org/gene/10090:Pcyt2 ^@ http://purl.uniprot.org/uniprot/A2ABY3|||http://purl.uniprot.org/uniprot/Q3USD5|||http://purl.uniprot.org/uniprot/Q922E4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Cytidyltransferase-like|||Disordered|||Ethanolamine-phosphate cytidylyltransferase|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000208462 http://togogenome.org/gene/10090:Rchy1 ^@ http://purl.uniprot.org/uniprot/G3UWD8|||http://purl.uniprot.org/uniprot/Q9CR50 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Strand|||Turn|||Zinc Finger ^@ CHY-type|||CTCHY-type|||RING finger and CHY zinc finger domain-containing protein 1|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056313 http://togogenome.org/gene/10090:Zfp972 ^@ http://purl.uniprot.org/uniprot/A2AW64 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Or13a17 ^@ http://purl.uniprot.org/uniprot/Q8VGM1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ano9 ^@ http://purl.uniprot.org/uniprot/P86044 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Anoctamin-9|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000353191 http://togogenome.org/gene/10090:Vmn1r4 ^@ http://purl.uniprot.org/uniprot/Q8R2D3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp869 ^@ http://purl.uniprot.org/uniprot/Q8C0L3|||http://purl.uniprot.org/uniprot/Q9DC47 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Dnaaf3 ^@ http://purl.uniprot.org/uniprot/Q3UYV8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Dynein axonemal assembly factor 3|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000297582 http://togogenome.org/gene/10090:Fry ^@ http://purl.uniprot.org/uniprot/E9Q8I9|||http://purl.uniprot.org/uniprot/Q8BIX6 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||Loss of PLK1-binding.|||Loss of phosphorylation by CDK1. Loss of PLK1-binding.|||Phosphoserine|||Phosphothreonine; by CDK1|||Phosphotyrosine|||Polar residues|||Protein furry C-terminal|||Protein furry homolog ^@ http://purl.uniprot.org/annotation/PRO_0000420369|||http://purl.uniprot.org/annotation/VSP_044441|||http://purl.uniprot.org/annotation/VSP_044442|||http://purl.uniprot.org/annotation/VSP_044443|||http://purl.uniprot.org/annotation/VSP_044444|||http://purl.uniprot.org/annotation/VSP_044445 http://togogenome.org/gene/10090:Tac1 ^@ http://purl.uniprot.org/uniprot/B7ZMQ2|||http://purl.uniprot.org/uniprot/P41539|||http://purl.uniprot.org/uniprot/Q149W7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide|||Site|||Splice Variant ^@ C-terminal-flanking peptide|||Cleavage; by ACE|||Cleavage; by ACE and MME|||Cleavage; by FAP|||Cleavage; by MME|||In isoform Gamma.|||Methionine amide|||Neurokinin A|||Neuropeptide K|||Neuropeptide gamma, 1st part|||Neuropeptide gamma, 2nd part|||Protachykinin-1|||Substance P|||Tachykinin ^@ http://purl.uniprot.org/annotation/PRO_0000033543|||http://purl.uniprot.org/annotation/PRO_0000033544|||http://purl.uniprot.org/annotation/PRO_0000033545|||http://purl.uniprot.org/annotation/PRO_0000033546|||http://purl.uniprot.org/annotation/PRO_0000033547|||http://purl.uniprot.org/annotation/PRO_0000033548|||http://purl.uniprot.org/annotation/PRO_0000033549|||http://purl.uniprot.org/annotation/PRO_5014300194|||http://purl.uniprot.org/annotation/PRO_5014306904|||http://purl.uniprot.org/annotation/VSP_006379 http://togogenome.org/gene/10090:Asb14 ^@ http://purl.uniprot.org/uniprot/A0A0R4J236|||http://purl.uniprot.org/uniprot/E9QPD0|||http://purl.uniprot.org/uniprot/Q8C6Y6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict|||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|||Ankyrin repeat and SOCS box protein 14|||In isoform 2.|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000370366|||http://purl.uniprot.org/annotation/VSP_036929|||http://purl.uniprot.org/annotation/VSP_036930 http://togogenome.org/gene/10090:Prl3d2 ^@ http://purl.uniprot.org/uniprot/Q8CGZ8 ^@ Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099097 http://togogenome.org/gene/10090:Slc1a6 ^@ http://purl.uniprot.org/uniprot/B2RQX4|||http://purl.uniprot.org/uniprot/O35544|||http://purl.uniprot.org/uniprot/Q3TXM3 ^@ Binding Site|||Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Discontinuously helical|||Excitatory amino acid transporter 4|||Helical|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000202071 http://togogenome.org/gene/10090:Med21 ^@ http://purl.uniprot.org/uniprot/Q9CQ39 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Mediator of RNA polymerase II transcription subunit 21 ^@ http://purl.uniprot.org/annotation/PRO_0000305947 http://togogenome.org/gene/10090:Or8c9 ^@ http://purl.uniprot.org/uniprot/Q7TRD6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zpbp ^@ http://purl.uniprot.org/uniprot/B7ZP49|||http://purl.uniprot.org/uniprot/Q5NC84|||http://purl.uniprot.org/uniprot/Q62522 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Polar residues|||Zona pellucida-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000041599 http://togogenome.org/gene/10090:Fam170b ^@ http://purl.uniprot.org/uniprot/E9PXT9|||http://purl.uniprot.org/uniprot/Q08ED8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Pro residues|||Protein FAM170B ^@ http://purl.uniprot.org/annotation/PRO_0000435474 http://togogenome.org/gene/10090:Ccdc110 ^@ http://purl.uniprot.org/uniprot/Q3V125 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Coiled-coil domain-containing protein 110|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000249078 http://togogenome.org/gene/10090:Or8k39 ^@ http://purl.uniprot.org/uniprot/A0A1L1SRK6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kifc3 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLM0|||http://purl.uniprot.org/uniprot/E9PWU7|||http://purl.uniprot.org/uniprot/O35231 ^@ 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 ^@ Disordered|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIFC3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000125432|||http://purl.uniprot.org/annotation/VSP_022363|||http://purl.uniprot.org/annotation/VSP_022364 http://togogenome.org/gene/10090:Mug2 ^@ http://purl.uniprot.org/uniprot/P28666 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Bait region|||Basic and acidic residues|||Disordered|||Isoglutamyl cysteine thioester (Cys-Gln)|||Murinoglobulin-2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000000060 http://togogenome.org/gene/10090:Trappc6a ^@ http://purl.uniprot.org/uniprot/Q78XR0 ^@ 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|||Trafficking protein particle complex subunit 6A ^@ http://purl.uniprot.org/annotation/PRO_0000211586|||http://purl.uniprot.org/annotation/VSP_019586 http://togogenome.org/gene/10090:Itpka ^@ http://purl.uniprot.org/uniprot/Q8R071 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Calmodulin-binding|||Disordered|||Inositol-trisphosphate 3-kinase A|||Omega-N-methylarginine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000066866 http://togogenome.org/gene/10090:Samd14 ^@ http://purl.uniprot.org/uniprot/Q8K070 ^@ 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|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM|||Sterile alpha motif domain-containing protein 14 ^@ http://purl.uniprot.org/annotation/PRO_0000250564 http://togogenome.org/gene/10090:Ccdc121 ^@ http://purl.uniprot.org/uniprot/Q9D496 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ DUF4515 ^@ http://togogenome.org/gene/10090:Frg1 ^@ http://purl.uniprot.org/uniprot/P97376|||http://purl.uniprot.org/uniprot/Q78P92 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ Bipartite nuclear localization signal|||Disordered|||Nuclear localization signal|||Protein FRG1 ^@ http://purl.uniprot.org/annotation/PRO_0000220768 http://togogenome.org/gene/10090:Anxa9 ^@ http://purl.uniprot.org/uniprot/Q9JHQ0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A9 ^@ http://purl.uniprot.org/annotation/PRO_0000067506 http://togogenome.org/gene/10090:Cthrc1 ^@ http://purl.uniprot.org/uniprot/Q9D1D6 ^@ 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 ^@ Collagen triple helix repeat-containing protein 1|||Collagen-like|||Disordered|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000021039 http://togogenome.org/gene/10090:Vmn2r107 ^@ http://purl.uniprot.org/uniprot/E9PZJ7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003243041 http://togogenome.org/gene/10090:Ablim1 ^@ http://purl.uniprot.org/uniprot/E9Q030|||http://purl.uniprot.org/uniprot/E9Q9C0|||http://purl.uniprot.org/uniprot/E9Q9C1|||http://purl.uniprot.org/uniprot/E9Q9C7|||http://purl.uniprot.org/uniprot/E9Q9D1|||http://purl.uniprot.org/uniprot/E9QK41|||http://purl.uniprot.org/uniprot/Q3UP03|||http://purl.uniprot.org/uniprot/Q8K4G5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||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 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||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_0000075698|||http://purl.uniprot.org/annotation/VSP_012103|||http://purl.uniprot.org/annotation/VSP_012104|||http://purl.uniprot.org/annotation/VSP_012105|||http://purl.uniprot.org/annotation/VSP_012106|||http://purl.uniprot.org/annotation/VSP_012107|||http://purl.uniprot.org/annotation/VSP_012108|||http://purl.uniprot.org/annotation/VSP_012109|||http://purl.uniprot.org/annotation/VSP_012110|||http://purl.uniprot.org/annotation/VSP_012111 http://togogenome.org/gene/10090:Tomm7 ^@ http://purl.uniprot.org/uniprot/Q9D173 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Mitochondrial import receptor subunit TOM7 homolog|||Mitochondrial intermembrane ^@ http://purl.uniprot.org/annotation/PRO_0000046760 http://togogenome.org/gene/10090:Thop1 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZY0|||http://purl.uniprot.org/uniprot/Q8C1A5 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ N6-acetyllysine|||Peptidase M3A/M3B catalytic|||Phosphoserine|||Phosphotyrosine|||Thimet oligopeptidase ^@ http://purl.uniprot.org/annotation/PRO_0000319044 http://togogenome.org/gene/10090:Mcf2 ^@ http://purl.uniprot.org/uniprot/A2AET8|||http://purl.uniprot.org/uniprot/Q8BLE2|||http://purl.uniprot.org/uniprot/Q8C067 ^@ Domain Extent|||Region ^@ Domain Extent ^@ CRAL-TRIO|||DH|||PH ^@ http://togogenome.org/gene/10090:Bnip1 ^@ http://purl.uniprot.org/uniprot/Q6QD59 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Lumenal|||Vesicle transport protein SEC20 ^@ http://purl.uniprot.org/annotation/PRO_0000232417 http://togogenome.org/gene/10090:Slc12a5 ^@ http://purl.uniprot.org/uniprot/A0A076FSX1|||http://purl.uniprot.org/uniprot/Q91V14 ^@ 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|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Amino acid permease/ SLC12A|||Basic and acidic residues|||Cytoplasmic|||Decreases endocytosis.|||Discontinuously helical|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Inhibits endocytosis. Abolishes interaction with AP2A1.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by OXSR1 and STK39|||SLC12A transporter C-terminal|||Solute carrier family 12 member 5 ^@ http://purl.uniprot.org/annotation/PRO_0000178035|||http://purl.uniprot.org/annotation/VSP_029910 http://togogenome.org/gene/10090:Gys2 ^@ http://purl.uniprot.org/uniprot/Q8VCB3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes phosphorylation. No effect on the interaction with GYG1. Does not affect the result of other mutations; when associated with A-135; R-135; R-141; A-239; A-243; or R-243.|||Acidic residues|||Basic residues|||Disordered|||Glycogen [starch] synthase, liver|||Loss of catalytic activity.|||Loss of interaction with GYG1. Loss of function. Loss of interaction with GYG1; when associated with A-8.|||Loss of interaction with GYG1. Loss of interaction with GYG1; when associated with A-8.|||No effect on the interaction with GYG1. Loss of interaction with GYG1; when associated with A-8.|||No effect on the interaction with GYG1. No effect on the interaction with GYG1; when associated with A-8.|||Phosphoserine|||Phosphoserine; by AMPK and PKA|||Phosphoserine; by CK2|||Phosphoserine; by GSK3-alpha and GSK3-beta ^@ http://purl.uniprot.org/annotation/PRO_0000274489 http://togogenome.org/gene/10090:Map3k13 ^@ http://purl.uniprot.org/uniprot/Q1HKZ5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||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_0000277591 http://togogenome.org/gene/10090:Erich2 ^@ http://purl.uniprot.org/uniprot/D3Z5X9|||http://purl.uniprot.org/uniprot/E9Q1A6|||http://purl.uniprot.org/uniprot/Q9D4B3 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Or4c120 ^@ http://purl.uniprot.org/uniprot/Q7TR01 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp105 ^@ http://purl.uniprot.org/uniprot/G3X9I0|||http://purl.uniprot.org/uniprot/Q80WR2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:E2f7 ^@ http://purl.uniprot.org/uniprot/Q6S7F2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Transcription factor E2F7 ^@ http://purl.uniprot.org/annotation/PRO_0000298908|||http://purl.uniprot.org/annotation/VSP_044618|||http://purl.uniprot.org/annotation/VSP_044619 http://togogenome.org/gene/10090:Zfp553 ^@ http://purl.uniprot.org/uniprot/Q3US17 ^@ 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 ^@ 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)|||N-acetylmethionine|||Phosphoserine|||Pro residues|||Zinc finger protein 48 ^@ http://purl.uniprot.org/annotation/PRO_0000234587 http://togogenome.org/gene/10090:Hivep3 ^@ http://purl.uniprot.org/uniprot/A2A884 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ 1|||2|||3|||4|||5|||5 X 4 AA tandem repeats of [ST]-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|||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_0000331628 http://togogenome.org/gene/10090:Banf2 ^@ http://purl.uniprot.org/uniprot/Q8BVR0 ^@ Chain|||Molecule Processing ^@ Chain ^@ Barrier-to-autointegration factor-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000223617 http://togogenome.org/gene/10090:Lonp1 ^@ http://purl.uniprot.org/uniprot/Q8CGK3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Lon N-terminal|||Lon protease homolog, mitochondrial|||Lon proteolytic|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000254961 http://togogenome.org/gene/10090:Fam167b ^@ http://purl.uniprot.org/uniprot/P17257 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Protein FAM167B ^@ http://purl.uniprot.org/annotation/PRO_0000221432 http://togogenome.org/gene/10090:Fgg ^@ http://purl.uniprot.org/uniprot/Q3UEM7|||http://purl.uniprot.org/uniprot/Q3UER8|||http://purl.uniprot.org/uniprot/Q8VCM7 ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Signal Peptide ^@ Fibrinogen C-terminal|||Fibrinogen C-terminal domain-containing protein|||Fibrinogen gamma chain|||Impairs induction of SELP in activated platelets.|||Interchain (with alpha chain)|||Interchain (with beta chain)|||Interchain (with gamma chain)|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-431)|||Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-423)|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000009100|||http://purl.uniprot.org/annotation/PRO_5009970834|||http://purl.uniprot.org/annotation/PRO_5015097484 http://togogenome.org/gene/10090:Prox2 ^@ http://purl.uniprot.org/uniprot/Q8BII1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeo-Prospero|||Polar residues|||Prospero|||Prospero homeobox protein 2|||Prospero-type homeo ^@ http://purl.uniprot.org/annotation/PRO_0000342678 http://togogenome.org/gene/10090:Mndal ^@ http://purl.uniprot.org/uniprot/D0QMC3 ^@ 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|||HIN-200|||In strain: BALB/cAn.|||Myeloid cell nuclear differentiation antigen-like protein|||Polar residues|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000391681 http://togogenome.org/gene/10090:Or8i2 ^@ http://purl.uniprot.org/uniprot/A2AVB5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccdc170 ^@ http://purl.uniprot.org/uniprot/F6ST92 ^@ Coiled-Coil|||Region ^@ Coiled-Coil ^@ ^@ http://togogenome.org/gene/10090:Tmtc4 ^@ http://purl.uniprot.org/uniprot/Q8BG19 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||In isoform 3.|||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_0000280296|||http://purl.uniprot.org/annotation/VSP_023624|||http://purl.uniprot.org/annotation/VSP_023625|||http://purl.uniprot.org/annotation/VSP_023626 http://togogenome.org/gene/10090:Caprin1 ^@ http://purl.uniprot.org/uniprot/Q60865 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine; alternate|||Caprin-1|||Disordered|||G3BP1-binding|||N-acetylproline|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087550 http://togogenome.org/gene/10090:Pdx1 ^@ http://purl.uniprot.org/uniprot/P52946 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Abnormal subnuclear localization upon glucose accumulation.|||Antp-type hexapeptide|||Disordered|||Displays a more cytosolic distribution.|||Homeobox|||Nuclear localization signal|||Pancreas/duodenum homeobox protein 1|||Phosphoserine; by HIPK2|||Phosphothreonine; by PASK|||Pro residues|||Reduced phosphorylation by HIPK2.|||Transactivation domain ^@ http://purl.uniprot.org/annotation/PRO_0000049149 http://togogenome.org/gene/10090:Pnliprp1 ^@ http://purl.uniprot.org/uniprot/Q5BKQ4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Inactive pancreatic lipase-related protein 1|||Nucleophile|||PLAT ^@ http://purl.uniprot.org/annotation/PRO_0000017791 http://togogenome.org/gene/10090:Bace2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0I8|||http://purl.uniprot.org/uniprot/Q9JL18 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Beta-secretase 2|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase A1 ^@ http://purl.uniprot.org/annotation/PRO_0000383646|||http://purl.uniprot.org/annotation/PRO_0000383647|||http://purl.uniprot.org/annotation/PRO_5006451978 http://togogenome.org/gene/10090:Lrrfip1 ^@ http://purl.uniprot.org/uniprot/A0A087WPK3|||http://purl.uniprot.org/uniprot/A6H5U5|||http://purl.uniprot.org/uniprot/G5E8E1|||http://purl.uniprot.org/uniprot/Q3UZ39|||http://purl.uniprot.org/uniprot/Q8BLV4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||In isoform 3.|||Leucine-rich repeat flightless-interacting protein 1|||N-acetylthreonine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000248393|||http://purl.uniprot.org/annotation/VSP_020266|||http://purl.uniprot.org/annotation/VSP_020267|||http://purl.uniprot.org/annotation/VSP_020268|||http://purl.uniprot.org/annotation/VSP_020269|||http://purl.uniprot.org/annotation/VSP_020270|||http://purl.uniprot.org/annotation/VSP_020271|||http://purl.uniprot.org/annotation/VSP_020272 http://togogenome.org/gene/10090:Gm15080 ^@ http://purl.uniprot.org/uniprot/A2BI02 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tmprss15 ^@ http://purl.uniprot.org/uniprot/E9Q6Y6|||http://purl.uniprot.org/uniprot/P97435|||http://purl.uniprot.org/uniprot/Q8CC97 ^@ 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 ^@ CUB|||CUB 1|||CUB 2|||Charge relay system|||Cytoplasmic|||Enteropeptidase catalytic light chain|||Enteropeptidase non-catalytic heavy chain|||Extracellular|||Helical|||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|||Peptidase S1|||SEA|||SRCR ^@ http://purl.uniprot.org/annotation/PRO_0000027721|||http://purl.uniprot.org/annotation/PRO_0000027722 http://togogenome.org/gene/10090:Nrbp1 ^@ http://purl.uniprot.org/uniprot/D3YUV1|||http://purl.uniprot.org/uniprot/Q99J45 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||N-acetylserine|||Nuclear receptor-binding protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000086451 http://togogenome.org/gene/10090:Ikbkg ^@ http://purl.uniprot.org/uniprot/E9Q2Y3|||http://purl.uniprot.org/uniprot/O88522|||http://purl.uniprot.org/uniprot/Q7TSS3|||http://purl.uniprot.org/uniprot/Q8VC91 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ 40% decrease in IL1-induced NF-kappa-B activation.|||Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-293 and A-301.|||Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-293 and A-302.|||Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-301 and A-302.|||Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs of NF-kappa-B activation.|||Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-309 and A-313.|||Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-312 and A-313.|||Abolishes linear polyubiquitin-binding; when associated with A-313 and A-317.|||Abolishes linear polyubiquitin-binding; when associated with A-313 and A-320.|||CCHC NOA-type|||Decreases phosphorylation and increases NF-kappa-B activity.|||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|||Impairs linear polyubiquitin-binding. Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-309 and A-312. Abolishes linear polyubiquitin-binding; when associated with A-317 and A-320.|||Interaction with CHUK/IKBKB|||Interaction with CYLD|||Interaction with TANK|||Interchain|||Leucine-zipper|||Linear polyubiquitin-binding, does not bind to 'Lys-63'-linked polyubiquitin|||Loss of interaction with TRAF6 and TRAF6-induced polyubiquitination.|||NF-kappa-B essential modulator|||Phosphoserine|||Phosphoserine; by ATM|||Phosphoserine; by IKKB|||Polar residues|||Required for interaction with TNFAIP3|||Required for interaction with and ubiquitination by MARCHF2|||Self-association|||Slight decrease in TRAF6-induced polyubiquitination.|||Slight decrease in TRAF6-induced polyubiquitination. Decrease in TRAF6-induced polyubiquitination; when associated with R-318. Important decrease in TRAF6-induced polyubiquitination; when associated with R-314 and R-318.|||Slight decrease in TRAF6-induced polyubiquitination. Decrease in TRAF6-induced polyubiquitination; when associated with R-319. Important decrease in TRAF6-induced polyubiquitination; when associated with R-314 and R-319.|||Slight decrease in TRAF6-induced polyubiquitination. Important decrease in TRAF6-induced polyubiquitination; when associated with R-318 and R-319.|||Ubiquitin-binding (UBAN) ^@ http://purl.uniprot.org/annotation/PRO_0000096783 http://togogenome.org/gene/10090:Zfp365 ^@ http://purl.uniprot.org/uniprot/Q8BG89 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C2H2-type; degenerate|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Protein ZNF365 ^@ http://purl.uniprot.org/annotation/PRO_0000076375|||http://purl.uniprot.org/annotation/VSP_016601|||http://purl.uniprot.org/annotation/VSP_016602 http://togogenome.org/gene/10090:Atp1a4 ^@ http://purl.uniprot.org/uniprot/Q9WV27 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with phosphoinositide-3 kinase|||Phosphoserine; by PKA|||Sodium/potassium-transporting ATPase subunit alpha-4 ^@ http://purl.uniprot.org/annotation/PRO_0000046304 http://togogenome.org/gene/10090:Slc2a8 ^@ http://purl.uniprot.org/uniprot/Q9JIF3 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Abolishes interaction with AP2B1.|||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|||N-linked (GlcNAc...) asparagine|||Solute carrier family 2, facilitated glucose transporter member 8 ^@ http://purl.uniprot.org/annotation/PRO_0000050376 http://togogenome.org/gene/10090:Crip3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1I1|||http://purl.uniprot.org/uniprot/A0A8Q0P6Q3|||http://purl.uniprot.org/uniprot/Q6Q6R3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Cysteine-rich protein 3|||Disordered|||In isoform 1.|||In isoform 2.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2 ^@ http://purl.uniprot.org/annotation/PRO_0000225639|||http://purl.uniprot.org/annotation/VSP_061232|||http://purl.uniprot.org/annotation/VSP_061233 http://togogenome.org/gene/10090:Acot11 ^@ http://purl.uniprot.org/uniprot/A2AVR6|||http://purl.uniprot.org/uniprot/Q543P6|||http://purl.uniprot.org/uniprot/Q8CAL6|||http://purl.uniprot.org/uniprot/Q8VHQ9 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Transit Peptide ^@ Acyl-coenzyme A thioesterase 11|||Disordered|||HotDog ACOT-type|||HotDog ACOT-type 1|||HotDog ACOT-type 2|||Mitochondrion|||Phosphoserine|||START ^@ http://purl.uniprot.org/annotation/PRO_0000053814 http://togogenome.org/gene/10090:Tmed7 ^@ http://purl.uniprot.org/uniprot/D3YZZ5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ GOLD|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003052559 http://togogenome.org/gene/10090:Gng10 ^@ http://purl.uniprot.org/uniprot/Q9CXP8 ^@ 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_0000012657|||http://purl.uniprot.org/annotation/PRO_0000012658 http://togogenome.org/gene/10090:Btbd35f25 ^@ http://purl.uniprot.org/uniprot/A0A571BG45 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Grm5 ^@ http://purl.uniprot.org/uniprot/B2BH30|||http://purl.uniprot.org/uniprot/B7ZMP7|||http://purl.uniprot.org/uniprot/E9QMC2|||http://purl.uniprot.org/uniprot/Q3UVX5|||http://purl.uniprot.org/uniprot/Q4VA56 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 isoform 2.|||Metabotropic glutamate receptor 5|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000306853|||http://purl.uniprot.org/annotation/PRO_5009947260|||http://purl.uniprot.org/annotation/PRO_5015090382|||http://purl.uniprot.org/annotation/VSP_028519|||http://purl.uniprot.org/annotation/VSP_028520 http://togogenome.org/gene/10090:Dpp4 ^@ http://purl.uniprot.org/uniprot/P28843|||http://purl.uniprot.org/uniprot/Q3TR43 ^@ 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|||Dipeptidyl peptidase 4 low complexity region|||Dipeptidyl peptidase 4 membrane form|||Dipeptidyl peptidase 4 soluble form|||Dipeptidylpeptidase IV N-terminal|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Peptidase S9 prolyl oligopeptidase catalytic ^@ http://purl.uniprot.org/annotation/PRO_0000027215|||http://purl.uniprot.org/annotation/PRO_0000027216 http://togogenome.org/gene/10090:Parp4 ^@ http://purl.uniprot.org/uniprot/E9PYK3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ BRCT|||Disordered|||FH1|||Interaction with the major vault protein|||Nuclear localization signal|||PARP alpha-helical|||PARP catalytic|||Phosphoserine|||Pro residues|||Protein mono-ADP-ribosyltransferase PARP4|||VIT|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000446171 http://togogenome.org/gene/10090:Amer3 ^@ http://purl.uniprot.org/uniprot/Q6NS69 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ APC membrane recruitment protein 3|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000320595 http://togogenome.org/gene/10090:Scgb1b10 ^@ http://purl.uniprot.org/uniprot/A0A087WPW0 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015029547 http://togogenome.org/gene/10090:Mrpl52 ^@ http://purl.uniprot.org/uniprot/Q9D0Y8 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transit Peptide ^@ Chain|||Region|||Splice Variant|||Transit Peptide ^@ Disordered|||In isoform 2.|||Large ribosomal subunit protein mL52|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000273094|||http://purl.uniprot.org/annotation/VSP_022476 http://togogenome.org/gene/10090:Obox6 ^@ http://purl.uniprot.org/uniprot/G3X9U1 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:H2ac21 ^@ http://purl.uniprot.org/uniprot/Q64522 ^@ Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region ^@ 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|||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_0000227506 http://togogenome.org/gene/10090:Srl ^@ http://purl.uniprot.org/uniprot/Q7TQ48 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant ^@ Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||In isoform 2.|||N-linked (GlcNAc) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sarcalumenin ^@ http://purl.uniprot.org/annotation/PRO_0000045427|||http://purl.uniprot.org/annotation/VSP_060764 http://togogenome.org/gene/10090:Islr2 ^@ http://purl.uniprot.org/uniprot/E9Q9N7|||http://purl.uniprot.org/uniprot/Q5RKR3 ^@ 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 ^@ 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_0000317499 http://togogenome.org/gene/10090:Serpinb13 ^@ http://purl.uniprot.org/uniprot/Q8CDC0 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Sequence Conflict|||Site|||Splice Variant ^@ In isoform 2.|||Reactive bond|||Serpin B13 ^@ http://purl.uniprot.org/annotation/PRO_0000094122|||http://purl.uniprot.org/annotation/VSP_039855 http://togogenome.org/gene/10090:Mss51 ^@ http://purl.uniprot.org/uniprot/Q9D5Z5 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Zinc Finger ^@ MYND-type|||Putative protein MSS51 homolog, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000218318 http://togogenome.org/gene/10090:Or6z5 ^@ http://purl.uniprot.org/uniprot/Q8VGH6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vrk2 ^@ http://purl.uniprot.org/uniprot/Q8BN21 ^@ 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|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||Interaction with MAP3K7|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase VRK2 ^@ http://purl.uniprot.org/annotation/PRO_0000086807|||http://purl.uniprot.org/annotation/VSP_008541|||http://purl.uniprot.org/annotation/VSP_008542|||http://purl.uniprot.org/annotation/VSP_008543 http://togogenome.org/gene/10090:Calcrl ^@ http://purl.uniprot.org/uniprot/A2AR99|||http://purl.uniprot.org/uniprot/Q9R1W5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Calcitonin gene-related peptide type 1 receptor|||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|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000012812|||http://purl.uniprot.org/annotation/PRO_5014296798 http://togogenome.org/gene/10090:Exoc2 ^@ http://purl.uniprot.org/uniprot/Q9D4H1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Strand|||Turn ^@ Exocyst complex component 2|||IPT/TIG|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000118919 http://togogenome.org/gene/10090:Got1l1 ^@ http://purl.uniprot.org/uniprot/Q7TSV6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ In isoform 2.|||N6-(pyridoxal phosphate)lysine|||Putative aspartate aminotransferase, cytoplasmic 2 ^@ http://purl.uniprot.org/annotation/PRO_0000333000|||http://purl.uniprot.org/annotation/VSP_033430 http://togogenome.org/gene/10090:Mical2 ^@ http://purl.uniprot.org/uniprot/Q8BML1 ^@ 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 ^@ Abolishes interaction with MAPK1.|||Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||In isoform 1 and isoform 3.|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 5 and isoform 6.|||In isoform 5, isoform 7 and isoform 6.|||In isoform 5.|||In isoform 6.|||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_0000075845|||http://purl.uniprot.org/annotation/VSP_061300|||http://purl.uniprot.org/annotation/VSP_061301|||http://purl.uniprot.org/annotation/VSP_061302|||http://purl.uniprot.org/annotation/VSP_061303|||http://purl.uniprot.org/annotation/VSP_061304|||http://purl.uniprot.org/annotation/VSP_061305|||http://purl.uniprot.org/annotation/VSP_061306|||http://purl.uniprot.org/annotation/VSP_061307|||http://purl.uniprot.org/annotation/VSP_061308|||http://purl.uniprot.org/annotation/VSP_061309|||http://purl.uniprot.org/annotation/VSP_061310|||http://purl.uniprot.org/annotation/VSP_061311|||http://purl.uniprot.org/annotation/VSP_061312|||http://purl.uniprot.org/annotation/VSP_061313|||http://purl.uniprot.org/annotation/VSP_061314 http://togogenome.org/gene/10090:Ccser1 ^@ http://purl.uniprot.org/uniprot/Q8C0C4 ^@ 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|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Serine-rich coiled-coil domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000349293|||http://purl.uniprot.org/annotation/VSP_035320|||http://purl.uniprot.org/annotation/VSP_035321|||http://purl.uniprot.org/annotation/VSP_035322|||http://purl.uniprot.org/annotation/VSP_035323 http://togogenome.org/gene/10090:Rbm19 ^@ http://purl.uniprot.org/uniprot/Q8R3C6 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Probable RNA-binding protein 19|||RRM 1|||RRM 2|||RRM 3|||RRM 4|||RRM 5|||RRM 6 ^@ http://purl.uniprot.org/annotation/PRO_0000081782|||http://purl.uniprot.org/annotation/VSP_015005|||http://purl.uniprot.org/annotation/VSP_015006 http://togogenome.org/gene/10090:Ndufa4l2 ^@ http://purl.uniprot.org/uniprot/Q4FZG9 ^@ Chain|||Molecule Processing ^@ Chain ^@ NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000245773 http://togogenome.org/gene/10090:Ces1g ^@ http://purl.uniprot.org/uniprot/Q3UW56|||http://purl.uniprot.org/uniprot/Q8VCC2 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Acyl-ester intermediate|||Carboxylesterase type B|||Carboxylic ester hydrolase|||Charge relay system|||Liver carboxylesterase 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000008571|||http://purl.uniprot.org/annotation/PRO_5014205836 http://togogenome.org/gene/10090:Hhipl1 ^@ http://purl.uniprot.org/uniprot/Q14DK5 ^@ 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 ^@ Basic residues|||Disordered|||HHIP-like protein 1|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues|||SRCR ^@ http://purl.uniprot.org/annotation/PRO_0000314963|||http://purl.uniprot.org/annotation/VSP_030457|||http://purl.uniprot.org/annotation/VSP_030458 http://togogenome.org/gene/10090:Aph1b ^@ http://purl.uniprot.org/uniprot/Q8C7N7 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||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_0000221053|||http://purl.uniprot.org/annotation/VSP_008359|||http://purl.uniprot.org/annotation/VSP_008360 http://togogenome.org/gene/10090:Gm20896 ^@ http://purl.uniprot.org/uniprot/A0A087WRK1|||http://purl.uniprot.org/uniprot/A0A087WSR0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Tnpo2 ^@ http://purl.uniprot.org/uniprot/E9PV58|||http://purl.uniprot.org/uniprot/Q3U1S0|||http://purl.uniprot.org/uniprot/Q99LG2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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|||N6-acetyllysine|||Transportin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000120768 http://togogenome.org/gene/10090:Rimbp2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFB0|||http://purl.uniprot.org/uniprot/D3YXR8|||http://purl.uniprot.org/uniprot/Q80U40 ^@ 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|||Basic residues|||Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pro residues|||RIMS-binding protein 2|||SH3|||SH3 1|||SH3 2|||SH3 3 ^@ http://purl.uniprot.org/annotation/PRO_0000221384|||http://purl.uniprot.org/annotation/VSP_037437 http://togogenome.org/gene/10090:Nlrc3 ^@ http://purl.uniprot.org/uniprot/J3QQ49|||http://purl.uniprot.org/uniprot/Q5DU56 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||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|||Polar residues|||Protein NLRC3 ^@ http://purl.uniprot.org/annotation/PRO_0000296188|||http://purl.uniprot.org/annotation/VSP_027139|||http://purl.uniprot.org/annotation/VSP_027140|||http://purl.uniprot.org/annotation/VSP_027141|||http://purl.uniprot.org/annotation/VSP_027142|||http://purl.uniprot.org/annotation/VSP_027143|||http://purl.uniprot.org/annotation/VSP_027144|||http://purl.uniprot.org/annotation/VSP_027145|||http://purl.uniprot.org/annotation/VSP_027146|||http://purl.uniprot.org/annotation/VSP_027147|||http://purl.uniprot.org/annotation/VSP_027148|||http://purl.uniprot.org/annotation/VSP_027149 http://togogenome.org/gene/10090:Tdpoz2 ^@ http://purl.uniprot.org/uniprot/A0A0A6YVW8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB|||MATH ^@ http://togogenome.org/gene/10090:Or13c7d ^@ http://purl.uniprot.org/uniprot/Q9QZ19 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r163 ^@ http://purl.uniprot.org/uniprot/K9J7G0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clta ^@ http://purl.uniprot.org/uniprot/B1AWD8|||http://purl.uniprot.org/uniprot/B1AWD9|||http://purl.uniprot.org/uniprot/B1AWE0|||http://purl.uniprot.org/uniprot/B1AWE1|||http://purl.uniprot.org/uniprot/Q6PFA2 ^@ Coiled-Coil|||Region ^@ Coiled-Coil|||Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Cdkn1b ^@ http://purl.uniprot.org/uniprot/P46414 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||Cyclin-dependent kinase inhibitor 1B|||Disordered|||Interaction with CDK2|||Loss of cMYC-induced CDK2-mediated phosphorylation Dissociates very slowly from the cyclin E/CDK2 complex after induction by cMYC. Cell cycle arrest.|||Loss of cMyc-induced CDK2-mediated phosphorylation. Rapid dissociation from the cyclin E/CDK2 complex after induction by c-Myc.|||Loss of interaction with NUP50. No cyclin E-mediated degradation of phosphorylated p27KIP1.|||Loss of phosphorylation in G(0) phase. No change in cMYC-induced CDK2-mediated phosphorylation. Rapid dissociation from the cyclin E/CDK2 complex after induction by cMYC. Loss of protein stability in G(0) phase. No change in protein stability at S-phase.|||Nuclear localization signal|||Phosphoserine; by UHMK1|||Phosphothreonine; by CaMK1|||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|||Polar residues|||Required for interaction with NUP50 ^@ http://purl.uniprot.org/annotation/PRO_0000190085 http://togogenome.org/gene/10090:Camk4 ^@ http://purl.uniprot.org/uniprot/Q8BGR3 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||Protein kinase ^@ http://togogenome.org/gene/10090:AI593442 ^@ http://purl.uniprot.org/uniprot/Q32M26 ^@ 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 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000320197 http://togogenome.org/gene/10090:Klc1 ^@ http://purl.uniprot.org/uniprot/E9Q7C9|||http://purl.uniprot.org/uniprot/Q5UE59|||http://purl.uniprot.org/uniprot/Q7M6Z7|||http://purl.uniprot.org/uniprot/Q7M6Z8|||http://purl.uniprot.org/uniprot/Q7M6Z9|||http://purl.uniprot.org/uniprot/Q7M701|||http://purl.uniprot.org/uniprot/Q7M702|||http://purl.uniprot.org/uniprot/Q7TNF4|||http://purl.uniprot.org/uniprot/Q8CD76 ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Polar residues|||TPR ^@ http://togogenome.org/gene/10090:Ftsj1 ^@ http://purl.uniprot.org/uniprot/Q8CBC7 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Region|||Splice Variant ^@ In isoform 2 and isoform 3.|||In isoform 3.|||Proton acceptor|||Required for binding to WDR6|||tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000458463|||http://purl.uniprot.org/annotation/VSP_061948|||http://purl.uniprot.org/annotation/VSP_061949 http://togogenome.org/gene/10090:Trpc3 ^@ http://purl.uniprot.org/uniprot/Q8BNT8|||http://purl.uniprot.org/uniprot/Q8CCQ1|||http://purl.uniprot.org/uniprot/Q9QZC1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Short transient receptor potential channel 3|||Transient receptor ion channel ^@ http://purl.uniprot.org/annotation/PRO_0000215311 http://togogenome.org/gene/10090:Slc38a10 ^@ http://purl.uniprot.org/uniprot/Q5I012 ^@ 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 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||Solute carrier family 38 member 10 ^@ http://purl.uniprot.org/annotation/PRO_0000318976|||http://purl.uniprot.org/annotation/VSP_031328|||http://purl.uniprot.org/annotation/VSP_031329|||http://purl.uniprot.org/annotation/VSP_031330|||http://purl.uniprot.org/annotation/VSP_031331|||http://purl.uniprot.org/annotation/VSP_031332|||http://purl.uniprot.org/annotation/VSP_031333 http://togogenome.org/gene/10090:Serinc1 ^@ http://purl.uniprot.org/uniprot/A9CLV6|||http://purl.uniprot.org/uniprot/Q9QZI8 ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Removed|||Serine incorporator 1 ^@ http://purl.uniprot.org/annotation/PRO_0000218967 http://togogenome.org/gene/10090:Phc1 ^@ http://purl.uniprot.org/uniprot/Q3TJ47|||http://purl.uniprot.org/uniprot/Q3V116|||http://purl.uniprot.org/uniprot/Q64028 ^@ Binding Site|||Chain|||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|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||FCS-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Polyhomeotic-like protein 1|||Pro residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000058376|||http://purl.uniprot.org/annotation/VSP_004040|||http://purl.uniprot.org/annotation/VSP_004041 http://togogenome.org/gene/10090:Nop16 ^@ http://purl.uniprot.org/uniprot/Q9CPT5 ^@ 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)|||In strain: NOD.|||N6-acetyllysine|||Nucleolar protein 16|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000250158 http://togogenome.org/gene/10090:Slc6a1 ^@ http://purl.uniprot.org/uniprot/P31648|||http://purl.uniprot.org/uniprot/Q6PCX2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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|||PDZ-binding|||Phosphoserine|||Polar residues|||Sodium- and chloride-dependent GABA transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000214744 http://togogenome.org/gene/10090:Or2r11 ^@ http://purl.uniprot.org/uniprot/Q8VF80 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rtel1 ^@ http://purl.uniprot.org/uniprot/Q0VGM9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes G4-DNA unwinding activity.|||Abolishes interaction with PCNA.|||Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Nuclear localization signal|||PIP-box|||Polar residues|||Regulator of telomere elongation helicase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000370610|||http://purl.uniprot.org/annotation/VSP_036945|||http://purl.uniprot.org/annotation/VSP_036946|||http://purl.uniprot.org/annotation/VSP_036947|||http://purl.uniprot.org/annotation/VSP_036948|||http://purl.uniprot.org/annotation/VSP_036949|||http://purl.uniprot.org/annotation/VSP_036950 http://togogenome.org/gene/10090:Shisal2b ^@ http://purl.uniprot.org/uniprot/Q9D1Y9 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Protein shisa-like-2B ^@ http://purl.uniprot.org/annotation/PRO_0000343652 http://togogenome.org/gene/10090:Dsel ^@ http://purl.uniprot.org/uniprot/Q0VBN2 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Signal Peptide|||Transmembrane ^@ Dermatan-sulfate epimerase-like protein|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000278289 http://togogenome.org/gene/10090:Arhgef33 ^@ http://purl.uniprot.org/uniprot/Q8BW86 ^@ 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|||DH|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Polar residues|||Rho guanine nucleotide exchange factor 33 ^@ http://purl.uniprot.org/annotation/PRO_0000342344|||http://purl.uniprot.org/annotation/VSP_039455 http://togogenome.org/gene/10090:Sval3 ^@ http://purl.uniprot.org/uniprot/Q76I99 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Signal Peptide ^@ Prolactin-induced protein|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_5015098639 http://togogenome.org/gene/10090:Dcp2 ^@ http://purl.uniprot.org/uniprot/Q3U671|||http://purl.uniprot.org/uniprot/Q9CYC6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Nudix box|||Nudix hydrolase|||Phosphoserine|||Polar residues|||m7GpppN-mRNA hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000057052 http://togogenome.org/gene/10090:Psmg4 ^@ http://purl.uniprot.org/uniprot/P0C7N9 ^@ Chain|||Molecule Processing ^@ Chain ^@ Proteasome assembly chaperone 4 ^@ http://purl.uniprot.org/annotation/PRO_0000341398 http://togogenome.org/gene/10090:Sik1 ^@ http://purl.uniprot.org/uniprot/Q60670 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes phosphorylation by PKA and impairs nuclear export following ACTH treatment.|||Constitutively active.|||Disordered|||Does not affect phosphorylation by PKA and nuclear export following ACTH treatment.|||Localizes mainly in cytoplasm and not in nucleus.|||Localizes mainly in cytoplasm and not in nucleus; when associated with D-483 and A-607.|||Localizes mainly in cytoplasm and not in nucleus; when associated with D-483 and A-610.|||Loss of kinase activity.|||Low levels of constitutive activity.|||Phosphoserine; by PKA|||Phosphoserine; by autocatalysis|||Phosphothreonine; by CaMK1|||Phosphothreonine; by LKB1 and GSK3-beta|||Polar residues|||Protein kinase|||Proton acceptor|||RK-rich region|||Serine/threonine-protein kinase SIK1|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000086660 http://togogenome.org/gene/10090:Tex2 ^@ http://purl.uniprot.org/uniprot/Q6ZPJ0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SMP-LTD|||Testis-expressed protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000244480 http://togogenome.org/gene/10090:Ppp1r14c ^@ http://purl.uniprot.org/uniprot/Q8R4S0 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ 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_0000071495 http://togogenome.org/gene/10090:Czib ^@ http://purl.uniprot.org/uniprot/Q8BHG2 ^@ 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 ^@ CXXC motif containing zinc binding protein|||In isoform 2.|||In isoform 3.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000264152|||http://purl.uniprot.org/annotation/VSP_021887|||http://purl.uniprot.org/annotation/VSP_021888 http://togogenome.org/gene/10090:Usp26 ^@ http://purl.uniprot.org/uniprot/Q3V059|||http://purl.uniprot.org/uniprot/Q99MX1 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 26|||Ubiquitin carboxyl-terminal hydrolase 37 pleckstrin homology-like ^@ http://purl.uniprot.org/annotation/PRO_0000080656 http://togogenome.org/gene/10090:Ptpdc1 ^@ http://purl.uniprot.org/uniprot/Q6NZK8 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Protein tyrosine phosphatase domain-containing protein 1|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000312213|||http://purl.uniprot.org/annotation/VSP_029737|||http://purl.uniprot.org/annotation/VSP_029738|||http://purl.uniprot.org/annotation/VSP_029739 http://togogenome.org/gene/10090:Fbxo44 ^@ http://purl.uniprot.org/uniprot/A2A7H5|||http://purl.uniprot.org/uniprot/A2A7H6|||http://purl.uniprot.org/uniprot/Q8BK26 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Splice Variant ^@ Disordered|||F-box|||F-box only protein 44|||FBA|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000119946|||http://purl.uniprot.org/annotation/VSP_011348|||http://purl.uniprot.org/annotation/VSP_011349 http://togogenome.org/gene/10090:Iqgap2 ^@ http://purl.uniprot.org/uniprot/Q3UQ44 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Calponin-homology (CH)|||IQ 1|||IQ 2|||IQ 3|||Phosphoserine|||Phosphothreonine|||Ras GTPase-activating-like protein IQGAP2|||Ras-GAP|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000354074 http://togogenome.org/gene/10090:Rabif ^@ http://purl.uniprot.org/uniprot/Q91X96 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Guanine nucleotide exchange factor MSS4|||MSS4|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000174175 http://togogenome.org/gene/10090:Washc4 ^@ http://purl.uniprot.org/uniprot/Q3UMB9 ^@ 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|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||Sufficient for interaction with WASHC5|||WASH complex subunit 4 ^@ http://purl.uniprot.org/annotation/PRO_0000282576 http://togogenome.org/gene/10090:Nppb ^@ http://purl.uniprot.org/uniprot/P40753|||http://purl.uniprot.org/uniprot/Q54AE9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Basic and acidic residues|||Brain natriuretic peptide 45|||Cleavage; by FAP|||Cleavage; by FURIN|||Disordered|||In isoform Short.|||Natriuretic peptides B ^@ http://purl.uniprot.org/annotation/PRO_0000001533|||http://purl.uniprot.org/annotation/PRO_0000001534|||http://purl.uniprot.org/annotation/PRO_5014309634|||http://purl.uniprot.org/annotation/VSP_000263 http://togogenome.org/gene/10090:Cox10 ^@ http://purl.uniprot.org/uniprot/Q3U3N1|||http://purl.uniprot.org/uniprot/Q3UDN4|||http://purl.uniprot.org/uniprot/Q8CFY5 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Transit Peptide|||Transmembrane ^@ Chain|||Non-terminal Residue|||Region|||Transit Peptide|||Transmembrane ^@ Disordered|||Helical|||Mitochondrion|||Protoheme IX farnesyltransferase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000035924 http://togogenome.org/gene/10090:Eif4e ^@ http://purl.uniprot.org/uniprot/P63073|||http://purl.uniprot.org/uniprot/Q3TK95|||http://purl.uniprot.org/uniprot/Q8C470 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolishes binding to the 4ESE element in mRNAs; when associated with E-157 and E-159.|||Abolishes binding to the 4ESE element in mRNAs; when associated with E-157 and E-162.|||Abolishes binding to the 4ESE element in mRNAs; when associated with E-159 and E-162.|||Abolishes mRNA nuclear export. Impairs nuclear pore complex reprogramming. No effect on interaction with PML or viral Z protein but reduces binding to the mRNA cap. Capable of AKT1 activation. Does not impair interaction with HHEX or HOXA9.|||Abolishes phosphorylation and abrogates the ability to transform cells.|||Abolishes phosphorylation, abrogates the ability to transform cells and impairs nuclear export of CCND1 but does not affect subcellular location.|||Binding to CYFIP1 reduced by 70%. Does not affect mRNA nuclear export or nuclear pore complex reprogramming. Does not affect affinity for mRNA cap. Reduces interaction with LRPPRC. Reduces affinity for PML and viral Z protein. Abolishes AKT1 activation. Abolishes interaction with HHEX. Inhibits interaction with HOXA9. Abolishes interaction with LRPPRC and abolishes CCND1 mRNA export; when associated with A-69.|||Disordered|||EIF4EBP1/2/3 binding|||Eukaryotic translation initiation factor 4E|||N-acetylalanine|||No increase in protein levels of ODC1 or CCND1 in NIH 3T3 cells overexpressing the mutant in comparison to a 3-fold increase in cells overexpressing the wild-type. Abolishes stimulation of splice factor synthesis. Abolishes binding to mRNAs in the nucleus and impairs nuclear pore complex reprogramming and mRNA export. Does not affect interaction with HHEX.|||Phosphoserine; by PKC and MKNK2|||Phosphothreonine|||Polar residues|||Reduces interaction with LRPPRC. Abolishes interaction with LRPPRC and abolishes CCND1 mRNA export; when associated with A-73.|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000193635 http://togogenome.org/gene/10090:Phf14 ^@ http://purl.uniprot.org/uniprot/G5E8S0|||http://purl.uniprot.org/uniprot/Q9D4H9 ^@ 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|||C2HC pre-PHD-type|||Disordered|||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_0000059307|||http://purl.uniprot.org/annotation/VSP_061648|||http://purl.uniprot.org/annotation/VSP_061649|||http://purl.uniprot.org/annotation/VSP_061650 http://togogenome.org/gene/10090:Oprd1 ^@ http://purl.uniprot.org/uniprot/A2AD37|||http://purl.uniprot.org/uniprot/P32300|||http://purl.uniprot.org/uniprot/Q8BLP9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Region|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Delta-type opioid receptor|||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|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069963 http://togogenome.org/gene/10090:Cd320 ^@ http://purl.uniprot.org/uniprot/Q9Z1P5 ^@ Binding Site|||Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ CD320 antigen|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||LDL-receptor class A 1|||LDL-receptor class A 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000354052|||http://purl.uniprot.org/annotation/VSP_035723 http://togogenome.org/gene/10090:Rsph3b ^@ http://purl.uniprot.org/uniprot/Q9DA80 ^@ 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|||Phosphothreonine; by MAPK1|||Polar residues|||Radial spoke head protein 3 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000313743 http://togogenome.org/gene/10090:Or2w2 ^@ http://purl.uniprot.org/uniprot/Q5SZS9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Yipf1 ^@ http://purl.uniprot.org/uniprot/Q91VU1 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein YIPF1 ^@ http://purl.uniprot.org/annotation/PRO_0000240869 http://togogenome.org/gene/10090:Numb ^@ http://purl.uniprot.org/uniprot/Q9QZS3 ^@ 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 and isoform 4.|||In isoform 3 and isoform 4.|||PID|||Phosphoserine|||Phosphoserine; by CaMK1|||Phosphothreonine|||Polar residues|||Protein numb homolog ^@ http://purl.uniprot.org/annotation/PRO_0000058002|||http://purl.uniprot.org/annotation/VSP_004350|||http://purl.uniprot.org/annotation/VSP_004351 http://togogenome.org/gene/10090:Zscan2 ^@ http://purl.uniprot.org/uniprot/Q07230 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger ^@ Chain|||Domain Extent|||Helix|||Region|||Strand|||Turn|||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|||SCAN box|||Zinc finger and SCAN domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000047750 http://togogenome.org/gene/10090:Awat2 ^@ http://purl.uniprot.org/uniprot/A2ADU0|||http://purl.uniprot.org/uniprot/Q6E1M8 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Acyl-CoA wax alcohol acyltransferase 2|||Helical|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000249053|||http://purl.uniprot.org/annotation/VSP_020357 http://togogenome.org/gene/10090:Akr1c14 ^@ http://purl.uniprot.org/uniprot/Q91WT7 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Site ^@ Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor ^@ http://togogenome.org/gene/10090:Inpp5k ^@ http://purl.uniprot.org/uniprot/Q5ND43|||http://purl.uniprot.org/uniprot/Q8C5L6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Catalytic|||Inositol polyphosphate 5-phosphatase K|||Inositol polyphosphate-related phosphatase|||Required for interaction with GPR78 and PAK1|||Required for ruffle localization ^@ http://purl.uniprot.org/annotation/PRO_0000209728 http://togogenome.org/gene/10090:Lrrc45 ^@ http://purl.uniprot.org/uniprot/Q8CIM1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||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_0000223924 http://togogenome.org/gene/10090:Sycp3 ^@ http://purl.uniprot.org/uniprot/A2RSE7|||http://purl.uniprot.org/uniprot/P70281 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Turn ^@ Basic and acidic residues|||Disordered|||Important for oligomerization and fiber formation|||Interaction with DNA|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Synaptonemal complex protein 3|||XLR/SYCP3/FAM9 ^@ http://purl.uniprot.org/annotation/PRO_0000223044 http://togogenome.org/gene/10090:Crtam ^@ http://purl.uniprot.org/uniprot/Q149L7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||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.|||In isoform 3.|||In response to TCR stimulation, increases CD4+ T-cell proliferation and impairs IFNG and IL22 production.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000292603|||http://purl.uniprot.org/annotation/VSP_052473|||http://purl.uniprot.org/annotation/VSP_052474|||http://purl.uniprot.org/annotation/VSP_059946 http://togogenome.org/gene/10090:Or8c10 ^@ http://purl.uniprot.org/uniprot/E9PV37 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Adcy7 ^@ http://purl.uniprot.org/uniprot/P51829|||http://purl.uniprot.org/uniprot/Q3U1P1|||http://purl.uniprot.org/uniprot/Q3U1X9|||http://purl.uniprot.org/uniprot/Q3UU15 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Adenylate cyclase type 7|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Guanylate cyclase|||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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000195704 http://togogenome.org/gene/10090:I830077J02Rik ^@ http://purl.uniprot.org/uniprot/Q3U7U4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Polar residues|||Transmembrane protein C1orf162 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000304788 http://togogenome.org/gene/10090:Ldlrad2 ^@ http://purl.uniprot.org/uniprot/Q3V0V0 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Tent2 ^@ http://purl.uniprot.org/uniprot/Q91YI6 ^@ 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 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ In isoform 2.|||Loss of enzyme activity.|||Nuclear localization signal|||PAP-associated|||Phosphoserine|||Poly(A) RNA polymerase GLD2 ^@ http://purl.uniprot.org/annotation/PRO_0000341550|||http://purl.uniprot.org/annotation/VSP_034325 http://togogenome.org/gene/10090:Rbks ^@ http://purl.uniprot.org/uniprot/Q8R1Q9 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Proton acceptor|||Ribokinase ^@ http://purl.uniprot.org/annotation/PRO_0000375977 http://togogenome.org/gene/10090:Zfp11 ^@ http://purl.uniprot.org/uniprot/P10751 ^@ 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 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|||Zinc finger protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000047283 http://togogenome.org/gene/10090:Ccl19 ^@ http://purl.uniprot.org/uniprot/O70460|||http://purl.uniprot.org/uniprot/Q548P0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ C-C motif chemokine|||C-C motif chemokine 19|||Chemokine interleukin-8-like|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000005215|||http://purl.uniprot.org/annotation/PRO_5014205872 http://togogenome.org/gene/10090:Supt16 ^@ http://purl.uniprot.org/uniprot/G3X956|||http://purl.uniprot.org/uniprot/Q920B9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||FACT complex subunit SPT16|||FACT complex subunit Spt16|||FACT complex subunit Spt16 N-terminal lobe|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Histone chaperone RTT106/FACT complex subunit SPT16-like middle|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000245170 http://togogenome.org/gene/10090:Vmn1r201 ^@ http://purl.uniprot.org/uniprot/Q8R262 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tjp2 ^@ http://purl.uniprot.org/uniprot/A0A3B2WCN9|||http://purl.uniprot.org/uniprot/Q9Z0U1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Guanylate kinase-like|||Interaction with SCRIB|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH3|||Tight junction protein ZO-2 ^@ http://purl.uniprot.org/annotation/PRO_0000094544 http://togogenome.org/gene/10090:Gab2 ^@ http://purl.uniprot.org/uniprot/Q3ZB57|||http://purl.uniprot.org/uniprot/Q3ZB59 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Tshb ^@ http://purl.uniprot.org/uniprot/E9Q4F3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Glycoprotein hormone subunit beta ^@ http://purl.uniprot.org/annotation/PRO_5015090362 http://togogenome.org/gene/10090:Sdhaf3 ^@ http://purl.uniprot.org/uniprot/Q8BQU3 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||Succinate dehydrogenase assembly factor 3, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000042654 http://togogenome.org/gene/10090:Rsph3a ^@ http://purl.uniprot.org/uniprot/Q3UFY4 ^@ 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|||Phosphothreonine; by MAPK1|||Polar residues|||Radial spoke head protein 3 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000313742 http://togogenome.org/gene/10090:Guca2a ^@ http://purl.uniprot.org/uniprot/P33680 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Signal Peptide ^@ Guanylin ^@ http://purl.uniprot.org/annotation/PRO_0000013137|||http://purl.uniprot.org/annotation/PRO_0000013138 http://togogenome.org/gene/10090:Aunip ^@ http://purl.uniprot.org/uniprot/E9Q6Z5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Aurora kinase A- and ninein-interacting protein|||Disordered|||Interaction with AURKA|||Interaction with RBBP8/CtIP|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000419630 http://togogenome.org/gene/10090:Ghrh ^@ http://purl.uniprot.org/uniprot/P16043|||http://purl.uniprot.org/uniprot/Q544X5 ^@ Chain|||Domain Extent|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Peptide|||Propeptide|||Signal Peptide ^@ Glucagon / GIP / secretin / VIP family|||Somatoliberin ^@ http://purl.uniprot.org/annotation/PRO_0000011444|||http://purl.uniprot.org/annotation/PRO_0000011445|||http://purl.uniprot.org/annotation/PRO_0000011446|||http://purl.uniprot.org/annotation/PRO_5014309636 http://togogenome.org/gene/10090:Sel1l2 ^@ http://purl.uniprot.org/uniprot/Q3V172 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||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_0000305160 http://togogenome.org/gene/10090:Or5h25 ^@ http://purl.uniprot.org/uniprot/Q7TS43 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gtpbp6 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Z0|||http://purl.uniprot.org/uniprot/Q3U6U5|||http://purl.uniprot.org/uniprot/Q8K372 ^@ 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_0000304799 http://togogenome.org/gene/10090:Zfp39 ^@ http://purl.uniprot.org/uniprot/Q02525 ^@ 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; 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 39 ^@ http://purl.uniprot.org/annotation/PRO_0000047298 http://togogenome.org/gene/10090:Dapk2 ^@ http://purl.uniprot.org/uniprot/Q8VDF3 ^@ 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|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Autoinhibitory domain|||Calmodulin-binding|||Death-associated protein kinase 2|||In isoform 2.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085913|||http://purl.uniprot.org/annotation/VSP_042058 http://togogenome.org/gene/10090:Trim8 ^@ http://purl.uniprot.org/uniprot/Q99PJ2 ^@ 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 ^@ B box-type 1|||B box-type 2|||Disordered|||E3 ubiquitin-protein ligase TRIM8|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056207 http://togogenome.org/gene/10090:Snrpc ^@ http://purl.uniprot.org/uniprot/Q569X3|||http://purl.uniprot.org/uniprot/Q62241 ^@ 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|||Matrin-type|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Pro residues|||U1 small nuclear ribonucleoprotein C ^@ http://purl.uniprot.org/annotation/PRO_0000097526 http://togogenome.org/gene/10090:Ankrd34a ^@ http://purl.uniprot.org/uniprot/B2RW11|||http://purl.uniprot.org/uniprot/Q7TST1 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ ANK|||Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Plscr4 ^@ http://purl.uniprot.org/uniprot/P58196 ^@ Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Lipid Binding|||Modified Residue|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||PPxY motif|||Phospholipid scramblase 4|||Phosphotyrosine; by ABL|||Proline-rich domain (PRD)|||S-palmitoyl cysteine|||SH3-binding 1|||SH3-binding 2|||SH3-binding 3 ^@ http://purl.uniprot.org/annotation/PRO_0000100793 http://togogenome.org/gene/10090:Jmy ^@ http://purl.uniprot.org/uniprot/A0A0R4J0V4|||http://purl.uniprot.org/uniprot/Q9QXM1 ^@ 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 ^@ Acidic residues|||Decreases the activation of Arp2/3 without affecting the intrinsic nucleation activity.|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with p300/EP300|||Junction-mediating and -regulatory protein|||Phosphoserine|||Polar residues|||Pro residues|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000324612|||http://purl.uniprot.org/annotation/VSP_032311|||http://purl.uniprot.org/annotation/VSP_032312|||http://purl.uniprot.org/annotation/VSP_032313 http://togogenome.org/gene/10090:Prtn3 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZY6|||http://purl.uniprot.org/uniprot/Q61096 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Myeloblastin|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027710|||http://purl.uniprot.org/annotation/PRO_0000027711|||http://purl.uniprot.org/annotation/PRO_0000027712|||http://purl.uniprot.org/annotation/PRO_5015044277 http://togogenome.org/gene/10090:Or52n3 ^@ http://purl.uniprot.org/uniprot/Q8VG79 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Elovl1 ^@ http://purl.uniprot.org/uniprot/Q4V9V3|||http://purl.uniprot.org/uniprot/Q548M4|||http://purl.uniprot.org/uniprot/Q9JLJ5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Motif|||Sequence Conflict|||Transmembrane ^@ Di-lysine motif|||Elongation of very long chain fatty acids protein 1|||Helical|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000207537 http://togogenome.org/gene/10090:Brd4 ^@ http://purl.uniprot.org/uniprot/B2RSE4|||http://purl.uniprot.org/uniprot/Q3UH70|||http://purl.uniprot.org/uniprot/Q9ESU6 ^@ 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|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Turn ^@ Acetylated histone binding|||BID region|||Basic and acidic residues|||Basic residues|||Bromo|||Bromo 1|||Bromo 2|||Bromodomain-containing protein 4|||C-terminal (CTD) region|||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; alternate|||NET|||NPS region|||No effect on acetylated histone binding.|||Phosphoserine|||Phosphoserine; by CK2|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000211184|||http://purl.uniprot.org/annotation/VSP_010904|||http://purl.uniprot.org/annotation/VSP_010905 http://togogenome.org/gene/10090:Palld ^@ http://purl.uniprot.org/uniprot/K0BWC3|||http://purl.uniprot.org/uniprot/Q9ET54 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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 3, isoform 4 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||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_0000302721|||http://purl.uniprot.org/annotation/VSP_027931|||http://purl.uniprot.org/annotation/VSP_027932|||http://purl.uniprot.org/annotation/VSP_027933|||http://purl.uniprot.org/annotation/VSP_027934|||http://purl.uniprot.org/annotation/VSP_027935|||http://purl.uniprot.org/annotation/VSP_027936 http://togogenome.org/gene/10090:Zfp984 ^@ http://purl.uniprot.org/uniprot/A2A7A2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Kap ^@ http://purl.uniprot.org/uniprot/P61110|||http://purl.uniprot.org/uniprot/Q3UQF0 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Kidney androgen-regulated protein ^@ http://purl.uniprot.org/annotation/PRO_0000020736|||http://purl.uniprot.org/annotation/PRO_5009970839 http://togogenome.org/gene/10090:Tbc1d22a ^@ http://purl.uniprot.org/uniprot/Q8R5A6 ^@ 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 ^@ Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pro residues|||Rab-GAP TBC|||Removed|||TBC1 domain family member 22A ^@ http://purl.uniprot.org/annotation/PRO_0000208053|||http://purl.uniprot.org/annotation/VSP_016761 http://togogenome.org/gene/10090:Btbd35f11 ^@ http://purl.uniprot.org/uniprot/A2BFZ7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Cstb ^@ http://purl.uniprot.org/uniprot/Q62426 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Chain|||Modified Residue|||Motif|||Site ^@ Cystatin-B|||N-acetylmethionine|||Reactive site|||Secondary area of contact ^@ http://purl.uniprot.org/annotation/PRO_0000207141 http://togogenome.org/gene/10090:Lrp1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0I9|||http://purl.uniprot.org/uniprot/Q3U454|||http://purl.uniprot.org/uniprot/Q91ZX7 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||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|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Helical|||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|||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...) asparagine|||N6-acetyllysine|||NPXY motif|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Prolow-density lipoprotein receptor-related protein 1|||Recognition site for proteolytical processing ^@ http://purl.uniprot.org/annotation/PRO_0000273273|||http://purl.uniprot.org/annotation/PRO_0000302753|||http://purl.uniprot.org/annotation/PRO_0000302754|||http://purl.uniprot.org/annotation/PRO_0000302755|||http://purl.uniprot.org/annotation/PRO_5015044288 http://togogenome.org/gene/10090:Kctd17 ^@ http://purl.uniprot.org/uniprot/A6H697 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BTB|||Disordered ^@ http://togogenome.org/gene/10090:Zmat2 ^@ http://purl.uniprot.org/uniprot/Q9CPW7 ^@ 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_0000047328 http://togogenome.org/gene/10090:Psmb3 ^@ http://purl.uniprot.org/uniprot/Q9R1P1 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn ^@ N-acetylserine|||N6-acetyllysine|||Proteasome subunit beta type-3|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000148058 http://togogenome.org/gene/10090:Uhrf2 ^@ http://purl.uniprot.org/uniprot/Q7TMI3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Abolishes in vitro binding to 'Lys-10' methylated H3, H3K9me3. Prevents enrichment at pericentric heterochromatin.|||Abolishes in vitro binding to H3K9me3. Prevents enrichment at pericentric heterochromatin.|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase UHRF2|||In isoform 2.|||In isoform 3.|||Interaction with PCNP|||Interchain|||Methyl-CpG binding and interaction with HDAC1|||PHD-type|||Phosphoserine|||Polar residues|||RING-type|||Required for interaction with histone H3|||Ubiquitin-like|||YDG ^@ http://purl.uniprot.org/annotation/PRO_0000056148|||http://purl.uniprot.org/annotation/VSP_013876|||http://purl.uniprot.org/annotation/VSP_013877|||http://purl.uniprot.org/annotation/VSP_013878 http://togogenome.org/gene/10090:Cfap97 ^@ http://purl.uniprot.org/uniprot/Q6ZPR1 ^@ 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|||Cilia- and flagella-associated protein 97|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000309225 http://togogenome.org/gene/10090:Smpdl3a ^@ http://purl.uniprot.org/uniprot/P70158 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Turn ^@ Abolishes enzyme activity.|||Acid sphingomyelinase-like phosphodiesterase 3a|||N-linked (GlcNAc...) asparagine|||Nearly abolishes enzyme activity. ^@ http://purl.uniprot.org/annotation/PRO_0000002329 http://togogenome.org/gene/10090:Trim80 ^@ http://purl.uniprot.org/uniprot/Q3V061 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ B box-type|||B30.2/SPRY|||Disordered|||Polar residues|||RING-type ^@ http://togogenome.org/gene/10090:Gm94 ^@ http://purl.uniprot.org/uniprot/B2RV94|||http://purl.uniprot.org/uniprot/Q3V2D2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Uncharacterized protein C5orf46 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000317637|||http://purl.uniprot.org/annotation/PRO_5014298346 http://togogenome.org/gene/10090:Scfd2 ^@ http://purl.uniprot.org/uniprot/Q3UXF7|||http://purl.uniprot.org/uniprot/Q8BTY8 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Splice Variant ^@ Chain|||Non-terminal Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Sec1 family domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000206291|||http://purl.uniprot.org/annotation/VSP_010711|||http://purl.uniprot.org/annotation/VSP_010712|||http://purl.uniprot.org/annotation/VSP_010713|||http://purl.uniprot.org/annotation/VSP_010714 http://togogenome.org/gene/10090:Csl ^@ http://purl.uniprot.org/uniprot/Q80X68|||http://purl.uniprot.org/uniprot/Q9DAM4 ^@ Active Site|||Site ^@ Active Site ^@ ^@ http://togogenome.org/gene/10090:H2-M10.2 ^@ http://purl.uniprot.org/uniprot/Q85ZW9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015098995 http://togogenome.org/gene/10090:Gm4631 ^@ http://purl.uniprot.org/uniprot/A2ART4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Cyb5r2 ^@ http://purl.uniprot.org/uniprot/Q3KNK3 ^@ 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 ^@ FAD-binding FR-type|||In isoform 2.|||N6-acetyllysine|||NADH-cytochrome b5 reductase 2|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000287549|||http://purl.uniprot.org/annotation/VSP_025560 http://togogenome.org/gene/10090:Ctsw ^@ http://purl.uniprot.org/uniprot/P56203|||http://purl.uniprot.org/uniprot/Q8C2M0 ^@ 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 ^@ Cathepsin W|||Cathepsin propeptide inhibitor|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000026329|||http://purl.uniprot.org/annotation/PRO_0000026330|||http://purl.uniprot.org/annotation/PRO_5015020115 http://togogenome.org/gene/10090:Slk ^@ http://purl.uniprot.org/uniprot/A2RRK3|||http://purl.uniprot.org/uniprot/O54988 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||In isoform 2.|||No change in caspase-3-induced cleavage product.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||STE20-like serine/threonine-protein kinase|||UVR ^@ http://purl.uniprot.org/annotation/PRO_0000233240|||http://purl.uniprot.org/annotation/VSP_018101 http://togogenome.org/gene/10090:Tstd3 ^@ http://purl.uniprot.org/uniprot/Q9D0B5 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue ^@ Cysteine persulfide intermediate|||N6-succinyllysine|||Rhodanese|||Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000419461 http://togogenome.org/gene/10090:Hunk ^@ http://purl.uniprot.org/uniprot/O88866 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Hormonally up-regulated neu tumor-associated kinase|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086005 http://togogenome.org/gene/10090:Cd300e ^@ http://purl.uniprot.org/uniprot/Q8K249 ^@ 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 ^@ CMRF35-like molecule 2|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000320124 http://togogenome.org/gene/10090:Eya2 ^@ http://purl.uniprot.org/uniprot/O08575|||http://purl.uniprot.org/uniprot/Q3UR62|||http://purl.uniprot.org/uniprot/Q3UV00 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Eyes absent homolog 2|||In isoform 2.|||Nucleophile|||Polar residues|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000218647|||http://purl.uniprot.org/annotation/VSP_001492 http://togogenome.org/gene/10090:Vps4a ^@ http://purl.uniprot.org/uniprot/Q8VEJ9 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||MIT|||N6-acetyllysine|||Perinuclear localization.|||Phosphoserine|||Vacuolar protein sorting-associated protein 4A ^@ http://purl.uniprot.org/annotation/PRO_0000084766 http://togogenome.org/gene/10090:Ube2dnl2 ^@ http://purl.uniprot.org/uniprot/A2AFH2 ^@ Active Site|||Domain Extent|||Region|||Site ^@ Active Site|||Domain Extent ^@ Glycyl thioester intermediate|||UBC core ^@ http://togogenome.org/gene/10090:Or5ak23 ^@ http://purl.uniprot.org/uniprot/Q8VF75 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Egfem1 ^@ http://purl.uniprot.org/uniprot/B7ZCE7|||http://purl.uniprot.org/uniprot/Q8C088 ^@ 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|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5|||EGF-like and EMI domain-containing protein 1|||EMI|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000340647|||http://purl.uniprot.org/annotation/PRO_5002863946|||http://purl.uniprot.org/annotation/VSP_034213 http://togogenome.org/gene/10090:Mep1a ^@ http://purl.uniprot.org/uniprot/A0A0R4J043|||http://purl.uniprot.org/uniprot/P28825 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||Impaired ability to form homodimers or oligomers; when associated with A-141.|||Impaired ability to form homodimers or oligomers; when associated with A-259.|||Increased susceptibility to heat-inactivation. Forms homodimers and oligomers; when associated with Q-139 or Q-257. Inactive, impaired ability to form homodimers or oligomers; when associated with Q-139 and Q-257.|||Increased susceptibility to heat-inactivation. Forms homodimers and oligomers; when associated with Q-221. Inactive, impaired ability to form homodimers or oligomers; when associated with Q-139 or Q-139 and Q-221.|||Increased susceptibility to heat-inactivation. Forms homodimers and oligomers; when associated with Q-221. Inactive, impaired ability to form homodimers or oligomers; when associated with Q-257 or Q-221 and Q-257.|||Interchain|||MAM|||MATH|||Meprin A subunit alpha|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||Peptidase M12A ^@ http://purl.uniprot.org/annotation/PRO_0000028879|||http://purl.uniprot.org/annotation/PRO_0000028880 http://togogenome.org/gene/10090:Thsd4 ^@ http://purl.uniprot.org/uniprot/Q3UTY6 ^@ 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.|||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_0000313584|||http://purl.uniprot.org/annotation/VSP_030042|||http://purl.uniprot.org/annotation/VSP_030043 http://togogenome.org/gene/10090:Kcnf1 ^@ http://purl.uniprot.org/uniprot/E9PYC0|||http://purl.uniprot.org/uniprot/Q7TSH7 ^@ Chain|||Domain Extent|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||INTRAMEM|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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|||Ion transport|||Pore-forming; Name=Segment H5|||Potassium channel tetramerisation-type BTB|||Potassium voltage-gated channel subfamily F member 1|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000320105 http://togogenome.org/gene/10090:Best2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0P0|||http://purl.uniprot.org/uniprot/Q8BGM5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Bestrophin-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000143119 http://togogenome.org/gene/10090:Nop9 ^@ http://purl.uniprot.org/uniprot/Q8BMC4 ^@ 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|||Nucleolar protein 9|||Phosphoserine|||Polar residues|||Pumilio 1|||Pumilio 2|||Pumilio 3|||Pumilio 4|||Pumilio 5|||Pumilio 6 ^@ http://purl.uniprot.org/annotation/PRO_0000075928 http://togogenome.org/gene/10090:2810004N23Rik ^@ http://purl.uniprot.org/uniprot/Q8CIL4|||http://purl.uniprot.org/uniprot/Q9CSU7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||N6-acetyllysine|||Phosphoserine|||Uncharacterized protein C1orf131 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000285030 http://togogenome.org/gene/10090:Kyat1 ^@ http://purl.uniprot.org/uniprot/Q05CI8|||http://purl.uniprot.org/uniprot/Q8BTY1 ^@ 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 ^@ Aminotransferase class I/classII|||Kynurenine--oxoglutarate transaminase 1|||N6-(pyridoxal phosphate)lysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000123943 http://togogenome.org/gene/10090:Fmr1 ^@ http://purl.uniprot.org/uniprot/E9QAT0|||http://purl.uniprot.org/uniprot/Q547R0|||http://purl.uniprot.org/uniprot/Q6AXB7|||http://purl.uniprot.org/uniprot/Q8BPK8 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Agenet-like|||Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Serpinb3a ^@ http://purl.uniprot.org/uniprot/G3X9V8|||http://purl.uniprot.org/uniprot/Q8BG86 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Cdr2l ^@ http://purl.uniprot.org/uniprot/A2A6T1 ^@ 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|||Cerebellar degeneration-related protein 2-like|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000307235 http://togogenome.org/gene/10090:Ipmk ^@ http://purl.uniprot.org/uniprot/D3YWA2|||http://purl.uniprot.org/uniprot/Q7TT16 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||Inositol polyphosphate multikinase|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000066871|||http://purl.uniprot.org/annotation/VSP_010923|||http://purl.uniprot.org/annotation/VSP_010924 http://togogenome.org/gene/10090:Spint5 ^@ http://purl.uniprot.org/uniprot/Q32ZM2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ BPTI/Kunitz inhibitor ^@ http://purl.uniprot.org/annotation/PRO_5015097389 http://togogenome.org/gene/10090:Mfge8 ^@ http://purl.uniprot.org/uniprot/P21956|||http://purl.uniprot.org/uniprot/Q3TDU5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Cell attachment site|||EGF-like|||EGF-like 1|||EGF-like 2|||F5/8 type C|||F5/8 type C 1|||F5/8 type C 2|||In isoform 2.|||Lactadherin|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000007653|||http://purl.uniprot.org/annotation/PRO_5014309104|||http://purl.uniprot.org/annotation/VSP_009880 http://togogenome.org/gene/10090:Ubap2l ^@ http://purl.uniprot.org/uniprot/A0A0G2JDV6|||http://purl.uniprot.org/uniprot/A0A0H2UH17|||http://purl.uniprot.org/uniprot/Q80X50|||http://purl.uniprot.org/uniprot/Q8BJ53 ^@ 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|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In strain: FVB/N.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||UBA|||Ubiquitin-associated protein 2-like ^@ http://purl.uniprot.org/annotation/PRO_0000240665|||http://purl.uniprot.org/annotation/VSP_019418|||http://purl.uniprot.org/annotation/VSP_019419|||http://purl.uniprot.org/annotation/VSP_019420|||http://purl.uniprot.org/annotation/VSP_019421|||http://purl.uniprot.org/annotation/VSP_019422|||http://purl.uniprot.org/annotation/VSP_019423 http://togogenome.org/gene/10090:Amh ^@ http://purl.uniprot.org/uniprot/A0A8Q0P8A2|||http://purl.uniprot.org/uniprot/P27106 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage|||Interchain|||Muellerian-inhibiting factor|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033748|||http://purl.uniprot.org/annotation/PRO_0000033749|||http://purl.uniprot.org/annotation/PRO_5035925193 http://togogenome.org/gene/10090:Setmar ^@ http://purl.uniprot.org/uniprot/Q80UJ9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Histone-lysine N-methyltransferase SETMAR|||Post-SET|||Pre-SET|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000259527 http://togogenome.org/gene/10090:Adgrb1 ^@ http://purl.uniprot.org/uniprot/Q3UHD1 ^@ Chain|||Compositionally Biased Region|||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|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Adhesion G protein-coupled receptor B1|||Basic and acidic residues|||Cleavage|||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|||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|||Reduced binding to ELMO1 and failure to promote engulfment of apoptotic thymocytes.|||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_0000245046|||http://purl.uniprot.org/annotation/PRO_0000441806|||http://purl.uniprot.org/annotation/PRO_0000441807 http://togogenome.org/gene/10090:Esp16 ^@ http://purl.uniprot.org/uniprot/A8R0U9 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015086679 http://togogenome.org/gene/10090:Pigh ^@ http://purl.uniprot.org/uniprot/Q5M9N4 ^@ Chain|||Molecule Processing ^@ Chain ^@ Phosphatidylinositol N-acetylglucosaminyltransferase subunit H ^@ http://purl.uniprot.org/annotation/PRO_0000281862 http://togogenome.org/gene/10090:Xkr9 ^@ http://purl.uniprot.org/uniprot/Q5GH62 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Transmembrane ^@ Chain|||Mutagenesis Site|||Site|||Transmembrane ^@ Cleavage; by caspase-3, caspase-6 and caspase-7|||Helical|||In 2DA mutant; abolished cleavage by caspase, preventing phospholipid scramblase activity.|||XK-related protein 9|||XK-related protein 9, processed form ^@ http://purl.uniprot.org/annotation/PRO_0000190797|||http://purl.uniprot.org/annotation/PRO_0000453294 http://togogenome.org/gene/10090:Or2t49 ^@ http://purl.uniprot.org/uniprot/Q5NC44 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ddx55 ^@ http://purl.uniprot.org/uniprot/E9Q9T6|||http://purl.uniprot.org/uniprot/Q6ZPL9|||http://purl.uniprot.org/uniprot/Q810A4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ ATP-dependent RNA helicase DDX55|||Basic and acidic residues|||Basic residues|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000252211 http://togogenome.org/gene/10090:Fgf3 ^@ http://purl.uniprot.org/uniprot/Q0VG15 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Fibroblast growth factor|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015019988 http://togogenome.org/gene/10090:Alas2 ^@ http://purl.uniprot.org/uniprot/A2AFM0|||http://purl.uniprot.org/uniprot/A2AFM1|||http://purl.uniprot.org/uniprot/P08680 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ 5-aminolevulinate synthase presequence|||5-aminolevulinate synthase, erythroid-specific, mitochondrial|||Abolishes enzyme activity.|||Aminotransferase class I/classII|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000001224 http://togogenome.org/gene/10090:Zfp84 ^@ http://purl.uniprot.org/uniprot/Q3ULL7|||http://purl.uniprot.org/uniprot/Q9D654 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Nt5dc3 ^@ http://purl.uniprot.org/uniprot/Q3UHB1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ 5'-nucleotidase domain-containing protein 3|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000326248 http://togogenome.org/gene/10090:Krtap9-3 ^@ http://purl.uniprot.org/uniprot/Q3V2C1 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ 1|||10|||11|||11 X 5 AA repeats of C-C-[AEQVR]-[ALPTV]-[AGHST]|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 9-3 ^@ http://purl.uniprot.org/annotation/PRO_0000361043 http://togogenome.org/gene/10090:Edem1 ^@ http://purl.uniprot.org/uniprot/Q925U4 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||ER degradation-enhancing alpha-mannosidase-like protein 1|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000210322 http://togogenome.org/gene/10090:Eddm3b ^@ http://purl.uniprot.org/uniprot/Q8K0E4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_5015099247 http://togogenome.org/gene/10090:Smg1 ^@ http://purl.uniprot.org/uniprot/Q8BKX6 ^@ 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 ^@ Activation loop|||Basic and acidic residues|||Catalytic loop|||Disordered|||FAT|||FATC|||G-loop|||HEAT|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||PI3K/PI4K catalytic|||Phosphoserine|||Phosphothreonine|||Polar residues|||Serine/threonine-protein kinase SMG1 ^@ http://purl.uniprot.org/annotation/PRO_0000229792|||http://purl.uniprot.org/annotation/VSP_017749|||http://purl.uniprot.org/annotation/VSP_017750|||http://purl.uniprot.org/annotation/VSP_017751|||http://purl.uniprot.org/annotation/VSP_017752 http://togogenome.org/gene/10090:Hsf5 ^@ http://purl.uniprot.org/uniprot/Q5ND04 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region ^@ Disordered|||Heat shock factor protein 5|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000333042 http://togogenome.org/gene/10090:Pla2g4f ^@ http://purl.uniprot.org/uniprot/Q50L41 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ C2|||Cytosolic phospholipase A2 zeta|||Nucleophile|||PLA2c|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000247028 http://togogenome.org/gene/10090:Oxct2b ^@ http://purl.uniprot.org/uniprot/A0A0R4J198|||http://purl.uniprot.org/uniprot/Q9ESL0 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transit Peptide ^@ Active Site|||Chain|||Region|||Sequence Conflict|||Signal Peptide|||Transit Peptide ^@ 5-glutamyl coenzyme A thioester intermediate|||Disordered|||Mitochondrion|||Succinyl-CoA:3-ketoacid coenzyme A transferase 2B, mitochondrial|||Succinyl-CoA:3-ketoacid-coenzyme A transferase ^@ http://purl.uniprot.org/annotation/PRO_0000366211|||http://purl.uniprot.org/annotation/PRO_5006452001 http://togogenome.org/gene/10090:Clec12b ^@ http://purl.uniprot.org/uniprot/A0A0R4J0A7|||http://purl.uniprot.org/uniprot/Q149M0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 12 member B|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||ITIM motif|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000313582 http://togogenome.org/gene/10090:Vma21 ^@ http://purl.uniprot.org/uniprot/F2Z446|||http://purl.uniprot.org/uniprot/F2Z447|||http://purl.uniprot.org/uniprot/Q78T54 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||Vacuolar ATPase assembly integral membrane protein Vma21 ^@ http://purl.uniprot.org/annotation/PRO_0000331500|||http://purl.uniprot.org/annotation/VSP_037464 http://togogenome.org/gene/10090:Or4x15 ^@ http://purl.uniprot.org/uniprot/A2ATW2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Acss2 ^@ http://purl.uniprot.org/uniprot/Q9QXG4 ^@ 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 ^@ Acetyl-coenzyme A synthetase, cytoplasmic|||Basic and acidic residues|||Disordered|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000208424 http://togogenome.org/gene/10090:Erp27 ^@ http://purl.uniprot.org/uniprot/Q9D8U3 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Endoplasmic reticulum resident protein 27|||N-linked (GlcNAc...) asparagine|||PDIA3-binding site|||Prevents secretion from ER|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000281119 http://togogenome.org/gene/10090:Efcab9 ^@ http://purl.uniprot.org/uniprot/Q9DAM2 ^@ 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 ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand calcium-binding domain-containing protein 9|||Reduced interaction with CATSPERZ due to defects in Ca(2+)-binding; when associated with N-72.|||Reduced interaction with CATSPERZ due to defects in Ca(2+)-binding; when associated with Q-160. ^@ http://purl.uniprot.org/annotation/PRO_0000340649 http://togogenome.org/gene/10090:Mal ^@ http://purl.uniprot.org/uniprot/O09198 ^@ 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 2.|||MARVEL|||Myelin and lymphocyte protein ^@ http://purl.uniprot.org/annotation/PRO_0000156806|||http://purl.uniprot.org/annotation/VSP_031253 http://togogenome.org/gene/10090:Cacna2d4 ^@ http://purl.uniprot.org/uniprot/F8VPL1|||http://purl.uniprot.org/uniprot/Q5RJF7 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cache|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||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_0000304658|||http://purl.uniprot.org/annotation/PRO_0000304659|||http://purl.uniprot.org/annotation/PRO_0000304660|||http://purl.uniprot.org/annotation/VSP_044323 http://togogenome.org/gene/10090:Lasp1 ^@ http://purl.uniprot.org/uniprot/Q543N3|||http://purl.uniprot.org/uniprot/Q61792 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||LIM and SH3 domain protein 1|||LIM zinc-binding|||N-acetylmethionine|||N6-acetyllysine|||N6-methyllysine|||N6-succinyllysine|||Nebulin 1|||Nebulin 2|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKA|||Polar residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000075762 http://togogenome.org/gene/10090:Phka1 ^@ http://purl.uniprot.org/uniprot/A2AI91|||http://purl.uniprot.org/uniprot/P18826|||http://purl.uniprot.org/uniprot/Q3TQJ0|||http://purl.uniprot.org/uniprot/Q3UV91|||http://purl.uniprot.org/uniprot/Q8CBA7 ^@ Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Calmodulin-binding|||GH15-like|||In isoform 2.|||Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform|||Phosphorylase b kinase regulatory subunit alpha/beta C-terminal|||Phosphoserine|||Phosphoserine; by PKA|||Phosphoserine; by autocatalysis|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000057727|||http://purl.uniprot.org/annotation/VSP_004698 http://togogenome.org/gene/10090:Msl3 ^@ http://purl.uniprot.org/uniprot/Q9WVG9 ^@ 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.|||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_0000080248|||http://purl.uniprot.org/annotation/VSP_007638|||http://purl.uniprot.org/annotation/VSP_007639 http://togogenome.org/gene/10090:Vipr1 ^@ http://purl.uniprot.org/uniprot/P97751 ^@ 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; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Vasoactive intestinal polypeptide receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000012856 http://togogenome.org/gene/10090:Asah1 ^@ http://purl.uniprot.org/uniprot/Q78P93|||http://purl.uniprot.org/uniprot/Q9WV54 ^@ 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|||Site ^@ Acid ceramidase N-terminal|||Acid ceramidase subunit alpha|||Acid ceramidase subunit beta|||Choloylglycine hydrolase/NAAA C-terminal|||Important for catalytic activity|||Interchain (between alpha and beta subunits)|||N-linked (GlcNAc...) asparagine|||Nucleophile|||ceramidase ^@ http://purl.uniprot.org/annotation/PRO_0000002316|||http://purl.uniprot.org/annotation/PRO_0000002317|||http://purl.uniprot.org/annotation/PRO_5014310819 http://togogenome.org/gene/10090:Defa2 ^@ http://purl.uniprot.org/uniprot/Q8C1N9|||http://purl.uniprot.org/uniprot/Q8C1P0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Alpha-defensin N-terminal|||Beta/alpha-defensin C-terminal|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5004303924|||http://purl.uniprot.org/annotation/PRO_5015099048 http://togogenome.org/gene/10090:Zfp40 ^@ http://purl.uniprot.org/uniprot/B1B1D3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Gemin5 ^@ http://purl.uniprot.org/uniprot/E9PUU4|||http://purl.uniprot.org/uniprot/Q3TR97|||http://purl.uniprot.org/uniprot/Q8BX17 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site ^@ Anaphase-promoting complex subunit 4-like WD40|||Disordered|||Gem-associated protein 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Important for interaction with U1 snRNA|||Interaction with U4 snRNA|||Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA molecules|||Phosphoserine|||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_0000051005 http://togogenome.org/gene/10090:Rad54b ^@ http://purl.uniprot.org/uniprot/A0A0A0MQB1|||http://purl.uniprot.org/uniprot/Q6PFE3|||http://purl.uniprot.org/uniprot/Q8BKE5 ^@ 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 ^@ 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 isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000074341|||http://purl.uniprot.org/annotation/PRO_0000087353|||http://purl.uniprot.org/annotation/VSP_010775 http://togogenome.org/gene/10090:Tmem45b ^@ http://purl.uniprot.org/uniprot/Q8VCZ2 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Phosphoserine|||Transmembrane protein 45B ^@ http://purl.uniprot.org/annotation/PRO_0000271200 http://togogenome.org/gene/10090:Zfp512 ^@ http://purl.uniprot.org/uniprot/Q69Z99 ^@ 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 and acidic residues|||Basic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 512 ^@ http://purl.uniprot.org/annotation/PRO_0000333737 http://togogenome.org/gene/10090:Nup62cl ^@ http://purl.uniprot.org/uniprot/A2AG10|||http://purl.uniprot.org/uniprot/Q497V0 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Nucleoporin NSP1-like C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Eif5b ^@ http://purl.uniprot.org/uniprot/Q05D44|||http://purl.uniprot.org/uniprot/Q6A002 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Elongation factor Tu-type|||Eukaryotic translation initiation factor 5B|||G1|||G2|||G3|||G4|||G5|||Phosphoserine|||Phosphothreonine|||Translation initiation factor IF- 2|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000354071 http://togogenome.org/gene/10090:Sub1 ^@ http://purl.uniprot.org/uniprot/P11031 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ 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|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||Regulatory ^@ http://purl.uniprot.org/annotation/PRO_0000023286 http://togogenome.org/gene/10090:Arfrp1 ^@ http://purl.uniprot.org/uniprot/Q8BXL7 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ ADP-ribosylation factor-related protein 1|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000207488 http://togogenome.org/gene/10090:Mrpl19 ^@ http://purl.uniprot.org/uniprot/Q9D338 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Transit Peptide ^@ Disordered|||Large ribosomal subunit protein bL19m|||Mitochondrion|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000030474 http://togogenome.org/gene/10090:Cenph ^@ http://purl.uniprot.org/uniprot/Q9QYM8 ^@ Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Crosslink|||Modified Residue|||Region|||Sequence Conflict ^@ Centromere protein H|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000089479 http://togogenome.org/gene/10090:Rpl8 ^@ http://purl.uniprot.org/uniprot/P62918 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Modified Residue|||Region ^@ (3S)-3-hydroxyhistidine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein uL2 ^@ http://purl.uniprot.org/annotation/PRO_0000129744 http://togogenome.org/gene/10090:Irf2bp2 ^@ http://purl.uniprot.org/uniprot/E9Q1P8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interferon regulatory factor 2-binding protein 2|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pro residues|||RING-type; degenerate|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000418085 http://togogenome.org/gene/10090:Fastkd3 ^@ http://purl.uniprot.org/uniprot/Q8BSN9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ FAST kinase domain-containing protein 3, mitochondrial|||In isoform 2.|||In isoform 3.|||Mitochondrion|||RAP ^@ http://purl.uniprot.org/annotation/PRO_0000284716|||http://purl.uniprot.org/annotation/VSP_024624|||http://purl.uniprot.org/annotation/VSP_024625|||http://purl.uniprot.org/annotation/VSP_024626 http://togogenome.org/gene/10090:Cadm2 ^@ http://purl.uniprot.org/uniprot/Q8BLQ9 ^@ 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|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Cell adhesion molecule 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 2 and isoform 3.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000291971|||http://purl.uniprot.org/annotation/VSP_026336|||http://purl.uniprot.org/annotation/VSP_026337 http://togogenome.org/gene/10090:Tmem50a ^@ http://purl.uniprot.org/uniprot/Q52KP1|||http://purl.uniprot.org/uniprot/Q9CXL1 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Transmembrane ^@ Helical|||N-acetylserine|||Phosphoserine|||Removed|||Transmembrane protein 50A ^@ http://purl.uniprot.org/annotation/PRO_0000174182 http://togogenome.org/gene/10090:Rab10 ^@ http://purl.uniprot.org/uniprot/P61027 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict ^@ Effector region|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N6-acetyllysine|||Phosphothreonine; by LRRK2|||Probable constitutively active mutant unable to hydrolyze GTP; stimulates translocation of SLC2A4 to the plasma membrane.|||Ras-related protein Rab-10|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121147 http://togogenome.org/gene/10090:Kcne2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1J2|||http://purl.uniprot.org/uniprot/Q9D808 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||N-linked (GlcNAc...) asparagine|||Potassium voltage-gated channel subfamily E member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000144286 http://togogenome.org/gene/10090:Polr2b ^@ http://purl.uniprot.org/uniprot/Q8CFI7 ^@ 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 RPB2|||N6-methyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000048086 http://togogenome.org/gene/10090:Lrit3 ^@ http://purl.uniprot.org/uniprot/W8DXL4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Defects in depolarization of photoreceptors in the inner retina, and defects in cone photoreceptor light response. Gross morphology is normal.|||Disordered|||Helical|||Ig-like|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 3|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5007218087 http://togogenome.org/gene/10090:Gm13305 ^@ http://purl.uniprot.org/uniprot/P70225 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like C2-type|||Interleukin-11 receptor subunit alpha-2|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010915 http://togogenome.org/gene/10090:Rhbdd3 ^@ http://purl.uniprot.org/uniprot/B7ZNJ8|||http://purl.uniprot.org/uniprot/Q8BP97 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Peptidase S54 rhomboid|||Rhomboid domain-containing protein 3|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000079570|||http://purl.uniprot.org/annotation/VSP_014669 http://togogenome.org/gene/10090:Pcdha1 ^@ http://purl.uniprot.org/uniprot/Q91Y21 ^@ 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|||Cadherin|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099510 http://togogenome.org/gene/10090:Alox5ap ^@ http://purl.uniprot.org/uniprot/P30355 ^@ Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Arachidonate 5-lipoxygenase-activating protein|||Cytoplasmic|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000217753 http://togogenome.org/gene/10090:Spink13 ^@ http://purl.uniprot.org/uniprot/Q3UTS8 ^@ 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 13 ^@ http://purl.uniprot.org/annotation/PRO_0000344511 http://togogenome.org/gene/10090:Cog1 ^@ http://purl.uniprot.org/uniprot/Q9Z160 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Conserved oligomeric Golgi complex subunit 1|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213492 http://togogenome.org/gene/10090:Ppp1r14d ^@ http://purl.uniprot.org/uniprot/Q7TT52 ^@ 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.|||Interaction with protein phosphatase 1|||Polar residues|||Protein phosphatase 1 regulatory subunit 14D ^@ http://purl.uniprot.org/annotation/PRO_0000071498|||http://purl.uniprot.org/annotation/VSP_011842 http://togogenome.org/gene/10090:Rnf208 ^@ http://purl.uniprot.org/uniprot/Q8K0W3 ^@ 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_0000274614 http://togogenome.org/gene/10090:Gm14525 ^@ http://purl.uniprot.org/uniprot/B1AZA0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Wwc1 ^@ http://purl.uniprot.org/uniprot/Q5SXA9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ ADDV motif|||Acidic residues|||Basic and acidic residues|||C2|||Disordered|||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_0000242154 http://togogenome.org/gene/10090:Cpsf4 ^@ http://purl.uniprot.org/uniprot/B2LVG5|||http://purl.uniprot.org/uniprot/B2LVG6|||http://purl.uniprot.org/uniprot/Q8BQZ5 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Splice Variant|||Zinc Finger ^@ C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||CCHC-type|||Cleavage and polyadenylation specificity factor subunit 4|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000074403|||http://purl.uniprot.org/annotation/VSP_008603|||http://purl.uniprot.org/annotation/VSP_008604|||http://purl.uniprot.org/annotation/VSP_008605|||http://purl.uniprot.org/annotation/VSP_008606|||http://purl.uniprot.org/annotation/VSP_008607|||http://purl.uniprot.org/annotation/VSP_008608 http://togogenome.org/gene/10090:Nhlrc2 ^@ http://purl.uniprot.org/uniprot/B2RR26|||http://purl.uniprot.org/uniprot/Q8BZW8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Region|||Repeat ^@ Disordered|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||NHL 6|||NHL repeat-containing protein 2|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000313809 http://togogenome.org/gene/10090:Or5w8 ^@ http://purl.uniprot.org/uniprot/Q8VFQ8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sptb ^@ http://purl.uniprot.org/uniprot/Q3UGX2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Tex56 ^@ http://purl.uniprot.org/uniprot/Q497N7 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Testis expressed protein 56 ^@ http://purl.uniprot.org/annotation/PRO_0000297589 http://togogenome.org/gene/10090:Gcc2 ^@ http://purl.uniprot.org/uniprot/Q6P0A4|||http://purl.uniprot.org/uniprot/Q8CHG3 ^@ 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|||GRIP|||GRIP and coiled-coil domain-containing protein 2|||Mediates interaction with RAB6A|||Mediates interaction with RAB9A|||N-acetylmethionine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000190075 http://togogenome.org/gene/10090:Nars ^@ http://purl.uniprot.org/uniprot/A0A498WGK2|||http://purl.uniprot.org/uniprot/Q8BP47 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Aminoacyl-transfer RNA synthetases class-II family profile|||Asparagine--tRNA ligase, cytoplasmic|||Disordered|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000176497 http://togogenome.org/gene/10090:Adamts9 ^@ http://purl.uniprot.org/uniprot/E9PYV8 ^@ Disulfide Bond|||Domain Extent|||Modification|||Region ^@ Disulfide Bond|||Domain Extent ^@ GON ^@ http://togogenome.org/gene/10090:Gps2 ^@ http://purl.uniprot.org/uniprot/Q921N8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolished methylation; when associated with A-323.|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Decreased stability of the protein, probably due inability to interact with TBL1X; when associated with R-45. Abolishes sumoylation; when associated with R-45.|||Decreased stability of the protein, probably due inability to interact with TBL1X; when associated with R-71. Abolishes sumoylation; when associated with R-71.|||Disordered|||Does not affect localization to the nucleus.|||G protein pathway suppressor 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Increased stability due to impaired ubiquitination; when associated with A-254 and A-300.|||Increased stability due to impaired ubiquitination; when associated with A-254 and A-327.|||Increased stability due to impaired ubiquitination; when associated with A-300 and A-327.|||Omega-N-methylarginine; alternate|||Polar residues|||Promotes ubiquitination and degradation by the proteasome. Abolished methylation; when associated with A-312.|||interaction with SUMO ^@ http://purl.uniprot.org/annotation/PRO_0000441803 http://togogenome.org/gene/10090:Dnase1l1 ^@ http://purl.uniprot.org/uniprot/A0A158SIT2|||http://purl.uniprot.org/uniprot/Q9D7J6 ^@ 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 ^@ Deoxyribonuclease-1-like 1|||Endonuclease/exonuclease/phosphatase|||Essential for enzymatic activity|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000007285 http://togogenome.org/gene/10090:Pafah1b2 ^@ http://purl.uniprot.org/uniprot/Q61206 ^@ Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ N-acetylserine|||Phosphoserine|||Phosphothreonine|||Platelet-activating factor acetylhydrolase IB subunit alpha2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000058152 http://togogenome.org/gene/10090:Rgs3 ^@ http://purl.uniprot.org/uniprot/Q3TAS0|||http://purl.uniprot.org/uniprot/Q542M0|||http://purl.uniprot.org/uniprot/Q9DC04|||http://purl.uniprot.org/uniprot/Z4YJQ4 ^@ 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|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Polar residues|||Pro residues|||RGS|||Regulator of G-protein signaling 3 ^@ http://purl.uniprot.org/annotation/PRO_0000204183|||http://purl.uniprot.org/annotation/VSP_005663|||http://purl.uniprot.org/annotation/VSP_005664|||http://purl.uniprot.org/annotation/VSP_013966|||http://purl.uniprot.org/annotation/VSP_013967|||http://purl.uniprot.org/annotation/VSP_013968|||http://purl.uniprot.org/annotation/VSP_013969|||http://purl.uniprot.org/annotation/VSP_013970 http://togogenome.org/gene/10090:Mtnr1b ^@ http://purl.uniprot.org/uniprot/Q3SXF8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Atp2b1 ^@ http://purl.uniprot.org/uniprot/G5E829 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Basic and acidic residues|||Calmodulin-binding subdomain A|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-acetylglycine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKC|||Plasma membrane calcium-transporting ATPase 1|||Polar residues|||Removed|||Required for basolateral membrane targeting ^@ http://purl.uniprot.org/annotation/PRO_0000430669 http://togogenome.org/gene/10090:Gnat2 ^@ http://purl.uniprot.org/uniprot/A2AE33|||http://purl.uniprot.org/uniprot/P50149 ^@ 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-2|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000203741 http://togogenome.org/gene/10090:Gpr171 ^@ http://purl.uniprot.org/uniprot/Q8BG55 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||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_0000303237 http://togogenome.org/gene/10090:Cox20 ^@ http://purl.uniprot.org/uniprot/Q9D7J4 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytochrome c oxidase assembly protein COX20, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000186816 http://togogenome.org/gene/10090:Cldn34c1 ^@ http://purl.uniprot.org/uniprot/Q8CCR8|||http://purl.uniprot.org/uniprot/Q8K193 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Kdm4c ^@ http://purl.uniprot.org/uniprot/A2BEG5|||http://purl.uniprot.org/uniprot/Q8VCD7 ^@ 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 ^@ Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||JmjC|||JmjN|||Lysine-specific demethylase 4C|||PHD-type|||PHD-type 1|||PHD-type 2|||Tudor 1|||Tudor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000183178 http://togogenome.org/gene/10090:Neurod2 ^@ http://purl.uniprot.org/uniprot/Q3TYB2|||http://purl.uniprot.org/uniprot/Q62414 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Acidic residues|||BHLH|||Basic and acidic residues|||Basic residues|||Disordered|||Inhibits neurons differentiation.|||Neurogenic differentiation factor 2|||Nuclear localization signal|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127388 http://togogenome.org/gene/10090:Mettl27 ^@ http://purl.uniprot.org/uniprot/Q8BGM4|||http://purl.uniprot.org/uniprot/Q8BY07 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Methyltransferase ^@ http://togogenome.org/gene/10090:Ccdc90b ^@ http://purl.uniprot.org/uniprot/Q8C3X2 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide|||Transmembrane ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant|||Transit Peptide|||Transmembrane ^@ Coiled-coil domain-containing protein 90B, mitochondrial|||Helical|||In isoform 2.|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000295696|||http://purl.uniprot.org/annotation/VSP_027004 http://togogenome.org/gene/10090:Acat2 ^@ http://purl.uniprot.org/uniprot/Q8CAY6 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site ^@ Acetyl-CoA acetyltransferase, cytosolic|||Acyl-thioester intermediate|||Increases nucleophilicity of active site Cys|||N-acetylmethionine|||N6-acetyllysine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000206410 http://togogenome.org/gene/10090:Pim3 ^@ http://purl.uniprot.org/uniprot/P58750|||http://purl.uniprot.org/uniprot/Q3TX64 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site ^@ Enhances insulin secretion after glucose stimulation.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase pim-3 ^@ http://purl.uniprot.org/annotation/PRO_0000086534 http://togogenome.org/gene/10090:Or5b122 ^@ http://purl.uniprot.org/uniprot/Q8VEU6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tmprss11a ^@ http://purl.uniprot.org/uniprot/Q3UQ41 ^@ 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|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SEA|||Transmembrane protease serine 11A ^@ http://purl.uniprot.org/annotation/PRO_0000299318 http://togogenome.org/gene/10090:Rprd1a ^@ http://purl.uniprot.org/uniprot/Q8VDS4 ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ CID|||N-acetylserine|||Phosphoserine|||Regulation of nuclear pre-mRNA domain-containing protein 1A|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000311345 http://togogenome.org/gene/10090:Prkrip1 ^@ http://purl.uniprot.org/uniprot/Q9CWV6 ^@ 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|||Interaction with EIF2AK2|||PRKR-interacting protein 1|||Required for RNA-binding|||Required for nuclear localization ^@ http://purl.uniprot.org/annotation/PRO_0000324788 http://togogenome.org/gene/10090:Emb ^@ http://purl.uniprot.org/uniprot/P21995 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Embigin|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000014750 http://togogenome.org/gene/10090:Lins1 ^@ http://purl.uniprot.org/uniprot/Q3U1D0 ^@ 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.|||In isoform 3.|||Phosphoserine|||Protein Lines homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000397874|||http://purl.uniprot.org/annotation/VSP_039707|||http://purl.uniprot.org/annotation/VSP_039708 http://togogenome.org/gene/10090:Bhlhe40 ^@ http://purl.uniprot.org/uniprot/O35185|||http://purl.uniprot.org/uniprot/Q542A5 ^@ 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 ^@ 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|||Necessary for interaction with RXRA and repressor activity against RXRA|||Orange|||Phosphoserine|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127145 http://togogenome.org/gene/10090:Sult1c2 ^@ http://purl.uniprot.org/uniprot/Q9D939 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Proton acceptor|||Sulfotransferase 1C2 ^@ http://purl.uniprot.org/annotation/PRO_0000085133 http://togogenome.org/gene/10090:Rab40b ^@ http://purl.uniprot.org/uniprot/B1ATT4|||http://purl.uniprot.org/uniprot/Q4VA07|||http://purl.uniprot.org/uniprot/Q8VHP8 ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Region ^@ Disordered|||Ras-related protein Rab-40B|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000121260 http://togogenome.org/gene/10090:Ugt1a1 ^@ http://purl.uniprot.org/uniprot/Q63886 ^@ 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|||UDP-glucuronosyltransferase 1A1 ^@ http://purl.uniprot.org/annotation/PRO_0000036010 http://togogenome.org/gene/10090:Slc26a6 ^@ http://purl.uniprot.org/uniprot/Q8CIW6 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Does not inhibit formate transport in PMA-induced cells.|||Extracellular|||Helical|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc) asparagine|||Phosphoserine|||STAS|||Solute carrier family 26 member 6 ^@ http://purl.uniprot.org/annotation/PRO_0000423423|||http://purl.uniprot.org/annotation/VSP_047853|||http://purl.uniprot.org/annotation/VSP_047854|||http://purl.uniprot.org/annotation/VSP_061788|||http://purl.uniprot.org/annotation/VSP_061789 http://togogenome.org/gene/10090:Stk17b ^@ http://purl.uniprot.org/uniprot/Q8BG48 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 17B ^@ http://purl.uniprot.org/annotation/PRO_0000086707 http://togogenome.org/gene/10090:Pet117 ^@ http://purl.uniprot.org/uniprot/P0DJF2 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||Protein PET117 homolog, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000416097 http://togogenome.org/gene/10090:Fezf1 ^@ http://purl.uniprot.org/uniprot/Q0VDQ9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||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|||Engrailed homology 1 repressor|||Fez family zinc finger protein 1|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000295115 http://togogenome.org/gene/10090:Or2a20 ^@ http://purl.uniprot.org/uniprot/Q8VF17 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trhr ^@ http://purl.uniprot.org/uniprot/P21761|||http://purl.uniprot.org/uniprot/Q32MS1 ^@ 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|||Thyrotropin-releasing hormone receptor ^@ http://purl.uniprot.org/annotation/PRO_0000070188 http://togogenome.org/gene/10090:Lamtor5 ^@ http://purl.uniprot.org/uniprot/Q9D1L9 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ N-acetylmethionine|||Ragulator complex protein LAMTOR5 ^@ http://purl.uniprot.org/annotation/PRO_0000066008 http://togogenome.org/gene/10090:Dlgap1 ^@ http://purl.uniprot.org/uniprot/A0A3B2WD59|||http://purl.uniprot.org/uniprot/D3Z508|||http://purl.uniprot.org/uniprot/D3Z6F4|||http://purl.uniprot.org/uniprot/E9QAR5|||http://purl.uniprot.org/uniprot/Q3UHD8|||http://purl.uniprot.org/uniprot/Q3UVU8|||http://purl.uniprot.org/uniprot/Q9D415 ^@ 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|||Disks large-associated protein 1|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with DYL2|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000174289|||http://purl.uniprot.org/annotation/VSP_015408|||http://purl.uniprot.org/annotation/VSP_015409|||http://purl.uniprot.org/annotation/VSP_015410|||http://purl.uniprot.org/annotation/VSP_015411|||http://purl.uniprot.org/annotation/VSP_015412|||http://purl.uniprot.org/annotation/VSP_015413|||http://purl.uniprot.org/annotation/VSP_015414 http://togogenome.org/gene/10090:Dpagt1 ^@ http://purl.uniprot.org/uniprot/P42867|||http://purl.uniprot.org/uniprot/Q9CPT1 ^@ 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 ^@ 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|||In RNA edited version.|||Lumenal|||N-linked (GlcNAc...) asparagine|||UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000108762 http://togogenome.org/gene/10090:Map10 ^@ http://purl.uniprot.org/uniprot/Q8BJS7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Microtubule-associated protein 10|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000403447 http://togogenome.org/gene/10090:Or14c46 ^@ http://purl.uniprot.org/uniprot/B2RVZ1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp219 ^@ http://purl.uniprot.org/uniprot/Q4VA98|||http://purl.uniprot.org/uniprot/Q6IQX8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||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|||C2H2-type 8|||C2H2-type 9|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger protein 219 ^@ http://purl.uniprot.org/annotation/PRO_0000442537 http://togogenome.org/gene/10090:Grk1 ^@ http://purl.uniprot.org/uniprot/G3X905|||http://purl.uniprot.org/uniprot/Q4V9Z9 ^@ Active Site|||Binding Site|||Domain Extent|||Modification|||Modified Residue|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Modified Residue ^@ AGC-kinase C-terminal|||Cysteine methyl ester|||Protein kinase|||Proton acceptor|||RGS ^@ http://togogenome.org/gene/10090:Stard4 ^@ http://purl.uniprot.org/uniprot/Q80SX0|||http://purl.uniprot.org/uniprot/Q99JV5 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Turn ^@ In strain: C57BL/6.|||START|||StAR-related lipid transfer protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000220668 http://togogenome.org/gene/10090:Polr3a ^@ http://purl.uniprot.org/uniprot/B2RXC6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ RNA polymerase N-terminal ^@ http://togogenome.org/gene/10090:Dap ^@ http://purl.uniprot.org/uniprot/Q3U706|||http://purl.uniprot.org/uniprot/Q91XC8 ^@ 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|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000079783 http://togogenome.org/gene/10090:Hoxd3 ^@ http://purl.uniprot.org/uniprot/P09027|||http://purl.uniprot.org/uniprot/Q3UZR4 ^@ 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 ^@ Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-D3|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000200205 http://togogenome.org/gene/10090:Aspdh ^@ http://purl.uniprot.org/uniprot/Q9DCQ2 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Aspartate dehydrogenase domain-containing protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000144901 http://togogenome.org/gene/10090:Trex2 ^@ http://purl.uniprot.org/uniprot/Q3SXB3|||http://purl.uniprot.org/uniprot/Q9R1A9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Strand|||Turn ^@ Exonuclease|||Proton donor/acceptor|||Three prime repair exonuclease 2 ^@ http://purl.uniprot.org/annotation/PRO_0000109871 http://togogenome.org/gene/10090:Nos1 ^@ http://purl.uniprot.org/uniprot/Q9Z0J4 ^@ 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Calmodulin-binding|||Disordered|||FAD-binding FR-type|||Flavodoxin-like|||In isoform N-NOS-2.|||In isoform NNOS beta.|||In isoform NNOS gamma.|||In isoform NNOSMu.|||Interaction with DYNLL1/PIN|||Interaction with NOSIP|||Nitric oxide synthase 1|||PDZ|||Phosphoserine|||Polar residues|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000170922|||http://purl.uniprot.org/annotation/VSP_003575|||http://purl.uniprot.org/annotation/VSP_003576|||http://purl.uniprot.org/annotation/VSP_003577|||http://purl.uniprot.org/annotation/VSP_003578|||http://purl.uniprot.org/annotation/VSP_003579 http://togogenome.org/gene/10090:Tmem184c ^@ http://purl.uniprot.org/uniprot/Q3TPR7 ^@ 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.|||Polar residues|||Transmembrane protein 184C ^@ http://purl.uniprot.org/annotation/PRO_0000287568|||http://purl.uniprot.org/annotation/VSP_025567 http://togogenome.org/gene/10090:Rnf5 ^@ http://purl.uniprot.org/uniprot/O35445 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane|||Zinc Finger ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNF5|||Helical|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||RING-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000240394 http://togogenome.org/gene/10090:H2-Q2 ^@ http://purl.uniprot.org/uniprot/Q4KN81 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015097622 http://togogenome.org/gene/10090:Dusp6 ^@ http://purl.uniprot.org/uniprot/Q9DBB1 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Dual specificity protein phosphatase 6|||Phosphocysteine intermediate|||Rhodanese|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094805 http://togogenome.org/gene/10090:Tmem235 ^@ http://purl.uniprot.org/uniprot/A0A811BM33|||http://purl.uniprot.org/uniprot/B1AQL3 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||Transmembrane protein 235 ^@ http://purl.uniprot.org/annotation/PRO_0000406903|||http://purl.uniprot.org/annotation/PRO_5032919286 http://togogenome.org/gene/10090:Macir ^@ http://purl.uniprot.org/uniprot/Q8VEB3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Macrophage immunometabolism regulator|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000316777 http://togogenome.org/gene/10090:Rnf215 ^@ http://purl.uniprot.org/uniprot/Q5SPX3 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||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_0000287535 http://togogenome.org/gene/10090:Or2g25 ^@ http://purl.uniprot.org/uniprot/L7N1Z1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sfswap ^@ http://purl.uniprot.org/uniprot/Q3USH5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||Basic residues|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SURP motif 1|||SURP motif 2|||Splicing factor, suppressor of white-apricot homolog ^@ http://purl.uniprot.org/annotation/PRO_0000413023 http://togogenome.org/gene/10090:Ifnl3 ^@ http://purl.uniprot.org/uniprot/Q8CGK6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ Interferon lambda-3 ^@ http://purl.uniprot.org/annotation/PRO_0000015512 http://togogenome.org/gene/10090:Necap2 ^@ http://purl.uniprot.org/uniprot/Q9D1J1 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand ^@ Chain|||Helix|||Modified Residue|||Motif|||Region|||Strand ^@ Adaptin ear-binding coat-associated protein 2|||Disordered|||Phosphoserine|||WXXF motif 1|||WXXF motif 2 ^@ http://purl.uniprot.org/annotation/PRO_0000213072 http://togogenome.org/gene/10090:Usp19 ^@ http://purl.uniprot.org/uniprot/A0A0A6YWX1|||http://purl.uniprot.org/uniprot/E9Q9M5|||http://purl.uniprot.org/uniprot/J3KMM1|||http://purl.uniprot.org/uniprot/Q3UJD6 ^@ 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|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Basic and acidic residues|||CS|||CS 1|||CS 2|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||MYND-type|||Nucleophile|||Phosphoserine|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 19 ^@ http://purl.uniprot.org/annotation/PRO_0000295157|||http://purl.uniprot.org/annotation/VSP_026769|||http://purl.uniprot.org/annotation/VSP_026770 http://togogenome.org/gene/10090:C1ql1 ^@ http://purl.uniprot.org/uniprot/A0A3B0ITH6|||http://purl.uniprot.org/uniprot/O88992|||http://purl.uniprot.org/uniprot/Q0VF50|||http://purl.uniprot.org/uniprot/Q8R1Z2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ C1q|||C1q-related factor|||Collagen-like|||Disordered|||Does not affect heterooligomerization with C1QL4; when associated with A-28.|||Does not affect heterooligomerization with C1QL4; when associated with A-32.|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000003528|||http://purl.uniprot.org/annotation/PRO_5004178687|||http://purl.uniprot.org/annotation/PRO_5017323397 http://togogenome.org/gene/10090:Skint2 ^@ http://purl.uniprot.org/uniprot/A7XUX6|||http://purl.uniprot.org/uniprot/B2ZEZ5|||http://purl.uniprot.org/uniprot/M9MMJ5 ^@ 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|||Helical|||Ig-like|||Ig-like C1-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Selection and upkeep of intraepithelial T-cells protein 2 ^@ http://purl.uniprot.org/annotation/PRO_5000271635|||http://purl.uniprot.org/annotation/PRO_5004100763|||http://purl.uniprot.org/annotation/PRO_5015087183|||http://purl.uniprot.org/annotation/VSP_034877|||http://purl.uniprot.org/annotation/VSP_034878|||http://purl.uniprot.org/annotation/VSP_034879 http://togogenome.org/gene/10090:Pcdhga11 ^@ http://purl.uniprot.org/uniprot/Q91XY8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Cadherin|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:2010106E10Rik ^@ http://purl.uniprot.org/uniprot/A2ANY3|||http://purl.uniprot.org/uniprot/Q9D3Q9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015086029|||http://purl.uniprot.org/annotation/PRO_5015099680 http://togogenome.org/gene/10090:Tada1 ^@ http://purl.uniprot.org/uniprot/Q99LM9 ^@ Chain|||Molecule Processing ^@ Chain ^@ Transcriptional adapter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000316016 http://togogenome.org/gene/10090:Fignl2 ^@ http://purl.uniprot.org/uniprot/J3QK54 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ AAA+ ATPase|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gm36079 ^@ http://purl.uniprot.org/uniprot/Q3T9V6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gon4l ^@ http://purl.uniprot.org/uniprot/E9Q507|||http://purl.uniprot.org/uniprot/Q32NZ8 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Myb-like|||Polar residues ^@ http://togogenome.org/gene/10090:Rpl11 ^@ http://purl.uniprot.org/uniprot/Q9CXW4 ^@ 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)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Large ribosomal subunit protein uL5|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000125083 http://togogenome.org/gene/10090:Pdcd4 ^@ http://purl.uniprot.org/uniprot/Q61823 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||MI 1|||MI 2|||N-acetylmethionine|||No effect on interaction with EIF4A1.|||Nuclear localization signal|||Phosphodegron|||Phosphoserine|||Phosphoserine; by PKB|||Phosphoserine; by PKB and RPS6KB1|||Phosphotyrosine|||Polar residues|||Programmed cell death protein 4|||Strongly reduced interaction with EIF4A1. ^@ http://purl.uniprot.org/annotation/PRO_0000256520 http://togogenome.org/gene/10090:Ppp1r36 ^@ http://purl.uniprot.org/uniprot/D3Z0R2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein phosphatase 1 regulatory subunit 36 ^@ http://purl.uniprot.org/annotation/PRO_0000415809 http://togogenome.org/gene/10090:Or11q2 ^@ http://purl.uniprot.org/uniprot/A2AHM8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trex1 ^@ http://purl.uniprot.org/uniprot/Q91XB0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||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|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||Impaired ability to associate with CGAS-DNA droplets.|||Interaction with UBQLN1|||Loss of activity. Loss of endogenous retroelement metabolization.|||Necessary for cytoplasmic retention|||Necessary for endoplasmic reticulum localization|||Phosphoserine|||Polar residues|||Proton donor/acceptor|||Reduces activity. Loss of endogenous retroelement metabolization.|||Strongly reduces activity.|||Three-prime repair exonuclease 1 ^@ http://purl.uniprot.org/annotation/PRO_0000109869 http://togogenome.org/gene/10090:Mef2bl ^@ http://purl.uniprot.org/uniprot/K7N7F1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||MADS-box ^@ http://togogenome.org/gene/10090:Or13a22 ^@ http://purl.uniprot.org/uniprot/Q8VGL3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or6c201 ^@ http://purl.uniprot.org/uniprot/Q8VGC2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp879 ^@ http://purl.uniprot.org/uniprot/Q147Z4|||http://purl.uniprot.org/uniprot/Q8BI99 ^@ 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 879 ^@ http://purl.uniprot.org/annotation/PRO_0000393968 http://togogenome.org/gene/10090:Fzd10 ^@ http://purl.uniprot.org/uniprot/Q149J3|||http://purl.uniprot.org/uniprot/Q8BKG4 ^@ 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_0000013006|||http://purl.uniprot.org/annotation/PRO_5014306907 http://togogenome.org/gene/10090:Tada2b ^@ http://purl.uniprot.org/uniprot/D3Z4Z0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Myb-like|||SANT|||ZZ-type ^@ http://togogenome.org/gene/10090:Asb8 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1W1|||http://purl.uniprot.org/uniprot/Q8CDF0|||http://purl.uniprot.org/uniprot/Q91ZT9|||http://purl.uniprot.org/uniprot/Q9D4Y2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat and SOCS box protein 8|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066939 http://togogenome.org/gene/10090:Prl7d1 ^@ http://purl.uniprot.org/uniprot/P04769|||http://purl.uniprot.org/uniprot/Q5SVM4|||http://purl.uniprot.org/uniprot/Q9DAY8 ^@ Binding Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Signal Peptide ^@ Prolactin-7D1 ^@ http://purl.uniprot.org/annotation/PRO_0000032970|||http://purl.uniprot.org/annotation/PRO_5015098022|||http://purl.uniprot.org/annotation/PRO_5015099690 http://togogenome.org/gene/10090:Med31 ^@ http://purl.uniprot.org/uniprot/Q9CXU1 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Mediator of RNA polymerase II transcription subunit 31|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000212528 http://togogenome.org/gene/10090:Or8d4 ^@ http://purl.uniprot.org/uniprot/Q8VGB4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:B4galnt4 ^@ http://purl.uniprot.org/uniprot/Q766D5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 1|||N-linked (GlcNAc...) asparagine|||PA14 ^@ http://purl.uniprot.org/annotation/PRO_0000252371|||http://purl.uniprot.org/annotation/VSP_020917 http://togogenome.org/gene/10090:Zbtb32 ^@ http://purl.uniprot.org/uniprot/B2RQ06|||http://purl.uniprot.org/uniprot/Q9JKD9 ^@ 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 ^@ BTB|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In isoform 2.|||Zinc finger and BTB domain-containing protein 32 ^@ http://purl.uniprot.org/annotation/PRO_0000273418|||http://purl.uniprot.org/annotation/VSP_022552 http://togogenome.org/gene/10090:Fam178b ^@ http://purl.uniprot.org/uniprot/E9PUL8|||http://purl.uniprot.org/uniprot/E9PXB2|||http://purl.uniprot.org/uniprot/Q24JP3 ^@ 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|||Coiled-coil SMC6 And NSE5 INteracting (CANIN)|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Protein FAM178B ^@ http://purl.uniprot.org/annotation/PRO_0000320194|||http://purl.uniprot.org/annotation/VSP_031637|||http://purl.uniprot.org/annotation/VSP_031638|||http://purl.uniprot.org/annotation/VSP_031639|||http://purl.uniprot.org/annotation/VSP_031640 http://togogenome.org/gene/10090:Ppm1g ^@ http://purl.uniprot.org/uniprot/Q61074 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ 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_0000057751 http://togogenome.org/gene/10090:Ccdc122 ^@ http://purl.uniprot.org/uniprot/Q4VA24|||http://purl.uniprot.org/uniprot/Q8BVN0 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Coiled-coil domain-containing protein 122 ^@ http://purl.uniprot.org/annotation/PRO_0000286599 http://togogenome.org/gene/10090:Nfkbib ^@ http://purl.uniprot.org/uniprot/Q60778 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Disordered|||NF-kappa-B inhibitor beta|||Phosphoserine|||Phosphoserine; by RPS6KA1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000067005 http://togogenome.org/gene/10090:Hoxa7 ^@ http://purl.uniprot.org/uniprot/P02830 ^@ 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|||Disordered|||Homeobox|||Homeobox protein Hox-A7 ^@ http://purl.uniprot.org/annotation/PRO_0000200072 http://togogenome.org/gene/10090:Slco2b1 ^@ http://purl.uniprot.org/uniprot/Q3TQJ3|||http://purl.uniprot.org/uniprot/Q3V1K7|||http://purl.uniprot.org/uniprot/Q8BXB6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic 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|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier organic anion transporter family member 2B1 ^@ http://purl.uniprot.org/annotation/PRO_0000191062 http://togogenome.org/gene/10090:Mybpc3 ^@ http://purl.uniprot.org/uniprot/Q3UIK0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Fibronectin type-III|||Ig-like|||Polar residues ^@ http://togogenome.org/gene/10090:Trdmt1 ^@ http://purl.uniprot.org/uniprot/O55055|||http://purl.uniprot.org/uniprot/Q5I0V6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ SAM-dependent MTase C5-type|||tRNA (cytosine(38)-C(5))-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000088041 http://togogenome.org/gene/10090:Ccdc185 ^@ http://purl.uniprot.org/uniprot/Q3V118 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:5730507C01Rik ^@ http://purl.uniprot.org/uniprot/J3QPX0|||http://purl.uniprot.org/uniprot/Q3UT17 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ccdc175 ^@ http://purl.uniprot.org/uniprot/E9PVB3 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Coiled-coil domain-containing protein 175 ^@ http://purl.uniprot.org/annotation/PRO_0000420180 http://togogenome.org/gene/10090:Oxtr ^@ http://purl.uniprot.org/uniprot/P97926 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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|||Oxytocin receptor|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000070000 http://togogenome.org/gene/10090:Zfp934 ^@ http://purl.uniprot.org/uniprot/K7N6H3|||http://purl.uniprot.org/uniprot/Q8BSR1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Taf4b ^@ http://purl.uniprot.org/uniprot/A0A3B2W725|||http://purl.uniprot.org/uniprot/G5E8Z2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Histone-fold|||Nuclear export signal|||Phosphoserine|||Polar residues|||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_0000430940 http://togogenome.org/gene/10090:Col24a1 ^@ http://purl.uniprot.org/uniprot/Q30D77 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ 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 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|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000317617 http://togogenome.org/gene/10090:Vmn2r111 ^@ http://purl.uniprot.org/uniprot/K7N674 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908716 http://togogenome.org/gene/10090:Pde6h ^@ http://purl.uniprot.org/uniprot/P61249 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic residues|||Disordered|||Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma ^@ http://purl.uniprot.org/annotation/PRO_0000166121 http://togogenome.org/gene/10090:Abracl ^@ http://purl.uniprot.org/uniprot/E9QMV2|||http://purl.uniprot.org/uniprot/Q4KML4 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Costars|||Costars family protein ABRACL|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000365536 http://togogenome.org/gene/10090:Irgq ^@ http://purl.uniprot.org/uniprot/Q8VIM9 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||IRG-type G|||Immunity-related GTPase family Q protein|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000264464 http://togogenome.org/gene/10090:Kcnh8 ^@ http://purl.uniprot.org/uniprot/F6TUN6|||http://purl.uniprot.org/uniprot/P59111 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||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_0000054019 http://togogenome.org/gene/10090:Apol7b ^@ http://purl.uniprot.org/uniprot/B1AQP7 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Garin1a ^@ http://purl.uniprot.org/uniprot/B2RXB0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Golgi-associated RAB2 interactor protein 1A|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000455123 http://togogenome.org/gene/10090:Rab27a ^@ http://purl.uniprot.org/uniprot/Q9ERI2 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Strand|||Turn ^@ Cysteine methyl ester|||Effector region|||Loss of GTPase activity.|||N-acetylserine|||Phosphoserine|||Ras-related protein Rab-27A|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121222 http://togogenome.org/gene/10090:Atp5a1 ^@ http://purl.uniprot.org/uniprot/Q03265 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ ATP synthase subunit alpha, mitochondrial|||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_0000002425 http://togogenome.org/gene/10090:Slc13a5 ^@ http://purl.uniprot.org/uniprot/Q67BT3 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Na(+)/citrate cotransporter ^@ http://purl.uniprot.org/annotation/PRO_0000260102 http://togogenome.org/gene/10090:H1f8 ^@ http://purl.uniprot.org/uniprot/Q8VIK3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||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_0000343413|||http://purl.uniprot.org/annotation/VSP_034593 http://togogenome.org/gene/10090:Sord ^@ http://purl.uniprot.org/uniprot/Q64442 ^@ 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-acetylalanine|||Phosphoserine|||Removed|||Sorbitol dehydrogenase ^@ http://purl.uniprot.org/annotation/PRO_0000000882 http://togogenome.org/gene/10090:Slc35e3 ^@ http://purl.uniprot.org/uniprot/Q6PGC7 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Solute carrier family 35 member E3 ^@ http://purl.uniprot.org/annotation/PRO_0000297900 http://togogenome.org/gene/10090:Marveld1 ^@ http://purl.uniprot.org/uniprot/Q7TQJ1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||MARVEL|||MARVEL domain-containing protein 1|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000271523 http://togogenome.org/gene/10090:Rps19bp1 ^@ http://purl.uniprot.org/uniprot/Q8C6B9 ^@ 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_0000252394 http://togogenome.org/gene/10090:Cdkl2 ^@ http://purl.uniprot.org/uniprot/Q149A0|||http://purl.uniprot.org/uniprot/Q9QUK0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Cyclin-dependent kinase-like 2|||Disordered|||In isoform 2.|||Protein kinase|||Proton acceptor|||[NKR]KIAxRE ^@ http://purl.uniprot.org/annotation/PRO_0000085816|||http://purl.uniprot.org/annotation/VSP_016146|||http://purl.uniprot.org/annotation/VSP_016147 http://togogenome.org/gene/10090:Sap25 ^@ http://purl.uniprot.org/uniprot/E9Q529|||http://purl.uniprot.org/uniprot/Q1EHW4 ^@ Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Region|||Strand|||Turn ^@ Disordered|||Histone deacetylase complex subunit SAP25|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000350874 http://togogenome.org/gene/10090:Col6a4 ^@ http://purl.uniprot.org/uniprot/A2AX52|||http://purl.uniprot.org/uniprot/Q9CTL0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Cell attachment site|||Collagen alpha-4(VI) chain|||Disordered|||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 ^@ http://purl.uniprot.org/annotation/PRO_5000214197 http://togogenome.org/gene/10090:Fzd7 ^@ http://purl.uniprot.org/uniprot/Q61090|||http://purl.uniprot.org/uniprot/Q810L8|||http://purl.uniprot.org/uniprot/Q9CUZ6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Essential for SDCBP-mediated plasma membrane phosphatidylinositol-4,5-bisphosphate recognition|||Extracellular|||FZ|||Frizzled-7|||Frizzled/Smoothened 7TM|||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_0000012997 http://togogenome.org/gene/10090:Cts7 ^@ http://purl.uniprot.org/uniprot/Q91ZF2 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cathepsin 7|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000415396|||http://purl.uniprot.org/annotation/PRO_5000088249 http://togogenome.org/gene/10090:Wfdc10 ^@ http://purl.uniprot.org/uniprot/Q3V2J9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ WAP ^@ http://purl.uniprot.org/annotation/PRO_5015097535 http://togogenome.org/gene/10090:Fhl1 ^@ http://purl.uniprot.org/uniprot/A2AEX8|||http://purl.uniprot.org/uniprot/A2AEY2|||http://purl.uniprot.org/uniprot/P97447 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ C4-type|||Four and a half LIM domains protein 1|||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|||N-acetylserine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000075736|||http://purl.uniprot.org/annotation/VSP_003120|||http://purl.uniprot.org/annotation/VSP_003121 http://togogenome.org/gene/10090:Prpf31 ^@ http://purl.uniprot.org/uniprot/Q8CCF0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||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|||U4/U6 small nuclear ribonucleoprotein Prp31 ^@ http://purl.uniprot.org/annotation/PRO_0000227800|||http://purl.uniprot.org/annotation/VSP_017589|||http://purl.uniprot.org/annotation/VSP_017590|||http://purl.uniprot.org/annotation/VSP_017591 http://togogenome.org/gene/10090:Mob4 ^@ http://purl.uniprot.org/uniprot/Q6PEB6 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ MOB-like protein phocein ^@ http://purl.uniprot.org/annotation/PRO_0000193577 http://togogenome.org/gene/10090:Or8k17 ^@ http://purl.uniprot.org/uniprot/Q8VGS2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wsb1 ^@ http://purl.uniprot.org/uniprot/O54927|||http://purl.uniprot.org/uniprot/Q3TFQ2|||http://purl.uniprot.org/uniprot/Q8C841 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ SOCS box|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat and SOCS box-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000051458 http://togogenome.org/gene/10090:Cetn3 ^@ http://purl.uniprot.org/uniprot/O35648|||http://purl.uniprot.org/uniprot/Q545L8 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Centrin-3|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000073564 http://togogenome.org/gene/10090:Spata45 ^@ http://purl.uniprot.org/uniprot/Q9CVW4 ^@ Chain|||Molecule Processing ^@ Chain ^@ Spermatogenesis-associated protein 45 ^@ http://purl.uniprot.org/annotation/PRO_0000285786 http://togogenome.org/gene/10090:Btnl9 ^@ http://purl.uniprot.org/uniprot/Q8BJE2 ^@ 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 ^@ B30.2/SPRY|||Butyrophilin-like protein 9|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000416100|||http://purl.uniprot.org/annotation/VSP_042501|||http://purl.uniprot.org/annotation/VSP_042502|||http://purl.uniprot.org/annotation/VSP_042503 http://togogenome.org/gene/10090:Amtn ^@ http://purl.uniprot.org/uniprot/Q9D3J8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Amelotin|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000022614 http://togogenome.org/gene/10090:Akap8l ^@ http://purl.uniprot.org/uniprot/Q5RL57|||http://purl.uniprot.org/uniprot/Q9D0K8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||C2H2 AKAP95-type|||Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Pglyrp1 ^@ http://purl.uniprot.org/uniprot/O88593|||http://purl.uniprot.org/uniprot/Q4FK86 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ N-acetylmuramoyl-L-alanine amidase|||Peptidoglycan recognition protein 1|||Peptidoglycan recognition protein family|||Peptidoglycan-recognition protein ^@ http://purl.uniprot.org/annotation/PRO_0000023902|||http://purl.uniprot.org/annotation/PRO_5009970951 http://togogenome.org/gene/10090:Hsd17b13 ^@ http://purl.uniprot.org/uniprot/Q8VCR2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 17-beta-hydroxysteroid dehydrogenase 13|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000042584|||http://purl.uniprot.org/annotation/VSP_015861 http://togogenome.org/gene/10090:Ecel1 ^@ http://purl.uniprot.org/uniprot/Q3TX93|||http://purl.uniprot.org/uniprot/Q9JMI0 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Endothelin-converting enzyme-like 1|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Peptidase M13 C-terminal|||Peptidase M13 N-terminal|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000078225 http://togogenome.org/gene/10090:Bbs5 ^@ http://purl.uniprot.org/uniprot/Q9CZQ9 ^@ Chain|||Molecule Processing ^@ Chain ^@ Bardet-Biedl syndrome 5 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000223256 http://togogenome.org/gene/10090:Tfdp2 ^@ http://purl.uniprot.org/uniprot/E9PWL5|||http://purl.uniprot.org/uniprot/F6QG91|||http://purl.uniprot.org/uniprot/J3QK26|||http://purl.uniprot.org/uniprot/Q3TY79|||http://purl.uniprot.org/uniprot/Q56A02|||http://purl.uniprot.org/uniprot/Q8BHD2|||http://purl.uniprot.org/uniprot/Q8C537|||http://purl.uniprot.org/uniprot/Q8C8M7 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Acidic residues|||Disordered|||E2F/DP family winged-helix DNA-binding|||Polar residues|||Transcription factor DP C-terminal ^@ http://togogenome.org/gene/10090:Tnfrsf18 ^@ http://purl.uniprot.org/uniprot/O35714|||http://purl.uniprot.org/uniprot/Q540M6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Does not bind to SIVA1.|||Extracellular|||Helical|||In isoform B.|||In isoform C.|||In isoform D.|||N-linked (GlcNAc...) asparagine|||No effect on binding to SIVA1; when associated with G-204.|||No effect on binding to SIVA1; when associated with R-201.|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 18 ^@ http://purl.uniprot.org/annotation/PRO_0000034596|||http://purl.uniprot.org/annotation/PRO_5010139287|||http://purl.uniprot.org/annotation/VSP_006509|||http://purl.uniprot.org/annotation/VSP_006510|||http://purl.uniprot.org/annotation/VSP_006511 http://togogenome.org/gene/10090:Ctnna2 ^@ http://purl.uniprot.org/uniprot/Q61301 ^@ 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|||Catenin alpha-2|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000064264|||http://purl.uniprot.org/annotation/VSP_006734|||http://purl.uniprot.org/annotation/VSP_038010 http://togogenome.org/gene/10090:Mypn ^@ http://purl.uniprot.org/uniprot/Q5DTJ9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||Myopalladin|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000240490 http://togogenome.org/gene/10090:Syde2 ^@ http://purl.uniprot.org/uniprot/E9PUP1|||http://purl.uniprot.org/uniprot/Q8BKW6 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Rho-GAP ^@ http://togogenome.org/gene/10090:Kpna1 ^@ http://purl.uniprot.org/uniprot/Q60960 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ 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|||N-acetylmethionine|||NLS binding site (major)|||NLS binding site (minor)|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000120720 http://togogenome.org/gene/10090:Acot7 ^@ http://purl.uniprot.org/uniprot/E9PYH2|||http://purl.uniprot.org/uniprot/Q91V12 ^@ 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 ^@ Basic and acidic residues|||Cytosolic acyl coenzyme A thioester hydrolase|||Disordered|||Dramatic reduction in catalytic activity.|||HotDog ACOT-type|||HotDog ACOT-type 1|||HotDog ACOT-type 2|||In isoform A.|||In isoform C.|||In isoform D.|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000053807|||http://purl.uniprot.org/annotation/VSP_000157|||http://purl.uniprot.org/annotation/VSP_000158|||http://purl.uniprot.org/annotation/VSP_016955 http://togogenome.org/gene/10090:Cebpd ^@ http://purl.uniprot.org/uniprot/B9EIA9|||http://purl.uniprot.org/uniprot/Q00322|||http://purl.uniprot.org/uniprot/Q3UE64 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ BZIP|||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|||N-acetylserine|||Pro residues|||Removed|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076622 http://togogenome.org/gene/10090:Dqx1 ^@ http://purl.uniprot.org/uniprot/Q924H9 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Splice Variant ^@ ATP-dependent RNA helicase DQX1|||DEAQ box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000284378|||http://purl.uniprot.org/annotation/VSP_024473 http://togogenome.org/gene/10090:Wwc2 ^@ http://purl.uniprot.org/uniprot/Q6NXJ0 ^@ 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|||C2|||Disordered|||Phosphoserine|||Phosphothreonine|||Protein WWC2|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000309491 http://togogenome.org/gene/10090:Gckr ^@ http://purl.uniprot.org/uniprot/Q91X44 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Region|||Splice Variant ^@ Essential for interaction with GCK|||Glucokinase regulatory protein|||Important for interaction with GCK|||In isoform 1.|||SIS 1|||SIS 2 ^@ http://purl.uniprot.org/annotation/PRO_0000248832|||http://purl.uniprot.org/annotation/VSP_061733 http://togogenome.org/gene/10090:Phox2a ^@ http://purl.uniprot.org/uniprot/Q62066 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Paired mesoderm homeobox protein 2A|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000049260 http://togogenome.org/gene/10090:Svs3b ^@ http://purl.uniprot.org/uniprot/Q8BZH8 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099056 http://togogenome.org/gene/10090:Serinc4 ^@ http://purl.uniprot.org/uniprot/Q5XK03 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Serine incorporator 4 ^@ http://purl.uniprot.org/annotation/PRO_0000333872 http://togogenome.org/gene/10090:Rdm1 ^@ http://purl.uniprot.org/uniprot/Q9CQK3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000299530 http://togogenome.org/gene/10090:Hmmr ^@ http://purl.uniprot.org/uniprot/Q00547|||http://purl.uniprot.org/uniprot/Q3UPW7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 1|||2|||3|||4|||5|||5 X 21 AA tandem repeats|||Basic and acidic residues|||Disordered|||Hyaluronan mediated motility receptor|||Hyaluronic acid-binding|||In isoform RHAMM1.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with FAM83D ^@ http://purl.uniprot.org/annotation/PRO_0000084008|||http://purl.uniprot.org/annotation/VSP_004287 http://togogenome.org/gene/10090:Pxt1 ^@ http://purl.uniprot.org/uniprot/Q8K459 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Motif|||Mutagenesis Site ^@ Abolishes peroxisome localization.|||Microbody targeting signal|||Peroxisomal testis-specific protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000324594 http://togogenome.org/gene/10090:Gm5591 ^@ http://purl.uniprot.org/uniprot/Q8CDK1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF4629|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or11h23 ^@ http://purl.uniprot.org/uniprot/E9Q9Z0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Crebzf ^@ http://purl.uniprot.org/uniprot/Q91ZR3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Basic motif|||CREB/ATF bZIP transcription factor|||Disordered|||HCFC1-binding motif (HBM)|||Leucine-zipper|||Phosphoserine|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076646 http://togogenome.org/gene/10090:Fitm1 ^@ http://purl.uniprot.org/uniprot/Q91V79 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Fat storage-inducing transmembrane protein 1|||Helical|||Important for catalytic activity|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000319576 http://togogenome.org/gene/10090:Crygf ^@ http://purl.uniprot.org/uniprot/Q9CXV3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ 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 F ^@ http://purl.uniprot.org/annotation/PRO_0000057600 http://togogenome.org/gene/10090:Vsig10l ^@ http://purl.uniprot.org/uniprot/A0A0N4SUI1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5012655664 http://togogenome.org/gene/10090:Disc1 ^@ http://purl.uniprot.org/uniprot/Q811T9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Abolished interaction with ATF4.|||Disordered|||Disrupted in schizophrenia 1 homolog|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ATF4 and ATF5|||Interaction with MAP1A|||Interaction with NDEL1|||Interaction with NDEL1 and PAFAH1B1|||Interaction with PAFAH1B1|||Interaction with TRAF3IP1|||Necessary and sufficient for interaction with PCNT and localization at the centrosome|||Polar residues|||Required for localization to punctate cytoplasmic foci ^@ http://purl.uniprot.org/annotation/PRO_0000240230|||http://purl.uniprot.org/annotation/VSP_019318|||http://purl.uniprot.org/annotation/VSP_019319|||http://purl.uniprot.org/annotation/VSP_019320|||http://purl.uniprot.org/annotation/VSP_019321 http://togogenome.org/gene/10090:Camk2n1 ^@ http://purl.uniprot.org/uniprot/Q6QWF9 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ CAMK2 inhibitory domain|||Calcium/calmodulin-dependent protein kinase II inhibitor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000338394 http://togogenome.org/gene/10090:Dpysl4 ^@ http://purl.uniprot.org/uniprot/Q3TMU8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Amidohydrolase-related ^@ http://togogenome.org/gene/10090:Gpatch1 ^@ http://purl.uniprot.org/uniprot/Q9DBM1 ^@ 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|||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_0000287458 http://togogenome.org/gene/10090:Ndufaf6 ^@ http://purl.uniprot.org/uniprot/A2AIL4 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||NADH dehydrogenase (ubiquinone) complex I, assembly factor 6 ^@ http://purl.uniprot.org/annotation/PRO_0000291773 http://togogenome.org/gene/10090:Aqp6 ^@ http://purl.uniprot.org/uniprot/Q8C4A0 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Topological Domain|||Transmembrane ^@ Aquaporin-6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000063956 http://togogenome.org/gene/10090:Ephx2 ^@ http://purl.uniprot.org/uniprot/A8JYK8|||http://purl.uniprot.org/uniprot/P34914|||http://purl.uniprot.org/uniprot/Q3UQ71 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||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|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ AB hydrolase-1|||Bifunctional epoxide hydrolase 2|||Epoxide hydrolase|||In isoform 2.|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Phosphatase|||Phosphoserine|||Proton acceptor|||Proton donor|||S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000084112|||http://purl.uniprot.org/annotation/VSP_013904 http://togogenome.org/gene/10090:Zmym2 ^@ http://purl.uniprot.org/uniprot/Q9CU65 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Zinc Finger ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterozygous mutant mice show anomalies of the kidney and urinary tract.|||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|||Zinc finger MYM-type protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000191383 http://togogenome.org/gene/10090:Klra10 ^@ http://purl.uniprot.org/uniprot/Q9R1G6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Lyrm9 ^@ http://purl.uniprot.org/uniprot/Q3UN90 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ LYR motif-containing protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000345399 http://togogenome.org/gene/10090:C1qtnf1 ^@ http://purl.uniprot.org/uniprot/A0A3B0J1J8|||http://purl.uniprot.org/uniprot/Q9QXP7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 1|||Disordered|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000320081|||http://purl.uniprot.org/annotation/PRO_5030075162 http://togogenome.org/gene/10090:Krtap6-2 ^@ http://purl.uniprot.org/uniprot/O08884 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ 66 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 6-2 ^@ http://purl.uniprot.org/annotation/PRO_0000361662 http://togogenome.org/gene/10090:Tdrd12 ^@ http://purl.uniprot.org/uniprot/Q9CWU0 ^@ 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 ^@ CS|||DEAH box|||Disordered|||Helicase ATP-binding|||In isoform 2.|||Putative ATP-dependent RNA helicase TDRD12|||Tudor 1|||Tudor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000311969|||http://purl.uniprot.org/annotation/VSP_029677|||http://purl.uniprot.org/annotation/VSP_029678 http://togogenome.org/gene/10090:Or4e1 ^@ http://purl.uniprot.org/uniprot/Q9R0K4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Klf12 ^@ http://purl.uniprot.org/uniprot/O35738 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ 9aaTAD; inactive|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 12|||N6-methylated lysine; by EHMT2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000047183 http://togogenome.org/gene/10090:Fuom ^@ http://purl.uniprot.org/uniprot/Q8R2K1 ^@ Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand ^@ Active Site|||Binding Site|||Chain|||Helix|||Splice Variant|||Strand ^@ Fucose mutarotase|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000286554|||http://purl.uniprot.org/annotation/VSP_025082|||http://purl.uniprot.org/annotation/VSP_025083|||http://purl.uniprot.org/annotation/VSP_025084|||http://purl.uniprot.org/annotation/VSP_025085 http://togogenome.org/gene/10090:Reep5 ^@ http://purl.uniprot.org/uniprot/G3X8R0|||http://purl.uniprot.org/uniprot/Q9CQG4 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Trpc7 ^@ http://purl.uniprot.org/uniprot/E9PVJ9|||http://purl.uniprot.org/uniprot/Q0VFY2|||http://purl.uniprot.org/uniprot/Q3UXW9|||http://purl.uniprot.org/uniprot/Q9WVC5 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphothreonine; by PKG/PRKG1|||Short transient receptor potential channel 7|||Transient receptor ion channel ^@ http://purl.uniprot.org/annotation/PRO_0000215325 http://togogenome.org/gene/10090:Serpinb7 ^@ http://purl.uniprot.org/uniprot/Q6P3F8|||http://purl.uniprot.org/uniprot/Q9D695 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Domain Extent|||Modified Residue|||Site ^@ Phosphoserine|||Reactive bond|||Serpin|||Serpin B7 ^@ http://purl.uniprot.org/annotation/PRO_0000094109 http://togogenome.org/gene/10090:Crhbp ^@ http://purl.uniprot.org/uniprot/Q3UY07|||http://purl.uniprot.org/uniprot/Q60571 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Corticotropin-releasing factor-binding protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000020995|||http://purl.uniprot.org/annotation/PRO_5014309200 http://togogenome.org/gene/10090:Slc9a9 ^@ http://purl.uniprot.org/uniprot/Q8BZ00 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Does not rescue the hyperacidication of axonal vesicles as well as Ca2(+) influx in response to single action potential in neurons from Slc9a9-deficient mice.|||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|||Lumenal|||Polar residues|||Sodium/hydrogen exchanger 9 ^@ http://purl.uniprot.org/annotation/PRO_0000052368 http://togogenome.org/gene/10090:Mbd5 ^@ http://purl.uniprot.org/uniprot/B1AYB5|||http://purl.uniprot.org/uniprot/B1AYB6|||http://purl.uniprot.org/uniprot/Q69ZJ2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||MBD|||Methyl-CpG-binding domain protein 5|||PWWP|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000406940 http://togogenome.org/gene/10090:Rtl8b ^@ http://purl.uniprot.org/uniprot/Q9D1F0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ DUF4939 ^@ http://togogenome.org/gene/10090:Sit1 ^@ http://purl.uniprot.org/uniprot/Q8C503 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||Interaction with CSK|||Interaction with GRB2|||Interaction with PTPN11|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Signaling threshold-regulating transmembrane adapter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000083341 http://togogenome.org/gene/10090:Ddah1 ^@ http://purl.uniprot.org/uniprot/D3YU15|||http://purl.uniprot.org/uniprot/Q3UF01|||http://purl.uniprot.org/uniprot/Q9CWS0 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Non-terminal Residue ^@ N(G),N(G)-dimethylarginine dimethylaminohydrolase 1|||N-acetylalanine|||Nucleophile|||Phosphoserine|||Proton donor|||Removed|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000171119 http://togogenome.org/gene/10090:Slc6a21 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSD2|||http://purl.uniprot.org/uniprot/Q3V0K1 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Hdhd3 ^@ http://purl.uniprot.org/uniprot/Q9CYW4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Haloacid dehalogenase-like hydrolase domain-containing protein 3|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000287314 http://togogenome.org/gene/10090:Gm4064 ^@ http://purl.uniprot.org/uniprot/A0A087WR82 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||RRM ^@ http://togogenome.org/gene/10090:D16Ertd472e ^@ http://purl.uniprot.org/uniprot/Q8VE27|||http://purl.uniprot.org/uniprot/Q9D7G4 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Disordered|||Protein EURL homolog ^@ http://purl.uniprot.org/annotation/PRO_0000087078 http://togogenome.org/gene/10090:Utp14a ^@ http://purl.uniprot.org/uniprot/Q640M1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||U3 small nucleolar RNA-associated protein 14 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000065734|||http://purl.uniprot.org/annotation/VSP_014477|||http://purl.uniprot.org/annotation/VSP_014478 http://togogenome.org/gene/10090:Pde2a ^@ http://purl.uniprot.org/uniprot/A0A1B0GRJ9|||http://purl.uniprot.org/uniprot/Q3TYK5|||http://purl.uniprot.org/uniprot/Q3TYU3|||http://purl.uniprot.org/uniprot/Q5PR72|||http://purl.uniprot.org/uniprot/Q922S4 ^@ Active Site|||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|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Disordered|||GAF 1|||GAF 2|||In isoform PDE2A1 and isoform PDE2A2.|||In isoform PDE2A1.|||In isoform PDE2A2.|||N-myristoyl glycine|||PDEase|||Phosphoserine|||Proton donor|||Removed|||S-palmitoyl cysteine|||cGMP-dependent 3',5'-cyclic phosphodiesterase ^@ http://purl.uniprot.org/annotation/PRO_0000198797|||http://purl.uniprot.org/annotation/VSP_059395|||http://purl.uniprot.org/annotation/VSP_059396|||http://purl.uniprot.org/annotation/VSP_059397 http://togogenome.org/gene/10090:Dyrk1a ^@ http://purl.uniprot.org/uniprot/A1L341|||http://purl.uniprot.org/uniprot/A9C475|||http://purl.uniprot.org/uniprot/Q61214|||http://purl.uniprot.org/uniprot/Q8C774 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic residues|||Bipartite nuclear localization signal|||Disordered|||Dual specificity tyrosine-phosphorylation-regulated kinase 1A|||Histidine-rich domain (HRD)|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085932 http://togogenome.org/gene/10090:Irgm2 ^@ http://purl.uniprot.org/uniprot/A0A140LIF8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict ^@ Abolished GTPase activity, preventing ability to mediate host resistance to acute infection by T.gondii.|||Abolished localization to parasitophorous vacuole membranes or Golgi apparatus.|||Abolished polyubiquitination; when associated with A-269, A-314, A-316 and A-379.|||Abolished polyubiquitination; when associated with A-92, A-269, A-314 and A-316.|||Abolished polyubiquitination; when associated with A-92, A-269, A-314 and A-379.|||Abolished polyubiquitination; when associated with A-92, A-269, A-316 and A-379.|||Abolished polyubiquitination; when associated with A-92, A-314, A-316 and A-379.|||Does not affect localization to parasitophorous vacuole membranes or Golgi apparatus.|||IRG-type G|||Immunity-related GTPase family M protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000457975 http://togogenome.org/gene/10090:Or13l2 ^@ http://purl.uniprot.org/uniprot/Q8VET1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wdcp ^@ http://purl.uniprot.org/uniprot/A0A1Y7VJP4|||http://purl.uniprot.org/uniprot/Q6NV72 ^@ 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.|||Interaction with HCK|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD repeat and coiled-coil-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000299502|||http://purl.uniprot.org/annotation/VSP_027716 http://togogenome.org/gene/10090:Nptn ^@ http://purl.uniprot.org/uniprot/P97300 ^@ 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.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Narpin; mediates binding with FGFR1 and has antidepressant-like activity|||Neuroplastin ^@ http://purl.uniprot.org/annotation/PRO_0000394471|||http://purl.uniprot.org/annotation/VSP_039254|||http://purl.uniprot.org/annotation/VSP_039255|||http://purl.uniprot.org/annotation/VSP_039256|||http://purl.uniprot.org/annotation/VSP_039257 http://togogenome.org/gene/10090:Ncbp2 ^@ http://purl.uniprot.org/uniprot/Q9CQ49 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||N-acetylserine|||Nuclear cap-binding protein subunit 2|||Omega-N-methylarginine|||Phosphoserine|||RRM|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000081500 http://togogenome.org/gene/10090:Cplx4 ^@ http://purl.uniprot.org/uniprot/Q80WM3 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict ^@ Chain|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict ^@ Complexin-4|||Cysteine methyl ester|||Disordered|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000240237|||http://purl.uniprot.org/annotation/PRO_0000240238 http://togogenome.org/gene/10090:Hif1a ^@ http://purl.uniprot.org/uniprot/A0A0R4J1E9|||http://purl.uniprot.org/uniprot/Q3UCW2|||http://purl.uniprot.org/uniprot/Q61221 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ (3S)-3-hydroxyasparagine|||4-hydroxyproline|||BHLH|||C-terminal VHL recognition site|||CTAD|||DNA-binding|||Decreases heterodimer formation with ARNT. Impairs heterodimer formation with ARNT; when associated with A-170.|||Decreases heterodimer formation with ARNT. Impairs heterodimer formation with ARNT; when associated with D-191.|||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|||Hypoxia-inducible factor 1-alpha|||ID|||In isoform 2.|||Interaction with TSGA10|||N-terminal VHL recognition site|||N6-acetyllysine|||N6-acetyllysine; alternate|||NTAD|||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|||Required for heterodimer formation with ARNT|||S-nitrosocysteine|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127221|||http://purl.uniprot.org/annotation/VSP_007739 http://togogenome.org/gene/10090:Eif4g2 ^@ http://purl.uniprot.org/uniprot/A0JNY7|||http://purl.uniprot.org/uniprot/Q62448 ^@ 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|||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_0000213326|||http://purl.uniprot.org/annotation/VSP_021640 http://togogenome.org/gene/10090:Phf23 ^@ http://purl.uniprot.org/uniprot/Q8BSN5 ^@ 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 ^@ Acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||PHD finger protein 23|||PHD-type|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000302831|||http://purl.uniprot.org/annotation/VSP_027964|||http://purl.uniprot.org/annotation/VSP_027965 http://togogenome.org/gene/10090:Or2y15 ^@ http://purl.uniprot.org/uniprot/Q8VFA9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Unc5a ^@ http://purl.uniprot.org/uniprot/Q8K1S4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 UNC5A|||TSP type-1 1|||TSP type-1 2|||ZU5 ^@ http://purl.uniprot.org/annotation/PRO_0000036069|||http://purl.uniprot.org/annotation/VSP_011696|||http://purl.uniprot.org/annotation/VSP_011697 http://togogenome.org/gene/10090:1700013G24Rik ^@ http://purl.uniprot.org/uniprot/Q9DAC6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ston1 ^@ http://purl.uniprot.org/uniprot/Q8CDJ8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||MHD|||Polar residues|||SHD|||Stonin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000185737 http://togogenome.org/gene/10090:Zscan29 ^@ http://purl.uniprot.org/uniprot/A2ARU5|||http://purl.uniprot.org/uniprot/Q8BGW7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||C2H2-type|||Disordered|||Myb/SANT-like DNA-binding|||SCAN box ^@ http://togogenome.org/gene/10090:Irf2 ^@ http://purl.uniprot.org/uniprot/P23906|||http://purl.uniprot.org/uniprot/Q3U2Z2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ 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|||IRF tryptophan pentad repeat|||Interferon regulatory factor 2|||N6-acetyllysine|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000154550 http://togogenome.org/gene/10090:Lrrc75b ^@ http://purl.uniprot.org/uniprot/Q7TPD7 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ Disordered|||LRR 1|||LRR 2|||Leucine-rich repeat-containing protein 75B ^@ http://purl.uniprot.org/annotation/PRO_0000254047 http://togogenome.org/gene/10090:Azi2 ^@ http://purl.uniprot.org/uniprot/Q9QYP6 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ 5-azacytidine-induced protein 2|||Abolishes interaction with TBK1 and IKBKE.|||Abolishes interaction with TBK1 but not with IKBKE.|||Disordered|||Homodimerization|||In isoform 2.|||In isoform 3.|||Interaction with TBK1 and IKBKE|||No effect on interaction with TBK1 and IKBKE.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000280604|||http://purl.uniprot.org/annotation/VSP_023822|||http://purl.uniprot.org/annotation/VSP_023823|||http://purl.uniprot.org/annotation/VSP_023824 http://togogenome.org/gene/10090:Cdh16 ^@ http://purl.uniprot.org/uniprot/O88338|||http://purl.uniprot.org/uniprot/Q3TPA4|||http://purl.uniprot.org/uniprot/Q546A8|||http://purl.uniprot.org/uniprot/Q8C730 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin-16|||Cytoplasmic|||Ectodomain G|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000003810|||http://purl.uniprot.org/annotation/PRO_5014309637|||http://purl.uniprot.org/annotation/PRO_5015099073 http://togogenome.org/gene/10090:Morc3 ^@ http://purl.uniprot.org/uniprot/F7BJB9 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ CW-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|||MORC family CW-type zinc finger protein 3|||Nuclear matrix binding|||Phosphoserine|||Polar residues|||RNA binding ^@ http://purl.uniprot.org/annotation/PRO_0000435141 http://togogenome.org/gene/10090:Actl7b ^@ http://purl.uniprot.org/uniprot/Q9QY83 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Actin-like protein 7B|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000089141 http://togogenome.org/gene/10090:Gmfg ^@ http://purl.uniprot.org/uniprot/A7VJA4|||http://purl.uniprot.org/uniprot/D3YY16|||http://purl.uniprot.org/uniprot/Q9ERL7 ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn ^@ ADF-H|||Glia maturation factor gamma|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000214948 http://togogenome.org/gene/10090:Zc3h12b ^@ http://purl.uniprot.org/uniprot/G3X9I7|||http://purl.uniprot.org/uniprot/Q3UYJ7 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Basic and acidic residues|||C3H1-type|||Disordered|||Polar residues|||RNase NYN|||Rege-1 UBA-like ^@ http://togogenome.org/gene/10090:Clybl ^@ http://purl.uniprot.org/uniprot/Q8R4N0 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Citramalyl-CoA lyase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000286390 http://togogenome.org/gene/10090:Lekr1 ^@ http://purl.uniprot.org/uniprot/A0A571BF98|||http://purl.uniprot.org/uniprot/B2RVN1|||http://purl.uniprot.org/uniprot/Q3UVB4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ DH|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rbm12b2 ^@ http://purl.uniprot.org/uniprot/Q66JV4 ^@ 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|||In isoform 2.|||Phosphoserine|||RNA-binding protein 12B-B|||RRM 1|||RRM 2|||RRM 3|||RRM 4 ^@ http://purl.uniprot.org/annotation/PRO_0000273369|||http://purl.uniprot.org/annotation/VSP_022525 http://togogenome.org/gene/10090:Zfp277 ^@ http://purl.uniprot.org/uniprot/E9Q6D6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 2|||In isoform 2.|||Zinc finger protein 277 ^@ http://purl.uniprot.org/annotation/PRO_0000455248|||http://purl.uniprot.org/annotation/VSP_061466 http://togogenome.org/gene/10090:Msra ^@ http://purl.uniprot.org/uniprot/A0A1B0GT40|||http://purl.uniprot.org/uniprot/Q9D6Y7 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Cysteine sulfenic acid (-SOH) intermediate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrial peptide methionine sulfoxide reductase|||Mitochondrion|||N-myristoyl glycine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Peptide methionine sulphoxide reductase MsrA|||Redox-active; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000138627|||http://purl.uniprot.org/annotation/VSP_041408|||http://purl.uniprot.org/annotation/VSP_041409|||http://purl.uniprot.org/annotation/VSP_042133 http://togogenome.org/gene/10090:Vmn1r208 ^@ http://purl.uniprot.org/uniprot/Q8R275 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fbxw16 ^@ http://purl.uniprot.org/uniprot/Q497Z0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Igfbp2 ^@ http://purl.uniprot.org/uniprot/D3YU40|||http://purl.uniprot.org/uniprot/P47877 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Cell attachment site|||Disordered|||IGFBP N-terminal|||Insulin-like growth factor-binding protein 2|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000014371 http://togogenome.org/gene/10090:Magea9 ^@ http://purl.uniprot.org/uniprot/Q8BQJ2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Tsku ^@ http://purl.uniprot.org/uniprot/Q08EE6|||http://purl.uniprot.org/uniprot/Q8CBR6 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||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_0000240408|||http://purl.uniprot.org/annotation/PRO_5014306705 http://togogenome.org/gene/10090:Sdsl ^@ http://purl.uniprot.org/uniprot/Q8R238 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ N-acetylmethionine|||N6-(pyridoxal phosphate)lysine|||Serine dehydratase-like ^@ http://purl.uniprot.org/annotation/PRO_0000264625 http://togogenome.org/gene/10090:Il15 ^@ http://purl.uniprot.org/uniprot/P48346 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Secondary Structure|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Signal Peptide|||Strand ^@ Interleukin-15|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015399|||http://purl.uniprot.org/annotation/PRO_0000015400 http://togogenome.org/gene/10090:Fabp12 ^@ http://purl.uniprot.org/uniprot/Q9DAK4 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Fatty acid-binding protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000342882 http://togogenome.org/gene/10090:Or1aa2 ^@ http://purl.uniprot.org/uniprot/Q8VEU7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pop4 ^@ http://purl.uniprot.org/uniprot/Q9CR08 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Phosphoserine|||Ribonuclease P protein subunit p29 ^@ http://purl.uniprot.org/annotation/PRO_0000128419 http://togogenome.org/gene/10090:Fgd6 ^@ http://purl.uniprot.org/uniprot/Q69ZL1 ^@ 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|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ 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_0000080953|||http://purl.uniprot.org/annotation/VSP_013093 http://togogenome.org/gene/10090:Pip5k1a ^@ http://purl.uniprot.org/uniprot/P70182 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2 and isoform 3.|||In isoform 2.|||PIPK|||Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000185457|||http://purl.uniprot.org/annotation/VSP_016009|||http://purl.uniprot.org/annotation/VSP_053437 http://togogenome.org/gene/10090:Haus4 ^@ http://purl.uniprot.org/uniprot/Q8BFT2 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ HAUS augmin-like complex subunit 4 ^@ http://purl.uniprot.org/annotation/PRO_0000089902 http://togogenome.org/gene/10090:Lgals12 ^@ http://purl.uniprot.org/uniprot/Q91VD1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ Galectin 1|||Galectin 2|||Galectin-12|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000076950|||http://purl.uniprot.org/annotation/VSP_010321 http://togogenome.org/gene/10090:Or5an6 ^@ http://purl.uniprot.org/uniprot/Q8VFV4 ^@ 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|||Helical; Name=8|||Olfactory receptor 5AN6 ^@ http://purl.uniprot.org/annotation/PRO_0000430080 http://togogenome.org/gene/10090:Glyctk ^@ http://purl.uniprot.org/uniprot/A0A0R4J1H2|||http://purl.uniprot.org/uniprot/Q8QZY2 ^@ 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 ^@ Glycerate kinase|||In isoform 2.|||MOFRL|||MOFRL-associated|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000287194|||http://purl.uniprot.org/annotation/VSP_025366 http://togogenome.org/gene/10090:Or4d2 ^@ http://purl.uniprot.org/uniprot/Q5SW49 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dazap1 ^@ http://purl.uniprot.org/uniprot/Q3UGB5|||http://purl.uniprot.org/uniprot/Q9JII5 ^@ 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|||DAZ-associated protein 1|||Disordered|||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_0000081566|||http://purl.uniprot.org/annotation/VSP_009443 http://togogenome.org/gene/10090:Ankrd42 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1P5|||http://purl.uniprot.org/uniprot/Q3V096 ^@ 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|||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 42|||Disordered|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000244372|||http://purl.uniprot.org/annotation/VSP_019562|||http://purl.uniprot.org/annotation/VSP_019563|||http://purl.uniprot.org/annotation/VSP_019564|||http://purl.uniprot.org/annotation/VSP_019565 http://togogenome.org/gene/10090:Sntg2 ^@ http://purl.uniprot.org/uniprot/Q8BZG8|||http://purl.uniprot.org/uniprot/Q925E0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Gamma-2-syntrophin|||PDZ|||PH ^@ http://purl.uniprot.org/annotation/PRO_0000184016 http://togogenome.org/gene/10090:V1ra8 ^@ http://purl.uniprot.org/uniprot/Q9EQ48 ^@ 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|||Vomeronasal type-1 receptor A8 ^@ http://purl.uniprot.org/annotation/PRO_0000239964 http://togogenome.org/gene/10090:Pm20d1 ^@ http://purl.uniprot.org/uniprot/Q8C165 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Loss of N-fatty-acyl-amino acid synthase/hydrolase activity.|||N-fatty-acyl-amino acid synthase/hydrolase PM20D1|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000321929 http://togogenome.org/gene/10090:Pxmp4 ^@ http://purl.uniprot.org/uniprot/Q9JJW0 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Peroxisomal membrane protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000218933 http://togogenome.org/gene/10090:Sfrp2 ^@ http://purl.uniprot.org/uniprot/P97299|||http://purl.uniprot.org/uniprot/Q3UI35 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ FZ|||NTR|||Secreted frizzled-related protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000032543|||http://purl.uniprot.org/annotation/PRO_5014309230 http://togogenome.org/gene/10090:Vmn1r248 ^@ http://purl.uniprot.org/uniprot/D3YTX5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trarg1 ^@ http://purl.uniprot.org/uniprot/Q8C838 ^@ Chain|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Trafficking regulator of GLUT4 1 ^@ http://purl.uniprot.org/annotation/PRO_0000263640 http://togogenome.org/gene/10090:Ppp1r3a ^@ http://purl.uniprot.org/uniprot/Q99MR9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ CBM21|||Disordered|||Helical|||PP1-binding motif|||Phosphoserine|||Phosphoserine; by GSK3|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Protein phosphatase 1 regulatory subunit 3A ^@ http://purl.uniprot.org/annotation/PRO_0000071501 http://togogenome.org/gene/10090:Or52r1 ^@ http://purl.uniprot.org/uniprot/Q8VGZ2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc1a7 ^@ http://purl.uniprot.org/uniprot/Q8JZR4|||http://purl.uniprot.org/uniprot/Z4YKJ7 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Excitatory amino acid transporter 5|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000284451 http://togogenome.org/gene/10090:Elp5 ^@ http://purl.uniprot.org/uniprot/Q99L85 ^@ 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|||Elongator complex protein 5|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000280818 http://togogenome.org/gene/10090:Fam162a ^@ http://purl.uniprot.org/uniprot/Q9D6U8 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Helical|||Protein FAM162A|||Required for proapoptotic activity ^@ http://purl.uniprot.org/annotation/PRO_0000254636 http://togogenome.org/gene/10090:Brdt ^@ http://purl.uniprot.org/uniprot/Q8BNZ8|||http://purl.uniprot.org/uniprot/Q91Y44 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Abolishes interaction with histone H4 acetylated N-terminus; when associated with 293-AA-294.|||Abolishes interaction with histone H4 acetylated N-terminus; when associated with 50-AA-51.|||Abolishes interaction with histone H4 acetylated N-terminus; when associated with A-298.|||Abolishes interaction with histone H4 acetylated N-terminus; when associated with A-55.|||Basic and acidic residues|||Bromo 1|||Bromo 2|||Bromodomain protein 4 C-terminal|||Bromodomain testis-specific protein|||Disordered|||Histone H4K5ac binding|||In isoform 2.|||NET|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000239227|||http://purl.uniprot.org/annotation/VSP_019119|||http://purl.uniprot.org/annotation/VSP_019120 http://togogenome.org/gene/10090:Mup2 ^@ http://purl.uniprot.org/uniprot/A2AKN9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5015086024 http://togogenome.org/gene/10090:Gtdc1 ^@ http://purl.uniprot.org/uniprot/Q8BW56 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Region|||Splice Variant ^@ Disordered|||Glycosyltransferase-like domain-containing protein 1|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000311089|||http://purl.uniprot.org/annotation/VSP_029380|||http://purl.uniprot.org/annotation/VSP_029381|||http://purl.uniprot.org/annotation/VSP_029382 http://togogenome.org/gene/10090:Sirt6 ^@ http://purl.uniprot.org/uniprot/P59941|||http://purl.uniprot.org/uniprot/Q3UKP1 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolished NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase activities.|||Abolished NAD-dependent protein deacetylase, defatty-acylase and mono-ADP-ribosyltransferase activities.|||Deacetylase sirtuin-type|||Disordered|||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.|||Embryonic lethality in knockin mice; mice fail to form embryonic bodies and retain pluripotent gene expression, leading to impaired embryonic stem cell differentiation. Defects are caused by a failure to deacetylate histone H3 at 'Lys-9' (H3K9).|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Increased histone deacetylase activity, ability to promote double-strand break (DSB) repair, leading to increased life span; when associated with H-249 and 260-D--Q-264.|||Increased histone deacetylase activity, ability to promote double-strand break (DSB) repair, leading to increased life span; when associated with K-235 and 260-D--Q-264.|||Increased histone deacetylase activity, ability to promote double-strand break (DSB) repair, leading to increased life span; when associated with K-235 and H-249.|||N-acetylserine|||N6-acetyllysine|||NAD-dependent protein deacylase sirtuin-6|||Phosphoserine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000110270 http://togogenome.org/gene/10090:Kcna7 ^@ http://purl.uniprot.org/uniprot/Q17ST2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Lipid Binding|||Motif|||Sequence Conflict|||Splice 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|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Potassium voltage-gated channel subfamily A member 7|||S-palmitoyl cysteine|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000308274|||http://purl.uniprot.org/annotation/VSP_028953 http://togogenome.org/gene/10090:Hook3 ^@ http://purl.uniprot.org/uniprot/Q8BUK6 ^@ 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 ^@ Calponin-homology (CH)|||Disordered|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein Hook homolog 3|||Required for association with Golgi|||Sufficient for interaction with IIGP1|||Sufficient for interaction with microtubules ^@ http://purl.uniprot.org/annotation/PRO_0000219198 http://togogenome.org/gene/10090:Nat8f3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J157|||http://purl.uniprot.org/uniprot/Q9JIY8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ Helical|||N-acetyltransferase|||N-acetyltransferase family 8 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000284690 http://togogenome.org/gene/10090:Opa1 ^@ http://purl.uniprot.org/uniprot/H7BX01|||http://purl.uniprot.org/uniprot/P58281 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant|||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 isoform 2.|||LQQQIQ motif|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000007398|||http://purl.uniprot.org/annotation/PRO_0000253480|||http://purl.uniprot.org/annotation/VSP_021037 http://togogenome.org/gene/10090:Zdhhc3 ^@ http://purl.uniprot.org/uniprot/Q8R173 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Decreased ZDHHC3 palmitoylation. Changed protein structure. Decreased protein-cysteine S-palmitoyltransferase activity.|||Decreased phosphorylation by FGFR1.|||Decreased phosphorylation by SRC and increased autopalmitoylation; when associated with F-295.|||Decreased phosphorylation by SRC and increased autopalmitoylation; when associated with F-297.|||Helical|||Increased protein-cysteine S-stearoyltransferase activity.|||Loss of function in calcium transport.|||Loss of protein-cysteine S-acyltransferase activity. Loss of ZDHHC3 palmitoylation.|||Lumenal|||No effect on ZDHHC3 palmitoylation. Changed protein structure. Decreased protein-cysteine S-palmitoyltransferase activity.|||No effect on ZDHHC3 palmitoylation. No effect on protein-cysteine S-palmitoyltransferase activity.|||Palmitoyltransferase ZDHHC3|||Phosphotyrosine; by FGFR1|||S-palmitoyl cysteine|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212863 http://togogenome.org/gene/10090:Cfap52 ^@ http://purl.uniprot.org/uniprot/Q147Z1|||http://purl.uniprot.org/uniprot/Q5F201 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ Cilia- and flagella-associated protein 52|||In isoform 2.|||WD|||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_0000233155|||http://purl.uniprot.org/annotation/VSP_018069|||http://purl.uniprot.org/annotation/VSP_018070 http://togogenome.org/gene/10090:Ssh3 ^@ http://purl.uniprot.org/uniprot/Q8K330 ^@ 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|||In isoform 2.|||N-acetylalanine|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Protein phosphatase Slingshot homolog 3|||Removed|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094846|||http://purl.uniprot.org/annotation/VSP_016337 http://togogenome.org/gene/10090:Zrsr2 ^@ http://purl.uniprot.org/uniprot/B1B0E8|||http://purl.uniprot.org/uniprot/B1B0E9|||http://purl.uniprot.org/uniprot/Q8BG24 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||C3H1-type|||Disordered|||Polar residues|||RRM ^@ http://togogenome.org/gene/10090:Psmb8 ^@ http://purl.uniprot.org/uniprot/P28063 ^@ Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn ^@ Cleavage; by autolysis|||In allele LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7.|||In allele LMP7q.|||Nucleophile|||Proteasome subunit beta type-8|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000026599|||http://purl.uniprot.org/annotation/PRO_0000026600 http://togogenome.org/gene/10090:Cfdp1 ^@ http://purl.uniprot.org/uniprot/O88271 ^@ 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 ^@ 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|||N6-methyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000212495 http://togogenome.org/gene/10090:Cerk ^@ http://purl.uniprot.org/uniprot/Q8K4Q7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Ceramide kinase|||DAGKc|||Essential for enzyme activity|||Phosphoserine|||Proton donor/acceptor|||Required for binding to sulfatide and phosphoinositides ^@ http://purl.uniprot.org/annotation/PRO_0000181355 http://togogenome.org/gene/10090:Ahsa2 ^@ http://purl.uniprot.org/uniprot/Q8N9S3 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ Activator of 90 kDa heat shock protein ATPase homolog 2|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000315606|||http://purl.uniprot.org/annotation/VSP_030572|||http://purl.uniprot.org/annotation/VSP_030573 http://togogenome.org/gene/10090:Jmjd6 ^@ http://purl.uniprot.org/uniprot/Q9ERI5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6|||Disordered|||In isoform 2.|||JmjC|||Loss of lysyl-hydroxylase activity.|||Nuclear localization signal 1|||Nuclear localization signal 2|||Nuclear localization signal 3|||Nuclear localization signal 4|||Nuclear localization signal 5|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000129370|||http://purl.uniprot.org/annotation/VSP_014024|||http://purl.uniprot.org/annotation/VSP_014025 http://togogenome.org/gene/10090:Prkd3 ^@ http://purl.uniprot.org/uniprot/D3Z6I0|||http://purl.uniprot.org/uniprot/Q5FWX6|||http://purl.uniprot.org/uniprot/Q8K1Y2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||PH|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphoserine; by PKC|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase D3 ^@ http://purl.uniprot.org/annotation/PRO_0000055718 http://togogenome.org/gene/10090:Or8b57 ^@ http://purl.uniprot.org/uniprot/Q8VG90 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cby1 ^@ http://purl.uniprot.org/uniprot/Q9D1C2 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Region ^@ Disordered|||Minimal region for the interaction with PKD2|||Phosphoserine|||Protein chibby homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000058355 http://togogenome.org/gene/10090:Tmem161b ^@ http://purl.uniprot.org/uniprot/A0A286YCA7|||http://purl.uniprot.org/uniprot/Q8C2L6 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 161B ^@ http://purl.uniprot.org/annotation/PRO_0000288090 http://togogenome.org/gene/10090:Luc7l3 ^@ http://purl.uniprot.org/uniprot/Q5SUF2 ^@ 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 SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Luc7-like protein 3|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000233411|||http://purl.uniprot.org/annotation/VSP_018138|||http://purl.uniprot.org/annotation/VSP_018139 http://togogenome.org/gene/10090:Ranbp3l ^@ http://purl.uniprot.org/uniprot/Q6PDH4 ^@ 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.|||Polar residues|||Ran-binding protein 3-like|||RanBD1 ^@ http://purl.uniprot.org/annotation/PRO_0000312750|||http://purl.uniprot.org/annotation/VSP_029895|||http://purl.uniprot.org/annotation/VSP_029896 http://togogenome.org/gene/10090:Rnase12 ^@ http://purl.uniprot.org/uniprot/Q5GAM8|||http://purl.uniprot.org/uniprot/W0UUY1 ^@ 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_0000308703|||http://purl.uniprot.org/annotation/PRO_5009977275 http://togogenome.org/gene/10090:Pik3cb ^@ http://purl.uniprot.org/uniprot/Q8BTI9 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ Activation loop|||C2 PI3K-type|||Catalytic loop|||G-loop|||Nuclear localization signal (NLS)|||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_0000088788 http://togogenome.org/gene/10090:Cxcl15 ^@ http://purl.uniprot.org/uniprot/Q9WVL7 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Signal Peptide ^@ C-X-C motif chemokine 15|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000005117 http://togogenome.org/gene/10090:Gm10486 ^@ http://purl.uniprot.org/uniprot/Q62478 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Cnmd ^@ http://purl.uniprot.org/uniprot/G5E8Z6|||http://purl.uniprot.org/uniprot/Q9Z1F6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Transmembrane ^@ BRICHOS|||Chondromodulin-1|||Chondrosurfactant protein|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000005349|||http://purl.uniprot.org/annotation/PRO_0000005350|||http://purl.uniprot.org/annotation/PRO_0000005351 http://togogenome.org/gene/10090:Tdgf1 ^@ http://purl.uniprot.org/uniprot/P51865|||http://purl.uniprot.org/uniprot/Q3UZP8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand ^@ EGF-like|||GPI-anchor amidated aspartate|||Growth factor|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Teratocarcinoma-derived growth factor|||Unable to bind Cripto receptor. ^@ http://purl.uniprot.org/annotation/PRO_0000007504|||http://purl.uniprot.org/annotation/PRO_0000395411|||http://purl.uniprot.org/annotation/PRO_5004230415 http://togogenome.org/gene/10090:Snrpb2 ^@ http://purl.uniprot.org/uniprot/Q9CQI7 ^@ 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 ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6-acetyllysine; alternate|||Phosphotyrosine|||Polar residues|||RRM 1|||RRM 2|||U2 small nuclear ribonucleoprotein B""" /id="PRO_0000081893 ^@ http://togogenome.org/gene/10090:Ptdss2 ^@ http://purl.uniprot.org/uniprot/Q9Z1X2 ^@ 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 ^@ Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphatidylserine synthase 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000056833|||http://purl.uniprot.org/annotation/VSP_010637|||http://purl.uniprot.org/annotation/VSP_010638 http://togogenome.org/gene/10090:Mrtfb ^@ http://purl.uniprot.org/uniprot/A0A8D4USI8|||http://purl.uniprot.org/uniprot/G3X8R8|||http://purl.uniprot.org/uniprot/P59759|||http://purl.uniprot.org/uniprot/Q5DTZ3|||http://purl.uniprot.org/uniprot/Q8R2L3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat ^@ Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Myocardin-related transcription factor B|||Phosphoserine|||Polar residues|||RPEL|||RPEL 1|||RPEL 2|||RPEL 3|||Required for interaction with itself and with MRTFA|||SAP ^@ http://purl.uniprot.org/annotation/PRO_0000126629 http://togogenome.org/gene/10090:Ube2i ^@ http://purl.uniprot.org/uniprot/P63280 ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Site|||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)|||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|||Interaction with RANBP2|||Interaction with SUMO1|||N-acetylserine|||N6-acetyllysine|||Phosphoserine; by CDK1|||Removed|||SUMO-conjugating enzyme UBC9|||Substrate binding|||UBC core ^@ http://purl.uniprot.org/annotation/PRO_0000082456 http://togogenome.org/gene/10090:Aoc3 ^@ http://purl.uniprot.org/uniprot/O70423 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 2',4',5'-topaquinone|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||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_0000064103|||http://purl.uniprot.org/annotation/VSP_016604 http://togogenome.org/gene/10090:Pcare ^@ http://purl.uniprot.org/uniprot/Q6PAC4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||N-myristoyl glycine|||Photoreceptor cilium actin regulator|||Polar residues|||Pro residues|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000329079 http://togogenome.org/gene/10090:Mettl1 ^@ http://purl.uniprot.org/uniprot/Q9Z120 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Alpha6 helix|||AlphaC helix|||Disordered|||Phosphoserine|||tRNA (guanine-N(7)-)-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000171432 http://togogenome.org/gene/10090:Or10d5 ^@ http://purl.uniprot.org/uniprot/Q8VG91 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Isoc1 ^@ http://purl.uniprot.org/uniprot/Q91V64 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Isochorismatase domain-containing protein 1|||N6-succinyllysine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000268665 http://togogenome.org/gene/10090:Dis3l ^@ http://purl.uniprot.org/uniprot/Q8C0S1 ^@ 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|||DIS3-like exonuclease 1|||Disordered|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000314811|||http://purl.uniprot.org/annotation/VSP_030370 http://togogenome.org/gene/10090:Zfp72 ^@ http://purl.uniprot.org/uniprot/Q0VFY0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Fkbp5 ^@ http://purl.uniprot.org/uniprot/Q4FJN2|||http://purl.uniprot.org/uniprot/Q64378 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Disordered|||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_0000075325 http://togogenome.org/gene/10090:Synj1 ^@ http://purl.uniprot.org/uniprot/D3Z656|||http://purl.uniprot.org/uniprot/E9Q7S0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Pro residues|||RRM|||SAC ^@ http://togogenome.org/gene/10090:Armc8 ^@ http://purl.uniprot.org/uniprot/G3X920|||http://purl.uniprot.org/uniprot/Q9DBR3 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Splice Variant ^@ 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 3.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000284410|||http://purl.uniprot.org/annotation/VSP_024515|||http://purl.uniprot.org/annotation/VSP_024516|||http://purl.uniprot.org/annotation/VSP_024517 http://togogenome.org/gene/10090:Serpinb9e ^@ http://purl.uniprot.org/uniprot/O08806 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Nupl2 ^@ http://purl.uniprot.org/uniprot/E9QL43|||http://purl.uniprot.org/uniprot/Q8CIC2 ^@ 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 ^@ C3H1-type|||Disordered|||FG 1|||FG 10|||FG 11|||FG 2|||FG 3|||FG 4|||FG 5|||FG 6|||FG 7|||FG 8|||FG 9|||In isoform 2.|||Interaction with GLE1|||Nucleoporin NUP42|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204896|||http://purl.uniprot.org/annotation/VSP_016483|||http://purl.uniprot.org/annotation/VSP_016484 http://togogenome.org/gene/10090:Ipo7 ^@ http://purl.uniprot.org/uniprot/Q9EPL8 ^@ 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 ^@ Acidic residues|||Disordered|||Importin N-terminal|||Importin-7|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000120751 http://togogenome.org/gene/10090:Spock1 ^@ http://purl.uniprot.org/uniprot/A0A087WPP6|||http://purl.uniprot.org/uniprot/B2RXY1|||http://purl.uniprot.org/uniprot/Q6DIC9|||http://purl.uniprot.org/uniprot/Q8BKQ3|||http://purl.uniprot.org/uniprot/Q8BM07|||http://purl.uniprot.org/uniprot/Q8BM19 ^@ 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 ^@ Acidic residues|||Disordered|||Kazal-like|||Kazal-like domain-containing protein|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_5001831799|||http://purl.uniprot.org/annotation/PRO_5002781918|||http://purl.uniprot.org/annotation/PRO_5004305880|||http://purl.uniprot.org/annotation/PRO_5015098214|||http://purl.uniprot.org/annotation/PRO_5015099014|||http://purl.uniprot.org/annotation/PRO_5015099025 http://togogenome.org/gene/10090:Aph1a ^@ http://purl.uniprot.org/uniprot/Q6GTF1|||http://purl.uniprot.org/uniprot/Q8BVF7 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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|||In isoform 2.|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000221051|||http://purl.uniprot.org/annotation/VSP_008357|||http://purl.uniprot.org/annotation/VSP_008358 http://togogenome.org/gene/10090:Adgrf2 ^@ http://purl.uniprot.org/uniprot/A0A668KM90|||http://purl.uniprot.org/uniprot/E9Q4J9|||http://purl.uniprot.org/uniprot/Q3UQ38 ^@ 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 ^@ Adhesion G-protein coupled receptor F2|||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_0000433228|||http://purl.uniprot.org/annotation/PRO_5025445147 http://togogenome.org/gene/10090:Esp31 ^@ http://purl.uniprot.org/uniprot/A8R0W3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015086685 http://togogenome.org/gene/10090:Mmp13 ^@ http://purl.uniprot.org/uniprot/P33435|||http://purl.uniprot.org/uniprot/Q3U9V5 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Propeptide|||Region|||Repeat|||Signal Peptide|||Strand|||Turn ^@ Activation peptide|||Collagenase 3|||Cysteine switch|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Interaction with TIMP2|||Interaction with collagen|||N-linked (GlcNAc...) asparagine|||Peptidase metallopeptidase|||Phosphotyrosine; by PKDCC|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028790|||http://purl.uniprot.org/annotation/PRO_0000028791|||http://purl.uniprot.org/annotation/PRO_5014309186 http://togogenome.org/gene/10090:Timeless ^@ http://purl.uniprot.org/uniprot/Q3U574|||http://purl.uniprot.org/uniprot/Q9R1X4 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||DNA-binding domain|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 6.|||Interaction with PARP1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein timeless homolog|||Required for homodimerization and for interaction with CRY1 and CHEK1|||Required for nuclear localization|||Timeless C-terminal|||Timeless N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000072539|||http://purl.uniprot.org/annotation/VSP_051694|||http://purl.uniprot.org/annotation/VSP_051695|||http://purl.uniprot.org/annotation/VSP_051696|||http://purl.uniprot.org/annotation/VSP_051697 http://togogenome.org/gene/10090:Rab21 ^@ http://purl.uniprot.org/uniprot/P35282 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide ^@ Cysteine methyl ester|||Defects in GTP hydrolysis. Increase in integrin-binding.|||Defects in GTP-binding. Decrease in integrin-binding.|||Effector region|||N-acetylalanine|||Ras-related protein Rab-21|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121206|||http://purl.uniprot.org/annotation/PRO_0000370769 http://togogenome.org/gene/10090:Fgfr4 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZY3|||http://purl.uniprot.org/uniprot/Q03142 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Results in increased cell proliferation. Results in STAT3 phosphorylation and signaling activation. ^@ http://purl.uniprot.org/annotation/PRO_0000016788|||http://purl.uniprot.org/annotation/PRO_5015044275|||http://purl.uniprot.org/annotation/VSP_017545 http://togogenome.org/gene/10090:Srpk3 ^@ http://purl.uniprot.org/uniprot/Q0VAW8|||http://purl.uniprot.org/uniprot/Q9Z0G2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic residues|||Disordered|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||SRSF protein kinase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000086710 http://togogenome.org/gene/10090:Nwd1 ^@ http://purl.uniprot.org/uniprot/A6H603|||http://purl.uniprot.org/uniprot/E0CX99 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Anaphase-promoting complex subunit 4-like WD40|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||NACHT|||NACHT domain- and WD repeat-containing protein 1|||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_0000308255|||http://purl.uniprot.org/annotation/VSP_028942|||http://purl.uniprot.org/annotation/VSP_028943|||http://purl.uniprot.org/annotation/VSP_028944|||http://purl.uniprot.org/annotation/VSP_028945|||http://purl.uniprot.org/annotation/VSP_028946 http://togogenome.org/gene/10090:Rhoa ^@ http://purl.uniprot.org/uniprot/Q9QUI0 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Crosslink|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Strand|||Turn ^@ 5-glutamyl serotonin|||Cysteine methyl ester|||Effector region|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine; by PKG/PRKG1|||Removed in mature form|||S-geranylgeranyl cysteine|||Switch II region; involved in RAP1GDS1 isoform 3 binding|||Transforming protein RhoA ^@ http://purl.uniprot.org/annotation/PRO_0000030413|||http://purl.uniprot.org/annotation/PRO_0000030414 http://togogenome.org/gene/10090:Tedc2 ^@ http://purl.uniprot.org/uniprot/Q6GQV0 ^@ 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|||Tubulin epsilon and delta complex protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000286558|||http://purl.uniprot.org/annotation/VSP_025089 http://togogenome.org/gene/10090:Or5ac16 ^@ http://purl.uniprot.org/uniprot/Q7TS40 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gprin2 ^@ http://purl.uniprot.org/uniprot/A0A2I3BRN2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||G protein-regulated inducer of neurite outgrowth C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Timd4 ^@ http://purl.uniprot.org/uniprot/Q6U7R4 ^@ 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|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||In strain: C57BL/6.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||T-cell immunoglobulin and mucin domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000042104 http://togogenome.org/gene/10090:Vmn1r103 ^@ http://purl.uniprot.org/uniprot/K7N6X7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clec2f ^@ http://purl.uniprot.org/uniprot/F5CSM8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Timp2 ^@ http://purl.uniprot.org/uniprot/Q6PI17|||http://purl.uniprot.org/uniprot/Q8BSJ3 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Site ^@ Involved in metalloproteinase-binding|||NTR|||NTR domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5004307222|||http://purl.uniprot.org/annotation/PRO_5015098443 http://togogenome.org/gene/10090:Cct6a ^@ http://purl.uniprot.org/uniprot/P80317 ^@ 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)|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed|||T-complex protein 1 subunit zeta ^@ http://purl.uniprot.org/annotation/PRO_0000128356 http://togogenome.org/gene/10090:Sfxn4 ^@ http://purl.uniprot.org/uniprot/Q925N1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||N6-acetyllysine|||Sideroflexin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000177042 http://togogenome.org/gene/10090:Efnb1 ^@ http://purl.uniprot.org/uniprot/P52795|||http://purl.uniprot.org/uniprot/Q544L9 ^@ 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|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Ephrin RBD|||Ephrin RBD domain-containing protein|||Ephrin-B1|||Ephrin-B1 C-terminal fragment|||Ephrin-B1 intracellular domain|||Extracellular|||Helical|||Interaction with ZHX2|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||PDZ-binding|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000008388|||http://purl.uniprot.org/annotation/PRO_0000445793|||http://purl.uniprot.org/annotation/PRO_0000445794|||http://purl.uniprot.org/annotation/PRO_5014309583 http://togogenome.org/gene/10090:Ltb4r2 ^@ http://purl.uniprot.org/uniprot/Q9JJL9 ^@ 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|||Leukotriene B4 receptor 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069712 http://togogenome.org/gene/10090:Gm6902 ^@ http://purl.uniprot.org/uniprot/Q3UTA8 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Defa28 ^@ http://purl.uniprot.org/uniprot/D3Z1V9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Mammalian defensins ^@ http://purl.uniprot.org/annotation/PRO_5008952435 http://togogenome.org/gene/10090:Zfp420 ^@ http://purl.uniprot.org/uniprot/Q7TMN8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type ^@ http://togogenome.org/gene/10090:H3f3a ^@ http://purl.uniprot.org/uniprot/P84244 ^@ Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand ^@ 5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Abolished serotonylation by TGM2. Reduced neurite length.|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.3|||Interaction with ZMYND11|||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; 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_0000221251 http://togogenome.org/gene/10090:Pmpca ^@ http://purl.uniprot.org/uniprot/Q9DC61 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ Mitochondrial-processing peptidase subunit alpha|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000026768 http://togogenome.org/gene/10090:Mapkbp1 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQA2|||http://purl.uniprot.org/uniprot/Q6NS57 ^@ 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|||Disordered|||In isoform 2.|||Mitogen-activated protein kinase-binding protein 1|||Phosphoserine|||Polar residues|||WD|||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_0000334159|||http://purl.uniprot.org/annotation/VSP_033636 http://togogenome.org/gene/10090:Or52z13 ^@ http://purl.uniprot.org/uniprot/K7N6B3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp521 ^@ http://purl.uniprot.org/uniprot/Q6KAS7 ^@ 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 ^@ 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)|||In isoform 2.|||Phosphoserine|||Polar residues|||Zinc finger protein 521 ^@ http://purl.uniprot.org/annotation/PRO_0000306872|||http://purl.uniprot.org/annotation/VSP_028553 http://togogenome.org/gene/10090:Arhgap17 ^@ http://purl.uniprot.org/uniprot/E9QAJ9|||http://purl.uniprot.org/uniprot/Q3UIA2 ^@ 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 ^@ BAR|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho GTPase-activating protein 17|||Rho-GAP|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000280463|||http://purl.uniprot.org/annotation/VSP_023690|||http://purl.uniprot.org/annotation/VSP_023691|||http://purl.uniprot.org/annotation/VSP_023692 http://togogenome.org/gene/10090:Sufu ^@ http://purl.uniprot.org/uniprot/Q3U0Z8|||http://purl.uniprot.org/uniprot/Q9Z0P7 ^@ 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)|||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.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Suppressor of fused C-terminal|||Suppressor of fused homolog|||Suppressor of fused-like ^@ http://purl.uniprot.org/annotation/PRO_0000072303|||http://purl.uniprot.org/annotation/VSP_013281|||http://purl.uniprot.org/annotation/VSP_013282|||http://purl.uniprot.org/annotation/VSP_013283 http://togogenome.org/gene/10090:Eno4 ^@ http://purl.uniprot.org/uniprot/A0A0J9YUP0|||http://purl.uniprot.org/uniprot/Q8C042 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Enolase 4|||Enolase C-terminal TIM barrel|||Enolase N-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Pro residues|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000348455|||http://purl.uniprot.org/annotation/VSP_035167|||http://purl.uniprot.org/annotation/VSP_035168|||http://purl.uniprot.org/annotation/VSP_035169|||http://purl.uniprot.org/annotation/VSP_058229|||http://purl.uniprot.org/annotation/VSP_058230 http://togogenome.org/gene/10090:Brpf3 ^@ http://purl.uniprot.org/uniprot/B2KF05 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Bromo|||Bromodomain and PHD finger-containing protein 3|||C2HC pre-PHD-type|||Disordered|||In isoform 2.|||N6-acetyllysine|||PHD-type 1|||PHD-type 2|||PWWP|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000449611|||http://purl.uniprot.org/annotation/VSP_060569|||http://purl.uniprot.org/annotation/VSP_060570 http://togogenome.org/gene/10090:Tmem104 ^@ http://purl.uniprot.org/uniprot/Q3TB48 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 104 ^@ http://purl.uniprot.org/annotation/PRO_0000254179 http://togogenome.org/gene/10090:Adad2 ^@ http://purl.uniprot.org/uniprot/Q9D5P4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ A to I editase|||Adenosine deaminase domain-containing protein 2|||DRBM|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000309526 http://togogenome.org/gene/10090:Irf9 ^@ http://purl.uniprot.org/uniprot/E9PZJ2|||http://purl.uniprot.org/uniprot/E9Q8M6|||http://purl.uniprot.org/uniprot/Q3UKQ7|||http://purl.uniprot.org/uniprot/Q61179 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand ^@ Disordered|||IRF tryptophan pentad repeat|||Interferon regulatory factor 9|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000154568 http://togogenome.org/gene/10090:Ubc ^@ http://purl.uniprot.org/uniprot/P0CG50 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Site|||Strand|||Turn ^@ ADP-ribosylglycine|||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|||Phosphoserine|||Phosphoserine; by PINK1|||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|||Ubiquitin-related 1|||Ubiquitin-related 2 ^@ http://purl.uniprot.org/annotation/PRO_0000396192|||http://purl.uniprot.org/annotation/PRO_0000396193|||http://purl.uniprot.org/annotation/PRO_0000396194|||http://purl.uniprot.org/annotation/PRO_0000396195|||http://purl.uniprot.org/annotation/PRO_0000396196|||http://purl.uniprot.org/annotation/PRO_0000396197|||http://purl.uniprot.org/annotation/PRO_0000396198|||http://purl.uniprot.org/annotation/PRO_0000396199|||http://purl.uniprot.org/annotation/PRO_0000396200|||http://purl.uniprot.org/annotation/PRO_0000396201 http://togogenome.org/gene/10090:Fau ^@ http://purl.uniprot.org/uniprot/P62862 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic residues|||Disordered|||N6-succinyllysine|||Small ribosomal subunit protein eS30|||Ubiquitin-like FUBI-ribosomal protein eS30 fusion protein|||Ubiquitin-like protein FUBI ^@ http://purl.uniprot.org/annotation/PRO_0000174000|||http://purl.uniprot.org/annotation/PRO_0000457810|||http://purl.uniprot.org/annotation/PRO_0000457811 http://togogenome.org/gene/10090:P3h3 ^@ http://purl.uniprot.org/uniprot/Q8CG70 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Fe2OG dioxygenase|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Pro residues|||Prolyl 3-hydroxylase 3|||TPR 1|||TPR 2|||TPR 3|||TPR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000240361 http://togogenome.org/gene/10090:Tmem53 ^@ http://purl.uniprot.org/uniprot/Q9D0Z3 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||In isoform 3.|||Transmembrane protein 53 ^@ http://purl.uniprot.org/annotation/PRO_0000284119|||http://purl.uniprot.org/annotation/VSP_024447|||http://purl.uniprot.org/annotation/VSP_024448|||http://purl.uniprot.org/annotation/VSP_024449 http://togogenome.org/gene/10090:Calca ^@ http://purl.uniprot.org/uniprot/P70160|||http://purl.uniprot.org/uniprot/Q3V1A7|||http://purl.uniprot.org/uniprot/Q99JA0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Calcitonin|||Calcitonin gene-related peptide 1|||Calcitonin peptide-like|||Disordered|||N-linked (GlcNAc...) asparagine|||Phenylalanine amide|||Phosphoserine|||Proline amide ^@ http://purl.uniprot.org/annotation/PRO_0000004056|||http://purl.uniprot.org/annotation/PRO_0000004057|||http://purl.uniprot.org/annotation/PRO_0000004058|||http://purl.uniprot.org/annotation/PRO_0000004059|||http://purl.uniprot.org/annotation/PRO_0000004060|||http://purl.uniprot.org/annotation/PRO_0000004061|||http://purl.uniprot.org/annotation/PRO_5004230459 http://togogenome.org/gene/10090:Pp2d1 ^@ http://purl.uniprot.org/uniprot/Q8BVT6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ PPM-type phosphatase|||Protein phosphatase 2C-like domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000320673 http://togogenome.org/gene/10090:Lrp4 ^@ http://purl.uniprot.org/uniprot/Q8VI56 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like 1; atypical|||EGF-like 2; calcium-binding|||EGF-like 3|||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|||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_0000017326|||http://purl.uniprot.org/annotation/VSP_010034 http://togogenome.org/gene/10090:Gm13871 ^@ http://purl.uniprot.org/uniprot/A2BEI6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Rps12 ^@ http://purl.uniprot.org/uniprot/P63323 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant ^@ N-acetylalanine|||N6-succinyllysine|||Removed|||Requires 2 nucleotide substitutions.|||Small ribosomal subunit protein eS12 ^@ http://purl.uniprot.org/annotation/PRO_0000122324 http://togogenome.org/gene/10090:Tas2r124 ^@ http://purl.uniprot.org/uniprot/Q7M718 ^@ 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 124 ^@ http://purl.uniprot.org/annotation/PRO_0000248481 http://togogenome.org/gene/10090:0610009B22Rik ^@ http://purl.uniprot.org/uniprot/Q9CQP2 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand ^@ Aberrant protein folding and increased proteasomal degradation.|||Increased interaction with TRAPPC3.|||Trafficking protein particle complex subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000211567 http://togogenome.org/gene/10090:Shroom4 ^@ http://purl.uniprot.org/uniprot/Q1W617 ^@ 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 ^@ ASD2|||Basic and acidic residues|||Disordered|||In isoform 2.|||PDZ|||Phosphoserine|||Polar residues|||Protein Shroom4 ^@ http://purl.uniprot.org/annotation/PRO_0000287078|||http://purl.uniprot.org/annotation/VSP_025291 http://togogenome.org/gene/10090:Zkscan16 ^@ http://purl.uniprot.org/uniprot/A2ALW2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||SCAN box ^@ http://togogenome.org/gene/10090:Klri2 ^@ http://purl.uniprot.org/uniprot/Q5DT36 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||C-type lectin|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Killer cell lectin-like receptor subfamily I member 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000442201 http://togogenome.org/gene/10090:Sult2a4 ^@ http://purl.uniprot.org/uniprot/D3Z6M7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Srm ^@ http://purl.uniprot.org/uniprot/Q543H0|||http://purl.uniprot.org/uniprot/Q64674 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ N-acetylmethionine|||PABS|||Proton acceptor|||Spermidine synthase ^@ http://purl.uniprot.org/annotation/PRO_0000156446 http://togogenome.org/gene/10090:Cpvl ^@ http://purl.uniprot.org/uniprot/Q9D3S9 ^@ Active Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Glycosylation Site|||Propeptide|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||N-linked (GlcNAc...) asparagine|||Probable serine carboxypeptidase CPVL ^@ http://purl.uniprot.org/annotation/PRO_0000331586|||http://purl.uniprot.org/annotation/PRO_0000331587|||http://purl.uniprot.org/annotation/VSP_033260 http://togogenome.org/gene/10090:Xylt1 ^@ http://purl.uniprot.org/uniprot/F8VPK6|||http://purl.uniprot.org/uniprot/Q811B1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In pug; strongly reduced enzyme activity leads to defects in proteoglycan synthesis, abnormal chondrocyte maturation, premature ossification and dwarfism with short limbs and a compressed ribcage, which may be the cause for the increased mortality before weaning.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Xylosyltransferase 1|||Xylosyltransferase C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000191401 http://togogenome.org/gene/10090:Slc25a14 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQJ8|||http://purl.uniprot.org/uniprot/Q9Z2B2 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane ^@ Chain|||Repeat|||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.|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090678|||http://purl.uniprot.org/annotation/VSP_003274 http://togogenome.org/gene/10090:Tgfbr2 ^@ http://purl.uniprot.org/uniprot/Q3UG22|||http://purl.uniprot.org/uniprot/Q543C0|||http://purl.uniprot.org/uniprot/Q62312|||http://purl.uniprot.org/uniprot/Q8BQS9 ^@ Active Site|||Binding Site|||Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform RII-2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein kinase|||Proton acceptor|||TGF-beta receptor type-2 ^@ http://purl.uniprot.org/annotation/PRO_0000024427|||http://purl.uniprot.org/annotation/PRO_5004229973|||http://purl.uniprot.org/annotation/PRO_5004304221|||http://purl.uniprot.org/annotation/PRO_5014309597|||http://purl.uniprot.org/annotation/VSP_061515 http://togogenome.org/gene/10090:Dgki ^@ http://purl.uniprot.org/uniprot/D3YWQ0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Repeat|||Splice Variant|||Zinc Finger ^@ ANK 1|||ANK 2|||Basic residues|||DAGKc|||Diacylglycerol kinase iota|||Disordered|||In isoform 2.|||PDZ-binding|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000451698|||http://purl.uniprot.org/annotation/VSP_060832 http://togogenome.org/gene/10090:Gde1 ^@ http://purl.uniprot.org/uniprot/Q9JL56 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||GP-PDE|||Glycerophosphodiester phosphodiesterase 1|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000251945 http://togogenome.org/gene/10090:Fbln5 ^@ http://purl.uniprot.org/uniprot/Q9WVH9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000007578 http://togogenome.org/gene/10090:Adcy2 ^@ http://purl.uniprot.org/uniprot/Q3V1Q3 ^@ Binding Site|||Domain Extent|||Region|||Site|||Transmembrane ^@ Binding Site|||Domain Extent|||Transmembrane ^@ Guanylate cyclase|||Helical ^@ http://togogenome.org/gene/10090:Gpx8 ^@ http://purl.uniprot.org/uniprot/Q9D7B7 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||N-acetylmethionine|||Probable glutathione peroxidase 8 ^@ http://purl.uniprot.org/annotation/PRO_0000317757 http://togogenome.org/gene/10090:Dnm1 ^@ http://purl.uniprot.org/uniprot/A0A0J9YUN4|||http://purl.uniprot.org/uniprot/P39053 ^@ 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 ^@ 3'-nitrotyrosine; alternate|||Disordered|||Dynamin-1|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||GED|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; alternate|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000206564|||http://purl.uniprot.org/annotation/VSP_007643|||http://purl.uniprot.org/annotation/VSP_007644|||http://purl.uniprot.org/annotation/VSP_007645|||http://purl.uniprot.org/annotation/VSP_007647|||http://purl.uniprot.org/annotation/VSP_024845 http://togogenome.org/gene/10090:Paip1 ^@ http://purl.uniprot.org/uniprot/D3Z3J6|||http://purl.uniprot.org/uniprot/Q8VE62 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||MIF4G|||PABPC1-interacting motif-1 (PAM1)|||PABPC1-interacting motif-2 (PAM2)|||PAIP1 middle domain (PAIP1M)|||Polar residues|||Polyadenylate-binding protein-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000058178 http://togogenome.org/gene/10090:Prdx4 ^@ http://purl.uniprot.org/uniprot/O08807 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Strand|||Turn ^@ Cysteine sulfenic acid (-SOH) intermediate|||Interchain (with C-127); in linked form|||Interchain (with C-248); in linked form|||Peroxiredoxin-4|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000135099 http://togogenome.org/gene/10090:Myoz3 ^@ http://purl.uniprot.org/uniprot/E9QJU4|||http://purl.uniprot.org/uniprot/Q8R4E4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Binding to ACTN2|||Binding to ACTN2, PPP3CA and TCAP|||Binding to FLNC|||Disordered|||Myozenin-3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000111103 http://togogenome.org/gene/10090:Trp53inp1 ^@ http://purl.uniprot.org/uniprot/Q9QXE4 ^@ Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Motif|||Splice Variant ^@ In isoform 2.|||LIR|||Tumor protein p53-inducible nuclear protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072407|||http://purl.uniprot.org/annotation/VSP_013177 http://togogenome.org/gene/10090:Ppp1r9b ^@ http://purl.uniprot.org/uniprot/Q6R891 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant ^@ Acidic residues|||Actin-binding|||Basic and acidic residues|||Disordered|||In isoform 2.|||Increases filopodial density.|||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|||Phosphoserine; by CDK5|||Phosphoserine; by MAPK1|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000228615|||http://purl.uniprot.org/annotation/VSP_017674|||http://purl.uniprot.org/annotation/VSP_017675 http://togogenome.org/gene/10090:Or7g33 ^@ http://purl.uniprot.org/uniprot/Q8VGG6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gpr21 ^@ http://purl.uniprot.org/uniprot/Q8BX79 ^@ 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 21 ^@ http://purl.uniprot.org/annotation/PRO_0000303234 http://togogenome.org/gene/10090:Atp4a ^@ http://purl.uniprot.org/uniprot/Q64436|||http://purl.uniprot.org/uniprot/Q91WH7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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_0000046254 http://togogenome.org/gene/10090:Gngt1 ^@ http://purl.uniprot.org/uniprot/Q61012 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Propeptide ^@ Chain|||Initiator Methionine|||Lipid Binding|||Mass|||Modified Residue|||Propeptide ^@ Cysteine methyl ester|||Guanine nucleotide-binding protein G(T) subunit gamma-T1|||Includes farnesylation and methylation.|||Removed|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000012607|||http://purl.uniprot.org/annotation/PRO_0000012608 http://togogenome.org/gene/10090:Casp4 ^@ http://purl.uniprot.org/uniprot/P70343 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ (Microbial infection) ADP-riboxanated arginine|||Abolished ability to cleave Gasdermin-D (GSDMD).|||CARD|||Caspase-4 subunit p10|||Caspase-4 subunit p20|||Cleavage; by autolysis|||Complete loss of LPS-binding, LPS-induced oligomerization, and LPS-induced pyroptosis; when associated with E-53 and A-55.|||Complete loss of LPS-binding, LPS-induced oligomerization, and LPS-induced pyroptosis; when associated with E-54 and A-55.|||Impaired NLRP6 inflammasome-dependent activation and release of IL1B and IL18.|||In isoform 2.|||Loss of autocatalytic processing and subsequent activation.|||Loss of catalytic activity and of autocatalytic processing. Loss of LPS-induced pyroptosis. No effect on the interaction with LPS.|||No cell death.|||No effect on LPS-binding, LPS-induced oligomerization, and LPS-induced pyroptosis; when associated with E-38.|||No effect on LPS-binding, LPS-induced oligomerization, and LPS-induced pyroptosis; when associated with M-40.|||Phosphoserine|||Required for LPS-binding|||Severely attenuated LPS-binding, LPS-induced oligomerization and activation, and LPS-induced pyroptosis.|||Severely attenuated LPS-binding, LPS-induced oligomerization and activation, and LPS-induced pyroptosis; when associated with E-62 and E-63.|||Severely attenuated LPS-binding, LPS-induced oligomerization and activation, and LPS-induced pyroptosis; when associated with E-62 and E-64.|||Severely attenuated LPS-binding, LPS-induced oligomerization and activation, and LPS-induced pyroptosis; when associated with E-63 and E-64. ^@ http://purl.uniprot.org/annotation/PRO_0000004600|||http://purl.uniprot.org/annotation/PRO_0000004601|||http://purl.uniprot.org/annotation/PRO_0000004602|||http://purl.uniprot.org/annotation/PRO_0000004603|||http://purl.uniprot.org/annotation/VSP_058183|||http://purl.uniprot.org/annotation/VSP_058184 http://togogenome.org/gene/10090:Matn2 ^@ http://purl.uniprot.org/uniprot/Q3TQ80 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Non-terminal Residue|||Signal Peptide ^@ VWFA|||VWFA domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5004229605 http://togogenome.org/gene/10090:Cradd ^@ http://purl.uniprot.org/uniprot/O88843|||http://purl.uniprot.org/uniprot/Q3UMW0|||http://purl.uniprot.org/uniprot/Q549T4 ^@ 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 ^@ CARD|||Death|||Death domain-containing protein CRADD|||Disordered|||Impairs the interaction with PIDD.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079327 http://togogenome.org/gene/10090:Vmn2r85 ^@ http://purl.uniprot.org/uniprot/G3UW56 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015091588 http://togogenome.org/gene/10090:Bmper ^@ http://purl.uniprot.org/uniprot/Q8CJ69 ^@ 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 ^@ BMP-binding endothelial regulator protein|||N-linked (GlcNAc...) asparagine|||TIL|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4|||VWFC 5|||VWFD ^@ http://purl.uniprot.org/annotation/PRO_0000020821 http://togogenome.org/gene/10090:Nf1 ^@ http://purl.uniprot.org/uniprot/Q04690 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Bipartite nuclear localization signal|||CRAL-TRIO|||Disordered|||In isoform I and isoform IV.|||In isoform III and isoform IV.|||Lipid binding|||N-acetylalanine|||Neurofibromin|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ras-GAP|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056666|||http://purl.uniprot.org/annotation/VSP_001633|||http://purl.uniprot.org/annotation/VSP_001634|||http://purl.uniprot.org/annotation/VSP_001635 http://togogenome.org/gene/10090:Mettl9 ^@ http://purl.uniprot.org/uniprot/Q9EPL4 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Abolished protein-histidine N-methyltransferase activity.|||N-linked (GlcNAc...) asparagine|||Protein-L-histidine N-pros-methyltransferase|||Reduced protein-histidine N-methyltransferase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000317491 http://togogenome.org/gene/10090:Ccdc97 ^@ http://purl.uniprot.org/uniprot/Q9DBT3 ^@ 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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000286097 http://togogenome.org/gene/10090:Naxe ^@ http://purl.uniprot.org/uniprot/Q8K4Z3 ^@ 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|||Strand|||Transit Peptide|||Turn ^@ Mitochondrion|||N6-succinyllysine|||NAD(P)H-hydrate epimerase|||Phosphoserine; by PKA|||YjeF N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000292423 http://togogenome.org/gene/10090:Agmo ^@ http://purl.uniprot.org/uniprot/Q8BS35 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Motif|||Splice Variant|||Transmembrane ^@ Alkylglycerol monooxygenase|||Fatty acid hydroxylase|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000299301|||http://purl.uniprot.org/annotation/VSP_027599|||http://purl.uniprot.org/annotation/VSP_027600 http://togogenome.org/gene/10090:Smim6 ^@ http://purl.uniprot.org/uniprot/Q3U0I6 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Hdac9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1F3|||http://purl.uniprot.org/uniprot/A0A1B0GR65|||http://purl.uniprot.org/uniprot/A0A1B0GRH0|||http://purl.uniprot.org/uniprot/A0A1B0GSQ5|||http://purl.uniprot.org/uniprot/A0A668KM95|||http://purl.uniprot.org/uniprot/Q99N13 ^@ 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|||Site|||Splice Variant ^@ Abolishes binding to CTBP1 and impairs function in transcription repression.|||Basic and acidic residues|||Contributes to catalysis|||Disordered|||Histone deacetylase|||Histone deacetylase 9|||Histone deacetylase glutamine rich N-terminal|||In isoform 2.|||In isoform 3.|||Interaction with CTBP1|||Interaction with ETV6|||Interaction with MAPK10|||Interaction with MEF2|||Phosphoserine|||Phosphoserine; by DYRK1B|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000114711|||http://purl.uniprot.org/annotation/VSP_023769|||http://purl.uniprot.org/annotation/VSP_029173 http://togogenome.org/gene/10090:Tmprss4 ^@ http://purl.uniprot.org/uniprot/Q8VCA5 ^@ 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|||Site|||Topological Domain|||Transmembrane ^@ Charge relay system|||Cleavage|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||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_0000088693|||http://purl.uniprot.org/annotation/PRO_0000451628 http://togogenome.org/gene/10090:Akt3 ^@ http://purl.uniprot.org/uniprot/Q8C6X4|||http://purl.uniprot.org/uniprot/Q9WUA6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant ^@ AGC-kinase C-terminal|||Basic and acidic residues|||Disordered|||Enhances kinase activity and causes low seizure threshold, sporadic tonic-clonic seizures, brain enlargement and ectopic neurons in the dentate hilus and molecular layer of the hippocampus.|||In isoform 2.|||N-acetylserine|||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_0000085612|||http://purl.uniprot.org/annotation/VSP_004948 http://togogenome.org/gene/10090:Hes7 ^@ http://purl.uniprot.org/uniprot/Q8BKT2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disordered|||Loss of repressor activity.|||No loss of repressor activity, somite segmentation disrupted at later stages.|||No loss of repressor activity.|||Orange|||Partial loss of repressor activity.|||Pro residues|||Transcription factor HES-7|||WRPW motif|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000252423 http://togogenome.org/gene/10090:Aatk ^@ http://purl.uniprot.org/uniprot/B1AZF3|||http://purl.uniprot.org/uniprot/B1AZF9|||http://purl.uniprot.org/uniprot/Q80YE4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase LMTK1|||Significant decrease in autophosphorylation. ^@ http://purl.uniprot.org/annotation/PRO_0000248301|||http://purl.uniprot.org/annotation/PRO_5002760507|||http://purl.uniprot.org/annotation/VSP_020229|||http://purl.uniprot.org/annotation/VSP_020230|||http://purl.uniprot.org/annotation/VSP_020231|||http://purl.uniprot.org/annotation/VSP_020232 http://togogenome.org/gene/10090:Eif2d ^@ http://purl.uniprot.org/uniprot/A0A0R4J298|||http://purl.uniprot.org/uniprot/E9PUG7|||http://purl.uniprot.org/uniprot/Q61211 ^@ 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 ^@ DM2|||Disordered|||Eukaryotic translation initiation factor 2D|||In isoform 2.|||N-acetylmethionine|||PUA|||Phosphoserine|||Polar residues|||SUI1|||SWIB/MDM2 ^@ http://purl.uniprot.org/annotation/PRO_0000130612|||http://purl.uniprot.org/annotation/VSP_016233 http://togogenome.org/gene/10090:Tbxas1 ^@ http://purl.uniprot.org/uniprot/P36423|||http://purl.uniprot.org/uniprot/Q3UTF0 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Thromboxane-A synthase|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000052257 http://togogenome.org/gene/10090:Nudt16 ^@ http://purl.uniprot.org/uniprot/Q6P3D0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict ^@ Nudix box|||Nudix hydrolase|||U8 snoRNA-decapping enzyme ^@ http://purl.uniprot.org/annotation/PRO_0000057118 http://togogenome.org/gene/10090:Bmp10 ^@ http://purl.uniprot.org/uniprot/Q9R229 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Bone morphogenetic protein 10|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033890|||http://purl.uniprot.org/annotation/PRO_0000033891 http://togogenome.org/gene/10090:Lpar4 ^@ http://purl.uniprot.org/uniprot/Q8BLG2 ^@ 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_0000250204 http://togogenome.org/gene/10090:Kics2 ^@ http://purl.uniprot.org/uniprot/Q6P1I3 ^@ 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.|||KICSTOR subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000321903|||http://purl.uniprot.org/annotation/VSP_031819|||http://purl.uniprot.org/annotation/VSP_031820 http://togogenome.org/gene/10090:Foxp3 ^@ http://purl.uniprot.org/uniprot/Q53Z59|||http://purl.uniprot.org/uniprot/Q99JB6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Site|||Strand|||Turn|||Zinc Finger ^@ C2H2-type|||Cleavage|||Cleavage; by PCSK1 or PCSK2|||Disordered|||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|||Increase in protein stability, transcriptional activity and the ability to suppress the proliferation of conventional T-cells in vitro; when associated with A-19; A-114 and A-175.|||Increase in protein stability, transcriptional activity and the ability to suppress the proliferation of conventional T-cells in vitro; when associated with A-19; A-88 and A-114.|||Increase in protein stability, transcriptional activity and the ability to suppress the proliferation of conventional T-cells in vitro; when associated with A-19; A-88 and A-175.|||Interaction with IKZF4|||Interaction with RUNX1|||LXXLL motif|||Leucine-zipper|||Loss of ability to suppress the proliferation of effector T-cells.|||Loss of homodimerization, decrease in transcriptional repressor activity, elimination of its Treg suppressor activity, defects in Th1 and Th2 cytokine secretion and down-regulation of cell surface markers on regulatory T-cells.|||Loss of interaction with RUNX1 but no effect on interaction with NFATC2 and loss of its ability to regulate the expression of IL2, TNFRSF18, IL2RA and CTLA4 in a RUNX1-dependent manner; when associated with 329-VH-330.|||Loss of phosphorylation. Increase in protein stability, transcriptional activity and the ability to suppress the proliferation of conventional T-cells in vitro; when associated with A-88; A-114 and A-175.|||Loss of proteolytic processing.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphothreonine; by CDK2|||Polar residues|||Reduced interaction with RUNX1, decrease in its ability to regulate the expression of IL2, TNFRSF18, IL2RA and CTLA4 in a RUNX1-dependent manner. Loss of interaction with RUNX1 but no effect on interaction with NFATC2 and loss of its ability to regulate the expression of IL2, TNFRSF18, IL2RA and CTLA4 in a RUNX1-dependent manner; when associated with L-332. ^@ http://purl.uniprot.org/annotation/PRO_0000091888|||http://purl.uniprot.org/annotation/PRO_0000432436|||http://purl.uniprot.org/annotation/PRO_0000432437|||http://purl.uniprot.org/annotation/PRO_0000432438 http://togogenome.org/gene/10090:Slc17a4 ^@ http://purl.uniprot.org/uniprot/A0A2C9F2D4|||http://purl.uniprot.org/uniprot/Q5NCM1|||http://purl.uniprot.org/uniprot/Q8BWR0 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Transmembrane ^@ Disordered|||Helical|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Probable small intestine urate exporter ^@ http://purl.uniprot.org/annotation/PRO_0000318167 http://togogenome.org/gene/10090:Cep97 ^@ http://purl.uniprot.org/uniprot/Q9CZ62 ^@ 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|||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|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000263706|||http://purl.uniprot.org/annotation/VSP_021883 http://togogenome.org/gene/10090:Lats2 ^@ http://purl.uniprot.org/uniprot/Q7TSJ6|||http://purl.uniprot.org/uniprot/Q8VHE2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ AGC-kinase C-terminal|||Basic and acidic residues|||Disordered|||PPxY motif|||Phosphoserine|||Phosphoserine; by AURKA|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase LATS2|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000086235 http://togogenome.org/gene/10090:Or2a54 ^@ http://purl.uniprot.org/uniprot/Q8VFS5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Prg2 ^@ http://purl.uniprot.org/uniprot/Q545D8|||http://purl.uniprot.org/uniprot/Q61878 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide ^@ Acidic|||Basic and acidic residues|||Bone marrow proteoglycan|||C-type lectin|||Disordered|||Eosinophil granule major basic protein|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine; partial|||O-linked (Xyl...) (chondroitin sulfate) serine ^@ http://purl.uniprot.org/annotation/PRO_0000017387|||http://purl.uniprot.org/annotation/PRO_0000017388|||http://purl.uniprot.org/annotation/PRO_0000259924|||http://purl.uniprot.org/annotation/PRO_5014309628 http://togogenome.org/gene/10090:Dpf2 ^@ http://purl.uniprot.org/uniprot/D3Z5N6|||http://purl.uniprot.org/uniprot/Q61103 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Zinc finger protein ubi-d4 ^@ http://purl.uniprot.org/annotation/PRO_0000168150 http://togogenome.org/gene/10090:Uts2 ^@ http://purl.uniprot.org/uniprot/Q541G7|||http://purl.uniprot.org/uniprot/Q9QZQ3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||Polar residues|||Urotensin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000036350|||http://purl.uniprot.org/annotation/PRO_0000036351|||http://purl.uniprot.org/annotation/PRO_0000036352|||http://purl.uniprot.org/annotation/PRO_5014309544 http://togogenome.org/gene/10090:Cyp2d12 ^@ http://purl.uniprot.org/uniprot/Q8BVD2 ^@ Binding Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Gsta2 ^@ http://purl.uniprot.org/uniprot/P10648 ^@ 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 ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase A2|||N-acetylalanine|||N6-succinyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000185789 http://togogenome.org/gene/10090:Nmur1 ^@ http://purl.uniprot.org/uniprot/O55040 ^@ 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|||Neuromedin-U receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000069907 http://togogenome.org/gene/10090:Vps39 ^@ http://purl.uniprot.org/uniprot/Q3USV9|||http://purl.uniprot.org/uniprot/Q5KU38|||http://purl.uniprot.org/uniprot/Q8R5L3 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Splice Variant ^@ CHCR|||CNH|||In isoform 2.|||Vam6/Vps39-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000065902|||http://purl.uniprot.org/annotation/VSP_004076 http://togogenome.org/gene/10090:Vmn2r13 ^@ http://purl.uniprot.org/uniprot/L7N1X2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982194 http://togogenome.org/gene/10090:Cpe ^@ http://purl.uniprot.org/uniprot/Q00493|||http://purl.uniprot.org/uniprot/Q543R4 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ Activation peptide|||Carboxypeptidase E|||In hyperproinsulinemia obese fat/fat mice; reduced activity.|||N-linked (GlcNAc...) asparagine|||Peptidase M14 carboxypeptidase A|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004386|||http://purl.uniprot.org/annotation/PRO_0000004387|||http://purl.uniprot.org/annotation/PRO_5009971089 http://togogenome.org/gene/10090:Chd8 ^@ http://purl.uniprot.org/uniprot/Q09XV5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ 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 isoform 2.|||Interaction with FAM124B|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000367310|||http://purl.uniprot.org/annotation/VSP_036676|||http://purl.uniprot.org/annotation/VSP_036677 http://togogenome.org/gene/10090:Atad1 ^@ http://purl.uniprot.org/uniprot/Q9D5T0 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Mitochondrial intermembrane|||Outer mitochondrial transmembrane helix translocase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000084792 http://togogenome.org/gene/10090:Trim29 ^@ http://purl.uniprot.org/uniprot/Q8R2Q0 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ B box-type|||Disordered|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Tripartite motif-containing protein 29 ^@ http://purl.uniprot.org/annotation/PRO_0000056243 http://togogenome.org/gene/10090:Notch4 ^@ http://purl.uniprot.org/uniprot/P31695 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||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|||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|||LNR 1|||LNR 2|||LNR 3|||N-linked (GlcNAc...) asparagine|||NICD processing severely reduced.|||Neurogenic locus notch homolog protein 4|||Notch 4 extracellular truncation|||Notch 4 intracellular domain|||Transforming protein Int-3 ^@ http://purl.uniprot.org/annotation/PRO_0000007704|||http://purl.uniprot.org/annotation/PRO_0000007705|||http://purl.uniprot.org/annotation/PRO_0000007706|||http://purl.uniprot.org/annotation/PRO_0000007707 http://togogenome.org/gene/10090:Myo1h ^@ http://purl.uniprot.org/uniprot/A0A0J9YUC4 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent|||Region ^@ Actin-binding|||Myosin motor|||TH1 ^@ http://togogenome.org/gene/10090:Ifnab ^@ http://purl.uniprot.org/uniprot/L7MTU6|||http://purl.uniprot.org/uniprot/Q61719 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5014310245|||http://purl.uniprot.org/annotation/PRO_5040056769 http://togogenome.org/gene/10090:Dynlrb2 ^@ http://purl.uniprot.org/uniprot/Q9DAJ5 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ Dynein light chain roadblock-type 2|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000220959|||http://purl.uniprot.org/annotation/VSP_007238 http://togogenome.org/gene/10090:Or2y13 ^@ http://purl.uniprot.org/uniprot/Q7TQT2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Igfn1 ^@ http://purl.uniprot.org/uniprot/Q3KNY0 ^@ 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|||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.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000347187|||http://purl.uniprot.org/annotation/VSP_035061|||http://purl.uniprot.org/annotation/VSP_035062|||http://purl.uniprot.org/annotation/VSP_035065|||http://purl.uniprot.org/annotation/VSP_039842|||http://purl.uniprot.org/annotation/VSP_039843 http://togogenome.org/gene/10090:Tcof1 ^@ http://purl.uniprot.org/uniprot/H3BL37|||http://purl.uniprot.org/uniprot/O08784|||http://purl.uniprot.org/uniprot/Q6PFZ6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||10|||10 X approximate tandem repeats|||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 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|||LisH|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Treacle protein ^@ http://purl.uniprot.org/annotation/PRO_0000072460 http://togogenome.org/gene/10090:Large2 ^@ http://purl.uniprot.org/uniprot/A2AHG6|||http://purl.uniprot.org/uniprot/Q14AT0|||http://purl.uniprot.org/uniprot/Q5XPT3 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Glucuronyltransferase activity|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Xylosyl- and glucuronyltransferase LARGE2|||Xylosyltransferase activity ^@ http://purl.uniprot.org/annotation/PRO_0000226812|||http://purl.uniprot.org/annotation/PRO_5015086011|||http://purl.uniprot.org/annotation/PRO_5015097034|||http://purl.uniprot.org/annotation/VSP_017489|||http://purl.uniprot.org/annotation/VSP_041607|||http://purl.uniprot.org/annotation/VSP_041608 http://togogenome.org/gene/10090:Rapgef2 ^@ http://purl.uniprot.org/uniprot/E9QNQ4|||http://purl.uniprot.org/uniprot/Q6NXI4 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Cyclic nucleotide-binding|||Disordered|||N-terminal Ras-GEF|||PDZ|||Polar residues|||Ras-GEF|||Ras-associating ^@ http://togogenome.org/gene/10090:Nenf ^@ http://purl.uniprot.org/uniprot/Q9CQ45 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Signal Peptide ^@ Cytochrome b5 heme-binding|||Does not bind heme.|||N6-acetyllysine|||Neudesin ^@ http://purl.uniprot.org/annotation/PRO_0000018599 http://togogenome.org/gene/10090:C4bp ^@ http://purl.uniprot.org/uniprot/P08607 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ C4b-binding protein|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6 ^@ http://purl.uniprot.org/annotation/PRO_0000005889 http://togogenome.org/gene/10090:Pcdhga5 ^@ http://purl.uniprot.org/uniprot/Q91XY3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099528 http://togogenome.org/gene/10090:Tubb4b ^@ http://purl.uniprot.org/uniprot/P68372 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 5-glutamyl polyglutamate|||Acidic residues|||Disordered|||MREI motif|||N6-acetyllysine|||Phosphoserine; by CDK1|||Phosphothreonine|||Tubulin beta-4B chain ^@ http://purl.uniprot.org/annotation/PRO_0000048249 http://togogenome.org/gene/10090:Rab4b ^@ http://purl.uniprot.org/uniprot/Q91ZR1 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict ^@ 5-glutamyl serotonin|||Cysteine methyl ester|||Effector region|||N-acetylalanine|||Phosphoserine|||Ras-related protein Rab-4B|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121100 http://togogenome.org/gene/10090:Cdk2 ^@ http://purl.uniprot.org/uniprot/P97377|||http://purl.uniprot.org/uniprot/Q3U6X7|||http://purl.uniprot.org/uniprot/Q3UGB9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Site|||Splice Variant ^@ CDK7 binding|||Cyclin-dependent kinase 2|||In isoform CDK2-alpha.|||Loss of tyrosine phosphorylation by WEE1 and CABLES1.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CAK and CCRK|||Phosphotyrosine|||Phosphotyrosine; by WEE1|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085771|||http://purl.uniprot.org/annotation/VSP_004800 http://togogenome.org/gene/10090:Fis1 ^@ http://purl.uniprot.org/uniprot/D3YZ32|||http://purl.uniprot.org/uniprot/G3X9U9|||http://purl.uniprot.org/uniprot/Q9CQ92 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Helix|||Modified Residue|||Repeat|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Mitochondrial fission 1 protein|||Mitochondrial intermembrane|||N-acetylmethionine|||Phosphoserine|||TPR ^@ http://purl.uniprot.org/annotation/PRO_0000106394 http://togogenome.org/gene/10090:Fsip2l ^@ http://purl.uniprot.org/uniprot/A2AF73 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Saa4 ^@ http://purl.uniprot.org/uniprot/P31532 ^@ 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|||Serum amyloid A-4 protein ^@ http://purl.uniprot.org/annotation/PRO_0000031592 http://togogenome.org/gene/10090:Rpl24 ^@ http://purl.uniprot.org/uniprot/Q8BP67 ^@ 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 ^@ ADP-ribosyl glutamic acid|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000136869 http://togogenome.org/gene/10090:Ppp1r8 ^@ http://purl.uniprot.org/uniprot/A2ADR8|||http://purl.uniprot.org/uniprot/Q8R3G1 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Strand|||Turn ^@ Disordered|||FHA|||Interaction with CDC5L, SF3B1 and MELK|||Interaction with EED|||Involved in PP-1 binding|||Involved in PP-1 inhibition|||Nuclear inhibitor of protein phosphatase 1|||Nuclear localization signal 1|||Nuclear localization signal 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||RNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000071506 http://togogenome.org/gene/10090:Rrp12 ^@ http://purl.uniprot.org/uniprot/Q3UJA1|||http://purl.uniprot.org/uniprot/Q6P5B0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||Phosphoserine|||Phosphothreonine|||RRP12-like protein|||Ribosomal RNA-processing protein 12-like conserved ^@ http://purl.uniprot.org/annotation/PRO_0000050769 http://togogenome.org/gene/10090:Megf11 ^@ http://purl.uniprot.org/uniprot/E9Q918|||http://purl.uniprot.org/uniprot/Q80T91 ^@ 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|||EGF-like|||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|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Laminin EGF-like|||Multiple epidermal growth factor-like domains protein 11|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000309736|||http://purl.uniprot.org/annotation/PRO_5003244516|||http://purl.uniprot.org/annotation/VSP_029253|||http://purl.uniprot.org/annotation/VSP_029254|||http://purl.uniprot.org/annotation/VSP_029255|||http://purl.uniprot.org/annotation/VSP_029256|||http://purl.uniprot.org/annotation/VSP_029257|||http://purl.uniprot.org/annotation/VSP_029258|||http://purl.uniprot.org/annotation/VSP_029259 http://togogenome.org/gene/10090:Or6c208 ^@ http://purl.uniprot.org/uniprot/Q8VFZ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gid4 ^@ http://purl.uniprot.org/uniprot/Q9CPY6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Site ^@ Disordered|||Glucose-induced degradation protein 4 homolog|||Interaction with the N-terminal Pro (Pro/N-degron) of proteins that are targeted for degradation|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079303 http://togogenome.org/gene/10090:Rfx8 ^@ http://purl.uniprot.org/uniprot/D3YU81 ^@ Chain|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||DNA Binding ^@ DNA-binding protein RFX8|||RFX-type winged-helix ^@ http://purl.uniprot.org/annotation/PRO_0000395345 http://togogenome.org/gene/10090:Vwf ^@ http://purl.uniprot.org/uniprot/E9QPU1|||http://purl.uniprot.org/uniprot/Q8CIZ8 ^@ Chain|||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|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Accelerated clearance of VWF from blood plasma.|||Amino-terminal|||CTCK|||CX|||Cell attachment site|||E1|||E2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Or C-1899 with C-1942|||TIL 1|||TIL 2|||TIL 3|||TIL 4|||VWFA|||VWFA 1; binding site for platelet glycoprotein Ib|||VWFA 2|||VWFA 3; principal binding site for collagens type I and III|||VWFC|||VWFC 1|||VWFC 2|||VWFC 3|||VWFD|||VWFD 1|||VWFD 2|||VWFD 3|||VWFD 4|||von Willebrand antigen 2|||von Willebrand factor ^@ http://purl.uniprot.org/annotation/PRO_0000022684|||http://purl.uniprot.org/annotation/PRO_0000022685|||http://purl.uniprot.org/annotation/PRO_5005911211|||http://purl.uniprot.org/annotation/VSP_051618|||http://purl.uniprot.org/annotation/VSP_051619 http://togogenome.org/gene/10090:Wfdc17 ^@ http://purl.uniprot.org/uniprot/Q5SSJ1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ WAP ^@ http://purl.uniprot.org/annotation/PRO_5015098020 http://togogenome.org/gene/10090:BC061237 ^@ http://purl.uniprot.org/uniprot/Q6P8I2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Exo1 ^@ http://purl.uniprot.org/uniprot/Q9QZ11 ^@ 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|||Exonuclease 1|||I-domain|||Interaction with MLH1|||Interaction with MSH2|||Interaction with MSH3|||N-domain|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000154040 http://togogenome.org/gene/10090:Zc3h15 ^@ http://purl.uniprot.org/uniprot/Q3TIV5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||C3H1-type 1|||C3H1-type 2|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Required for interaction with DRG1|||Zinc finger CCCH domain-containing protein 15 ^@ http://purl.uniprot.org/annotation/PRO_0000324643|||http://purl.uniprot.org/annotation/VSP_032341|||http://purl.uniprot.org/annotation/VSP_032342|||http://purl.uniprot.org/annotation/VSP_032343 http://togogenome.org/gene/10090:Ppp1r17 ^@ http://purl.uniprot.org/uniprot/Q9Z2E4 ^@ 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|||Does not potentiate the phosphorylation of the CREB transcription factor; when associated with A-123.|||Does not potentiate the phosphorylation of the CREB transcription factor; when associated with A-72.|||Phosphothreonine; by PKG/PRKG1|||Protein phosphatase 1 regulatory subunit 17 ^@ http://purl.uniprot.org/annotation/PRO_0000414576 http://togogenome.org/gene/10090:Krt40 ^@ http://purl.uniprot.org/uniprot/E9PV64|||http://purl.uniprot.org/uniprot/Q6IFX3 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||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_0000314858 http://togogenome.org/gene/10090:Mpnd ^@ http://purl.uniprot.org/uniprot/Q3TV65 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ Acidic residues|||Disordered|||JAMM motif|||MPN|||MPN domain-containing protein|||N-acetylalanine|||Phosphoserine|||RAMA|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000278805 http://togogenome.org/gene/10090:Nfrkb ^@ http://purl.uniprot.org/uniprot/Q6PIJ4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ 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|||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_0000227808 http://togogenome.org/gene/10090:Hp ^@ http://purl.uniprot.org/uniprot/Q3UBS3|||http://purl.uniprot.org/uniprot/Q61646 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Haptoglobin|||Haptoglobin alpha chain|||Haptoglobin beta chain|||Interaction with CD163|||Interchain|||Interchain (between alpha and beta chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_0000028462|||http://purl.uniprot.org/annotation/PRO_0000028463|||http://purl.uniprot.org/annotation/PRO_0000028464|||http://purl.uniprot.org/annotation/PRO_5014309141 http://togogenome.org/gene/10090:Slfn14 ^@ http://purl.uniprot.org/uniprot/V9GXG1 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ C-terminally truncated SLFN14 endoribonuclease|||Protein SLFN14|||Required for endoribonuclease activity|||Required for ribosome binding ^@ http://purl.uniprot.org/annotation/PRO_0000436154|||http://purl.uniprot.org/annotation/PRO_0000436155 http://togogenome.org/gene/10090:Tagln2 ^@ http://purl.uniprot.org/uniprot/Q9WVA4 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ Calponin-homology (CH)|||Calponin-like|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Removed|||Transgelin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000204787 http://togogenome.org/gene/10090:6820408C15Rik ^@ http://purl.uniprot.org/uniprot/B2RQ99|||http://purl.uniprot.org/uniprot/Q8BJX2 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:P2rx7 ^@ http://purl.uniprot.org/uniprot/C8YIX4|||http://purl.uniprot.org/uniprot/F8WI93|||http://purl.uniprot.org/uniprot/Q3UN00|||http://purl.uniprot.org/uniprot/Q6P5P0|||http://purl.uniprot.org/uniprot/Q8CHP4|||http://purl.uniprot.org/uniprot/Q9Z1M0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ADP-ribosylarginine; by ART2B|||Abolishes calcium responses to NAD.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||N-linked (GlcNAc...) asparagine|||No effect on calcium responses to NAD.|||P2X purinoceptor 7|||P2X purinoreceptor 7 intracellular|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000161561 http://togogenome.org/gene/10090:Il6st ^@ http://purl.uniprot.org/uniprot/Q00560|||http://purl.uniprot.org/uniprot/Q6PDI9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Ig-like C2-type|||Interleukin-6 receptor subunit beta|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010900|||http://purl.uniprot.org/annotation/PRO_5004279459 http://togogenome.org/gene/10090:Taf8 ^@ http://purl.uniprot.org/uniprot/Q9EQH4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Histone-fold|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Transcription initiation factor TFIID subunit 8 ^@ http://purl.uniprot.org/annotation/PRO_0000315398|||http://purl.uniprot.org/annotation/VSP_030550|||http://purl.uniprot.org/annotation/VSP_030551|||http://purl.uniprot.org/annotation/VSP_030552|||http://purl.uniprot.org/annotation/VSP_030553|||http://purl.uniprot.org/annotation/VSP_030554|||http://purl.uniprot.org/annotation/VSP_030555 http://togogenome.org/gene/10090:Mcoln3 ^@ http://purl.uniprot.org/uniprot/Q3KP78|||http://purl.uniprot.org/uniprot/Q8R4F0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Abolishes channel activity.|||Cytoplasmic|||Extracellular|||Extracellular/lumenal pore loop|||Helical|||In Va and Va-J; constitutive active cation channel localized to plasma membrane.|||In Va-J.|||Interaction with phosphoinositides|||Mucolipin-3|||N-linked (GlcNAc...) asparagine|||Polycystin cation channel PKD1/PKD2|||Pore-forming|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000215368 http://togogenome.org/gene/10090:Gm5800 ^@ http://purl.uniprot.org/uniprot/Q497L3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Saraf ^@ http://purl.uniprot.org/uniprot/A0A0R4J0D1|||http://purl.uniprot.org/uniprot/Q8R3Q0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Polar residues|||Store-operated calcium entry-associated regulatory factor ^@ http://purl.uniprot.org/annotation/PRO_0000045486 http://togogenome.org/gene/10090:Apold1 ^@ http://purl.uniprot.org/uniprot/E9Q0X2 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Kcnj1 ^@ http://purl.uniprot.org/uniprot/G3UWE7|||http://purl.uniprot.org/uniprot/O88335 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Site|||Topological Domain|||Transmembrane ^@ ATP-sensitive inward rectifier potassium channel 1|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||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_0000154918 http://togogenome.org/gene/10090:Zfand5 ^@ http://purl.uniprot.org/uniprot/O88878 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Strand|||Turn|||Zinc Finger ^@ A20-type|||AN1-type|||AN1-type zinc finger protein 5|||Disordered|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000066558 http://togogenome.org/gene/10090:Rab36 ^@ http://purl.uniprot.org/uniprot/Q8CAM5 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Motif ^@ Effector region|||Ras-related protein Rab-36|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000315237 http://togogenome.org/gene/10090:Garin5a ^@ http://purl.uniprot.org/uniprot/A0A0U1RNU0|||http://purl.uniprot.org/uniprot/A1L3C1 ^@ 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 ^@ Acidic residues|||Disordered|||Golgi associated RAB2 interactor protein-like Rab2B-binding|||Golgi-associated RAB2 interactor protein 5A|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000334698|||http://purl.uniprot.org/annotation/VSP_033761 http://togogenome.org/gene/10090:Rps28 ^@ http://purl.uniprot.org/uniprot/P62858 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ N-acetylmethionine|||Phosphoserine|||Small ribosomal subunit protein eS28 ^@ http://purl.uniprot.org/annotation/PRO_0000136823 http://togogenome.org/gene/10090:Spon1 ^@ http://purl.uniprot.org/uniprot/Q8VCC9 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||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_0000035866 http://togogenome.org/gene/10090:Ntrk1 ^@ http://purl.uniprot.org/uniprot/Q3UFB7 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||High affinity nerve growth factor receptor|||Ig-like C2-type 1|||Ig-like C2-type 2|||Interaction with PLCG1|||Interaction with SHC1|||Interaction with SQSTM1|||LRR 1|||LRR 2|||LRRCT|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000278537 http://togogenome.org/gene/10090:Slc39a9 ^@ http://purl.uniprot.org/uniprot/Q8BFU1 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Zinc transporter ZIP9 ^@ http://purl.uniprot.org/annotation/PRO_0000297599 http://togogenome.org/gene/10090:Dnai7 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0S9|||http://purl.uniprot.org/uniprot/Q6TDU8 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant ^@ Disordered|||Dynein axonemal intermediate chain 7|||IC97/Casc1 N-terminal|||In isoform 2.|||In isoform 3.|||In strain: C57BL/6J; could be associated with tumor susceptibility; does not affect binding with tubulin; more unstable. ^@ http://purl.uniprot.org/annotation/PRO_0000332733|||http://purl.uniprot.org/annotation/VSP_033384|||http://purl.uniprot.org/annotation/VSP_033385|||http://purl.uniprot.org/annotation/VSP_033386|||http://purl.uniprot.org/annotation/VSP_033387|||http://purl.uniprot.org/annotation/VSP_033388 http://togogenome.org/gene/10090:Szt2 ^@ http://purl.uniprot.org/uniprot/A2A9C3 ^@ 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.|||KICSTOR complex protein SZT2|||Mediates interaction with the GATOR1 complex|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000399821|||http://purl.uniprot.org/annotation/VSP_039917 http://togogenome.org/gene/10090:Trim15 ^@ http://purl.uniprot.org/uniprot/G3UY57|||http://purl.uniprot.org/uniprot/Q8R096 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ B box-type|||RING-type ^@ http://togogenome.org/gene/10090:Cdkn1c ^@ http://purl.uniprot.org/uniprot/P49919|||http://purl.uniprot.org/uniprot/Q791X1 ^@ 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 ^@ Acidic residues|||Cyclin-dependent kinase inhibitor|||Cyclin-dependent kinase inhibitor 1C|||Disordered|||In isoform KIP2b.|||Nuclear localization signal|||Omega-N-methylarginine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000190088|||http://purl.uniprot.org/annotation/VSP_000868 http://togogenome.org/gene/10090:Sarm1 ^@ http://purl.uniprot.org/uniprot/Q6PDS3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||NAD(+) hydrolase SARM1|||Phosphoserine|||SAM 1|||SAM 2|||TIR ^@ http://purl.uniprot.org/annotation/PRO_0000097590|||http://purl.uniprot.org/annotation/VSP_013604|||http://purl.uniprot.org/annotation/VSP_013605|||http://purl.uniprot.org/annotation/VSP_013606|||http://purl.uniprot.org/annotation/VSP_013607 http://togogenome.org/gene/10090:Copb2 ^@ http://purl.uniprot.org/uniprot/O55029 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Coatomer subunit beta'|||Disordered|||N6-acetyllysine|||No effect on protein abundance. Mice homozygous for that mutation do not display any developmental abnormality.|||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_0000050913 http://togogenome.org/gene/10090:Pdzk1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1V0|||http://purl.uniprot.org/uniprot/Q9JIL4 ^@ 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|||Disordered|||Disrupts interaction of the first PDZ domain with SCARB1. Abolishes interaction with SCARB1; when associated with A-253.|||Disrupts interaction of the third PDZ domain with SCARB1. Abolishes interaction with SCARB1; when associated with A-20.|||Impairs interaction of the first PDZ domain with SCARB1.|||Na(+)/H(+) exchange regulatory cofactor NHE-RF3|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000058288 http://togogenome.org/gene/10090:Mtmr10 ^@ http://purl.uniprot.org/uniprot/Q7TPM9 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Myotubularin phosphatase|||Myotubularin-related protein 10|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000284361 http://togogenome.org/gene/10090:Igbp1 ^@ http://purl.uniprot.org/uniprot/Q61249 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Site|||Strand|||Turn ^@ Basic and acidic residues|||Cleavage; by calpain|||Disordered|||Immunoglobulin-binding protein 1|||Interaction with MID1|||Interaction with PPP2CA|||N6-acetyllysine|||UIM ^@ http://purl.uniprot.org/annotation/PRO_0000218619 http://togogenome.org/gene/10090:Ctsm ^@ http://purl.uniprot.org/uniprot/A0A0R4J182|||http://purl.uniprot.org/uniprot/Q9JL96 ^@ 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|||Cathepsin M|||Cathepsin propeptide inhibitor|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000026281|||http://purl.uniprot.org/annotation/PRO_0000026282|||http://purl.uniprot.org/annotation/PRO_5015044299 http://togogenome.org/gene/10090:Pfdn2 ^@ http://purl.uniprot.org/uniprot/O70591 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Prefoldin subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000124836 http://togogenome.org/gene/10090:Lmo3 ^@ http://purl.uniprot.org/uniprot/Q8BZL8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ LIM domain only protein 3|||LIM zinc-binding 1|||LIM zinc-binding 2 ^@ http://purl.uniprot.org/annotation/PRO_0000075818 http://togogenome.org/gene/10090:Or2ag15 ^@ http://purl.uniprot.org/uniprot/Q8VFM4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:C1s2 ^@ http://purl.uniprot.org/uniprot/A0A1W2P7F1|||http://purl.uniprot.org/uniprot/Q8CFG8 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide ^@ (3R)-3-hydroxyasparagine|||CUB|||CUB 1|||CUB 2|||Charge relay system|||Complement C1s-1 subcomponent|||Complement C1s-B subcomponent heavy chain|||Complement C1s-B subcomponent light chain|||EGF-like; calcium-binding|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi|||Sushi 1|||Sushi 2 ^@ http://purl.uniprot.org/annotation/PRO_0000042196|||http://purl.uniprot.org/annotation/PRO_0000042197|||http://purl.uniprot.org/annotation/PRO_0000042198|||http://purl.uniprot.org/annotation/PRO_5015071725 http://togogenome.org/gene/10090:Akr1c20 ^@ http://purl.uniprot.org/uniprot/Q8VC77|||http://purl.uniprot.org/uniprot/Q9CZU0 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Site ^@ Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor ^@ http://togogenome.org/gene/10090:Cfl2 ^@ http://purl.uniprot.org/uniprot/P45591|||http://purl.uniprot.org/uniprot/Q3UHW9 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif ^@ ADF-H|||Cofilin-2|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000214908 http://togogenome.org/gene/10090:Atp6ap1 ^@ http://purl.uniprot.org/uniprot/Q3TWN7|||http://purl.uniprot.org/uniprot/Q3UWN7|||http://purl.uniprot.org/uniprot/Q9R1Q9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cleavage; by furin|||Cytoplasmic|||Helical|||Impairs propeptide cleavage.|||Lumenal|||N-linked (GlcNAc...) asparagine|||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_0000002544|||http://purl.uniprot.org/annotation/PRO_0000454042|||http://purl.uniprot.org/annotation/PRO_5014309151 http://togogenome.org/gene/10090:Psap ^@ http://purl.uniprot.org/uniprot/B2RUD7|||http://purl.uniprot.org/uniprot/E9PZ00|||http://purl.uniprot.org/uniprot/Q3TWM9|||http://purl.uniprot.org/uniprot/Q3TXJ0|||http://purl.uniprot.org/uniprot/Q3UAS4|||http://purl.uniprot.org/uniprot/Q3UE29|||http://purl.uniprot.org/uniprot/Q3UFE8|||http://purl.uniprot.org/uniprot/Q61207|||http://purl.uniprot.org/uniprot/Q8BFQ1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Turn ^@ Affects the intracellular trafficking, resulting in endoplasmic reticulum retention. Mice carrying homozygous and heterozygous C509S exhibit a progressive decline in locomotor function and a reduction in the number of tyrosine hydroxylase-positive neurons.|||N-linked (GlcNAc...) asparagine|||Prosaposin|||Saposin A-type|||Saposin A-type 1|||Saposin A-type 2|||Saposin B-type|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000031626|||http://purl.uniprot.org/annotation/PRO_0000434953|||http://purl.uniprot.org/annotation/PRO_0000434954|||http://purl.uniprot.org/annotation/PRO_0000434955|||http://purl.uniprot.org/annotation/PRO_0000434956|||http://purl.uniprot.org/annotation/PRO_0000434957|||http://purl.uniprot.org/annotation/PRO_0000434958|||http://purl.uniprot.org/annotation/PRO_0000434959|||http://purl.uniprot.org/annotation/PRO_0000434960|||http://purl.uniprot.org/annotation/PRO_0000434961|||http://purl.uniprot.org/annotation/PRO_0000434962|||http://purl.uniprot.org/annotation/PRO_5010843349|||http://purl.uniprot.org/annotation/PRO_5010843390|||http://purl.uniprot.org/annotation/PRO_5010843411|||http://purl.uniprot.org/annotation/PRO_5015099031|||http://purl.uniprot.org/annotation/PRO_5019622159 http://togogenome.org/gene/10090:Vcpip1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0M9|||http://purl.uniprot.org/uniprot/Q8CDG3 ^@ 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 ^@ Deubiquitinating protein VCPIP1|||Disordered|||In isoform 2.|||N6-acetyllysine|||Nucleophile|||OTU|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000065770|||http://purl.uniprot.org/annotation/VSP_009376|||http://purl.uniprot.org/annotation/VSP_009377 http://togogenome.org/gene/10090:Txndc8 ^@ http://purl.uniprot.org/uniprot/Q14AP0|||http://purl.uniprot.org/uniprot/Q69AB2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Redox-active|||Thioredoxin|||Thioredoxin domain-containing protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000120163|||http://purl.uniprot.org/annotation/VSP_014334 http://togogenome.org/gene/10090:Mrgpra9 ^@ http://purl.uniprot.org/uniprot/A0A140T8U8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hsd3b4 ^@ http://purl.uniprot.org/uniprot/Q3UIU9|||http://purl.uniprot.org/uniprot/Q61767 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transmembrane ^@ 3-beta hydroxysteroid dehydrogenase/isomerase|||Helical|||N6-acetyllysine|||NADPH-dependent 3-keto-steroid reductase Hsd3b4|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000087783 http://togogenome.org/gene/10090:Parvb ^@ http://purl.uniprot.org/uniprot/Q3UGT9|||http://purl.uniprot.org/uniprot/Q9ES46 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Beta-parvin|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000121584 http://togogenome.org/gene/10090:Ecm1 ^@ http://purl.uniprot.org/uniprot/F8WI14|||http://purl.uniprot.org/uniprot/Q61508 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 1|||2|||2 X approximate repeats|||Disordered|||Extracellular matrix protein 1|||In isoform Short.|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000021147|||http://purl.uniprot.org/annotation/PRO_5003385608|||http://purl.uniprot.org/annotation/VSP_004230 http://togogenome.org/gene/10090:Bcap31 ^@ http://purl.uniprot.org/uniprot/Q61335 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Motif|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ B-cell receptor-associated protein 31|||Cleavage; by caspase-8|||Cytoplasmic|||Di-lysine motif|||Helical|||Lumenal|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000142892 http://togogenome.org/gene/10090:Tfpi2 ^@ http://purl.uniprot.org/uniprot/O35536|||http://purl.uniprot.org/uniprot/Q3V1S9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Site ^@ BPTI/Kunitz inhibitor|||BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||BPTI/Kunitz inhibitor 3|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Tissue factor pathway inhibitor|||Tissue factor pathway inhibitor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000016877|||http://purl.uniprot.org/annotation/PRO_5014212504 http://togogenome.org/gene/10090:Ccl21b ^@ http://purl.uniprot.org/uniprot/P86792|||http://purl.uniprot.org/uniprot/P86793 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Region|||Sequence Conflict|||Signal Peptide ^@ C-C motif chemokine 21b|||C-C motif chemokine 21c|||C-terminal basic extension|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000005222|||http://purl.uniprot.org/annotation/PRO_0000403422 http://togogenome.org/gene/10090:Gpr139 ^@ http://purl.uniprot.org/uniprot/A0A142CHG4|||http://purl.uniprot.org/uniprot/Q80UC8 ^@ 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 139 ^@ http://purl.uniprot.org/annotation/PRO_0000069616 http://togogenome.org/gene/10090:Krit1 ^@ http://purl.uniprot.org/uniprot/B2RUA8|||http://purl.uniprot.org/uniprot/Q6S5J6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||FERM|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ITGB1BP1|||Interaction with RAP1B|||Krev interaction trapped protein 1|||N-terminal domain similar to Nudix hydrolase domain ^@ http://purl.uniprot.org/annotation/PRO_0000067024|||http://purl.uniprot.org/annotation/VSP_015801|||http://purl.uniprot.org/annotation/VSP_015802|||http://purl.uniprot.org/annotation/VSP_015803 http://togogenome.org/gene/10090:Scimp ^@ http://purl.uniprot.org/uniprot/Q3UU41 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane ^@ Chain|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Transmembrane ^@ Disordered|||Helical|||Inhibits interaction with BLNK. No effect on interactions with TLR4, GRB2 and CSK.|||Inhibits interaction with BLNK. Slightly inhibits interaction with GRB2. No effect on interactions with TLR4 and CSK.|||Inhibits interaction with TLR4. Decreases IL12B expression after TLR4 activation by lipopolysaccharide. Inhibits interaction with CSK. No effect on interactions with LYN, GRB2, and BLNK.|||Inhibits interaction with TLR4. Inhibits IL12B expression after TLR4 activation by lipopolysaccharide. No effect on interaction with LYN.|||Interaction with TLR4|||No effect on interaction with TLR4.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by LYN|||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_0000295238 http://togogenome.org/gene/10090:Gins2 ^@ http://purl.uniprot.org/uniprot/Q9D600 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Crosslink|||Modified Residue|||Sequence Conflict ^@ DNA replication complex GINS protein PSF2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000194814 http://togogenome.org/gene/10090:Spcs2 ^@ http://purl.uniprot.org/uniprot/Q9CYN2 ^@ 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_0000221160 http://togogenome.org/gene/10090:Inafm2 ^@ http://purl.uniprot.org/uniprot/A0A1L1STD6 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Pik3c2a ^@ http://purl.uniprot.org/uniprot/F8VPL2|||http://purl.uniprot.org/uniprot/Q61194 ^@ 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 ^@ Activation loop|||C2|||C2 PI3K-type|||Catalytic loop|||Disordered|||G-loop|||In isoform 2.|||Interaction with PtdIns(4,5)P2-containing membranes|||Interaction with clathrin; sufficient to induce clathrin assembly|||N-acetylalanine|||Nuclear localization signal|||PI3K-RBD|||PI3K/PI4K catalytic|||PIK helical|||PX|||Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000088796|||http://purl.uniprot.org/annotation/VSP_015254 http://togogenome.org/gene/10090:Tvp23b ^@ http://purl.uniprot.org/uniprot/Q9D8T4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Golgi apparatus membrane protein TVP23 homolog B|||Helical|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000212829 http://togogenome.org/gene/10090:Serpina1a ^@ http://purl.uniprot.org/uniprot/A0A0A0MQA3|||http://purl.uniprot.org/uniprot/P07758 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Alpha-1-antitrypsin 1-1|||N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_0000032388 http://togogenome.org/gene/10090:Adam39 ^@ http://purl.uniprot.org/uniprot/Q7M762 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disintegrin|||Disordered|||EGF-like|||Helical|||Peptidase M12B ^@ http://togogenome.org/gene/10090:Tnfaip8l1 ^@ http://purl.uniprot.org/uniprot/Q8K288 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Tumor necrosis factor alpha-induced protein 8-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000285725 http://togogenome.org/gene/10090:Eqtn ^@ http://purl.uniprot.org/uniprot/Q9D9V2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not affect MN9 antibody detectability.|||Equatorin|||Helical|||In isoform 2.|||Lumenal|||MN9 antibody detectability is lost.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000286594|||http://purl.uniprot.org/annotation/VSP_025111 http://togogenome.org/gene/10090:Gm572 ^@ http://purl.uniprot.org/uniprot/B1ARY8 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5002761464 http://togogenome.org/gene/10090:Dctn3 ^@ http://purl.uniprot.org/uniprot/Q9Z0Y1 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Dynactin subunit 3|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000225604 http://togogenome.org/gene/10090:Or12j2 ^@ http://purl.uniprot.org/uniprot/Q7TRT9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pcdhgb6 ^@ http://purl.uniprot.org/uniprot/Q91XX4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099536 http://togogenome.org/gene/10090:Plekha7 ^@ http://purl.uniprot.org/uniprot/Q3UIL6 ^@ 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, isoform 4 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with CTNND1|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology domain-containing family A member 7|||Polar residues|||Pro residues|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000287693|||http://purl.uniprot.org/annotation/VSP_025593|||http://purl.uniprot.org/annotation/VSP_025595|||http://purl.uniprot.org/annotation/VSP_025596|||http://purl.uniprot.org/annotation/VSP_039544|||http://purl.uniprot.org/annotation/VSP_044626|||http://purl.uniprot.org/annotation/VSP_044627 http://togogenome.org/gene/10090:Nanos2 ^@ http://purl.uniprot.org/uniprot/I6ZHM2|||http://purl.uniprot.org/uniprot/P60322 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2HC 1|||C2HC 2|||Disordered|||Nanos homolog 2|||Nanos-type ^@ http://purl.uniprot.org/annotation/PRO_0000207688 http://togogenome.org/gene/10090:Tmem33 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Z3|||http://purl.uniprot.org/uniprot/Q9CR67|||http://purl.uniprot.org/uniprot/Q9CZM3 ^@ 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_0000220900 http://togogenome.org/gene/10090:Fnbp4 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZZ6|||http://purl.uniprot.org/uniprot/Q6ZQ03 ^@ 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 ^@ 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.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||WW|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000289864|||http://purl.uniprot.org/annotation/VSP_026025|||http://purl.uniprot.org/annotation/VSP_026026|||http://purl.uniprot.org/annotation/VSP_029267|||http://purl.uniprot.org/annotation/VSP_029268 http://togogenome.org/gene/10090:Ctdspl ^@ http://purl.uniprot.org/uniprot/G3UXN0|||http://purl.uniprot.org/uniprot/P58465 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Site ^@ 4-aspartylphosphate intermediate|||CTD small phosphatase-like protein|||Disordered|||FCP1 homology|||Proton donor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000212570 http://togogenome.org/gene/10090:Or51i2 ^@ http://purl.uniprot.org/uniprot/Q8VGX6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dsg2 ^@ http://purl.uniprot.org/uniprot/O55111 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||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 repeat 6|||Desmoglein-2|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000003847|||http://purl.uniprot.org/annotation/PRO_0000003848 http://togogenome.org/gene/10090:Dmrta1 ^@ http://purl.uniprot.org/uniprot/Q8CFG4 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||DM|||DMA|||Disordered|||Doublesex- and mab-3-related transcription factor A1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000242701 http://togogenome.org/gene/10090:Bltp3a ^@ http://purl.uniprot.org/uniprot/B2KF50 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Chorein N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Lrch4 ^@ http://purl.uniprot.org/uniprot/Q921G6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Helical|||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 4|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000084481|||http://purl.uniprot.org/annotation/VSP_061971|||http://purl.uniprot.org/annotation/VSP_061972 http://togogenome.org/gene/10090:Ckap5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0K2|||http://purl.uniprot.org/uniprot/A2AGT5|||http://purl.uniprot.org/uniprot/K3W4R5 ^@ 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|||Cytoskeleton-associated protein 5|||Disordered|||HEAT|||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|||TOG 1|||TOG 2|||TOG 3|||TOG 4|||TOG 5 ^@ http://purl.uniprot.org/annotation/PRO_0000364005|||http://purl.uniprot.org/annotation/VSP_053003|||http://purl.uniprot.org/annotation/VSP_053004 http://togogenome.org/gene/10090:Uspl1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1P9|||http://purl.uniprot.org/uniprot/D3YW34|||http://purl.uniprot.org/uniprot/E9QLC6|||http://purl.uniprot.org/uniprot/Q3ULM6 ^@ 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 ^@ Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||SUMO-binding|||SUMO-specific isopeptidase USPL1|||USP ^@ http://purl.uniprot.org/annotation/PRO_0000279527|||http://purl.uniprot.org/annotation/VSP_023480|||http://purl.uniprot.org/annotation/VSP_023481|||http://purl.uniprot.org/annotation/VSP_023482 http://togogenome.org/gene/10090:9130008F23Rik ^@ http://purl.uniprot.org/uniprot/Q9D2Z6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Epn3 ^@ http://purl.uniprot.org/uniprot/Q91W69 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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|||Phosphoserine|||Polar residues|||UIM 1|||UIM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000074520 http://togogenome.org/gene/10090:Kpna2 ^@ http://purl.uniprot.org/uniprot/P52293|||http://purl.uniprot.org/uniprot/Q52L97 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ ARM|||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-1|||N-acetylserine|||NLS binding site (major)|||NLS binding site (minor)|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000120723 http://togogenome.org/gene/10090:C1rb ^@ http://purl.uniprot.org/uniprot/Q8CFG9 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide ^@ (3R)-3-hydroxyasparagine|||CUB 1|||CUB 2|||Charge relay system|||Complement C1r-B subcomponent|||Complement C1r-B subcomponent heavy chain|||Complement C1r-B subcomponent light chain|||EGF-like; calcium-binding|||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_0000042187|||http://purl.uniprot.org/annotation/PRO_0000042188|||http://purl.uniprot.org/annotation/PRO_0000042189 http://togogenome.org/gene/10090:Mrps11 ^@ http://purl.uniprot.org/uniprot/Q3U8Y1 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Lama1 ^@ http://purl.uniprot.org/uniprot/P19137 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ 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|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000017055 http://togogenome.org/gene/10090:Traf7 ^@ http://purl.uniprot.org/uniprot/F8WJF7|||http://purl.uniprot.org/uniprot/Q8C2K8 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Zinc Finger ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Zinc Finger ^@ Disordered|||Polar residues|||RING-type|||TRAF-type|||WD ^@ http://togogenome.org/gene/10090:Zfp36l3 ^@ http://purl.uniprot.org/uniprot/Q5ISE2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Transmembrane|||Zinc Finger ^@ Basic and acidic residues|||C3H1-type 1|||C3H1-type 2|||Disordered|||Helical|||Necessary for cytoplasmic localization|||Polar residues|||Reduces ARE-containing RNA-binding. Loss of ARE-containing RNA-binding; when associated with A-153.|||Reduces ARE-containing RNA-binding. Loss of ARE-containing RNA-binding; when associated with A-157.|||mRNA decay activator protein ZFP36L3 ^@ http://purl.uniprot.org/annotation/PRO_0000423554 http://togogenome.org/gene/10090:Ear1 ^@ http://purl.uniprot.org/uniprot/P97426|||http://purl.uniprot.org/uniprot/Q53ZF0 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Eosinophil cationic protein 1|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Proton donor|||Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_0000030867|||http://purl.uniprot.org/annotation/PRO_5014205861 http://togogenome.org/gene/10090:Stk40 ^@ http://purl.uniprot.org/uniprot/Q7TNL3 ^@ 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.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 40 ^@ http://purl.uniprot.org/annotation/PRO_0000252262|||http://purl.uniprot.org/annotation/VSP_020901 http://togogenome.org/gene/10090:Apoc2 ^@ http://purl.uniprot.org/uniprot/Q05020|||http://purl.uniprot.org/uniprot/Q3UJG0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Region|||Sequence Conflict|||Signal Peptide ^@ Apolipoprotein C-II|||Lipid binding|||Lipoprotein lipase cofactor ^@ http://purl.uniprot.org/annotation/PRO_0000002026|||http://purl.uniprot.org/annotation/PRO_5014309204 http://togogenome.org/gene/10090:Reg3g ^@ http://purl.uniprot.org/uniprot/O09049|||http://purl.uniprot.org/uniprot/Q545I1 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Motif|||Propeptide|||Region|||Signal Peptide ^@ C-type lectin|||C-type lectin domain-containing protein|||EPN|||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_0000017435|||http://purl.uniprot.org/annotation/PRO_0000422753|||http://purl.uniprot.org/annotation/PRO_0000422754|||http://purl.uniprot.org/annotation/PRO_5014309578 http://togogenome.org/gene/10090:Pcbp4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J044|||http://purl.uniprot.org/uniprot/P57724|||http://purl.uniprot.org/uniprot/Q8BP63|||http://purl.uniprot.org/uniprot/Q9DB01 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ K Homology|||KH 1|||KH 2|||KH 3|||Poly(rC)-binding protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000050095 http://togogenome.org/gene/10090:Csnk1g3 ^@ http://purl.uniprot.org/uniprot/A0A494BAP2|||http://purl.uniprot.org/uniprot/Q8C4X2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Casein kinase I isoform gamma-3|||Disordered|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000305924 http://togogenome.org/gene/10090:Ints4 ^@ http://purl.uniprot.org/uniprot/Q8CIM8 ^@ 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 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_0000259539|||http://purl.uniprot.org/annotation/VSP_021454|||http://purl.uniprot.org/annotation/VSP_021455|||http://purl.uniprot.org/annotation/VSP_021456 http://togogenome.org/gene/10090:Fam3a ^@ http://purl.uniprot.org/uniprot/A0A158SIT7|||http://purl.uniprot.org/uniprot/Q9D8T0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Strand|||Transmembrane|||Turn ^@ GG-type lectin|||Helical|||ILEI/PANDER|||Protein FAM3A ^@ http://purl.uniprot.org/annotation/PRO_0000008749 http://togogenome.org/gene/10090:Ace2 ^@ http://purl.uniprot.org/uniprot/Q3URC9|||http://purl.uniprot.org/uniprot/Q8R0I0 ^@ 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|||Region|||Secondary Structure|||Sequence Conflict|||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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Angiotensin-converting enzyme|||Angiotensin-converting enzyme 2|||Collectrin|||Collectrin-like|||Cytoplasmic|||Disordered|||Endocytic sorting signal|||Essential for cleavage by ADAM17|||Essential for cleavage by TMPRSS11D and TMPRSS2|||Extracellular|||Helical|||In isoform 2.|||LIR|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||PTB|||Peptidase M2|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Processed angiotensin-converting enzyme 2|||Proton acceptor|||Proton donor|||SH2-binding ^@ http://purl.uniprot.org/annotation/PRO_0000028571|||http://purl.uniprot.org/annotation/PRO_0000292269|||http://purl.uniprot.org/annotation/PRO_5014309218|||http://purl.uniprot.org/annotation/VSP_014903 http://togogenome.org/gene/10090:Slc6a9 ^@ http://purl.uniprot.org/uniprot/P28571 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Essential for interaction with EXOC1|||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 GlyT-1A.|||In isoform GlyT-1B.|||Phosphoserine|||Phosphothreonine|||Sodium- and chloride-dependent glycine transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000214781|||http://purl.uniprot.org/annotation/VSP_006272|||http://purl.uniprot.org/annotation/VSP_039241 http://togogenome.org/gene/10090:Hgfac ^@ http://purl.uniprot.org/uniprot/Q545J3|||http://purl.uniprot.org/uniprot/Q9R098 ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||Fibronectin type-I|||Fibronectin type-II|||Hepatocyte growth factor activator|||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|||Polar residues|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000027914|||http://purl.uniprot.org/annotation/PRO_0000027915|||http://purl.uniprot.org/annotation/PRO_0000027916|||http://purl.uniprot.org/annotation/PRO_5010844034 http://togogenome.org/gene/10090:Neb ^@ http://purl.uniprot.org/uniprot/A0A571BF58|||http://purl.uniprot.org/uniprot/E9Q1W3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||SH3 ^@ http://togogenome.org/gene/10090:Pgbd5 ^@ http://purl.uniprot.org/uniprot/A0A510C1L5|||http://purl.uniprot.org/uniprot/D3YZI9 ^@ 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.|||Phosphoserine|||PiggyBac transposable element-derived protein|||PiggyBac transposable element-derived protein 5|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000441912|||http://purl.uniprot.org/annotation/VSP_059132 http://togogenome.org/gene/10090:Calcb ^@ http://purl.uniprot.org/uniprot/Q3UW96 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Calcitonin peptide-like ^@ http://purl.uniprot.org/annotation/PRO_5015097507 http://togogenome.org/gene/10090:Dytn ^@ http://purl.uniprot.org/uniprot/A2CI98 ^@ Binding Site|||Chain|||Coiled-Coil|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Zinc Finger ^@ Dystrotelin|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000298935 http://togogenome.org/gene/10090:Pde4dip ^@ http://purl.uniprot.org/uniprot/E9Q1A0|||http://purl.uniprot.org/uniprot/G3X9L9|||http://purl.uniprot.org/uniprot/Q80YT7 ^@ 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.|||Myomegalin|||Olduvai|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000307691|||http://purl.uniprot.org/annotation/VSP_028784|||http://purl.uniprot.org/annotation/VSP_028785|||http://purl.uniprot.org/annotation/VSP_028786 http://togogenome.org/gene/10090:Dnaaf2 ^@ http://purl.uniprot.org/uniprot/Q8BPI1 ^@ 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.|||Phosphoserine|||Protein kintoun ^@ http://purl.uniprot.org/annotation/PRO_0000089912|||http://purl.uniprot.org/annotation/VSP_036538 http://togogenome.org/gene/10090:Gm13279 ^@ http://purl.uniprot.org/uniprot/Q8CD73 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099103 http://togogenome.org/gene/10090:Snrpe ^@ http://purl.uniprot.org/uniprot/P62305 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Sm|||Small nuclear ribonucleoprotein E ^@ http://purl.uniprot.org/annotation/PRO_0000125530 http://togogenome.org/gene/10090:Cops9 ^@ http://purl.uniprot.org/uniprot/Q3U898 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ COP9 signalosome complex subunit 9|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000332925 http://togogenome.org/gene/10090:Ndc1 ^@ http://purl.uniprot.org/uniprot/Q8VCB1 ^@ 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|||Helical; Name=5|||Helical; Name=6|||Nucleoporin NDC1|||Perinuclear space|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000235241 http://togogenome.org/gene/10090:Or13p5 ^@ http://purl.uniprot.org/uniprot/Q8VGB1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sprr2d ^@ http://purl.uniprot.org/uniprot/O70555 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1|||2|||3|||4|||4 X 9 AA approximate tandem repeats|||Disordered|||Small proline-rich protein 2D ^@ http://purl.uniprot.org/annotation/PRO_0000150016 http://togogenome.org/gene/10090:Unc80 ^@ http://purl.uniprot.org/uniprot/Q8BLN6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Basic and acidic residues|||Decreases interaction with UNC79.|||Disordered|||Does not affect interaction with NALCN. Does not affect interaction with UNC79. Affects NALCN channel activation.|||Helical|||In isoform 2.|||Leads to neonatal lethality in homozygote mice. Abolishes association of UNC79 with the NALCN complex. Affects subcellular location, retained in soma and absence in axons and dendrites.|||Partially restored current Na(+) leak current when expressed in UNC80 knockout neurons.|||Phosphoserine|||Polar residues|||Protein unc-80 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089349|||http://purl.uniprot.org/annotation/VSP_015007|||http://purl.uniprot.org/annotation/VSP_015008 http://togogenome.org/gene/10090:Bcl2a1d ^@ http://purl.uniprot.org/uniprot/O55179 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Bcl-2 Bcl-2 homology region 1-3 ^@ http://togogenome.org/gene/10090:1700021F07Rik ^@ http://purl.uniprot.org/uniprot/Q9DA42 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Ciliary microtubule inner protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000079449 http://togogenome.org/gene/10090:Stx17 ^@ http://purl.uniprot.org/uniprot/Q9D0I4 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endoplasmic reticulum retention signal|||Helical|||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_0000210229 http://togogenome.org/gene/10090:Spag7 ^@ http://purl.uniprot.org/uniprot/Q7TNE3 ^@ 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|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||R3H|||Removed|||Sperm-associated antigen 7 ^@ http://purl.uniprot.org/annotation/PRO_0000072098 http://togogenome.org/gene/10090:Cdh3 ^@ http://purl.uniprot.org/uniprot/P10287|||http://purl.uniprot.org/uniprot/Q8BRE1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin domain-containing protein|||Cadherin-3|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000003747|||http://purl.uniprot.org/annotation/PRO_0000003748|||http://purl.uniprot.org/annotation/PRO_5010846908 http://togogenome.org/gene/10090:Morn1 ^@ http://purl.uniprot.org/uniprot/A2RTS7 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Gmps ^@ http://purl.uniprot.org/uniprot/B2RRH9|||http://purl.uniprot.org/uniprot/Q3THK7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ For GATase activity|||GMP synthase [glutamine-hydrolyzing]|||GMPS ATP-PPase|||Glutamine amidotransferase type-1|||N-acetylalanine|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000284365 http://togogenome.org/gene/10090:Dab1 ^@ http://purl.uniprot.org/uniprot/B2RRQ8|||http://purl.uniprot.org/uniprot/P97318 ^@ 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 binding to PtdIns(4,5)P2.|||Abolishes interaction with APLP1.|||Basic and acidic residues|||Disabled homolog 1|||Disordered|||Greatly impairs interaction with APLP1.|||Impairs binding to PtdIns(4,5)P2.|||In isoform DAB197 and isoform DAB217.|||In isoform DAB197.|||In isoform DAB204.|||In isoform DAB271.|||In isoform DAB553.|||In isoform DAB555 and isoform DAB271.|||PID|||Phosphoserine; by CDK5|||Phosphotyrosine|||Polar residues|||Reduces phosphorylation by SRC or downstream kinase; when associated with F-185 and F-198. Abolishes phosphorylation by SRC or downstream kinase; when associated with F-185; F-198; F-220 and F-232.|||Reduces phosphorylation by SRC or downstream kinase; when associated with F-185 and F-200. Abolishes phosphorylation by SRC or downstream kinase; when associated with F-185; F-200; F-220 and F-232.|||Reduces phosphorylation by SRC or downstream kinase; when associated with F-198 and F-200. Abolishes phosphorylation by SRC or downstream kinase; when associated with F-198; F-200; F-220 and F-232.|||Reduces phosphorylation by SRC or downstream kinase; when associated with F-220. Abolishes phosphorylation by SRC or downstream kinase; when associated with F-185; F-198; F-200 and F-220. Abolishes interaction with CRKLSH2 domain; when associated with F-220.|||Reduces phosphorylation by SRC or downstream kinase; when associated with F-232. Abolishes phosphorylation by SRC or downstream kinase; when associated with F-185; F-198; F-200 and F-232. Abolishes interaction with CRKLSH2 domain; when associated with F-232. ^@ http://purl.uniprot.org/annotation/PRO_0000079769|||http://purl.uniprot.org/annotation/VSP_003841|||http://purl.uniprot.org/annotation/VSP_003842|||http://purl.uniprot.org/annotation/VSP_003843|||http://purl.uniprot.org/annotation/VSP_003844|||http://purl.uniprot.org/annotation/VSP_003845|||http://purl.uniprot.org/annotation/VSP_026205|||http://purl.uniprot.org/annotation/VSP_026206|||http://purl.uniprot.org/annotation/VSP_026208|||http://purl.uniprot.org/annotation/VSP_026209 http://togogenome.org/gene/10090:Zc3h3 ^@ http://purl.uniprot.org/uniprot/Q3UUL4|||http://purl.uniprot.org/uniprot/Q8CHP0 ^@ 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 ^@ C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||C3H1-type 5|||Disordered|||Phosphoserine|||Polar residues|||Zinc finger CCCH domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000213897 http://togogenome.org/gene/10090:Gcm1 ^@ http://purl.uniprot.org/uniprot/P70348|||http://purl.uniprot.org/uniprot/Q3UQD1 ^@ Binding Site|||Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand ^@ Chorion-specific transcription factor GCMa|||GCM|||Loss of DNA binding.|||Loss of transcription activation.|||No effect on DNA binding.|||Slight decrease of DNA binding.|||Strong decrease of DNA binding. ^@ http://purl.uniprot.org/annotation/PRO_0000126648 http://togogenome.org/gene/10090:Cmss1 ^@ http://purl.uniprot.org/uniprot/Q3UW28|||http://purl.uniprot.org/uniprot/Q9CZT6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein CMSS1 ^@ http://purl.uniprot.org/annotation/PRO_0000239015 http://togogenome.org/gene/10090:Nr2f6 ^@ http://purl.uniprot.org/uniprot/P43136 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Important for dimerization|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 2 group F member 6|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000053614 http://togogenome.org/gene/10090:Fcho2 ^@ http://purl.uniprot.org/uniprot/Q3UQN2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ 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)|||Loss of function mutant which is unable to promote clathrin coated-pits formation. Binds to membrane but is unable to induce membrane tubulation. Induces the formation of large and static clathrin-coated pits.|||Loss of function mutant which is unable to promote clathrin coated-pits formation. Cytosolic mutant which is unable to bind and induce membrane tubulation; when associated with E-146.|||Loss of function mutant which is unable to promote clathrin coated-pits formation. Cytosolic mutant which is unable to bind and induce membrane tubulation; when associated with E-165.|||Loss of function mutant which is unable to promote clathrin coated-pits formation. Cytosolic mutant; when associated with E-38.|||Loss of function mutant which is unable to promote clathrin coated-pits formation. Cytosolic mutant; when associated with E-73.|||Loss of interaction with EPS15 and ITSN1.|||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_0000266006|||http://purl.uniprot.org/annotation/VSP_021912|||http://purl.uniprot.org/annotation/VSP_021913|||http://purl.uniprot.org/annotation/VSP_021914|||http://purl.uniprot.org/annotation/VSP_021915 http://togogenome.org/gene/10090:Iglon5 ^@ http://purl.uniprot.org/uniprot/Q8HW98 ^@ 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 ^@ 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_0000332302 http://togogenome.org/gene/10090:Mageh1 ^@ http://purl.uniprot.org/uniprot/Q3UKU3|||http://purl.uniprot.org/uniprot/Q9NWG9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||MAGE|||Melanoma-associated antigen H1|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000156736 http://togogenome.org/gene/10090:Tgfbrap1 ^@ http://purl.uniprot.org/uniprot/Q3UR70 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Splice Variant ^@ CHCR|||CNH|||In isoform 2.|||Transforming growth factor-beta receptor-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000345406|||http://purl.uniprot.org/annotation/VSP_034944|||http://purl.uniprot.org/annotation/VSP_034945 http://togogenome.org/gene/10090:Rdx ^@ http://purl.uniprot.org/uniprot/P26043|||http://purl.uniprot.org/uniprot/Q3TH46|||http://purl.uniprot.org/uniprot/Q7TSG6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||FERM|||N6-succinyllysine|||Phosphothreonine; by ROCK2|||Pro residues|||Radixin ^@ http://purl.uniprot.org/annotation/PRO_0000219422 http://togogenome.org/gene/10090:Pebp4 ^@ http://purl.uniprot.org/uniprot/Q9D9G2|||http://purl.uniprot.org/uniprot/Q9D9L9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Important for secretion|||N-linked (GlcNAc...) asparagine|||Phosphatidylethanolamine-binding protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000023280|||http://purl.uniprot.org/annotation/PRO_5014312721 http://togogenome.org/gene/10090:Aifm3 ^@ http://purl.uniprot.org/uniprot/Q3TY86 ^@ 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 ^@ Apoptosis-inducing factor 3|||Disordered|||In isoform 2.|||In isoform 3.|||Rieske ^@ http://purl.uniprot.org/annotation/PRO_0000255661|||http://purl.uniprot.org/annotation/VSP_021304|||http://purl.uniprot.org/annotation/VSP_021305|||http://purl.uniprot.org/annotation/VSP_021306 http://togogenome.org/gene/10090:Il18 ^@ http://purl.uniprot.org/uniprot/P70380 ^@ Chain|||Experimental Information|||Molecule Processing|||Propeptide|||Sequence Conflict ^@ Chain|||Propeptide|||Sequence Conflict ^@ Interleukin-18 ^@ http://purl.uniprot.org/annotation/PRO_0000015345|||http://purl.uniprot.org/annotation/PRO_0000015346 http://togogenome.org/gene/10090:Vmn1r8 ^@ http://purl.uniprot.org/uniprot/Q8R2C2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Faim ^@ http://purl.uniprot.org/uniprot/Q9WUD8 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ Fas apoptotic inhibitory molecule 1|||N-acetylthreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087174 http://togogenome.org/gene/10090:Or1o4 ^@ http://purl.uniprot.org/uniprot/Q8VFE4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gask1a ^@ http://purl.uniprot.org/uniprot/Q3UY90 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Cleavage|||Disordered|||Golgi-associated kinase 1A|||In isoform 2.|||In isoform 3.|||Polar residues|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000301949|||http://purl.uniprot.org/annotation/PRO_0000446053|||http://purl.uniprot.org/annotation/PRO_0000446054|||http://purl.uniprot.org/annotation/VSP_027885|||http://purl.uniprot.org/annotation/VSP_027886 http://togogenome.org/gene/10090:Pou5f2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J273|||http://purl.uniprot.org/uniprot/Q9DAC9 ^@ 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_0000100757 http://togogenome.org/gene/10090:Hemgn ^@ http://purl.uniprot.org/uniprot/Q9ERZ0 ^@ 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_0000245362 http://togogenome.org/gene/10090:Slc5a1 ^@ http://purl.uniprot.org/uniprot/Q8C3K6|||http://purl.uniprot.org/uniprot/Q8CCA7|||http://purl.uniprot.org/uniprot/Q9QXI6 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Implicated in sodium coupling|||Involved in sugar-binding/transport and inhibitor binding|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Sodium/glucose cotransporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000105367 http://togogenome.org/gene/10090:Pira12 ^@ http://purl.uniprot.org/uniprot/E9Q1Z6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5003245801 http://togogenome.org/gene/10090:Or5b106 ^@ http://purl.uniprot.org/uniprot/Q8VFV9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lgals9 ^@ http://purl.uniprot.org/uniprot/G3X9T7|||http://purl.uniprot.org/uniprot/O08573 ^@ 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|||Galectin|||Galectin 1|||Galectin 2|||Galectin-9|||In isoform 2 and isoform 3.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000076947|||http://purl.uniprot.org/annotation/VSP_003097|||http://purl.uniprot.org/annotation/VSP_057844 http://togogenome.org/gene/10090:Gm10058 ^@ http://purl.uniprot.org/uniprot/Q62478 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Or4f47 ^@ http://purl.uniprot.org/uniprot/Q8VF84 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Osbp ^@ http://purl.uniprot.org/uniprot/Q3B7Z2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||FFAT|||In isoform 2.|||N-acetylalanine|||Oxysterol-binding protein 1|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000349262|||http://purl.uniprot.org/annotation/VSP_035281|||http://purl.uniprot.org/annotation/VSP_035282 http://togogenome.org/gene/10090:Zfp780b ^@ http://purl.uniprot.org/uniprot/E9Q2S6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Dtd1 ^@ http://purl.uniprot.org/uniprot/Q9DD18 ^@ 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|||D-aminoacyl-tRNA deacylase 1|||Disordered|||Gly-cisPro motif, important for rejection of L-amino acids|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000164627|||http://purl.uniprot.org/annotation/VSP_026130 http://togogenome.org/gene/10090:Pym1 ^@ http://purl.uniprot.org/uniprot/Q8CHP5 ^@ 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.|||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_0000287286|||http://purl.uniprot.org/annotation/VSP_025431 http://togogenome.org/gene/10090:Kri1 ^@ http://purl.uniprot.org/uniprot/F6WIU1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Kri1-like C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Vmn1r253 ^@ http://purl.uniprot.org/uniprot/K9J7G6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnot2 ^@ http://purl.uniprot.org/uniprot/A0A1S6GWJ6|||http://purl.uniprot.org/uniprot/E9Q027|||http://purl.uniprot.org/uniprot/Q5CZY5|||http://purl.uniprot.org/uniprot/Q8C5L3 ^@ 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 ^@ CCR4-NOT transcription complex subunit 2|||Disordered|||In isoform 2.|||In isoform 3.|||NOT2/NOT3/NOT5 C-terminal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000198332|||http://purl.uniprot.org/annotation/VSP_009917|||http://purl.uniprot.org/annotation/VSP_009918 http://togogenome.org/gene/10090:Sgcd ^@ http://purl.uniprot.org/uniprot/P82347|||http://purl.uniprot.org/uniprot/Q544D4 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Delta-sarcoglycan|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000175247 http://togogenome.org/gene/10090:Trim56 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Q6|||http://purl.uniprot.org/uniprot/Q80VI1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ B box-type|||B box-type 1|||B box-type 2|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase TRIM56|||Phosphoserine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056289 http://togogenome.org/gene/10090:Slc25a36 ^@ http://purl.uniprot.org/uniprot/Q922G0 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Repeat|||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 36 ^@ http://purl.uniprot.org/annotation/PRO_0000291798 http://togogenome.org/gene/10090:Dcxr ^@ http://purl.uniprot.org/uniprot/Q91X52 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ L-xylulose reductase|||N-acetylmethionine|||Omega-N-methylarginine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054556 http://togogenome.org/gene/10090:Ap2a2 ^@ http://purl.uniprot.org/uniprot/P17427|||http://purl.uniprot.org/uniprot/Q69ZW4|||http://purl.uniprot.org/uniprot/Q6PEE6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ AP-2 complex subunit alpha-2|||Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding.|||Abolishes AMPH, BIN1, DGKD, EPS15, EPN1, auxilin and SNAP91 binding.|||Basic and acidic residues|||Clathrin adaptor alpha/beta/gamma-adaptin appendage Ig-like subdomain|||Disordered|||No effect on DENND1A-,DENND1B- nor DENND1C-binding.|||No effect.|||Reduces DENND1A- and DENND1C-binding.|||Reduces SNAP91, AMPH and BIN1 binding. Abolishes AMPH and SNAP91 binding; when associated with A-916. Abolishes EPN1 and EPS15 binding; when associated with A-905.|||Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15.|||Reduces phosphatidylinositol binding.|||Strongly reduces AMPH and SNAP91 binding. Abolishes DENND1B-binding; no effect on DENND1A-, nor DENND1C-binding. Abolishes AMPH and SNAP91 binding; when associated with A-837.|||Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding.|||Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837.|||Strongly reduces phosphatidylinositol binding.|||Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56.|||Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57.|||Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57. ^@ http://purl.uniprot.org/annotation/PRO_0000193733 http://togogenome.org/gene/10090:Kat14 ^@ http://purl.uniprot.org/uniprot/Q8CID0 ^@ 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|||Cysteine-rich protein 2-binding protein|||Disordered|||N-acetyltransferase|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000304937 http://togogenome.org/gene/10090:Fam177a ^@ http://purl.uniprot.org/uniprot/Q8BR63 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM177A1 ^@ http://purl.uniprot.org/annotation/PRO_0000089886 http://togogenome.org/gene/10090:Krt24 ^@ http://purl.uniprot.org/uniprot/A1L317 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type I cytoskeletal 24|||Linker 1|||Linker 12|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000314851 http://togogenome.org/gene/10090:Mup6 ^@ http://purl.uniprot.org/uniprot/A2AV72 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5015086027 http://togogenome.org/gene/10090:Gtf2f2 ^@ http://purl.uniprot.org/uniprot/Q3UMJ4|||http://purl.uniprot.org/uniprot/Q8R0A0 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ General transcription factor IIF subunit 2|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed|||TFIIF beta subunit HTH|||TFIIF beta subunit N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000211236 http://togogenome.org/gene/10090:Ska1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0M5|||http://purl.uniprot.org/uniprot/Q9CPV1 ^@ 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|||Microtubule binding|||Spindle and kinetochore-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000273156 http://togogenome.org/gene/10090:Dhcr7 ^@ http://purl.uniprot.org/uniprot/A0A140LIT2|||http://purl.uniprot.org/uniprot/O88455 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ 7-dehydrocholesterol reductase|||Disordered|||Helical|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000207503 http://togogenome.org/gene/10090:Pitx2 ^@ http://purl.uniprot.org/uniprot/B1VD84|||http://purl.uniprot.org/uniprot/B1VD85|||http://purl.uniprot.org/uniprot/P97474|||http://purl.uniprot.org/uniprot/Q6DIA6 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Homeobox|||In isoform Pitx2Calpha.|||In isoform Pitx2Cbeta.|||In isoform Ptx2A.|||In isoform Ptx2C.|||Nuclear localization signal|||OAR|||Phosphothreonine; by PKB/AKT2|||Pituitary homeobox 2 ^@ http://purl.uniprot.org/annotation/PRO_0000049224|||http://purl.uniprot.org/annotation/VSP_002262|||http://purl.uniprot.org/annotation/VSP_002263|||http://purl.uniprot.org/annotation/VSP_031521|||http://purl.uniprot.org/annotation/VSP_031522 http://togogenome.org/gene/10090:Rdh19 ^@ http://purl.uniprot.org/uniprot/G5E8H9 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015091900 http://togogenome.org/gene/10090:Ly6h ^@ http://purl.uniprot.org/uniprot/Q544M1|||http://purl.uniprot.org/uniprot/Q8K356|||http://purl.uniprot.org/uniprot/Q9WUC3 ^@ 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 ^@ GPI-anchor amidated asparagine|||Lymphocyte antigen 6H|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6|||UPAR/Ly6 domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000036150|||http://purl.uniprot.org/annotation/PRO_0000036151|||http://purl.uniprot.org/annotation/PRO_5010844024|||http://purl.uniprot.org/annotation/PRO_5015099253 http://togogenome.org/gene/10090:Oprm1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Z2|||http://purl.uniprot.org/uniprot/A1KZZ4|||http://purl.uniprot.org/uniprot/P42866 ^@ 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|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes receptor recycling; when associated with A-387.|||Abolishes receptor recycling; when associated with A-390.|||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 10.|||In isoform 11.|||In isoform 12.|||In isoform 13.|||In isoform 14, isoform 15 and isoform 16.|||In isoform 17.|||In isoform 18.|||In isoform 19.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8 and isoform 15.|||In isoform 9 and isoform 16.|||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_0000069975|||http://purl.uniprot.org/annotation/VSP_042332|||http://purl.uniprot.org/annotation/VSP_042333|||http://purl.uniprot.org/annotation/VSP_042334|||http://purl.uniprot.org/annotation/VSP_042335|||http://purl.uniprot.org/annotation/VSP_042336|||http://purl.uniprot.org/annotation/VSP_042337|||http://purl.uniprot.org/annotation/VSP_042338|||http://purl.uniprot.org/annotation/VSP_042339|||http://purl.uniprot.org/annotation/VSP_042340|||http://purl.uniprot.org/annotation/VSP_042341|||http://purl.uniprot.org/annotation/VSP_042342|||http://purl.uniprot.org/annotation/VSP_042343|||http://purl.uniprot.org/annotation/VSP_042344|||http://purl.uniprot.org/annotation/VSP_042345|||http://purl.uniprot.org/annotation/VSP_042346|||http://purl.uniprot.org/annotation/VSP_042347 http://togogenome.org/gene/10090:Zeb2 ^@ http://purl.uniprot.org/uniprot/Q3URW5|||http://purl.uniprot.org/uniprot/Q8BSG9|||http://purl.uniprot.org/uniprot/Q9R0G7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5; degenerate|||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|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SMAD-MH2 binding domain|||Zinc finger E-box-binding homeobox 2 ^@ http://purl.uniprot.org/annotation/PRO_0000047237 http://togogenome.org/gene/10090:Fnta ^@ http://purl.uniprot.org/uniprot/Q541Z2|||http://purl.uniprot.org/uniprot/Q61239 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||Inhibits prenylation activity. In myoblasts, impaired insulin-induced RAC1 activation, possibly due to impaired insulin-induced geranyl-geranyltransferase activation. 68% decrease in MUSK-binding.|||Inhibits prenylation activity. In myoblasts, impaired insulin-induced RAC1 activation, possibly due to impaired insulin-induced geranyl-geranyltransferase activation. No effect on MUSK-binding.|||N-acetylalanine|||PFTA 1|||PFTA 2|||PFTA 3|||PFTA 4|||PFTA 5|||Pro residues|||Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000119747 http://togogenome.org/gene/10090:Ssrp1 ^@ http://purl.uniprot.org/uniprot/Q08943 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ 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|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000048607|||http://purl.uniprot.org/annotation/VSP_019626 http://togogenome.org/gene/10090:Gmcl1 ^@ http://purl.uniprot.org/uniprot/Q920G9 ^@ 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_0000087521 http://togogenome.org/gene/10090:C5ar1 ^@ http://purl.uniprot.org/uniprot/P30993 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C5a anaphylatoxin chemotactic 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000069211 http://togogenome.org/gene/10090:Cetn4 ^@ http://purl.uniprot.org/uniprot/Q8K4K1 ^@ 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 ^@ Centrin-4|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||In isoform 3.|||Phosphothreonine; by CK2 ^@ http://purl.uniprot.org/annotation/PRO_0000420789|||http://purl.uniprot.org/annotation/VSP_044649|||http://purl.uniprot.org/annotation/VSP_044650 http://togogenome.org/gene/10090:Psg23 ^@ http://purl.uniprot.org/uniprot/Q9D2U0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Arhgap23 ^@ http://purl.uniprot.org/uniprot/B1AQY2|||http://purl.uniprot.org/uniprot/F8VQ11|||http://purl.uniprot.org/uniprot/Q69ZH9 ^@ 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.|||PDZ|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho GTPase-activating protein 23|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000280472|||http://purl.uniprot.org/annotation/VSP_023710 http://togogenome.org/gene/10090:Jund ^@ http://purl.uniprot.org/uniprot/P15066 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic motif|||Disordered|||Interchain (with C-172 in FOSB)|||Leucine-zipper|||MAP kinase docking motif; essential for its phosphorylation|||Menin-binding motif (MBM)|||Phosphoserine|||Phosphoserine; by MAPK8|||Phosphothreonine|||Transcription factor JunD|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076443 http://togogenome.org/gene/10090:Tmem86b ^@ http://purl.uniprot.org/uniprot/Q497J1 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Lysoplasmalogenase TMEM86B ^@ http://purl.uniprot.org/annotation/PRO_0000201842 http://togogenome.org/gene/10090:Fcrla ^@ http://purl.uniprot.org/uniprot/Q920A9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Acidic residues|||Disordered|||Fc receptor-like A|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000227936|||http://purl.uniprot.org/annotation/VSP_017610 http://togogenome.org/gene/10090:Mcm2 ^@ http://purl.uniprot.org/uniprot/P97310 ^@ 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 ^@ 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 interaction with KAT7.|||Interaction with DNJC9|||Interaction with KAT7|||MCM|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDC7|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194088 http://togogenome.org/gene/10090:Rexo4 ^@ http://purl.uniprot.org/uniprot/Q6PAQ4 ^@ 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|||Exonuclease|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||RNA exonuclease 4 ^@ http://purl.uniprot.org/annotation/PRO_0000131704 http://togogenome.org/gene/10090:Or8c16 ^@ http://purl.uniprot.org/uniprot/Q9EQB2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mxra7 ^@ http://purl.uniprot.org/uniprot/Q9CZH7|||http://purl.uniprot.org/uniprot/Q9D1T2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Matrix-remodeling-associated protein 7|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000239449|||http://purl.uniprot.org/annotation/PRO_5015099670 http://togogenome.org/gene/10090:Chrng ^@ http://purl.uniprot.org/uniprot/F8VQK4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_5022271628 http://togogenome.org/gene/10090:Atp6v0d2 ^@ http://purl.uniprot.org/uniprot/Q80SY3 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ V-type proton ATPase subunit d 2 ^@ http://purl.uniprot.org/annotation/PRO_0000285658 http://togogenome.org/gene/10090:Gtf3c4 ^@ http://purl.uniprot.org/uniprot/E9Q2B0|||http://purl.uniprot.org/uniprot/Q8BMQ2 ^@ 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|||DUF5921|||Disordered|||General transcription factor 3C polypeptide 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Transcription factor IIIC 90kDa subunit N-terminal|||Transcription factor IIIC putative zinc-finger ^@ http://purl.uniprot.org/annotation/PRO_0000209714|||http://purl.uniprot.org/annotation/VSP_010577|||http://purl.uniprot.org/annotation/VSP_010578 http://togogenome.org/gene/10090:Zfp52 ^@ http://purl.uniprot.org/uniprot/Q8BJ45 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ly6c2 ^@ http://purl.uniprot.org/uniprot/P0CW03 ^@ 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 glycine|||Lymphocyte antigen 6C2|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036132|||http://purl.uniprot.org/annotation/PRO_0000036133 http://togogenome.org/gene/10090:Tmem175 ^@ http://purl.uniprot.org/uniprot/Q8BM80|||http://purl.uniprot.org/uniprot/Q9CXY1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Endosomal/lysosomal proton channel TMEM175|||Gain-of-function mutant; increased potassium channel activity in knockin mice.|||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|||Lumenal|||Phosphothreonine|||Reduced potassium channel activity in knockin mice.|||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_0000282589 http://togogenome.org/gene/10090:Rnaset2a ^@ http://purl.uniprot.org/uniprot/C0HKG5|||http://purl.uniprot.org/uniprot/C0HKG6|||http://purl.uniprot.org/uniprot/Q5FWA0 ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Ribonuclease T2-A|||Ribonuclease T2-B ^@ http://purl.uniprot.org/annotation/PRO_0000030988|||http://purl.uniprot.org/annotation/PRO_0000440153 http://togogenome.org/gene/10090:Serpina9 ^@ http://purl.uniprot.org/uniprot/Q9D7D2 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Serpin A9 ^@ http://purl.uniprot.org/annotation/PRO_0000041972 http://togogenome.org/gene/10090:Dynll2 ^@ http://purl.uniprot.org/uniprot/Q9D0M5 ^@ Chain|||Helix|||Molecule Processing|||Secondary Structure|||Site|||Strand ^@ Chain|||Helix|||Site|||Strand ^@ Dynein light chain 2, cytoplasmic|||Interaction with myosin V motor complex ^@ http://purl.uniprot.org/annotation/PRO_0000195133 http://togogenome.org/gene/10090:Haus6 ^@ http://purl.uniprot.org/uniprot/Q6NV99 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||HAUS augmin-like complex subunit 6 N-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Tfam ^@ http://purl.uniprot.org/uniprot/P40630 ^@ Chain|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Chain|||DNA Binding|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ HMG box 1|||HMG box 2|||In isoform Nuclear.|||Intercalates between bases and promotes DNA bending|||Mitochondrion|||N6-succinyllysine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Transcription factor A, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000013471|||http://purl.uniprot.org/annotation/VSP_002185|||http://purl.uniprot.org/annotation/VSP_002186 http://togogenome.org/gene/10090:Napa ^@ http://purl.uniprot.org/uniprot/Q9DB05 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Alpha-soluble NSF attachment protein|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000219057 http://togogenome.org/gene/10090:Otulin ^@ http://purl.uniprot.org/uniprot/Q3UCV8 ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site ^@ Abolishes deubiquitinase activity without affecting interaction with RNF31. Lethality at midgestation in knockin mice caused by inactivation of the LUBAC complex, leading to cell death mediated by TNFR1 and RIPK1.|||Disordered|||Does not affect interaction with RNF31.|||In Gum(D366E) mutant; defects in embryonic angiogenesis. Weaker mutant compared to Gum(W96R) mutant.|||In Gum(W96R) mutant; defects in embryonic angiogenesis. Embryos appear normal before 11.5 dpc but die between 12.5 dpc-14 dpc, probably due to defects in organization of branching vascular networks in the head and trunk.|||Linear diubiquitin binding|||Nucleophile|||OTU|||PDZ-binding|||PIM motif|||Phosphotyrosine|||Ubiquitin thioesterase otulin ^@ http://purl.uniprot.org/annotation/PRO_0000261638 http://togogenome.org/gene/10090:Klhl5 ^@ http://purl.uniprot.org/uniprot/E9Q1L2|||http://purl.uniprot.org/uniprot/Q6PFE1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BTB|||Disordered ^@ http://togogenome.org/gene/10090:Fer1l4 ^@ http://purl.uniprot.org/uniprot/Z4YL23 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||C2|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Lrrk1 ^@ http://purl.uniprot.org/uniprot/Q3UHC2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||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|||Polar residues|||Protein kinase|||Proton acceptor|||Roc ^@ http://purl.uniprot.org/annotation/PRO_0000233378|||http://purl.uniprot.org/annotation/VSP_052013|||http://purl.uniprot.org/annotation/VSP_052014|||http://purl.uniprot.org/annotation/VSP_052015|||http://purl.uniprot.org/annotation/VSP_052016 http://togogenome.org/gene/10090:Pcdh10 ^@ http://purl.uniprot.org/uniprot/E9PX28|||http://purl.uniprot.org/uniprot/E9PXQ7|||http://purl.uniprot.org/uniprot/Q6P0A6|||http://purl.uniprot.org/uniprot/Q80TE2|||http://purl.uniprot.org/uniprot/Q8CC37|||http://purl.uniprot.org/uniprot/Q925I8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Cadherin|||Cadherin cytoplasmic C-terminal|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003243008|||http://purl.uniprot.org/annotation/PRO_5003244305|||http://purl.uniprot.org/annotation/PRO_5015098403|||http://purl.uniprot.org/annotation/PRO_5015099544 http://togogenome.org/gene/10090:Ppara ^@ http://purl.uniprot.org/uniprot/P23204|||http://purl.uniprot.org/uniprot/Q542P9 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Chain|||DNA Binding|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Essential for heterodimerization with RXRA|||NR C4-type|||NR LBD|||No effect on interaction with PER2.|||Nuclear receptor|||Peroxisome proliferator-activated receptor alpha|||Reduces DNA binding and strongly decreases transcriptional activation; when associated with A-119.|||Reduces DNA binding and strongly decreases transcriptional activation; when associated with A-122.|||Required for heterodimerization with RXRA|||Slightly reduces interaction with PER2. ^@ http://purl.uniprot.org/annotation/PRO_0000053482 http://togogenome.org/gene/10090:Pax5 ^@ http://purl.uniprot.org/uniprot/Q02650 ^@ Chain|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Region ^@ Disordered|||PAI subdomain|||Paired|||Paired box protein Pax-5|||RED subdomain ^@ http://purl.uniprot.org/annotation/PRO_0000050184 http://togogenome.org/gene/10090:Tprkb ^@ http://purl.uniprot.org/uniprot/Q8QZZ7 ^@ Chain|||Molecule Processing ^@ Chain ^@ EKC/KEOPS complex subunit Tprkb ^@ http://purl.uniprot.org/annotation/PRO_0000279221 http://togogenome.org/gene/10090:Mcts1 ^@ http://purl.uniprot.org/uniprot/Q9DB27 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Splice Variant ^@ In isoform 2.|||Malignant T-cell-amplified sequence 1|||PUA|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000344787|||http://purl.uniprot.org/annotation/VSP_034857 http://togogenome.org/gene/10090:Itgb3 ^@ http://purl.uniprot.org/uniprot/O54890 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ CX3CL1-binding|||Cytoplasmic|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||Integrin beta-3|||Involved in CX3CL1-, NRG1-, FGF1- and IGF1-binding|||LIR|||Mice display deficits in anxiety as well as in repetitive and social behaviors. Decreases levels of serotonin synapses in midbrain, SLC6A4 activity and location at integrin adhesion complexes in synapses.|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphothreonine|||Phosphotyrosine|||VWFA|||in ADMIDAS binding site|||in ADMIDAS binding site and liganded-open conformation|||in LIMBS binding site|||in MIDAS binding site ^@ http://purl.uniprot.org/annotation/PRO_0000016345 http://togogenome.org/gene/10090:Sox21 ^@ http://purl.uniprot.org/uniprot/Q811W0 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Sequence Conflict ^@ HMG box|||Transcription factor SOX-21 ^@ http://purl.uniprot.org/annotation/PRO_0000048771 http://togogenome.org/gene/10090:Or10g7 ^@ http://purl.uniprot.org/uniprot/E9Q985 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or5p58 ^@ http://purl.uniprot.org/uniprot/Q8VG03 ^@ 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 5P58 ^@ http://purl.uniprot.org/annotation/PRO_0000150840 http://togogenome.org/gene/10090:Dkc1 ^@ http://purl.uniprot.org/uniprot/Q9ESX5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Destabilization of TERC, impaired telomerase function, and reduced rRNA pseudouridylation and pre-rRNA processing.|||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|||H/ACA ribonucleoprotein complex subunit DKC1|||N-acetylalanine|||Nuclear and nucleolar localization|||Nucleolar localization|||Nucleophile|||PUA|||Phosphoserine|||Phosphothreonine|||Reduced rRNA pseudouridylation and pre-rRNA processing.|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000121984 http://togogenome.org/gene/10090:Armcx4 ^@ http://purl.uniprot.org/uniprot/E9PWM3 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ ARM|||Acidic residues|||Armadillo repeat-containing|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Hand2 ^@ http://purl.uniprot.org/uniprot/Q61039 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Heart- and neural crest derivatives-expressed protein 2|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127192 http://togogenome.org/gene/10090:Med24 ^@ http://purl.uniprot.org/uniprot/Q99K74 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||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_0000305912|||http://purl.uniprot.org/annotation/VSP_028355|||http://purl.uniprot.org/annotation/VSP_028356|||http://purl.uniprot.org/annotation/VSP_028357|||http://purl.uniprot.org/annotation/VSP_028358 http://togogenome.org/gene/10090:Gm4841 ^@ http://purl.uniprot.org/uniprot/E9QAA8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ IRG-type G ^@ http://togogenome.org/gene/10090:Clca4a ^@ http://purl.uniprot.org/uniprot/A0A5F8MQB6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5023895996 http://togogenome.org/gene/10090:Nelfa ^@ http://purl.uniprot.org/uniprot/Q8BG30 ^@ 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|||HDAg|||NELF-C/D-binding|||Negative elongation factor A|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RNAPII-binding ^@ http://purl.uniprot.org/annotation/PRO_0000219127 http://togogenome.org/gene/10090:Hmgcl ^@ http://purl.uniprot.org/uniprot/P38060 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Transit Peptide ^@ Hydroxymethylglutaryl-CoA lyase, mitochondrial|||Interchain|||Microbody targeting signal|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Pyruvate carboxyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000013480 http://togogenome.org/gene/10090:Slc66a2 ^@ http://purl.uniprot.org/uniprot/Q80XM9 ^@ 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 and isoform 3.|||In isoform 3.|||In isoform 4.|||PQ-loop 1|||PQ-loop 2|||Phosphoserine|||Solute carrier family 66 member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000282431|||http://purl.uniprot.org/annotation/VSP_024146|||http://purl.uniprot.org/annotation/VSP_024147|||http://purl.uniprot.org/annotation/VSP_024148|||http://purl.uniprot.org/annotation/VSP_024149 http://togogenome.org/gene/10090:Mmp20 ^@ http://purl.uniprot.org/uniprot/P57748 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Motif|||Propeptide|||Repeat|||Signal Peptide ^@ Cysteine switch|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Matrix metalloproteinase-20|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028835|||http://purl.uniprot.org/annotation/PRO_0000028836 http://togogenome.org/gene/10090:Ccdc102a ^@ http://purl.uniprot.org/uniprot/B2RTE5|||http://purl.uniprot.org/uniprot/Q3TMW1 ^@ 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|||Coiled-coil domain-containing protein 102A|||Disordered|||Myosin tail|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000274401 http://togogenome.org/gene/10090:4930402F06Rik ^@ http://purl.uniprot.org/uniprot/A2AUQ8|||http://purl.uniprot.org/uniprot/Q14BP7 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Signal Peptide ^@ Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_5015086036 http://togogenome.org/gene/10090:Sry ^@ http://purl.uniprot.org/uniprot/Q05738|||http://purl.uniprot.org/uniprot/Q53WV7 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant ^@ Abolishes acetylation.|||Basic and acidic residues|||Degron|||Disordered|||Eliminates the C-terminal degron and promotes stabilization of the protein.|||HMG box|||In isoform Sry-S.|||In strain: Torino.|||N6-acetyllysine|||Necessary for interaction with SLC9A3R2 and nuclear accumulation of SLC9A3R2|||Necessary for interaction with ZNF208 isoform KRAB-O|||Polar residues|||Required for nuclear localization|||Sex-determining region Y protein|||Sufficient for interaction with EP300|||Sufficient for interaction with KPNB1 ^@ http://purl.uniprot.org/annotation/PRO_0000048687|||http://purl.uniprot.org/annotation/VSP_060898 http://togogenome.org/gene/10090:Sec24c ^@ http://purl.uniprot.org/uniprot/A0A286YDI8|||http://purl.uniprot.org/uniprot/G3X972|||http://purl.uniprot.org/uniprot/Q80U83 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Gelsolin-like|||Polar residues|||Pro residues|||Sec23/Sec24 beta-sandwich|||Sec23/Sec24 helical|||Sec23/Sec24 trunk|||Zinc finger Sec23/Sec24-type ^@ http://togogenome.org/gene/10090:Or5al1 ^@ http://purl.uniprot.org/uniprot/Q7TR81 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Grm6 ^@ http://purl.uniprot.org/uniprot/A7MD55|||http://purl.uniprot.org/uniprot/Q5NCH9|||http://purl.uniprot.org/uniprot/Q8CFQ7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Metabotropic glutamate receptor 6|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000012935 http://togogenome.org/gene/10090:Iars2 ^@ http://purl.uniprot.org/uniprot/E9PWN3|||http://purl.uniprot.org/uniprot/Q8BIJ6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Transit Peptide ^@ 'HIGH' region|||'KMSKS' region|||Aminoacyl-tRNA synthetase class Ia|||Isoleucine--tRNA ligase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000233337 http://togogenome.org/gene/10090:Gabra1 ^@ http://purl.uniprot.org/uniprot/P62812|||http://purl.uniprot.org/uniprot/Q3URD4|||http://purl.uniprot.org/uniprot/Q544F7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit alpha-1|||Helical|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000429|||http://purl.uniprot.org/annotation/PRO_5014309620|||http://purl.uniprot.org/annotation/PRO_5022259436 http://togogenome.org/gene/10090:Pwwp2b ^@ http://purl.uniprot.org/uniprot/E9Q9M8|||http://purl.uniprot.org/uniprot/Q14AS8|||http://purl.uniprot.org/uniprot/Q3TYY8 ^@ 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|||PWWP|||PWWP domain-containing protein 2B|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000454860 http://togogenome.org/gene/10090:Tln1 ^@ http://purl.uniprot.org/uniprot/P26039|||http://purl.uniprot.org/uniprot/Q0V930|||http://purl.uniprot.org/uniprot/Q3UHS6|||http://purl.uniprot.org/uniprot/Q80TM2 ^@ 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|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence 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|||Interaction with LAYN|||Interaction with SYNM|||Interaction with VCL and F-actin|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Reduces stability and binding to VCL with little effect on binding to APBB1IP; when associated with I-809; V-833 and I-901.|||Reduces stability and binding to VCL with little effect on binding to APBB1IP; when associated with I-809; V-833 and V-867.|||Reduces stability and binding to VCL with little effect on binding to APBB1IP; when associated with I-809; V-867 and I-901.|||Reduces stability and binding to VCL with little effect on binding to APBB1IP; when associated with V-833; V-867 and I-901.|||Talin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000219429 http://togogenome.org/gene/10090:Ap3d1 ^@ http://purl.uniprot.org/uniprot/O54774 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat ^@ AP-3 complex subunit delta-1|||Basic and acidic residues|||Basic residues|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000193767 http://togogenome.org/gene/10090:Sertad3 ^@ http://purl.uniprot.org/uniprot/Q3UYB0|||http://purl.uniprot.org/uniprot/Q9ERC3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||SERTA|||SERTA domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000191616 http://togogenome.org/gene/10090:Ppm1j ^@ http://purl.uniprot.org/uniprot/Q149T7 ^@ 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|||PPM-type phosphatase|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein phosphatase 1J ^@ http://purl.uniprot.org/annotation/PRO_0000289059 http://togogenome.org/gene/10090:Btbd17 ^@ http://purl.uniprot.org/uniprot/Q9DB72 ^@ 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_0000340705 http://togogenome.org/gene/10090:Ptprf ^@ http://purl.uniprot.org/uniprot/A2A8L5|||http://purl.uniprot.org/uniprot/Q3V0J9 ^@ 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|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||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 C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Receptor-type tyrosine-protein phosphatase F|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000370193 http://togogenome.org/gene/10090:Ttc39a ^@ http://purl.uniprot.org/uniprot/A2ACP1 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 39A ^@ http://purl.uniprot.org/annotation/PRO_0000291997|||http://purl.uniprot.org/annotation/VSP_026354 http://togogenome.org/gene/10090:Cdc7 ^@ http://purl.uniprot.org/uniprot/Q66JY4|||http://purl.uniprot.org/uniprot/Q9Z0H0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||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|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Cell division cycle 7-related protein kinase|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085764|||http://purl.uniprot.org/annotation/VSP_004864 http://togogenome.org/gene/10090:Luzp1 ^@ http://purl.uniprot.org/uniprot/Q8R4U7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Leucine zipper protein 1|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000234551 http://togogenome.org/gene/10090:Pnkd ^@ http://purl.uniprot.org/uniprot/A0A0R4J1J1|||http://purl.uniprot.org/uniprot/Q69ZP3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||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.|||Phosphoserine|||Probable hydrolase PNKD ^@ http://purl.uniprot.org/annotation/PRO_0000299550|||http://purl.uniprot.org/annotation/VSP_027741|||http://purl.uniprot.org/annotation/VSP_027742|||http://purl.uniprot.org/annotation/VSP_027743|||http://purl.uniprot.org/annotation/VSP_027744 http://togogenome.org/gene/10090:Marchf10 ^@ http://purl.uniprot.org/uniprot/E9PX79|||http://purl.uniprot.org/uniprot/Q497L7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||RING-CH-type ^@ http://togogenome.org/gene/10090:Zfp61 ^@ http://purl.uniprot.org/uniprot/Q923D1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Or56b1 ^@ http://purl.uniprot.org/uniprot/Q7TRP7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bscl2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J225|||http://purl.uniprot.org/uniprot/Q9Z2E9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Seipin ^@ http://purl.uniprot.org/annotation/PRO_0000191680 http://togogenome.org/gene/10090:Tmem116 ^@ http://purl.uniprot.org/uniprot/G3X901|||http://purl.uniprot.org/uniprot/G3X9M9|||http://purl.uniprot.org/uniprot/Q8VCT8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Vmn1r121 ^@ http://purl.uniprot.org/uniprot/K7N6J4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Adat2 ^@ http://purl.uniprot.org/uniprot/Q6P6J0 ^@ 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|||Strand|||Turn ^@ CMP/dCMP-type deaminase|||Proton donor|||tRNA-specific adenosine deaminase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000287654 http://togogenome.org/gene/10090:Ahcyl ^@ http://purl.uniprot.org/uniprot/P50247|||http://purl.uniprot.org/uniprot/Q3TF14 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ Adenosylhomocysteinase|||N-acetylserine|||N6-(2-hydroxyisobutyryl)lysine|||NAD binding|||Phosphoserine|||Phosphotyrosine|||Removed|||S-adenosyl-L-homocysteine hydrolase NAD binding ^@ http://purl.uniprot.org/annotation/PRO_0000116903 http://togogenome.org/gene/10090:Cd52 ^@ http://purl.uniprot.org/uniprot/Q3U1T8|||http://purl.uniprot.org/uniprot/Q64389 ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Lipid Binding|||Peptide|||Propeptide|||Region|||Signal Peptide|||Transmembrane ^@ CAMPATH-1 antigen|||Disordered|||GPI-anchor amidated serine|||Helical|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000020908|||http://purl.uniprot.org/annotation/PRO_0000020909|||http://purl.uniprot.org/annotation/PRO_5004229739 http://togogenome.org/gene/10090:Ube2g2 ^@ http://purl.uniprot.org/uniprot/P60605|||http://purl.uniprot.org/uniprot/Q3U431 ^@ 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-acetylalanine|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 G2 ^@ http://purl.uniprot.org/annotation/PRO_0000082484 http://togogenome.org/gene/10090:Padi1 ^@ http://purl.uniprot.org/uniprot/Q544I4|||http://purl.uniprot.org/uniprot/Q9Z185 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent ^@ Nucleophile|||Protein-arginine deiminase (PAD) N-terminal|||Protein-arginine deiminase (PAD) central|||Protein-arginine deiminase C-terminal|||Protein-arginine deiminase type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000220024 http://togogenome.org/gene/10090:Macroh2a2 ^@ http://purl.uniprot.org/uniprot/Q8CCK0 ^@ 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|||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_0000227906 http://togogenome.org/gene/10090:Mul1 ^@ http://purl.uniprot.org/uniprot/Q8VCM5 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Crosslink|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||In isoform 3.|||Mitochondrial intermembrane|||Mitochondrial ubiquitin ligase activator of NFKB 1|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000277662|||http://purl.uniprot.org/annotation/VSP_034453|||http://purl.uniprot.org/annotation/VSP_034454|||http://purl.uniprot.org/annotation/VSP_034455 http://togogenome.org/gene/10090:Hdhd2 ^@ http://purl.uniprot.org/uniprot/Q3UGR5 ^@ Binding Site|||Chain|||Coiled-Coil|||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|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Haloacid dehalogenase-like hydrolase domain-containing protein 2|||In isoform 2.|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000287204|||http://purl.uniprot.org/annotation/VSP_025374|||http://purl.uniprot.org/annotation/VSP_025375 http://togogenome.org/gene/10090:Ssxb2 ^@ http://purl.uniprot.org/uniprot/Q80ZT4|||http://purl.uniprot.org/uniprot/Q8C5Z3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB|||KRAB-related ^@ http://togogenome.org/gene/10090:Prkab1 ^@ http://purl.uniprot.org/uniprot/Q542K0|||http://purl.uniprot.org/uniprot/Q9R078 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region ^@ 5'-AMP-activated protein kinase subunit beta-1|||Association with the SNF1 complex (ASC)|||Basic and acidic residues|||Disordered|||Glycogen-binding domain|||N-myristoyl glycine|||N6-succinyllysine|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000204364 http://togogenome.org/gene/10090:Slc25a31 ^@ http://purl.uniprot.org/uniprot/B2RTC8|||http://purl.uniprot.org/uniprot/Q3V132 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Motif|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ADP/ATP translocase 4|||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|||Nucleotide carrier signature motif|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000297626 http://togogenome.org/gene/10090:Tdpoz3 ^@ http://purl.uniprot.org/uniprot/Q717B4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ BTB|||MATH|||TD and POZ domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000191625 http://togogenome.org/gene/10090:1110017D15Rik ^@ http://purl.uniprot.org/uniprot/Q2MH31 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Sperm microtubule inner protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000296260|||http://purl.uniprot.org/annotation/VSP_027172|||http://purl.uniprot.org/annotation/VSP_027173 http://togogenome.org/gene/10090:Sidt2 ^@ http://purl.uniprot.org/uniprot/Q3U1L8|||http://purl.uniprot.org/uniprot/Q8CIF6 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreased gymnosis and RNA and DNA uptake by lysosomes and degradation. Decreased affinity for 700-bp RNA. No effect on lysosomal subcellular location, nor on LAMP2-binding.|||Decreased gymnosis and decreased affinity for 700-bp RNA. No effect on subcellular location.|||Decreased lysosomal localization. Decreased interaction with AP-1 and AP-2 complexes; when associated with S-410. Almost complete loss of lysosomal localization and decreased interaction with AP-1 and AP-2 complexes; when associated with S-428. Decreased interaction with AP-1 and AP-2 complexes, almost complete loss of lysosomal localization, mislocalization to the Golgi apparatus and almost complete loss of RNA degradation by lysosomes; when associated with S-410 and S-428.|||Drastically decreased lysosomal localization. Almost complete loss of lysosomal localization and decreased interaction with AP-1 and AP-2 complexes; when associated with S-359. No effect on interaction with AP-1 and AP-2 complexes, nor on RNA uptake by lysosomes; when associated with S-410. Decreased interaction with AP-1 and AP-2 complexes, almost complete loss of lysosomal localization, mislocalization to the Golgi apparatus and almost complete loss of RNA degradation by lysosomes; when associated with S-359 and S-410.|||Drastically decreased lysosomal localization. Decreased interaction with AP-1 and AP-2 complexes; when associated with S-359. Decreased interaction with AP-1 and AP-2 complexes, almost complete loss of lysosomal localization, mislocalization to the Golgi apparatus and almost complete loss of RNA degradation by lysosomes; when associated with S-359 and S-428. No effect on interaction with AP-1 and AP-2 complexes, nor on RNA uptake by lysosomes; when associated with S-428.|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on lysosomal localization, nor on RNA uptake by lysosomes.|||Phosphoserine|||SID1 transmembrane family member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000032579|||http://purl.uniprot.org/annotation/PRO_5004229848|||http://purl.uniprot.org/annotation/VSP_013525 http://togogenome.org/gene/10090:Zkscan5 ^@ http://purl.uniprot.org/uniprot/Q69ZT2|||http://purl.uniprot.org/uniprot/Q6PAK4|||http://purl.uniprot.org/uniprot/Q9Z1D8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||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)|||KRAB|||SCAN box|||Zinc finger protein with KRAB and SCAN domains 5 ^@ http://purl.uniprot.org/annotation/PRO_0000047316 http://togogenome.org/gene/10090:Kctd3 ^@ http://purl.uniprot.org/uniprot/Q8BFX3 ^@ 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 ^@ BTB|||BTB/POZ domain-containing protein KCTD3|||Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with HCN3|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000247840|||http://purl.uniprot.org/annotation/VSP_020070|||http://purl.uniprot.org/annotation/VSP_020071 http://togogenome.org/gene/10090:Sult2b1 ^@ http://purl.uniprot.org/uniprot/O35400 ^@ 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.|||Proton acceptor|||Sulfotransferase 2B1 ^@ http://purl.uniprot.org/annotation/PRO_0000085150|||http://purl.uniprot.org/annotation/VSP_012511 http://togogenome.org/gene/10090:Ribc2 ^@ http://purl.uniprot.org/uniprot/Q9D4Q1 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Disordered|||RIB43A-like with coiled-coils protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000254099 http://togogenome.org/gene/10090:Chrnd ^@ http://purl.uniprot.org/uniprot/P02716|||http://purl.uniprot.org/uniprot/Q80VZ5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Acetylcholine receptor subunit delta|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Phosphotyrosine; by Tyr-kinases ^@ http://purl.uniprot.org/annotation/PRO_0000000323|||http://purl.uniprot.org/annotation/PRO_5014311913 http://togogenome.org/gene/10090:Ankrd13c ^@ http://purl.uniprot.org/uniprot/Q3UX43 ^@ 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 1|||ANK 2|||ANK 3|||Ankyrin repeat domain-containing protein 13C|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000240646|||http://purl.uniprot.org/annotation/VSP_019409|||http://purl.uniprot.org/annotation/VSP_019410 http://togogenome.org/gene/10090:Fbxl16 ^@ http://purl.uniprot.org/uniprot/A2RT62|||http://purl.uniprot.org/uniprot/B2RPY3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Disordered|||F-box|||F-box/LRR-repeat protein 16|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Omega-N-methylarginine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000307721 http://togogenome.org/gene/10090:Rnf125 ^@ http://purl.uniprot.org/uniprot/Q9D9R0 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C2HC RNF-type|||Disordered|||E3 ubiquitin-protein ligase RNF125|||In isoform 2.|||Interaction with the C2HC RNF-type zinc finger|||Interaction with the RING-type zinc finger|||Linker region|||N-myristoyl glycine|||RING-type|||Removed|||Required for interaction with ubiquitin and for autoubiquitination ^@ http://purl.uniprot.org/annotation/PRO_0000056092|||http://purl.uniprot.org/annotation/VSP_015216 http://togogenome.org/gene/10090:Nom1 ^@ http://purl.uniprot.org/uniprot/Q3UFM5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||MI|||MIF4G|||Necessary for nucleolar localization and for targeting PPP1CA to the nucleolus|||Nucleolar MIF4G domain-containing protein 1|||Phosphoserine|||Polar residues|||Required for efficient binding to PPP1CA and for targeting PPP1CA to the nucleolus ^@ http://purl.uniprot.org/annotation/PRO_0000286824 http://togogenome.org/gene/10090:Tmem167 ^@ http://purl.uniprot.org/uniprot/Q9CR64 ^@ 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|||Protein kish-A ^@ http://purl.uniprot.org/annotation/PRO_0000247769|||http://purl.uniprot.org/annotation/VSP_020044 http://togogenome.org/gene/10090:Prex2 ^@ http://purl.uniprot.org/uniprot/Q3LAC4|||http://purl.uniprot.org/uniprot/Q3UWW3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ DEP 1|||DEP 2|||DH|||Disordered|||In isoform 2.|||PDZ 1|||PDZ 2|||PH|||Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein ^@ http://purl.uniprot.org/annotation/PRO_0000286796|||http://purl.uniprot.org/annotation/VSP_025164|||http://purl.uniprot.org/annotation/VSP_025165 http://togogenome.org/gene/10090:Prag1 ^@ http://purl.uniprot.org/uniprot/Q571I4 ^@ 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|||Inactive tyrosine-protein kinase PRAG1|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Protein kinase|||Required for homodimerization ^@ http://purl.uniprot.org/annotation/PRO_0000263009 http://togogenome.org/gene/10090:Trp73 ^@ http://purl.uniprot.org/uniprot/Q9D6A3|||http://purl.uniprot.org/uniprot/Q9JJP2|||http://purl.uniprot.org/uniprot/Z4YK94 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ DNA-binding|||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 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with HIPK2|||Oligomerization|||PPxY motif|||Phosphothreonine; by PLK1|||Phosphotyrosine; by ABL1|||Phosphotyrosine; by SRC and HCK|||Polar residues|||SAM|||Transactivation|||Tumor protein p73 ^@ http://purl.uniprot.org/annotation/PRO_0000370211|||http://purl.uniprot.org/annotation/VSP_053081|||http://purl.uniprot.org/annotation/VSP_053082|||http://purl.uniprot.org/annotation/VSP_053083|||http://purl.uniprot.org/annotation/VSP_053084 http://togogenome.org/gene/10090:Or8b101 ^@ http://purl.uniprot.org/uniprot/Q9EQA5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r31 ^@ http://purl.uniprot.org/uniprot/H3BKW5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnpy3 ^@ http://purl.uniprot.org/uniprot/Q9DAU1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Does not affect association with TLR2, TLR4 and TLR9; does not affect cell-surface expression of TLR2, TLR4 and TLR9; does not affect responses of TLR2, TLR4 and TLR9.|||In isoform 2.|||Loss of HSP90B1-binding. Impairs association with TLR2 and TLR4; does not impair association with TLR9; partially affects responses of TLR2 and TLR4; affects responses of TLR9; does not affect cell-surface expression of TLR2; affects cell-surface expression of TLR4 and TLR9.|||N-linked (GlcNAc...) asparagine|||Protein canopy homolog 3|||Saposin B-type ^@ http://purl.uniprot.org/annotation/PRO_0000313781|||http://purl.uniprot.org/annotation/VSP_030134 http://togogenome.org/gene/10090:Slc7a12 ^@ http://purl.uniprot.org/uniprot/Q8VIE6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Interchain|||Solute carrier family 7 member 12 ^@ http://purl.uniprot.org/annotation/PRO_0000458860 http://togogenome.org/gene/10090:Abcc8 ^@ http://purl.uniprot.org/uniprot/B2RUS7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Cass4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J199|||http://purl.uniprot.org/uniprot/Q08EC4 ^@ 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 ^@ Cas scaffolding protein family member 4|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000351205|||http://purl.uniprot.org/annotation/VSP_052948|||http://purl.uniprot.org/annotation/VSP_052949|||http://purl.uniprot.org/annotation/VSP_052950|||http://purl.uniprot.org/annotation/VSP_052951 http://togogenome.org/gene/10090:Max ^@ http://purl.uniprot.org/uniprot/A0A1W2P7P4|||http://purl.uniprot.org/uniprot/P28574 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Leucine-zipper|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Protein max|||Removed|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127270|||http://purl.uniprot.org/annotation/VSP_059578 http://togogenome.org/gene/10090:Fam220a ^@ http://purl.uniprot.org/uniprot/Q3ZN08 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Protein FAM220A ^@ http://purl.uniprot.org/annotation/PRO_0000321925 http://togogenome.org/gene/10090:Creb3l3 ^@ http://purl.uniprot.org/uniprot/Q91XE9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Basic motif|||Cleavage; by PS1|||Cyclic AMP-responsive element-binding protein 3-like protein 3|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Signal-anchor for type II membrane protein|||Leucine-zipper|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Processed cyclic AMP-responsive element-binding protein 3-like protein 3|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000288075|||http://purl.uniprot.org/annotation/PRO_0000307123 http://togogenome.org/gene/10090:Vmn2r9 ^@ http://purl.uniprot.org/uniprot/K7N6Z8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5040056752 http://togogenome.org/gene/10090:Cyp7a1 ^@ http://purl.uniprot.org/uniprot/Q64505 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Cytochrome P450 7A1|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051902 http://togogenome.org/gene/10090:Borcs6 ^@ http://purl.uniprot.org/uniprot/Q9D6W8 ^@ 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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000393961 http://togogenome.org/gene/10090:Lce3a ^@ http://purl.uniprot.org/uniprot/Q497I5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ncam2 ^@ http://purl.uniprot.org/uniprot/O35136|||http://purl.uniprot.org/uniprot/Q71VC5 ^@ 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|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||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 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 Short.|||N-linked (GlcNAc...) asparagine|||Neural cell adhesion molecule 2|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000042589|||http://purl.uniprot.org/annotation/VSP_002590 http://togogenome.org/gene/10090:Agtr1a ^@ http://purl.uniprot.org/uniprot/P29754 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||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|||Type-1 angiotensin II receptor A ^@ http://purl.uniprot.org/annotation/PRO_0000069155 http://togogenome.org/gene/10090:Smndc1 ^@ http://purl.uniprot.org/uniprot/Q8BGT7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Motif ^@ N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Survival of motor neuron-related-splicing factor 30|||Tudor ^@ http://purl.uniprot.org/annotation/PRO_0000218909 http://togogenome.org/gene/10090:Arpc4 ^@ http://purl.uniprot.org/uniprot/P59999 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Actin-related protein 2/3 complex subunit 4|||N-acetylthreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000124050 http://togogenome.org/gene/10090:Ptpre ^@ http://purl.uniprot.org/uniprot/A0A1B0GRH2|||http://purl.uniprot.org/uniprot/A0A1B0GRT6|||http://purl.uniprot.org/uniprot/P49446|||http://purl.uniprot.org/uniprot/Q3V1H5 ^@ Active Site|||Binding Site|||Chain|||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|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphotyrosine|||Receptor-type tyrosine-protein phosphatase|||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_0000025440|||http://purl.uniprot.org/annotation/PRO_5016196252|||http://purl.uniprot.org/annotation/VSP_038491|||http://purl.uniprot.org/annotation/VSP_038492 http://togogenome.org/gene/10090:Tmem62 ^@ http://purl.uniprot.org/uniprot/Q8BXJ9 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 62 ^@ http://purl.uniprot.org/annotation/PRO_0000254137 http://togogenome.org/gene/10090:Mif4gd ^@ http://purl.uniprot.org/uniprot/Q3UBZ5|||http://purl.uniprot.org/uniprot/Q8BTE1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||MIF4G|||MIF4G domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000337090|||http://purl.uniprot.org/annotation/VSP_033878|||http://purl.uniprot.org/annotation/VSP_033879 http://togogenome.org/gene/10090:Abca3 ^@ http://purl.uniprot.org/uniprot/Q3TN91|||http://purl.uniprot.org/uniprot/Q6AXE3|||http://purl.uniprot.org/uniprot/Q8R420 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Site|||Transmembrane ^@ 150 Kda mature form|||ABC transporter|||ABC transporter 1|||ABC transporter 2|||Cleavage; by CTSL|||Helical|||Knockin new born mice are healthy and survive into adulthood without overt signs of respiratory distress. Knockin mice show a severe lung phenotype that begins with alveolar inflammatory cell infiltration at the early stage of the mouse life followed by aberrant lung remodeling with characteristics of diffuse parenchymal lung disease (DPLD)- and emphysema-like alveolar disruption in older mice.|||N-linked (GlcNAc...) asparagine|||Phospholipid-transporting ATPase ABCA3 ^@ http://purl.uniprot.org/annotation/PRO_0000093294|||http://purl.uniprot.org/annotation/PRO_0000452298 http://togogenome.org/gene/10090:Hfm1 ^@ http://purl.uniprot.org/uniprot/D3Z4R1|||http://purl.uniprot.org/uniprot/Q8CA92 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ DEAD/DEAH box helicase|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Polar residues|||Probable ATP-dependent DNA helicase HFM1|||SEC63 ^@ http://purl.uniprot.org/annotation/PRO_0000430642 http://togogenome.org/gene/10090:Alox15 ^@ http://purl.uniprot.org/uniprot/A2CF88|||http://purl.uniprot.org/uniprot/P39654 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Abolishes arachidonate 15-lipoxygenase activity. Abolishes arachidonate 12-lipoxygenase activity. Abolishes linoleate 13-lipoxygenase activity.|||Essential for stabilizing binding to COTL1|||Lipoxygenase|||PLAT|||Polyunsaturated fatty acid lipoxygenase ALOX15 ^@ http://purl.uniprot.org/annotation/PRO_0000220686 http://togogenome.org/gene/10090:Rgs9bp ^@ http://purl.uniprot.org/uniprot/Q148R9 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict|||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_0000287587 http://togogenome.org/gene/10090:Eif3k ^@ http://purl.uniprot.org/uniprot/Q3TY56|||http://purl.uniprot.org/uniprot/Q9DBZ5 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Splice Variant ^@ Eukaryotic translation initiation factor 3 subunit K|||In isoform 2.|||N-acetylalanine|||PCI|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000123547|||http://purl.uniprot.org/annotation/VSP_013425 http://togogenome.org/gene/10090:Klk1b24 ^@ http://purl.uniprot.org/uniprot/A0A1R3UCH3|||http://purl.uniprot.org/uniprot/Q61754 ^@ 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|||Kallikrein 1-related peptidase b24|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027991|||http://purl.uniprot.org/annotation/PRO_0000027992|||http://purl.uniprot.org/annotation/PRO_5010210889 http://togogenome.org/gene/10090:Tcea1 ^@ http://purl.uniprot.org/uniprot/E9PYD5|||http://purl.uniprot.org/uniprot/P10711|||http://purl.uniprot.org/uniprot/Q3UWX7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 1.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||TFIIS N-terminal|||TFIIS central|||TFIIS-type|||Transcription elongation factor A protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000121447|||http://purl.uniprot.org/annotation/VSP_006410 http://togogenome.org/gene/10090:Nudt22 ^@ http://purl.uniprot.org/uniprot/Q9DD16 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict ^@ Nudix box|||Nudix hydrolase|||Uridine diphosphate glucose pyrophosphatase NUDT22 ^@ http://purl.uniprot.org/annotation/PRO_0000263732 http://togogenome.org/gene/10090:Tomm40 ^@ http://purl.uniprot.org/uniprot/Q9QYA2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Mitochondrial import receptor subunit TOM40 homolog|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000051524 http://togogenome.org/gene/10090:Lrrc20 ^@ http://purl.uniprot.org/uniprot/Q8CI70 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Leucine-rich repeat-containing protein 20|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000084476 http://togogenome.org/gene/10090:Kif16b ^@ http://purl.uniprot.org/uniprot/B1AVY7 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue ^@ FHA|||Kinesin motor|||Kinesin-like protein KIF16B|||PX|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000409500 http://togogenome.org/gene/10090:Foxred2 ^@ http://purl.uniprot.org/uniprot/Q3USW5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||FAD-dependent oxidoreductase domain-containing protein 2|||N-linked (GlcNAc...) asparagine|||Polar residues|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000337693 http://togogenome.org/gene/10090:S100a16 ^@ http://purl.uniprot.org/uniprot/Q9D708 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||EF-hand 1; degenerate|||EF-hand 2|||Protein S100-A16 ^@ http://purl.uniprot.org/annotation/PRO_0000441802 http://togogenome.org/gene/10090:Ocel1 ^@ http://purl.uniprot.org/uniprot/D3Z3P2|||http://purl.uniprot.org/uniprot/G5E815|||http://purl.uniprot.org/uniprot/Q8VCR9 ^@ 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|||OCEL|||Occludin/ELL domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000271532 http://togogenome.org/gene/10090:Zbtb45 ^@ http://purl.uniprot.org/uniprot/Q52KG4 ^@ 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 ^@ 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_0000439879 http://togogenome.org/gene/10090:Clec14a ^@ http://purl.uniprot.org/uniprot/Q8VCP9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 14 member A|||Cytoplasmic|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000017378 http://togogenome.org/gene/10090:Clic5 ^@ http://purl.uniprot.org/uniprot/A0A668KLB7|||http://purl.uniprot.org/uniprot/Q8BXK9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Chloride intracellular channel protein 5|||Disordered|||GST C-terminal|||Helical; Note=After insertion into the membrane|||Polar residues|||Required for insertion into the membrane ^@ http://purl.uniprot.org/annotation/PRO_0000144215 http://togogenome.org/gene/10090:Fthl17b ^@ http://purl.uniprot.org/uniprot/A2AHC5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ferritin-like diiron ^@ http://togogenome.org/gene/10090:Prkca ^@ http://purl.uniprot.org/uniprot/P20444|||http://purl.uniprot.org/uniprot/Q4VA93 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Zinc Finger ^@ AGC-kinase C-terminal|||C2|||In mutant form UV25.|||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|||Protein kinase|||Protein kinase C alpha type|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000055680 http://togogenome.org/gene/10090:Slc1a3 ^@ http://purl.uniprot.org/uniprot/P56564|||http://purl.uniprot.org/uniprot/Q543U3 ^@ Binding Site|||Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Discontinuously helical|||Disordered|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000202058 http://togogenome.org/gene/10090:Bsdc1 ^@ http://purl.uniprot.org/uniprot/Q80Y55 ^@ 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 ^@ BSD|||BSD domain-containing protein 1|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000282640 http://togogenome.org/gene/10090:Csrp1 ^@ http://purl.uniprot.org/uniprot/P97315|||http://purl.uniprot.org/uniprot/Q4FJX4 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif ^@ 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_0000075716 http://togogenome.org/gene/10090:Afap1l2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1L6|||http://purl.uniprot.org/uniprot/Q5DTU0 ^@ 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 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000050806|||http://purl.uniprot.org/annotation/VSP_014257 http://togogenome.org/gene/10090:Slc39a5 ^@ http://purl.uniprot.org/uniprot/Q9D856 ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pros-methylhistidine|||Zinc transporter ZIP5 ^@ http://purl.uniprot.org/annotation/PRO_0000045796 http://togogenome.org/gene/10090:Gspt2 ^@ http://purl.uniprot.org/uniprot/Q149F3 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Eukaryotic peptide chain release factor GTP-binding subunit ERF3B|||G1|||G2|||G3|||G4|||G5|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000327257 http://togogenome.org/gene/10090:Galntl5 ^@ http://purl.uniprot.org/uniprot/Q9D4M9 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000059145 http://togogenome.org/gene/10090:Vav2 ^@ http://purl.uniprot.org/uniprot/Q60992|||http://purl.uniprot.org/uniprot/Q7TSI6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Zinc Finger ^@ Calponin-homology (CH)|||DH|||Guanine nucleotide exchange factor VAV2|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphotyrosine; by EGFR|||SH2|||SH3|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000080985 http://togogenome.org/gene/10090:Cyp2j5 ^@ http://purl.uniprot.org/uniprot/O54749|||http://purl.uniprot.org/uniprot/Q3TNC5 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Cytochrome P450 2J5|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051771 http://togogenome.org/gene/10090:Dtymk ^@ http://purl.uniprot.org/uniprot/P97930|||http://purl.uniprot.org/uniprot/Q6GRA7 ^@ 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 ^@ In isoform 2.|||LID|||N-acetylalanine|||Removed|||Thymidylate kinase|||Thymidylate kinase-like ^@ http://purl.uniprot.org/annotation/PRO_0000155211|||http://purl.uniprot.org/annotation/VSP_003029 http://togogenome.org/gene/10090:Pcdhac1 ^@ http://purl.uniprot.org/uniprot/Q91Y10 ^@ 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|||Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099508 http://togogenome.org/gene/10090:Tmco3 ^@ http://purl.uniprot.org/uniprot/Q8BH01 ^@ Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane ^@ 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_0000249857|||http://purl.uniprot.org/annotation/VSP_020565|||http://purl.uniprot.org/annotation/VSP_020566|||http://purl.uniprot.org/annotation/VSP_020567 http://togogenome.org/gene/10090:Wif1 ^@ http://purl.uniprot.org/uniprot/Q3TYU1|||http://purl.uniprot.org/uniprot/Q9WUA1 ^@ 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 ^@ Basic and acidic residues|||Disordered|||EGF-like|||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_0000007776|||http://purl.uniprot.org/annotation/PRO_5014309157 http://togogenome.org/gene/10090:Vps54 ^@ http://purl.uniprot.org/uniprot/Q5SPW0|||http://purl.uniprot.org/uniprot/Q91ZJ4 ^@ 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 ^@ Disordered|||In isoform 2.|||In wr; destabilizes and consequently reduces protein levels, as well as those of the GARP complex.|||Phosphoserine|||Polar residues|||Vacuolar protein sorting-associated protein 54|||Vacuolar protein sorting-associated protein 54 C-terminal|||Vacuolar protein sorting-associated protein 54 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000148732|||http://purl.uniprot.org/annotation/VSP_013757 http://togogenome.org/gene/10090:Nod1 ^@ http://purl.uniprot.org/uniprot/Q540J8|||http://purl.uniprot.org/uniprot/Q8BHB0 ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site ^@ Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Repeat|||Sequence Variant ^@ CARD|||In strain: Czech II.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||NACHT|||Nucleotide-binding oligomerization domain-containing protein 1|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000144078 http://togogenome.org/gene/10090:Or10p1 ^@ http://purl.uniprot.org/uniprot/Q8VGJ1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cip2a ^@ http://purl.uniprot.org/uniprot/Q8BWY9 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Helical|||N-acetylmethionine|||Phosphoserine|||Protein CIP2A|||Required for homodimerization|||Required for interaction with PPP2R5C ^@ http://purl.uniprot.org/annotation/PRO_0000287142 http://togogenome.org/gene/10090:Crabp2 ^@ http://purl.uniprot.org/uniprot/P22935 ^@ Binding Site|||Chain|||Crosslink|||Modification|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Motif ^@ Cellular retinoic acid-binding protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000067416 http://togogenome.org/gene/10090:Hbb-bh1 ^@ http://purl.uniprot.org/uniprot/P04444|||http://purl.uniprot.org/uniprot/Q5EBL1 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Globin family profile|||Hemoglobin subunit beta-H1|||distal binding residue|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000053023 http://togogenome.org/gene/10090:BC028528 ^@ http://purl.uniprot.org/uniprot/Q8R2K8 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Uncharacterized protein C1orf54 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000251201|||http://purl.uniprot.org/annotation/VSP_020746 http://togogenome.org/gene/10090:Glrx ^@ http://purl.uniprot.org/uniprot/Q3U6L3|||http://purl.uniprot.org/uniprot/Q9QUH0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site ^@ Glutaredoxin|||Glutaredoxin-1|||Loss of activity.|||N-acetylalanine|||N6-succinyllysine|||Redox-active|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000141601 http://togogenome.org/gene/10090:Ubtd2 ^@ http://purl.uniprot.org/uniprot/Q6PGH0 ^@ 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|||Ubiquitin domain-containing protein 2|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000244333 http://togogenome.org/gene/10090:Copb1 ^@ http://purl.uniprot.org/uniprot/Q9JIF7 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ Coatomer subunit beta|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||N-acetylthreonine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000193834 http://togogenome.org/gene/10090:Spz1 ^@ http://purl.uniprot.org/uniprot/Q99MY0 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Basic motif|||Disordered|||Helix-loop-helix motif|||Interaction with PPP1CC isoform gamma-2|||Leucine-zipper|||Phosphoserine|||Spermatogenic leucine zipper protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000280508 http://togogenome.org/gene/10090:Ifngr2 ^@ http://purl.uniprot.org/uniprot/Q63953 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Fibronectin type-III|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015098098 http://togogenome.org/gene/10090:Tppp ^@ http://purl.uniprot.org/uniprot/Q3URG1|||http://purl.uniprot.org/uniprot/Q7TQD2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Mediates interaction with LIMK1|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine|||Tubulin polymerization-promoting protein ^@ http://purl.uniprot.org/annotation/PRO_0000221136 http://togogenome.org/gene/10090:Mllt11 ^@ http://purl.uniprot.org/uniprot/P97783|||http://purl.uniprot.org/uniprot/Q543U0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Disordered|||Nuclear export signal|||Phosphoserine|||Polar residues|||Protein AF1q|||Putative WW-binding ^@ http://purl.uniprot.org/annotation/PRO_0000064472 http://togogenome.org/gene/10090:Cd68 ^@ http://purl.uniprot.org/uniprot/P31996 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ 1-1|||1-2|||2-1|||2-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform Short.|||Macrosialin|||Mucin-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000017103|||http://purl.uniprot.org/annotation/VSP_003043 http://togogenome.org/gene/10090:Las1l ^@ http://purl.uniprot.org/uniprot/A2BE28 ^@ 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|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Ribosomal biogenesis protein LAS1L ^@ http://purl.uniprot.org/annotation/PRO_0000390998|||http://purl.uniprot.org/annotation/VSP_038670 http://togogenome.org/gene/10090:Ubald1 ^@ http://purl.uniprot.org/uniprot/Q6P3B2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Pro residues|||UBA-like domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000236080 http://togogenome.org/gene/10090:Dffa ^@ http://purl.uniprot.org/uniprot/O54786|||http://purl.uniprot.org/uniprot/Q8C535 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand ^@ CIDE-N|||Cleavage; by caspase-3|||DNA fragmentation factor subunit alpha|||Disordered|||In isoform ICAD-S.|||N-acetylmethionine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000144717|||http://purl.uniprot.org/annotation/VSP_001087|||http://purl.uniprot.org/annotation/VSP_001088 http://togogenome.org/gene/10090:Rabep2 ^@ http://purl.uniprot.org/uniprot/Q91WG2 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Rab GTPase-binding effector protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000187560|||http://purl.uniprot.org/annotation/VSP_010460|||http://purl.uniprot.org/annotation/VSP_010461 http://togogenome.org/gene/10090:Fam117a ^@ http://purl.uniprot.org/uniprot/Q7TNF9 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM117A ^@ http://purl.uniprot.org/annotation/PRO_0000264989|||http://purl.uniprot.org/annotation/VSP_021901 http://togogenome.org/gene/10090:Scg5 ^@ http://purl.uniprot.org/uniprot/P12961|||http://purl.uniprot.org/uniprot/Q3TT51 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Abolishes proteolytic processing; when associated with A-177.|||Basic and acidic residues|||C-terminal peptide|||Disordered|||N-terminal peptide|||Neuroendocrine protein 7B2|||No effect on proteolytic processing. Abolishes proteolytic processing; when associated with G-178.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000000044|||http://purl.uniprot.org/annotation/PRO_0000000045|||http://purl.uniprot.org/annotation/PRO_0000000046|||http://purl.uniprot.org/annotation/PRO_5015097459 http://togogenome.org/gene/10090:Ift81 ^@ http://purl.uniprot.org/uniprot/O35594 ^@ 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|||CH (calponin-homology)-like region|||Disordered|||In isoform CDV-1.|||Intraflagellar transport protein 81 homolog|||N-acetylserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000020918|||http://purl.uniprot.org/annotation/VSP_018785 http://togogenome.org/gene/10090:Evi2a ^@ http://purl.uniprot.org/uniprot/P20934 ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protein EVI2A ^@ http://purl.uniprot.org/annotation/PRO_0000021212 http://togogenome.org/gene/10090:Cd300c2 ^@ http://purl.uniprot.org/uniprot/Q7TSN2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Abolishes interaction with TYROBP or FcR gamma.|||CMRF-35-like molecule 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||Interaction with TYROBP or FcR gamma|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000320127 http://togogenome.org/gene/10090:Actbl2 ^@ http://purl.uniprot.org/uniprot/Q8BFZ3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Beta-actin-like protein 2|||Methionine (R)-sulfoxide ^@ http://purl.uniprot.org/annotation/PRO_0000318850 http://togogenome.org/gene/10090:Piezo1 ^@ http://purl.uniprot.org/uniprot/E9PUQ9 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Piezo|||Piezo non-specific cation channel R-Ras-binding|||Polar residues ^@ http://togogenome.org/gene/10090:Pecam1 ^@ http://purl.uniprot.org/uniprot/Q08481|||http://purl.uniprot.org/uniprot/Q8CAW4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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 C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like domain-containing protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||May play a role in cytoprotective signaling|||Membrane-bound segment which detaches upon phosphorylation|||N-linked (GlcNAc...) asparagine|||No significant effect on phosphorylation by FER.|||Phosphoserine|||Phosphotyrosine; by FER|||Platelet endothelial cell adhesion molecule|||Reduces tyrosine phosphorylation by FER by about 60%.|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000014896|||http://purl.uniprot.org/annotation/PRO_5004306264|||http://purl.uniprot.org/annotation/VSP_038723|||http://purl.uniprot.org/annotation/VSP_038724|||http://purl.uniprot.org/annotation/VSP_038725 http://togogenome.org/gene/10090:Or10v5 ^@ http://purl.uniprot.org/uniprot/Q8VGJ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gipc2 ^@ http://purl.uniprot.org/uniprot/Q9Z2H7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||PDZ|||PDZ domain-containing protein GIPC2 ^@ http://purl.uniprot.org/annotation/PRO_0000247189 http://togogenome.org/gene/10090:Mapkapk2 ^@ http://purl.uniprot.org/uniprot/P49138|||http://purl.uniprot.org/uniprot/Q3U2P8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Autoinhibitory helix|||Bipartite nuclear localization signal 1|||Bipartite nuclear localization signal 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Leads to constitutive protein kinase activity.|||MAP kinase-activated protein kinase 2|||Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-208.|||Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-320.|||Nuclear export signal (NES)|||Phosphoserine; by MAPK14|||Phosphoserine; by autocatalysis|||Phosphothreonine; by MAPK14|||Pro residues|||Protein kinase|||Proton acceptor|||Strong decrease in kinase activity; when associated with A-208.|||Strong decrease in kinase activity; when associated with A-320.|||p38 MAPK-binding site ^@ http://purl.uniprot.org/annotation/PRO_0000086289 http://togogenome.org/gene/10090:Or1j4 ^@ http://purl.uniprot.org/uniprot/Q8VFP8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or4b1 ^@ http://purl.uniprot.org/uniprot/Q8VGP3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dock11 ^@ http://purl.uniprot.org/uniprot/A2AF47 ^@ 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 ^@ C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 11|||Disordered|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000299559 http://togogenome.org/gene/10090:Atp11a ^@ http://purl.uniprot.org/uniprot/E9Q3G7|||http://purl.uniprot.org/uniprot/P98197 ^@ 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|||Site|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cleavage; by CASP3|||Cytoplasmic|||Extracellular|||Helical|||Mutant mice surviving beyond the perinatal period show a reduction in brain size, dilated lateral ventricles and neurologic deficits. Increased shingomyelin levels in various regions of mutant embryos.|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Phospholipid-transporting ATPase IH|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000046370 http://togogenome.org/gene/10090:Krt87 ^@ http://purl.uniprot.org/uniprot/Q6IMF0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type II cuticular 87|||Linker 1|||Linker 12|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000361692 http://togogenome.org/gene/10090:Mrgprh ^@ http://purl.uniprot.org/uniprot/Q99MT8|||http://purl.uniprot.org/uniprot/W8W3M0 ^@ 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|||Mas-related G-protein coupled receptor member H|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069770 http://togogenome.org/gene/10090:Sdc3 ^@ http://purl.uniprot.org/uniprot/Q64519 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||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_0000033508 http://togogenome.org/gene/10090:Tas2r102 ^@ http://purl.uniprot.org/uniprot/F8VPL4|||http://purl.uniprot.org/uniprot/Q0VFY9 ^@ Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Non-terminal Residue|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Gripap1 ^@ http://purl.uniprot.org/uniprot/A2AEW8|||http://purl.uniprot.org/uniprot/Q8VD04 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Cleavage; by caspase-3|||Disordered|||GRASP-1 C-terminal chain|||GRIP1-associated protein 1|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087582|||http://purl.uniprot.org/annotation/PRO_0000441812 http://togogenome.org/gene/10090:Inhbe ^@ http://purl.uniprot.org/uniprot/O08717 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Inhibin beta E chain|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033738|||http://purl.uniprot.org/annotation/PRO_0000033739 http://togogenome.org/gene/10090:Ubqln5 ^@ http://purl.uniprot.org/uniprot/Q9D4I8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||UBA|||Ubiquitin-like ^@ http://togogenome.org/gene/10090:Gm5891 ^@ http://purl.uniprot.org/uniprot/Q3UT86 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Sbds ^@ http://purl.uniprot.org/uniprot/P70122 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylserine|||Phosphoserine|||Removed|||Ribosome maturation protein SBDS ^@ http://purl.uniprot.org/annotation/PRO_0000123763 http://togogenome.org/gene/10090:Cdrt4 ^@ http://purl.uniprot.org/uniprot/Q9DA64 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ CMT1A duplicated region transcript 4 protein homolog|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000314904 http://togogenome.org/gene/10090:Zfp120 ^@ http://purl.uniprot.org/uniprot/A2ANU5|||http://purl.uniprot.org/uniprot/Q8BZW4|||http://purl.uniprot.org/uniprot/Q9EQK2 ^@ 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 1|||C2H2-type 10|||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|||In isoform 2.|||KRAB|||Zinc finger protein 120 ^@ http://purl.uniprot.org/annotation/PRO_0000374052|||http://purl.uniprot.org/annotation/PRO_5002642560|||http://purl.uniprot.org/annotation/VSP_053088 http://togogenome.org/gene/10090:Rps6ka6 ^@ http://purl.uniprot.org/uniprot/B1B0X3|||http://purl.uniprot.org/uniprot/Q7TPS0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ AGC-kinase C-terminal|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Ribosomal protein S6 kinase alpha-6 ^@ http://purl.uniprot.org/annotation/PRO_0000278162|||http://purl.uniprot.org/annotation/VSP_023128|||http://purl.uniprot.org/annotation/VSP_023129 http://togogenome.org/gene/10090:Tmsb15l ^@ http://purl.uniprot.org/uniprot/Q8C0W0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Dnajc8 ^@ http://purl.uniprot.org/uniprot/A2ALF2|||http://purl.uniprot.org/uniprot/Q6NZB0 ^@ 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_0000071061 http://togogenome.org/gene/10090:Hrh1 ^@ http://purl.uniprot.org/uniprot/B3Y5T0|||http://purl.uniprot.org/uniprot/P70174 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||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|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||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|||Histamine H1 receptor|||Important for agonist binding|||In strain: C3H/HeJ and CBA/J.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069677 http://togogenome.org/gene/10090:Ralgds ^@ http://purl.uniprot.org/uniprot/A2AK33|||http://purl.uniprot.org/uniprot/Q03385|||http://purl.uniprot.org/uniprot/Q3TWC1|||http://purl.uniprot.org/uniprot/Q3TXZ3|||http://purl.uniprot.org/uniprot/Q3UQY9|||http://purl.uniprot.org/uniprot/Q6ZPU1 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Disordered|||N-terminal Ras-GEF|||Phosphotyrosine|||Polar residues|||Ral guanine nucleotide dissociation stimulator|||Ras-GEF|||Ras-associating ^@ http://purl.uniprot.org/annotation/PRO_0000068878 http://togogenome.org/gene/10090:Nus1 ^@ http://purl.uniprot.org/uniprot/Q99LJ8 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Dehydrodolichyl diphosphate synthase complex subunit Nus1|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||N-linked (GlcNAc...) asparagine|||RXG motif; crucial for prenyltransferase activity ^@ http://purl.uniprot.org/annotation/PRO_0000273168 http://togogenome.org/gene/10090:Abcb7 ^@ http://purl.uniprot.org/uniprot/Q61102 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||Disordered|||Exhibits siderocytosis with increased zinc protoporphyrin.|||Helical|||Iron-sulfur clusters transporter ABCB7, mitochondrial|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000093295 http://togogenome.org/gene/10090:Slc25a40 ^@ http://purl.uniprot.org/uniprot/Q8BGP6 ^@ 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.|||Probable mitochondrial glutathione transporter SLC25A40|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000291810|||http://purl.uniprot.org/annotation/VSP_026243 http://togogenome.org/gene/10090:Nxph2 ^@ http://purl.uniprot.org/uniprot/Q3KP70|||http://purl.uniprot.org/uniprot/Q61199 ^@ 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-2|||V (Cys-rich) ^@ http://purl.uniprot.org/annotation/PRO_0000020064|||http://purl.uniprot.org/annotation/PRO_5014309074 http://togogenome.org/gene/10090:Mvb12b ^@ http://purl.uniprot.org/uniprot/Q6KAU4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||MABP|||Multivesicular body subunit 12B|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||UMA ^@ http://purl.uniprot.org/annotation/PRO_0000249075 http://togogenome.org/gene/10090:Igsf6 ^@ http://purl.uniprot.org/uniprot/P0C6B7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Immunoglobulin superfamily member 6 ^@ http://purl.uniprot.org/annotation/PRO_0000320138 http://togogenome.org/gene/10090:Pes1 ^@ http://purl.uniprot.org/uniprot/Q9EQ61 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ 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|||N6-acetyllysine|||Pescadillo homolog|||Required for 28S ribosomal RNA processing|||Sufficient for interaction with MAP1B|||Sufficient for nucleolar localization ^@ http://purl.uniprot.org/annotation/PRO_0000186189 http://togogenome.org/gene/10090:Scly ^@ http://purl.uniprot.org/uniprot/A0A0R4J069|||http://purl.uniprot.org/uniprot/Q9JLI6 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Aminotransferase class V|||In isoform 2.|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine|||Phosphoserine|||S-selanylcysteine intermediate|||Selenocysteine lyase ^@ http://purl.uniprot.org/annotation/PRO_0000317013|||http://purl.uniprot.org/annotation/VSP_030855 http://togogenome.org/gene/10090:Pfkfb3 ^@ http://purl.uniprot.org/uniprot/A0A0A6YY64|||http://purl.uniprot.org/uniprot/A2AUP1|||http://purl.uniprot.org/uniprot/A2AUP5|||http://purl.uniprot.org/uniprot/A7UAK4|||http://purl.uniprot.org/uniprot/A7UAK5|||http://purl.uniprot.org/uniprot/A7UAK8|||http://purl.uniprot.org/uniprot/Q3U3S6|||http://purl.uniprot.org/uniprot/Q7TS91|||http://purl.uniprot.org/uniprot/Q8BVM1 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ 6-phosphofructo-2-kinase|||Basic and acidic residues|||Disordered|||Polar residues|||Proton donor/acceptor|||Tele-phosphohistidine intermediate ^@ http://togogenome.org/gene/10090:Ctnnal1 ^@ http://purl.uniprot.org/uniprot/O88327 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Alpha-catulin|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000064269 http://togogenome.org/gene/10090:Lmtk3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0W7|||http://purl.uniprot.org/uniprot/Q5XJV6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase LMTK3|||Significant decrease in autophosphorylation. ^@ http://purl.uniprot.org/annotation/PRO_0000259461|||http://purl.uniprot.org/annotation/PRO_5015044314 http://togogenome.org/gene/10090:Supt6 ^@ http://purl.uniprot.org/uniprot/Q3TY72|||http://purl.uniprot.org/uniprot/Q3UWU8|||http://purl.uniprot.org/uniprot/Q62383 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Interaction with IWS1|||Interaction with KDM6A|||Interaction with PAAF1|||Interaction with histone H2B and H3|||Loss of binding to POLR2A. Retains the ability to support transcription elongation but the resulting transcripts contain splicing defects and accumulate to high levels within the nucleus.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||S1 motif|||SH2|||Spt6 acidic N-terminal|||Transcription elongation factor SPT6 ^@ http://purl.uniprot.org/annotation/PRO_0000072172 http://togogenome.org/gene/10090:Or2ag2 ^@ http://purl.uniprot.org/uniprot/Q9EPF8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cyp27a1 ^@ http://purl.uniprot.org/uniprot/Q9DBG1 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Region|||Transit Peptide ^@ Disordered|||Mitochondrion|||N6-acetyllysine|||Sterol 26-hydroxylase, mitochondrial|||Sterol-binding|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000003619 http://togogenome.org/gene/10090:Atp6v0e2 ^@ http://purl.uniprot.org/uniprot/A0A0N4SVQ2|||http://purl.uniprot.org/uniprot/Q91XE7 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||V-type proton ATPase subunit e 2 ^@ http://purl.uniprot.org/annotation/PRO_0000270200 http://togogenome.org/gene/10090:Vmn2r7 ^@ http://purl.uniprot.org/uniprot/E9PZ74 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://togogenome.org/gene/10090:Txnrd2 ^@ http://purl.uniprot.org/uniprot/Q9JLT4 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non standard residue|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Helix|||Modified Residue|||Non standard residue|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Cysteinyl-selenocysteine (Cys-Sec)|||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_0000030289|||http://purl.uniprot.org/annotation/VSP_008293|||http://purl.uniprot.org/annotation/VSP_008294|||http://purl.uniprot.org/annotation/VSP_008295|||http://purl.uniprot.org/annotation/VSP_008296 http://togogenome.org/gene/10090:Aicda ^@ http://purl.uniprot.org/uniprot/Q9WVE0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ 10-fold decrease in MCM3AP-binding affinity, loss of relocalization to the nucleus in the presence of MCM3AP, decreased deamination activity to about 33% of the wild-type protein.|||Bipartite nuclear localization signal|||CMP/dCMP-type deaminase|||Important for interaction with CTNNBL1|||Interaction with SUPT6H|||Loss of the cytidine deaminase activity; when associated with Q-58.|||Loss of the cytidine deaminase activity; when associated with R-56.|||Nuclear export signal|||Phosphoserine; by PKA|||Phosphothreonine; by PKA|||Proton donor|||Required for interaction with RNF126|||Severely decreased cytidine deaminase activity. Loss of mutagenic activity.|||Single-stranded DNA cytosine deaminase ^@ http://purl.uniprot.org/annotation/PRO_0000171688 http://togogenome.org/gene/10090:Pcdha9 ^@ http://purl.uniprot.org/uniprot/Q91Y11 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||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|||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_0000431484 http://togogenome.org/gene/10090:Ywhab ^@ http://purl.uniprot.org/uniprot/A2A5N2|||http://purl.uniprot.org/uniprot/Q9CQV8 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Turn ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Turn ^@ 14-3-3|||14-3-3 protein beta/alpha|||14-3-3 protein beta/alpha, N-terminally processed|||3'-nitrotyrosine|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform Short.|||Interaction with phosphoserine on interacting protein|||N-acetylmethionine|||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_0000000005|||http://purl.uniprot.org/annotation/PRO_0000367902|||http://purl.uniprot.org/annotation/VSP_018634 http://togogenome.org/gene/10090:Ammecr1l ^@ http://purl.uniprot.org/uniprot/Q3UAR8|||http://purl.uniprot.org/uniprot/Q3V0N3|||http://purl.uniprot.org/uniprot/Q8JZZ6 ^@ 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_0000278480 http://togogenome.org/gene/10090:Il23a ^@ http://purl.uniprot.org/uniprot/Q9EQ14 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Interleukin-23 subunit alpha ^@ http://purl.uniprot.org/annotation/PRO_0000259489 http://togogenome.org/gene/10090:Mrps2 ^@ http://purl.uniprot.org/uniprot/Q8BQ99|||http://purl.uniprot.org/uniprot/Q924T2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Small ribosomal subunit protein uS2m ^@ http://purl.uniprot.org/annotation/PRO_0000134344 http://togogenome.org/gene/10090:Ccl27b ^@ http://purl.uniprot.org/uniprot/Q9Z1X0 ^@ 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 27|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000005240|||http://purl.uniprot.org/annotation/VSP_001065 http://togogenome.org/gene/10090:Gpr153 ^@ http://purl.uniprot.org/uniprot/Q8K0Z9 ^@ 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|||Polar residues|||Probable G-protein coupled receptor 153 ^@ http://purl.uniprot.org/annotation/PRO_0000069638 http://togogenome.org/gene/10090:Iffo1 ^@ http://purl.uniprot.org/uniprot/Q8BXL9 ^@ 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|||IF rod|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 6.|||LMNA binding|||Non-homologous end joining factor IFFO1|||Polar residues|||XCCR4 binding. Required for localization to the double-strand breaks (DSBs) ^@ http://purl.uniprot.org/annotation/PRO_0000316795|||http://purl.uniprot.org/annotation/VSP_030785|||http://purl.uniprot.org/annotation/VSP_030786|||http://purl.uniprot.org/annotation/VSP_030787|||http://purl.uniprot.org/annotation/VSP_030788 http://togogenome.org/gene/10090:Smpx ^@ http://purl.uniprot.org/uniprot/Q9DC77 ^@ 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|||Phosphothreonine|||Small muscular protein ^@ http://purl.uniprot.org/annotation/PRO_0000071979 http://togogenome.org/gene/10090:Pilra ^@ http://purl.uniprot.org/uniprot/Q2YFS3 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Paired immunoglobulin-like type 2 receptor alpha|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000226823|||http://purl.uniprot.org/annotation/VSP_017505 http://togogenome.org/gene/10090:Scml2 ^@ http://purl.uniprot.org/uniprot/B1AVB4|||http://purl.uniprot.org/uniprot/B1AVB5|||http://purl.uniprot.org/uniprot/I6L9E4|||http://purl.uniprot.org/uniprot/Q8BYC8 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||MBT|||Polar residues|||Polycomb group protein RNA binding region|||SLED ^@ http://togogenome.org/gene/10090:Gpha2 ^@ http://purl.uniprot.org/uniprot/A2RSW3|||http://purl.uniprot.org/uniprot/Q925Q5 ^@ 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_0000011673|||http://purl.uniprot.org/annotation/PRO_5014296823 http://togogenome.org/gene/10090:Nub1 ^@ http://purl.uniprot.org/uniprot/A0A0G2JGQ4|||http://purl.uniprot.org/uniprot/P54729|||http://purl.uniprot.org/uniprot/Q3UYM1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Strand|||Turn ^@ Acidic residues|||Disordered|||NEDD8 ultimate buster 1|||NEDD8-binding 1|||NEDD8-binding 2|||Nuclear localization signal|||Polar residues|||UBA|||UBA 1|||UBA 2|||UBA 3 ^@ http://purl.uniprot.org/annotation/PRO_0000210993 http://togogenome.org/gene/10090:Glis1 ^@ http://purl.uniprot.org/uniprot/Q8K1M4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Bipartite nuclear localization signal|||C2H2-type 1|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||Polar residues|||Zinc finger protein GLIS1 ^@ http://purl.uniprot.org/annotation/PRO_0000047210|||http://purl.uniprot.org/annotation/VSP_051623 http://togogenome.org/gene/10090:Spdye4c ^@ http://purl.uniprot.org/uniprot/I6XKQ3 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ing1 ^@ http://purl.uniprot.org/uniprot/Q3ULE3|||http://purl.uniprot.org/uniprot/Q9QXV3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||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 SUMO2)|||Histone H3K4me3 binding|||In isoform 2.|||Inhibitor of growth protein 1|||PBR|||PHD-type ^@ http://purl.uniprot.org/annotation/PRO_0000212662|||http://purl.uniprot.org/annotation/VSP_050378 http://togogenome.org/gene/10090:AY074887 ^@ http://purl.uniprot.org/uniprot/Q8R5F9 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Tcf12 ^@ http://purl.uniprot.org/uniprot/Q3TE72|||http://purl.uniprot.org/uniprot/Q3UXQ3|||http://purl.uniprot.org/uniprot/Q3UZ69|||http://purl.uniprot.org/uniprot/Q3UZA4|||http://purl.uniprot.org/uniprot/Q61286|||http://purl.uniprot.org/uniprot/V9GX46 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ BHLH|||Basic and acidic residues|||Class A specific domain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform ALF1A.|||Leucine-zipper|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription factor 12|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127230|||http://purl.uniprot.org/annotation/VSP_002105 http://togogenome.org/gene/10090:Plxdc2 ^@ http://purl.uniprot.org/uniprot/B1AY85|||http://purl.uniprot.org/uniprot/Q9DC11 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Plexin domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000234575|||http://purl.uniprot.org/annotation/PRO_5002760500 http://togogenome.org/gene/10090:Vps41 ^@ http://purl.uniprot.org/uniprot/Q5KU39 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||CHCR|||Disordered|||Interaction with ARL8B|||RING-type; atypical|||Vacuolar protein sorting-associated protein 41 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000253020 http://togogenome.org/gene/10090:Adamts10 ^@ http://purl.uniprot.org/uniprot/P58459 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ A disintegrin and metalloproteinase with thrombospondin motifs 10|||Disintegrin|||In isoform 2.|||In isoform 3.|||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_0000078211|||http://purl.uniprot.org/annotation/PRO_0000270149|||http://purl.uniprot.org/annotation/VSP_026108|||http://purl.uniprot.org/annotation/VSP_026109|||http://purl.uniprot.org/annotation/VSP_026110|||http://purl.uniprot.org/annotation/VSP_026111|||http://purl.uniprot.org/annotation/VSP_026112 http://togogenome.org/gene/10090:B3galt2 ^@ http://purl.uniprot.org/uniprot/O54905 ^@ 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 ^@ Beta-1,3-galactosyltransferase 2|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In strain: BLG2/Msf and NJL/Msf.|||In strain: BLG2/Msf, MSM/Msf, SWN/Msf and NJL/Msf.|||In strain: BLG2/Msf, NJL/Msf, MSM/Msf and SWN/Msf.|||In strain: CAST/Ei and HMI/Msf.|||In strain: HMI/Msf.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219151 http://togogenome.org/gene/10090:Pcdhb20 ^@ http://purl.uniprot.org/uniprot/Q91XZ9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099539 http://togogenome.org/gene/10090:Ercc2 ^@ http://purl.uniprot.org/uniprot/O08811 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ DEAH box|||General transcription and DNA repair factor IIH helicase subunit XPD|||Helicase ATP-binding|||Mediates interaction with MMS19 ^@ http://purl.uniprot.org/annotation/PRO_0000101981 http://togogenome.org/gene/10090:Git1 ^@ http://purl.uniprot.org/uniprot/Q68FF6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Strand|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Strand|||Zinc Finger ^@ ANK 1|||ANK 2|||ANK 3|||ARF GTPase-activating protein GIT1|||Arf-GAP|||C4-type|||Disordered|||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|||Loss of interaction with MAPK1.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Required for localization at synapses ^@ http://purl.uniprot.org/annotation/PRO_0000074201 http://togogenome.org/gene/10090:Rasal2 ^@ http://purl.uniprot.org/uniprot/E9PW37|||http://purl.uniprot.org/uniprot/Q0VAV5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2|||Disordered|||PH|||Polar residues|||Ras-GAP ^@ http://togogenome.org/gene/10090:Psmd8 ^@ http://purl.uniprot.org/uniprot/Q9CPS5|||http://purl.uniprot.org/uniprot/Q9CX56 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Region ^@ 26S proteasome non-ATPase regulatory subunit 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||PCI ^@ http://purl.uniprot.org/annotation/PRO_0000173847 http://togogenome.org/gene/10090:Naaa ^@ http://purl.uniprot.org/uniprot/G3XA18|||http://purl.uniprot.org/uniprot/Q3V023|||http://purl.uniprot.org/uniprot/Q9D7V9 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Acid ceramidase N-terminal|||Choloylglycine hydrolase/NAAA C-terminal|||Important for 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|||ceramidase ^@ http://purl.uniprot.org/annotation/PRO_0000002319|||http://purl.uniprot.org/annotation/PRO_0000419652|||http://purl.uniprot.org/annotation/PRO_0000419653|||http://purl.uniprot.org/annotation/PRO_5004230430|||http://purl.uniprot.org/annotation/PRO_5015091843 http://togogenome.org/gene/10090:Abra ^@ http://purl.uniprot.org/uniprot/Q8BUZ1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Actin-binding 1|||Actin-binding 2|||Actin-binding Rho-activating protein|||Basic and acidic residues|||Disordered|||Interaction with actin|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000247740 http://togogenome.org/gene/10090:Peli2 ^@ http://purl.uniprot.org/uniprot/Q8BST6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ E3 ubiquitin-protein ligase pellino homolog 2|||FHA; atypical|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000194175|||http://purl.uniprot.org/annotation/VSP_008636|||http://purl.uniprot.org/annotation/VSP_008637|||http://purl.uniprot.org/annotation/VSP_008638 http://togogenome.org/gene/10090:Ugt2b38 ^@ http://purl.uniprot.org/uniprot/Q91WH2 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099524 http://togogenome.org/gene/10090:Plekhg1 ^@ http://purl.uniprot.org/uniprot/Q3UX37|||http://purl.uniprot.org/uniprot/Q3V3S7 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||DH|||Disordered|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Spag6l ^@ http://purl.uniprot.org/uniprot/Q9JLI7 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||Sperm-associated antigen 6 ^@ http://purl.uniprot.org/annotation/PRO_0000072096 http://togogenome.org/gene/10090:Nbeal1 ^@ http://purl.uniprot.org/uniprot/E9PYP2|||http://purl.uniprot.org/uniprot/Q8BS04 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat ^@ BEACH|||BEACH-type PH|||DUF4704|||Disordered|||Polar residues|||WD ^@ http://togogenome.org/gene/10090:Rffl ^@ http://purl.uniprot.org/uniprot/Q148A8|||http://purl.uniprot.org/uniprot/Q3TEV8|||http://purl.uniprot.org/uniprot/Q3UCG9|||http://purl.uniprot.org/uniprot/Q3UD78|||http://purl.uniprot.org/uniprot/Q6ZQM0 ^@ 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 ^@ Disordered|||E3 ubiquitin-protein ligase rififylin|||FYVE-type|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 4.|||Phosphoserine|||Polar residues|||RING-type|||SAP 1|||SAP 2 ^@ http://purl.uniprot.org/annotation/PRO_0000056026|||http://purl.uniprot.org/annotation/VSP_015753|||http://purl.uniprot.org/annotation/VSP_015754|||http://purl.uniprot.org/annotation/VSP_015755|||http://purl.uniprot.org/annotation/VSP_015756 http://togogenome.org/gene/10090:Colec12 ^@ http://purl.uniprot.org/uniprot/Q8K4Q8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||Collagen-like 1|||Collagen-like 2|||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_0000318682 http://togogenome.org/gene/10090:Or51q1 ^@ http://purl.uniprot.org/uniprot/K7N6B1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ces2h ^@ http://purl.uniprot.org/uniprot/F6Z9B9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Carboxylesterase type B|||Carboxylic ester hydrolase ^@ http://purl.uniprot.org/annotation/PRO_5005130027 http://togogenome.org/gene/10090:Scn4a ^@ http://purl.uniprot.org/uniprot/G3X8T7|||http://purl.uniprot.org/uniprot/Q9ER60 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ A very low percentage of homozygous mice are present at 30 days after birth, suggesting high perinatal lethality. In anesthesized heterozygous mice, electromyographs from hind-limb muscle show high background activity, indicative of myotonia. Isolated extensor digitorum longus muscle from heterozygous mice displays reduced twitch force, with a normal speed of muscle contraction, but an increased muscle relaxation half-time. Isolated skeletal muscle from heterozygous mice has strongly decreased force when the K(+) levels are increased to 10 mM. Homozygous mice display prominent hind-limb weakness and muscle atrophy.|||Acidic residues|||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|||Homozygous mice are born at the expected Mendelian rate and have no visible phenotype. Hind-limb muscles show decreased excitability and decreased force when K(+) levels are low (in vivo). Isolated soleus muscle from homozygous mice has an increased susceptibility to loss of force generation at 2 mMK(+).|||I|||II|||III|||IQ|||IV|||Important for inhibition by tetrodotoxin|||Important for rapid channel inactivation|||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; by PKC|||Pore-forming|||Pro residues|||Sodium channel protein type 4 subunit alpha|||Sodium ion transport-associated ^@ http://purl.uniprot.org/annotation/PRO_0000371316 http://togogenome.org/gene/10090:Zfp768 ^@ http://purl.uniprot.org/uniprot/Q8R0T2 ^@ 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 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|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Zinc finger protein 768 ^@ http://purl.uniprot.org/annotation/PRO_0000304409 http://togogenome.org/gene/10090:Or4c15b ^@ http://purl.uniprot.org/uniprot/Q7TQZ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gm4922 ^@ http://purl.uniprot.org/uniprot/Q8C0N0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Protein kinase|||Proton acceptor|||Sperm motility kinase Z|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000307877 http://togogenome.org/gene/10090:Bmf ^@ http://purl.uniprot.org/uniprot/Q91ZE9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure ^@ Chain|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region ^@ Acidic residues|||BH3|||Bcl-2-modifying factor|||Decrease in the interaction with BCL2 and BCL2L2.|||Disordered|||Interaction with DLC2|||Loss of interaction with DLC2. ^@ http://purl.uniprot.org/annotation/PRO_0000143112 http://togogenome.org/gene/10090:Ep400 ^@ http://purl.uniprot.org/uniprot/Q8CHI8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||DEAD box-like|||Disordered|||E1A-binding protein p400|||HSA|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||Interaction with ZNF42|||Interactions with RUVBL1 and RUVBL2|||Myb-like|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000074313|||http://purl.uniprot.org/annotation/VSP_011996|||http://purl.uniprot.org/annotation/VSP_011997|||http://purl.uniprot.org/annotation/VSP_011998|||http://purl.uniprot.org/annotation/VSP_017127 http://togogenome.org/gene/10090:Rhob ^@ http://purl.uniprot.org/uniprot/P62746 ^@ 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|||Phosphotyrosine|||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_0000030419|||http://purl.uniprot.org/annotation/PRO_0000030420 http://togogenome.org/gene/10090:Utp4 ^@ http://purl.uniprot.org/uniprot/Q8R2N2 ^@ Chain|||Crosslink|||Modification|||Molecule Processing|||Region|||Repeat ^@ Chain|||Crosslink|||Repeat ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||U3 small nucleolar RNA-associated protein 4 homolog|||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_0000050909 http://togogenome.org/gene/10090:Ell3 ^@ http://purl.uniprot.org/uniprot/Q80VR2 ^@ 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|||OCEL|||Phosphoserine|||RNA polymerase II elongation factor ELL3 ^@ http://purl.uniprot.org/annotation/PRO_0000146737 http://togogenome.org/gene/10090:Clasp2 ^@ http://purl.uniprot.org/uniprot/A2RRR3|||http://purl.uniprot.org/uniprot/B9EJA4|||http://purl.uniprot.org/uniprot/E9Q8N5|||http://purl.uniprot.org/uniprot/Q08EB5|||http://purl.uniprot.org/uniprot/Q08EB6|||http://purl.uniprot.org/uniprot/Q3UF57|||http://purl.uniprot.org/uniprot/Q8BRT1|||http://purl.uniprot.org/uniprot/Q8BSE7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||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|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||CLIP-associating protein 2|||Disordered|||Golgi localization|||HEAT|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||Impairs Golgi localization; when associated with S-10.|||Impairs Golgi localization; when associated with S-6.|||In isoform 2.|||In isoform 3.|||Interaction with RSN and localization to the Golgi and kinetochores|||Interaction with microtubules, MAPRE1 and MAPRE3|||Phosphoserine|||Phosphothreonine|||Polar residues|||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_0000089850|||http://purl.uniprot.org/annotation/VSP_015808|||http://purl.uniprot.org/annotation/VSP_015809|||http://purl.uniprot.org/annotation/VSP_015810|||http://purl.uniprot.org/annotation/VSP_015811|||http://purl.uniprot.org/annotation/VSP_015812 http://togogenome.org/gene/10090:Cyp4a29 ^@ http://purl.uniprot.org/uniprot/A0A087WPC3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Or52l1 ^@ http://purl.uniprot.org/uniprot/Q7TRN7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kcns3 ^@ http://purl.uniprot.org/uniprot/Q8BQZ8 ^@ 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 3|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000320143 http://togogenome.org/gene/10090:Fig4 ^@ http://purl.uniprot.org/uniprot/Q91WF7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Polyphosphoinositide phosphatase|||SAC ^@ http://purl.uniprot.org/annotation/PRO_0000209744 http://togogenome.org/gene/10090:Lipf ^@ http://purl.uniprot.org/uniprot/Q9CPP7 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ AB hydrolase-1|||Charge relay system|||Gastric triacylglycerol lipase|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000017767 http://togogenome.org/gene/10090:Srcap ^@ http://purl.uniprot.org/uniprot/A0A087WQ44 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||HSA|||Helicase ATP-binding|||Helicase C-terminal|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Plekhn1 ^@ http://purl.uniprot.org/uniprot/E9QP36 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Sdk2 ^@ http://purl.uniprot.org/uniprot/Q6V4S5 ^@ Chain|||Compositionally Biased Region|||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|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes localization to synapses and induces diffuse expression in photoreceptor cells.|||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|||Polar residues|||Protein sidekick-2 ^@ http://purl.uniprot.org/annotation/PRO_0000226979|||http://purl.uniprot.org/annotation/VSP_017526|||http://purl.uniprot.org/annotation/VSP_017527|||http://purl.uniprot.org/annotation/VSP_017528 http://togogenome.org/gene/10090:Map2 ^@ http://purl.uniprot.org/uniprot/P20357|||http://purl.uniprot.org/uniprot/Q3TLQ0|||http://purl.uniprot.org/uniprot/Q3URJ7|||http://purl.uniprot.org/uniprot/Q80ZL4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Calmodulin-binding|||Disordered|||Interaction with KNDC1|||MAP2/Tau projection|||Microtubule-associated protein 2|||Phosphoserine|||Phosphoserine; by MARK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RII binding|||Tau/MAP 1|||Tau/MAP 2|||Tau/MAP 3 ^@ http://purl.uniprot.org/annotation/PRO_0000072748 http://togogenome.org/gene/10090:Or52ac1 ^@ http://purl.uniprot.org/uniprot/E9Q252 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp385a ^@ http://purl.uniprot.org/uniprot/A0A2R8VHX5|||http://purl.uniprot.org/uniprot/Q8VD12 ^@ 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|||Disordered|||In isoform 2.|||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_0000422970|||http://purl.uniprot.org/annotation/VSP_047450 http://togogenome.org/gene/10090:Edn2 ^@ http://purl.uniprot.org/uniprot/P22389 ^@ Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage; by KEL|||Endothelin-2|||Endothelin-like ^@ http://purl.uniprot.org/annotation/PRO_0000008099|||http://purl.uniprot.org/annotation/PRO_0000008100|||http://purl.uniprot.org/annotation/PRO_0000008101 http://togogenome.org/gene/10090:Stoml2 ^@ http://purl.uniprot.org/uniprot/Q99JB2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by PKC/PRKCZ|||Phosphotyrosine|||Polar residues|||Stomatin-like protein 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000094032 http://togogenome.org/gene/10090:Apol11a ^@ http://purl.uniprot.org/uniprot/E9PZG0 ^@ Coiled-Coil|||Region ^@ Coiled-Coil|||Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Bnipl ^@ http://purl.uniprot.org/uniprot/E9Q8I3|||http://purl.uniprot.org/uniprot/E9QME1|||http://purl.uniprot.org/uniprot/Q3UQG4 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||CRAL-TRIO|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Tle3 ^@ http://purl.uniprot.org/uniprot/E0CXS9|||http://purl.uniprot.org/uniprot/F8WIE2|||http://purl.uniprot.org/uniprot/Q08122|||http://purl.uniprot.org/uniprot/Q80TC1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||CcN domain|||Disordered|||GP domain|||Groucho/TLE N-terminal Q-rich|||In isoform 1.|||In isoform 2.|||In isoform 4.|||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_0000051281|||http://purl.uniprot.org/annotation/VSP_007025|||http://purl.uniprot.org/annotation/VSP_038441|||http://purl.uniprot.org/annotation/VSP_038442 http://togogenome.org/gene/10090:Pcnx ^@ http://purl.uniprot.org/uniprot/A0A1Y7VKR5|||http://purl.uniprot.org/uniprot/Q9QYC1 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Pecanex C-terminal|||Pecanex-like protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000215794|||http://purl.uniprot.org/annotation/VSP_022167 http://togogenome.org/gene/10090:Intu ^@ http://purl.uniprot.org/uniprot/Q059U7 ^@ 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.|||PDZ|||Phosphoserine|||Polar residues|||Protein inturned ^@ http://purl.uniprot.org/annotation/PRO_0000416283|||http://purl.uniprot.org/annotation/VSP_042603|||http://purl.uniprot.org/annotation/VSP_042604|||http://purl.uniprot.org/annotation/VSP_042605 http://togogenome.org/gene/10090:Tspan17 ^@ http://purl.uniprot.org/uniprot/Q3TAQ3|||http://purl.uniprot.org/uniprot/Q9D7W4 ^@ 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-17 ^@ http://purl.uniprot.org/annotation/PRO_0000219266 http://togogenome.org/gene/10090:Fam53a ^@ http://purl.uniprot.org/uniprot/E9PV82 ^@ 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_0000440956 http://togogenome.org/gene/10090:Rhox8 ^@ http://purl.uniprot.org/uniprot/Q6VSS7 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Nkd1 ^@ http://purl.uniprot.org/uniprot/E9Q5K6|||http://purl.uniprot.org/uniprot/Q99MH6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||EF-hand|||Impairs inhibition of the Wnt signaling pathway.|||Impairs inhibition of the Wnt signaling pathway; when associated with V-144.|||Impairs inhibition of the Wnt signaling pathway; when associated with V-146.|||Interaction with DVL1, DVL2 and DVL3|||N-myristoyl glycine|||Polar residues|||Protein naked cuticle homolog 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000301991 http://togogenome.org/gene/10090:Ccdc68 ^@ http://purl.uniprot.org/uniprot/Q8BVC4 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Splice Variant ^@ Coiled-coil domain-containing protein 68|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000264612|||http://purl.uniprot.org/annotation/VSP_021897 http://togogenome.org/gene/10090:Phf13 ^@ http://purl.uniprot.org/uniprot/Q3V230|||http://purl.uniprot.org/uniprot/Q8K2W6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||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_0000059305 http://togogenome.org/gene/10090:Nefm ^@ http://purl.uniprot.org/uniprot/A0A0R4J036|||http://purl.uniprot.org/uniprot/P08553 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2A|||Coil 2B|||Disordered|||Head|||IF rod|||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_0000063795 http://togogenome.org/gene/10090:Clpb ^@ http://purl.uniprot.org/uniprot/Q3URM1|||http://purl.uniprot.org/uniprot/Q60649 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Site|||Transit Peptide ^@ AAA+ ATPase|||ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Autoinhibitory|||Cleavage; by PARL|||Clp ATPase C-terminal|||Disordered|||Mitochondrial disaggregase|||Mitochondrial disaggregase, cleaved form|||Mitochondrion|||N6-acetyllysine|||Regulatory; slows ATPase and disaggregase activities ^@ http://purl.uniprot.org/annotation/PRO_0000191240|||http://purl.uniprot.org/annotation/PRO_0000458242 http://togogenome.org/gene/10090:Sh3d19 ^@ http://purl.uniprot.org/uniprot/A0A571BGG1|||http://purl.uniprot.org/uniprot/Q91X43 ^@ 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.|||Phosphoserine|||Polar residues|||Pro residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||SH3 5|||SH3 domain-containing protein 19 ^@ http://purl.uniprot.org/annotation/PRO_0000318198|||http://purl.uniprot.org/annotation/VSP_031185 http://togogenome.org/gene/10090:Slc7a10 ^@ http://purl.uniprot.org/uniprot/P63115 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Asc-type amino acid transporter 1|||Disordered|||Helical|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000054277 http://togogenome.org/gene/10090:Zfp974 ^@ http://purl.uniprot.org/uniprot/Q3UVF6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Dnajb8 ^@ http://purl.uniprot.org/uniprot/Q9QYI7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ DnaJ homolog subfamily B member 8|||J ^@ http://purl.uniprot.org/annotation/PRO_0000071030 http://togogenome.org/gene/10090:Itpk1 ^@ http://purl.uniprot.org/uniprot/Q8BYN3 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ ATP-grasp|||Inositol-tetrakisphosphate 1-kinase|||N6-acetyllysine; by EP300 and CREBBP|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000220834 http://togogenome.org/gene/10090:Sod1 ^@ http://purl.uniprot.org/uniprot/P08228 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Removed|||S-palmitoyl cysteine|||Superoxide dismutase [Cu-Zn] ^@ http://purl.uniprot.org/annotation/PRO_0000164062 http://togogenome.org/gene/10090:Defb48 ^@ http://purl.uniprot.org/uniprot/Q3UW22 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015097505 http://togogenome.org/gene/10090:Xrcc4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J024|||http://purl.uniprot.org/uniprot/Q924T3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||DNA repair protein XRCC4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-193, A-254, A-295, A-307, A-312, A-315, A-319 and A-320.|||In 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-295, A-307, A-312, A-315 and A-319.|||In 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-295, A-307, A-312, A-315 and A-320.|||In 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-295, A-307, A-312, A-319 and A-320.|||In 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-295, A-307, A-315, A-319 and A-320.|||In 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-295, A-312, A-315, A-319 and A-320.|||In 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-254, A-307, A-312, A-315, A-319 and A-320.|||In 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-193, A-295, A-307, A-312, A-315, A-319 and A-320.|||In 9A mutant; abolished phosphorylation by PRKDC; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with NHEJ1/XLF phosphorylation sites; when associated with A-53, A-254, A-295, A-307, A-312, A-315, A-319 and A-320.|||In isoform 2.|||Interaction with IFFO1|||Interaction with LIG4|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PRKDC|||Phosphothreonine|||Phosphothreonine; by PRKDC|||Phosphotyrosine|||Polar residues|||Protein XRCC4, C-terminus ^@ http://purl.uniprot.org/annotation/PRO_0000066048|||http://purl.uniprot.org/annotation/PRO_0000453297|||http://purl.uniprot.org/annotation/VSP_009475 http://togogenome.org/gene/10090:Nxnl1 ^@ http://purl.uniprot.org/uniprot/Q8VC33 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Nucleoredoxin-like protein 1|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000319544 http://togogenome.org/gene/10090:Sprr2k ^@ http://purl.uniprot.org/uniprot/O70562 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1; truncated|||2|||3|||3.5 X 9 AA approximate tandem repeats|||4|||Small proline-rich protein 2K ^@ http://purl.uniprot.org/annotation/PRO_0000150023 http://togogenome.org/gene/10090:Bdkrb2 ^@ http://purl.uniprot.org/uniprot/P32299 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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_0000069191|||http://purl.uniprot.org/annotation/VSP_001866 http://togogenome.org/gene/10090:Wls ^@ http://purl.uniprot.org/uniprot/Q6DID7 ^@ 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|||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.|||Interaction with Wnt proteins|||Knockin mice have several structural anomalies recapitulating the major defects observed in patients with Zaki syndrome.|||Lumenal|||Protein wntless homolog ^@ http://purl.uniprot.org/annotation/PRO_0000271779|||http://purl.uniprot.org/annotation/VSP_022348 http://togogenome.org/gene/10090:Fabp6 ^@ http://purl.uniprot.org/uniprot/P51162 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Gastrotropin|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067381 http://togogenome.org/gene/10090:Arhgef16 ^@ http://purl.uniprot.org/uniprot/Q3U5C8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||DH|||Disordered|||PDZ-binding motif|||PH|||Phosphoserine|||Phosphothreonine|||Pro residues|||Required for RHOG activation and mediates interaction with EPHA2|||Rho guanine nucleotide exchange factor 16|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000233691 http://togogenome.org/gene/10090:Hnrnpa0 ^@ http://purl.uniprot.org/uniprot/Q9CX86 ^@ 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_0000415269 http://togogenome.org/gene/10090:Trim62 ^@ http://purl.uniprot.org/uniprot/Q80V85 ^@ 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|||E3 ubiquitin-protein ligase TRIM62|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000249575 http://togogenome.org/gene/10090:Or6f2 ^@ http://purl.uniprot.org/uniprot/Q8VFE7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gdf5 ^@ http://purl.uniprot.org/uniprot/P43027|||http://purl.uniprot.org/uniprot/Q8BRW9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Growth/differentiation factor 5|||Interchain|||N-linked (GlcNAc...) asparagine|||Polar residues|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033914|||http://purl.uniprot.org/annotation/PRO_0000033915 http://togogenome.org/gene/10090:Gm28553 ^@ http://purl.uniprot.org/uniprot/A0A9L6KDW0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Tas1r3 ^@ http://purl.uniprot.org/uniprot/Q925D8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||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|||In strain: 129/J, 129/SvEv, AKR/J, BALB/c, C3H/HeJ, CAST/Ei, DBA/2J, FVB/N, ST/bJ and SWR/J.|||In strain: 129/J, 129/SvEv, AKR/J, BALB/c, C3H/HeJ, DBA/2J and DBA/2J.|||In strain: 129/J, 129/SvEv, AKR/J, BALB/c, C3H/HeJ, DBA/2J and DBA/2J; may influence the ability to form dimers or bind sweeteners.|||In strain: 129/J, 129/SvEv, AKR/J, BALB/c, C3H/HeJ, DBA/2J, DBA/2J, FVB/N, ST/bJ and SWR/J.|||In strain: 129/J, 129/SvEv, AKR/J, BALB/c, CAST/Ei, C3H/HeJ, DBA/2J, FVB/N, ST/bJ and SWR/J.|||In strain: 129/J, AKR/J, CAST/Ei, DBA/2J and SWR/J.|||In strain: FVB/N, ST/bJ and SWR/J.|||In strain: FVB/N, ST/bJ, SWR/J.|||In strain: SWR/J.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; when associated with variant T-60|||Taste receptor type 1 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000012962 http://togogenome.org/gene/10090:Ly75 ^@ http://purl.uniprot.org/uniprot/Q60767 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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 lectin 9|||Cytoplasmic|||Extracellular|||Fibronectin type-II|||Helical|||Lymphocyte antigen 75|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000017554 http://togogenome.org/gene/10090:Mapk1ip1l ^@ http://purl.uniprot.org/uniprot/Q8BH93 ^@ 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 ^@ Disordered|||MAPK-interacting and spindle-stabilizing protein-like|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000209892 http://togogenome.org/gene/10090:Capn1 ^@ http://purl.uniprot.org/uniprot/O35350|||http://purl.uniprot.org/uniprot/Q3TB79|||http://purl.uniprot.org/uniprot/Q3TI07|||http://purl.uniprot.org/uniprot/Q3UF24 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ 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|||Linker|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000207696 http://togogenome.org/gene/10090:Bcl2l12 ^@ http://purl.uniprot.org/uniprot/Q9D3J3 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Tgm5 ^@ http://purl.uniprot.org/uniprot/Q9D7I9 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylalanine|||Protein-glutamine gamma-glutamyltransferase 5|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213714 http://togogenome.org/gene/10090:Reep3 ^@ http://purl.uniprot.org/uniprot/A0A1W2P8A8|||http://purl.uniprot.org/uniprot/Q99KK1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Receptor expression-enhancing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000101827 http://togogenome.org/gene/10090:Usf2 ^@ http://purl.uniprot.org/uniprot/Q64705 ^@ 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 USF2B.|||Leucine-zipper|||Upstream stimulatory factor 2|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127501|||http://purl.uniprot.org/annotation/VSP_002166 http://togogenome.org/gene/10090:1810009J06Rik ^@ http://purl.uniprot.org/uniprot/Q9CPN7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015099697 http://togogenome.org/gene/10090:Vmn1r84 ^@ http://purl.uniprot.org/uniprot/Q8R284 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gatad2a ^@ http://purl.uniprot.org/uniprot/E9QMN5|||http://purl.uniprot.org/uniprot/Q8CHY6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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|||GATA-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with ZMYND8|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcriptional repressor p66 alpha|||Transcriptional repressor p66 coiled-coil MBD2-interaction ^@ http://purl.uniprot.org/annotation/PRO_0000083501 http://togogenome.org/gene/10090:Mfsd1 ^@ http://purl.uniprot.org/uniprot/Q9DC37 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Transmembrane ^@ Dileucine internalization motif|||Helical|||Major facilitator superfamily domain-containing protein 1|||Mislocalization to the plasma membrane. Localizes to lysosomes when expressed with wild-type Glmp.|||No change in molecular weight, indicating lack of N-glycosylation.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000273383 http://togogenome.org/gene/10090:Adam18 ^@ http://purl.uniprot.org/uniprot/Q9R157 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 18|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B ^@ http://purl.uniprot.org/annotation/PRO_0000029100|||http://purl.uniprot.org/annotation/PRO_0000029101 http://togogenome.org/gene/10090:Hcn3 ^@ http://purl.uniprot.org/uniprot/B2RRB5|||http://purl.uniprot.org/uniprot/O88705 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||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|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000054115 http://togogenome.org/gene/10090:AA467197 ^@ http://purl.uniprot.org/uniprot/Q3UCF3|||http://purl.uniprot.org/uniprot/Q810Q5 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Normal mucosa of esophagus-specific gene 1 protein ^@ http://purl.uniprot.org/annotation/PRO_0000118824 http://togogenome.org/gene/10090:Efl1 ^@ http://purl.uniprot.org/uniprot/Q8C0D5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Elongation factor-like GTPase 1|||N6-acetyllysine|||Polar residues|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000313806 http://togogenome.org/gene/10090:Serpinb5 ^@ http://purl.uniprot.org/uniprot/P70124 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Site ^@ Chain|||Glycosylation Site|||Site ^@ N-linked (GlcNAc...) asparagine|||Reactive bond homolog|||Serpin B5 ^@ http://purl.uniprot.org/annotation/PRO_0000032487 http://togogenome.org/gene/10090:Osbpl6 ^@ http://purl.uniprot.org/uniprot/F8WIZ7|||http://purl.uniprot.org/uniprot/Q8BXR9 ^@ 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 ^@ Disordered|||In isoform 2.|||N-acetylserine|||Oxysterol-binding protein-related protein 6|||PH|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000100376|||http://purl.uniprot.org/annotation/VSP_010012 http://togogenome.org/gene/10090:Zfp790 ^@ http://purl.uniprot.org/uniprot/Q80ZX2 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Ifi202b ^@ http://purl.uniprot.org/uniprot/Q9R002 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ Abolished DNA-binding.|||Abolished homomultimerization.|||Disordered|||Does not affect DNA-binding.|||Does not affect DNA-binding. Strongly reduces affinity for DNA; when associated with A-76 and A-79.|||HIN-200 1|||HIN-200 2|||Impaired homotetramerization.|||Interferon-activable protein 202|||Loss of interaction with TP53BP1; when associated with F-283.|||Loss of interaction with TP53BP1; when associated with F-84.|||Mediates interaction with TP53BP1|||Polar residues|||Promotes formation of a homodimer.|||Reduced DNA-binding.|||Reduced DNA-binding. Strongly reduces affinity for DNA; when associated with A-48 and W-54.|||Reduced DNA-binding. Strongly reduces affinity for DNA; when associated with A-53 and W-54.|||Required for homomultimerization|||Strongly reduces affinity for DNA.|||Strongly reduces affinity for DNA; when associated with A-166; A-227 and A-229.|||Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-227.|||Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-229.|||Strongly reduces affinity for DNA; when associated with A-187 and A-189.|||Strongly reduces affinity for DNA; when associated with A-187 and A-198.|||Strongly reduces affinity for DNA; when associated with A-189 and A-198.|||Strongly reduces affinity for DNA; when associated with A-48 and A-53.|||Strongly reduces affinity for DNA; when associated with A-76 and A-236.|||Strongly reduces affinity for DNA; when associated with A-79 and A-236.|||Strongly reduces affinity for DNA; when associated with. ^@ http://purl.uniprot.org/annotation/PRO_0000153719 http://togogenome.org/gene/10090:Fhip2b ^@ http://purl.uniprot.org/uniprot/Q80YR2 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||FHF complex subunit HOOK-interacting protein 2B|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000284646|||http://purl.uniprot.org/annotation/VSP_024588|||http://purl.uniprot.org/annotation/VSP_024589 http://togogenome.org/gene/10090:Dusp19 ^@ http://purl.uniprot.org/uniprot/Q99N12 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://togogenome.org/gene/10090:Krtap19-2 ^@ http://purl.uniprot.org/uniprot/Q925I0 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ 48 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 19-2 ^@ http://purl.uniprot.org/annotation/PRO_0000356212 http://togogenome.org/gene/10090:Ddc ^@ http://purl.uniprot.org/uniprot/O88533|||http://purl.uniprot.org/uniprot/Q5SUV8 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Repeat ^@ 1|||2|||2 X approximate tandem repeats|||Aromatic-L-amino-acid decarboxylase|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_0000146940 http://togogenome.org/gene/10090:Ap4b1 ^@ http://purl.uniprot.org/uniprot/B0V3P4|||http://purl.uniprot.org/uniprot/Q7TND3|||http://purl.uniprot.org/uniprot/Q9D8S2|||http://purl.uniprot.org/uniprot/Q9WV76 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ AP-4 complex subunit beta-1|||Beta-adaptin appendage C-terminal subdomain|||Ear; mediates interaction with TEPSIN|||Hinge ^@ http://purl.uniprot.org/annotation/PRO_0000193751 http://togogenome.org/gene/10090:Sparcl1 ^@ http://purl.uniprot.org/uniprot/P70663|||http://purl.uniprot.org/uniprot/Q3TYD5|||http://purl.uniprot.org/uniprot/Q3UYK7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Disordered|||EF-hand|||Follistatin-like|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||SPARC-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000020313|||http://purl.uniprot.org/annotation/PRO_5004229814|||http://purl.uniprot.org/annotation/PRO_5004230403 http://togogenome.org/gene/10090:Kat6b ^@ http://purl.uniprot.org/uniprot/A0A5F8MQ39|||http://purl.uniprot.org/uniprot/Q3UH94|||http://purl.uniprot.org/uniprot/Q501M5|||http://purl.uniprot.org/uniprot/Q8BRB7 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||C2HC MYST-type|||Catalytic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H15|||Histone acetyltransferase KAT6B|||In isoform 2.|||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_0000051577|||http://purl.uniprot.org/annotation/VSP_014592 http://togogenome.org/gene/10090:Pnn ^@ http://purl.uniprot.org/uniprot/O35691|||http://purl.uniprot.org/uniprot/Q3TUQ5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||Omega-N-methylarginine|||Phosphoserine|||Pinin|||Pinin/SDK|||Pinin/SDK/MemA protein|||Polar residues|||Pro residues|||Removed|||Sufficient for PSAP complex assembly ^@ http://purl.uniprot.org/annotation/PRO_0000190243 http://togogenome.org/gene/10090:Krt5 ^@ http://purl.uniprot.org/uniprot/Q32P04|||http://purl.uniprot.org/uniprot/Q922U2 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Decreases phosphorylation by AURKB.|||Decreases phosphorylation by CDK1.|||Disordered|||Head|||IF rod|||Keratin, type II cytoskeletal 5|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine; by AURKB|||Phosphothreonine; by CDK1|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063728 http://togogenome.org/gene/10090:Epb41l5 ^@ http://purl.uniprot.org/uniprot/Q8BGS1 ^@ 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 ^@ Band 4.1-like protein 5|||Disordered|||FERM|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Required for interaction with CRB1 ^@ http://purl.uniprot.org/annotation/PRO_0000330355|||http://purl.uniprot.org/annotation/VSP_033039|||http://purl.uniprot.org/annotation/VSP_033040|||http://purl.uniprot.org/annotation/VSP_033041 http://togogenome.org/gene/10090:Pjvk ^@ http://purl.uniprot.org/uniprot/Q0ZLH2 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Mutagenesis Site ^@ Abolished interaction with MAP1LC3B and subsequent pexophagy.|||Does not affect interaction with MAP1LC3B.|||Induces abnormal auditory brainstem responses indicative of neuronal dysfunction along the auditory pathway.|||Pejvakin ^@ http://purl.uniprot.org/annotation/PRO_0000249043 http://togogenome.org/gene/10090:Lyg2 ^@ http://purl.uniprot.org/uniprot/Q3V1I0 ^@ Active Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Signal Peptide ^@ Lysozyme g-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000287122 http://togogenome.org/gene/10090:Tra2a ^@ http://purl.uniprot.org/uniprot/A0A0N4SVC2|||http://purl.uniprot.org/uniprot/E9QP00 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||RRM ^@ http://togogenome.org/gene/10090:Or4k15b ^@ http://purl.uniprot.org/uniprot/Q05A45 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vapa ^@ http://purl.uniprot.org/uniprot/Q9WV55 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||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_0000213471 http://togogenome.org/gene/10090:4930523C07Rik ^@ http://purl.uniprot.org/uniprot/E9Q2T4|||http://purl.uniprot.org/uniprot/Q8CE67 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Slc17a3 ^@ http://purl.uniprot.org/uniprot/G3UWD9|||http://purl.uniprot.org/uniprot/Q5SZ92 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:C8a ^@ http://purl.uniprot.org/uniprot/A2A997|||http://purl.uniprot.org/uniprot/A2A998|||http://purl.uniprot.org/uniprot/Q8K182 ^@ 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|||Region|||Sequence Variant|||Signal Peptide ^@ C-linked (Man) tryptophan|||Complement component C8 alpha chain|||Disordered|||EGF-like|||In strain: BALB/c.|||In strain: BALB/c; requires 2 nucleotide substitutions.|||In strain: Mae/Stm.|||Interchain (with C-60 in C8-gamma chain)|||LDL-receptor class A|||MACPF|||N-linked (GlcNAc...) asparagine|||TSP type-1 1|||TSP type-1 2 ^@ http://purl.uniprot.org/annotation/PRO_0000023587|||http://purl.uniprot.org/annotation/PRO_0000023588|||http://purl.uniprot.org/annotation/PRO_5002642438 http://togogenome.org/gene/10090:Vmn1r60 ^@ http://purl.uniprot.org/uniprot/G3UY47 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Arl13a ^@ http://purl.uniprot.org/uniprot/Q9D416 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ ADP-ribosylation factor-like protein 13A ^@ http://purl.uniprot.org/annotation/PRO_0000284146 http://togogenome.org/gene/10090:Gpr174 ^@ http://purl.uniprot.org/uniprot/Q3U507 ^@ 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 174 ^@ http://purl.uniprot.org/annotation/PRO_0000069655 http://togogenome.org/gene/10090:Cln8 ^@ http://purl.uniprot.org/uniprot/Q542J5|||http://purl.uniprot.org/uniprot/Q9QUK3 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Motif|||Region|||Transmembrane ^@ Disordered|||ER-retrieval signal|||Helical|||Protein CLN8|||TLC ^@ http://purl.uniprot.org/annotation/PRO_0000185538 http://togogenome.org/gene/10090:Tmem9b ^@ http://purl.uniprot.org/uniprot/Q9JJR8 ^@ 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|||Phosphoserine|||Transmembrane protein 9B ^@ http://purl.uniprot.org/annotation/PRO_0000045787 http://togogenome.org/gene/10090:Or6c5 ^@ http://purl.uniprot.org/uniprot/Q7TRI5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mybpc1 ^@ http://purl.uniprot.org/uniprot/D3YU50|||http://purl.uniprot.org/uniprot/Q6P6L5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Fibronectin type-III|||Ig-like ^@ http://togogenome.org/gene/10090:Chst9 ^@ http://purl.uniprot.org/uniprot/Q76EC5 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 9|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000189656 http://togogenome.org/gene/10090:B230219D22Rik ^@ http://purl.uniprot.org/uniprot/Q80X32 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||UPF0461 protein C5orf24 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000295709 http://togogenome.org/gene/10090:Gtpbp4 ^@ http://purl.uniprot.org/uniprot/Q99ME9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||N-acetylalanine|||N6-acetyllysine; alternate|||OBG-type G|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000195024 http://togogenome.org/gene/10090:Strada ^@ http://purl.uniprot.org/uniprot/Q3UUJ4 ^@ 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 and isoform 3.|||In isoform 2.|||Phosphoserine|||Phosphothreonine; by LKB1|||Polar residues|||Protein kinase|||STE20-related kinase adapter protein alpha ^@ http://purl.uniprot.org/annotation/PRO_0000260037|||http://purl.uniprot.org/annotation/VSP_052217|||http://purl.uniprot.org/annotation/VSP_052218 http://togogenome.org/gene/10090:Prr18 ^@ http://purl.uniprot.org/uniprot/Q6PAN7 ^@ 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.|||Omega-N-methylarginine|||Phosphoserine|||Pro residues|||Proline-rich protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000307748|||http://purl.uniprot.org/annotation/VSP_028816 http://togogenome.org/gene/10090:Mon1a ^@ http://purl.uniprot.org/uniprot/A0A0R4J0D5|||http://purl.uniprot.org/uniprot/Q6PDG8 ^@ 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|||FUZ/MON1/HPS1 first Longin|||FUZ/MON1/HPS1 second Longin|||FUZ/MON1/HPS1 third Longin|||In isoform 2.|||In strain: C57BL.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Vacuolar fusion protein MON1 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000285763|||http://purl.uniprot.org/annotation/VSP_024913|||http://purl.uniprot.org/annotation/VSP_024914 http://togogenome.org/gene/10090:Or8s10 ^@ http://purl.uniprot.org/uniprot/A1L1B4 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Domain Extent|||Non-terminal Residue|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dynlt2a2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J284|||http://purl.uniprot.org/uniprot/P11985 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Disordered|||Dynein light chain Tctex-type protein 2|||In T-haplotype.|||In isoform 2.|||Requires 2 nucleotide substitutions; in T-haplotype. ^@ http://purl.uniprot.org/annotation/PRO_0000072471|||http://purl.uniprot.org/annotation/VSP_004449 http://togogenome.org/gene/10090:Hectd3 ^@ http://purl.uniprot.org/uniprot/Q3U487 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ DOC|||E3 ubiquitin-protein ligase HECTD3|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000241446|||http://purl.uniprot.org/annotation/VSP_019441 http://togogenome.org/gene/10090:Spocd1 ^@ http://purl.uniprot.org/uniprot/B1ASB6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||SPOC|||SPOC domain-containing protein 1|||TFIIS central ^@ http://purl.uniprot.org/annotation/PRO_0000451971 http://togogenome.org/gene/10090:Fam83d ^@ http://purl.uniprot.org/uniprot/Q9D7I8 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Protein FAM83D|||Required for interaction with KIF22 and function in chromosome congression ^@ http://purl.uniprot.org/annotation/PRO_0000079461|||http://purl.uniprot.org/annotation/VSP_036447|||http://purl.uniprot.org/annotation/VSP_039768 http://togogenome.org/gene/10090:Natd1 ^@ http://purl.uniprot.org/uniprot/Q9DBW3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ N-acetyltransferase|||Protein NATD1 ^@ http://purl.uniprot.org/annotation/PRO_0000320657 http://togogenome.org/gene/10090:Tmem255a ^@ http://purl.uniprot.org/uniprot/Q8BHS0|||http://purl.uniprot.org/uniprot/Q8BHW5 ^@ 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.|||In isoform 3.|||Transmembrane protein 255A ^@ http://purl.uniprot.org/annotation/PRO_0000266039|||http://purl.uniprot.org/annotation/VSP_021922|||http://purl.uniprot.org/annotation/VSP_021923 http://togogenome.org/gene/10090:Rnf41 ^@ http://purl.uniprot.org/uniprot/Q8BH75 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ E3 ubiquitin-protein ligase NRDP1|||In isoform 2.|||RING-type; degenerate|||SIAH-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000223955|||http://purl.uniprot.org/annotation/VSP_058649|||http://purl.uniprot.org/annotation/VSP_058650 http://togogenome.org/gene/10090:Ptgdr2 ^@ http://purl.uniprot.org/uniprot/Q9Z2J6 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||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|||Involved in the recycling of CRTH2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Prostaglandin D2 receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000069573 http://togogenome.org/gene/10090:Oxld1 ^@ http://purl.uniprot.org/uniprot/B2RVP3|||http://purl.uniprot.org/uniprot/Q9CR10 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Oxidoreductase-like|||Oxidoreductase-like domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000314124 http://togogenome.org/gene/10090:Ifna12 ^@ http://purl.uniprot.org/uniprot/A0A7R8C3H7|||http://purl.uniprot.org/uniprot/Q80SS5 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Interferon alpha-12|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_5000090450|||http://purl.uniprot.org/annotation/PRO_5030940923 http://togogenome.org/gene/10090:Klk11 ^@ http://purl.uniprot.org/uniprot/A0A0B6VLT0|||http://purl.uniprot.org/uniprot/A0A1R3UCI4|||http://purl.uniprot.org/uniprot/Q9QYN3 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Signal Peptide|||Splice Variant ^@ Activation peptide|||Charge relay system|||In isoform 1.|||Kallikrein-11|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000224185|||http://purl.uniprot.org/annotation/PRO_0000224186|||http://purl.uniprot.org/annotation/PRO_5010813332|||http://purl.uniprot.org/annotation/VSP_017318 http://togogenome.org/gene/10090:Ccdc59 ^@ http://purl.uniprot.org/uniprot/Q8R2N0 ^@ 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|||Thyroid transcription factor 1-associated protein 26 ^@ http://purl.uniprot.org/annotation/PRO_0000298942|||http://purl.uniprot.org/annotation/VSP_027489|||http://purl.uniprot.org/annotation/VSP_027490 http://togogenome.org/gene/10090:Fetub ^@ http://purl.uniprot.org/uniprot/Q6YJU1|||http://purl.uniprot.org/uniprot/Q8CB17|||http://purl.uniprot.org/uniprot/Q9QXC1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Signal Peptide|||Strand|||Turn ^@ Basic and acidic residues|||Cystatin fetuin-B-type|||Cystatin fetuin-B-type 1|||Cystatin fetuin-B-type 2|||Cystatin fetuin-B-type domain-containing protein|||Disordered|||Fetuin-B|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000008900|||http://purl.uniprot.org/annotation/PRO_5004304004 http://togogenome.org/gene/10090:Rpl26 ^@ http://purl.uniprot.org/uniprot/P61255|||http://purl.uniprot.org/uniprot/Q4FZH2 ^@ 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)|||KOW|||Large ribosomal subunit protein uL24|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000130789 http://togogenome.org/gene/10090:Lyplal1 ^@ http://purl.uniprot.org/uniprot/E9QLB2|||http://purl.uniprot.org/uniprot/Q3UFF7 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Charge relay system|||Lysophospholipase-like protein 1|||N-acetylalanine|||Phospholipase/carboxylesterase/thioesterase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000227558 http://togogenome.org/gene/10090:Neu4 ^@ http://purl.uniprot.org/uniprot/C5NTX9|||http://purl.uniprot.org/uniprot/Q8BZL1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Repeat|||Splice Variant ^@ BNR 1|||BNR 2|||BNR 3|||Disordered|||FRIP motif|||In isoform 2.|||Nucleophile|||Polar residues|||Proton acceptor|||Sialidase|||Sialidase-4 ^@ http://purl.uniprot.org/annotation/PRO_0000208907|||http://purl.uniprot.org/annotation/VSP_037492 http://togogenome.org/gene/10090:Cdc40 ^@ http://purl.uniprot.org/uniprot/Q9DC48 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat ^@ Chain|||Mutagenesis Site|||Region|||Repeat ^@ Disordered|||Loss of proline isomerization; no phenotype when introduced in mice, animals are viable and fertile with no microcephaly or defective cortical lamination; no splicing defect.|||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_0000051143 http://togogenome.org/gene/10090:Ppcdc ^@ http://purl.uniprot.org/uniprot/A0A1L1ST77|||http://purl.uniprot.org/uniprot/Q8BZB2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent ^@ Flavoprotein|||Phosphopantothenoylcysteine decarboxylase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000182031 http://togogenome.org/gene/10090:Retnlg ^@ http://purl.uniprot.org/uniprot/Q8K426 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Resistin-like gamma ^@ http://purl.uniprot.org/annotation/PRO_5009715783 http://togogenome.org/gene/10090:Mdfi ^@ http://purl.uniprot.org/uniprot/P70331 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Disordered|||In isoform I-mfA.|||In isoform I-mfC.|||MyoD family inhibitor|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096325|||http://purl.uniprot.org/annotation/VSP_004055|||http://purl.uniprot.org/annotation/VSP_004056|||http://purl.uniprot.org/annotation/VSP_004057 http://togogenome.org/gene/10090:Pcdha10 ^@ http://purl.uniprot.org/uniprot/Q91Y20 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||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|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||PXXP 6|||Protocadherin alpha-10 ^@ http://purl.uniprot.org/annotation/PRO_0000431485 http://togogenome.org/gene/10090:Cox18 ^@ http://purl.uniprot.org/uniprot/G5E8U6|||http://purl.uniprot.org/uniprot/Q8VC74 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Cytochrome c oxidase assembly protein COX18, mitochondrial|||Helical|||Membrane insertase YidC/Oxa/ALB C-terminal|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000043327 http://togogenome.org/gene/10090:Vmn2r44 ^@ http://purl.uniprot.org/uniprot/L7N2E1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982462 http://togogenome.org/gene/10090:Or5p64 ^@ http://purl.uniprot.org/uniprot/Q8VG02 ^@ 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 5P64 ^@ http://purl.uniprot.org/annotation/PRO_0000150844 http://togogenome.org/gene/10090:Acsl1 ^@ http://purl.uniprot.org/uniprot/P41216 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 3'-nitrotyrosine|||Cytoplasmic|||Helical; Signal-anchor for type III membrane protein|||Long-chain-fatty-acid--CoA ligase 1|||N-acetylmethionine|||N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000193105 http://togogenome.org/gene/10090:6030498E09Rik ^@ http://purl.uniprot.org/uniprot/B1AX85 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Fzd3 ^@ http://purl.uniprot.org/uniprot/Q61086 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||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_0000012983 http://togogenome.org/gene/10090:Med8 ^@ http://purl.uniprot.org/uniprot/Q9CY05|||http://purl.uniprot.org/uniprot/Q9D7W5|||http://purl.uniprot.org/uniprot/Q9DAY7 ^@ 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|||Interaction with the Elongin BC complex|||Mediator of RNA polymerase II transcription subunit 8|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096395 http://togogenome.org/gene/10090:Thbd ^@ http://purl.uniprot.org/uniprot/P15306|||http://purl.uniprot.org/uniprot/Q543W3 ^@ 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 ^@ Basic and acidic residues|||C-type lectin|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5|||EGF-like 6; calcium-binding|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Thrombomodulin ^@ http://purl.uniprot.org/annotation/PRO_0000007772|||http://purl.uniprot.org/annotation/PRO_5014309606 http://togogenome.org/gene/10090:Wdr12 ^@ http://purl.uniprot.org/uniprot/Q4V9X1|||http://purl.uniprot.org/uniprot/Q9JJA4 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||N-acetylalanine|||NLE|||Phosphoserine|||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_0000051359 http://togogenome.org/gene/10090:H4c17 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Dnajb1 ^@ http://purl.uniprot.org/uniprot/Q3TU79|||http://purl.uniprot.org/uniprot/Q3TYL7|||http://purl.uniprot.org/uniprot/Q9QYJ3 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Chaperone DnaJ C-terminal|||Disordered|||DnaJ homolog subfamily B member 1|||J|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000071017 http://togogenome.org/gene/10090:Mrgprd ^@ http://purl.uniprot.org/uniprot/Q5UCB4|||http://purl.uniprot.org/uniprot/Q91ZB8 ^@ 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|||Mas-related G-protein coupled receptor member D|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069758 http://togogenome.org/gene/10090:Klra7 ^@ http://purl.uniprot.org/uniprot/F8WJ94|||http://purl.uniprot.org/uniprot/Q60654 ^@ 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|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform Ly-49G.2.|||In isoform Ly-49G.3.|||Killer cell lectin-like receptor 7|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046685|||http://purl.uniprot.org/annotation/VSP_003069|||http://purl.uniprot.org/annotation/VSP_003070 http://togogenome.org/gene/10090:Asnsd1 ^@ http://purl.uniprot.org/uniprot/Q3TGY6|||http://purl.uniprot.org/uniprot/Q8BFS9 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Region|||Sequence Conflict|||Splice Variant ^@ Asparagine synthetase|||Asparagine synthetase domain-containing protein 1|||Disordered|||For GATase activity|||Glutamine amidotransferase type-2|||In isoform 2.|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000324762|||http://purl.uniprot.org/annotation/VSP_032353 http://togogenome.org/gene/10090:Defa22 ^@ http://purl.uniprot.org/uniprot/Q8C1N8|||http://purl.uniprot.org/uniprot/W4VSN6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Alpha-defensin 22|||Alpha-defensin N-terminal|||Beta/alpha-defensin C-terminal|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000300070|||http://purl.uniprot.org/annotation/PRO_0000300071|||http://purl.uniprot.org/annotation/PRO_5015102295 http://togogenome.org/gene/10090:Nemp1 ^@ http://purl.uniprot.org/uniprot/Q6ZQE4|||http://purl.uniprot.org/uniprot/Q8K2N3 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Transmembrane ^@ A; required for its colocalization with lamins at the nuclear envelope|||B; required for interaction with RAN-GTP|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Nuclear envelope integral membrane protein 1|||Partial loss of phosphorylation and loss of interaction with RAN-GTP; when associated with A/E-366; A/E-376; A/E-380 and A/E-419.|||Partial loss of phosphorylation and loss of interaction with RAN-GTP; when associated with A/E-366; A/E-376; A/E-419 and A/E-420.|||Partial loss of phosphorylation and loss of interaction with RAN-GTP; when associated with A/E-366; A/E-380; A/E-419 and A/E-420.|||Partial loss of phosphorylation and loss of interaction with RAN-GTP; when associated with A/E-376; A/E-380; A/E-419 and A/E-420.|||Partial loss of phosphorylation and loss of interaction with RAN; when associated with A/E-366; A/E-376; A/E-380 and A/E-420.|||Phosphoserine|||Required for nuclear localization ^@ http://purl.uniprot.org/annotation/PRO_0000050745 http://togogenome.org/gene/10090:Hmox2 ^@ http://purl.uniprot.org/uniprot/O70252|||http://purl.uniprot.org/uniprot/Q544R7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ 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|||N-acetylserine|||Phosphoserine|||Removed|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000209692|||http://purl.uniprot.org/annotation/PRO_0000455627 http://togogenome.org/gene/10090:Slc6a17 ^@ http://purl.uniprot.org/uniprot/A0A0R4J087|||http://purl.uniprot.org/uniprot/Q8BJI1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Sodium-dependent neutral amino acid transporter SLC6A17 ^@ http://purl.uniprot.org/annotation/PRO_0000214804 http://togogenome.org/gene/10090:Tatdn3 ^@ http://purl.uniprot.org/uniprot/D3Z0V5|||http://purl.uniprot.org/uniprot/E9QL22|||http://purl.uniprot.org/uniprot/Q3U1C6 ^@ 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 deoxyribonuclease TATDN3 ^@ http://purl.uniprot.org/annotation/PRO_0000313596|||http://purl.uniprot.org/annotation/VSP_030049|||http://purl.uniprot.org/annotation/VSP_030050|||http://purl.uniprot.org/annotation/VSP_030051 http://togogenome.org/gene/10090:Spout1 ^@ http://purl.uniprot.org/uniprot/Q3UHX9 ^@ 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.|||Putative methyltransferase C9orf114 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000238469|||http://purl.uniprot.org/annotation/VSP_018611 http://togogenome.org/gene/10090:M1ap ^@ http://purl.uniprot.org/uniprot/Q9Z0E1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Meiosis 1 arrest protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000349269 http://togogenome.org/gene/10090:Fmn1 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPL0|||http://purl.uniprot.org/uniprot/E9Q7P6|||http://purl.uniprot.org/uniprot/Q05860 ^@ 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|||FH1|||FH2|||Formin-1|||In isoform 2, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Mediates interaction with alpha-catenin|||Microtubule-binding|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000194886|||http://purl.uniprot.org/annotation/VSP_001570|||http://purl.uniprot.org/annotation/VSP_001571|||http://purl.uniprot.org/annotation/VSP_001572|||http://purl.uniprot.org/annotation/VSP_027214|||http://purl.uniprot.org/annotation/VSP_027215|||http://purl.uniprot.org/annotation/VSP_027216|||http://purl.uniprot.org/annotation/VSP_029424|||http://purl.uniprot.org/annotation/VSP_029425 http://togogenome.org/gene/10090:Prss50 ^@ http://purl.uniprot.org/uniprot/Q8BLH5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic residues|||Charge relay system|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Polar residues|||Probable threonine protease PRSS50 ^@ http://purl.uniprot.org/annotation/PRO_0000415813 http://togogenome.org/gene/10090:Mpzl2 ^@ http://purl.uniprot.org/uniprot/F6RG10 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_5015091070 http://togogenome.org/gene/10090:Osgep ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Y3|||http://purl.uniprot.org/uniprot/Q3UQ67|||http://purl.uniprot.org/uniprot/Q8BWU5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Gcp-like|||tRNA N6-adenosine threonylcarbamoyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000096985 http://togogenome.org/gene/10090:Rras2 ^@ http://purl.uniprot.org/uniprot/P62071|||http://purl.uniprot.org/uniprot/Q9CTF6 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Non-terminal Residue|||Propeptide|||Sequence Conflict ^@ Cysteine methyl ester|||Effector region|||N-acetylalanine|||N6-palmitoyl lysine|||Phosphoserine|||Ras-related protein R-Ras2|||Removed|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000082653|||http://purl.uniprot.org/annotation/PRO_0000281303 http://togogenome.org/gene/10090:Gabrb1 ^@ http://purl.uniprot.org/uniprot/P50571|||http://purl.uniprot.org/uniprot/Q53WT3 ^@ 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|||Gamma-aminobutyric acid receptor subunit beta-1|||Helical|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000457|||http://purl.uniprot.org/annotation/PRO_5014309526 http://togogenome.org/gene/10090:Pwwp4d ^@ http://purl.uniprot.org/uniprot/A2BG95 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rpgrip1 ^@ http://purl.uniprot.org/uniprot/E9QQ97|||http://purl.uniprot.org/uniprot/Q0VGR8|||http://purl.uniprot.org/uniprot/Q9EPQ2 ^@ 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|||C2|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with RPGR|||Polar residues|||X-linked retinitis pigmentosa GTPase regulator-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000097433|||http://purl.uniprot.org/annotation/VSP_009528|||http://purl.uniprot.org/annotation/VSP_009529|||http://purl.uniprot.org/annotation/VSP_009530|||http://purl.uniprot.org/annotation/VSP_009531|||http://purl.uniprot.org/annotation/VSP_009532|||http://purl.uniprot.org/annotation/VSP_009533|||http://purl.uniprot.org/annotation/VSP_009534|||http://purl.uniprot.org/annotation/VSP_009535 http://togogenome.org/gene/10090:Sh3bp4 ^@ http://purl.uniprot.org/uniprot/Q921I6 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||SH3 1|||SH3 2|||SH3 domain-binding protein 4|||ZU5 ^@ http://purl.uniprot.org/annotation/PRO_0000274575 http://togogenome.org/gene/10090:Nrsn2 ^@ http://purl.uniprot.org/uniprot/Q5HZK2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Neurensin-2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000270585 http://togogenome.org/gene/10090:Ppp1r14b ^@ http://purl.uniprot.org/uniprot/Q62084 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolishes phosphorylation and strongly reduces inhibitory activity.|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Protein phosphatase 1 regulatory subunit 14B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000071491 http://togogenome.org/gene/10090:Btnl6 ^@ http://purl.uniprot.org/uniprot/A2CG22 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ B30.2/SPRY|||Disordered|||Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015086058 http://togogenome.org/gene/10090:Defa20 ^@ http://purl.uniprot.org/uniprot/Q45VN2 ^@ Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Alpha-defensin 20|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000300066|||http://purl.uniprot.org/annotation/PRO_0000300067 http://togogenome.org/gene/10090:Cdcp3 ^@ http://purl.uniprot.org/uniprot/Q8BZE1 ^@ 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 ^@ CUB 1|||CUB 2|||CUB 3|||Disordered|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Putative DMBT1-like protein|||SRCR 1|||SRCR 2|||SRCR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000343686 http://togogenome.org/gene/10090:Ttr ^@ http://purl.uniprot.org/uniprot/P07309|||http://purl.uniprot.org/uniprot/Q5M9K1 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Strand|||Turn ^@ 4-carboxyglutamate|||4-carboxyglutamate; in a patient with Moyamoya disease|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sulfocysteine|||Transthyretin|||Transthyretin/hydroxyisourate hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000035760|||http://purl.uniprot.org/annotation/PRO_5014205895 http://togogenome.org/gene/10090:Ntf3 ^@ http://purl.uniprot.org/uniprot/P20181|||http://purl.uniprot.org/uniprot/Q3V1A4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Nerve growth factor-related|||Neurotrophin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000019661|||http://purl.uniprot.org/annotation/PRO_0000019662 http://togogenome.org/gene/10090:Cxxc5 ^@ http://purl.uniprot.org/uniprot/Q91WA4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ CXXC-type|||CXXC-type zinc finger protein 5|||Disordered|||Nuclear localization signal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317549 http://togogenome.org/gene/10090:Ilkap ^@ http://purl.uniprot.org/uniprot/Q8R0F6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Integrin-linked kinase-associated serine/threonine phosphatase 2C|||N-acetylmethionine|||N6-acetyllysine|||PPM-type phosphatase|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000272272|||http://purl.uniprot.org/annotation/VSP_022384|||http://purl.uniprot.org/annotation/VSP_022385 http://togogenome.org/gene/10090:Hspa12b ^@ http://purl.uniprot.org/uniprot/Q9CZJ2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Heat shock 70 kDa protein 12B|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000078295 http://togogenome.org/gene/10090:Zik1 ^@ http://purl.uniprot.org/uniprot/Q80YP6 ^@ 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 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|||Polar residues|||Zinc finger protein interacting with ribonucleoprotein K ^@ http://purl.uniprot.org/annotation/PRO_0000286794 http://togogenome.org/gene/10090:Adam19 ^@ http://purl.uniprot.org/uniprot/O35674|||http://purl.uniprot.org/uniprot/Q3UH67|||http://purl.uniprot.org/uniprot/Q3UHT3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 19|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Polar residues|||Pro residues|||SH3-binding|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029104|||http://purl.uniprot.org/annotation/PRO_0000029105|||http://purl.uniprot.org/annotation/PRO_5010843417 http://togogenome.org/gene/10090:Pdss2 ^@ http://purl.uniprot.org/uniprot/Q33DR3 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ All trans-polyprenyl-diphosphate synthase PDSS2|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000123979|||http://purl.uniprot.org/annotation/VSP_017102|||http://purl.uniprot.org/annotation/VSP_017103|||http://purl.uniprot.org/annotation/VSP_017104|||http://purl.uniprot.org/annotation/VSP_017105 http://togogenome.org/gene/10090:Lin37 ^@ http://purl.uniprot.org/uniprot/E9Q0Q9|||http://purl.uniprot.org/uniprot/Q9D8N6 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Modified Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Protein lin-37 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000238480 http://togogenome.org/gene/10090:Or1f12 ^@ http://purl.uniprot.org/uniprot/A0A1W2P740 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cd79a ^@ http://purl.uniprot.org/uniprot/P11911 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Associates more strongly with SYK. Increases calcium response upon BCR ligation.|||Asymmetric dimethylarginine; by PRMT1|||B-cell antigen receptor complex-associated protein alpha chain|||Cytoplasmic|||Extracellular|||Has little effect on tyrosine phosphorylation. Reduces pre-B-cell differentiation. Abolishes binding to BLNK. Inhibits phosphorylation of BLNK. No effect on cap formation or BCR internalization. Impaired antigen presentation; when associated with F-176.|||Helical|||ITAM|||Ig-like C2-type|||Increases tyrosine phosphorylation. Inhibits phosphorylation of BLNK. Impaired antigen presentation; when associated with F-204.|||Interchain (with C-135 in beta chain)|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC-type Tyr-kinases|||Phosphotyrosine; by Tyr-kinases|||Required for binding to BLNK|||Strongly reduces tyrosine phosphorylation and pre-B-cell differentiation; when associated with F-182. No effect on constitutive internalization of BCR.|||Strongly reduces tyrosine phosphorylation and pre-B-cell differentiation; when associated with F-193. Abolishes constitutive internalization of BCR. ^@ http://purl.uniprot.org/annotation/PRO_0000014559 http://togogenome.org/gene/10090:Zfp691 ^@ http://purl.uniprot.org/uniprot/A2A7P4|||http://purl.uniprot.org/uniprot/Q3TDE8 ^@ 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 ^@ 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)|||Phosphoserine|||Zinc finger protein 691 ^@ http://purl.uniprot.org/annotation/PRO_0000234013 http://togogenome.org/gene/10090:Atg2b ^@ http://purl.uniprot.org/uniprot/Q80XK6 ^@ 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 ^@ Autophagy-related protein 2 homolog B|||Basic and acidic residues|||Chorein N-terminal|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089910|||http://purl.uniprot.org/annotation/VSP_035038|||http://purl.uniprot.org/annotation/VSP_035039 http://togogenome.org/gene/10090:Hsd17b8 ^@ http://purl.uniprot.org/uniprot/P50171 ^@ 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 ^@ (3R)-3-hydroxyacyl-CoA dehydrogenase|||In isoform Long.|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054599|||http://purl.uniprot.org/annotation/VSP_006030 http://togogenome.org/gene/10090:Mybbp1a ^@ http://purl.uniprot.org/uniprot/Q3U2W2|||http://purl.uniprot.org/uniprot/Q7TPV4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with MYB|||Myb-binding protein 1A|||N-acetylalanine|||N6-acetyllysine|||Nuclear export signal 1|||Nuclear export signal 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced nuclear export; when associated with A-249.|||Reduced nuclear export; when associated with A-251.|||Reduced nuclear export; when associated with A-272.|||Reduced nuclear export; when associated with A-274.|||Removed|||Required for nuclear and nucleolar localization ^@ http://purl.uniprot.org/annotation/PRO_0000096256 http://togogenome.org/gene/10090:Mrgprb4 ^@ http://purl.uniprot.org/uniprot/Q91ZC0 ^@ 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|||Mas-related G-protein coupled receptor member B4|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000305299 http://togogenome.org/gene/10090:Ubash3a ^@ http://purl.uniprot.org/uniprot/A0A498WGR9|||http://purl.uniprot.org/uniprot/Q3V3E1 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn ^@ Phosphatase-like|||SH3|||UBA|||Ubiquitin-associated and SH3 domain-containing protein A ^@ http://purl.uniprot.org/annotation/PRO_0000415372 http://togogenome.org/gene/10090:Jak3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0R7|||http://purl.uniprot.org/uniprot/Q62137 ^@ 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|||Splice Variant ^@ FERM|||In isoform 2.|||Interaction with cytokine/interferon/growth hormone receptors|||Loss of activity.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||SH2; atypical|||Tyrosine-protein kinase JAK3 ^@ http://purl.uniprot.org/annotation/PRO_0000088116|||http://purl.uniprot.org/annotation/VSP_027575|||http://purl.uniprot.org/annotation/VSP_027576 http://togogenome.org/gene/10090:St3gal1 ^@ http://purl.uniprot.org/uniprot/P54751|||http://purl.uniprot.org/uniprot/Q544T4 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149254 http://togogenome.org/gene/10090:Prkar1a ^@ http://purl.uniprot.org/uniprot/Q9DBC7 ^@ Binding Site|||Chain|||Disulfide Bond|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Dimerization and phosphorylation|||Disordered|||Interchain (with C-18)|||Interchain (with C-39)|||N-acetylalanine; in cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Pseudophosphorylation motif|||Removed; alternate|||cAMP-dependent protein kinase type I-alpha regulatory subunit|||cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed ^@ http://purl.uniprot.org/annotation/PRO_0000205378|||http://purl.uniprot.org/annotation/PRO_0000421786 http://togogenome.org/gene/10090:Slc26a9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0F7|||http://purl.uniprot.org/uniprot/Q8BU91 ^@ Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||INTRAMEM|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Alters chloride anion transport behavior.|||Cytoplasmic|||Extracellular|||Has very little effect on anion transport.|||Helical|||Impairs outward anion transport properties.|||STAS|||Solute carrier family 26 member 9 ^@ http://purl.uniprot.org/annotation/PRO_0000324493 http://togogenome.org/gene/10090:Golga4 ^@ http://purl.uniprot.org/uniprot/Q91VW5 ^@ 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|||GRIP|||Golgin subfamily A member 4|||In strain: C57BL/6.|||In strain: Czech II.|||Interaction with MACF1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000190060 http://togogenome.org/gene/10090:Or8b41 ^@ http://purl.uniprot.org/uniprot/Q7TRD9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gys1 ^@ http://purl.uniprot.org/uniprot/Q9Z1E4 ^@ 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|||Glycogen [starch] synthase, muscle|||Phosphoserine|||Phosphoserine; by AMPK and PKA|||Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and PASK|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000194765 http://togogenome.org/gene/10090:Scamp5 ^@ http://purl.uniprot.org/uniprot/Q9JKD3 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Secretory carrier-associated membrane protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000191263 http://togogenome.org/gene/10090:Riok2 ^@ http://purl.uniprot.org/uniprot/Q9CQS5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Nuclear export signal|||Phosphoserine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase RIO2 ^@ http://purl.uniprot.org/annotation/PRO_0000213528 http://togogenome.org/gene/10090:Fras1 ^@ http://purl.uniprot.org/uniprot/Q80T14 ^@ 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|||Repeat|||Sequence Conflict|||Signal Peptide|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4|||VWFC 5|||VWFC 6 ^@ http://purl.uniprot.org/annotation/PRO_0000010121 http://togogenome.org/gene/10090:Chst2 ^@ http://purl.uniprot.org/uniprot/Q80WV3 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 2|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000085187 http://togogenome.org/gene/10090:Gm2026 ^@ http://purl.uniprot.org/uniprot/A2ART4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Rnf14 ^@ http://purl.uniprot.org/uniprot/G3XA54|||http://purl.uniprot.org/uniprot/Q9JI90 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ D-box|||E3 ubiquitin-protein ligase RNF14|||IBR-type|||In isoform 2.|||Phosphoserine|||RING-type|||RING-type 1|||RING-type 2; atypical|||RWD|||TRIAD supradomain ^@ http://purl.uniprot.org/annotation/PRO_0000056058|||http://purl.uniprot.org/annotation/VSP_005751|||http://purl.uniprot.org/annotation/VSP_005752 http://togogenome.org/gene/10090:Noto ^@ http://purl.uniprot.org/uniprot/Q5TIS6 ^@ 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|||In truncate (tc); affects homeodomain stability.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000343224 http://togogenome.org/gene/10090:Tmem178 ^@ http://purl.uniprot.org/uniprot/Q9CZ16 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 178A ^@ http://purl.uniprot.org/annotation/PRO_0000287281 http://togogenome.org/gene/10090:Cntln ^@ http://purl.uniprot.org/uniprot/A2AM05 ^@ 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|||Centlein|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000328976|||http://purl.uniprot.org/annotation/VSP_032866|||http://purl.uniprot.org/annotation/VSP_052785|||http://purl.uniprot.org/annotation/VSP_052786|||http://purl.uniprot.org/annotation/VSP_052787 http://togogenome.org/gene/10090:Pabpc5 ^@ http://purl.uniprot.org/uniprot/Q8C7D3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ RRM ^@ http://togogenome.org/gene/10090:Pax2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J267|||http://purl.uniprot.org/uniprot/P32114 ^@ 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|||Disordered|||In isoform Short.|||PAI subdomain|||Paired|||Paired box protein Pax-2|||Phosphothreonine|||Polar residues|||RED subdomain ^@ http://purl.uniprot.org/annotation/PRO_0000050176|||http://purl.uniprot.org/annotation/VSP_002347 http://togogenome.org/gene/10090:Fam243 ^@ http://purl.uniprot.org/uniprot/Q8CDS7|||http://purl.uniprot.org/uniprot/Q9CUG6 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue ^@ Chain|||Non-terminal Residue ^@ Uncharacterized protein C21orf140 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000415167 http://togogenome.org/gene/10090:Or4n4 ^@ http://purl.uniprot.org/uniprot/Q8VFT5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tssc4 ^@ http://purl.uniprot.org/uniprot/Q9JHE7|||http://purl.uniprot.org/uniprot/Q9JHE9 ^@ 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|||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|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||U5 small nuclear ribonucleoprotein TSSC4 ^@ http://purl.uniprot.org/annotation/PRO_0000076361|||http://purl.uniprot.org/annotation/VSP_016562|||http://purl.uniprot.org/annotation/VSP_016563 http://togogenome.org/gene/10090:Dct ^@ http://purl.uniprot.org/uniprot/P29812 ^@ Binding Site|||Chain|||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|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In slaty-2j.|||In slaty-lt.|||In slaty; decreased DOPAchrome tautomerase activity.|||L-dopachrome tautomerase|||Lumenal, melanosome|||Mutant mice show an hypopigmentation of the coat and have the retinal pigmented epithelium significantly less pigmented than wild-type retinas.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000035893 http://togogenome.org/gene/10090:Slc18a3 ^@ http://purl.uniprot.org/uniprot/Q3TYJ1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:Bdp1 ^@ http://purl.uniprot.org/uniprot/Q571C7 ^@ 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|||Basic residues|||Disordered|||In isoform 2.|||Interaction with ZBTB43|||Myb-like|||Polar residues|||Pro residues|||Required for phosphorylation by CSNK2A1|||Transcription factor TFIIIB component B"" homolog ^@ http://purl.uniprot.org/annotation/PRO_0000333864|||http://purl.uniprot.org/annotation/VSP_033583 http://togogenome.org/gene/10090:Lck ^@ http://purl.uniprot.org/uniprot/E9Q696|||http://purl.uniprot.org/uniprot/P06240 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolishes myristoylation and palmitoylation.|||Abolishes plasma membrane association; when associated with S-21.|||Abolishes plasma membrane association; when associated with S-41. Reduced palmitoylation level.|||Causes thymic tumors.|||Complete loss of interaction with CD4 or CD8.|||Interaction with PTPRH|||Interactions with CD4 and CD8|||Loss of activity.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by CSK|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proto-oncogene tyrosine-protein kinase LCK|||Proton acceptor|||Reduced activity.|||Reduced palmitoylation level.|||Removed|||S-palmitoyl cysteine|||SH2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000088125 http://togogenome.org/gene/10090:Sacm1l ^@ http://purl.uniprot.org/uniprot/Q9EP69 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Essential for phosphatidylinositol-4-phosphate phosphatase activity|||Helical|||Lumenal|||N6-acetyllysine|||Phosphatidylinositol-3-phosphatase SAC1|||SAC ^@ http://purl.uniprot.org/annotation/PRO_0000317172 http://togogenome.org/gene/10090:Arrdc1 ^@ http://purl.uniprot.org/uniprot/Q99KN1 ^@ 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 ^@ Arrestin domain-containing protein 1|||Disordered|||In isoform 2.|||PPxY motif 1|||PPxY motif 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000244346|||http://purl.uniprot.org/annotation/VSP_019543 http://togogenome.org/gene/10090:Sytl4 ^@ http://purl.uniprot.org/uniprot/Q549X6|||http://purl.uniprot.org/uniprot/Q9R0Q1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger ^@ Abolishes interaction with RAB27A.|||Basic and acidic residues|||C2|||C2 1|||C2 2|||Disordered|||FYVE-type|||In isoform 2.|||In isoform 3.|||Phosphoserine|||RabBD|||Strongly reduces interaction with RAB27A.|||Strongly reduces interaction with STX1A.|||Synaptotagmin-like protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000190217|||http://purl.uniprot.org/annotation/VSP_007900|||http://purl.uniprot.org/annotation/VSP_007901|||http://purl.uniprot.org/annotation/VSP_007902 http://togogenome.org/gene/10090:Vpreb1a ^@ http://purl.uniprot.org/uniprot/P13372|||http://purl.uniprot.org/uniprot/Q545E0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide ^@ Complementarity-determining-1|||Complementarity-determining-2|||Framework-1|||Framework-2|||Framework-3|||Ig-like|||Immunoglobulin iota chain ^@ http://purl.uniprot.org/annotation/PRO_0000015001|||http://purl.uniprot.org/annotation/PRO_5014309564 http://togogenome.org/gene/10090:Ptprn ^@ http://purl.uniprot.org/uniprot/A6MDD2 ^@ 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|||Polar residues|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_5015086522 http://togogenome.org/gene/10090:Tmem71 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0I5|||http://purl.uniprot.org/uniprot/Q149F5 ^@ 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 71 ^@ http://purl.uniprot.org/annotation/PRO_0000278284 http://togogenome.org/gene/10090:Minar2 ^@ http://purl.uniprot.org/uniprot/Q8C4X7 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Major intrinsically disordered NOTCH2-binding receptor 1-like homolog|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000157136|||http://purl.uniprot.org/annotation/VSP_059939 http://togogenome.org/gene/10090:Rhov ^@ http://purl.uniprot.org/uniprot/Q8VDU1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Pro residues|||Rho-related GTP-binding protein RhoV|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000326439 http://togogenome.org/gene/10090:Wnt1 ^@ http://purl.uniprot.org/uniprot/P04426|||http://purl.uniprot.org/uniprot/Q3UR96 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt|||Proto-oncogene Wnt-1 ^@ http://purl.uniprot.org/annotation/PRO_0000041406|||http://purl.uniprot.org/annotation/PRO_5014309179 http://togogenome.org/gene/10090:Cbarp ^@ http://purl.uniprot.org/uniprot/Q66L44 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||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|||Loss of N-glycosylation.|||Loss of interaction with CACNB3 and loss of the ability to negatively regulate voltage-dependent L-type calcium channel; when associated with 426-A-A-427.|||Loss of interaction with CACNB3 and loss of the ability to negatively regulate voltage-dependent L-type calcium channel; when associated with 545-A--A-550.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Voltage-dependent calcium channel beta subunit-associated regulatory protein ^@ http://purl.uniprot.org/annotation/PRO_0000079984 http://togogenome.org/gene/10090:Top1 ^@ http://purl.uniprot.org/uniprot/Q04750|||http://purl.uniprot.org/uniprot/Q3TPX7|||http://purl.uniprot.org/uniprot/Q3ULF5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||DNA topoisomerase 1|||DNA topoisomerase I DNA binding 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|||Interaction with DNA|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||O-(3'-phospho-DNA)-tyrosine intermediate|||Phosphoserine|||Phosphoserine; by CK2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000145202 http://togogenome.org/gene/10090:Kcnv1 ^@ http://purl.uniprot.org/uniprot/Q8BZN2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||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|||Potassium voltage-gated channel subfamily V member 1|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000308353 http://togogenome.org/gene/10090:Hnrnpa3 ^@ http://purl.uniprot.org/uniprot/Q0VG47|||http://purl.uniprot.org/uniprot/Q3UZG3|||http://purl.uniprot.org/uniprot/Q5FB19|||http://purl.uniprot.org/uniprot/Q5U3M2|||http://purl.uniprot.org/uniprot/Q8BG05 ^@ 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_0000081839|||http://purl.uniprot.org/annotation/VSP_007350 http://togogenome.org/gene/10090:Emilin2 ^@ http://purl.uniprot.org/uniprot/Q3U1J9|||http://purl.uniprot.org/uniprot/Q8K482 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide ^@ C1q|||Collagen-like|||Disordered|||EMI|||EMILIN-2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000007818|||http://purl.uniprot.org/annotation/PRO_5014309130 http://togogenome.org/gene/10090:Pigt ^@ http://purl.uniprot.org/uniprot/Q3U5R2|||http://purl.uniprot.org/uniprot/Q8BXQ2 ^@ 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|||GPI transamidase component PIG-T|||Helical|||Interchain (with C-92 in PIGK/GPI8)|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000024108|||http://purl.uniprot.org/annotation/PRO_5010843371 http://togogenome.org/gene/10090:S100a6 ^@ http://purl.uniprot.org/uniprot/P14069|||http://purl.uniprot.org/uniprot/Q545I9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand ^@ EF-hand|||EF-hand 1|||EF-hand 2|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Protein S100-A6 ^@ http://purl.uniprot.org/annotation/PRO_0000143985 http://togogenome.org/gene/10090:Or4c10b ^@ http://purl.uniprot.org/uniprot/Q8VGP0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zbtb7b ^@ http://purl.uniprot.org/uniprot/Q5BJ24|||http://purl.uniprot.org/uniprot/Q64321 ^@ Chain|||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|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger ^@ BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||Disordered|||Fails to repress CD8 expression. Abolishes interaction with HDAC4 and HDAC5. No effect on homodimerization and DNA binding.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In HD; disrupts sequence-specific DNA-binding; no effect on homodimerization or interaction with HDAC4 and HDAC5.|||In helpless.|||N6-acetyllysine; by EP300; alternate|||No effect on acetylation levels. Slightly decreases acetylation levels; when associated with R-210. Slightly decreases acetylation levels; when associated with R-216.|||No effect on acetylation levels. Slightly decreases acetylation levels; when associated with R-339. Decreases acetylation levels; when associated with R-210 and R-216.|||Phosphoserine|||Phosphothreonine|||Pro residues|||Required for interaction with and acetylation by EP300|||Slightly decreases acetylation levels. No effect on protein stability. Slightly decreases acetylation levels; when associated with R-207. Slightly decreases acetylation levels and increases protein stability; when associated with R-210. Increases protein stability; when associated with R-339. Decreases acetylation levels; when associated with R-210 and R-343. Abolishes acetylation levels and ubiquitination and highly increases protein stability; when associated with R-210 and R-339.|||Slightly decreases acetylation levels. No effect on protein stability. Slightly decreases acetylation levels; when associated with R-207. Slightly decreases acetylation levels and increases protein stability; when associated with R-216. Increases protein stability; when associated with R-339. Decreases acetylation levels; when associated with R-216 and R-343. Abolishes acetylation levels and ubiquitination and highly increases protein stability; when associated with R-216 and R-339.|||Slightly decreases acetylation levels. Slightly increases protein stability. Slightly decreases acetylation levels; when associated with R-343. Increases protein stability; when associated with R-210 or R-216. Abolishes acetylation levels and ubiquitination and highly increases protein stability; when associated with R-210 and R-216.|||Zinc finger and BTB domain-containing protein 7B ^@ http://purl.uniprot.org/annotation/PRO_0000047720 http://togogenome.org/gene/10090:Ovol1 ^@ http://purl.uniprot.org/uniprot/Q9WTJ2 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||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_0000047012 http://togogenome.org/gene/10090:Cmtm1 ^@ http://purl.uniprot.org/uniprot/B7ZP21 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||MARVEL|||Polar residues ^@ http://togogenome.org/gene/10090:Cabp4 ^@ http://purl.uniprot.org/uniprot/Q8VHC5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Calcium-binding protein 4|||Decreased phosphorylation.|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Loss of calcium binding; when associated with Q-149 and Q-226.|||Loss of calcium binding; when associated with Q-149 and Q-263.|||Loss of calcium binding; when associated with Q-226 and Q-263.|||No effect on phosphorylation.|||Phosphoserine; by PKC/PRKCZ|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000073522 http://togogenome.org/gene/10090:Mettl24 ^@ http://purl.uniprot.org/uniprot/Q8CCB5 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Region|||Signal Peptide ^@ Disordered|||Probable methyltransferase-like protein 24 ^@ http://purl.uniprot.org/annotation/PRO_0000343744 http://togogenome.org/gene/10090:Csta3 ^@ http://purl.uniprot.org/uniprot/Q6IE28 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Cystatin ^@ http://togogenome.org/gene/10090:Alg13 ^@ http://purl.uniprot.org/uniprot/Q9D8C3 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Deubiquitinase activity|||Disordered|||For deubiquitinase activity|||Glycosyltransferase activity|||In isoform 2.|||Nucleophile; for deubiquitinase activity|||OTU|||Polar residues|||Pro residues|||Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13|||Tudor ^@ http://purl.uniprot.org/annotation/PRO_0000254574|||http://purl.uniprot.org/annotation/VSP_039304|||http://purl.uniprot.org/annotation/VSP_039305 http://togogenome.org/gene/10090:Slc43a1 ^@ http://purl.uniprot.org/uniprot/A2ATS4|||http://purl.uniprot.org/uniprot/G3X8X3|||http://purl.uniprot.org/uniprot/Q8BSM7 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Transmembrane ^@ Helical|||Large neutral amino acids transporter small subunit 3|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000218641 http://togogenome.org/gene/10090:Abcg2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0B6|||http://purl.uniprot.org/uniprot/Q7TMS5 ^@ 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 ^@ ABC transmembrane type-2|||ABC transporter|||Broad substrate specificity ATP-binding cassette transporter ABCG2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000093388 http://togogenome.org/gene/10090:Gstt4 ^@ http://purl.uniprot.org/uniprot/Q9D4P7 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase theta-4 ^@ http://purl.uniprot.org/annotation/PRO_0000329076 http://togogenome.org/gene/10090:Champ1 ^@ http://purl.uniprot.org/uniprot/Q8K327 ^@ 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 ^@ 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_0000248320 http://togogenome.org/gene/10090:Mtss1 ^@ http://purl.uniprot.org/uniprot/G3X9H7|||http://purl.uniprot.org/uniprot/Q6ZQB7|||http://purl.uniprot.org/uniprot/Q8R1S4 ^@ 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|||Splice Variant|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Turn ^@ Basic and acidic residues|||Disordered|||IMD|||In isoform 2.|||Loss of actin-binding.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein MTSS 1|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000096640|||http://purl.uniprot.org/annotation/VSP_050527|||http://purl.uniprot.org/annotation/VSP_050528|||http://purl.uniprot.org/annotation/VSP_050529 http://togogenome.org/gene/10090:Dus2 ^@ http://purl.uniprot.org/uniprot/Q14A90|||http://purl.uniprot.org/uniprot/Q9D7B1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Catalytic domain|||DRBM|||Disordered|||Interaction with tRNA|||Phosphoserine|||Proton donor|||tRNA-dihydrouridine(20) synthase [NAD(P)+]-like ^@ http://purl.uniprot.org/annotation/PRO_0000162158 http://togogenome.org/gene/10090:Pcgf2 ^@ http://purl.uniprot.org/uniprot/P23798 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Zinc Finger ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nuclear localization signal|||Phosphothreonine; by PKA|||Polar residues|||Polycomb group RING finger protein 2|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055985 http://togogenome.org/gene/10090:Ddx52 ^@ http://purl.uniprot.org/uniprot/Q3TKX4|||http://purl.uniprot.org/uniprot/Q8K301 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Sequence Conflict ^@ DEAD box|||DEAD-box RNA helicase Q|||Helicase ATP-binding|||Helicase C-terminal|||N6-acetyllysine|||Phosphoserine|||Probable ATP-dependent RNA helicase DDX52|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000055061 http://togogenome.org/gene/10090:Tmed5 ^@ http://purl.uniprot.org/uniprot/A2RS96|||http://purl.uniprot.org/uniprot/Q3V440|||http://purl.uniprot.org/uniprot/Q9CXE7 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Helix|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||GOLD|||Helical|||Lumenal|||Transmembrane emp24 domain-containing protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000010390|||http://purl.uniprot.org/annotation/PRO_5014296832|||http://purl.uniprot.org/annotation/PRO_5015097532 http://togogenome.org/gene/10090:Lrrc8b ^@ http://purl.uniprot.org/uniprot/Q5DU41 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Volume-regulated anion channel subunit LRRC8B ^@ http://purl.uniprot.org/annotation/PRO_0000076246|||http://purl.uniprot.org/annotation/VSP_055395 http://togogenome.org/gene/10090:Or10x4 ^@ http://purl.uniprot.org/uniprot/A2RS36|||http://purl.uniprot.org/uniprot/E9Q1L6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ttll13 ^@ http://purl.uniprot.org/uniprot/A4Q9F6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Essential for specifying alpha-elongation versus initiation step of the polyglutamylase activity|||TTL|||Tubulin polyglutamylase TTLL13|||c-MTBD region ^@ http://purl.uniprot.org/annotation/PRO_0000326168 http://togogenome.org/gene/10090:Sema6d ^@ http://purl.uniprot.org/uniprot/A2AW73|||http://purl.uniprot.org/uniprot/Q76KF0 ^@ 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 ^@ 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.|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sema|||Semaphorin-6D ^@ http://purl.uniprot.org/annotation/PRO_0000044616|||http://purl.uniprot.org/annotation/PRO_5002642614|||http://purl.uniprot.org/annotation/VSP_016568|||http://purl.uniprot.org/annotation/VSP_016569|||http://purl.uniprot.org/annotation/VSP_016570|||http://purl.uniprot.org/annotation/VSP_016571 http://togogenome.org/gene/10090:Odf3l2 ^@ http://purl.uniprot.org/uniprot/Q3TZ65 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ Disordered|||Protein CIMAP1D|||STPGR 1|||STPGR 2|||STPGR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000274521 http://togogenome.org/gene/10090:Hcls1 ^@ http://purl.uniprot.org/uniprot/P49710|||http://purl.uniprot.org/uniprot/Q8CA06 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Cortactin 1|||Cortactin 2|||Cortactin 3|||Cortactin 4; truncated|||Disordered|||Hematopoietic lineage cell-specific protein|||Involved in HAX-1 binding|||Minor effect on phosphorylation by FES. Abolishes phosphorylation by FES; when associated with F-388.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FGR|||Phosphotyrosine; by SYK and FES|||SH3|||Strongly reduces phosphorylation by FES. Abolishes phosphorylation by FES; when associated with F-405. ^@ http://purl.uniprot.org/annotation/PRO_0000083922 http://togogenome.org/gene/10090:BC037156 ^@ http://purl.uniprot.org/uniprot/H9CWD5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5003618658 http://togogenome.org/gene/10090:Glt6d1 ^@ http://purl.uniprot.org/uniprot/Q2NKH9 ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Glycosyltransferase 6 domain-containing protein 1|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000311973 http://togogenome.org/gene/10090:Smpd2 ^@ http://purl.uniprot.org/uniprot/O70572 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Site|||Transmembrane ^@ Helical|||Important for substrate recognition|||Proton acceptor|||Sphingomyelin phosphodiesterase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000075687 http://togogenome.org/gene/10090:Ubxn4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J078|||http://purl.uniprot.org/uniprot/Q8VCH8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Turn ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Interaction with UBQLN1|||Phosphothreonine|||Polar residues|||UBX|||UBX domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000211028 http://togogenome.org/gene/10090:Atn1 ^@ http://purl.uniprot.org/uniprot/O35126 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ Asymmetric dimethylarginine|||Atrophin-1|||Basic and acidic residues|||Cleavage|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Involved in binding BAIAP2|||N6-acetyllysine|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by MAPK8|||Phosphothreonine|||Polar residues|||Pro residues|||Required for interaction with FAT1 ^@ http://purl.uniprot.org/annotation/PRO_0000356253 http://togogenome.org/gene/10090:Wdr35 ^@ http://purl.uniprot.org/uniprot/Q8BND3 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat-containing protein 35 ^@ http://purl.uniprot.org/annotation/PRO_0000051385|||http://purl.uniprot.org/annotation/VSP_009733 http://togogenome.org/gene/10090:Agbl4 ^@ http://purl.uniprot.org/uniprot/E4W7Y4|||http://purl.uniprot.org/uniprot/Q09LZ8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes deglutamylase activity; when associated with Q-233.|||Abolishes deglutamylase activity; when associated with S-230.|||Cytosolic carboxypeptidase 6|||Disordered|||In isoform 2.|||Nucleophile|||Peptidase M14 carboxypeptidase A ^@ http://purl.uniprot.org/annotation/PRO_0000284836|||http://purl.uniprot.org/annotation/VSP_024671|||http://purl.uniprot.org/annotation/VSP_024672 http://togogenome.org/gene/10090:Snx29 ^@ http://purl.uniprot.org/uniprot/Q3TS66|||http://purl.uniprot.org/uniprot/Q9D3S3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||PX|||Phosphoserine|||Phosphothreonine|||Polar residues|||RUN|||Sorting nexin-29 ^@ http://purl.uniprot.org/annotation/PRO_0000297566|||http://purl.uniprot.org/annotation/VSP_041966 http://togogenome.org/gene/10090:Cd80 ^@ http://purl.uniprot.org/uniprot/Q00609|||http://purl.uniprot.org/uniprot/Q549R2 ^@ 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|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-hinge-like|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||T-lymphocyte activation antigen CD80 ^@ http://purl.uniprot.org/annotation/PRO_0000014548|||http://purl.uniprot.org/annotation/PRO_5014309656|||http://purl.uniprot.org/annotation/VSP_012552 http://togogenome.org/gene/10090:Mlycd ^@ http://purl.uniprot.org/uniprot/Q99J39 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Alpha-helical domain|||Catalytic domain|||Decreased acetylation, leading to reduced malonyl-CoA decarboxylase activity.|||Disordered|||Essential for catalytic activity|||In isoform Cytoplasmic+peroxisomal.|||Interchain|||Malonyl-CoA decarboxylase, mitochondrial|||Microbody targeting signal|||Mimicks constitutive acetylation, leading to increased malonyl-CoA decarboxylase activity.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000021090|||http://purl.uniprot.org/annotation/VSP_018817 http://togogenome.org/gene/10090:Spaca1 ^@ http://purl.uniprot.org/uniprot/B1AWF1|||http://purl.uniprot.org/uniprot/B1AWF2|||http://purl.uniprot.org/uniprot/Q9DA48 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Sperm acrosome membrane-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000248153|||http://purl.uniprot.org/annotation/PRO_5002760004|||http://purl.uniprot.org/annotation/PRO_5014298187 http://togogenome.org/gene/10090:Polq ^@ http://purl.uniprot.org/uniprot/Q80XB7|||http://purl.uniprot.org/uniprot/Q8CGS6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes ATP-binding in the helicase domain without affecting the ability to confer resistance to DNA damage.|||Abolishes DNA polymerase activity and ability to confer resistance to DNA damage.|||Basic and acidic residues|||DEAH box|||DNA polymerase theta|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In chaos1; mice display higher frequencies of spontaneous and radiation- or mitomycin C-induced micronucleated erythrocytes.|||In isoform 2.|||Interaction with RAD51|||Loop 1|||Loop 2|||Loop 3|||N6-acetyllysine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000432702|||http://purl.uniprot.org/annotation/VSP_057561 http://togogenome.org/gene/10090:Klrc3 ^@ http://purl.uniprot.org/uniprot/Q9QXN7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ C-type lectin|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Or5d40 ^@ http://purl.uniprot.org/uniprot/Q7TR25 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fam149a ^@ http://purl.uniprot.org/uniprot/Q8CFV2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM149A ^@ http://purl.uniprot.org/annotation/PRO_0000319931 http://togogenome.org/gene/10090:Entpd4 ^@ http://purl.uniprot.org/uniprot/Q8BSQ5|||http://purl.uniprot.org/uniprot/Q9DBT4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Non-terminal Residue|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Ectonucleoside triphosphate diphosphohydrolase 4|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000209912|||http://purl.uniprot.org/annotation/VSP_003615 http://togogenome.org/gene/10090:BC147527 ^@ http://purl.uniprot.org/uniprot/Q3V185 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Tex16 ^@ http://purl.uniprot.org/uniprot/A2RT18|||http://purl.uniprot.org/uniprot/F6UK53 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rbm43 ^@ http://purl.uniprot.org/uniprot/Q99J64 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ RNA-binding protein 43|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000264248 http://togogenome.org/gene/10090:Nrip3 ^@ http://purl.uniprot.org/uniprot/Q9JJR9 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Nuclear receptor-interacting protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000057954 http://togogenome.org/gene/10090:Vmn1r178 ^@ http://purl.uniprot.org/uniprot/Q8R2B6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pate6 ^@ http://purl.uniprot.org/uniprot/Q9CQB8 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099663 http://togogenome.org/gene/10090:Ccng2 ^@ http://purl.uniprot.org/uniprot/O08918|||http://purl.uniprot.org/uniprot/Q3TG40|||http://purl.uniprot.org/uniprot/Q5HZK4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Cyclin-G2|||Cyclin-like|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000080470 http://togogenome.org/gene/10090:Igf1 ^@ http://purl.uniprot.org/uniprot/E9PU89|||http://purl.uniprot.org/uniprot/E9Q138|||http://purl.uniprot.org/uniprot/P05017|||http://purl.uniprot.org/uniprot/Q4VJB9|||http://purl.uniprot.org/uniprot/Q4VJC0|||http://purl.uniprot.org/uniprot/Q8CAR0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ A|||B|||Basic and acidic residues|||C|||D|||Disordered|||E peptide|||In isoform IGF-IB.|||Insulin-like|||Insulin-like growth factor I|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000015666|||http://purl.uniprot.org/annotation/PRO_0000015667|||http://purl.uniprot.org/annotation/PRO_0000015668|||http://purl.uniprot.org/annotation/PRO_5003242978|||http://purl.uniprot.org/annotation/PRO_5015090368|||http://purl.uniprot.org/annotation/PRO_5015099086|||http://purl.uniprot.org/annotation/VSP_012165 http://togogenome.org/gene/10090:Afmid ^@ http://purl.uniprot.org/uniprot/Q8K4H1 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant ^@ HGGXW|||In isoform 2.|||Kynurenine formamidase|||Loss of enzyme activity.|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000248309|||http://purl.uniprot.org/annotation/VSP_020237 http://togogenome.org/gene/10090:Vmn1r222 ^@ http://purl.uniprot.org/uniprot/Q8R269 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ewsr1 ^@ http://purl.uniprot.org/uniprot/Q3UGI7|||http://purl.uniprot.org/uniprot/Q5SUT0|||http://purl.uniprot.org/uniprot/Q61545|||http://purl.uniprot.org/uniprot/Q6NVA3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||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|||Disordered|||EAD (Gln/Pro/Thr-rich)|||IQ|||N6-acetyllysine|||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_0000081587 http://togogenome.org/gene/10090:Gak ^@ http://purl.uniprot.org/uniprot/A0A0R4J0F6|||http://purl.uniprot.org/uniprot/Q99KY4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||C2 tensin-type|||Cyclin-G-associated kinase|||Disordered|||In isoform 2.|||J|||N-acetylserine|||Omega-N-methylarginine|||Phosphatase tensin-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000085959|||http://purl.uniprot.org/annotation/VSP_015821 http://togogenome.org/gene/10090:Ndst1 ^@ http://purl.uniprot.org/uniprot/Q3UHN9 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1|||Cytoplasmic|||For sulfotransferase activity|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate N-deacetylase 1|||Heparan sulfate N-sulfotransferase 1|||In isoform 2.|||In isoform 3.|||Loss of deacetylase activity. No effect on sulfotransferase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on deacetylase activity. Loss of sulfotransferase activity.|||Sufficient for localization to Golgi membrane ^@ http://purl.uniprot.org/annotation/PRO_0000225655|||http://purl.uniprot.org/annotation/VSP_017399|||http://purl.uniprot.org/annotation/VSP_017400|||http://purl.uniprot.org/annotation/VSP_017401|||http://purl.uniprot.org/annotation/VSP_017402 http://togogenome.org/gene/10090:Pigbos1 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPY0 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Marco ^@ http://purl.uniprot.org/uniprot/A2RT24|||http://purl.uniprot.org/uniprot/Q60754 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Strand|||Topological Domain|||Transmembrane ^@ Collagen-like|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Macrophage receptor MARCO|||N-linked (GlcNAc...) asparagine|||Polar residues|||SRCR ^@ http://purl.uniprot.org/annotation/PRO_0000181632 http://togogenome.org/gene/10090:Or13ae2 ^@ http://purl.uniprot.org/uniprot/Q8VF43 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rack1 ^@ http://purl.uniprot.org/uniprot/P68040 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ N-acetylmethionine|||N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Removed; alternate|||Small ribosomal subunit protein RACK1|||Small ribosomal subunit protein RACK1, N-terminally processed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000127732|||http://purl.uniprot.org/annotation/PRO_0000424482 http://togogenome.org/gene/10090:Usp1 ^@ http://purl.uniprot.org/uniprot/Q8BJQ2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||Cleavage; by autolysis|||Disordered|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 1|||Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment ^@ http://purl.uniprot.org/annotation/PRO_0000306287|||http://purl.uniprot.org/annotation/PRO_0000453163 http://togogenome.org/gene/10090:Or4c10 ^@ http://purl.uniprot.org/uniprot/Q8VGN6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Chrdl2 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1E8|||http://purl.uniprot.org/uniprot/D3YV59|||http://purl.uniprot.org/uniprot/Q8VEA6 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chordin-like protein 2|||Disordered|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||VWFC|||VWFC 1|||VWFC 2|||VWFC 3 ^@ http://purl.uniprot.org/annotation/PRO_0000005372|||http://purl.uniprot.org/annotation/PRO_5015034593 http://togogenome.org/gene/10090:Or6c5c ^@ http://purl.uniprot.org/uniprot/Q7TRI1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp653 ^@ http://purl.uniprot.org/uniprot/Q6YND2|||http://purl.uniprot.org/uniprot/Q8BHR7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Conflict|||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.|||Polar residues|||Zinc finger protein 653 ^@ http://purl.uniprot.org/annotation/PRO_0000253345|||http://purl.uniprot.org/annotation/VSP_021015 http://togogenome.org/gene/10090:Dll4 ^@ http://purl.uniprot.org/uniprot/Q9JI71 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ 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|||Interaction with Notch1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000007513 http://togogenome.org/gene/10090:Selenbp1 ^@ http://purl.uniprot.org/uniprot/P17563 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Methanethiol oxidase|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000174634 http://togogenome.org/gene/10090:Clspn ^@ http://purl.uniprot.org/uniprot/Q80YR7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Site ^@ Acidic patch|||Acidic residues|||Basic and acidic residues|||CKB motif 1|||CKB motif 2|||CKB motif 3|||Claspin|||Cleavage; by caspase-7|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine; by CHEK1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089876 http://togogenome.org/gene/10090:Hmgxb3 ^@ http://purl.uniprot.org/uniprot/G3X9M3|||http://purl.uniprot.org/uniprot/Q6AXF8|||http://purl.uniprot.org/uniprot/Q6NZP6|||http://purl.uniprot.org/uniprot/Q6PEF4|||http://purl.uniprot.org/uniprot/Q8BY57|||http://purl.uniprot.org/uniprot/Q8R168|||http://purl.uniprot.org/uniprot/Q9JJ64 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||HMG|||HMG box|||Polar residues ^@ http://togogenome.org/gene/10090:Dcaf12l1 ^@ http://purl.uniprot.org/uniprot/Q8CBW4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict ^@ DDB1- and CUL4-associated factor 12-like protein 1|||Disordered|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000306849 http://togogenome.org/gene/10090:H4c4 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Itpripl1 ^@ http://purl.uniprot.org/uniprot/A2ASA8 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Inositol 1,4,5-trisphosphate receptor-interacting protein-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000320567 http://togogenome.org/gene/10090:Ankrd7 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1L1|||http://purl.uniprot.org/uniprot/Q9D504 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 7|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000320067 http://togogenome.org/gene/10090:Akr1b7 ^@ http://purl.uniprot.org/uniprot/P21300|||http://purl.uniprot.org/uniprot/Q5M9J9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Site ^@ Aldo-keto reductase family 1 member B7|||Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000124629 http://togogenome.org/gene/10090:Aopep ^@ http://purl.uniprot.org/uniprot/Q8BXQ6 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Motif|||Site|||Splice Variant ^@ Aminopeptidase O|||In isoform 2.|||Nucleolar localization signal|||Proton acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000095092|||http://purl.uniprot.org/annotation/VSP_061019|||http://purl.uniprot.org/annotation/VSP_061020 http://togogenome.org/gene/10090:Defb1 ^@ http://purl.uniprot.org/uniprot/P56386|||http://purl.uniprot.org/uniprot/Q3UQE2 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Peptide|||Propeptide|||Signal Peptide ^@ BD-1|||Beta-defensin 1 ^@ http://purl.uniprot.org/annotation/PRO_0000006925|||http://purl.uniprot.org/annotation/PRO_0000006926|||http://purl.uniprot.org/annotation/PRO_5014309158 http://togogenome.org/gene/10090:Ucn3 ^@ http://purl.uniprot.org/uniprot/Q3UFJ9|||http://purl.uniprot.org/uniprot/Q924A4 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Propeptide|||Region|||Signal Peptide ^@ Corticotropin-releasing factor|||Disordered|||Isoleucine amide|||Urocortin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000006247|||http://purl.uniprot.org/annotation/PRO_0000006248|||http://purl.uniprot.org/annotation/PRO_5014309208 http://togogenome.org/gene/10090:Prune2 ^@ http://purl.uniprot.org/uniprot/Q52KR3|||http://purl.uniprot.org/uniprot/Q8CA96 ^@ 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 ^@ Basic and acidic residues|||CRAL-TRIO|||DHH motif|||DHHA2|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4 and isoform 6.|||In isoform 5.|||N-acetylmethionine|||Polar residues|||Protein prune homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000274881|||http://purl.uniprot.org/annotation/VSP_022905|||http://purl.uniprot.org/annotation/VSP_022906|||http://purl.uniprot.org/annotation/VSP_022908|||http://purl.uniprot.org/annotation/VSP_039356|||http://purl.uniprot.org/annotation/VSP_039357|||http://purl.uniprot.org/annotation/VSP_039358 http://togogenome.org/gene/10090:Fasn ^@ http://purl.uniprot.org/uniprot/P19096 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Acyl and malonyl transferases|||Beta-ketoacyl reductase|||C-terminal hotdog fold|||Carrier|||Disordered|||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|||Proton acceptor; for dehydratase activity|||Proton donor; for dehydratase activity|||S-nitrosocysteine|||Thioesterase ^@ http://purl.uniprot.org/annotation/PRO_0000180277 http://togogenome.org/gene/10090:Fam168b ^@ http://purl.uniprot.org/uniprot/Q80XQ8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Myelin-associated neurite-outgrowth inhibitor|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000325979 http://togogenome.org/gene/10090:Btbd35f7 ^@ http://purl.uniprot.org/uniprot/A2BHG6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Or5p1 ^@ http://purl.uniprot.org/uniprot/Q8VG06 ^@ 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 5P1 ^@ http://purl.uniprot.org/annotation/PRO_0000150846 http://togogenome.org/gene/10090:Lgalsl ^@ http://purl.uniprot.org/uniprot/Q8VED9 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Galectin|||Galectin-related protein|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000315767 http://togogenome.org/gene/10090:Rcsd1 ^@ http://purl.uniprot.org/uniprot/Q3UZA1 ^@ 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|||CapZ-interacting protein|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000320263|||http://purl.uniprot.org/annotation/VSP_031649 http://togogenome.org/gene/10090:Ramacl ^@ http://purl.uniprot.org/uniprot/Q3TQP0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Obi1 ^@ http://purl.uniprot.org/uniprot/G3X8V5|||http://purl.uniprot.org/uniprot/Q8K2Y0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||ORC ubiquitin ligase 1|||Phosphoserine|||Polar residues|||RING-type|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000055877|||http://purl.uniprot.org/annotation/VSP_015335|||http://purl.uniprot.org/annotation/VSP_015336|||http://purl.uniprot.org/annotation/VSP_015337|||http://purl.uniprot.org/annotation/VSP_015338 http://togogenome.org/gene/10090:Zmat1 ^@ http://purl.uniprot.org/uniprot/G5E8E4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ap2s1 ^@ http://purl.uniprot.org/uniprot/P62743|||http://purl.uniprot.org/uniprot/Q3UJ76 ^@ 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 ^@ AP complex mu/sigma subunit|||AP-2 complex subunit sigma|||Abolishes interaction with CD4 endocytosis signal motif.|||Phosphoserine|||Reduces interaction with CD4 endocytosis signal motif.|||Reduces interaction with CD4 endocytosis signal motif; when associated with AP2A2 E-21.|||Slightly reduces interaction with CD4 endocytosis signal motif. ^@ http://purl.uniprot.org/annotation/PRO_0000193805 http://togogenome.org/gene/10090:Abcd1 ^@ http://purl.uniprot.org/uniprot/P48410 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||ATP-binding cassette sub-family D member 1|||Helical|||Interaction with PEX19|||N-linked (GlcNAc...) asparagine|||PEX19 binding site and required for peroxisomal targeting|||Required for homodimerization ^@ http://purl.uniprot.org/annotation/PRO_0000093305 http://togogenome.org/gene/10090:Vmn1r69 ^@ http://purl.uniprot.org/uniprot/Q8VIC1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trhde ^@ http://purl.uniprot.org/uniprot/Q8BZN0|||http://purl.uniprot.org/uniprot/Q8K093 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||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|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Aminopeptidase N-like N-terminal|||Cytoplasmic|||Disordered|||ERAP1-like C-terminal|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Interchain|||N-linked (GlcNAc...) asparagine|||Peptidase M1 membrane alanine aminopeptidase|||Phosphothreonine; by PKC|||Polar residues|||Proton acceptor|||Thyrotropin-releasing hormone-degrading ectoenzyme|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000095119 http://togogenome.org/gene/10090:Frmpd4 ^@ http://purl.uniprot.org/uniprot/A0A571BG68|||http://purl.uniprot.org/uniprot/A2AFR3 ^@ 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|||FERM|||FERM and PDZ domain-containing protein 4|||In isoform 2.|||In isoform 3.|||PDZ|||Polar residues|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000307133|||http://purl.uniprot.org/annotation/VSP_028581|||http://purl.uniprot.org/annotation/VSP_028582 http://togogenome.org/gene/10090:Slc25a10 ^@ http://purl.uniprot.org/uniprot/Q9QZD8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial dicarboxylate carrier|||N6-acetyllysine|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090610 http://togogenome.org/gene/10090:Cep250 ^@ http://purl.uniprot.org/uniprot/A3KGJ7|||http://purl.uniprot.org/uniprot/E9Q5A8|||http://purl.uniprot.org/uniprot/Q60952 ^@ 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 ^@ Basic and acidic residues|||Centrosome-associated protein CEP250|||Disordered|||Knockin mutant mice show retinal morphological anomalies and altered electroretinographic responses to light stimuli.|||Phosphoserine|||Phosphoserine; by NEK2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089488 http://togogenome.org/gene/10090:Sdha ^@ http://purl.uniprot.org/uniprot/Q8K2B3 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ 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_0000010337 http://togogenome.org/gene/10090:Dtna ^@ http://purl.uniprot.org/uniprot/A0A1Y7VL34|||http://purl.uniprot.org/uniprot/Q3UHJ2|||http://purl.uniprot.org/uniprot/Q3UHP1|||http://purl.uniprot.org/uniprot/Q8BTD9|||http://purl.uniprot.org/uniprot/Q8CFR5|||http://purl.uniprot.org/uniprot/Q9D2N4 ^@ 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 ^@ Disordered|||Dystrobrevin alpha|||In isoform 2 and isoform 7.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 7.|||In isoform 5 and isoform 6.|||In isoform 5 and isoform 7.|||Interaction with MAGEE1|||Phosphoserine|||Polar residues|||Syntrophin-binding region|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000080037|||http://purl.uniprot.org/annotation/VSP_004214|||http://purl.uniprot.org/annotation/VSP_004215|||http://purl.uniprot.org/annotation/VSP_004216|||http://purl.uniprot.org/annotation/VSP_004217|||http://purl.uniprot.org/annotation/VSP_004218|||http://purl.uniprot.org/annotation/VSP_004219|||http://purl.uniprot.org/annotation/VSP_004220|||http://purl.uniprot.org/annotation/VSP_004221|||http://purl.uniprot.org/annotation/VSP_004222 http://togogenome.org/gene/10090:Cts6 ^@ http://purl.uniprot.org/uniprot/Q9ET52 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Cathepsin propeptide inhibitor|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_5015020151 http://togogenome.org/gene/10090:Svs4 ^@ http://purl.uniprot.org/uniprot/P18419 ^@ 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|||Polar residues|||Seminal vesicle secretory protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000022452 http://togogenome.org/gene/10090:Or9i1b ^@ http://purl.uniprot.org/uniprot/Q7TQQ2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cyp2d26 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZY2|||http://purl.uniprot.org/uniprot/Q8CIM7 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Cytochrome P450 2D26|||Helical|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051746 http://togogenome.org/gene/10090:Kiss1r ^@ http://purl.uniprot.org/uniprot/B2CP06|||http://purl.uniprot.org/uniprot/C5H7S2|||http://purl.uniprot.org/uniprot/Q91V45 ^@ 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|||KiSS-1 receptor|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069696 http://togogenome.org/gene/10090:Kdelr1 ^@ http://purl.uniprot.org/uniprot/Q99JH8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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|||Interaction with the K-D-E-L motif on target proteins|||Lumenal|||Phosphoserine; by PKA ^@ http://purl.uniprot.org/annotation/PRO_0000194154 http://togogenome.org/gene/10090:Cyp4f14 ^@ http://purl.uniprot.org/uniprot/Q9EP75 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Leukotriene-B4 omega-hydroxylase 3|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000051858 http://togogenome.org/gene/10090:Zbbx ^@ http://purl.uniprot.org/uniprot/F8WIV1|||http://purl.uniprot.org/uniprot/Q0P5X5 ^@ 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 ^@ B box-type|||B box-type; atypical|||Disordered|||Polar residues|||Zinc finger B-box domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000325814 http://togogenome.org/gene/10090:Fstl1 ^@ http://purl.uniprot.org/uniprot/Q62356 ^@ 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 ^@ EF-hand 1|||EF-hand 2|||Follistatin-like|||Follistatin-related protein 1|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000010113 http://togogenome.org/gene/10090:Ampd2 ^@ http://purl.uniprot.org/uniprot/Q9DBT5 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Splice Variant ^@ AMP deaminase 2|||Disordered|||In isoform 1.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000194408|||http://purl.uniprot.org/annotation/VSP_061947 http://togogenome.org/gene/10090:Il4 ^@ http://purl.uniprot.org/uniprot/P07750 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Interleukin-4|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015538 http://togogenome.org/gene/10090:Or2c1 ^@ http://purl.uniprot.org/uniprot/P23275 ^@ 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 2C1 ^@ http://purl.uniprot.org/annotation/PRO_0000150813 http://togogenome.org/gene/10090:Gstt2 ^@ http://purl.uniprot.org/uniprot/Q61133 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase theta-2 ^@ http://purl.uniprot.org/annotation/PRO_0000185941 http://togogenome.org/gene/10090:Smurf1 ^@ http://purl.uniprot.org/uniprot/E9PYU8|||http://purl.uniprot.org/uniprot/E9Q4K9|||http://purl.uniprot.org/uniprot/Q8BSC0|||http://purl.uniprot.org/uniprot/Q9CUN6 ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ C2|||Disordered|||E3 ubiquitin-protein ligase SMURF1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl thioester intermediate|||HECT|||Phosphoserine|||WW|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000120327 http://togogenome.org/gene/10090:Ifi208 ^@ http://purl.uniprot.org/uniprot/Q3V3Q4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Inteferon-activable protein 208|||Polar residues|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000334522 http://togogenome.org/gene/10090:Timm50 ^@ http://purl.uniprot.org/uniprot/Q9D880 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Disordered|||FCP1 homology|||Helical|||Mitochondrial import inner membrane translocase subunit TIM50|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000043116 http://togogenome.org/gene/10090:Pkn3 ^@ http://purl.uniprot.org/uniprot/Q3UQS3|||http://purl.uniprot.org/uniprot/Q8K045 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ AGC-kinase C-terminal|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||REM-1|||REM-1 1|||REM-1 2|||REM-1 3|||Serine/threonine-protein kinase N3 ^@ http://purl.uniprot.org/annotation/PRO_0000055726 http://togogenome.org/gene/10090:Lpcat2 ^@ http://purl.uniprot.org/uniprot/Q8BYI6 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EF-hand 1|||EF-hand 2|||EGTC motif|||HXXXXD motif|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||Lysophosphatidylcholine acyltransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000247059|||http://purl.uniprot.org/annotation/VSP_037079|||http://purl.uniprot.org/annotation/VSP_037080|||http://purl.uniprot.org/annotation/VSP_037081 http://togogenome.org/gene/10090:Igsf8 ^@ http://purl.uniprot.org/uniprot/A0A0R4J117|||http://purl.uniprot.org/uniprot/Q8R366 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EWI motif|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Immunoglobulin superfamily member 8|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000226248|||http://purl.uniprot.org/annotation/PRO_5015044315 http://togogenome.org/gene/10090:Shb ^@ http://purl.uniprot.org/uniprot/Q6PD21 ^@ 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.|||Phosphoserine|||Polar residues|||SH2|||SH2 domain-containing adapter protein B ^@ http://purl.uniprot.org/annotation/PRO_0000246325|||http://purl.uniprot.org/annotation/VSP_019848|||http://purl.uniprot.org/annotation/VSP_019849|||http://purl.uniprot.org/annotation/VSP_019850 http://togogenome.org/gene/10090:Erp29 ^@ http://purl.uniprot.org/uniprot/P57759 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Modified Residue|||Motif|||Signal Peptide ^@ Endoplasmic reticulum resident protein 29|||Phosphotyrosine; by PKDCC|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000021198 http://togogenome.org/gene/10090:Tcf3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J011|||http://purl.uniprot.org/uniprot/A0A0R4J014|||http://purl.uniprot.org/uniprot/E9PVV1|||http://purl.uniprot.org/uniprot/E9PVV2|||http://purl.uniprot.org/uniprot/E9PWE2|||http://purl.uniprot.org/uniprot/E9PWE4|||http://purl.uniprot.org/uniprot/P15806 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ BHLH|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform E47.|||Leucine-zipper|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription factor E2-alpha|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127468|||http://purl.uniprot.org/annotation/VSP_011354 http://togogenome.org/gene/10090:Vwa2 ^@ http://purl.uniprot.org/uniprot/Q70UZ7|||http://purl.uniprot.org/uniprot/Q8CE01 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||VWFA|||VWFA 1|||VWFA 2|||VWFA 3|||von Willebrand factor A domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_5000070397|||http://purl.uniprot.org/annotation/PRO_5004304064|||http://purl.uniprot.org/annotation/VSP_028740|||http://purl.uniprot.org/annotation/VSP_028741 http://togogenome.org/gene/10090:Pmch ^@ http://purl.uniprot.org/uniprot/P56942 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Isoleucine amide|||Melanin-concentrating hormone|||Neuropeptide-glutamic acid-isoleucine|||Neuropeptide-glycine-glutamic acid|||Pro-MCH ^@ http://purl.uniprot.org/annotation/PRO_0000019112|||http://purl.uniprot.org/annotation/PRO_0000019113|||http://purl.uniprot.org/annotation/PRO_0000019114|||http://purl.uniprot.org/annotation/PRO_0000019115 http://togogenome.org/gene/10090:Zfp354b ^@ http://purl.uniprot.org/uniprot/Q9QXT9 ^@ 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 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 354B ^@ http://purl.uniprot.org/annotation/PRO_0000280407 http://togogenome.org/gene/10090:B4galt5 ^@ http://purl.uniprot.org/uniprot/Q3U7I0|||http://purl.uniprot.org/uniprot/Q9JMK0 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Beta-1,4-galactosyltransferase 5|||Cytoplasmic|||Galactosyltransferase C-terminal|||Galactosyltransferase N-terminal|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000080546 http://togogenome.org/gene/10090:Dennd4a ^@ http://purl.uniprot.org/uniprot/E9Q8V6 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||MABP|||PPR|||Polar residues|||UDENN ^@ http://togogenome.org/gene/10090:Zfp574 ^@ http://purl.uniprot.org/uniprot/Q8BY46 ^@ 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 ^@ Asymmetric dimethylarginine|||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|||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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 574 ^@ http://purl.uniprot.org/annotation/PRO_0000274863 http://togogenome.org/gene/10090:Gja6 ^@ http://purl.uniprot.org/uniprot/A0A654ID52|||http://purl.uniprot.org/uniprot/Q6S5G4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Connexin N-terminal|||Cytoplasmic|||Extracellular|||Gap junction alpha-6 protein|||Gap junction protein cysteine-rich|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000057823 http://togogenome.org/gene/10090:Rasgrf1 ^@ http://purl.uniprot.org/uniprot/B2RS27|||http://purl.uniprot.org/uniprot/P27671|||http://purl.uniprot.org/uniprot/Q9QZR7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||DH|||Disordered|||IQ|||Loss of function and oligomerization.|||N-terminal Ras-GEF|||PH|||PH 1|||PH 2|||Partial loss of function. No effect on oligomerization.|||Phosphoserine|||Phosphoserine; by PLK2|||Ras-GEF|||Ras-specific guanine nucleotide-releasing factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000068881 http://togogenome.org/gene/10090:Lrat ^@ http://purl.uniprot.org/uniprot/B2RUR5|||http://purl.uniprot.org/uniprot/Q9JI60 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Acyl-thioester intermediate|||Cytoplasmic|||Helical|||Increases degradation via the proteasomal pathway. No effect on endoplasmic reticulum location. Impairs vitamin A uptake. No effect on retinol acyltransferase activity.|||LRAT|||Lecithin retinol acyltransferase|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000152479|||http://purl.uniprot.org/annotation/PRO_5014298389 http://togogenome.org/gene/10090:Nabp1 ^@ http://purl.uniprot.org/uniprot/Q8BGW5 ^@ 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|||In isoform 2.|||OB|||Polar residues|||SOSS complex subunit B2 ^@ http://purl.uniprot.org/annotation/PRO_0000333955|||http://purl.uniprot.org/annotation/VSP_033603 http://togogenome.org/gene/10090:Acad11 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0I6|||http://purl.uniprot.org/uniprot/Q80XL6 ^@ 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 ^@ Acyl-CoA dehydrogenase family member 11|||Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA dehydrogenase/oxidase N-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||Aminoglycoside phosphotransferase|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000254146 http://togogenome.org/gene/10090:Gpr35 ^@ http://purl.uniprot.org/uniprot/Q3TBY9|||http://purl.uniprot.org/uniprot/Q3TU48|||http://purl.uniprot.org/uniprot/Q8BS98|||http://purl.uniprot.org/uniprot/Q8CB97|||http://purl.uniprot.org/uniprot/Q9ES90 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069564 http://togogenome.org/gene/10090:Spata31 ^@ http://purl.uniprot.org/uniprot/E9QAF0|||http://purl.uniprot.org/uniprot/Q3V0C6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||SPATA31|||Spermatogenesis-associated protein 31 ^@ http://purl.uniprot.org/annotation/PRO_0000420572 http://togogenome.org/gene/10090:Uts2r ^@ http://purl.uniprot.org/uniprot/Q05AD1|||http://purl.uniprot.org/uniprot/Q8VIH9 ^@ 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|||Urotensin-2 receptor ^@ http://purl.uniprot.org/annotation/PRO_0000070195 http://togogenome.org/gene/10090:Fam199x ^@ http://purl.uniprot.org/uniprot/Q8K2D0 ^@ 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 FAM199X ^@ http://purl.uniprot.org/annotation/PRO_0000251211 http://togogenome.org/gene/10090:Scnn1a ^@ http://purl.uniprot.org/uniprot/Q3USG4|||http://purl.uniprot.org/uniprot/Q61180 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Amiloride-sensitive sodium channel subunit alpha|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000181262 http://togogenome.org/gene/10090:Or4f52 ^@ http://purl.uniprot.org/uniprot/Q7TQY8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Exoc7 ^@ http://purl.uniprot.org/uniprot/A2AAN0|||http://purl.uniprot.org/uniprot/O35250|||http://purl.uniprot.org/uniprot/Q3USE0|||http://purl.uniprot.org/uniprot/Q542L0 ^@ 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|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Exocyst complex component 7|||Exocyst complex subunit Exo70 C-terminal|||In isoform 2.|||Phosphoserine|||SEC8 and ARHQ binding ^@ http://purl.uniprot.org/annotation/PRO_0000118961|||http://purl.uniprot.org/annotation/VSP_001484|||http://purl.uniprot.org/annotation/VSP_001485 http://togogenome.org/gene/10090:Capzb ^@ http://purl.uniprot.org/uniprot/P47757 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Splice Variant ^@ F-actin-capping protein subunit beta|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000204635|||http://purl.uniprot.org/annotation/VSP_000768|||http://purl.uniprot.org/annotation/VSP_046517 http://togogenome.org/gene/10090:Tnfaip1 ^@ http://purl.uniprot.org/uniprot/O70479 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ BTB|||BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2|||Disordered|||Phosphoserine|||Phosphoserine; by CK2 ^@ http://purl.uniprot.org/annotation/PRO_0000331247 http://togogenome.org/gene/10090:Enpp3 ^@ http://purl.uniprot.org/uniprot/Q6DYE8 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cell attachment site|||Cytoplasmic|||Ectonucleotide pyrophosphatase/phosphodiesterase family member 3|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Nuclease|||Nucleophile|||Phosphodiesterase|||SMB 1|||SMB 2 ^@ http://purl.uniprot.org/annotation/PRO_0000281652 http://togogenome.org/gene/10090:Pnpt1 ^@ http://purl.uniprot.org/uniprot/Q8K1R3 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ In isoform 2.|||KH|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Polyribonucleotide nucleotidyltransferase 1, mitochondrial|||S1 motif ^@ http://purl.uniprot.org/annotation/PRO_0000024752|||http://purl.uniprot.org/annotation/VSP_013639|||http://purl.uniprot.org/annotation/VSP_013640 http://togogenome.org/gene/10090:Or56b1b ^@ http://purl.uniprot.org/uniprot/Q7TRU7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Basp1 ^@ http://purl.uniprot.org/uniprot/Q91XV3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region ^@ Basic and acidic residues|||Brain acid soluble protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000142896 http://togogenome.org/gene/10090:Kctd10 ^@ http://purl.uniprot.org/uniprot/F8WGQ9|||http://purl.uniprot.org/uniprot/Q922M3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ BTB|||BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||PCNA-binding|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000247422 http://togogenome.org/gene/10090:Psma5 ^@ http://purl.uniprot.org/uniprot/Q3UPK6|||http://purl.uniprot.org/uniprot/Q9Z2U1 ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Strand|||Turn ^@ N-acetylmethionine|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine|||Proteasome alpha-type subunits|||Proteasome subunit alpha type-5 ^@ http://purl.uniprot.org/annotation/PRO_0000124118 http://togogenome.org/gene/10090:Lrrn4cl ^@ http://purl.uniprot.org/uniprot/Q3TYX2|||http://purl.uniprot.org/uniprot/Q8C2Z8 ^@ 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|||Helical|||LRRN4 C-terminal-like protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000317753|||http://purl.uniprot.org/annotation/PRO_5004303942 http://togogenome.org/gene/10090:Lix1 ^@ http://purl.uniprot.org/uniprot/Q6P566 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Protein limb expression 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000232870 http://togogenome.org/gene/10090:Galnt17 ^@ http://purl.uniprot.org/uniprot/Q59J92|||http://purl.uniprot.org/uniprot/Q7TT15 ^@ 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|||Glycosyltransferase 2-like|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 17|||Ricin B lectin|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059140|||http://purl.uniprot.org/annotation/VSP_011232 http://togogenome.org/gene/10090:Ankle1 ^@ http://purl.uniprot.org/uniprot/A8VU90 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Motif|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat and LEM domain-containing protein 1|||GIY-YIG|||In isoform 2.|||LEM|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000438146|||http://purl.uniprot.org/annotation/VSP_058615 http://togogenome.org/gene/10090:Srgap1 ^@ http://purl.uniprot.org/uniprot/D3YZW1|||http://purl.uniprot.org/uniprot/Q91Z69 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||Disordered|||F-BAR|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho-GAP|||SH3|||SLIT-ROBO Rho GTPase-activating protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000056766 http://togogenome.org/gene/10090:Plin4 ^@ http://purl.uniprot.org/uniprot/O88492 ^@ 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 ^@ 1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||29 X 33 AA approximate tandem repeat|||3|||4|||5|||6|||7|||8|||9|||Disordered|||In isoform 2.|||Perilipin-4|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000297560|||http://purl.uniprot.org/annotation/VSP_027279|||http://purl.uniprot.org/annotation/VSP_027280 http://togogenome.org/gene/10090:Semp2l2a ^@ http://purl.uniprot.org/uniprot/G3X9P9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Ubiquitin-like protease family profile ^@ http://togogenome.org/gene/10090:Map2k6 ^@ http://purl.uniprot.org/uniprot/P70236|||http://purl.uniprot.org/uniprot/Q543Z5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ D domain|||DVD domain|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 6|||Phosphoserine; by MAPK3|||Phosphothreonine; by MAPK3|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086387 http://togogenome.org/gene/10090:Or52b3 ^@ http://purl.uniprot.org/uniprot/E9Q542 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ucp2 ^@ http://purl.uniprot.org/uniprot/P70406|||http://purl.uniprot.org/uniprot/Q549J5 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Helix|||Region|||Repeat|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Dicarboxylate carrier SLC25A8|||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|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090665 http://togogenome.org/gene/10090:Zfp472 ^@ http://purl.uniprot.org/uniprot/B0V2W5|||http://purl.uniprot.org/uniprot/Q3UQI7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Slc30a4 ^@ http://purl.uniprot.org/uniprot/A2AK40|||http://purl.uniprot.org/uniprot/O35149 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Phosphoserine|||Polar residues|||Probable proton-coupled zinc antiporter SLC30A4|||Zinc binding ^@ http://purl.uniprot.org/annotation/PRO_0000206100 http://togogenome.org/gene/10090:Tmem106b ^@ http://purl.uniprot.org/uniprot/Q80X71 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||Phosphoserine|||Removed|||Transmembrane protein 106B ^@ http://purl.uniprot.org/annotation/PRO_0000242651 http://togogenome.org/gene/10090:Golt1a ^@ http://purl.uniprot.org/uniprot/Q9DCQ3 ^@ 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_0000237608 http://togogenome.org/gene/10090:Tlk1 ^@ http://purl.uniprot.org/uniprot/Q8C0V0 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase tousled-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000086753 http://togogenome.org/gene/10090:Borcs5 ^@ http://purl.uniprot.org/uniprot/Q9D920 ^@ 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 ^@ BLOC-1-related complex subunit 5|||Disordered|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000318597 http://togogenome.org/gene/10090:Lyz1 ^@ http://purl.uniprot.org/uniprot/A0A077S9N1|||http://purl.uniprot.org/uniprot/P17897 ^@ 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 C-1 ^@ http://purl.uniprot.org/annotation/PRO_0000018473|||http://purl.uniprot.org/annotation/PRO_5014216939 http://togogenome.org/gene/10090:Grxcr1 ^@ http://purl.uniprot.org/uniprot/G3X9N2|||http://purl.uniprot.org/uniprot/Q50H32 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Glutaredoxin|||Glutaredoxin domain-containing cysteine-rich protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000349190 http://togogenome.org/gene/10090:Dppa1 ^@ http://purl.uniprot.org/uniprot/Q3TL00|||http://purl.uniprot.org/uniprot/Q810Y7 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5014309142|||http://purl.uniprot.org/annotation/PRO_5015098934 http://togogenome.org/gene/10090:Parvg ^@ http://purl.uniprot.org/uniprot/E9PYG5|||http://purl.uniprot.org/uniprot/Q8CEF2|||http://purl.uniprot.org/uniprot/Q9ERD8 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Gamma-parvin|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000121586 http://togogenome.org/gene/10090:Rif1 ^@ http://purl.uniprot.org/uniprot/Q6PR54 ^@ 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.|||Interaction with ERCC6|||Interaction with condensed chromosomes in telophase|||Phosphoserine|||Phosphothreonine|||Polar residues|||Telomere-associated protein RIF1 ^@ http://purl.uniprot.org/annotation/PRO_0000097334|||http://purl.uniprot.org/annotation/VSP_014432|||http://purl.uniprot.org/annotation/VSP_014433 http://togogenome.org/gene/10090:Olfr851 ^@ http://purl.uniprot.org/uniprot/Q7TRG0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tex13d ^@ http://purl.uniprot.org/uniprot/A0A0G2JGA3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||RanBP2-type ^@ http://togogenome.org/gene/10090:Ccdc120 ^@ http://purl.uniprot.org/uniprot/A2AEV7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Coiled-coil domain-containing protein 120|||Disordered|||Involved in CYTH2-binding|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000442769 http://togogenome.org/gene/10090:Mrps16 ^@ http://purl.uniprot.org/uniprot/Q9CPX7 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||Small ribosomal subunit protein bS16m ^@ http://purl.uniprot.org/annotation/PRO_0000030619 http://togogenome.org/gene/10090:Hacd1 ^@ http://purl.uniprot.org/uniprot/A2AQ81|||http://purl.uniprot.org/uniprot/B9EHK9|||http://purl.uniprot.org/uniprot/Q3V4A5|||http://purl.uniprot.org/uniprot/Q9QY80 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000349316 http://togogenome.org/gene/10090:H2ac6 ^@ http://purl.uniprot.org/uniprot/B2RVF0|||http://purl.uniprot.org/uniprot/C0HKE1|||http://purl.uniprot.org/uniprot/C0HKE2|||http://purl.uniprot.org/uniprot/C0HKE3|||http://purl.uniprot.org/uniprot/C0HKE4|||http://purl.uniprot.org/uniprot/C0HKE5|||http://purl.uniprot.org/uniprot/C0HKE6|||http://purl.uniprot.org/uniprot/C0HKE7|||http://purl.uniprot.org/uniprot/C0HKE8|||http://purl.uniprot.org/uniprot/C0HKE9 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Histone H2A type 1-C|||Histone H2A type 1-D|||Histone H2A type 1-E|||Histone H2A type 1-G|||Histone H2A type 1-I|||Histone H2A type 1-N|||Histone H2A type 1-O|||Histone H2A type 1-P|||Histone H2A/H2B/H3|||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_0000439715|||http://purl.uniprot.org/annotation/PRO_0000439716|||http://purl.uniprot.org/annotation/PRO_0000439717|||http://purl.uniprot.org/annotation/PRO_0000439718|||http://purl.uniprot.org/annotation/PRO_0000439719|||http://purl.uniprot.org/annotation/PRO_0000439720|||http://purl.uniprot.org/annotation/PRO_0000439721|||http://purl.uniprot.org/annotation/PRO_0000439722|||http://purl.uniprot.org/annotation/PRO_0000439723 http://togogenome.org/gene/10090:Srpx ^@ http://purl.uniprot.org/uniprot/Q9R0M3 ^@ 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 ^@ HYR|||In isoform 2.|||O-linked (Xyl...) (chondroitin sulfate) serine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi-repeat-containing protein SRPX ^@ http://purl.uniprot.org/annotation/PRO_0000022417|||http://purl.uniprot.org/annotation/VSP_014016 http://togogenome.org/gene/10090:Ist1 ^@ http://purl.uniprot.org/uniprot/Q9CX00 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||IST1 homolog|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000050728 http://togogenome.org/gene/10090:Mtfr2 ^@ http://purl.uniprot.org/uniprot/Q8VED8|||http://purl.uniprot.org/uniprot/Q9D0I1|||http://purl.uniprot.org/uniprot/Q9D456 ^@ 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|||Mitochondrial fission regulator 2|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000087165 http://togogenome.org/gene/10090:Serpinb9f ^@ http://purl.uniprot.org/uniprot/Q80UK5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Sh3glb1 ^@ http://purl.uniprot.org/uniprot/Q9JK48 ^@ 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|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ BAR|||Endophilin-B1|||In isoform 2.|||In isoform 3.|||Membrane-binding amphipathic helix|||N-acetylmethionine|||Phosphothreonine; by CDK5|||Required for membrane binding|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000146754|||http://purl.uniprot.org/annotation/VSP_009277|||http://purl.uniprot.org/annotation/VSP_058266 http://togogenome.org/gene/10090:Or7a37 ^@ http://purl.uniprot.org/uniprot/Q8VGU8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp980 ^@ http://purl.uniprot.org/uniprot/A2A9J5|||http://purl.uniprot.org/uniprot/Q4VA13 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Jpt2 ^@ http://purl.uniprot.org/uniprot/Q3TM10|||http://purl.uniprot.org/uniprot/Q6PGH2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Jupiter microtubule associated homolog 2|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000054922 http://togogenome.org/gene/10090:Fbxo8 ^@ http://purl.uniprot.org/uniprot/Q9QZN3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ F-box|||F-box only protein 8|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000120219 http://togogenome.org/gene/10090:Nr1d2 ^@ http://purl.uniprot.org/uniprot/Q4VAB7|||http://purl.uniprot.org/uniprot/Q60674|||http://purl.uniprot.org/uniprot/Q8C598|||http://purl.uniprot.org/uniprot/Q8C6J1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||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_0000053502 http://togogenome.org/gene/10090:Mid1 ^@ http://purl.uniprot.org/uniprot/B1AV01|||http://purl.uniprot.org/uniprot/O70583|||http://purl.uniprot.org/uniprot/Q3TVH5|||http://purl.uniprot.org/uniprot/Q6PD02 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Zinc Finger ^@ 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|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Polar residues|||RING-type|||RING-type E3 ubiquitin transferase ^@ http://purl.uniprot.org/annotation/PRO_0000056228|||http://purl.uniprot.org/annotation/PRO_5015098429|||http://purl.uniprot.org/annotation/VSP_005736|||http://purl.uniprot.org/annotation/VSP_010811 http://togogenome.org/gene/10090:Ccz1 ^@ http://purl.uniprot.org/uniprot/Q8C1Y8 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||Phosphoserine|||Removed|||Vacuolar fusion protein CCZ1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089585 http://togogenome.org/gene/10090:Rbm4b ^@ http://purl.uniprot.org/uniprot/A0A494B9C0|||http://purl.uniprot.org/uniprot/Q8VE92 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Zinc Finger ^@ CCHC-type|||Interaction with TNPO3|||RNA-binding protein 4B|||RRM|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081788 http://togogenome.org/gene/10090:Cfap161 ^@ http://purl.uniprot.org/uniprot/Q6P8Y0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Cilia- and flagella-associated protein 161 ^@ http://purl.uniprot.org/annotation/PRO_0000244093 http://togogenome.org/gene/10090:Tns2 ^@ http://purl.uniprot.org/uniprot/Q8CGB6 ^@ 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|||Zinc Finger ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C2 tensin-type|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||No abnormalities in glomerular morphology.|||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_0000292988|||http://purl.uniprot.org/annotation/VSP_026462|||http://purl.uniprot.org/annotation/VSP_026463|||http://purl.uniprot.org/annotation/VSP_026464 http://togogenome.org/gene/10090:Rin1 ^@ http://purl.uniprot.org/uniprot/Q921Q7 ^@ 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|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by PKD/PRKD1|||Phosphotyrosine; by ABL1 and ABL2|||Polar residues|||Pro residues|||Ras and Rab interactor 1|||Ras-associating|||SH2|||VPS9 ^@ http://purl.uniprot.org/annotation/PRO_0000191318 http://togogenome.org/gene/10090:Nlrp1a ^@ http://purl.uniprot.org/uniprot/Q2LKU9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant ^@ CARD|||Cleavage; by autolysis|||Constitutively active in IL1B release. In conventional housing conditions, mice bearing this mutation develop a systemic inflammatory phenotype associated with elevated IL1B and IL18 levels at 3-5 months of age. In a germ-free environment, they exhibit neutrophilia and myocarditis.|||Disordered|||FIIND|||In isoform 2.|||In strain: AKR/J.|||In strain: CAST/EiJ and DBA/2J.|||In strain: CAST/EiJ, DBA/2J and PWK/PhJ.|||In strain: CAST/EiJ.|||In strain: DBA/2J and CAST/EiJ.|||In strain: DBA/2J.|||In strain: PWK/PhJ.|||LRR 1|||LRR 2|||LRR 3|||NACHT|||NACHT, LRR and PYD domains-containing protein 1a|||NACHT, LRR and PYD domains-containing protein 1a, C-terminus|||NACHT, LRR and PYD domains-containing protein 1a, N-terminus|||Trigger for autolytic processing|||UPA|||ZU5 ^@ http://purl.uniprot.org/annotation/PRO_0000435102|||http://purl.uniprot.org/annotation/PRO_0000452853|||http://purl.uniprot.org/annotation/PRO_0000452854|||http://purl.uniprot.org/annotation/VSP_058002|||http://purl.uniprot.org/annotation/VSP_058003|||http://purl.uniprot.org/annotation/VSP_058004 http://togogenome.org/gene/10090:Arpc1a ^@ http://purl.uniprot.org/uniprot/Q9R0Q6 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ Actin-related protein 2/3 complex subunit 1A|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000050853 http://togogenome.org/gene/10090:Trim7 ^@ http://purl.uniprot.org/uniprot/Q5NCB7|||http://purl.uniprot.org/uniprot/Q923T7 ^@ 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 TRIM7|||In isoform 2.|||In isoform 3.|||Phosphoserine; by RPS6KA5|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056205|||http://purl.uniprot.org/annotation/VSP_012289|||http://purl.uniprot.org/annotation/VSP_012290|||http://purl.uniprot.org/annotation/VSP_012291 http://togogenome.org/gene/10090:Syt4 ^@ http://purl.uniprot.org/uniprot/P40749 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||Phosphoserine; by MAPK8|||Synaptotagmin-4|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000183949 http://togogenome.org/gene/10090:Vmn1r169 ^@ http://purl.uniprot.org/uniprot/L7N275 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cluh ^@ http://purl.uniprot.org/uniprot/A0A0R4J140|||http://purl.uniprot.org/uniprot/Q5SW19 ^@ 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|||Clu|||Clustered mitochondria protein homolog|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000366373|||http://purl.uniprot.org/annotation/VSP_036578|||http://purl.uniprot.org/annotation/VSP_036579|||http://purl.uniprot.org/annotation/VSP_036580 http://togogenome.org/gene/10090:Or6p1 ^@ http://purl.uniprot.org/uniprot/E9Q5P8|||http://purl.uniprot.org/uniprot/Q8VG29 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Capns1 ^@ http://purl.uniprot.org/uniprot/O88456 ^@ 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 ^@ Calpain small subunit 1|||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_0000073714 http://togogenome.org/gene/10090:Icam4 ^@ http://purl.uniprot.org/uniprot/Q14AB0|||http://purl.uniprot.org/uniprot/Q9ERM2 ^@ 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.|||Intercellular adhesion molecule 4|||Intercellular adhesion molecule N-terminal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014797|||http://purl.uniprot.org/annotation/PRO_5014306926|||http://purl.uniprot.org/annotation/VSP_013464 http://togogenome.org/gene/10090:AU018091 ^@ http://purl.uniprot.org/uniprot/E9PWS4|||http://purl.uniprot.org/uniprot/Q0PDJ1|||http://purl.uniprot.org/uniprot/Q66JW0 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Cationic amino acid transporter C-terminal|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Tax1bp3 ^@ http://purl.uniprot.org/uniprot/Q9DBG9 ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand ^@ N-acetylserine|||PDZ|||Phosphoserine|||Removed|||Tax1-binding protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000233944 http://togogenome.org/gene/10090:Capn3 ^@ http://purl.uniprot.org/uniprot/A4QPE6|||http://purl.uniprot.org/uniprot/Q0VGP9|||http://purl.uniprot.org/uniprot/Q64691 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ 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 isoform Short.|||Linker ^@ http://purl.uniprot.org/annotation/PRO_0000207708|||http://purl.uniprot.org/annotation/VSP_005230|||http://purl.uniprot.org/annotation/VSP_005231 http://togogenome.org/gene/10090:Mapk8ip3 ^@ http://purl.uniprot.org/uniprot/E9Q6B6|||http://purl.uniprot.org/uniprot/E9Q6E0|||http://purl.uniprot.org/uniprot/Q3UHB5|||http://purl.uniprot.org/uniprot/Q6P1F1|||http://purl.uniprot.org/uniprot/Q9ESN9 ^@ 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 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||C-Jun-amino-terminal kinase-interacting protein 3|||Disordered|||In isoform 1a and isoform 1b.|||In isoform 1a and isoform 1d.|||In isoform 1b and isoform 1e.|||In isoform 3a.|||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|||Results in inhibition of JNK binding.|||Results in loss of phosphorylation of MAPK8IP3; when associated with A-266 and A-287. Does not effect binding of components of the JNK pathway.|||Results in loss of phosphorylation of MAPK8IP3; when associated with A-276 and A-287. Does not effect binding of components of the JNK pathway. ^@ http://purl.uniprot.org/annotation/PRO_0000220634|||http://purl.uniprot.org/annotation/VSP_002775|||http://purl.uniprot.org/annotation/VSP_002776|||http://purl.uniprot.org/annotation/VSP_002777|||http://purl.uniprot.org/annotation/VSP_002778|||http://purl.uniprot.org/annotation/VSP_002779 http://togogenome.org/gene/10090:Slc38a8 ^@ http://purl.uniprot.org/uniprot/Q5HZH7 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Solute carrier family 38 member 8 ^@ http://purl.uniprot.org/annotation/PRO_0000319594 http://togogenome.org/gene/10090:Phf1 ^@ http://purl.uniprot.org/uniprot/A0A494BBE6|||http://purl.uniprot.org/uniprot/Q9Z1B8 ^@ 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 ^@ Basic and acidic residues|||Disordered|||PHD finger protein 1|||PHD-type|||PHD-type 1|||PHD-type 2|||Polar residues|||Tudor ^@ http://purl.uniprot.org/annotation/PRO_0000059289 http://togogenome.org/gene/10090:Npsr1 ^@ http://purl.uniprot.org/uniprot/A1KXK3|||http://purl.uniprot.org/uniprot/Q8BZP8 ^@ 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|||Neuropeptide S receptor ^@ http://purl.uniprot.org/annotation/PRO_0000069641 http://togogenome.org/gene/10090:L3mbtl1 ^@ http://purl.uniprot.org/uniprot/A2A5N8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||CCHHC-type|||Disordered|||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|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000405831 http://togogenome.org/gene/10090:Or2t47 ^@ http://purl.uniprot.org/uniprot/Q5NCD3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Arhgef5 ^@ http://purl.uniprot.org/uniprot/E9Q7D5 ^@ 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|||DH|||Disordered|||PH|||Phosphoserine|||Polar residues|||Pro residues|||Rho guanine nucleotide exchange factor 5|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000435143 http://togogenome.org/gene/10090:Svs3a ^@ http://purl.uniprot.org/uniprot/F2Z472 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 1|||2|||3|||4|||5|||5 X 4 AA tandem repeats of Q-X-K-[ST]|||In isoform 2.|||Seminal vesicle secretory protein 3A ^@ http://purl.uniprot.org/annotation/PRO_5003291021|||http://purl.uniprot.org/annotation/VSP_059284 http://togogenome.org/gene/10090:Ptafr ^@ http://purl.uniprot.org/uniprot/Q62035 ^@ 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|||Platelet-activating factor receptor ^@ http://purl.uniprot.org/annotation/PRO_0000070094 http://togogenome.org/gene/10090:Thada ^@ http://purl.uniprot.org/uniprot/A8C756 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||tRNA (32-2'-O)-methyltransferase regulator THADA ^@ http://purl.uniprot.org/annotation/PRO_0000344058|||http://purl.uniprot.org/annotation/VSP_034736|||http://purl.uniprot.org/annotation/VSP_034737|||http://purl.uniprot.org/annotation/VSP_034738|||http://purl.uniprot.org/annotation/VSP_034739|||http://purl.uniprot.org/annotation/VSP_034740 http://togogenome.org/gene/10090:Mfsd8 ^@ http://purl.uniprot.org/uniprot/Q8BH31 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dileucine internalization motif|||Disordered|||Extracellular|||Helical|||Major facilitator superfamily domain-containing protein 8|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000311233 http://togogenome.org/gene/10090:Adam26a ^@ http://purl.uniprot.org/uniprot/Q8BMR4|||http://purl.uniprot.org/uniprot/Q9R158 ^@ 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 26A|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029126|||http://purl.uniprot.org/annotation/PRO_0000029127|||http://purl.uniprot.org/annotation/PRO_5004304178 http://togogenome.org/gene/10090:AF067061 ^@ http://purl.uniprot.org/uniprot/O70616 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Prelid3a ^@ http://purl.uniprot.org/uniprot/Q8VE85 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Chain|||Domain Extent|||Site ^@ Important for interaction with TRIAP1|||PRELI domain containing protein 3A|||PRELI/MSF1 ^@ http://purl.uniprot.org/annotation/PRO_0000295216 http://togogenome.org/gene/10090:Ppil6 ^@ http://purl.uniprot.org/uniprot/Q9D6D8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ PPIase cyclophilin-type|||Probable inactive peptidyl-prolyl cis-trans isomerase-like 6 ^@ http://purl.uniprot.org/annotation/PRO_0000263756 http://togogenome.org/gene/10090:Prss16 ^@ http://purl.uniprot.org/uniprot/Q9QXE5 ^@ Active Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Glycosylation Site|||Signal Peptide ^@ Charge relay system|||N-linked (GlcNAc...) asparagine|||Thymus-specific serine protease ^@ http://purl.uniprot.org/annotation/PRO_0000027321 http://togogenome.org/gene/10090:Rasgef1b ^@ http://purl.uniprot.org/uniprot/Q8JZL7 ^@ 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.|||N-terminal Ras-GEF|||Ras-GEF|||Ras-GEF domain-containing family member 1B ^@ http://purl.uniprot.org/annotation/PRO_0000297639|||http://purl.uniprot.org/annotation/VSP_027315|||http://purl.uniprot.org/annotation/VSP_059002|||http://purl.uniprot.org/annotation/VSP_059003 http://togogenome.org/gene/10090:Ifna4 ^@ http://purl.uniprot.org/uniprot/P07351|||http://purl.uniprot.org/uniprot/Q540C2 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Interferon alpha-4|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000016377|||http://purl.uniprot.org/annotation/PRO_5014309524 http://togogenome.org/gene/10090:Pcnx2 ^@ http://purl.uniprot.org/uniprot/Q5DU28 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Pecanex-like protein 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000333966|||http://purl.uniprot.org/annotation/VSP_033612|||http://purl.uniprot.org/annotation/VSP_033613|||http://purl.uniprot.org/annotation/VSP_033614|||http://purl.uniprot.org/annotation/VSP_033615|||http://purl.uniprot.org/annotation/VSP_033616 http://togogenome.org/gene/10090:Rspry1 ^@ http://purl.uniprot.org/uniprot/Q8BVR6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Zinc Finger ^@ B30.2/SPRY|||Disordered|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||RING finger and SPRY domain-containing protein 1|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000278788|||http://purl.uniprot.org/annotation/VSP_023384|||http://purl.uniprot.org/annotation/VSP_023385|||http://purl.uniprot.org/annotation/VSP_023386 http://togogenome.org/gene/10090:Nup214 ^@ http://purl.uniprot.org/uniprot/Q80U93 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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|||45|||46|||46 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Leucine-zipper 1|||Leucine-zipper 2|||N-acetylglycine|||Nuclear pore complex protein Nup214|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Seven-bladed beta propeller ^@ http://purl.uniprot.org/annotation/PRO_0000345014 http://togogenome.org/gene/10090:Ylpm1 ^@ http://purl.uniprot.org/uniprot/D3YWX2|||http://purl.uniprot.org/uniprot/E9Q803|||http://purl.uniprot.org/uniprot/Q8C8U8 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Ccdc89 ^@ http://purl.uniprot.org/uniprot/Q9DA73 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Coiled-coil domain-containing protein 89|||Disordered|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000370201 http://togogenome.org/gene/10090:Alg9 ^@ http://purl.uniprot.org/uniprot/Q8VDI9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Alpha-1,2-mannosyltransferase ALG9|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000215788 http://togogenome.org/gene/10090:Pole ^@ http://purl.uniprot.org/uniprot/Q3UR94|||http://purl.uniprot.org/uniprot/Q80XH7|||http://purl.uniprot.org/uniprot/Q9WVF7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||CysA-type|||CysB motif|||DNA polymerase epsilon catalytic subunit A|||DNA polymerase epsilon catalytic subunit A C-terminal|||DNA-directed DNA polymerase family B exonuclease|||DNA-directed DNA polymerase family B multifunctional|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000046456 http://togogenome.org/gene/10090:Eif2s3x ^@ http://purl.uniprot.org/uniprot/Q3TML6|||http://purl.uniprot.org/uniprot/Q9Z0N1 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Eukaryotic translation initiation factor 2 subunit 3, X-linked|||G1|||G2|||G3|||G4|||G5|||N-acetylalanine|||Phosphoserine|||Removed|||Tr-type G|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000137439 http://togogenome.org/gene/10090:Or8j3b ^@ http://purl.uniprot.org/uniprot/Q7TR75 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Neurod4 ^@ http://purl.uniprot.org/uniprot/O09105|||http://purl.uniprot.org/uniprot/Q545C0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ BHLH|||Disordered|||Neurogenic differentiation factor 4|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127391 http://togogenome.org/gene/10090:Cryaa ^@ http://purl.uniprot.org/uniprot/A0A494B9Q6|||http://purl.uniprot.org/uniprot/P24622|||http://purl.uniprot.org/uniprot/Q546L9|||http://purl.uniprot.org/uniprot/Q569M7 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Splice Variant ^@ Alpha-crystallin A chain|||Deamidated asparagine; partial|||Deamidated glutamine; partial|||Disordered|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphoserine|||Required for complex formation with BFSP1 and BFSP2|||SHSP|||sHSP ^@ http://purl.uniprot.org/annotation/PRO_0000125872|||http://purl.uniprot.org/annotation/VSP_011916 http://togogenome.org/gene/10090:Add1 ^@ http://purl.uniprot.org/uniprot/E9Q1K3|||http://purl.uniprot.org/uniprot/F8WGR0|||http://purl.uniprot.org/uniprot/F8WHZ9|||http://purl.uniprot.org/uniprot/Q9QYC0 ^@ 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 ^@ Alpha-adducin|||Basic and acidic residues|||Class II aldolase/adducin N-terminal|||Disordered|||In isoform 2.|||Interaction with calmodulin|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphoserine; by PKA and PKC|||Phosphoserine; by PKC|||Phosphothreonine|||Phosphothreonine; by ROCK2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000218531|||http://purl.uniprot.org/annotation/VSP_000177|||http://purl.uniprot.org/annotation/VSP_000178 http://togogenome.org/gene/10090:Foxd4 ^@ http://purl.uniprot.org/uniprot/Q60688 ^@ 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 D4|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000091822 http://togogenome.org/gene/10090:Vcpkmt ^@ http://purl.uniprot.org/uniprot/Q8C436 ^@ 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.|||N-acetylalanine|||Protein N-lysine methyltransferase METTL21D|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089938|||http://purl.uniprot.org/annotation/VSP_026588 http://togogenome.org/gene/10090:Ccl3 ^@ http://purl.uniprot.org/uniprot/P10855|||http://purl.uniprot.org/uniprot/Q5QNW0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Signal Peptide|||Strand ^@ C-C motif chemokine|||C-C motif chemokine 3|||Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_0000005158|||http://purl.uniprot.org/annotation/PRO_5014205896 http://togogenome.org/gene/10090:Slc19a1 ^@ http://purl.uniprot.org/uniprot/P41438|||http://purl.uniprot.org/uniprot/Q542F3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic 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 isoform 2.|||In isoform 3.|||Induces resistance to 5,10-dideazatetrahydrofolate; when associated with F-48.|||Induces resistance to 5,10-dideazatetrahydrofolate; when associated with G-105.|||N-acetylmethionine|||Phosphoserine|||Reduced folate transporter|||Required for substrate-binding ^@ http://purl.uniprot.org/annotation/PRO_0000178661|||http://purl.uniprot.org/annotation/VSP_006125|||http://purl.uniprot.org/annotation/VSP_006126|||http://purl.uniprot.org/annotation/VSP_006127 http://togogenome.org/gene/10090:Tcf23 ^@ http://purl.uniprot.org/uniprot/Q9JLR5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||Transcription factor 23|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000315821 http://togogenome.org/gene/10090:4930558K02Rik ^@ http://purl.uniprot.org/uniprot/E0CXC6 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Lrif1 ^@ http://purl.uniprot.org/uniprot/G3X9P5|||http://purl.uniprot.org/uniprot/G5E8M8|||http://purl.uniprot.org/uniprot/Q505B0|||http://purl.uniprot.org/uniprot/Q8CDD9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Non-terminal 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.|||Ligand-dependent nuclear receptor-interacting factor 1|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||PxVxL motif ^@ http://purl.uniprot.org/annotation/PRO_0000250687|||http://purl.uniprot.org/annotation/VSP_020722|||http://purl.uniprot.org/annotation/VSP_020723 http://togogenome.org/gene/10090:Usp21 ^@ http://purl.uniprot.org/uniprot/E9PUE2|||http://purl.uniprot.org/uniprot/Q9QZL6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes ability to deubiquitinate histone H2A and ability to regulate transcription.|||Basic and acidic residues|||Disordered|||Nuclear export signal|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 21 ^@ http://purl.uniprot.org/annotation/PRO_0000080649 http://togogenome.org/gene/10090:Cngb3 ^@ http://purl.uniprot.org/uniprot/Q9JJZ9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cyclic nucleotide-gated cation channel beta-3|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=H1|||Helical; Name=H2|||Helical; Name=H3|||Helical; Name=H4|||Helical; Name=H5|||Helical; Name=H6|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000219321 http://togogenome.org/gene/10090:Rtf1 ^@ http://purl.uniprot.org/uniprot/A2AQ19|||http://purl.uniprot.org/uniprot/Q9CTY6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Plus3|||Polar residues|||RNA polymerase-associated protein RTF1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000401196 http://togogenome.org/gene/10090:Gzma ^@ http://purl.uniprot.org/uniprot/P11032|||http://purl.uniprot.org/uniprot/Q3U0N0 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Signal Peptide|||Splice Variant ^@ Activation peptide|||Charge relay system|||Granzyme A|||In isoform HF2.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Peptidase S1 domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000027395|||http://purl.uniprot.org/annotation/PRO_0000027396|||http://purl.uniprot.org/annotation/PRO_5004229713|||http://purl.uniprot.org/annotation/VSP_005373 http://togogenome.org/gene/10090:Stk11 ^@ http://purl.uniprot.org/uniprot/Q3V4A1|||http://purl.uniprot.org/uniprot/Q9WTK7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes ability to suppress cell growth. Decreased phosphorylation; when associated with A-366. No change in kinase activity; when associated with A-31; A-325 and A-366.|||Cysteine methyl ester|||Diminished interaction with CDKN1A and impaired ability to repair UV-induced DNA damage by affecting CDKN1AUV-induced degradation. Decreased phosphorylation; when associated with A-336. No change in kinase activity; when associated with A-31; A-325 and A-336.|||Disordered|||Does not affect nuclear localization. Does not prevent phosphorylation at S-431.|||Does not prevent S-farnesylation. Defects in neuron polarization.|||In isoform 2.|||In isoform 3.|||Loss of kinase activity and descreased phosphorylation.|||Loss of kinase activity.|||N6-acetyllysine|||No change in kinase activity; when associated with A-31; A-336 and A-366.|||No change in kinase activity; when associated with A-325; A-336 and A-366.|||Phosphoserine|||Phosphoserine; by autocatalysis, PKA, PKC/PRKCZ and RPS6KA1|||Phosphothreonine; by ATM and autocatalysis|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||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_0000260032|||http://purl.uniprot.org/annotation/PRO_0000422301|||http://purl.uniprot.org/annotation/VSP_052222|||http://purl.uniprot.org/annotation/VSP_052223|||http://purl.uniprot.org/annotation/VSP_060609|||http://purl.uniprot.org/annotation/VSP_060610 http://togogenome.org/gene/10090:Aven ^@ http://purl.uniprot.org/uniprot/A2AGL5|||http://purl.uniprot.org/uniprot/Q9D9K3 ^@ 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|||Cell death regulator Aven|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000064769 http://togogenome.org/gene/10090:Gigyf2 ^@ http://purl.uniprot.org/uniprot/G3UYG6|||http://purl.uniprot.org/uniprot/Q6Y7W8|||http://purl.uniprot.org/uniprot/Q8C585 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ 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 isoform 2.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Required for GRB10-binding ^@ http://purl.uniprot.org/annotation/PRO_0000270838|||http://purl.uniprot.org/annotation/VSP_022247 http://togogenome.org/gene/10090:Or6y1 ^@ http://purl.uniprot.org/uniprot/E9Q050 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Strn3 ^@ http://purl.uniprot.org/uniprot/B2RQS1|||http://purl.uniprot.org/uniprot/Q3TNV4|||http://purl.uniprot.org/uniprot/Q9ERG2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat ^@ Acidic residues|||Calmodulin-binding|||Caveolin-binding|||Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Striatin N-terminal|||Striatin-3|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000051237 http://togogenome.org/gene/10090:Prr27 ^@ http://purl.uniprot.org/uniprot/E9Q591|||http://purl.uniprot.org/uniprot/Q3SYJ2|||http://purl.uniprot.org/uniprot/Q9D5J3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Disordered|||Polar residues|||Pro residues|||Proline-rich 27 ^@ http://purl.uniprot.org/annotation/PRO_5012768116|||http://purl.uniprot.org/annotation/PRO_5013084978|||http://purl.uniprot.org/annotation/PRO_5015097429 http://togogenome.org/gene/10090:Mpc2 ^@ http://purl.uniprot.org/uniprot/Q9D023 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Topological Domain|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrial pyruvate carrier 2|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000212794 http://togogenome.org/gene/10090:Or8u9 ^@ http://purl.uniprot.org/uniprot/Q8VGR9 ^@ 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 8U9 ^@ http://purl.uniprot.org/annotation/PRO_0000150864 http://togogenome.org/gene/10090:Catsperb ^@ http://purl.uniprot.org/uniprot/A2RTF1 ^@ 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 ^@ Cation channel sperm-associated auxiliary subunit beta|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000295703 http://togogenome.org/gene/10090:Fam8a1 ^@ http://purl.uniprot.org/uniprot/Q3URQ4 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||RDD ^@ http://togogenome.org/gene/10090:Hypk ^@ http://purl.uniprot.org/uniprot/A0A8Q0PQH5|||http://purl.uniprot.org/uniprot/Q9CR41 ^@ 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|||Huntingtin-interacting protein K|||In isoform 2.|||Nascent polypeptide-associated complex subunit alpha-like UBA|||Phosphoserine|||Required for association with the NAA10-NAA15 complex ^@ http://purl.uniprot.org/annotation/PRO_0000274607|||http://purl.uniprot.org/annotation/VSP_022833 http://togogenome.org/gene/10090:Tmem262 ^@ http://purl.uniprot.org/uniprot/D3Z338 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cation channel sperm-associated auxiliary subunit TMEM262|||Cytoplasmic|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000454936 http://togogenome.org/gene/10090:Ccdc61 ^@ http://purl.uniprot.org/uniprot/Q3UJV1 ^@ 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|||Centrosomal protein CCDC61|||Disordered|||Head domain|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000311256 http://togogenome.org/gene/10090:Rnft2 ^@ http://purl.uniprot.org/uniprot/Q3UF64 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||RING finger and transmembrane domain-containing protein 2|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000279509|||http://purl.uniprot.org/annotation/VSP_023467 http://togogenome.org/gene/10090:Ptms ^@ http://purl.uniprot.org/uniprot/Q9D0J8 ^@ 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|||Disordered|||N-acetylserine|||N6-acetyllysine|||Parathymosin|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000191633 http://togogenome.org/gene/10090:Nipsnap3a ^@ http://purl.uniprot.org/uniprot/G3X8S9|||http://purl.uniprot.org/uniprot/Q9D9L2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ NIPSNAP ^@ http://togogenome.org/gene/10090:Nsd2 ^@ http://purl.uniprot.org/uniprot/D3Z3E0|||http://purl.uniprot.org/uniprot/Q8BJU7|||http://purl.uniprot.org/uniprot/Q8BVE8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||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|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ AWS|||Basic and acidic residues|||Disordered|||HMG box|||Histone-lysine N-methyltransferase NSD2|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform RE-IIBP.|||No methyltransferase activity.|||PHD-type 1|||PHD-type 2|||PHD-type 3|||PHD-type 4; atypical|||PWWP|||PWWP 1|||PWWP 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Post-SET|||Reduction in class switch recombination of the immunoglobulin heavy chain in B cells.|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000259520|||http://purl.uniprot.org/annotation/VSP_021424|||http://purl.uniprot.org/annotation/VSP_021425|||http://purl.uniprot.org/annotation/VSP_021426|||http://purl.uniprot.org/annotation/VSP_044420 http://togogenome.org/gene/10090:Commd7 ^@ http://purl.uniprot.org/uniprot/A2AU52|||http://purl.uniprot.org/uniprot/Q56A13|||http://purl.uniprot.org/uniprot/Q8BG94 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ COMM|||COMM domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000077400 http://togogenome.org/gene/10090:Cdca5 ^@ http://purl.uniprot.org/uniprot/Q9CPY3 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Disordered|||FGF motif|||In isoform 2.|||KEN box|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sororin ^@ http://purl.uniprot.org/annotation/PRO_0000089450|||http://purl.uniprot.org/annotation/VSP_014402 http://togogenome.org/gene/10090:Pan3 ^@ http://purl.uniprot.org/uniprot/Q640Q5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Splice Variant|||Zinc Finger ^@ C3H1-type|||Disordered|||In isoform 2.|||In isoform 3.|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000280526|||http://purl.uniprot.org/annotation/VSP_041650|||http://purl.uniprot.org/annotation/VSP_041651|||http://purl.uniprot.org/annotation/VSP_061950|||http://purl.uniprot.org/annotation/VSP_061951 http://togogenome.org/gene/10090:Zfp991 ^@ http://purl.uniprot.org/uniprot/Q8R1N3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Tbc1d2b ^@ http://purl.uniprot.org/uniprot/Q3U0J8 ^@ 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|||PH|||Phosphoserine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 2B ^@ http://purl.uniprot.org/annotation/PRO_0000315714 http://togogenome.org/gene/10090:Cox8c ^@ http://purl.uniprot.org/uniprot/A6H666 ^@ 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_0000370690 http://togogenome.org/gene/10090:9930111J21Rik2 ^@ http://purl.uniprot.org/uniprot/Q8CB10 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||IRG-type G ^@ http://togogenome.org/gene/10090:Acss3 ^@ http://purl.uniprot.org/uniprot/Q14DH7 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Acyl-CoA synthetase short-chain family member 3, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000320625|||http://purl.uniprot.org/annotation/VSP_031693|||http://purl.uniprot.org/annotation/VSP_031694 http://togogenome.org/gene/10090:Pde7b ^@ http://purl.uniprot.org/uniprot/E9Q0W7|||http://purl.uniprot.org/uniprot/Q8CBS2|||http://purl.uniprot.org/uniprot/Q9QXQ1 ^@ 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|||Phosphothreonine|||Proton donor|||cAMP-specific 3',5'-cyclic phosphodiesterase 7B ^@ http://purl.uniprot.org/annotation/PRO_0000198837 http://togogenome.org/gene/10090:Arhgap4 ^@ http://purl.uniprot.org/uniprot/B1AUX5|||http://purl.uniprot.org/uniprot/B1AUY2|||http://purl.uniprot.org/uniprot/Q80Z68|||http://purl.uniprot.org/uniprot/Q8BM00 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||F-BAR|||Polar residues|||Rho-GAP|||SH3 ^@ http://togogenome.org/gene/10090:Gabarapl1 ^@ http://purl.uniprot.org/uniprot/Q8R3R8 ^@ Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Chain|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Site|||Strand ^@ Cleavage; by ATG4B|||Gamma-aminobutyric acid receptor-associated protein-like 1|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000212370|||http://purl.uniprot.org/annotation/PRO_0000420209 http://togogenome.org/gene/10090:Lst1 ^@ http://purl.uniprot.org/uniprot/B8JJ61 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Or14c41 ^@ http://purl.uniprot.org/uniprot/Q7TS08 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Smyd3 ^@ http://purl.uniprot.org/uniprot/Q9CWR2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ C-terminal domain; essential for histone methyltransferase activity, nuclear localization and mediates interaction with HSP90AA1|||Histone-lysine N-methyltransferase SMYD3|||MYND-type|||N-acetylmethionine|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000218313 http://togogenome.org/gene/10090:Dnajb4 ^@ http://purl.uniprot.org/uniprot/Q9D832 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ DnaJ homolog subfamily B member 4|||J|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000071022 http://togogenome.org/gene/10090:Asphd2 ^@ http://purl.uniprot.org/uniprot/Q80VP9 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Aspartate beta-hydroxylase domain-containing protein 2|||Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000254163 http://togogenome.org/gene/10090:Klrb1c ^@ http://purl.uniprot.org/uniprot/A0A1U9W192|||http://purl.uniprot.org/uniprot/A0A1U9W195|||http://purl.uniprot.org/uniprot/E9Q3U6|||http://purl.uniprot.org/uniprot/G3UZI0|||http://purl.uniprot.org/uniprot/P27814 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Absence of Ca(2+) mobilization and no LCK association.|||C-type lectin|||Cytoplasmic|||Decreased Ca(2+) mobilization.|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Killer cell lectin-like receptor subfamily B member 1C|||LCK-binding motif|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046678|||http://purl.uniprot.org/annotation/VSP_022317 http://togogenome.org/gene/10090:Mrpl50 ^@ http://purl.uniprot.org/uniprot/Q8VDT9 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Large ribosomal subunit protein mL50 ^@ http://purl.uniprot.org/annotation/PRO_0000261660 http://togogenome.org/gene/10090:Mfsd10 ^@ http://purl.uniprot.org/uniprot/Q9D2V8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ Helical|||Major facilitator superfamily domain-containing protein 10|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000324659 http://togogenome.org/gene/10090:Trip10 ^@ http://purl.uniprot.org/uniprot/Q8CJ53 ^@ 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 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Cdc42-interacting protein 4|||Disordered|||F-BAR|||Impairs interaction with CDC42 and RHOQ and reduces insulin-stimulated translocation to the plasma membrane.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||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|||Polar 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_0000261439|||http://purl.uniprot.org/annotation/VSP_021722|||http://purl.uniprot.org/annotation/VSP_021723 http://togogenome.org/gene/10090:Gja8 ^@ http://purl.uniprot.org/uniprot/P28236|||http://purl.uniprot.org/uniprot/Q548M7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Initiator Methionine|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Initiator Methionine|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction alpha-8 protein|||Gap junction protein cysteine-rich|||Helical|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057831 http://togogenome.org/gene/10090:Tbc1d14 ^@ http://purl.uniprot.org/uniprot/E9PYB1|||http://purl.uniprot.org/uniprot/E9Q8K4|||http://purl.uniprot.org/uniprot/G3UVU5|||http://purl.uniprot.org/uniprot/Q5U224|||http://purl.uniprot.org/uniprot/Q76LY3|||http://purl.uniprot.org/uniprot/Q8CGA2|||http://purl.uniprot.org/uniprot/Q921M0 ^@ 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|||Phosphoserine|||Rab-GAP TBC|||TBC1 domain family member 14 ^@ http://purl.uniprot.org/annotation/PRO_0000208041 http://togogenome.org/gene/10090:Srd5a1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J136|||http://purl.uniprot.org/uniprot/Q68FF9|||http://purl.uniprot.org/uniprot/Q8BUR8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ 3-oxo-5-alpha-steroid 4-dehydrogenase 1|||Helical|||Steroid 5-alpha reductase C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000317711 http://togogenome.org/gene/10090:Gm3264 ^@ http://purl.uniprot.org/uniprot/A6NAU0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cyfip1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J119|||http://purl.uniprot.org/uniprot/Q7TMB8 ^@ 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 ^@ CYRIA/CYRIB Rac1 binding|||Cytoplasmic FMR1-interacting protein 1|||EIF4E-binding|||EIF4E-binding reduced by 20%; when associated with A-724.|||EIF4E-binding reduced by 20%; when associated with A-726.|||EIF4E-binding reduced by 60%; when associated with E-725, E-726 and K-730.|||EIF4E-binding reduced by 60%; when associated with K-724, E-725 and E-726.|||EIF4E-binding reduced by 60%; when associated with K-724, E-725 and K-730.|||EIF4E-binding reduced by 70%. EIF4E-binding reduced by 60%; when associated with K-724, E-726 and K-730.|||In isoform 2.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000279707|||http://purl.uniprot.org/annotation/VSP_052348 http://togogenome.org/gene/10090:Vmn2r59 ^@ http://purl.uniprot.org/uniprot/E9PUT5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245375 http://togogenome.org/gene/10090:Slx ^@ http://purl.uniprot.org/uniprot/D3Z347 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Ttc39c ^@ http://purl.uniprot.org/uniprot/Q8VE09 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 39C ^@ http://purl.uniprot.org/annotation/PRO_0000274353 http://togogenome.org/gene/10090:Prss57 ^@ http://purl.uniprot.org/uniprot/Q14B24 ^@ 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 57 ^@ http://purl.uniprot.org/annotation/PRO_0000295854 http://togogenome.org/gene/10090:Fmo2 ^@ http://purl.uniprot.org/uniprot/Q8K2I3 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Dimethylaniline monooxygenase [N-oxide-forming] 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000147648 http://togogenome.org/gene/10090:LOC122152371 ^@ http://purl.uniprot.org/uniprot/Q3U1U6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:P2rx3 ^@ http://purl.uniprot.org/uniprot/Q3UR32 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000269195 http://togogenome.org/gene/10090:Rs1 ^@ http://purl.uniprot.org/uniprot/Q9Z1L4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Signal Peptide ^@ Decreases phosphatidylserine binding.|||F5/8 type C|||Interchain|||Interchain (with C-223)|||Interchain (with C-59)|||Retinoschisin ^@ http://purl.uniprot.org/annotation/PRO_0000022696 http://togogenome.org/gene/10090:Cdc5l ^@ http://purl.uniprot.org/uniprot/Q3UCF2|||http://purl.uniprot.org/uniprot/Q6A068 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||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|||HTH myb-type 1|||HTH myb-type 2|||Interaction with DAPK3|||Interaction with PLRG1|||Interaction with PPP1R8|||Myb-like|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with CTNNBL1 ^@ http://purl.uniprot.org/annotation/PRO_0000197092 http://togogenome.org/gene/10090:Ednrb ^@ http://purl.uniprot.org/uniprot/P48302 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000012730 http://togogenome.org/gene/10090:Plaat5 ^@ http://purl.uniprot.org/uniprot/Q9CPX5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Acyl-thioester intermediate|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 3.|||LRAT|||Phospholipase A and acyltransferase 5|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000152489|||http://purl.uniprot.org/annotation/VSP_007448|||http://purl.uniprot.org/annotation/VSP_007449|||http://purl.uniprot.org/annotation/VSP_007450|||http://purl.uniprot.org/annotation/VSP_044623 http://togogenome.org/gene/10090:Rpl15 ^@ http://purl.uniprot.org/uniprot/Q5M8Q0|||http://purl.uniprot.org/uniprot/Q9CZM2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL15|||N-myristoyl glycine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000127528 http://togogenome.org/gene/10090:Or51a42 ^@ http://purl.uniprot.org/uniprot/Q8VGY1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Defb34 ^@ http://purl.uniprot.org/uniprot/Q7TNV8 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Region|||Signal Peptide ^@ Beta-defensin 34|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000006946 http://togogenome.org/gene/10090:Egln2 ^@ http://purl.uniprot.org/uniprot/Q80X29|||http://purl.uniprot.org/uniprot/Q91YE2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Beta(2)beta(3) 'finger-like' loop|||Bipartite nuclear localization signal|||Disordered|||Fe2OG dioxygenase|||Phosphoserine|||Polar residues|||Prolyl hydroxylase EGLN2 ^@ http://purl.uniprot.org/annotation/PRO_0000206665 http://togogenome.org/gene/10090:Kcnv2 ^@ http://purl.uniprot.org/uniprot/Q8CFS6 ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Motif|||Region|||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|||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_0000320144 http://togogenome.org/gene/10090:Tial1 ^@ http://purl.uniprot.org/uniprot/D3Z3Y4|||http://purl.uniprot.org/uniprot/P70318|||http://purl.uniprot.org/uniprot/Q545C1|||http://purl.uniprot.org/uniprot/Q921W2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolishes nuclear export.|||Disordered|||Impairs nuclear localization.|||N6-acetyllysine|||No effect on nuclear localization.|||Nucleolysin TIAR|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000081979 http://togogenome.org/gene/10090:Bfar ^@ http://purl.uniprot.org/uniprot/A0A0R4J040|||http://purl.uniprot.org/uniprot/Q8R079 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger ^@ Basic and acidic residues|||Bifunctional apoptosis regulator|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||RING-type|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000055823|||http://purl.uniprot.org/annotation/VSP_016651 http://togogenome.org/gene/10090:Rab6a ^@ http://purl.uniprot.org/uniprot/P35279 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Splice Variant ^@ Cysteine methyl ester|||Effector region|||In isoform 2.|||Loss of binding to rabkinesin-6.|||Loss of binding to rabkinesin-6; when associated with L-73.|||Loss of binding to rabkinesin-6; when associated with N-28.|||N-acetylserine|||Phosphoserine|||Ras-related protein Rab-6A|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121113|||http://purl.uniprot.org/annotation/VSP_005528 http://togogenome.org/gene/10090:Tuba3b ^@ http://purl.uniprot.org/uniprot/P05214|||http://purl.uniprot.org/uniprot/Q5FW91 ^@ 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|||Site ^@ 3'-nitrotyrosine|||Detyrosinated tubulin alpha-3 chain|||Involved in polymerization|||MREC motif|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Tubulin alpha-3 chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase ^@ http://purl.uniprot.org/annotation/PRO_0000048122|||http://purl.uniprot.org/annotation/PRO_0000437401 http://togogenome.org/gene/10090:Cyb5a ^@ http://purl.uniprot.org/uniprot/G5E850|||http://purl.uniprot.org/uniprot/P56395|||http://purl.uniprot.org/uniprot/Q544Z9 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Transmembrane ^@ Cytochrome b5|||Cytochrome b5 heme-binding|||Helical|||N-acetylalanine|||N6-acetyllysine|||Removed|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000166011 http://togogenome.org/gene/10090:Nphp3 ^@ http://purl.uniprot.org/uniprot/Q7TNH6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Disordered|||In isoform 2.|||In pcy.|||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_0000106302|||http://purl.uniprot.org/annotation/VSP_014492|||http://purl.uniprot.org/annotation/VSP_014493 http://togogenome.org/gene/10090:4921504E06Rik ^@ http://purl.uniprot.org/uniprot/Q8CET2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ DUF4709|||DUF4724|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Syt12 ^@ http://purl.uniprot.org/uniprot/Q14AG7|||http://purl.uniprot.org/uniprot/Q920N7 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ C2|||C2 1|||C2 2|||Cytoplasmic|||Helical|||Loss of phosphorylation by PKA. Reduces long-term potentiation in mossy-fiber synapses in the hippocampus but has no effect on short-term potentiation. Inhibits the effect of forskolin on synaptic transmission and inhibitory post-synaptic currents. No effect on excitatory and inhibitory synaptic transmission in the hippocampus. No effect on brain structure.|||Phosphoserine|||Phosphoserine; by PKA|||Synaptotagmin-12|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000183973 http://togogenome.org/gene/10090:Fnbp1l ^@ http://purl.uniprot.org/uniprot/E9PUI5|||http://purl.uniprot.org/uniprot/E9PUK3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||F-BAR|||Polar residues|||REM-1|||SH3 ^@ http://togogenome.org/gene/10090:Cdyl ^@ http://purl.uniprot.org/uniprot/Q9WTK2 ^@ 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 ^@ Abolishes CoA-binding. No effect on transcriptional repressor activity.|||Acetyl-CoA-binding domain|||Chromo|||Chromodomain Y-like protein|||Disordered|||In isoform 2.|||Interaction with EZH2|||N6,N6,N6-trimethyllysine; by EHMT2; alternate|||N6,N6-dimethyllysine; by EHMT2; alternate|||N6-methyllysine; by EHMT2; alternate|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080222|||http://purl.uniprot.org/annotation/VSP_026385|||http://purl.uniprot.org/annotation/VSP_026386 http://togogenome.org/gene/10090:Adam3 ^@ http://purl.uniprot.org/uniprot/F8VQ03|||http://purl.uniprot.org/uniprot/Q62287|||http://purl.uniprot.org/uniprot/Q810R6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ A disintegrin and metallopeptidase domain 3|||Basic and acidic residues|||Disintegrin|||Disordered|||EGF-like|||Helical|||Peptidase M12B ^@ http://purl.uniprot.org/annotation/PRO_5004265883|||http://purl.uniprot.org/annotation/PRO_5010674208 http://togogenome.org/gene/10090:Pdzd4 ^@ http://purl.uniprot.org/uniprot/A2AFG3|||http://purl.uniprot.org/uniprot/Q9QY39 ^@ 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|||PDZ|||PDZ domain-containing protein 4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000055922 http://togogenome.org/gene/10090:Lingo1 ^@ http://purl.uniprot.org/uniprot/A9DA50|||http://purl.uniprot.org/uniprot/Q9D1T0 ^@ 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|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||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 and immunoglobulin-like domain-containing nogo receptor-interacting protein 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000328643|||http://purl.uniprot.org/annotation/PRO_5015086723 http://togogenome.org/gene/10090:Pou2af1 ^@ http://purl.uniprot.org/uniprot/Q542H4|||http://purl.uniprot.org/uniprot/Q64693 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||OCA|||POU domain class 2-associating factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000058019 http://togogenome.org/gene/10090:Ube2cbp ^@ http://purl.uniprot.org/uniprot/Q8BX13 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ E3 ubiquitin-protein ligase E3D|||HECT-like|||Interaction with UBE2C|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000311191 http://togogenome.org/gene/10090:Or1j13 ^@ http://purl.uniprot.org/uniprot/Q8VGK9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sf3b2 ^@ http://purl.uniprot.org/uniprot/Q3UJB0 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Pro residues|||SAP ^@ http://togogenome.org/gene/10090:Cst6 ^@ http://purl.uniprot.org/uniprot/Q9D1B1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Cystatin ^@ http://purl.uniprot.org/annotation/PRO_5015020149 http://togogenome.org/gene/10090:Hsp90ab1 ^@ http://purl.uniprot.org/uniprot/P11499|||http://purl.uniprot.org/uniprot/Q71LX8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ Basic and acidic residues|||Cleaved under oxidative stress|||Disordered|||Heat shock protein HSP 90-beta|||Histidine kinase/HSP90-like ATPase|||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|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphoserine; by PLK2 and PLK3|||Phosphothreonine|||Phosphotyrosine|||Removed|||S-nitrosocysteine|||TPR repeat-binding ^@ http://purl.uniprot.org/annotation/PRO_0000062918 http://togogenome.org/gene/10090:Atg5 ^@ http://purl.uniprot.org/uniprot/Q99J83 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Crosslink|||Modified Residue|||Mutagenesis Site ^@ Autophagy protein 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12)|||Loss of conjugation.|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000218995 http://togogenome.org/gene/10090:Ubqlnl ^@ http://purl.uniprot.org/uniprot/Q14DL0 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Domain Extent|||Helix|||Sequence Conflict ^@ UBA|||Ubiquilin-like protein|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000307792 http://togogenome.org/gene/10090:Decr2 ^@ http://purl.uniprot.org/uniprot/Q9WV68 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif ^@ Microbody targeting signal|||N-acetylalanine|||N6-acetyllysine|||Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000054560 http://togogenome.org/gene/10090:Xlr4a ^@ http://purl.uniprot.org/uniprot/A2BI40 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Aldh2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JEU1|||http://purl.uniprot.org/uniprot/P47738|||http://purl.uniprot.org/uniprot/Q544B1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ Aldehyde dehydrogenase|||Aldehyde dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Nucleophile|||Proton acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000007169 http://togogenome.org/gene/10090:Zic3 ^@ http://purl.uniprot.org/uniprot/Q62521 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Motif|||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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Nuclear localization signal|||Polar residues|||Zinc finger protein ZIC 3 ^@ http://purl.uniprot.org/annotation/PRO_0000047251|||http://purl.uniprot.org/annotation/VSP_044011 http://togogenome.org/gene/10090:Vstm5 ^@ http://purl.uniprot.org/uniprot/Q9D806 ^@ 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_0000340694 http://togogenome.org/gene/10090:Mreg ^@ http://purl.uniprot.org/uniprot/Q6NVG5 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure ^@ Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site ^@ Cholesterol-binding sequence motif|||Loss of location at the melanosome membrane; when associated with 11-SSSS-14 and S-16.|||Loss of location at the melanosome membrane; when associated with 11-SSSS-14 and S-18.|||Loss of location at the melanosome membrane; when associated with S-16 and S-18.|||Loss of the ability to promote lysosome clustering at the center of the cell. No effect on location at lysosome membranes.|||Melanoregulin|||Mildly reduced ability to promote lysosome clustering at the center of the cell; when associated with K-177 and K-180.|||Mildly reduced ability to promote lysosome clustering at the center of the cell; when associated with K-177 and K-181.|||Mildly reduced ability to promote lysosome clustering at the center of the cell; when associated with K-180 and K-181.|||No effect on location at the melanosome membrane.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000292176 http://togogenome.org/gene/10090:Golm1 ^@ http://purl.uniprot.org/uniprot/Q3TIZ8|||http://purl.uniprot.org/uniprot/Q91XA2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Golgi membrane protein 1|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087553 http://togogenome.org/gene/10090:Eid2 ^@ http://purl.uniprot.org/uniprot/Q6X7S9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||EP300-interacting inhibitor of differentiation 2|||Omega-N-methylarginine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315902 http://togogenome.org/gene/10090:Hspa5 ^@ http://purl.uniprot.org/uniprot/P20029|||http://purl.uniprot.org/uniprot/Q3U7T8 ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 3'-nitrotyrosine|||78 kDa glucose-regulated protein|||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)|||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_0000013568|||http://purl.uniprot.org/annotation/PRO_5004229975 http://togogenome.org/gene/10090:Ppp1r1c ^@ http://purl.uniprot.org/uniprot/Q8BKK4 ^@ 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.|||Polar residues|||Protein phosphatase 1 regulatory subunit 1C ^@ http://purl.uniprot.org/annotation/PRO_0000286444|||http://purl.uniprot.org/annotation/VSP_025059|||http://purl.uniprot.org/annotation/VSP_025060 http://togogenome.org/gene/10090:Pak2 ^@ http://purl.uniprot.org/uniprot/Q5DTJ2|||http://purl.uniprot.org/uniprot/Q8CIN4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Site ^@ Autoregulatory region|||Basic and acidic residues|||CRIB|||Cleavage; by caspase-3 or caspase-3-like proteases|||Disordered|||GTPase-binding|||N-acetylserine|||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_0000086466|||http://purl.uniprot.org/annotation/PRO_0000304924|||http://purl.uniprot.org/annotation/PRO_0000304925 http://togogenome.org/gene/10090:H1f7 ^@ http://purl.uniprot.org/uniprot/Q8CJI4 ^@ 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|||Basic residues|||Disordered|||Phosphoserine|||Polar residues|||Testis-specific H1 histone ^@ http://purl.uniprot.org/annotation/PRO_0000343415 http://togogenome.org/gene/10090:Or6b6 ^@ http://purl.uniprot.org/uniprot/Q9EPG2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Esd ^@ http://purl.uniprot.org/uniprot/H3BKH6|||http://purl.uniprot.org/uniprot/Q9R0P3 ^@ Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Charge relay system|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Removed|||S-formylglutathione hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000210340 http://togogenome.org/gene/10090:Lcat ^@ http://purl.uniprot.org/uniprot/P16301 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site ^@ Charge relay system|||Determinant for substrate specificity|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphatidylcholine-sterol acyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000017804 http://togogenome.org/gene/10090:Maml2 ^@ http://purl.uniprot.org/uniprot/E9Q7L5|||http://purl.uniprot.org/uniprot/F6U238|||http://purl.uniprot.org/uniprot/Q6ZPH8|||http://purl.uniprot.org/uniprot/Q8BYF1 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Neurogenic mastermind-like N-terminal|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Cacng5 ^@ http://purl.uniprot.org/uniprot/Q544Q4|||http://purl.uniprot.org/uniprot/Q8VHW4 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Voltage-dependent calcium channel gamma-5 subunit ^@ http://purl.uniprot.org/annotation/PRO_0000164682 http://togogenome.org/gene/10090:Pias4 ^@ http://purl.uniprot.org/uniprot/Q3ULQ6|||http://purl.uniprot.org/uniprot/Q9JM05 ^@ 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 ^@ Abrogates sumoylation of LEF1 and increases LEF1-mediated transcriptional activity; when associated with S-330; A-337 and S-340.|||Abrogates sumoylation of LEF1 and increases LEF1-mediated transcriptional activity; when associated with S-330; S-335 and A-337.|||Abrogates sumoylation of LEF1 and increases LEF1-mediated transcriptional activity; when associated with S-330; S-335 and S-340.|||Abrogates sumoylation of LEF1 and increases LEF1-mediated transcriptional activity; when associated with S-335; A-337 and S-340.|||Acidic residues|||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|||LXXLL motif|||N-acetylalanine|||N6-acetyllysine|||No effect on sumoylation of LEF1, nor on LEF1-binding.|||PINIT|||Removed|||SAP|||SP-RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000218983 http://togogenome.org/gene/10090:Gfap ^@ http://purl.uniprot.org/uniprot/P03995 ^@ 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 ^@ Citrulline|||Coil 1A|||Coil 1B|||Coil 2A|||Coil 2B|||Glial fibrillary acidic protein|||Head|||IF rod|||In isoform 2.|||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_0000063806|||http://purl.uniprot.org/annotation/VSP_017053 http://togogenome.org/gene/10090:Raet1e ^@ http://purl.uniprot.org/uniprot/D7F2B6|||http://purl.uniprot.org/uniprot/Q9CZQ6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||GPI-anchor amidated serine|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form|||Retinoic acid early-inducible protein 1|||Retinoic acid early-inducible protein 1-epsilon ^@ http://purl.uniprot.org/annotation/PRO_0000019735|||http://purl.uniprot.org/annotation/PRO_0000019736|||http://purl.uniprot.org/annotation/PRO_5009952602 http://togogenome.org/gene/10090:Myo10 ^@ http://purl.uniprot.org/uniprot/F8VQB6|||http://purl.uniprot.org/uniprot/Q80TR9 ^@ 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|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Actin-binding|||Basic and acidic residues|||Disordered|||FERM|||IQ 1|||IQ 2|||IQ 3|||In isoform Headless.|||MyTH4|||Myosin motor|||N-acetylmethionine|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAH|||Unconventional myosin-X ^@ http://purl.uniprot.org/annotation/PRO_0000416244|||http://purl.uniprot.org/annotation/VSP_054978 http://togogenome.org/gene/10090:Pcdhb12 ^@ http://purl.uniprot.org/uniprot/Q91Y07 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099519 http://togogenome.org/gene/10090:4930590J08Rik ^@ http://purl.uniprot.org/uniprot/Q8CDN1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Uncharacterized protein C3orf20 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000228844 http://togogenome.org/gene/10090:Tmprss11d ^@ http://purl.uniprot.org/uniprot/Q8VHK8 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Charge relay system|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Interchain (between non-catalytic and catalytic chains)|||Peptidase S1|||SEA|||Transmembrane protease serine 11D catalytic chain|||Transmembrane protease serine 11D non-catalytic chain ^@ http://purl.uniprot.org/annotation/PRO_0000027887|||http://purl.uniprot.org/annotation/PRO_0000027888|||http://purl.uniprot.org/annotation/VSP_014519|||http://purl.uniprot.org/annotation/VSP_014520 http://togogenome.org/gene/10090:Rps17 ^@ http://purl.uniprot.org/uniprot/P63276 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Crosslink|||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|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Small ribosomal subunit protein eS17 ^@ http://purl.uniprot.org/annotation/PRO_0000141526 http://togogenome.org/gene/10090:Ttbk1 ^@ http://purl.uniprot.org/uniprot/A0A286YDE4|||http://purl.uniprot.org/uniprot/Q6PCN3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Tau-tubulin kinase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000278542 http://togogenome.org/gene/10090:Cenpm ^@ http://purl.uniprot.org/uniprot/Q9CQA0 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ Centromere protein M|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000058225|||http://purl.uniprot.org/annotation/VSP_020440 http://togogenome.org/gene/10090:Rnaset2b ^@ http://purl.uniprot.org/uniprot/C0HKG5|||http://purl.uniprot.org/uniprot/C0HKG6|||http://purl.uniprot.org/uniprot/Q5FWA0 ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Ribonuclease T2-A|||Ribonuclease T2-B ^@ http://purl.uniprot.org/annotation/PRO_0000030988|||http://purl.uniprot.org/annotation/PRO_0000440153 http://togogenome.org/gene/10090:Cks2 ^@ http://purl.uniprot.org/uniprot/P56390 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Cyclin-dependent kinases regulatory subunit 2|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000206238 http://togogenome.org/gene/10090:Mecp2 ^@ http://purl.uniprot.org/uniprot/Q9Z2D6 ^@ 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|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ A.T hook 1|||A.T hook 2|||Abolishes interaction with NCOR2.|||Abolishes interaction with NCOR2. Mice exhibit a severe neurological Rett syndrome-like phenotype.|||Basic and acidic residues|||Disordered|||In isoform B.|||Interaction with NCOR2|||Interaction with TBL1XR1|||Loss of localization to the nucleus. Distributes diffusely in cells. Interacts normally with NCOR2.|||MBD|||Methyl-CpG-binding protein 2|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CaMK2|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000096347|||http://purl.uniprot.org/annotation/VSP_022949 http://togogenome.org/gene/10090:Or2y1c ^@ http://purl.uniprot.org/uniprot/Q7TQT0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kcnh1 ^@ http://purl.uniprot.org/uniprot/A0A1L1M1J8|||http://purl.uniprot.org/uniprot/Q3UHC9|||http://purl.uniprot.org/uniprot/Q60603 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||CAD (involved in subunit assembly)|||Calmodulin-binding|||Cyclic nucleotide-binding|||Cytoplasmic|||Decreases affinity for CALM 230-fold; when associated with S-737.|||Decreases affinity for CALM 230-fold; when associated with S-740.|||Decreases affinity for CALM about 30-fold.|||Decreases the affinity for CALM.|||Decreases the rate of channel opening. No effect; when associated with D-57.|||Decreases the rate of channel opening. No effect; when associated with R-642.|||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|||Increases the affinity for CALM.|||Interaction with cyclic nucleotide-binding pocket|||Mildly increases the affinity for CALM.|||N-linked (GlcNAc...) asparagine|||No effect on affinity for CALM; when associated with A-737.|||No effect on affinity for CALM; when associated with A-740.|||PAC|||PAS|||Phosphoserine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 1|||Required for phosphatidylinositol bisphosphate binding|||Selectivity filter|||Strongly shifts the voltage-dependent channel activation to more depolarized membrane potentials.|||Strongly shifts the voltage-dependent channel activation to much more depolarized membrane potentials. ^@ http://purl.uniprot.org/annotation/PRO_0000053995 http://togogenome.org/gene/10090:Eif2b2 ^@ http://purl.uniprot.org/uniprot/Q99LD9 ^@ Chain|||Molecule Processing ^@ Chain ^@ Translation initiation factor eIF-2B subunit beta ^@ http://purl.uniprot.org/annotation/PRO_0000156062 http://togogenome.org/gene/10090:Col1a1 ^@ http://purl.uniprot.org/uniprot/P11087 ^@ 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|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 3-hydroxyproline|||4-hydroxyproline|||5-hydroxylysine|||5-hydroxylysine; alternate|||Allysine|||C-terminal propeptide|||Cell attachment site|||Collagen alpha-1(I) chain|||Disordered|||Fibrillar collagen NC1|||In isoform 2.|||Interchain (with C-1254)|||Interchain (with C-1271)|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide|||Nonhelical region (C-terminal)|||Nonhelical region (N-terminal)|||O-linked (Gal...) hydroxylysine; alternate|||Phosphoserine|||Pro residues|||Triple-helical region|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000005722|||http://purl.uniprot.org/annotation/PRO_0000005723|||http://purl.uniprot.org/annotation/PRO_0000005724|||http://purl.uniprot.org/annotation/VSP_016548 http://togogenome.org/gene/10090:Spink7 ^@ http://purl.uniprot.org/uniprot/Q6IE32 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Site ^@ Kazal-like|||Reactive bond|||Serine protease inhibitor Kazal-type 7 ^@ http://purl.uniprot.org/annotation/PRO_0000016566 http://togogenome.org/gene/10090:Snx7 ^@ http://purl.uniprot.org/uniprot/F8WI30|||http://purl.uniprot.org/uniprot/Q5M8N3 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||PX ^@ http://togogenome.org/gene/10090:Als2cl ^@ http://purl.uniprot.org/uniprot/A0A0R4J1X4|||http://purl.uniprot.org/uniprot/Q60I26 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant ^@ ALS2 C-terminal-like protein|||In isoform 2.|||In isoform 3.|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN 8|||VPS9 ^@ http://purl.uniprot.org/annotation/PRO_0000313850|||http://purl.uniprot.org/annotation/VSP_030172|||http://purl.uniprot.org/annotation/VSP_030173 http://togogenome.org/gene/10090:Wsb2 ^@ http://purl.uniprot.org/uniprot/O54929 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ SOCS box|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat and SOCS box-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000051461 http://togogenome.org/gene/10090:Kdm8 ^@ http://purl.uniprot.org/uniprot/Q9CXT6 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region ^@ Bifunctional peptidase and arginyl-hydroxylase JMJD5|||Disordered|||Interaction with RCCD1|||JmjC ^@ http://purl.uniprot.org/annotation/PRO_0000292011 http://togogenome.org/gene/10090:Rnpepl1 ^@ http://purl.uniprot.org/uniprot/G5E872 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Region|||Site ^@ Aminopeptidase RNPEPL1|||Disordered|||Proton acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000439278 http://togogenome.org/gene/10090:Hnrnpf ^@ http://purl.uniprot.org/uniprot/Q9Z2X1 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ 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|||In isoform 2.|||Interaction with RNA|||N-acetylmethionine|||N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F, N-terminally processed|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2|||RRM 3|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000253053|||http://purl.uniprot.org/annotation/PRO_0000367116|||http://purl.uniprot.org/annotation/VSP_021004 http://togogenome.org/gene/10090:Eml4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0H0|||http://purl.uniprot.org/uniprot/A0A0R4J1G7|||http://purl.uniprot.org/uniprot/A0A3Q4EHV9|||http://purl.uniprot.org/uniprot/A7ISP9|||http://purl.uniprot.org/uniprot/F8WJ93|||http://purl.uniprot.org/uniprot/Q3UMY5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Echinoderm microtubule-associated protein-like 4|||HELP|||Helical|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Microtubule-binding|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by NEK6|||Phosphoserine; by NEK7|||Phosphothreonine|||Phosphothreonine; by NEK6 and NEK7|||Phosphotyrosine|||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_0000284392|||http://purl.uniprot.org/annotation/VSP_024484|||http://purl.uniprot.org/annotation/VSP_024485|||http://purl.uniprot.org/annotation/VSP_024486|||http://purl.uniprot.org/annotation/VSP_024487 http://togogenome.org/gene/10090:Pigyl ^@ http://purl.uniprot.org/uniprot/P0C1P0|||http://purl.uniprot.org/uniprot/Q9CQH2 ^@ 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|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y ^@ http://purl.uniprot.org/annotation/PRO_0000246312 http://togogenome.org/gene/10090:Or4c114 ^@ http://purl.uniprot.org/uniprot/Q7TR04 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:P2ry13 ^@ http://purl.uniprot.org/uniprot/Q9D8I2 ^@ 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 13 ^@ http://purl.uniprot.org/annotation/PRO_0000070042 http://togogenome.org/gene/10090:Taar7f ^@ http://purl.uniprot.org/uniprot/Q5QD08 ^@ 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|||Trace amine-associated receptor 7f ^@ http://purl.uniprot.org/annotation/PRO_0000070171 http://togogenome.org/gene/10090:Puf60 ^@ http://purl.uniprot.org/uniprot/Q3UEB3 ^@ 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 and isoform 3.|||In isoform 3.|||Inhibits homodimerization|||Inhibits transcriptional repression, interaction with ERCC3 and apoptosis induction|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Poly(U)-binding-splicing factor PUF60|||RRM 1|||RRM 2|||RRM 3; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000299520|||http://purl.uniprot.org/annotation/VSP_027720|||http://purl.uniprot.org/annotation/VSP_027721 http://togogenome.org/gene/10090:Pbsn ^@ http://purl.uniprot.org/uniprot/O08976|||http://purl.uniprot.org/uniprot/Q3UV89 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding|||Lipocalin/cytosolic fatty-acid binding domain-containing protein|||Probasin ^@ http://purl.uniprot.org/annotation/PRO_0000017954|||http://purl.uniprot.org/annotation/PRO_5010843488 http://togogenome.org/gene/10090:Tnfsf18 ^@ http://purl.uniprot.org/uniprot/Q7TS55 ^@ 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; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Tumor necrosis factor ligand superfamily member 18 ^@ http://purl.uniprot.org/annotation/PRO_0000415333 http://togogenome.org/gene/10090:Alyref2 ^@ http://purl.uniprot.org/uniprot/G3X9I4|||http://purl.uniprot.org/uniprot/Q9JJW6 ^@ 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 NXF1; when associated with E-29.|||Abolishes interaction with NXF1; when associated with E-30.|||Aly/REF export factor 2|||Asymmetric dimethylarginine; alternate; by PRMT1; in vitro|||Asymmetric dimethylarginine; by PRMT1; in vitro|||Basic and acidic residues|||Disordered|||Impairs interaction with NXF1.|||In isoform 2.|||Interaction with HHV-8 ORF57 protein and with ICP27 from HHV-1|||Omega-N-methylarginine; alternate; by PRMT1; in vitro|||Polar residues|||RRM|||Sufficient for RNA-binding, interaction with NXF1-NXT1 ^@ http://purl.uniprot.org/annotation/PRO_0000081976|||http://purl.uniprot.org/annotation/VSP_008598 http://togogenome.org/gene/10090:Zfp110 ^@ http://purl.uniprot.org/uniprot/A0A0R4J249|||http://purl.uniprot.org/uniprot/Q923B3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Abolishes ubiquitination by TRAF6, binding to SQSTM1/p62, translocation to the nucleus and NGFR/p75(NTR)-mediated apoptosis.|||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 ubiquitin)|||KRAB|||KRAB 1|||KRAB 2|||Neurotrophin receptor-interacting factor 1|||Polar residues|||SCAN box ^@ http://purl.uniprot.org/annotation/PRO_0000406966 http://togogenome.org/gene/10090:Mup4 ^@ http://purl.uniprot.org/uniprot/A2ANT5|||http://purl.uniprot.org/uniprot/P11590 ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Strand ^@ Lipocalin/cytosolic fatty-acid binding|||Major urinary protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000017930|||http://purl.uniprot.org/annotation/PRO_5014296802 http://togogenome.org/gene/10090:Cpa1 ^@ http://purl.uniprot.org/uniprot/Q7TPZ8 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Propeptide|||Signal Peptide ^@ Activation peptide|||Carboxypeptidase A1|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004347|||http://purl.uniprot.org/annotation/PRO_0000004348 http://togogenome.org/gene/10090:Kifbp ^@ http://purl.uniprot.org/uniprot/Q6ZPU9 ^@ 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.|||In isoform 3.|||KIF-binding protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000050792|||http://purl.uniprot.org/annotation/VSP_015213|||http://purl.uniprot.org/annotation/VSP_015214|||http://purl.uniprot.org/annotation/VSP_015215 http://togogenome.org/gene/10090:Mtus2 ^@ http://purl.uniprot.org/uniprot/Q3UHD3 ^@ 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 3.|||In isoform 4.|||Localization to the growing distal tip of microtubules|||Mediates interaction with MAPRE1|||Microtubule-associated tumor suppressor candidate 2 homolog|||Phosphoserine|||Polar residues|||Sufficient for interaction with KIF2C ^@ http://purl.uniprot.org/annotation/PRO_0000280112|||http://purl.uniprot.org/annotation/VSP_023544|||http://purl.uniprot.org/annotation/VSP_023545|||http://purl.uniprot.org/annotation/VSP_023546|||http://purl.uniprot.org/annotation/VSP_023548 http://togogenome.org/gene/10090:Chd2 ^@ http://purl.uniprot.org/uniprot/E9PZM4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Acidic residues|||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|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000425206 http://togogenome.org/gene/10090:Slc22a16 ^@ http://purl.uniprot.org/uniprot/B2RRB7|||http://purl.uniprot.org/uniprot/Q497L8 ^@ 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|||Solute carrier family 22 member 16 ^@ http://purl.uniprot.org/annotation/PRO_0000318992|||http://purl.uniprot.org/annotation/VSP_031339 http://togogenome.org/gene/10090:Dgkd ^@ http://purl.uniprot.org/uniprot/E9PUQ8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ DAGKc|||Diacylglycerol kinase delta|||Disordered|||PH|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Polar residues|||Pro residues|||Regulates association with membranes|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000450663 http://togogenome.org/gene/10090:Il21 ^@ http://purl.uniprot.org/uniprot/E9PX58|||http://purl.uniprot.org/uniprot/Q5SUE2|||http://purl.uniprot.org/uniprot/Q9ES17 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Interleukin-21|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015506|||http://purl.uniprot.org/annotation/PRO_5003243005|||http://purl.uniprot.org/annotation/PRO_5014309957 http://togogenome.org/gene/10090:Defb4 ^@ http://purl.uniprot.org/uniprot/P82019|||http://purl.uniprot.org/uniprot/Q499H9 ^@ Chain|||Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Variant|||Signal Peptide ^@ Chain|||Disulfide Bond|||Helix|||Modified Residue|||Peptide|||Sequence Variant|||Signal Peptide ^@ Beta-defensin 4|||In strain: FVB.|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000006930|||http://purl.uniprot.org/annotation/PRO_5014309295 http://togogenome.org/gene/10090:Ttll7 ^@ http://purl.uniprot.org/uniprot/A0A0G2LB90|||http://purl.uniprot.org/uniprot/A4Q9F0 ^@ 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|||Site|||Splice Variant ^@ Binds negatively charged residues of beta-tubulin C-terminal tails|||Disordered|||In isoform 2.|||Loss of activity.|||Polar residues|||TTL|||Tubulin polyglutamylase TTLL7|||c-MTBD region ^@ http://purl.uniprot.org/annotation/PRO_0000326163|||http://purl.uniprot.org/annotation/VSP_052730|||http://purl.uniprot.org/annotation/VSP_052731 http://togogenome.org/gene/10090:Actb ^@ http://purl.uniprot.org/uniprot/P60710 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Actin, cytoplasmic 1|||Actin, cytoplasmic 1, N-terminally processed|||Methionine (R)-sulfoxide|||N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed|||N-acetylmethionine|||N6-methyllysine|||Removed; alternate|||Tele-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000000775|||http://purl.uniprot.org/annotation/PRO_0000367076 http://togogenome.org/gene/10090:Sall1 ^@ http://purl.uniprot.org/uniprot/Q6P5E3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ogfod1 ^@ http://purl.uniprot.org/uniprot/Q3U0K8 ^@ 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 ^@ Disordered|||Fe2OG dioxygenase|||In isoform 2.|||In isoform 3.|||Polar residues|||Prolyl 3-hydroxylase OGFOD1 ^@ http://purl.uniprot.org/annotation/PRO_0000288975|||http://purl.uniprot.org/annotation/VSP_025853|||http://purl.uniprot.org/annotation/VSP_025854 http://togogenome.org/gene/10090:Cbr4 ^@ http://purl.uniprot.org/uniprot/Q91VT4 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site ^@ 3-oxoacyl-[acyl-carrier-protein] reductase|||Important for interaction with acyl carrier protein (ACP)|||N-acetylmethionine|||N6-acetyllysine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000319879 http://togogenome.org/gene/10090:Tmem196 ^@ http://purl.uniprot.org/uniprot/D3YWQ9|||http://purl.uniprot.org/uniprot/V9GX04 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Prl5a1 ^@ http://purl.uniprot.org/uniprot/A0A0M6L0X8|||http://purl.uniprot.org/uniprot/Q9JII2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Polar residues|||Prolactin-5A1 ^@ http://purl.uniprot.org/annotation/PRO_0000045212|||http://purl.uniprot.org/annotation/PRO_5015043320 http://togogenome.org/gene/10090:Wdr45 ^@ http://purl.uniprot.org/uniprot/Q91VM3 ^@ Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Motif|||Repeat|||Splice Variant ^@ In isoform 2.|||L/FRRG motif|||WD 1|||WD 2|||WD 3|||WD repeat domain phosphoinositide-interacting protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000051453|||http://purl.uniprot.org/annotation/VSP_016977 http://togogenome.org/gene/10090:Ctbs ^@ http://purl.uniprot.org/uniprot/Q102J0|||http://purl.uniprot.org/uniprot/Q8R242 ^@ 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 ^@ Di-N-acetylchitobiase|||GH18|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000011962|||http://purl.uniprot.org/annotation/PRO_5015097022|||http://purl.uniprot.org/annotation/VSP_013909 http://togogenome.org/gene/10090:En1 ^@ http://purl.uniprot.org/uniprot/P09065|||http://purl.uniprot.org/uniprot/Q3USA2 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Disordered|||Homeobox|||Homeobox protein engrailed-1|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000196063 http://togogenome.org/gene/10090:Agl ^@ http://purl.uniprot.org/uniprot/F8VPN4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Eukaryotic glycogen debranching enzyme N-terminal|||Glycogen debranching enzyme C-terminal|||Glycogen debranching enzyme central|||Glycogen debranching enzyme glucanotransferase ^@ http://togogenome.org/gene/10090:Lipi ^@ http://purl.uniprot.org/uniprot/F6YQT7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Signal Peptide ^@ Charge relay system|||Lipase|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_5015091134 http://togogenome.org/gene/10090:Gm11127 ^@ http://purl.uniprot.org/uniprot/A7VMS2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015086579 http://togogenome.org/gene/10090:Spag1 ^@ http://purl.uniprot.org/uniprot/Q80ZX8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Sperm-associated antigen 1|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8 ^@ http://purl.uniprot.org/annotation/PRO_0000106325|||http://purl.uniprot.org/annotation/VSP_012684|||http://purl.uniprot.org/annotation/VSP_012685 http://togogenome.org/gene/10090:Supt7l ^@ http://purl.uniprot.org/uniprot/Q9CZV5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||STAGA complex 65 subunit gamma ^@ http://purl.uniprot.org/annotation/PRO_0000072234 http://togogenome.org/gene/10090:Polr2d ^@ http://purl.uniprot.org/uniprot/Q9D7M8 ^@ Chain|||Molecule Processing ^@ Chain ^@ DNA-directed RNA polymerase II subunit RPB4 ^@ http://purl.uniprot.org/annotation/PRO_0000073982 http://togogenome.org/gene/10090:Ptk7 ^@ http://purl.uniprot.org/uniprot/Q8BKG3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ 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|||Inactive tyrosine-protein kinase 7|||Interaction with CTNNB1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protein kinase; inactive ^@ http://purl.uniprot.org/annotation/PRO_0000260435 http://togogenome.org/gene/10090:Ugt1a9 ^@ http://purl.uniprot.org/uniprot/Q62452 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||UDP-glucuronosyltransferase 1A9 ^@ http://purl.uniprot.org/annotation/PRO_0000036020 http://togogenome.org/gene/10090:Or5g27 ^@ http://purl.uniprot.org/uniprot/Q7TRA0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Taf1d ^@ http://purl.uniprot.org/uniprot/Q9D4V4 ^@ 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 residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||TATA box-binding protein-associated factor RNA polymerase I subunit D ^@ http://purl.uniprot.org/annotation/PRO_0000250718|||http://purl.uniprot.org/annotation/VSP_020729|||http://purl.uniprot.org/annotation/VSP_020730 http://togogenome.org/gene/10090:Entrep1 ^@ http://purl.uniprot.org/uniprot/Q4FZH1 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Modified Residue|||Motif|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endosomal transmembrane epsin interactor 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||Lumenal|||Mediates interaction with EPN1|||PPxY; mediates interaction with ITCH|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000089699|||http://purl.uniprot.org/annotation/VSP_061675 http://togogenome.org/gene/10090:Bag5 ^@ http://purl.uniprot.org/uniprot/Q8CI32 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict ^@ BAG 1|||BAG 2|||BAG 3|||BAG 4|||BAG 5|||BAG family molecular chaperone regulator 5|||Results in lack of BAG5 at junctional membrane complexes in cardiomyocytes from homozygous mutant mice, disruption of junctional membrane complex structure, and calcium handling abnormalities. Homozygous mutant mice exhibit ventricular dilatation and arrhythmogenicity. ^@ http://purl.uniprot.org/annotation/PRO_0000088873 http://togogenome.org/gene/10090:Tex264 ^@ http://purl.uniprot.org/uniprot/E9Q137 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||LIR motif|||Lumenal|||Phosphoserine|||Polar residues|||Testis-expressed protein 264 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000451419|||http://purl.uniprot.org/annotation/VSP_060780 http://togogenome.org/gene/10090:Fgf21 ^@ http://purl.uniprot.org/uniprot/A0A7U3L6A3|||http://purl.uniprot.org/uniprot/Q9JJN1 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Region|||Signal Peptide ^@ Disordered|||Fibroblast growth factor|||Fibroblast growth factor 21 ^@ http://purl.uniprot.org/annotation/PRO_0000008995|||http://purl.uniprot.org/annotation/PRO_5031604612 http://togogenome.org/gene/10090:Rbm5 ^@ http://purl.uniprot.org/uniprot/Q91YE7 ^@ 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|||Disordered|||G-patch|||In isoform 2.|||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_0000253050|||http://purl.uniprot.org/annotation/VSP_021003 http://togogenome.org/gene/10090:Try4 ^@ http://purl.uniprot.org/uniprot/Q9R0T7 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Propeptide|||Signal Peptide|||Site ^@ Activation peptide|||Charge relay system|||Cleavage; by CTRC|||Cleavage; by autolysis|||Peptidase S1|||Slightly increases autoactivation.|||Trypsin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000457719|||http://purl.uniprot.org/annotation/PRO_5015099944 http://togogenome.org/gene/10090:Zfp609 ^@ http://purl.uniprot.org/uniprot/Q8BZ47 ^@ 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_0000280423|||http://purl.uniprot.org/annotation/VSP_059084|||http://purl.uniprot.org/annotation/VSP_059085 http://togogenome.org/gene/10090:Vmn1r229 ^@ http://purl.uniprot.org/uniprot/Q8R2A9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dlk2 ^@ http://purl.uniprot.org/uniprot/Q8K1E3 ^@ 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|||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 1.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Protein delta homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000396620|||http://purl.uniprot.org/annotation/VSP_039583|||http://purl.uniprot.org/annotation/VSP_039584 http://togogenome.org/gene/10090:Gal3st3 ^@ http://purl.uniprot.org/uniprot/P61315 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Galactose-3-O-sulfotransferase 3|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000085207 http://togogenome.org/gene/10090:Rdh13 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1N8|||http://purl.uniprot.org/uniprot/Q8CEE7 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ N-acetylserine|||Proton acceptor|||Removed|||Retinol dehydrogenase 13 ^@ http://purl.uniprot.org/annotation/PRO_0000054769|||http://purl.uniprot.org/annotation/PRO_5006452015 http://togogenome.org/gene/10090:Mapk8ip2 ^@ http://purl.uniprot.org/uniprot/Q548W8|||http://purl.uniprot.org/uniprot/Q6PIT2|||http://purl.uniprot.org/uniprot/Q9ERE9 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||C-Jun-amino-terminal kinase-interacting protein 2|||Disordered|||JNK-binding domain (JBD)|||Necessary for interaction with FGF13|||PID|||Phosphoserine|||Polar residues|||Pro residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000220632 http://togogenome.org/gene/10090:Ndufa5 ^@ http://purl.uniprot.org/uniprot/Q9CPP6 ^@ 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-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118633 http://togogenome.org/gene/10090:Vmn1r74 ^@ http://purl.uniprot.org/uniprot/Q8R290 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp24 ^@ http://purl.uniprot.org/uniprot/Q91VN1 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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|||Necessary and sufficient for nuclear localization|||Phosphoserine|||Phosphotyrosine|||SCAN box|||Zinc finger protein 24 ^@ http://purl.uniprot.org/annotation/PRO_0000047353 http://togogenome.org/gene/10090:Or1d2 ^@ http://purl.uniprot.org/uniprot/Q7TRW7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Galm ^@ http://purl.uniprot.org/uniprot/Q8K157 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ Galactose mutarotase|||Phosphoserine|||Proton acceptor|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000197434 http://togogenome.org/gene/10090:Fam120a ^@ http://purl.uniprot.org/uniprot/Q6A0A9 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Constitutive coactivator of PPAR-gamma-like protein 1|||Disordered|||Interaction with YES1, SRC and FYN|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA binding ^@ http://purl.uniprot.org/annotation/PRO_0000363780 http://togogenome.org/gene/10090:Polrmt ^@ http://purl.uniprot.org/uniprot/Q3U3J3|||http://purl.uniprot.org/uniprot/Q3V3C0|||http://purl.uniprot.org/uniprot/Q8BKF1 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Chain|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ DNA-directed RNA polymerase N-terminal|||DNA-directed RNA polymerase, mitochondrial|||Disordered|||Mediates interaction with TEFM|||Mitochondrion|||PPR|||PPR 1|||PPR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000031069 http://togogenome.org/gene/10090:Rag2 ^@ http://purl.uniprot.org/uniprot/P21784|||http://purl.uniprot.org/uniprot/Q542D1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn|||Zinc Finger ^@ Abolishes binding to H3K4me3 without affecting phosphoinositide-binding.|||Abolishes binding to H3K4me3 without affecting phosphoinositide-binding. Impairs enzymatic activity of the RAG complex.|||Binds PtdIns(4,5)P2 at wild-type level.|||Disordered|||Does not affect the endonuclease activity of the RAG complex.|||Induces a slight reduction in V(D)J recombination without affecting interaction with histones.|||Leads to a strong reduction in PtdIns(4,5)P2-binding.|||PHD-type; atypical|||Polar residues|||Recombination activating protein 2 PHD|||Reduced interaction with histones.|||Still binds H3K4me3 and H3R2me2 but with reduced affinity.|||V(D)J recombination-activating protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000167138 http://togogenome.org/gene/10090:Usp15 ^@ http://purl.uniprot.org/uniprot/Q3TSV9|||http://purl.uniprot.org/uniprot/Q8R5H1 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||DUSP|||Disordered|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||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_0000080642|||http://purl.uniprot.org/annotation/VSP_005262|||http://purl.uniprot.org/annotation/VSP_005263|||http://purl.uniprot.org/annotation/VSP_005264|||http://purl.uniprot.org/annotation/VSP_005265|||http://purl.uniprot.org/annotation/VSP_005266 http://togogenome.org/gene/10090:Defb10 ^@ http://purl.uniprot.org/uniprot/Q8R2I8 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 10 ^@ http://purl.uniprot.org/annotation/PRO_0000006938 http://togogenome.org/gene/10090:Chrna4 ^@ http://purl.uniprot.org/uniprot/O70174|||http://purl.uniprot.org/uniprot/Q53YK0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Associated with receptor activation|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-4|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000000352|||http://purl.uniprot.org/annotation/PRO_5014309566 http://togogenome.org/gene/10090:1700093K21Rik ^@ http://purl.uniprot.org/uniprot/Q810S2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Uncharacterized protein C2orf74 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000343567 http://togogenome.org/gene/10090:Senp5 ^@ http://purl.uniprot.org/uniprot/Q6NXL6 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Protease|||Sentrin-specific protease 5 ^@ http://purl.uniprot.org/annotation/PRO_0000267607 http://togogenome.org/gene/10090:Or5j1 ^@ http://purl.uniprot.org/uniprot/Q7TR57 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp661 ^@ http://purl.uniprot.org/uniprot/Q8BIQ3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||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|||C2H2-type 9; degenerate|||Disordered|||KRAB|||Zinc finger protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000274050 http://togogenome.org/gene/10090:Or6d12 ^@ http://purl.uniprot.org/uniprot/Q7TS33|||http://purl.uniprot.org/uniprot/Q8C0U2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dmrtb1 ^@ http://purl.uniprot.org/uniprot/A2A9I7|||http://purl.uniprot.org/uniprot/Q3V0Z3 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Non-terminal Residue|||Region ^@ DM|||Disordered|||Doublesex- and mab-3-related transcription factor B1|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000316013 http://togogenome.org/gene/10090:Btnl10 ^@ http://purl.uniprot.org/uniprot/Q9JK39 ^@ 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 ^@ Butyrophilin-like protein 10|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000417554|||http://purl.uniprot.org/annotation/VSP_043775 http://togogenome.org/gene/10090:Ice1 ^@ http://purl.uniprot.org/uniprot/E9Q286 ^@ 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|||Little elongation complex subunit 1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000430423 http://togogenome.org/gene/10090:Or5b24 ^@ http://purl.uniprot.org/uniprot/Q8VEV8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dcaf5 ^@ http://purl.uniprot.org/uniprot/Q3UV57|||http://purl.uniprot.org/uniprot/Q80T85 ^@ 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|||DDB1- and CUL4-associated factor 5|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000051370 http://togogenome.org/gene/10090:Ankub1 ^@ http://purl.uniprot.org/uniprot/Q3UUE9 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein ANKUB1 ^@ http://purl.uniprot.org/annotation/PRO_0000344464 http://togogenome.org/gene/10090:Ivns1abp ^@ http://purl.uniprot.org/uniprot/Q920Q8 ^@ 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 ^@ BACK|||BTB|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Influenza virus NS1A-binding protein homolog|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000285078|||http://purl.uniprot.org/annotation/VSP_024810|||http://purl.uniprot.org/annotation/VSP_024811|||http://purl.uniprot.org/annotation/VSP_024812|||http://purl.uniprot.org/annotation/VSP_024813 http://togogenome.org/gene/10090:Mad1l1 ^@ http://purl.uniprot.org/uniprot/Q9WTX8 ^@ Chain|||Coiled-Coil|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Crosslink|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000213801|||http://purl.uniprot.org/annotation/VSP_011638 http://togogenome.org/gene/10090:Tmem241 ^@ http://purl.uniprot.org/uniprot/Q3UME2 ^@ 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.|||In isoform 4.|||Transmembrane protein 241 ^@ http://purl.uniprot.org/annotation/PRO_0000307317|||http://purl.uniprot.org/annotation/VSP_028709|||http://purl.uniprot.org/annotation/VSP_028710|||http://purl.uniprot.org/annotation/VSP_028711|||http://purl.uniprot.org/annotation/VSP_028712|||http://purl.uniprot.org/annotation/VSP_028713|||http://purl.uniprot.org/annotation/VSP_028714 http://togogenome.org/gene/10090:Rnf224 ^@ http://purl.uniprot.org/uniprot/Q3UIW8 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Zinc Finger ^@ RING finger protein 224|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000412183 http://togogenome.org/gene/10090:Dgat1 ^@ http://purl.uniprot.org/uniprot/Q54AA6|||http://purl.uniprot.org/uniprot/Q9Z2A7 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Amphipathic helix (AH)|||Cytoplasmic|||Diacylglycerol O-acyltransferase 1|||Disordered|||Extracellular loop 1 (EL1)|||FYXDWWN motif|||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|||Impairs the ability to synthesize triacylglycerols, as well as retinyl and wax esters, in an in vitro acyltransferase assay.|||Important for catalytic activity|||Intracellular loop 1 (IL1)|||Intracellular loop 2 (IL2)|||Involved in homomerization|||Lumenal|||MBOAT fold|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000207655 http://togogenome.org/gene/10090:Ap1g2 ^@ http://purl.uniprot.org/uniprot/O88512|||http://purl.uniprot.org/uniprot/Q3U9D1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ AP-1 complex subunit gamma-like 2|||GAE ^@ http://purl.uniprot.org/annotation/PRO_0000193761 http://togogenome.org/gene/10090:Tom1 ^@ http://purl.uniprot.org/uniprot/O88746|||http://purl.uniprot.org/uniprot/Q3UDC3|||http://purl.uniprot.org/uniprot/Q561M4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Basic and acidic residues|||Clathrin box|||Disordered|||GAT|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with MYO6|||KRKK|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Target of Myb1 membrane trafficking protein|||VHS ^@ http://purl.uniprot.org/annotation/PRO_0000072629|||http://purl.uniprot.org/annotation/VSP_003991|||http://purl.uniprot.org/annotation/VSP_003992 http://togogenome.org/gene/10090:Gm12185 ^@ http://purl.uniprot.org/uniprot/Q5NCB2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ IRG-type G ^@ http://togogenome.org/gene/10090:Usp3 ^@ http://purl.uniprot.org/uniprot/E9Q8W9|||http://purl.uniprot.org/uniprot/Q3TT00|||http://purl.uniprot.org/uniprot/Q91W36 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Zinc Finger ^@ N-acetylmethionine|||Nucleophile|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000080620 http://togogenome.org/gene/10090:2310009B15Rik ^@ http://purl.uniprot.org/uniprot/D3Z1T2 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Skint7 ^@ http://purl.uniprot.org/uniprot/A7XV04 ^@ 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 C1-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Selection and upkeep of intraepithelial T-cells protein 7 ^@ http://purl.uniprot.org/annotation/PRO_5000271642|||http://purl.uniprot.org/annotation/VSP_034888|||http://purl.uniprot.org/annotation/VSP_034889|||http://purl.uniprot.org/annotation/VSP_034890|||http://purl.uniprot.org/annotation/VSP_034891 http://togogenome.org/gene/10090:Spesp1 ^@ http://purl.uniprot.org/uniprot/Q9D5A0 ^@ 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|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sperm equatorial segment protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000042709 http://togogenome.org/gene/10090:Kl ^@ http://purl.uniprot.org/uniprot/O35082 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Glycosyl hydrolase-1 1|||Glycosyl hydrolase-1 2|||Helical|||In isoform 2.|||Klotho|||Klotho peptide|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000042247|||http://purl.uniprot.org/annotation/PRO_0000042248|||http://purl.uniprot.org/annotation/VSP_015828|||http://purl.uniprot.org/annotation/VSP_015829 http://togogenome.org/gene/10090:Btf3 ^@ http://purl.uniprot.org/uniprot/Q3UJR8|||http://purl.uniprot.org/uniprot/Q64152 ^@ 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.|||N6-methyllysine|||NAC-A/B|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Transcription factor BTF3 ^@ http://purl.uniprot.org/annotation/PRO_0000213549|||http://purl.uniprot.org/annotation/VSP_013588 http://togogenome.org/gene/10090:Gosr2 ^@ http://purl.uniprot.org/uniprot/O35166 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Modified Residue|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Golgi SNAP receptor complex member 2|||Helical; Anchor for type IV membrane protein|||IxM motif; signal for cargo packaging into COPII-coated vesicles|||N-acetylmethionine|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000212550 http://togogenome.org/gene/10090:Slc16a11 ^@ http://purl.uniprot.org/uniprot/Q5NC32|||http://purl.uniprot.org/uniprot/Q9JJC0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Major facilitator superfamily (MFS) profile|||Monocarboxylate transporter 11 ^@ http://purl.uniprot.org/annotation/PRO_0000286674 http://togogenome.org/gene/10090:Pde11a ^@ http://purl.uniprot.org/uniprot/P0C1Q2 ^@ 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|||Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A|||GAF 1|||GAF 2|||PDEase|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000247041 http://togogenome.org/gene/10090:Or1e25 ^@ http://purl.uniprot.org/uniprot/Q7TRX8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zswim3 ^@ http://purl.uniprot.org/uniprot/Q8CFL8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Zinc Finger ^@ Disordered|||Polar residues|||SWIM-type|||Zinc finger SWIM domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000223100 http://togogenome.org/gene/10090:Or13c25 ^@ http://purl.uniprot.org/uniprot/Q8VGA0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Apol10a ^@ http://purl.uniprot.org/uniprot/Q8CCA5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Dnah6 ^@ http://purl.uniprot.org/uniprot/E9Q0B6 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ AAA+ ATPase ^@ http://togogenome.org/gene/10090:Zfp930 ^@ http://purl.uniprot.org/uniprot/A0A1D5RM15 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Stat4 ^@ http://purl.uniprot.org/uniprot/P42228|||http://purl.uniprot.org/uniprot/Q3V157 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict ^@ N6-acetyllysine|||Phosphoserine|||Phosphotyrosine; by JAK|||SH2|||Signal transducer and activator of transcription 4 ^@ http://purl.uniprot.org/annotation/PRO_0000182421 http://togogenome.org/gene/10090:Prlh ^@ http://purl.uniprot.org/uniprot/G3UWC3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015091571 http://togogenome.org/gene/10090:Mettl16 ^@ http://purl.uniprot.org/uniprot/Q9CQG2 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||K-loop|||Phosphoserine|||Phosphothreonine|||RNA N6-adenosine-methyltransferase METTL16|||RNA-binding|||VCR 1|||VCR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000310768|||http://purl.uniprot.org/annotation/VSP_029342 http://togogenome.org/gene/10090:Slc27a2 ^@ http://purl.uniprot.org/uniprot/O35488|||http://purl.uniprot.org/uniprot/Q3TN99 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ AMP-dependent synthetase/ligase|||Cytoplasmic|||Helical|||Long-chain fatty acid transport protein 2|||Lumenal|||N6-acetyllysine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000193205 http://togogenome.org/gene/10090:Or8g20 ^@ http://purl.uniprot.org/uniprot/Q9EQB8|||http://purl.uniprot.org/uniprot/Q9Z1V5 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Domain Extent|||Non-terminal Residue|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dtx2 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZY1|||http://purl.uniprot.org/uniprot/Q8R3P2 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Omega-N-methylarginine|||Probable E3 ubiquitin-protein ligase DTX2|||RING-type|||WWE|||WWE 1|||WWE 2 ^@ http://purl.uniprot.org/annotation/PRO_0000219084|||http://purl.uniprot.org/annotation/VSP_008351|||http://purl.uniprot.org/annotation/VSP_008352|||http://purl.uniprot.org/annotation/VSP_008353 http://togogenome.org/gene/10090:Fam187b ^@ http://purl.uniprot.org/uniprot/Q0VAY3 ^@ 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|||Protein FAM187B ^@ http://purl.uniprot.org/annotation/PRO_0000284628|||http://purl.uniprot.org/annotation/VSP_024580 http://togogenome.org/gene/10090:Ccdc136 ^@ http://purl.uniprot.org/uniprot/A0A0N4SW14|||http://purl.uniprot.org/uniprot/D3Z165|||http://purl.uniprot.org/uniprot/E6Y2W6|||http://purl.uniprot.org/uniprot/E6Y2W7|||http://purl.uniprot.org/uniprot/E9QP94|||http://purl.uniprot.org/uniprot/F6VCV9|||http://purl.uniprot.org/uniprot/Q3TVA9 ^@ 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 ^@ Acidic residues|||Coiled-coil domain-containing protein 136|||Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000300640|||http://purl.uniprot.org/annotation/VSP_027846|||http://purl.uniprot.org/annotation/VSP_027847|||http://purl.uniprot.org/annotation/VSP_027848 http://togogenome.org/gene/10090:Myh4 ^@ http://purl.uniprot.org/uniprot/Q3UUB1|||http://purl.uniprot.org/uniprot/Q5SX39 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ Actin-binding|||Disordered|||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_0000123399 http://togogenome.org/gene/10090:Tm9sf1 ^@ http://purl.uniprot.org/uniprot/Q9DBU0 ^@ 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 1 ^@ http://purl.uniprot.org/annotation/PRO_0000034362 http://togogenome.org/gene/10090:Klhl36 ^@ http://purl.uniprot.org/uniprot/Q8R124 ^@ 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 36 ^@ http://purl.uniprot.org/annotation/PRO_0000274692 http://togogenome.org/gene/10090:Fv1 ^@ http://purl.uniprot.org/uniprot/P70213 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Variant ^@ Basic and acidic residues|||Disordered|||Friend virus susceptibility protein 1|||In strain: AKR/J, C3H and DBA/2.|||In strain: AKR/J, C3H and DBA/2; requires 2 nucleotide substitutions.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087389 http://togogenome.org/gene/10090:Or51b17 ^@ http://purl.uniprot.org/uniprot/F8VPZ8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc3a1 ^@ http://purl.uniprot.org/uniprot/Q91WV7 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Amino acid transporter heavy chain SLC3A1|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Interchain (with C-144 in SLC7A5)|||Loss of localization at the brush border membrane.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000425741 http://togogenome.org/gene/10090:Vmn2r116 ^@ http://purl.uniprot.org/uniprot/E9Q6I0 ^@ 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|||Vomeronasal type-2 receptor 116 ^@ http://purl.uniprot.org/annotation/PRO_0000424696 http://togogenome.org/gene/10090:Col4a5 ^@ http://purl.uniprot.org/uniprot/Q63ZW6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Collagen IV NC1|||Disordered|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5015098108 http://togogenome.org/gene/10090:Acacb ^@ http://purl.uniprot.org/uniprot/E9Q4Z2|||http://purl.uniprot.org/uniprot/Q3UHC8|||http://purl.uniprot.org/uniprot/Q9ESZ3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ ATP-grasp|||Acetyl-CoA carboxylase 2|||Biotin carboxylase-like N-terminal|||Biotin carboxylation|||Biotinyl-binding|||Carboxyltransferase|||CoA carboxyltransferase C-terminal|||CoA carboxyltransferase N-terminal|||Disordered|||Lipoyl-binding|||Mitochondrion|||N6-biotinyllysine|||No phosphorylation by AMPK, reduced fatty acid oxidation in skeletal muscle, increased lipid deposition in skeletal muscle, and development of insulin resistance.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000430774 http://togogenome.org/gene/10090:Aqp2 ^@ http://purl.uniprot.org/uniprot/P56402|||http://purl.uniprot.org/uniprot/Q3UQD4 ^@ Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Aquaporin-2|||Cytoplasmic|||Discontinuously helical|||Disordered|||Does not cause loss of water channel activity, but impairs trafficking from cytoplasmic vesicles to the cell membrane.|||Extracellular|||Helical|||In cph; loss of a phosphorylation site and loss of trafficking to the apical cell membrane; causes aberrant location at the basolateral cell membrane.|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000063936 http://togogenome.org/gene/10090:Tll2 ^@ http://purl.uniprot.org/uniprot/Q9WVM6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||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_0000046038|||http://purl.uniprot.org/annotation/PRO_0000046039 http://togogenome.org/gene/10090:Ugp2 ^@ http://purl.uniprot.org/uniprot/Q3U548|||http://purl.uniprot.org/uniprot/Q91ZJ5 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Splice Variant ^@ Critical for end-to-end subunit interaction|||In isoform 2.|||N6-acetyllysine|||Oligomerization|||Phosphoserine|||Phosphothreonine|||UTP--glucose-1-phosphate uridylyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000185753|||http://purl.uniprot.org/annotation/VSP_012835 http://togogenome.org/gene/10090:Atp6v1b2 ^@ http://purl.uniprot.org/uniprot/P62814 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ V-type proton ATPase subunit B, brain isoform ^@ http://purl.uniprot.org/annotation/PRO_0000144627 http://togogenome.org/gene/10090:She ^@ http://purl.uniprot.org/uniprot/Q8BSD5 ^@ 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|||SH2|||SH2 domain-containing adapter protein E ^@ http://purl.uniprot.org/annotation/PRO_0000246776 http://togogenome.org/gene/10090:H2-M2 ^@ http://purl.uniprot.org/uniprot/Q6W9L1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015098577 http://togogenome.org/gene/10090:Entpd7 ^@ http://purl.uniprot.org/uniprot/Q3TCT4 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Ectonucleoside triphosphate diphosphohydrolase 7|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000274420|||http://purl.uniprot.org/annotation/VSP_022743|||http://purl.uniprot.org/annotation/VSP_022744 http://togogenome.org/gene/10090:Esx1 ^@ http://purl.uniprot.org/uniprot/A2AG22|||http://purl.uniprot.org/uniprot/O88933 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Pro residues ^@ http://togogenome.org/gene/10090:Mcph1 ^@ http://purl.uniprot.org/uniprot/Q7TT79 ^@ 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 ^@ BRCT 1|||BRCT 2|||BRCT 3|||Basic and acidic residues|||Disordered|||Microcephalin|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096299 http://togogenome.org/gene/10090:Gm8909 ^@ http://purl.uniprot.org/uniprot/A7VMS6|||http://purl.uniprot.org/uniprot/G3UXE9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5003457181|||http://purl.uniprot.org/annotation/PRO_5015086580 http://togogenome.org/gene/10090:Denr ^@ http://purl.uniprot.org/uniprot/Q9CQJ6 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Density-regulated protein|||Disordered|||N-acetylalanine|||Phosphoserine|||Removed|||SUI1 ^@ http://purl.uniprot.org/annotation/PRO_0000130601 http://togogenome.org/gene/10090:Gabra2 ^@ http://purl.uniprot.org/uniprot/P26048|||http://purl.uniprot.org/uniprot/Q544G1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Gamma-aminobutyric acid receptor subunit alpha-2|||Helical|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000434|||http://purl.uniprot.org/annotation/PRO_5014309553 http://togogenome.org/gene/10090:Taf1a ^@ http://purl.uniprot.org/uniprot/P97357|||http://purl.uniprot.org/uniprot/Q3V054 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue ^@ Chain|||Non-terminal Residue ^@ TATA box-binding protein-associated factor RNA polymerase I subunit A ^@ http://purl.uniprot.org/annotation/PRO_0000227988 http://togogenome.org/gene/10090:Lrp10 ^@ http://purl.uniprot.org/uniprot/Q7TQH7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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 10|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000017336 http://togogenome.org/gene/10090:Fam24a ^@ http://purl.uniprot.org/uniprot/Q8CF27 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Protein FAM24A ^@ http://purl.uniprot.org/annotation/PRO_0000353116 http://togogenome.org/gene/10090:Fibp ^@ http://purl.uniprot.org/uniprot/Q9JI19 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Acidic fibroblast growth factor intracellular-binding protein|||N-acetylthreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087238 http://togogenome.org/gene/10090:Prph ^@ http://purl.uniprot.org/uniprot/A0A2R8W6R6|||http://purl.uniprot.org/uniprot/G3X981|||http://purl.uniprot.org/uniprot/G5E846 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||IF rod|||Polar residues ^@ http://togogenome.org/gene/10090:Mon1b ^@ http://purl.uniprot.org/uniprot/Q8BMQ8 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Vacuolar fusion protein MON1 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000285767 http://togogenome.org/gene/10090:Or8k27 ^@ http://purl.uniprot.org/uniprot/Q7TR70 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ank ^@ http://purl.uniprot.org/uniprot/Q3UG85|||http://purl.uniprot.org/uniprot/Q8C438|||http://purl.uniprot.org/uniprot/Q9JHZ2 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In strain: C3H.|||Mineralization regulator ANKH ^@ http://purl.uniprot.org/annotation/PRO_0000137468 http://togogenome.org/gene/10090:Exosc7 ^@ http://purl.uniprot.org/uniprot/Q9D0M0 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Exosome complex exonuclease RRP42|||N-acetylalanine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000139964 http://togogenome.org/gene/10090:Car14 ^@ http://purl.uniprot.org/uniprot/Q9WVT6 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||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_0000004252 http://togogenome.org/gene/10090:Tnfrsf12a ^@ http://purl.uniprot.org/uniprot/E9PZT5|||http://purl.uniprot.org/uniprot/Q9CR75 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||TNFR-Cys; atypical|||Tumor necrosis factor receptor superfamily member 12A ^@ http://purl.uniprot.org/annotation/PRO_0000034612|||http://purl.uniprot.org/annotation/PRO_5003245561 http://togogenome.org/gene/10090:Phkg1 ^@ http://purl.uniprot.org/uniprot/P07934 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Calmodulin-binding (domain-C)|||Calmodulin-binding (domain-N)|||Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086509 http://togogenome.org/gene/10090:Pofut2 ^@ http://purl.uniprot.org/uniprot/B2RV73|||http://purl.uniprot.org/uniprot/Q8VHI3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Signal Peptide|||Site ^@ Abolishes in vitro enzyme activity.|||GDP-fucose protein O-fucosyltransferase 2|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Required for enzyme activity ^@ http://purl.uniprot.org/annotation/PRO_0000012155|||http://purl.uniprot.org/annotation/PRO_5014298366 http://togogenome.org/gene/10090:Bbs2 ^@ http://purl.uniprot.org/uniprot/Q9CWF6 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Bardet-Biedl syndrome 2 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000064844 http://togogenome.org/gene/10090:Psmb4 ^@ http://purl.uniprot.org/uniprot/P99026 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Strand|||Turn ^@ N-acetylmethionine|||Phosphotyrosine|||Proteasome subunit beta type-4 ^@ http://purl.uniprot.org/annotation/PRO_0000026581|||http://purl.uniprot.org/annotation/PRO_0000026582 http://togogenome.org/gene/10090:Lsamp ^@ http://purl.uniprot.org/uniprot/Q3TYE5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097456 http://togogenome.org/gene/10090:Tnfsf10 ^@ http://purl.uniprot.org/uniprot/P50592|||http://purl.uniprot.org/uniprot/Q3U5H0 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||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 10 ^@ http://purl.uniprot.org/annotation/PRO_0000185504 http://togogenome.org/gene/10090:Kif26b ^@ http://purl.uniprot.org/uniprot/B0G0X9|||http://purl.uniprot.org/uniprot/Q7TNC6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Kinesin motor|||Kinesin-like protein KIF26B|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced polyubiquitination when co-expressed with NEDD4; when associated with Ala-1859.|||Reduced polyubiquitination when co-expressed with NEDD4; when associated with Ala-1962. ^@ http://purl.uniprot.org/annotation/PRO_0000307302 http://togogenome.org/gene/10090:Syn3 ^@ http://purl.uniprot.org/uniprot/D3Z620|||http://purl.uniprot.org/uniprot/Q3KN99|||http://purl.uniprot.org/uniprot/Q8JZP2 ^@ 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 ^@ A|||B; linker|||C; actin-binding and synaptic-vesicle binding|||Disordered|||E|||J; Pro-rich linker|||Phosphoserine|||Polar residues|||Pro residues|||Synapsin ATP-binding|||Synapsin pre-ATP-grasp|||Synapsin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000183025 http://togogenome.org/gene/10090:Mterf4 ^@ http://purl.uniprot.org/uniprot/Q8BVN4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ Acidic residues|||Dimerization with NSUN4|||Disordered|||MTERF 1|||MTERF 2|||MTERF 3|||MTERF 4|||MTERF 5|||Mitochondrion|||Transcription termination factor 4, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000255462 http://togogenome.org/gene/10090:Vmn1r176 ^@ http://purl.uniprot.org/uniprot/G3UW31 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cenpb ^@ http://purl.uniprot.org/uniprot/P27790 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000126126 http://togogenome.org/gene/10090:Slc34a3 ^@ http://purl.uniprot.org/uniprot/Q80SU6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Change of cotransport Na(+):Pi stoichiometry to 3:1; when associated with 189-AGA-191.|||Change of cotransport Na(+):Pi stoichiometry to 3:1; when associated with D-195.|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium-dependent phosphate transport protein 2C ^@ http://purl.uniprot.org/annotation/PRO_0000068618 http://togogenome.org/gene/10090:AW146154 ^@ http://purl.uniprot.org/uniprot/Q3TPQ7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Tmem126b ^@ http://purl.uniprot.org/uniprot/Q9D1R1 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Complex I assembly factor TMEM126B, mitochondrial|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000280717 http://togogenome.org/gene/10090:Gp2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0B9|||http://purl.uniprot.org/uniprot/Q9D733 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide ^@ Beta hairpin|||D10C|||EGF-like|||External hydrophobic patch (EHP)|||Flexible ZP-N/ZP-C linker|||Internal hydrophobic patch (IHP)|||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_0000041659|||http://purl.uniprot.org/annotation/PRO_0000041660|||http://purl.uniprot.org/annotation/PRO_5015044286 http://togogenome.org/gene/10090:Fbxw5 ^@ http://purl.uniprot.org/uniprot/Q9QXW2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Repeat|||Splice Variant ^@ D-box|||F-box|||F-box/WD repeat-containing protein 5|||In isoform 2.|||Phosphoserine; by PLK4|||WD 1|||WD 2|||WD 3 ^@ http://purl.uniprot.org/annotation/PRO_0000050993|||http://purl.uniprot.org/annotation/VSP_042293|||http://purl.uniprot.org/annotation/VSP_042294 http://togogenome.org/gene/10090:Gsdmc2 ^@ http://purl.uniprot.org/uniprot/Q2KHK6 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Gasdermin-C2|||Gasdermin-C2, C-terminal|||Gasdermin-C2, N-terminal|||Triggers pyroptosis ^@ http://purl.uniprot.org/annotation/PRO_0000347331|||http://purl.uniprot.org/annotation/PRO_0000451678|||http://purl.uniprot.org/annotation/PRO_0000451679 http://togogenome.org/gene/10090:Ren1 ^@ http://purl.uniprot.org/uniprot/P06281 ^@ 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|||In allele Ren-1D.|||In allele Ren-1D; requires 2 nucleotide substitutions.|||N-linked (GlcNAc...) asparagine|||Peptidase A1|||Renin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000026089|||http://purl.uniprot.org/annotation/PRO_0000026090 http://togogenome.org/gene/10090:Zfp597 ^@ http://purl.uniprot.org/uniprot/E9Q6S0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Dpy30 ^@ http://purl.uniprot.org/uniprot/Q99LT0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylmethionine|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||Protein dpy-30 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000114684 http://togogenome.org/gene/10090:Hoxa13 ^@ http://purl.uniprot.org/uniprot/Q62424 ^@ Chain|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure ^@ Chain|||DNA Binding|||Helix|||Mutagenesis Site ^@ Decreased DNA binding and transcriptional activity.|||Homeobox|||Homeobox protein Hox-A13 ^@ http://purl.uniprot.org/annotation/PRO_0000200102 http://togogenome.org/gene/10090:Arhgap5 ^@ http://purl.uniprot.org/uniprot/P97393 ^@ 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 ^@ 3'-nitrotyrosine|||Basic and acidic residues|||Basic residues|||Disordered|||FF 1|||FF 2|||FF 3|||FF 4|||Phosphoserine|||Rho GTPase-activating protein 5|||Rho-GAP|||pG1 pseudoGTPase|||pG2 pseudoGTPase ^@ http://purl.uniprot.org/annotation/PRO_0000056703 http://togogenome.org/gene/10090:R3hcc1l ^@ http://purl.uniprot.org/uniprot/Q8BJM3 ^@ 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|||Coiled-coil domain-containing protein R3HCC1L|||Disordered|||EJC-binding motif; may mediate interaction with the EJC|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087488 http://togogenome.org/gene/10090:Mrps28 ^@ http://purl.uniprot.org/uniprot/Q9CY16 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Small ribosomal subunit protein bS1m ^@ http://purl.uniprot.org/annotation/PRO_0000087715 http://togogenome.org/gene/10090:Or10a3b ^@ http://purl.uniprot.org/uniprot/Q8VFZ5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cebpe ^@ http://purl.uniprot.org/uniprot/Q6PZD9 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ Basic motif|||CCAAT/enhancer-binding protein epsilon|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Leucine-zipper|||Phosphoserine|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076625 http://togogenome.org/gene/10090:H2bc11 ^@ http://purl.uniprot.org/uniprot/P10853 ^@ 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-F/J/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-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_0000071839 http://togogenome.org/gene/10090:Srrm2 ^@ http://purl.uniprot.org/uniprot/Q8BTI8 ^@ 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 ^@ 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|||Pro residues|||Serine/arginine repetitive matrix protein 2|||Sufficient for RNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000248155|||http://purl.uniprot.org/annotation/VSP_020188|||http://purl.uniprot.org/annotation/VSP_020189 http://togogenome.org/gene/10090:Itga10 ^@ http://purl.uniprot.org/uniprot/E9PXZ3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Repeat|||Signal Peptide|||Transmembrane ^@ FG-GAP|||Helical|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5001424267 http://togogenome.org/gene/10090:Sf3b4 ^@ http://purl.uniprot.org/uniprot/Q8QZY9 ^@ 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|||Phosphotyrosine|||Pro residues|||RRM 1|||RRM 2|||Removed|||Splicing factor 3B subunit 4 ^@ http://purl.uniprot.org/annotation/PRO_0000328585 http://togogenome.org/gene/10090:Or7d10 ^@ http://purl.uniprot.org/uniprot/Q8VEY9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vstm2b ^@ http://purl.uniprot.org/uniprot/Q9JME9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||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_0000319944 http://togogenome.org/gene/10090:Csf1 ^@ http://purl.uniprot.org/uniprot/P07141 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interchain|||Macrophage colony-stimulating factor 1|||Macrophage colony-stimulating factor 1 43 kDa subunit|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Polar residues|||Processed macrophage colony-stimulating factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000005858|||http://purl.uniprot.org/annotation/PRO_0000296232|||http://purl.uniprot.org/annotation/PRO_0000457792|||http://purl.uniprot.org/annotation/VSP_001189 http://togogenome.org/gene/10090:Capn6 ^@ http://purl.uniprot.org/uniprot/O35646|||http://purl.uniprot.org/uniprot/Q80VZ1 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ C2|||Calpain catalytic|||Calpain-6|||Domain III ^@ http://purl.uniprot.org/annotation/PRO_0000207718 http://togogenome.org/gene/10090:Fbxw18 ^@ http://purl.uniprot.org/uniprot/Q3TSA9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Nrtn ^@ http://purl.uniprot.org/uniprot/P97463 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Propeptide|||Signal Peptide ^@ Interchain|||Neurturin ^@ http://purl.uniprot.org/annotation/PRO_0000034012|||http://purl.uniprot.org/annotation/PRO_0000034013 http://togogenome.org/gene/10090:Mief1 ^@ http://purl.uniprot.org/uniprot/B2RPW2|||http://purl.uniprot.org/uniprot/Q8BGV8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes ADP binding.|||Abolishes interaction with DNM1L.|||Cytoplasmic|||Dimerization|||Disordered|||Helical|||Impairs interaction with DNM1L.|||Important for interaction with DNM1L|||Mab-21-like HhH/H2TH-like|||Mildly reduces affinity for ADP.|||Mitochondrial dynamics protein MID51|||Mitochondrial intermembrane|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000310449 http://togogenome.org/gene/10090:Cd180 ^@ http://purl.uniprot.org/uniprot/Q62192 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Sequence Conflict|||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_0000034742 http://togogenome.org/gene/10090:Gpn3 ^@ http://purl.uniprot.org/uniprot/Q9D3W4 ^@ Binding Site|||Chain|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Motif|||Region|||Site ^@ Disordered|||GPN-loop GTPase 3|||Gly-Pro-Asn (GPN)-loop; involved in dimer interface|||Stabilizes the phosphate intermediate; shared with dimeric partner ^@ http://purl.uniprot.org/annotation/PRO_0000304791 http://togogenome.org/gene/10090:Rbsn ^@ http://purl.uniprot.org/uniprot/Q80Y56 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type|||Disordered|||FYVE-type|||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|||Pro residues|||Rabenosyn-5|||Removed|||UIM ^@ http://purl.uniprot.org/annotation/PRO_0000098712 http://togogenome.org/gene/10090:Arhgap20 ^@ http://purl.uniprot.org/uniprot/Q6IFT4 ^@ 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.|||PH|||Phosphoserine|||Polar residues|||Ras-associating|||Rho GTPase-activating protein 20|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000283087|||http://purl.uniprot.org/annotation/VSP_024300|||http://purl.uniprot.org/annotation/VSP_024301 http://togogenome.org/gene/10090:Cfap410 ^@ http://purl.uniprot.org/uniprot/Q3U699|||http://purl.uniprot.org/uniprot/Q8C6G1|||http://purl.uniprot.org/uniprot/Q9D127 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ Cilia- and flagella-associated protein 410|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000419170 http://togogenome.org/gene/10090:Zmynd10 ^@ http://purl.uniprot.org/uniprot/Q99ML0 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Sequence Conflict|||Zinc Finger ^@ MYND-type|||Zinc finger MYND domain-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000218315 http://togogenome.org/gene/10090:Gm1527 ^@ http://purl.uniprot.org/uniprot/Q3V0P3 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Ras-associating|||Rho-GAP ^@ http://togogenome.org/gene/10090:Ripk1 ^@ http://purl.uniprot.org/uniprot/Q60855 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Abolished protein kinase activity and ability to regulate apoptosis and necroptosis. Knockin mice are viable.|||Basic and acidic residues|||Blocks homodimerization, activation of its kinase activity, formation of complex IIa, necroptosis and apoptosis.|||Cleavage; by CASP8|||Death|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In RIPK1(mRHIM); perinatal lethality in knockin mice caused by Ripk3- and Zbp1-dependent necroptosis. Lethality is prevented by Ripk3, Mlkl or Zbp1 deficiency. Knockin mice do not show defects caused by Casp8-dependent apoptosis observed in knockout mice.|||Inhibits its proteolytic cleavage and interaction with FADD. Promotes its interaction with RIPK3 to mediate necroptosis; when associated with E-332; E-334 and E-336.|||Interaction with SQSTM1|||Loss of CASP8-mediated cleavage. Embryonic lethality in knockin mice. Promotes activation of the protein kinase activity, leading to increased cell death.|||Loss of CASP8-mediated cleavage. Promotes both FADD-dependent apoptosis and RIPK3-dependent necroptosis, thus leading to embryonic lethality at midgestation stages in knockin mice. Heterozygous knockin mice are viable and grossly normal, but are hyperresponsive to inflammatory stimuli.|||Loss of kinase activity.|||Loss of kinase activity. Protects cells from TNF-induced cell death.|||Loss of phosphorylation at Ser-332 and Ser-334; when associated with A-321; A-332 and A-334.|||Loss of phosphorylation at Ser-332 and Ser-334; when associated with A-321; A-332 and A-336.|||Loss of phosphorylation at Ser-332 and Ser-334; when associated with A-321; A-334 and A-336.|||Loss of phosphorylation. Does not protect cells from TNF-induced cell death.|||Loss of phosphorylation. Promotes activation of its kinase activity, proteolytic cleavage, ubiquitination and interaction with FADD to mediate apoptosis. Loss of phosphorylation at Ser-332 and Ser-334; when associated with A-332; A-334 and A-336.|||Loss of ubiquitination. Decreases TNF-alpha-mediated NF-kappaB activation. Increases interaction with CFLAR, CASP8, FADD and RIPK3. Decreases interaction with MAP3K7. Enhances kinase activity and promotes apoptosis and necroptosis. Knockin mice display early embryonic lethality resulting from excessive cell death and severe inflammation.|||Phophomimetic mutant. Does not protect cells from TNF-induced cell death.|||Phophomimetic mutant. Significant loss of kinase activity. Protects cells from TNF-induced cell death.|||Phosphoserine|||Phosphoserine; by IKKA and IKKB|||Phosphoserine; by MAP3K7|||Phosphoserine; by RIPK3 and autocatalysis|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Promotes its interaction with RIPK3 to mediate necroptosis; when associated with E-321; E-332 and E-334.|||Promotes its interaction with RIPK3 to mediate necroptosis; when associated with E-321; E-332 and E-336.|||Promotes its interaction with RIPK3 to mediate necroptosis; when associated with E-321; E-334 and E-336.|||Protein kinase|||Proton acceptor|||RIP homotypic interaction motif (RHIM)|||Receptor-interacting serine/threonine-protein kinase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000086607 http://togogenome.org/gene/10090:Nlrp4e ^@ http://purl.uniprot.org/uniprot/Q66X19 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||NACHT|||NACHT, LRR and PYD domains-containing protein 4E|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000286332 http://togogenome.org/gene/10090:Or7g20 ^@ http://purl.uniprot.org/uniprot/Q7TRG7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zscan4f ^@ http://purl.uniprot.org/uniprot/Q3URS2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||SCAN box|||Zinc finger and SCAN domain containing protein 4F ^@ http://purl.uniprot.org/annotation/PRO_0000394246 http://togogenome.org/gene/10090:H2bc8 ^@ http://purl.uniprot.org/uniprot/Q6ZWY9 ^@ 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-C/E/G|||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-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_0000244831 http://togogenome.org/gene/10090:Tdrkh ^@ http://purl.uniprot.org/uniprot/Q80VL1 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||KH 1|||KH 2|||Phosphoserine|||Polar residues|||Tudor|||Tudor and KH domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000050142 http://togogenome.org/gene/10090:B020031M17Rik ^@ http://purl.uniprot.org/uniprot/Q3UT11 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Cmas ^@ http://purl.uniprot.org/uniprot/A0A0R4J0B4|||http://purl.uniprot.org/uniprot/Q99KK2 ^@ 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 ^@ Abolishes both the nuclear localization and the enzyme activity.|||Abolishes the nuclear localization but does not affect the enzyme activity; when associated with A-198.|||Abolishes the nuclear localization but does not affect the enzyme activity; when associated with A-201.|||BC1 motif|||BC2 motif|||BC3 motif|||Disordered|||Does not affect neither the nuclear localization nor the enzyme activity.|||Does not affect the nuclear localization but affects the enzyme activity.|||Does not affect the nuclear localization.|||Does not strongly affect the nuclear localization but strongly affects the enzyme activity.|||In isoform 2.|||N-acetylmethionine|||N-acylneuraminate cytidylyltransferase|||Omega-N-methylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000213200|||http://purl.uniprot.org/annotation/VSP_012765 http://togogenome.org/gene/10090:Tal2 ^@ http://purl.uniprot.org/uniprot/Q2TB09|||http://purl.uniprot.org/uniprot/Q62282 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ BHLH|||Disordered|||T-cell acute lymphocytic leukemia protein 2 homolog|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127457 http://togogenome.org/gene/10090:Or8a1b ^@ http://purl.uniprot.org/uniprot/Q8VGE3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Adgrb2 ^@ http://purl.uniprot.org/uniprot/B1ASC0|||http://purl.uniprot.org/uniprot/Q8CGM1 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Adhesion G protein-coupled receptor B2|||Cleavage; by furin|||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|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphotyrosine|||Polar residues|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4 ^@ http://purl.uniprot.org/annotation/PRO_0000245613|||http://purl.uniprot.org/annotation/PRO_5030165341|||http://purl.uniprot.org/annotation/VSP_019762|||http://purl.uniprot.org/annotation/VSP_019763 http://togogenome.org/gene/10090:Idh3g ^@ http://purl.uniprot.org/uniprot/P70404|||http://purl.uniprot.org/uniprot/Q3TGZ3 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial|||Isopropylmalate dehydrogenase-like|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000014451 http://togogenome.org/gene/10090:Car5a ^@ http://purl.uniprot.org/uniprot/P23589 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Transit Peptide|||Turn ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase 5A, mitochondrial|||In strain: BIO-HTT.|||Mitochondrion|||N6-succinyllysine|||No effect on carbonate dehydratase activity.|||No effect on carbonate dehydratase activity. Enhanced proton transfer due to removal of the steric hindrance of F-95; when associated with A-95.|||No effect on carbonate dehydratase activity. Enhanced proton transfer; when associated with A-95.|||No effect on carbonate dehydratase activity. Enhanced proton transfer; when associated with H-94 or C-161. ^@ http://purl.uniprot.org/annotation/PRO_0000004235 http://togogenome.org/gene/10090:Klhdc10 ^@ http://purl.uniprot.org/uniprot/Q6PAR0 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||Interaction with CUL2|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch domain-containing protein 10|||Omega-N-methylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000319437|||http://purl.uniprot.org/annotation/VSP_031485|||http://purl.uniprot.org/annotation/VSP_031486 http://togogenome.org/gene/10090:Fut2 ^@ http://purl.uniprot.org/uniprot/A6H6C9|||http://purl.uniprot.org/uniprot/Q9JL27 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Galactoside alpha-(1,2)-fucosyltransferase 2|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149109 http://togogenome.org/gene/10090:Cd247 ^@ http://purl.uniprot.org/uniprot/A2MZG6|||http://purl.uniprot.org/uniprot/P24161|||http://purl.uniprot.org/uniprot/Q3UU54 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Blocked amino end (Gln)|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITAM 1|||ITAM 2|||ITAM 3|||In isoform CD-3-eta.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||T-cell surface glycoprotein CD3 zeta chain ^@ http://purl.uniprot.org/annotation/PRO_0000016494|||http://purl.uniprot.org/annotation/PRO_5015086066|||http://purl.uniprot.org/annotation/PRO_5015097500|||http://purl.uniprot.org/annotation/VSP_058346 http://togogenome.org/gene/10090:Trps1 ^@ http://purl.uniprot.org/uniprot/G3UW90|||http://purl.uniprot.org/uniprot/Q3UQJ9|||http://purl.uniprot.org/uniprot/V9GX74|||http://purl.uniprot.org/uniprot/V9GXE9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||GATA-type|||Polar residues ^@ http://togogenome.org/gene/10090:Sf3a3 ^@ http://purl.uniprot.org/uniprot/Q58E59|||http://purl.uniprot.org/uniprot/Q9D554 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Zinc Finger ^@ Acidic residues|||Disordered|||Matrin-type|||N-acetylmethionine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Splicing factor 3A subunit 3 ^@ http://purl.uniprot.org/annotation/PRO_0000174319 http://togogenome.org/gene/10090:Or2w4 ^@ http://purl.uniprot.org/uniprot/Q5SZZ8|||http://purl.uniprot.org/uniprot/Q8VG14 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mbnl3 ^@ http://purl.uniprot.org/uniprot/Q3TJQ3|||http://purl.uniprot.org/uniprot/Q542D8|||http://purl.uniprot.org/uniprot/Q8BYC7|||http://purl.uniprot.org/uniprot/Q8R003 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Zinc Finger ^@ C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||Disordered|||Muscleblind-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000089181 http://togogenome.org/gene/10090:Slfn9 ^@ http://purl.uniprot.org/uniprot/B1ARD6 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict ^@ N'-domain region|||Schlafen family member 9 ^@ http://purl.uniprot.org/annotation/PRO_0000444608 http://togogenome.org/gene/10090:Rtp1 ^@ http://purl.uniprot.org/uniprot/B2RSL5|||http://purl.uniprot.org/uniprot/Q8C8C1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Topological Domain|||Transmembrane|||Zinc Finger ^@ 3CxxC-type|||Cytoplasmic|||Extracellular|||Helical|||Receptor-transporting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000181990 http://togogenome.org/gene/10090:Arid1b ^@ http://purl.uniprot.org/uniprot/A0A8Q0PK87 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ ARID|||Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Syce1l ^@ http://purl.uniprot.org/uniprot/Q5D525 ^@ 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|||Disordered|||In isoform 2.|||In isoform 3.|||Synaptonemal complex central element protein 1-like ^@ http://purl.uniprot.org/annotation/PRO_0000341222|||http://purl.uniprot.org/annotation/VSP_034227|||http://purl.uniprot.org/annotation/VSP_034228 http://togogenome.org/gene/10090:Ptch1 ^@ http://purl.uniprot.org/uniprot/Q3TQB0|||http://purl.uniprot.org/uniprot/Q3UUD4|||http://purl.uniprot.org/uniprot/Q5R252|||http://purl.uniprot.org/uniprot/Q61115 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Accumulates at the plasma membrane, increased half-life and increased CASP9-mediated cell death.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein patched homolog 1|||SSD ^@ http://purl.uniprot.org/annotation/PRO_0000205965|||http://purl.uniprot.org/annotation/PRO_5004229654 http://togogenome.org/gene/10090:Ticam1 ^@ http://purl.uniprot.org/uniprot/Q80UF7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolished ubiquitination by TRIM38.|||Disordered|||Does not affect ubiquitination by TRIM38.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Polar residues|||Pro residues|||Sufficient to induce apoptosis|||TIR|||TIR domain-containing adapter molecule 1|||TRAF6-binding|||TRIF-NTD|||pLxIS motif ^@ http://purl.uniprot.org/annotation/PRO_0000317664 http://togogenome.org/gene/10090:Xpa ^@ http://purl.uniprot.org/uniprot/Q64267 ^@ Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ DNA repair protein complementing XP-A cells homolog|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with CEP164 and required for UV resistance|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000208649|||http://purl.uniprot.org/annotation/VSP_036906 http://togogenome.org/gene/10090:D5Ertd579e ^@ http://purl.uniprot.org/uniprot/E9QPJ5|||http://purl.uniprot.org/uniprot/Q80U59 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Uncharacterized protein KIAA0232 ^@ http://purl.uniprot.org/annotation/PRO_0000261138|||http://purl.uniprot.org/annotation/VSP_021647|||http://purl.uniprot.org/annotation/VSP_021648|||http://purl.uniprot.org/annotation/VSP_021649|||http://purl.uniprot.org/annotation/VSP_021650 http://togogenome.org/gene/10090:Prom2 ^@ http://purl.uniprot.org/uniprot/Q3UUY6 ^@ Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Prominin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000331240|||http://purl.uniprot.org/annotation/VSP_033150 http://togogenome.org/gene/10090:Vbp1 ^@ http://purl.uniprot.org/uniprot/P61759 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||N6-acetyllysine|||Prefoldin subunit 3|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000153653 http://togogenome.org/gene/10090:Isca2 ^@ http://purl.uniprot.org/uniprot/Q9DCB8 ^@ Binding Site|||Chain|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Transit Peptide ^@ Iron-sulfur cluster assembly 2 homolog, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000277589 http://togogenome.org/gene/10090:Nqo2 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VL95|||http://purl.uniprot.org/uniprot/Q9CVF5|||http://purl.uniprot.org/uniprot/Q9JI75 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue ^@ Flavodoxin-like fold|||Phosphoserine|||Ribosyldihydronicotinamide dehydrogenase [quinone] ^@ http://purl.uniprot.org/annotation/PRO_0000071627 http://togogenome.org/gene/10090:Cpz ^@ http://purl.uniprot.org/uniprot/Q8R4V4 ^@ 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 ^@ Carboxypeptidase Z|||Disordered|||FZ|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000252457 http://togogenome.org/gene/10090:Hikeshi ^@ http://purl.uniprot.org/uniprot/A0A140LJ25|||http://purl.uniprot.org/uniprot/Q9DD02 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Flexible linker region involved in nuclear import of HSP70 proteins|||Hikeshi-like|||In isoform 2.|||Protein Hikeshi|||Required for F-X-F-G repeats-nucleoporins recognition and nuclear import ^@ http://purl.uniprot.org/annotation/PRO_0000245263|||http://purl.uniprot.org/annotation/VSP_043955 http://togogenome.org/gene/10090:Elac2 ^@ http://purl.uniprot.org/uniprot/Q3U0M8|||http://purl.uniprot.org/uniprot/Q80Y81 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Metallo-beta-lactamase|||Mitochondrion|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc phosphodiesterase ELAC protein 2|||tRNase Z endonuclease ^@ http://purl.uniprot.org/annotation/PRO_0000155830|||http://purl.uniprot.org/annotation/VSP_009173 http://togogenome.org/gene/10090:Phf8 ^@ http://purl.uniprot.org/uniprot/A2ABV3|||http://purl.uniprot.org/uniprot/Q80TJ7 ^@ 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|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Histone lysine demethylase PHF8|||In isoform 2.|||In isoform 3.|||JmjC|||Linker|||PHD-type|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000059296|||http://purl.uniprot.org/annotation/VSP_014966|||http://purl.uniprot.org/annotation/VSP_014967|||http://purl.uniprot.org/annotation/VSP_014968|||http://purl.uniprot.org/annotation/VSP_014969|||http://purl.uniprot.org/annotation/VSP_014970 http://togogenome.org/gene/10090:Rtkn ^@ http://purl.uniprot.org/uniprot/Q8C6B2 ^@ 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|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||PH|||Phosphoserine|||Polar residues|||REM-1|||Rhotekin ^@ http://purl.uniprot.org/annotation/PRO_0000233941|||http://purl.uniprot.org/annotation/VSP_052006 http://togogenome.org/gene/10090:Or2y1f ^@ http://purl.uniprot.org/uniprot/Q8VFA6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nup85 ^@ http://purl.uniprot.org/uniprot/Q8R480 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ N-acetylmethionine|||N6-acetyllysine|||Nuclear pore complex protein Nup85 ^@ http://purl.uniprot.org/annotation/PRO_0000324188 http://togogenome.org/gene/10090:Elane ^@ http://purl.uniprot.org/uniprot/Q3UP87 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||N-linked (GlcNAc...) asparagine|||Neutrophil elastase|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000228686 http://togogenome.org/gene/10090:Ankmy2 ^@ http://purl.uniprot.org/uniprot/Q3TPE9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat and MYND domain-containing protein 2|||Disordered|||In isoform 2.|||MYND-type|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247167|||http://purl.uniprot.org/annotation/VSP_019937|||http://purl.uniprot.org/annotation/VSP_019938 http://togogenome.org/gene/10090:Brms1 ^@ http://purl.uniprot.org/uniprot/Q547N0|||http://purl.uniprot.org/uniprot/Q99N20 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Region ^@ Acidic residues|||Breast cancer metastasis-suppressor 1 homolog|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) ^@ http://purl.uniprot.org/annotation/PRO_0000064989 http://togogenome.org/gene/10090:Itga2 ^@ http://purl.uniprot.org/uniprot/Q62469 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cell attachment site|||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-2|||N-linked (GlcNAc...) asparagine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000016234 http://togogenome.org/gene/10090:Lrrtm3 ^@ http://purl.uniprot.org/uniprot/Q8BZ81 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||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 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_0000018357|||http://purl.uniprot.org/annotation/VSP_014191|||http://purl.uniprot.org/annotation/VSP_014192 http://togogenome.org/gene/10090:Crybb3 ^@ http://purl.uniprot.org/uniprot/Q9JJU9 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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|||N-acetylalanine; in Beta-crystallin B3, N-terminally processed|||N-acetylmethionine|||N-terminal arm|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000057561|||http://purl.uniprot.org/annotation/PRO_0000421775 http://togogenome.org/gene/10090:Actrt1 ^@ http://purl.uniprot.org/uniprot/Q9D9J3 ^@ Chain|||Molecule Processing ^@ Chain ^@ Actin-related protein T1 ^@ http://purl.uniprot.org/annotation/PRO_0000255658 http://togogenome.org/gene/10090:Lepr ^@ http://purl.uniprot.org/uniprot/P48356|||http://purl.uniprot.org/uniprot/Q3UNU8|||http://purl.uniprot.org/uniprot/Q3US58|||http://purl.uniprot.org/uniprot/Q640Q2 ^@ 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|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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 ^@ Abrogates STAT3 phosphorylation.|||Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Helical|||Ig-like|||In isoform A.|||In isoform C.|||In isoform D.|||In isoform E.|||In strain: KKObese.|||In strain: NZO.|||Leptin receptor|||Leptin-binding|||N-linked (GlcNAc...) asparagine|||No change in EPO-induced JAK2 activation and EPO-induced tyrosine phosphorylation. No phosphorylation; when associated with L-985. No phosphorylation; when associated with L-985 and F-1077. No STAT3 activation. No change in SOCS3 binding nor signaling inhibition. No effect on ERK/FOS activation.|||No change in EPO-induced JAK2 activation and EPO-induced tyrosine phosphorylation. No phosphorylation; when associated with S-1138. No phosphorylation; when associated with both S-1138 and F-1077. No change in STAT3 activation. No PTPN11 binding. No SOCS3 binding nor inhibition of signaling. Greatly reduced ERK/FOS activation. Mutants are hyperphagic, obese and hyperglycaemic, females show a defect in lactation.|||No effect on EPO-induced tyrosine phosphorylation.|||No effect on STAT3 phosphorylation.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by JAK2|||Required for JAK2 activation|||Required for STAT3 phosphorylation|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010906|||http://purl.uniprot.org/annotation/VSP_001697|||http://purl.uniprot.org/annotation/VSP_001698|||http://purl.uniprot.org/annotation/VSP_001699|||http://purl.uniprot.org/annotation/VSP_001700|||http://purl.uniprot.org/annotation/VSP_001701|||http://purl.uniprot.org/annotation/VSP_001702|||http://purl.uniprot.org/annotation/VSP_001703|||http://purl.uniprot.org/annotation/VSP_001704 http://togogenome.org/gene/10090:Tesl1 ^@ http://purl.uniprot.org/uniprot/B1AXB9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||LIM zinc-binding|||PET ^@ http://togogenome.org/gene/10090:Rbm24 ^@ http://purl.uniprot.org/uniprot/D3Z4I3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Necessary for interaction with EIF4E|||RNA-binding protein 24|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000416117 http://togogenome.org/gene/10090:Cfap126 ^@ http://purl.uniprot.org/uniprot/Q6P8X9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Protein Flattop ^@ http://purl.uniprot.org/annotation/PRO_0000316973 http://togogenome.org/gene/10090:Mta1 ^@ http://purl.uniprot.org/uniprot/E9PX23|||http://purl.uniprot.org/uniprot/F8WHY8|||http://purl.uniprot.org/uniprot/Q2KHS8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BAH|||Disordered|||ELM2|||Polar residues|||SANT ^@ http://togogenome.org/gene/10090:Ccl9 ^@ http://purl.uniprot.org/uniprot/P51670|||http://purl.uniprot.org/uniprot/Q3U9T8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ C-C motif chemokine|||C-C motif chemokine 9|||CCL9(29-101)|||CCL9(30-101)|||CCL9(31-101)|||Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_0000005192|||http://purl.uniprot.org/annotation/PRO_0000041865|||http://purl.uniprot.org/annotation/PRO_0000041866|||http://purl.uniprot.org/annotation/PRO_0000041867|||http://purl.uniprot.org/annotation/PRO_5015020014 http://togogenome.org/gene/10090:Ttyh2 ^@ http://purl.uniprot.org/uniprot/Q3TH73 ^@ Chain|||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|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||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_0000312247|||http://purl.uniprot.org/annotation/VSP_029768 http://togogenome.org/gene/10090:Vmn1r213 ^@ http://purl.uniprot.org/uniprot/Q8R278 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tspan33 ^@ http://purl.uniprot.org/uniprot/Q8R3S2 ^@ 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|||Tetraspanin-33 ^@ http://purl.uniprot.org/annotation/PRO_0000282923|||http://purl.uniprot.org/annotation/VSP_024250 http://togogenome.org/gene/10090:Sec14l5 ^@ http://purl.uniprot.org/uniprot/B2RXM5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ CRAL-TRIO|||GOLD|||PRELI/MSF1 ^@ http://togogenome.org/gene/10090:Rtn4r ^@ http://purl.uniprot.org/uniprot/Q99PI8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Repeat|||Signal Peptide|||Strand|||Turn ^@ Disordered|||GPI-anchor amidated serine|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000022257|||http://purl.uniprot.org/annotation/PRO_0000022258 http://togogenome.org/gene/10090:Gzmf ^@ http://purl.uniprot.org/uniprot/P08883|||http://purl.uniprot.org/uniprot/Q497Z7 ^@ 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 ^@ Charge relay system|||Granzyme F|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027409|||http://purl.uniprot.org/annotation/PRO_0000027410|||http://purl.uniprot.org/annotation/PRO_5014309292 http://togogenome.org/gene/10090:Axdnd1 ^@ http://purl.uniprot.org/uniprot/Q3UZ57 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant ^@ Axonemal dynein light chain domain-containing protein 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284870|||http://purl.uniprot.org/annotation/VSP_061968|||http://purl.uniprot.org/annotation/VSP_061969|||http://purl.uniprot.org/annotation/VSP_061970 http://togogenome.org/gene/10090:Crygd ^@ http://purl.uniprot.org/uniprot/P04342 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000057598 http://togogenome.org/gene/10090:Trpv4 ^@ http://purl.uniprot.org/uniprot/Q9EPK8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ANK 1|||ANK 2|||ANK 3|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-672.|||Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-682.|||Helical|||Impairs Ca(2+) permeation.|||Increases protein abundance at plasma membrane. Greatly reduces channel activity.|||Interaction with calmodulin and ITPR3|||Loss of a probable N-glycosylation site. Increased expression at the cell membrane, leading to increased ion currents.|||Loss of phosphorylation but no significant effect on channel activity.|||N-linked (GlcNAc...) asparagine|||No changes in channel activation by 4-alpha-PDD or heat.|||No changes in channel activity.|||No effect on channel pore properties.|||Phosphomimetic mutant which enhances channel function.|||Phosphoserine; by PKC and PKA|||Phosphotyrosine; by LYN|||Phosphotyrosine; by SRC-type Tyr-kinases|||Pore-forming|||Reduces channel activation by 4-alpha-PDD and heat but not hypo-osmotic cell swelling.|||Results are conflicting as to whether hypotonicity-dependent channel activity is abolished.|||Selectivity filter|||Strongly reduced interaction with PACSIN3.|||Transient receptor potential cation channel subfamily V member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000215348 http://togogenome.org/gene/10090:Rhox2h ^@ http://purl.uniprot.org/uniprot/K7N6P1 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Vmn1r14 ^@ http://purl.uniprot.org/uniprot/H3BJ46 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Snx14 ^@ http://purl.uniprot.org/uniprot/Q8BHY8 ^@ 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|||PX|||PXA|||Phosphoserine|||RGS|||Sorting nexin-14 ^@ http://purl.uniprot.org/annotation/PRO_0000236201 http://togogenome.org/gene/10090:Ccdc113 ^@ http://purl.uniprot.org/uniprot/Q8C5T8 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Coiled-coil domain-containing protein 113 ^@ http://purl.uniprot.org/annotation/PRO_0000279400 http://togogenome.org/gene/10090:Pmm1 ^@ http://purl.uniprot.org/uniprot/O35621|||http://purl.uniprot.org/uniprot/Q545Q8|||http://purl.uniprot.org/uniprot/Q91W01 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||Nucleophile|||Phosphomannomutase 1|||Phosphoserine|||Proton donor/acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000199693 http://togogenome.org/gene/10090:Ide ^@ http://purl.uniprot.org/uniprot/Q8CGB9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Peptidase M16 C-terminal|||Peptidase M16 N-terminal|||Peptidase M16 middle/third ^@ http://togogenome.org/gene/10090:Ms4a20 ^@ http://purl.uniprot.org/uniprot/A0A9L6KDG8|||http://purl.uniprot.org/uniprot/G5E851|||http://purl.uniprot.org/uniprot/Q9DA92 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Or52u1 ^@ http://purl.uniprot.org/uniprot/Q8VF27 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Psg29 ^@ http://purl.uniprot.org/uniprot/Q3URN6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Gm16434 ^@ http://purl.uniprot.org/uniprot/K7N6G4 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:Emc4 ^@ http://purl.uniprot.org/uniprot/Q9CZX9 ^@ 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|||ER membrane protein complex subunit 4|||Helical|||Lumenal|||N-acetylthreonine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000251915 http://togogenome.org/gene/10090:Eef1d ^@ http://purl.uniprot.org/uniprot/A0A0R4J1E2|||http://purl.uniprot.org/uniprot/A0A0R4J1L2|||http://purl.uniprot.org/uniprot/P57776|||http://purl.uniprot.org/uniprot/Q80T06|||http://purl.uniprot.org/uniprot/Q91VK2 ^@ 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 ^@ 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.|||Leucine-zipper|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Polar residues|||Removed|||Translation elongation factor EF1B beta/delta subunit guanine nucleotide exchange ^@ http://purl.uniprot.org/annotation/PRO_0000155047|||http://purl.uniprot.org/annotation/VSP_001359|||http://purl.uniprot.org/annotation/VSP_037885 http://togogenome.org/gene/10090:Nkg7 ^@ http://purl.uniprot.org/uniprot/Q9CY55 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Or9s13 ^@ http://purl.uniprot.org/uniprot/Q0VBN7|||http://purl.uniprot.org/uniprot/Q60894 ^@ 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 9S13 ^@ http://purl.uniprot.org/annotation/PRO_0000150811 http://togogenome.org/gene/10090:Paox ^@ http://purl.uniprot.org/uniprot/Q3TXR6|||http://purl.uniprot.org/uniprot/Q8C0L6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Splice Variant|||Strand|||Turn ^@ Amine oxidase|||Decreased enzyme activity with N(1)-acetylspermine.|||In isoform 2.|||Microbody targeting signal|||Peroxisomal N(1)-acetyl-spermine/spermidine oxidase ^@ http://purl.uniprot.org/annotation/PRO_0000099876|||http://purl.uniprot.org/annotation/VSP_011263|||http://purl.uniprot.org/annotation/VSP_011264 http://togogenome.org/gene/10090:Zfp997 ^@ http://purl.uniprot.org/uniprot/A0A571BGF1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Kcnj4 ^@ http://purl.uniprot.org/uniprot/Q8R435|||http://purl.uniprot.org/uniprot/Q9QYK8 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Site|||Transmembrane ^@ Domain Extent|||Non-terminal Residue|||Site|||Transmembrane ^@ Helical|||Inward rectifier potassium channel C-terminal|||Potassium channel inwardly rectifying transmembrane|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium ^@ http://togogenome.org/gene/10090:Tbc1d5 ^@ http://purl.uniprot.org/uniprot/A0A286YDB3|||http://purl.uniprot.org/uniprot/Q3UN43|||http://purl.uniprot.org/uniprot/Q80XQ2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ Arginine finger|||Asymmetric dimethylarginine; alternate|||Disordered|||Glutamine finger|||LIR 1|||LIR 2|||Omega-N-methylarginine; alternate|||Phosphoserine|||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_0000208029 http://togogenome.org/gene/10090:Nle1 ^@ http://purl.uniprot.org/uniprot/Q3URT5|||http://purl.uniprot.org/uniprot/Q8VEJ4 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict ^@ In l11Jus1; embryos survive through implantation but fail prior to gastrulation. Cdkna1 expression is up-regulated while expression of several Wnt pathway members is down-regulated.|||In l11Jus4; embryos survive through implantation but fail prior to gastrulation.|||N-acetylalanine|||NLE|||Notchless protein homolog 1|||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_0000051099 http://togogenome.org/gene/10090:Cfap97d1 ^@ http://purl.uniprot.org/uniprot/Q9DAN9 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Sperm axonemal maintenance protein CFAP97D1 ^@ http://purl.uniprot.org/annotation/PRO_0000392550 http://togogenome.org/gene/10090:Ltk ^@ http://purl.uniprot.org/uniprot/P08923|||http://purl.uniprot.org/uniprot/Q0VGZ5 ^@ 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|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||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|||In isoform A and isoform B.|||In isoform A and isoform C.|||Leukocyte tyrosine kinase receptor|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000016739|||http://purl.uniprot.org/annotation/VSP_002950|||http://purl.uniprot.org/annotation/VSP_002951|||http://purl.uniprot.org/annotation/VSP_002952 http://togogenome.org/gene/10090:a ^@ http://purl.uniprot.org/uniprot/A0A510NUK5|||http://purl.uniprot.org/uniprot/Q03288|||http://purl.uniprot.org/uniprot/Q3TZL0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Agouti|||Agouti-signaling protein|||Basic residues|||CCHC-type|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000001029|||http://purl.uniprot.org/annotation/PRO_5015097468 http://togogenome.org/gene/10090:Psmc5 ^@ http://purl.uniprot.org/uniprot/P62196 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 26S proteasome regulatory subunit 8|||May mediate interaction with PRPF9|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000084722 http://togogenome.org/gene/10090:Trim43a ^@ http://purl.uniprot.org/uniprot/Q3TL54 ^@ 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 43A ^@ http://purl.uniprot.org/annotation/PRO_0000392434 http://togogenome.org/gene/10090:Cflar ^@ http://purl.uniprot.org/uniprot/O35732|||http://purl.uniprot.org/uniprot/Q5U4G3|||http://purl.uniprot.org/uniprot/Q812G4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ 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|||In isoform 2.|||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|||Loss of CASP8-mediated cleavage; when associated with A-371.|||Loss of CASP8-mediated cleavage; when associated with A-377. ^@ http://purl.uniprot.org/annotation/PRO_0000004680|||http://purl.uniprot.org/annotation/PRO_0000004681|||http://purl.uniprot.org/annotation/VSP_000842|||http://purl.uniprot.org/annotation/VSP_000843 http://togogenome.org/gene/10090:Snrnp35 ^@ http://purl.uniprot.org/uniprot/Q9D384 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||RRM|||U11/U12 small nuclear ribonucleoprotein 35 kDa protein ^@ http://purl.uniprot.org/annotation/PRO_0000307908 http://togogenome.org/gene/10090:Mfsd2b ^@ http://purl.uniprot.org/uniprot/B8JK43 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Trmo ^@ http://purl.uniprot.org/uniprot/Q562D6 ^@ 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|||In isoform 2.|||In isoform 3.|||TsaA-like|||tRNA (adenine(37)-N6)-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000288887|||http://purl.uniprot.org/annotation/VSP_025815|||http://purl.uniprot.org/annotation/VSP_025816 http://togogenome.org/gene/10090:Scgb1b3 ^@ http://purl.uniprot.org/uniprot/J3QJY4 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015095413 http://togogenome.org/gene/10090:Nipa1 ^@ http://purl.uniprot.org/uniprot/Q8BHK1 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Failure to correctly traffic to the cell membrane and complete loss of Mg(2+) transport.|||Failure to correctly traffic to the cell membrane and diminished Mg(2+) transport.|||Helical|||Magnesium transporter NIPA1 ^@ http://purl.uniprot.org/annotation/PRO_0000191742 http://togogenome.org/gene/10090:Acvr2a ^@ http://purl.uniprot.org/uniprot/A2AI38|||http://purl.uniprot.org/uniprot/P27038|||http://purl.uniprot.org/uniprot/Q8BRV4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Activin receptor type-2A|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase receptor ^@ http://purl.uniprot.org/annotation/PRO_0000024399|||http://purl.uniprot.org/annotation/PRO_5004304232|||http://purl.uniprot.org/annotation/PRO_5014296788 http://togogenome.org/gene/10090:Pitpnm1 ^@ http://purl.uniprot.org/uniprot/O35954 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ DDHD|||Disordered|||Membrane-associated phosphatidylinositol transfer protein 1|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000232739 http://togogenome.org/gene/10090:Vmn2r63 ^@ http://purl.uniprot.org/uniprot/E9Q0K5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245578 http://togogenome.org/gene/10090:Cxcr5 ^@ http://purl.uniprot.org/uniprot/Q04683 ^@ 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 ^@ C-X-C chemokine receptor type 5|||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_0000069361 http://togogenome.org/gene/10090:Smad5 ^@ http://purl.uniprot.org/uniprot/P97454 ^@ 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|||Exhibits impaired binding affinity to GC-BREDNA sequence.|||MH1|||MH2|||Mothers against decapentaplegic homolog 5|||N-acetylthreonine|||Phosphoserine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000090866 http://togogenome.org/gene/10090:Acvr1 ^@ http://purl.uniprot.org/uniprot/P37172 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Activin receptor type-1|||Cytoplasmic|||Extracellular|||GS|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000024395 http://togogenome.org/gene/10090:Ttl ^@ http://purl.uniprot.org/uniprot/P38585 ^@ 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_0000212435 http://togogenome.org/gene/10090:Lap3 ^@ http://purl.uniprot.org/uniprot/Q9CPY7 ^@ 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_0000165826|||http://purl.uniprot.org/annotation/VSP_022632 http://togogenome.org/gene/10090:Ggn ^@ http://purl.uniprot.org/uniprot/A0A140LI02|||http://purl.uniprot.org/uniprot/G5E8M4|||http://purl.uniprot.org/uniprot/Q80WJ1 ^@ 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|||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_0000239343|||http://purl.uniprot.org/annotation/VSP_019171|||http://purl.uniprot.org/annotation/VSP_019172|||http://purl.uniprot.org/annotation/VSP_019173 http://togogenome.org/gene/10090:Cdkl1 ^@ http://purl.uniprot.org/uniprot/Q14BG3|||http://purl.uniprot.org/uniprot/Q8CEQ0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Motif ^@ Cyclin-dependent kinase-like 1|||Protein kinase|||Proton acceptor|||[NKR]KIAxRE ^@ http://purl.uniprot.org/annotation/PRO_0000085811 http://togogenome.org/gene/10090:Hax1 ^@ http://purl.uniprot.org/uniprot/A0A0G2JE46|||http://purl.uniprot.org/uniprot/A0A0G2JFF9|||http://purl.uniprot.org/uniprot/B9EJR4|||http://purl.uniprot.org/uniprot/O35387|||http://purl.uniprot.org/uniprot/Q3UXX9|||http://purl.uniprot.org/uniprot/Q8R5I5 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Site ^@ Acidic residues|||Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||HCLS1-associated protein X-1|||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_0000083907 http://togogenome.org/gene/10090:Snurf ^@ http://purl.uniprot.org/uniprot/Q9WU12 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ SNRPN upstream reading frame protein ^@ http://purl.uniprot.org/annotation/PRO_0000312994 http://togogenome.org/gene/10090:Plcb1 ^@ http://purl.uniprot.org/uniprot/Q3UPW0|||http://purl.uniprot.org/uniprot/Q9Z1B3 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1|||Acidic residues|||Basic and acidic residues|||C2|||Disordered|||In isoform B.|||In isoform C.|||PI-PLC X-box|||PI-PLC Y-box|||Phosphatidylinositol-specific phospholipase C X|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000088487|||http://purl.uniprot.org/annotation/VSP_008917|||http://purl.uniprot.org/annotation/VSP_008918 http://togogenome.org/gene/10090:Ptgir ^@ http://purl.uniprot.org/uniprot/P43252|||http://purl.uniprot.org/uniprot/Q8CC99 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes isoprenylation.|||Cysteine methyl ester|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Prostacyclin receptor|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000070076|||http://purl.uniprot.org/annotation/PRO_0000240005 http://togogenome.org/gene/10090:Or51aa5 ^@ http://purl.uniprot.org/uniprot/K7N609 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ube2m ^@ http://purl.uniprot.org/uniprot/G5E919|||http://purl.uniprot.org/uniprot/P61082 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||Interaction with UBA3|||N-acetylmethionine|||N6-acetyllysine|||NEDD8-conjugating enzyme Ubc12|||Omega-N-methylarginine; alternate|||Phosphoserine|||UBC core ^@ http://purl.uniprot.org/annotation/PRO_0000082489 http://togogenome.org/gene/10090:Ms4a14 ^@ http://purl.uniprot.org/uniprot/A0A087WSD2 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Ptges2 ^@ http://purl.uniprot.org/uniprot/Q8BWM0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cleavage|||Cytoplasmic|||GST C-terminal|||Glutaredoxin|||Helical|||Lumenal|||Prostaglandin E synthase 2|||Prostaglandin E synthase 2 truncated form ^@ http://purl.uniprot.org/annotation/PRO_0000013131|||http://purl.uniprot.org/annotation/PRO_0000013132 http://togogenome.org/gene/10090:Ehd2 ^@ http://purl.uniprot.org/uniprot/Q8BH64 ^@ 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 ATP binding.|||Abolishes increase of intrinsic ATPase activity upon interaction with membranes.|||Abolishes localization at the plasma membrane.|||Abolishes localization at the plasma membrane; abolishes increase of intrinsic ATPase activity upon interaction with membranes.|||Abolishes localization at the plasma membrane; reduces increase of intrinsic ATPase activity upon interaction with membranes.|||Disordered|||Dynamin-type G|||EF-hand|||EH|||EH domain-containing protein 2|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Increases intrinsic ATPase activity.|||Inhibits myoblast fusion.|||Mediates membrane-binding|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000322643 http://togogenome.org/gene/10090:Kctd2 ^@ http://purl.uniprot.org/uniprot/Q4VBE7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BTB|||Disordered ^@ http://togogenome.org/gene/10090:Tigd2 ^@ http://purl.uniprot.org/uniprot/Q0VBL1 ^@ 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 2 ^@ http://purl.uniprot.org/annotation/PRO_0000271089 http://togogenome.org/gene/10090:Bgn ^@ http://purl.uniprot.org/uniprot/P28653|||http://purl.uniprot.org/uniprot/Q3TNY9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Biglycan|||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_0000032693|||http://purl.uniprot.org/annotation/PRO_0000032694|||http://purl.uniprot.org/annotation/PRO_5014205822 http://togogenome.org/gene/10090:Rabgap1 ^@ http://purl.uniprot.org/uniprot/A2AWA9|||http://purl.uniprot.org/uniprot/B2RRC5 ^@ 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 ^@ Arginine finger|||Disordered|||Glutamine finger|||In isoform 2.|||In isoform 3.|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rab GTPase-activating protein 1|||Rab-GAP TBC ^@ http://purl.uniprot.org/annotation/PRO_0000298780|||http://purl.uniprot.org/annotation/VSP_052516|||http://purl.uniprot.org/annotation/VSP_052517|||http://purl.uniprot.org/annotation/VSP_052518|||http://purl.uniprot.org/annotation/VSP_052519|||http://purl.uniprot.org/annotation/VSP_052520|||http://purl.uniprot.org/annotation/VSP_052521 http://togogenome.org/gene/10090:Nptx2 ^@ http://purl.uniprot.org/uniprot/O70340|||http://purl.uniprot.org/uniprot/Q3UYB9 ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Neuronal pentraxin-2|||Pentraxin (PTX) ^@ http://purl.uniprot.org/annotation/PRO_0000023552|||http://purl.uniprot.org/annotation/PRO_5004230397 http://togogenome.org/gene/10090:4930453N24Rik ^@ http://purl.uniprot.org/uniprot/Q3TTL0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Uncharacterized protein C3orf38 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000244990 http://togogenome.org/gene/10090:Tbc1d13 ^@ http://purl.uniprot.org/uniprot/Q3TZ63|||http://purl.uniprot.org/uniprot/Q8R3D1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Rab-GAP TBC|||TBC1 domain family member 13 ^@ http://purl.uniprot.org/annotation/PRO_0000208039 http://togogenome.org/gene/10090:Fndc3c1 ^@ http://purl.uniprot.org/uniprot/Q6DFV6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Fibronectin type III domain containing protein 3C1|||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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000379879 http://togogenome.org/gene/10090:Serpinf2 ^@ http://purl.uniprot.org/uniprot/Q5ND36|||http://purl.uniprot.org/uniprot/Q61247 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Signal Peptide|||Site|||Strand|||Turn ^@ Alpha-2-antiplasmin|||Cleavage; by prolyl endopeptidase FAP, antiplasmin-cleaving enzyme FAP soluble form|||Disordered|||N-linked (GlcNAc...) asparagine|||Reactive bond for chymotrypsin|||Reactive bond for plasmin|||Serpin|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000032513|||http://purl.uniprot.org/annotation/PRO_0000430668|||http://purl.uniprot.org/annotation/PRO_5014309901 http://togogenome.org/gene/10090:Ceacam18 ^@ http://purl.uniprot.org/uniprot/Q9D871 ^@ 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 ^@ Carcinoembryonic antigen-related cell adhesion molecule 18|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000339379 http://togogenome.org/gene/10090:Nxf1 ^@ http://purl.uniprot.org/uniprot/Q99JX7|||http://purl.uniprot.org/uniprot/V9GXF3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ 3'-nitrotyrosine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||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|||RNA binding|||RNA-binding (RBD)|||RRM|||Removed|||TAP-C ^@ http://purl.uniprot.org/annotation/PRO_0000220530 http://togogenome.org/gene/10090:Spp1 ^@ http://purl.uniprot.org/uniprot/F8WIP8|||http://purl.uniprot.org/uniprot/P10923|||http://purl.uniprot.org/uniprot/Q3UBR1|||http://purl.uniprot.org/uniprot/Q547B5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Cell attachment site|||Disordered|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Osteopontin|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000020322|||http://purl.uniprot.org/annotation/PRO_5003385657|||http://purl.uniprot.org/annotation/PRO_5004230059|||http://purl.uniprot.org/annotation/PRO_5014309650 http://togogenome.org/gene/10090:Appl2 ^@ http://purl.uniprot.org/uniprot/Q3TVI6|||http://purl.uniprot.org/uniprot/Q8K3G9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ BAR|||DCC-interacting protein 13-beta|||Disordered|||PH|||PID|||Polar residues|||Required for RAB5A binding ^@ http://purl.uniprot.org/annotation/PRO_0000079988 http://togogenome.org/gene/10090:Ube2e2 ^@ http://purl.uniprot.org/uniprot/Q91W82 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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_0000082473 http://togogenome.org/gene/10090:Cep104 ^@ http://purl.uniprot.org/uniprot/Q80V31 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Centrosomal protein of 104 kDa|||Disordered|||HEAT 1|||HEAT 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000050764 http://togogenome.org/gene/10090:Pou4f1 ^@ http://purl.uniprot.org/uniprot/P17208 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||DNA Binding|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes transcriptional activity. Increases transcriptional repression. Disrupts induction of neurite outgrowth and expression of synaptic genes. No effect on transactivation of BCL2 expression.|||Disordered|||Homeobox|||In isoform 2.|||POU domain, class 4, transcription factor 1|||POU-IV box|||POU-specific ^@ http://purl.uniprot.org/annotation/PRO_0000100737|||http://purl.uniprot.org/annotation/VSP_058637 http://togogenome.org/gene/10090:Sft2d1 ^@ http://purl.uniprot.org/uniprot/Q5SSN7 ^@ 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|||Phosphoserine|||Vesicle transport protein SFT2A ^@ http://purl.uniprot.org/annotation/PRO_0000238608 http://togogenome.org/gene/10090:Adgrg2 ^@ http://purl.uniprot.org/uniprot/Q14AX7|||http://purl.uniprot.org/uniprot/Q14BH6|||http://purl.uniprot.org/uniprot/Q8CJ12 ^@ 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 ^@ Adhesion G-protein coupled receptor G2|||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 isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000012887|||http://purl.uniprot.org/annotation/VSP_009806|||http://purl.uniprot.org/annotation/VSP_009807|||http://purl.uniprot.org/annotation/VSP_009808|||http://purl.uniprot.org/annotation/VSP_009809 http://togogenome.org/gene/10090:Ct55 ^@ http://purl.uniprot.org/uniprot/Q14BQ3 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Cancer/testis antigen 55 ^@ http://purl.uniprot.org/annotation/PRO_0000458875 http://togogenome.org/gene/10090:Pgls ^@ http://purl.uniprot.org/uniprot/D3Z4X1|||http://purl.uniprot.org/uniprot/Q9CQ60 ^@ 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_0000090079 http://togogenome.org/gene/10090:Timm8a2 ^@ http://purl.uniprot.org/uniprot/Q4FZG7 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Motif ^@ Putative mitochondrial import inner membrane translocase subunit Tim8 A-B|||Twin CX3C motif ^@ http://purl.uniprot.org/annotation/PRO_0000228021 http://togogenome.org/gene/10090:Rab33a ^@ http://purl.uniprot.org/uniprot/P97950 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue ^@ Cysteine methyl ester|||Ras-related protein Rab-33A|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121238 http://togogenome.org/gene/10090:Xpnpep1 ^@ http://purl.uniprot.org/uniprot/Q3UE92|||http://purl.uniprot.org/uniprot/Q3UKF5|||http://purl.uniprot.org/uniprot/Q6P1B1 ^@ 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 ^@ Creatinase N-terminal|||N6-acetyllysine|||Peptidase M24|||Peptidase M24 C-terminal|||Xaa-Pro aminopeptidase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000185084 http://togogenome.org/gene/10090:Cym ^@ http://purl.uniprot.org/uniprot/B7ZWD6 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Peptidase A1 ^@ http://purl.uniprot.org/annotation/PRO_5015087458 http://togogenome.org/gene/10090:Figla ^@ http://purl.uniprot.org/uniprot/H6UWL1|||http://purl.uniprot.org/uniprot/O55208 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Disordered|||Factor in the germline alpha|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127180 http://togogenome.org/gene/10090:Aldh7a1 ^@ http://purl.uniprot.org/uniprot/Q9DBF1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Alpha-aminoadipic semialdehyde dehydrogenase|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Proton acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000056491|||http://purl.uniprot.org/annotation/VSP_038989 http://togogenome.org/gene/10090:Zmynd19 ^@ http://purl.uniprot.org/uniprot/Q9CQG3 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Splice Variant|||Zinc Finger ^@ In isoform 2.|||MYND-type; degenerate|||Zinc finger MYND domain-containing protein 19 ^@ http://purl.uniprot.org/annotation/PRO_0000218320|||http://purl.uniprot.org/annotation/VSP_010075 http://togogenome.org/gene/10090:Oacyl ^@ http://purl.uniprot.org/uniprot/Q8BML2 ^@ 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 2.|||O-acyltransferase like protein ^@ http://purl.uniprot.org/annotation/PRO_5007927424|||http://purl.uniprot.org/annotation/VSP_058597 http://togogenome.org/gene/10090:Lair1 ^@ http://purl.uniprot.org/uniprot/Q8BG84 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||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|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||Ig-like C2-type|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||Leukocyte-associated immunoglobulin-like receptor 1|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000250683|||http://purl.uniprot.org/annotation/VSP_020714|||http://purl.uniprot.org/annotation/VSP_020715|||http://purl.uniprot.org/annotation/VSP_020716|||http://purl.uniprot.org/annotation/VSP_020718|||http://purl.uniprot.org/annotation/VSP_020719 http://togogenome.org/gene/10090:Rhoh ^@ http://purl.uniprot.org/uniprot/Q9D3G9 ^@ 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|||Region ^@ Abolishes interaction with ZAP70; when associated with F-73.|||Abolishes interaction with ZAP70; when associated with F-83.|||Cysteine methyl ester|||Effector region|||Interaction with ZAP70|||Removed in mature form|||Rho-related GTP-binding protein RhoH|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000198868|||http://purl.uniprot.org/annotation/PRO_0000281219 http://togogenome.org/gene/10090:Col4a3 ^@ http://purl.uniprot.org/uniprot/Q9QZS0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ 7S domain|||Cell attachment site|||Cleavage; by collagenase|||Collagen IV NC1|||Collagen alpha-3(IV) chain|||Disordered|||Epitope recognized by Goodpasture antibodies|||N-linked (GlcNAc...) asparagine|||Or C-1459 with C-1547|||Or C-1492 with C-1550|||Or C-1569 with C-1661|||Or C-1603 with C-1664|||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-1532)|||S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1650)|||Triple-helical region|||Tumstatin ^@ http://purl.uniprot.org/annotation/PRO_0000279698|||http://purl.uniprot.org/annotation/PRO_0000279699 http://togogenome.org/gene/10090:Smim18 ^@ http://purl.uniprot.org/uniprot/J3QNP2 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Hspd1 ^@ http://purl.uniprot.org/uniprot/P63038 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ 60 kDa heat shock protein, mitochondrial|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000005027|||http://purl.uniprot.org/annotation/VSP_025020 http://togogenome.org/gene/10090:Elmo3 ^@ http://purl.uniprot.org/uniprot/A0A1D5RMK9|||http://purl.uniprot.org/uniprot/Q8BYZ7 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Motif|||Splice Variant ^@ ELMO|||Engulfment and cell motility protein 3|||In isoform 2.|||PH|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000153717|||http://purl.uniprot.org/annotation/VSP_037343 http://togogenome.org/gene/10090:Tenm1 ^@ http://purl.uniprot.org/uniprot/A2ANL9|||http://purl.uniprot.org/uniprot/A2ANM0|||http://purl.uniprot.org/uniprot/Q9WTS4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Repeat|||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 isoform 2.|||N-linked (GlcNAc...) asparagine|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||Nuclear localization signal (NLS)|||Phosphoserine|||Phosphothreonine|||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_0000259499|||http://purl.uniprot.org/annotation/PRO_0000421007|||http://purl.uniprot.org/annotation/PRO_0000421008|||http://purl.uniprot.org/annotation/VSP_045018 http://togogenome.org/gene/10090:Parp12 ^@ http://purl.uniprot.org/uniprot/Q8BZ20 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ ADP-ribosyl aspartic acid|||ADP-ribosylcysteine|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||Disordered|||PARP catalytic|||Phosphoserine|||Polar residues|||Protein mono-ADP-ribosyltransferase PARP12|||WWE 1|||WWE 2 ^@ http://purl.uniprot.org/annotation/PRO_0000211342 http://togogenome.org/gene/10090:Tmc4 ^@ http://purl.uniprot.org/uniprot/F8VQ45|||http://purl.uniprot.org/uniprot/Q7TQ65 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||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_0000289469|||http://purl.uniprot.org/annotation/VSP_026014|||http://purl.uniprot.org/annotation/VSP_026015|||http://purl.uniprot.org/annotation/VSP_026016 http://togogenome.org/gene/10090:Vmn1r113 ^@ http://purl.uniprot.org/uniprot/G3UWI8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clec4a2 ^@ http://purl.uniprot.org/uniprot/Q923C7|||http://purl.uniprot.org/uniprot/Q9QZ15 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 4 member A|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||ITIM motif|||Loss of inhibition of B-cell calcium mobilization.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046613 http://togogenome.org/gene/10090:Or6c202 ^@ http://purl.uniprot.org/uniprot/Q8VFH6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sgk3 ^@ http://purl.uniprot.org/uniprot/Q9ERE3 ^@ 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 ^@ AGC-kinase C-terminal|||Basic and acidic residues|||Diminishes binding to phosphoinositides.|||Disordered|||No activity.|||Nuclear localization signal|||PX|||Phosphoserine|||Phosphothreonine; by PDPK1|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Sgk3 ^@ http://purl.uniprot.org/annotation/PRO_0000086650 http://togogenome.org/gene/10090:Esp18 ^@ http://purl.uniprot.org/uniprot/A8R0V1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015086683 http://togogenome.org/gene/10090:Ehd3 ^@ http://purl.uniprot.org/uniprot/Q9QXY6 ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 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)|||Loss of localization to membranes, reduced binding to phosphatidic acid.|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000146113 http://togogenome.org/gene/10090:Cadm3 ^@ http://purl.uniprot.org/uniprot/Q99N28 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||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|||N-linked (GlcNAc...) asparagine|||Nerves from mutant mice exhibit abnormal axonal organization.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000046068 http://togogenome.org/gene/10090:Gm715 ^@ http://purl.uniprot.org/uniprot/A0A804C8T0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||HUWE1-associated protein modifying stress responses 2|||Nuclear localization signal|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000457926 http://togogenome.org/gene/10090:Defa35 ^@ http://purl.uniprot.org/uniprot/E9QLQ1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Mammalian defensins ^@ http://purl.uniprot.org/annotation/PRO_5003246258 http://togogenome.org/gene/10090:Zfp429 ^@ http://purl.uniprot.org/uniprot/Q7M6Y0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Gfod1 ^@ http://purl.uniprot.org/uniprot/Q3UHD2 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Glucose-fructose oxidoreductase domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000282969 http://togogenome.org/gene/10090:Ralbp1 ^@ http://purl.uniprot.org/uniprot/Q62172 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||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_0000056734 http://togogenome.org/gene/10090:Myo19 ^@ http://purl.uniprot.org/uniprot/Q5SV80 ^@ 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 ^@ Actin-binding|||IQ 1|||IQ 2|||In isoform 2.|||MyMOMA region|||Myosin motor|||Unconventional myosin-XIX ^@ http://purl.uniprot.org/annotation/PRO_0000332970|||http://purl.uniprot.org/annotation/VSP_033407|||http://purl.uniprot.org/annotation/VSP_033408 http://togogenome.org/gene/10090:4933402J07Rik ^@ http://purl.uniprot.org/uniprot/Q8BHX0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Topors ^@ http://purl.uniprot.org/uniprot/Q80Z37 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Disordered|||E3 ubiquitin-protein ligase Topors|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with SUMO1|||Interaction with TOP1|||Interaction with UBE2I|||Interaction with p53/TP53|||Phosphoserine|||Phosphoserine; by PLK1|||Polar residues|||RING-type|||Required for DNA-binding|||Sumoylation and localization to discrete nuclear foci ^@ http://purl.uniprot.org/annotation/PRO_0000232627 http://togogenome.org/gene/10090:Zfp536 ^@ http://purl.uniprot.org/uniprot/Q8K083 ^@ 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 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_0000271042 http://togogenome.org/gene/10090:Ep300 ^@ http://purl.uniprot.org/uniprot/B2RWS6|||http://purl.uniprot.org/uniprot/Q8BJ14 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Asymmetric dimethylarginine; by CARM1|||Asymmetric dimethylarginine; by CARM1; alternate|||Basic and acidic residues|||Basic residues|||Bromo|||CBP/p300-type HAT|||CRD1; mediates transcriptional repression|||Citrulline; by PADI4; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Histone acetyltransferase p300|||Interaction with ALX1|||Interaction with NCOA2|||Interaction with RORA|||Interaction with histone|||KIX|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-acetyllysine; by autocatalysis|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by AMPK|||Polar residues|||Pro residues|||Removed|||TAZ-type|||TAZ-type 1|||TAZ-type 2|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000409386 http://togogenome.org/gene/10090:Sult1a1 ^@ http://purl.uniprot.org/uniprot/E9QNL5|||http://purl.uniprot.org/uniprot/Q91W19 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Arhgap26 ^@ http://purl.uniprot.org/uniprot/Q3U860|||http://purl.uniprot.org/uniprot/Q6ZQ82|||http://purl.uniprot.org/uniprot/Q9D0J3 ^@ 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 ^@ BAR|||Disordered|||PH|||Polar residues|||Pro residues|||Rho GTPase-activating protein 26|||Rho-GAP|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000355553 http://togogenome.org/gene/10090:Epm2a ^@ http://purl.uniprot.org/uniprot/Q9WUA5 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Abolishes phosphatase activity.|||CBM20|||Glucan phosphatase signature motif CXAGXGR|||Laforin|||Loss of glycogen phosphatase activity. Nearly abolishes phosphatase activity.|||Loss of phosphatase activity with glycogen and synthetic substrates.|||Nearly abolishes phosphatase activity.|||Phosphocysteine intermediate|||Phosphoserine; by AMPK|||Required for homodimerization|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094839 http://togogenome.org/gene/10090:Rps3 ^@ http://purl.uniprot.org/uniprot/P62908|||http://purl.uniprot.org/uniprot/Q5YLW3 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Asymmetric dimethylarginine; by PRMT1|||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|||KH type-2|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphoserine; by IKKB|||Phosphoserine; by PKC/PRKCD|||Phosphothreonine|||Phosphothreonine; by MAPK|||Phosphothreonine; by PKB|||Removed|||Small ribosomal subunit protein uS3 ^@ http://purl.uniprot.org/annotation/PRO_0000130321 http://togogenome.org/gene/10090:Irx6 ^@ http://purl.uniprot.org/uniprot/Q8BFT1|||http://purl.uniprot.org/uniprot/Q9ER75 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox|||Iroquois-class homeodomain protein IRX-6 ^@ http://purl.uniprot.org/annotation/PRO_0000049163 http://togogenome.org/gene/10090:Gm21518 ^@ http://purl.uniprot.org/uniprot/J3QNI1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Calhm4 ^@ http://purl.uniprot.org/uniprot/Q8CE93 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Calcium homeostasis modulator protein 4|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000186725 http://togogenome.org/gene/10090:Tmem63b ^@ http://purl.uniprot.org/uniprot/Q3TWI9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ CSC1-like protein 2|||Disordered|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000280729 http://togogenome.org/gene/10090:Defa23 ^@ http://purl.uniprot.org/uniprot/Q5G866 ^@ Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Alpha-defensin 23|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000300072|||http://purl.uniprot.org/annotation/PRO_0000300073 http://togogenome.org/gene/10090:Or4c104 ^@ http://purl.uniprot.org/uniprot/Q8VF94 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kcnip1 ^@ http://purl.uniprot.org/uniprot/Q3YAB5|||http://purl.uniprot.org/uniprot/Q3YAB6|||http://purl.uniprot.org/uniprot/Q9JJ57 ^@ 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|||EF-hand|||EF-hand 1; degenerate|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with KCND2|||Kv channel-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000073819|||http://purl.uniprot.org/annotation/VSP_015045|||http://purl.uniprot.org/annotation/VSP_015046|||http://purl.uniprot.org/annotation/VSP_015047 http://togogenome.org/gene/10090:Eif3m ^@ http://purl.uniprot.org/uniprot/Q99JX4 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Eukaryotic translation initiation factor 3 subunit M|||N-acetylserine|||N6-acetyllysine|||PCI|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000308196 http://togogenome.org/gene/10090:Lrrc14 ^@ http://purl.uniprot.org/uniprot/Q8VC16 ^@ 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|||Leucine-rich repeat-containing protein 14 ^@ http://purl.uniprot.org/annotation/PRO_0000343681 http://togogenome.org/gene/10090:Ppm1l ^@ http://purl.uniprot.org/uniprot/Q8BHN0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes phosphatase activity, prevents MAP3K7/TAK1 phosphorylation in vitro, does not abolish interaction with MAP3K7/TAK1, found in a complex with MAP3K7/TAK1, MAP2K4 or MAP2K6 and enhances the association between MAP3K7/TAK1, MAP2K4 or MAP2K6.|||Abolishes phosphatase activity.|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||PPM-type phosphatase|||Protein phosphatase 1L|||Slightly abolishes phosphatase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000057755|||http://purl.uniprot.org/annotation/VSP_016928|||http://purl.uniprot.org/annotation/VSP_016929 http://togogenome.org/gene/10090:Amfr ^@ http://purl.uniprot.org/uniprot/Q3TCI2|||http://purl.uniprot.org/uniprot/Q9R049 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ CUE|||Disordered|||E3 ubiquitin-protein ligase AMFR|||Helical|||In isoform 2.|||Phosphoserine|||RING-type|||VCP/p97-interacting motif (VIM) ^@ http://purl.uniprot.org/annotation/PRO_0000064580|||http://purl.uniprot.org/annotation/VSP_008224 http://togogenome.org/gene/10090:Epas1 ^@ http://purl.uniprot.org/uniprot/P97481 ^@ 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 ^@ (3S)-3-hydroxyasparagine|||4-hydroxyproline|||CTAD|||Confers transcriptional activity at normoxia; when associated with A-530.|||Confers transcriptional activity at normoxia; when associated with A-851.|||DNA-binding|||Decreases HREDNA binding.|||Decreases HREDNA binding; when associated with D-184.|||Decreases HREDNA binding; when associated with D-186.|||Decreases heterodimer formation with ARNT.|||Decreases interaction with CREBBP.|||Disordered|||Endothelial PAS domain-containing protein 1|||Markedly decreases heterodimer formation with ARNT. Impairs heterodimer formation with ARNT; when associated with A-171.|||Markedly decreases heterodimer formation with ARNT. Impairs heterodimer formation with ARNT; when associated with D-192.|||NTAD|||PAC|||PAS 1|||PAS 2|||Phosphothreonine|||Polar residues|||Required for heterodimer formation with ARNT|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127420 http://togogenome.org/gene/10090:Gm14744 ^@ http://purl.uniprot.org/uniprot/B1AVU4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5002760001 http://togogenome.org/gene/10090:Ythdf1 ^@ http://purl.uniprot.org/uniprot/P59326 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Removed|||YTH|||YTH domain-containing family protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000223074 http://togogenome.org/gene/10090:Cracd ^@ http://purl.uniprot.org/uniprot/Q5PR69 ^@ 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|||Capping protein-inhibiting regulator of actin dynamics|||Disordered|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with actin-capping proteins ^@ http://purl.uniprot.org/annotation/PRO_0000342476|||http://purl.uniprot.org/annotation/VSP_061664 http://togogenome.org/gene/10090:Slc25a2 ^@ http://purl.uniprot.org/uniprot/Q99ML6 ^@ Region|||Repeat|||Transmembrane ^@ Repeat|||Transmembrane ^@ Helical|||Solcar ^@ http://togogenome.org/gene/10090:Lect2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0R8|||http://purl.uniprot.org/uniprot/O88803 ^@ 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 ^@ In isoform 2.|||Leukocyte cell-derived chemotaxin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000017365|||http://purl.uniprot.org/annotation/PRO_5006451989|||http://purl.uniprot.org/annotation/VSP_003051 http://togogenome.org/gene/10090:Gramd2b ^@ http://purl.uniprot.org/uniprot/Q9D2W5 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||GRAM|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Dnmt1 ^@ http://purl.uniprot.org/uniprot/J3QNW0|||http://purl.uniprot.org/uniprot/P13864|||http://purl.uniprot.org/uniprot/Q3UHZ3|||http://purl.uniprot.org/uniprot/Q3UWN4|||http://purl.uniprot.org/uniprot/Q7TSJ0 ^@ 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 Conflict|||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 Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ 1|||2|||3|||4|||5|||6|||7 X 2 AA tandem repeats of K-G|||7; approximate|||Abolishes interaction with PCNA. No effect on activity.|||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|||In isoform 2.|||Interaction with DMAP1|||Interaction with DNMT3A|||Interaction with DNMT3B|||Interaction with HDAC1|||Interaction with PCNA|||Interaction with the PRC2/EED-EZH2 complex|||Loss of activity.|||Loss of activity. No effect on DNA-binding capacity.|||N6,N6-dimethyllysine; by EHMT2|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; by SETD7|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CK1|||Phosphothreonine|||Polar residues|||SAM-dependent MTase C5-type|||Slightly reduces activity. ^@ http://purl.uniprot.org/annotation/PRO_0000088035|||http://purl.uniprot.org/annotation/VSP_005619 http://togogenome.org/gene/10090:Pak6 ^@ http://purl.uniprot.org/uniprot/Q3ULB5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ CRIB|||Disordered|||Linker|||Phosphoserine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PAK 6 ^@ http://purl.uniprot.org/annotation/PRO_0000278117 http://togogenome.org/gene/10090:Tssk2 ^@ http://purl.uniprot.org/uniprot/O54863 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Protein kinase|||Proton acceptor|||Testis-specific serine/threonine-protein kinase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000086769 http://togogenome.org/gene/10090:Nags ^@ http://purl.uniprot.org/uniprot/Q8R4H7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Amino-acid kinase domain (AAK)|||Disordered|||In isoform 2.|||Mitochondrion|||N-acetylglutamate synthase conserved domain form|||N-acetylglutamate synthase long form|||N-acetylglutamate synthase short form|||N-acetyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000041933|||http://purl.uniprot.org/annotation/PRO_0000041934|||http://purl.uniprot.org/annotation/PRO_0000041935|||http://purl.uniprot.org/annotation/VSP_015620 http://togogenome.org/gene/10090:Zfp13 ^@ http://purl.uniprot.org/uniprot/P10754 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Propeptide|||Region|||Sequence Conflict|||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|||Removed in mature form|||Transcriptional repressor Rhit ^@ http://purl.uniprot.org/annotation/PRO_0000047284|||http://purl.uniprot.org/annotation/PRO_0000458417|||http://purl.uniprot.org/annotation/VSP_016902 http://togogenome.org/gene/10090:Gpr75 ^@ http://purl.uniprot.org/uniprot/Q059L0|||http://purl.uniprot.org/uniprot/Q6X632 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||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-linked (GlcNAc...) asparagine|||Polar residues|||Probable G-protein coupled receptor 75 ^@ http://purl.uniprot.org/annotation/PRO_0000069584 http://togogenome.org/gene/10090:Cpn1 ^@ http://purl.uniprot.org/uniprot/Q9JJN5 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Carboxypeptidase N catalytic chain|||Catalytic|||Disordered|||O-linked (GalNAc...) threonine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000042578 http://togogenome.org/gene/10090:Gp1ba ^@ http://purl.uniprot.org/uniprot/A2CFB8|||http://purl.uniprot.org/uniprot/O35930 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cleavage; by ADAM17|||Cytoplasmic|||Disordered|||Extracellular|||Glycocalicin|||Helical|||Interchain (with C-147 in GP1BB)|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||LRRNT|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Platelet glycoprotein Ib alpha chain|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000271749|||http://purl.uniprot.org/annotation/PRO_0000446254|||http://purl.uniprot.org/annotation/PRO_5015086050 http://togogenome.org/gene/10090:Klf9 ^@ http://purl.uniprot.org/uniprot/Q8CEC4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Nsun7 ^@ http://purl.uniprot.org/uniprot/A0A0J9YV71|||http://purl.uniprot.org/uniprot/E9QPI2|||http://purl.uniprot.org/uniprot/Q14AW5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Polar residues|||Putative methyltransferase NSUN7|||SAM-dependent MTase RsmB/NOP-type ^@ http://purl.uniprot.org/annotation/PRO_0000289240|||http://purl.uniprot.org/annotation/VSP_025982|||http://purl.uniprot.org/annotation/VSP_025983|||http://purl.uniprot.org/annotation/VSP_025984|||http://purl.uniprot.org/annotation/VSP_025985 http://togogenome.org/gene/10090:Dhx29 ^@ http://purl.uniprot.org/uniprot/Q6PGC1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ 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_0000245536 http://togogenome.org/gene/10090:Fblim1 ^@ http://purl.uniprot.org/uniprot/Q71FD7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||FERMT2-binding|||Filamin-binding|||Filamin-binding LIM protein 1|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000075733 http://togogenome.org/gene/10090:Ngp ^@ http://purl.uniprot.org/uniprot/O08692 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Neutrophilic granule protein ^@ http://purl.uniprot.org/annotation/PRO_0000432423 http://togogenome.org/gene/10090:Mfap3l ^@ http://purl.uniprot.org/uniprot/Q9D3X9 ^@ 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.|||Microfibrillar-associated protein 3-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014870|||http://purl.uniprot.org/annotation/VSP_014096 http://togogenome.org/gene/10090:Cck ^@ http://purl.uniprot.org/uniprot/P09240|||http://purl.uniprot.org/uniprot/Q8R041 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Cholecystokinin|||Cholecystokinin-12|||Cholecystokinin-33|||Cholecystokinin-8|||Gastrin/cholecystokinin peptide hormone|||Phenylalanine amide|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000010552|||http://purl.uniprot.org/annotation/PRO_0000010553|||http://purl.uniprot.org/annotation/PRO_0000010554|||http://purl.uniprot.org/annotation/PRO_0000010555|||http://purl.uniprot.org/annotation/PRO_0000010556|||http://purl.uniprot.org/annotation/PRO_0000010557|||http://purl.uniprot.org/annotation/PRO_5015099307 http://togogenome.org/gene/10090:4930583I09Rik ^@ http://purl.uniprot.org/uniprot/Q9D2E3 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Npepps ^@ http://purl.uniprot.org/uniprot/Q11011 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Site ^@ 3'-nitrotyrosine|||Nuclear localization signal|||Proton acceptor|||Puromycin-sensitive aminopeptidase|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000095117 http://togogenome.org/gene/10090:Tmsb15b1 ^@ http://purl.uniprot.org/uniprot/A2AF33 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Tmem201 ^@ http://purl.uniprot.org/uniprot/A2A8U2|||http://purl.uniprot.org/uniprot/Q3TXY3|||http://purl.uniprot.org/uniprot/Q8C397|||http://purl.uniprot.org/uniprot/Q8C9U2 ^@ 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|||Disordered|||Helical|||Ima1 N-terminal|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Nuclear|||Perinuclear space|||Phosphoserine|||Polar residues|||Transmembrane protein 201|||Transmembrane protein 201 C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000317199|||http://purl.uniprot.org/annotation/VSP_030917|||http://purl.uniprot.org/annotation/VSP_030918|||http://purl.uniprot.org/annotation/VSP_030919|||http://purl.uniprot.org/annotation/VSP_030920 http://togogenome.org/gene/10090:Prpf4 ^@ http://purl.uniprot.org/uniprot/Q059T9|||http://purl.uniprot.org/uniprot/Q9DAW6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Modified Residue|||Repeat ^@ N6-acetyllysine|||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_0000051150 http://togogenome.org/gene/10090:Ankrd36 ^@ http://purl.uniprot.org/uniprot/D3Z4K0 ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ ANK|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Lipo4 ^@ http://purl.uniprot.org/uniprot/F6RR30 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Signal Peptide ^@ Charge relay system|||Lipase|||Nucleophile|||Partial AB-hydrolase lipase|||Serine aminopeptidase S33 ^@ http://purl.uniprot.org/annotation/PRO_5019849072 http://togogenome.org/gene/10090:Srsf2 ^@ http://purl.uniprot.org/uniprot/Q62093 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||RRM|||Removed|||Serine/arginine-rich splicing factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081919 http://togogenome.org/gene/10090:Urad ^@ http://purl.uniprot.org/uniprot/B9EK13|||http://purl.uniprot.org/uniprot/Q283N4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent ^@ 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase|||Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000315241 http://togogenome.org/gene/10090:Bmp8b ^@ http://purl.uniprot.org/uniprot/P55105 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Bone morphogenetic protein 8B|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033886|||http://purl.uniprot.org/annotation/PRO_0000033887 http://togogenome.org/gene/10090:Sval2 ^@ http://purl.uniprot.org/uniprot/Q99N75 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Signal Peptide ^@ Prolactin-induced protein|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_5015099615 http://togogenome.org/gene/10090:Umodl1 ^@ http://purl.uniprot.org/uniprot/Q5DID3 ^@ 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|||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.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||SEA 1|||SEA 2|||Uromodulin-like 1|||WAP|||ZP ^@ http://purl.uniprot.org/annotation/PRO_0000228128|||http://purl.uniprot.org/annotation/VSP_017660|||http://purl.uniprot.org/annotation/VSP_017661 http://togogenome.org/gene/10090:Septin8 ^@ http://purl.uniprot.org/uniprot/B1AQY9|||http://purl.uniprot.org/uniprot/B1AQZ0|||http://purl.uniprot.org/uniprot/B7ZC46|||http://purl.uniprot.org/uniprot/Q8CHH9 ^@ 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 ^@ Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||Septin-8|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173534|||http://purl.uniprot.org/annotation/VSP_009645 http://togogenome.org/gene/10090:Fkbpl ^@ http://purl.uniprot.org/uniprot/O35450 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||FK506-binding protein-like|||Phosphothreonine|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000289879 http://togogenome.org/gene/10090:Spg7 ^@ http://purl.uniprot.org/uniprot/Q3ULF4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ 3'-nitrotyrosine|||Absence of proteolytic activity. No loss of its processing into the mature form.|||Basic and acidic residues|||Disordered|||Helical; Name=1|||Helical; Name=2|||Interaction with PPIF|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Paraplegin|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000442306|||http://purl.uniprot.org/annotation/PRO_0000442307 http://togogenome.org/gene/10090:Lce1a2 ^@ http://purl.uniprot.org/uniprot/Q9D1K4 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Gpank1 ^@ http://purl.uniprot.org/uniprot/Q61858|||http://purl.uniprot.org/uniprot/Q6PES3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||Disordered|||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_0000066973 http://togogenome.org/gene/10090:Dmap1 ^@ http://purl.uniprot.org/uniprot/Q9JI44 ^@ 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|||DNA methyltransferase 1-associated protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||SANT ^@ http://purl.uniprot.org/annotation/PRO_0000079936|||http://purl.uniprot.org/annotation/VSP_003850|||http://purl.uniprot.org/annotation/VSP_003851 http://togogenome.org/gene/10090:Plcl1 ^@ http://purl.uniprot.org/uniprot/Q3USB7 ^@ 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 ^@ Basic and acidic residues|||C2|||Decreased level of phosphorylation. Loss of phosphorylation; when associated with A-94.|||Decreased level of phosphorylation. Loss of phosphorylation; when associated with A-96.|||Disordered|||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|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by PKA|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000319415 http://togogenome.org/gene/10090:Mboat7 ^@ http://purl.uniprot.org/uniprot/Q8CHK3 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Lysophospholipid acyltransferase 7|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000317458 http://togogenome.org/gene/10090:Pgk1 ^@ http://purl.uniprot.org/uniprot/P09411 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ 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_0000145835 http://togogenome.org/gene/10090:Zfp267 ^@ http://purl.uniprot.org/uniprot/A0A0G2JEM5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Or1p1c ^@ http://purl.uniprot.org/uniprot/Q7TRX0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Galp ^@ http://purl.uniprot.org/uniprot/Q810H5 ^@ Chain|||Molecule Processing|||Natural Variation|||Propeptide|||Signal Peptide|||Splice Variant ^@ Chain|||Propeptide|||Signal Peptide|||Splice Variant ^@ Galanin-like peptide|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000316085|||http://purl.uniprot.org/annotation/PRO_0000316086|||http://purl.uniprot.org/annotation/VSP_030462 http://togogenome.org/gene/10090:Il3ra ^@ http://purl.uniprot.org/uniprot/P26952 ^@ Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Box 1 motif|||Cytoplasmic|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||In isoform 3.|||Interleukin-3 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Resistant to degradation.|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010884|||http://purl.uniprot.org/annotation/VSP_011265|||http://purl.uniprot.org/annotation/VSP_040623 http://togogenome.org/gene/10090:Fam133b ^@ http://purl.uniprot.org/uniprot/Q9CVI2 ^@ 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|||Protein FAM133B ^@ http://purl.uniprot.org/annotation/PRO_0000287617|||http://purl.uniprot.org/annotation/VSP_025572|||http://purl.uniprot.org/annotation/VSP_025573 http://togogenome.org/gene/10090:Pomgnt2 ^@ http://purl.uniprot.org/uniprot/Q8BW41 ^@ 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|||Fibronectin type-III|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000249015 http://togogenome.org/gene/10090:Defb35 ^@ http://purl.uniprot.org/uniprot/Q8R2I3 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 35 ^@ http://purl.uniprot.org/annotation/PRO_0000006947 http://togogenome.org/gene/10090:Or5k17 ^@ http://purl.uniprot.org/uniprot/Q8VGQ7 ^@ 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 5K17 ^@ http://purl.uniprot.org/annotation/PRO_0000269656 http://togogenome.org/gene/10090:Vmn2r17 ^@ http://purl.uniprot.org/uniprot/E9PYF5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245507 http://togogenome.org/gene/10090:Atic ^@ http://purl.uniprot.org/uniprot/Q9CWJ9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ AICAR formyltransferase|||Bifunctional purine biosynthesis protein ATIC|||IMP cyclohydrolase|||MGS-like|||N-acetylmethionine|||N6-acetyllysine|||Proton acceptor; for AICAR formyltransferase activity|||Proton donor/acceptor; for FAICAR cyclization activity|||Transition state stabilizer|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000192157 http://togogenome.org/gene/10090:Trim59 ^@ http://purl.uniprot.org/uniprot/Q922Y2 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ B box-type|||Helical|||RING-type|||Tripartite motif-containing protein 59 ^@ http://purl.uniprot.org/annotation/PRO_0000249680 http://togogenome.org/gene/10090:Bud23 ^@ http://purl.uniprot.org/uniprot/Q148S9|||http://purl.uniprot.org/uniprot/Q9CY21 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ 18S rRNA (guanine(1575)-N(7))-methyltransferase Bud23 C-terminal|||Basic and acidic residues|||Disordered|||Methyltransferase type 11|||Polar residues|||Probable 18S rRNA (guanine-N(7))-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000204451 http://togogenome.org/gene/10090:Or5b97 ^@ http://purl.uniprot.org/uniprot/Q8VFX3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cldn18 ^@ http://purl.uniprot.org/uniprot/P56857|||http://purl.uniprot.org/uniprot/Q8BZS5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Claudin-18|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform A1.2 and isoform A2.2.|||In isoform A2.1 and isoform A2.2.|||Phosphoserine|||Required for role in regulation of RANKL-induced osteoclast differentiation ^@ http://purl.uniprot.org/annotation/PRO_0000457666|||http://purl.uniprot.org/annotation/VSP_001103|||http://purl.uniprot.org/annotation/VSP_001104|||http://purl.uniprot.org/annotation/VSP_001105 http://togogenome.org/gene/10090:Myocos ^@ http://purl.uniprot.org/uniprot/Q3UWS6 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Myocilin opposite strand protein ^@ http://purl.uniprot.org/annotation/PRO_0000442230 http://togogenome.org/gene/10090:Carhsp1 ^@ http://purl.uniprot.org/uniprot/Q5M9P7|||http://purl.uniprot.org/uniprot/Q9CR86 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ CSD|||Calcium-regulated heat stable protein 1|||Disordered|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000100231 http://togogenome.org/gene/10090:H2ac23 ^@ http://purl.uniprot.org/uniprot/B2RVF0|||http://purl.uniprot.org/uniprot/C0HKE1|||http://purl.uniprot.org/uniprot/C0HKE2|||http://purl.uniprot.org/uniprot/C0HKE3|||http://purl.uniprot.org/uniprot/C0HKE4|||http://purl.uniprot.org/uniprot/C0HKE5|||http://purl.uniprot.org/uniprot/C0HKE6|||http://purl.uniprot.org/uniprot/C0HKE7|||http://purl.uniprot.org/uniprot/C0HKE8|||http://purl.uniprot.org/uniprot/C0HKE9 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Histone H2A type 1-C|||Histone H2A type 1-D|||Histone H2A type 1-E|||Histone H2A type 1-G|||Histone H2A type 1-I|||Histone H2A type 1-N|||Histone H2A type 1-O|||Histone H2A type 1-P|||Histone H2A/H2B/H3|||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_0000439715|||http://purl.uniprot.org/annotation/PRO_0000439716|||http://purl.uniprot.org/annotation/PRO_0000439717|||http://purl.uniprot.org/annotation/PRO_0000439718|||http://purl.uniprot.org/annotation/PRO_0000439719|||http://purl.uniprot.org/annotation/PRO_0000439720|||http://purl.uniprot.org/annotation/PRO_0000439721|||http://purl.uniprot.org/annotation/PRO_0000439722|||http://purl.uniprot.org/annotation/PRO_0000439723 http://togogenome.org/gene/10090:Ears2 ^@ http://purl.uniprot.org/uniprot/Q9CXJ1 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Transit Peptide ^@ 'HIGH' region|||'KMSKS' region|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Probable glutamate--tRNA ligase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000254562 http://togogenome.org/gene/10090:Maf ^@ http://purl.uniprot.org/uniprot/P54843 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes interaction with USF2.|||Basic motif|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Inhibition on transcriptional activation on CD13 proximal promoter in endothelial cells.|||Leucine-zipper|||No effect on transcriptional activation on CD13 proximal promoter. Increases liver specific transactivation on the IL-4 promoter.|||Represses ARE-mediated transcription|||Transcription factor Maf|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076492|||http://purl.uniprot.org/annotation/VSP_036408|||http://purl.uniprot.org/annotation/VSP_036409 http://togogenome.org/gene/10090:Rnf38 ^@ http://purl.uniprot.org/uniprot/Q3UH35|||http://purl.uniprot.org/uniprot/Q8BI21 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Zinc Finger ^@ Bipartite nuclear localization signal 1|||Bipartite nuclear localization signal 2|||Disordered|||E3 ubiquitin-protein ligase RNF38|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056079 http://togogenome.org/gene/10090:Or4a79 ^@ http://purl.uniprot.org/uniprot/Q7TQZ2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ndufs5 ^@ http://purl.uniprot.org/uniprot/Q99LY9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Region|||Strand ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000118787 http://togogenome.org/gene/10090:Il22ra1 ^@ http://purl.uniprot.org/uniprot/Q3TS18|||http://purl.uniprot.org/uniprot/Q80XZ4 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes phosphorylation by GSK3B; reduces stability of the protein.|||Cytoplasmic|||Degradation-resistant mutant.|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Interleukin-22 receptor subunit alpha-1|||N-linked (GlcNAc...) asparagine|||No effect on protein degradation.|||Phosphoserine; by GSK3-beta ^@ http://purl.uniprot.org/annotation/PRO_0000324321 http://togogenome.org/gene/10090:Ngdn ^@ http://purl.uniprot.org/uniprot/Q9DB96 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic residues|||Disordered|||N-acetylalanine|||Necessary for interaction with EIF4E|||Neuroguidin|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000114332 http://togogenome.org/gene/10090:Usp34 ^@ http://purl.uniprot.org/uniprot/Q6ZQ93 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 34 ^@ http://purl.uniprot.org/annotation/PRO_0000249520|||http://purl.uniprot.org/annotation/VSP_020464|||http://purl.uniprot.org/annotation/VSP_020465|||http://purl.uniprot.org/annotation/VSP_035641|||http://purl.uniprot.org/annotation/VSP_035642 http://togogenome.org/gene/10090:Cacybp ^@ http://purl.uniprot.org/uniprot/Q9CXW3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Turn ^@ Basic and acidic residues|||CS|||Calcyclin-binding protein|||Disordered|||Interaction with S100A6|||Interaction with SIAH1|||Interaction with SKP1|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed|||SGS ^@ http://purl.uniprot.org/annotation/PRO_0000185390 http://togogenome.org/gene/10090:Sla ^@ http://purl.uniprot.org/uniprot/A0A0R4J247|||http://purl.uniprot.org/uniprot/Q4FJX0|||http://purl.uniprot.org/uniprot/Q60898 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes localization to endosomes. Strongly affects inhibitory function. Abolishes inhibitory function; when associated with L-73.|||Abolishes myristoylation and localization to endosomes.|||Disordered|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Removed|||SH2|||SH3|||SLA C-terminal|||Slightly affects inhibitory function. Abolishes inhibitory function; when associated with E-111.|||Src-like-adapter ^@ http://purl.uniprot.org/annotation/PRO_0000071947|||http://purl.uniprot.org/annotation/VSP_007239 http://togogenome.org/gene/10090:2510002D24Rik ^@ http://purl.uniprot.org/uniprot/Q3U595 ^@ Chain|||Molecule Processing ^@ Chain ^@ UPF0545 protein C22orf39 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000326131 http://togogenome.org/gene/10090:Kcnj15 ^@ http://purl.uniprot.org/uniprot/O88932|||http://purl.uniprot.org/uniprot/Q3TNE6|||http://purl.uniprot.org/uniprot/Q53Z04 ^@ Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||INTRAMEM|||Motif|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ ATP-sensitive inward rectifier potassium channel 15|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Inward rectifier potassium channel C-terminal|||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_0000154973 http://togogenome.org/gene/10090:Fkbp15 ^@ http://purl.uniprot.org/uniprot/Q6P9Q6 ^@ 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|||FK506-binding protein 15|||Important for function in growth cone organization|||In isoform B.|||N-acetylmethionine|||N6-acetyllysine|||PPIase FKBP-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000299557|||http://purl.uniprot.org/annotation/VSP_027759 http://togogenome.org/gene/10090:Rims3 ^@ http://purl.uniprot.org/uniprot/Q14BY7|||http://purl.uniprot.org/uniprot/Q80U57 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ C2|||Disordered|||Phosphoserine|||Polar residues|||Regulating synaptic membrane exocytosis protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000190205 http://togogenome.org/gene/10090:Gm5945 ^@ http://purl.uniprot.org/uniprot/A0A571BDD5 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:H2-Q4 ^@ http://purl.uniprot.org/uniprot/Q0WXH7|||http://purl.uniprot.org/uniprot/Q8HWB2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide ^@ Disordered|||Ig-like|||MHC class I-like antigen recognition-like ^@ http://purl.uniprot.org/annotation/PRO_5015099160 http://togogenome.org/gene/10090:Slc16a6 ^@ http://purl.uniprot.org/uniprot/B1AT66 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Monocarboxylate transporter 7|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000416126|||http://purl.uniprot.org/annotation/VSP_042512 http://togogenome.org/gene/10090:Rpl37 ^@ http://purl.uniprot.org/uniprot/Q9D823 ^@ 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_0000139706 http://togogenome.org/gene/10090:Pde4a ^@ http://purl.uniprot.org/uniprot/B2RTL2|||http://purl.uniprot.org/uniprot/O89084|||http://purl.uniprot.org/uniprot/Q3TUD0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ 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.|||PDEase|||Phosphoserine|||Polar residues|||Proton donor|||cAMP-specific 3',5'-cyclic phosphodiesterase 4A ^@ http://purl.uniprot.org/annotation/PRO_0000198807|||http://purl.uniprot.org/annotation/VSP_004562|||http://purl.uniprot.org/annotation/VSP_004563|||http://purl.uniprot.org/annotation/VSP_004564 http://togogenome.org/gene/10090:Ppp2r2c ^@ http://purl.uniprot.org/uniprot/Q8BG02 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ 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_0000071430 http://togogenome.org/gene/10090:Rtn4rl1 ^@ http://purl.uniprot.org/uniprot/Q8K0S5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Propeptide|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||GPI-anchor amidated serine|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRRCT|||LRRNT|||Polar residues|||Removed in mature form|||Reticulon-4 receptor-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000046044|||http://purl.uniprot.org/annotation/PRO_0000046045 http://togogenome.org/gene/10090:Mageb6b1 ^@ http://purl.uniprot.org/uniprot/A2AHM1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Or13n4 ^@ http://purl.uniprot.org/uniprot/Q920Z2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or6c213 ^@ http://purl.uniprot.org/uniprot/Q8VFI2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dnai2 ^@ http://purl.uniprot.org/uniprot/A2AC93 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Region|||Repeat|||Splice Variant ^@ 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_0000365816|||http://purl.uniprot.org/annotation/VSP_036542 http://togogenome.org/gene/10090:Coq5 ^@ http://purl.uniprot.org/uniprot/Q9CXI0 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Sequence Conflict|||Transit Peptide ^@ 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000228629 http://togogenome.org/gene/10090:Steap2 ^@ http://purl.uniprot.org/uniprot/B2RX33|||http://purl.uniprot.org/uniprot/D3YUM6|||http://purl.uniprot.org/uniprot/Q8BWB6 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transmembrane ^@ Ferric oxidoreductase|||Helical|||Metalloreductase STEAP2|||Phosphoserine|||Pyrroline-5-carboxylate reductase catalytic N-terminal|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000191698 http://togogenome.org/gene/10090:Asic2 ^@ http://purl.uniprot.org/uniprot/B2RRQ1|||http://purl.uniprot.org/uniprot/Q925H0 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acid-sensing ion channel 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000181291|||http://purl.uniprot.org/annotation/VSP_015592|||http://purl.uniprot.org/annotation/VSP_015593 http://togogenome.org/gene/10090:Prmt9 ^@ http://purl.uniprot.org/uniprot/F8WIU7|||http://purl.uniprot.org/uniprot/Q3U3W5 ^@ 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.|||Protein arginine N-methyltransferase 9|||SAM-dependent MTase PRMT-type 1|||SAM-dependent MTase PRMT-type 2|||TPR|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000325930|||http://purl.uniprot.org/annotation/VSP_032488|||http://purl.uniprot.org/annotation/VSP_032489 http://togogenome.org/gene/10090:Mettl7a1 ^@ http://purl.uniprot.org/uniprot/Q8C6B0|||http://purl.uniprot.org/uniprot/Q9D7S5 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Methyltransferase type 11|||Polar residues ^@ http://togogenome.org/gene/10090:Rgn ^@ http://purl.uniprot.org/uniprot/Q64374 ^@ 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 ^@ N6-succinyllysine|||Proton donor/acceptor|||Regucalcin ^@ http://purl.uniprot.org/annotation/PRO_0000173047 http://togogenome.org/gene/10090:Or8g27 ^@ http://purl.uniprot.org/uniprot/Q9EQ91 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wfdc8 ^@ http://purl.uniprot.org/uniprot/A2A5H1|||http://purl.uniprot.org/uniprot/Q4KUS1|||http://purl.uniprot.org/uniprot/Q4KXB5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Transmembrane ^@ BPTI/Kunitz inhibitor|||Helical|||WAP|||WAP 1|||WAP 2|||WAP 3|||WAP four-disulfide core domain protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000307717 http://togogenome.org/gene/10090:Bhlha9 ^@ http://purl.uniprot.org/uniprot/Q5RJB0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Class A basic helix-loop-helix protein 9|||Disordered|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000341378 http://togogenome.org/gene/10090:Fam205a2 ^@ http://purl.uniprot.org/uniprot/C0HKD1|||http://purl.uniprot.org/uniprot/C0HKD2|||http://purl.uniprot.org/uniprot/C0HKD3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Protein SPATA31F1-2|||Protein SPATA31F1-3|||Protein SPATA31F1-4 ^@ http://purl.uniprot.org/annotation/PRO_0000341305|||http://purl.uniprot.org/annotation/PRO_0000444751|||http://purl.uniprot.org/annotation/PRO_0000444752 http://togogenome.org/gene/10090:Ccdc149 ^@ http://purl.uniprot.org/uniprot/F6V035 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Higd2a ^@ http://purl.uniprot.org/uniprot/Q9CQJ1 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Transmembrane ^@ HIG1|||HIG1 domain family member 2A|||Helical|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000215778 http://togogenome.org/gene/10090:Nfyc ^@ http://purl.uniprot.org/uniprot/P70353|||http://purl.uniprot.org/uniprot/Q7TPS7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Histone H2A/H2B/H3|||Nuclear transcription factor Y subunit gamma ^@ http://purl.uniprot.org/annotation/PRO_0000218247 http://togogenome.org/gene/10090:Hpgds ^@ http://purl.uniprot.org/uniprot/Q9JHF7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ GST C-terminal|||GST N-terminal|||Hematopoietic prostaglandin D synthase ^@ http://purl.uniprot.org/annotation/PRO_0000185935 http://togogenome.org/gene/10090:Slitrk2 ^@ http://purl.uniprot.org/uniprot/Q14DT0|||http://purl.uniprot.org/uniprot/Q810C0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes interaction with PTPRD. Abolishes synapse assembly.|||Abolishes interaction with PTPRD. Significantly reduces synapse assembly.|||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|||LRRCT 1|||LRRCT 2|||LRRNT|||N-linked (GlcNAc...) asparagine|||No effect on interaction with PTPRD. No effect on synapse assembly.|||Phosphotyrosine|||Polar residues|||Required for interaction with PTPRD|||SLIT and NTRK-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000032676|||http://purl.uniprot.org/annotation/PRO_5014306936 http://togogenome.org/gene/10090:Naglu ^@ http://purl.uniprot.org/uniprot/O88325 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Alpha-N-acetylglucosaminidase C-terminal|||Alpha-N-acetylglucosaminidase N-terminal|||Alpha-N-acetylglucosaminidase tim-barrel ^@ http://purl.uniprot.org/annotation/PRO_5015096837 http://togogenome.org/gene/10090:Ccdc30 ^@ http://purl.uniprot.org/uniprot/A0A571BEH3|||http://purl.uniprot.org/uniprot/A0A571BGB9|||http://purl.uniprot.org/uniprot/A8WHU1|||http://purl.uniprot.org/uniprot/Q8BVF4|||http://purl.uniprot.org/uniprot/Q8BX48 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 30|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000336046|||http://purl.uniprot.org/annotation/VSP_033798|||http://purl.uniprot.org/annotation/VSP_033799|||http://purl.uniprot.org/annotation/VSP_033800|||http://purl.uniprot.org/annotation/VSP_033801|||http://purl.uniprot.org/annotation/VSP_033802 http://togogenome.org/gene/10090:Nr1i3 ^@ http://purl.uniprot.org/uniprot/O35627|||http://purl.uniprot.org/uniprot/Q5FW96 ^@ Chain|||DNA Binding|||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|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Diminished binding of coactivator NCOA2 in the presence of TCPOBOP.|||Dramatic increase in binding NCOA2. Little effect on binding of coactivator NCOA2 in the presence of TCPOBOP.|||Important for TCPOBOP recognition|||In isoform CAR2.|||NR C4-type|||NR LBD|||No effect on binding of coactivator NCOA2 in the presence of TCPOBOP.|||Nuclear receptor|||Nuclear receptor subfamily 1 group I member 3|||Phosphothreonine; by PKC ^@ http://purl.uniprot.org/annotation/PRO_0000053554|||http://purl.uniprot.org/annotation/VSP_003671|||http://purl.uniprot.org/annotation/VSP_003672 http://togogenome.org/gene/10090:9330159F19Rik ^@ http://purl.uniprot.org/uniprot/D3Z623 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF4482|||Disordered ^@ http://togogenome.org/gene/10090:P2ry14 ^@ http://purl.uniprot.org/uniprot/A0A0G2JEW9|||http://purl.uniprot.org/uniprot/Q544F4|||http://purl.uniprot.org/uniprot/Q9ESG6 ^@ 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|||P2Y purinoceptor 14 ^@ http://purl.uniprot.org/annotation/PRO_0000070045 http://togogenome.org/gene/10090:Zfp943 ^@ http://purl.uniprot.org/uniprot/Q6NZP4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Tafazzin ^@ http://purl.uniprot.org/uniprot/H3BK99|||http://purl.uniprot.org/uniprot/I7HJS2|||http://purl.uniprot.org/uniprot/Q91WF0 ^@ Chain|||Domain Extent|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||INTRAMEM|||Motif|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ HXXXXD motif|||Helical|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial targeting sequence|||Phospholipid/glycerol acyltransferase|||Tafazzin ^@ http://purl.uniprot.org/annotation/PRO_0000452721|||http://purl.uniprot.org/annotation/VSP_061044|||http://purl.uniprot.org/annotation/VSP_061045 http://togogenome.org/gene/10090:Slc7a11 ^@ http://purl.uniprot.org/uniprot/Q542C8|||http://purl.uniprot.org/uniprot/Q9WTR6 ^@ Binding Site|||Chain|||Disulfide Bond|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||INTRAMEM|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cystine/glutamate transporter|||Cytoplasmic|||Extracellular|||Helical|||Interchain (with C-103 in SLC3A2)|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000054280 http://togogenome.org/gene/10090:Vmn2r121 ^@ http://purl.uniprot.org/uniprot/A2BE32 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5002642201 http://togogenome.org/gene/10090:Col6a6 ^@ http://purl.uniprot.org/uniprot/Q8C6K9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||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_5000253013|||http://purl.uniprot.org/annotation/VSP_033916|||http://purl.uniprot.org/annotation/VSP_033917 http://togogenome.org/gene/10090:Metrnl ^@ http://purl.uniprot.org/uniprot/Q8VE43 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Meteorin-like protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000289105|||http://purl.uniprot.org/annotation/VSP_025897 http://togogenome.org/gene/10090:Arf6 ^@ http://purl.uniprot.org/uniprot/P62331 ^@ 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|||Inactive GDP-bound form which does not bind TJAP1.|||Loss of activity; delays formation of epithelial polarity.|||Loss of interaction with KIF23, GGA1, SPAG9 and RAB11FIP4.|||N-myristoyl glycine|||N6-myristoyl lysine|||Probable constitutively active mutant that prevents EHD1 localization to endosome membranes. No effect on interaction with TJAP1.|||Removed|||Slightly impaired interaction with KIF23. Abolishes interaction with GGA1, SPAG9 and RAB11FIP4. ^@ http://purl.uniprot.org/annotation/PRO_0000207401 http://togogenome.org/gene/10090:Accs ^@ http://purl.uniprot.org/uniprot/A2AIG8 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Region|||Splice Variant ^@ 1-aminocyclopropane-1-carboxylate synthase-like protein 1|||Disordered|||In isoform 2.|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_0000318072|||http://purl.uniprot.org/annotation/VSP_052669 http://togogenome.org/gene/10090:Aqp12 ^@ http://purl.uniprot.org/uniprot/Q3V2I1|||http://purl.uniprot.org/uniprot/Q8CHJ2 ^@ Chain|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Motif|||Region|||Signal Peptide|||Transmembrane ^@ Aquaporin|||Aquaporin-12|||Disordered|||Helical|||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_0000063972|||http://purl.uniprot.org/annotation/PRO_5014309245 http://togogenome.org/gene/10090:Krt222 ^@ http://purl.uniprot.org/uniprot/Q8CCX5 ^@ 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_0000344216|||http://purl.uniprot.org/annotation/VSP_034745 http://togogenome.org/gene/10090:Gas2l1 ^@ http://purl.uniprot.org/uniprot/Q8JZP9|||http://purl.uniprot.org/uniprot/Q9D2H3 ^@ 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|||Calponin-homology (CH)|||Disordered|||GAR|||GAS2-like protein 1|||In isoform 2.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000190443|||http://purl.uniprot.org/annotation/VSP_015496 http://togogenome.org/gene/10090:Rab3gap1 ^@ http://purl.uniprot.org/uniprot/Q80UJ7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Rab3 GTPase-activating protein catalytic subunit ^@ http://purl.uniprot.org/annotation/PRO_0000191656 http://togogenome.org/gene/10090:Avp ^@ http://purl.uniprot.org/uniprot/P35455|||http://purl.uniprot.org/uniprot/Q3UUQ5 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Peptide|||Signal Peptide|||Site ^@ Arg-vasopressin|||Copeptin|||Glycine amide|||Important for agonist activity on V1aR/AVPR1A|||N-linked (GlcNAc...) asparagine|||Neurophysin 2|||Vasopressin-neurophysin 2-copeptin ^@ http://purl.uniprot.org/annotation/PRO_0000020518|||http://purl.uniprot.org/annotation/PRO_0000020519|||http://purl.uniprot.org/annotation/PRO_0000020520|||http://purl.uniprot.org/annotation/PRO_5014309236 http://togogenome.org/gene/10090:Gm4736 ^@ http://purl.uniprot.org/uniprot/Q61888 ^@ 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_5004266708 http://togogenome.org/gene/10090:St8sia6 ^@ http://purl.uniprot.org/uniprot/Q148N5|||http://purl.uniprot.org/uniprot/Q8K4T1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||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_0000149300|||http://purl.uniprot.org/annotation/PRO_5014306903 http://togogenome.org/gene/10090:Slc46a2 ^@ http://purl.uniprot.org/uniprot/Q8CA03 ^@ 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|||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|||Solute carrier family 46 member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000065660 http://togogenome.org/gene/10090:Megf9 ^@ http://purl.uniprot.org/uniprot/Q0VGR4|||http://purl.uniprot.org/uniprot/Q8BH27 ^@ 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|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000007527|||http://purl.uniprot.org/annotation/PRO_5014306873 http://togogenome.org/gene/10090:Tafa3 ^@ http://purl.uniprot.org/uniprot/Q7TPG6 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Chemokine-like protein TAFA-3 ^@ http://purl.uniprot.org/annotation/PRO_0000042727 http://togogenome.org/gene/10090:Trim26 ^@ http://purl.uniprot.org/uniprot/Q3UFX3|||http://purl.uniprot.org/uniprot/Q99PN3 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Acidic residues|||B box-type|||B30.2/SPRY|||Disordered|||In isoform Beta.|||RING-type|||Tripartite motif-containing protein 26 ^@ http://purl.uniprot.org/annotation/PRO_0000056236|||http://purl.uniprot.org/annotation/VSP_010812|||http://purl.uniprot.org/annotation/VSP_010813 http://togogenome.org/gene/10090:Meig1 ^@ http://purl.uniprot.org/uniprot/Q61845 ^@ Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Strand|||Turn ^@ Meiosis-expressed gene 1 protein ^@ http://purl.uniprot.org/annotation/PRO_0000096404 http://togogenome.org/gene/10090:Cdkn3 ^@ http://purl.uniprot.org/uniprot/Q810P3 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Region ^@ Cyclin-dependent kinase inhibitor 3|||Disordered|||Interaction with CDK2|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000396637 http://togogenome.org/gene/10090:Sass6 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFC9|||http://purl.uniprot.org/uniprot/Q80UK7 ^@ 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.|||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_0000189973|||http://purl.uniprot.org/annotation/VSP_013318|||http://purl.uniprot.org/annotation/VSP_013319 http://togogenome.org/gene/10090:Rexo1 ^@ http://purl.uniprot.org/uniprot/Q7TT28 ^@ 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|||Exonuclease|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RNA exonuclease 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000239233|||http://purl.uniprot.org/annotation/VSP_019121|||http://purl.uniprot.org/annotation/VSP_019122|||http://purl.uniprot.org/annotation/VSP_019123 http://togogenome.org/gene/10090:Gad2 ^@ http://purl.uniprot.org/uniprot/P48320|||http://purl.uniprot.org/uniprot/Q548L4 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glutamate decarboxylase 2|||N6-(pyridoxal phosphate)lysine|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000146969 http://togogenome.org/gene/10090:Ctxn3 ^@ http://purl.uniprot.org/uniprot/Q8BXZ0 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Cortexin-3|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000284514 http://togogenome.org/gene/10090:Filip1 ^@ http://purl.uniprot.org/uniprot/Q9CS72 ^@ 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|||Filamin-A-interacting protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000234541 http://togogenome.org/gene/10090:Cyp4v3 ^@ http://purl.uniprot.org/uniprot/B2RSR0|||http://purl.uniprot.org/uniprot/Q9DBW0 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Cytochrome P450 4V2|||Helical|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000051861 http://togogenome.org/gene/10090:Or8k38 ^@ http://purl.uniprot.org/uniprot/Q7TR64 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r241 ^@ http://purl.uniprot.org/uniprot/K9J7G2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:CYTB ^@ http://purl.uniprot.org/uniprot/P00158|||http://purl.uniprot.org/uniprot/Q7JCZ3 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Strand|||Transmembrane|||Turn ^@ Cytochrome b|||Cytochrome b/b6 C-terminal region profile|||Cytochrome b/b6 N-terminal region profile|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000061211 http://togogenome.org/gene/10090:Akt2 ^@ http://purl.uniprot.org/uniprot/Q3TY95|||http://purl.uniprot.org/uniprot/Q60823|||http://purl.uniprot.org/uniprot/Q8CE74 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue ^@ AGC-kinase C-terminal|||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_0000085609 http://togogenome.org/gene/10090:Chd1 ^@ http://purl.uniprot.org/uniprot/P40201 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||3 X 5 AA repeats of H-S-D-H-R|||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|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080225 http://togogenome.org/gene/10090:Pitpnc1 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ88|||http://purl.uniprot.org/uniprot/Q8K4R4 ^@ 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|||Cytoplasmic phosphatidylinositol transfer protein 1|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000287531|||http://purl.uniprot.org/annotation/VSP_025546|||http://purl.uniprot.org/annotation/VSP_025547|||http://purl.uniprot.org/annotation/VSP_025548|||http://purl.uniprot.org/annotation/VSP_025549|||http://purl.uniprot.org/annotation/VSP_025550|||http://purl.uniprot.org/annotation/VSP_025551 http://togogenome.org/gene/10090:Phox2b ^@ http://purl.uniprot.org/uniprot/O35690 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Paired mesoderm homeobox protein 2B ^@ http://purl.uniprot.org/annotation/PRO_0000049263 http://togogenome.org/gene/10090:Or4f58 ^@ http://purl.uniprot.org/uniprot/Q8VET0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ect2 ^@ http://purl.uniprot.org/uniprot/Q07139 ^@ Chain|||Crosslink|||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|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ BRCT 1|||BRCT 2|||DH|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Nuclear localization signal|||PH|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphothreonine; by PKC/PRKCI|||Protein ECT2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000080939|||http://purl.uniprot.org/annotation/VSP_041979|||http://purl.uniprot.org/annotation/VSP_041980|||http://purl.uniprot.org/annotation/VSP_041981 http://togogenome.org/gene/10090:Hoxc10 ^@ http://purl.uniprot.org/uniprot/P31257|||http://purl.uniprot.org/uniprot/Q8BZY5 ^@ 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_0000200191 http://togogenome.org/gene/10090:Tgfb1i1 ^@ http://purl.uniprot.org/uniprot/Q62219 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant ^@ Disordered|||In isoform 10.|||In isoform 2 and isoform 8.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 8.|||In isoform 7.|||In isoform 9.|||Increase in nuclear localization.|||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 interaction with PTPN12; when associated with G-366.|||Loss of interaction with PTPN12; when associated with G-369.|||Loss of localization to focal adhesion; when associated with A-369.|||Loss of localization to focal adhesion; when associated with A-372.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Reduced phosphorylation. Loss of phosphorylation; when associated with F-38.|||Reduced phosphorylation. Loss of phosphorylation; when associated with F-60.|||Transcription activation|||Transforming growth factor beta-1-induced transcript 1 protein ^@ http://purl.uniprot.org/annotation/PRO_0000291583|||http://purl.uniprot.org/annotation/VSP_026184|||http://purl.uniprot.org/annotation/VSP_026185|||http://purl.uniprot.org/annotation/VSP_026188|||http://purl.uniprot.org/annotation/VSP_026189|||http://purl.uniprot.org/annotation/VSP_026190|||http://purl.uniprot.org/annotation/VSP_026191|||http://purl.uniprot.org/annotation/VSP_026192|||http://purl.uniprot.org/annotation/VSP_026193|||http://purl.uniprot.org/annotation/VSP_026194|||http://purl.uniprot.org/annotation/VSP_026197|||http://purl.uniprot.org/annotation/VSP_039813|||http://purl.uniprot.org/annotation/VSP_039814 http://togogenome.org/gene/10090:Bcas3 ^@ http://purl.uniprot.org/uniprot/Q0VF62|||http://purl.uniprot.org/uniprot/Q8CCN5 ^@ 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 ^@ BCAS3|||BCAS3 microtubule associated cell migration factor|||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|||Polar residues|||Required for recruitment to preautophagosomal structure in response to mitophagy ^@ http://purl.uniprot.org/annotation/PRO_0000050884|||http://purl.uniprot.org/annotation/VSP_007861|||http://purl.uniprot.org/annotation/VSP_007862 http://togogenome.org/gene/10090:Tnfsf9 ^@ http://purl.uniprot.org/uniprot/P41274|||http://purl.uniprot.org/uniprot/Q3U1Z9 ^@ 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|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||TNF family profile|||Tumor necrosis factor ligand superfamily member 9 ^@ http://purl.uniprot.org/annotation/PRO_0000185502 http://togogenome.org/gene/10090:Or8b52 ^@ http://purl.uniprot.org/uniprot/Q7TRC3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kif3a ^@ http://purl.uniprot.org/uniprot/B1AQZ2|||http://purl.uniprot.org/uniprot/P28741|||http://purl.uniprot.org/uniprot/Q3TET1|||http://purl.uniprot.org/uniprot/Q3UF02|||http://purl.uniprot.org/uniprot/Q3UI47 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Globular|||Interaction with DCTN1|||Kinesin motor|||Kinesin-like protein KIF3A|||Phosphoserine|||Secreted protein ^@ http://purl.uniprot.org/annotation/PRO_0000125394|||http://purl.uniprot.org/annotation/PRO_5004230077 http://togogenome.org/gene/10090:Syne1 ^@ http://purl.uniprot.org/uniprot/A0A1L1STC6|||http://purl.uniprot.org/uniprot/Q0VGB8|||http://purl.uniprot.org/uniprot/Q6PI72|||http://purl.uniprot.org/uniprot/Q6ZWR1|||http://purl.uniprot.org/uniprot/Q6ZWR5|||http://purl.uniprot.org/uniprot/Q6ZWR6|||http://purl.uniprot.org/uniprot/Q7TQH5|||http://purl.uniprot.org/uniprot/Q80T95 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Actin-binding|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 5.|||Interchain (with C-577 in SUN2); alternate|||Interchain (with C-759 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_0000392209|||http://purl.uniprot.org/annotation/VSP_038791|||http://purl.uniprot.org/annotation/VSP_038792|||http://purl.uniprot.org/annotation/VSP_038793|||http://purl.uniprot.org/annotation/VSP_038794|||http://purl.uniprot.org/annotation/VSP_038795|||http://purl.uniprot.org/annotation/VSP_038796|||http://purl.uniprot.org/annotation/VSP_038797|||http://purl.uniprot.org/annotation/VSP_038798 http://togogenome.org/gene/10090:Cfap20 ^@ http://purl.uniprot.org/uniprot/Q8BTU1 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ Cilia- and flagella-associated protein 20|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000296399|||http://purl.uniprot.org/annotation/VSP_027219 http://togogenome.org/gene/10090:Antkmt ^@ http://purl.uniprot.org/uniprot/Q501J2 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Adenine nucleotide translocase lysine N-methyltransferase|||Helical|||Methyltransferase (MTase)|||N-terminal sequence (NTS)|||Pre-methyltransferase (preMT) ^@ http://purl.uniprot.org/annotation/PRO_0000263722 http://togogenome.org/gene/10090:Fcgbpl1 ^@ http://purl.uniprot.org/uniprot/E9PVG8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||VWFD ^@ http://purl.uniprot.org/annotation/PRO_5015090355 http://togogenome.org/gene/10090:Pipox ^@ http://purl.uniprot.org/uniprot/Q3UEJ8|||http://purl.uniprot.org/uniprot/Q9D826 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict ^@ FAD dependent oxidoreductase|||Microbody targeting signal|||N6-acetyllysine|||Peroxisomal sarcosine oxidase|||S-8alpha-FAD cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000213774 http://togogenome.org/gene/10090:Txlng ^@ http://purl.uniprot.org/uniprot/Q3TS51|||http://purl.uniprot.org/uniprot/Q3TT61|||http://purl.uniprot.org/uniprot/Q8BHN1 ^@ 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|||Gamma-taxilin|||In isoform 2 and isoform 3.|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000189427|||http://purl.uniprot.org/annotation/VSP_011835|||http://purl.uniprot.org/annotation/VSP_011836|||http://purl.uniprot.org/annotation/VSP_011837 http://togogenome.org/gene/10090:Sfr1 ^@ http://purl.uniprot.org/uniprot/Q8BP27 ^@ 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.|||Phosphoserine|||Polar residues|||Pro residues|||Swi5-dependent recombination DNA repair protein 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089806|||http://purl.uniprot.org/annotation/VSP_040905|||http://purl.uniprot.org/annotation/VSP_040906|||http://purl.uniprot.org/annotation/VSP_040907 http://togogenome.org/gene/10090:Hoxa6 ^@ http://purl.uniprot.org/uniprot/P09092|||http://purl.uniprot.org/uniprot/Q0VEU7 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-A6 ^@ http://purl.uniprot.org/annotation/PRO_0000200068 http://togogenome.org/gene/10090:Tnk1 ^@ http://purl.uniprot.org/uniprot/Q3TJU8|||http://purl.uniprot.org/uniprot/Q99ML2 ^@ 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 ^@ Active Site|||Binding Site|||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 autophosphorylation.|||Non-receptor tyrosine-protein kinase TNK1|||Phosphoserine|||Phosphothreonine|||Pro residues|||Protein kinase|||Proton acceptor|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000088174|||http://purl.uniprot.org/annotation/VSP_051664|||http://purl.uniprot.org/annotation/VSP_051665 http://togogenome.org/gene/10090:Rab39 ^@ http://purl.uniprot.org/uniprot/Q8BHD0 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif ^@ Cysteine methyl ester|||Effector region|||Ras-related protein Rab-39A|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121254 http://togogenome.org/gene/10090:Gm5795 ^@ http://purl.uniprot.org/uniprot/Q497R9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Rufy4 ^@ http://purl.uniprot.org/uniprot/Q3TYX8 ^@ 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|||RUN|||RUN and FYVE domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000284672|||http://purl.uniprot.org/annotation/VSP_035817 http://togogenome.org/gene/10090:Dcun1d3 ^@ http://purl.uniprot.org/uniprot/Q8K0V2 ^@ 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|||DCN1-like protein 3|||DCUN1|||Disordered|||N-myristoyl glycine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000320049 http://togogenome.org/gene/10090:Ulk3 ^@ http://purl.uniprot.org/uniprot/Q3U3Q1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||MIT 1|||MIT 2|||Phosphoserine|||Phosphoserine; by autocatalysis|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase ULK3 ^@ http://purl.uniprot.org/annotation/PRO_0000250151|||http://purl.uniprot.org/annotation/VSP_020602|||http://purl.uniprot.org/annotation/VSP_020603|||http://purl.uniprot.org/annotation/VSP_020604 http://togogenome.org/gene/10090:Or10ag52 ^@ http://purl.uniprot.org/uniprot/Q7TR54 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vti1b ^@ http://purl.uniprot.org/uniprot/Q91XH6 ^@ Coiled-Coil|||Domain Extent|||Region|||Transmembrane ^@ Coiled-Coil|||Domain Extent|||Transmembrane ^@ Helical|||T-SNARE coiled-coil homology ^@ http://togogenome.org/gene/10090:Csgalnact1 ^@ http://purl.uniprot.org/uniprot/Q8BJQ9 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chondroitin sulfate N-acetylgalactosaminyltransferase 1|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000189565 http://togogenome.org/gene/10090:Dvl2 ^@ http://purl.uniprot.org/uniprot/Q60838 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||DEP|||DIX|||Disordered|||Loss of oligomerization. Abolishes activation of Wnt signaling.|||Loss of oligomerization. Abolishes interaction with DIXDC1. Abolishes activation of Wnt signaling.|||Loss of oligomerization. Strongly reduced activation of Wnt signaling.|||PDZ|||Phosphoserine|||Polar residues|||Pro residues|||Reduces oligomerization. Abolishes interaction with DIXDC1. Reduces activation of Wnt signaling.|||Reduces oligomerization. Reduces activation of Wnt signaling.|||Reduces oligomerization. Strongly reduced activation of Wnt signaling.|||Segment polarity protein dishevelled homolog DVL-2|||Strongly reduced interaction with DIXDC1. ^@ http://purl.uniprot.org/annotation/PRO_0000145747 http://togogenome.org/gene/10090:Slc36a3 ^@ http://purl.uniprot.org/uniprot/Q811P0 ^@ 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|||Helical|||Polar residues|||Proton-coupled amino acid transporter 3 ^@ http://purl.uniprot.org/annotation/PRO_0000326205 http://togogenome.org/gene/10090:Gpr165 ^@ http://purl.uniprot.org/uniprot/Q3V3A3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ndufa10 ^@ http://purl.uniprot.org/uniprot/Q99LC3 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Leads to mitochondrial depolarization.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial|||Phosphomimetic mutant; able to rescue mitochondrial depolarization in a Pink1 mutant background.|||Phosphoserine; by PINK1 ^@ http://purl.uniprot.org/annotation/PRO_0000019989 http://togogenome.org/gene/10090:Arid4b ^@ http://purl.uniprot.org/uniprot/A2CG63 ^@ 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 ^@ ARID|||AT-rich interactive domain-containing protein 4B|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tudor-knot ^@ http://purl.uniprot.org/annotation/PRO_0000282864|||http://purl.uniprot.org/annotation/VSP_024236 http://togogenome.org/gene/10090:Drosha ^@ http://purl.uniprot.org/uniprot/Q5HZJ0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site ^@ Acidic residues|||Basic and acidic residues|||DRBM|||Disordered|||Important for activity|||Necessary for interaction with DGCR8 and pri-miRNA processing activity|||Phosphoserine|||Polar residues|||Pro residues|||RNase III 1|||RNase III 2|||Ribonuclease 3 ^@ http://purl.uniprot.org/annotation/PRO_0000384374 http://togogenome.org/gene/10090:Znfx1 ^@ http://purl.uniprot.org/uniprot/A2A5R6|||http://purl.uniprot.org/uniprot/Q8R151 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||NF-X1-type 1|||NF-X1-type 2|||NF-X1-type 3|||NF-X1-type 4|||NFX1-type zinc finger-containing protein 1|||Polar residues|||RZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000050796|||http://purl.uniprot.org/annotation/PRO_5002642420 http://togogenome.org/gene/10090:Krt1 ^@ http://purl.uniprot.org/uniprot/P04104 ^@ 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|||In EHK.|||Keratin, type II cytoskeletal 1|||Linker 1|||Linker 12|||N6,N6-dimethyllysine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063710 http://togogenome.org/gene/10090:Prok2 ^@ http://purl.uniprot.org/uniprot/G3X8R6|||http://purl.uniprot.org/uniprot/Q14AB2|||http://purl.uniprot.org/uniprot/Q9QXU7 ^@ 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.|||In isoform 3.|||Prokineticin|||Prokineticin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000025810|||http://purl.uniprot.org/annotation/PRO_5014306906|||http://purl.uniprot.org/annotation/PRO_5015091819|||http://purl.uniprot.org/annotation/VSP_005220|||http://purl.uniprot.org/annotation/VSP_005221 http://togogenome.org/gene/10090:Mmp27 ^@ http://purl.uniprot.org/uniprot/D3Z6I1 ^@ Active Site|||Binding Site|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Motif|||Region|||Repeat|||Site ^@ Active Site|||Binding Site|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Repeat ^@ Cysteine switch|||Hemopexin|||Peptidase metallopeptidase|||Phosphotyrosine; by PKDCC|||in inhibited form ^@ http://togogenome.org/gene/10090:Zwilch ^@ http://purl.uniprot.org/uniprot/Q8R060 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Protein zwilch homolog ^@ http://purl.uniprot.org/annotation/PRO_0000314801 http://togogenome.org/gene/10090:Lamc2 ^@ http://purl.uniprot.org/uniprot/G5E874 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Laminin EGF-like|||Laminin IV type A ^@ http://purl.uniprot.org/annotation/PRO_5015091894 http://togogenome.org/gene/10090:Tead4 ^@ http://purl.uniprot.org/uniprot/Q62296 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Disordered|||In isoform Short.|||Nuclear localization signal|||Polar residues|||Pro residues|||TEA|||Transcriptional enhancer factor TEF-3 ^@ http://purl.uniprot.org/annotation/PRO_0000205938|||http://purl.uniprot.org/annotation/VSP_006390 http://togogenome.org/gene/10090:H3c14 ^@ http://purl.uniprot.org/uniprot/B9EI85|||http://purl.uniprot.org/uniprot/P84228 ^@ Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||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 H2A/H2B/H3|||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; 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_0000221250 http://togogenome.org/gene/10090:B3galt5 ^@ http://purl.uniprot.org/uniprot/Q9JI67 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Beta-1,3-galactosyltransferase 5|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219165 http://togogenome.org/gene/10090:Trappc1 ^@ http://purl.uniprot.org/uniprot/Q5NCF2 ^@ Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Strand|||Turn ^@ Trafficking protein particle complex subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000211563 http://togogenome.org/gene/10090:Cbln3 ^@ http://purl.uniprot.org/uniprot/Q9JHG0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide ^@ C1q|||Cerebellin-3|||Interchain|||N-linked (GlcNAc...) asparagine|||Necessary for interaction with CBLN3, and homotrimerization|||Promotes self-association and secretion independent of CBLN1. ^@ http://purl.uniprot.org/annotation/PRO_0000003555 http://togogenome.org/gene/10090:Klhdc9 ^@ http://purl.uniprot.org/uniprot/Q3USL1 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ Kelch 1|||Kelch 2|||Kelch 3|||Kelch domain-containing protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000300465 http://togogenome.org/gene/10090:Fxyd2 ^@ http://purl.uniprot.org/uniprot/Q04646|||http://purl.uniprot.org/uniprot/Q6ITT1|||http://purl.uniprot.org/uniprot/Q6ITT2 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Sodium/potassium-transporting ATPase subunit gamma ^@ http://purl.uniprot.org/annotation/PRO_0000148186|||http://purl.uniprot.org/annotation/VSP_001581|||http://purl.uniprot.org/annotation/VSP_001582 http://togogenome.org/gene/10090:Rev3l ^@ http://purl.uniprot.org/uniprot/Q61493 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||CysA-type|||CysB motif|||DNA polymerase zeta catalytic subunit|||Disordered|||Mediates interaction with MAD2L2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000046469 http://togogenome.org/gene/10090:Trrap ^@ http://purl.uniprot.org/uniprot/E9QLK7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||FAT|||FATC|||PI3K/PI4K catalytic|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Smco1 ^@ http://purl.uniprot.org/uniprot/Q8CEZ1 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Single-pass membrane and coiled-coil domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000269484|||http://purl.uniprot.org/annotation/VSP_046481 http://togogenome.org/gene/10090:Mbtd1 ^@ http://purl.uniprot.org/uniprot/Q6P5G3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||FCS-type|||In isoform 2.|||MBT 1|||MBT 2|||MBT 3|||MBT 4|||MBT domain-containing protein 1|||N6-acetyllysine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000313718|||http://purl.uniprot.org/annotation/VSP_030119|||http://purl.uniprot.org/annotation/VSP_030120 http://togogenome.org/gene/10090:Sec23b ^@ http://purl.uniprot.org/uniprot/Q3TIS3|||http://purl.uniprot.org/uniprot/Q8CDS4|||http://purl.uniprot.org/uniprot/Q9D662 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ Gelsolin-like|||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_0000205149 http://togogenome.org/gene/10090:Acin1 ^@ http://purl.uniprot.org/uniprot/B8JJ91|||http://purl.uniprot.org/uniprot/Q52KR6|||http://purl.uniprot.org/uniprot/Q7TSL7|||http://purl.uniprot.org/uniprot/Q80TU6|||http://purl.uniprot.org/uniprot/Q9JIX8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ 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 isoform 2.|||In isoform 3.|||In isoform 4.|||N6,N6,N6-trimethyllysine; by EHMT2; alternate|||N6,N6-dimethyllysine; by EHMT2; alternate|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphoserine; by SRPK2 and PKB/AKT1|||Phosphothreonine|||Polar residues|||Pro residues|||SAP|||Sufficient for interaction with RNPS1 and SAP18 and formation of the ASAP complex ^@ http://purl.uniprot.org/annotation/PRO_0000064437|||http://purl.uniprot.org/annotation/VSP_004030|||http://purl.uniprot.org/annotation/VSP_004031|||http://purl.uniprot.org/annotation/VSP_004032|||http://purl.uniprot.org/annotation/VSP_004033 http://togogenome.org/gene/10090:Slc7a4 ^@ http://purl.uniprot.org/uniprot/Q8BLQ7 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Transmembrane ^@ Cationic amino acid transporter 4|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000304934 http://togogenome.org/gene/10090:Or2g7 ^@ http://purl.uniprot.org/uniprot/Q8VFC1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tekt4 ^@ http://purl.uniprot.org/uniprot/Q149S1 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Sequence Conflict ^@ Tektin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000261163 http://togogenome.org/gene/10090:Yme1l1 ^@ http://purl.uniprot.org/uniprot/O88967 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Region|||Topological Domain|||Transmembrane ^@ ATP-dependent zinc metalloprotease YME1L1|||Disordered|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix ^@ http://purl.uniprot.org/annotation/PRO_0000084668 http://togogenome.org/gene/10090:D830030K20Rik ^@ http://purl.uniprot.org/uniprot/Q8BGG1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:Snap25 ^@ http://purl.uniprot.org/uniprot/P60879 ^@ Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Splice Variant ^@ (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA)|||(Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E)|||58% reduction in palmitoylation level. 28% membrane association. Very little palmitoylation and less than 8% membrane association; when associated with S-92 or A-92.|||65% reduction in palmitoylation level. 29% membrane association. No palmitoylation and less than 8% membrane association; when associated with S-90 or A-90.|||79% reduction in palmitoylation level. 18% membrane association. No palmitoylation and less than 8% membrane association; when associated with S-85 or A-85.|||91% reduction in palmitoylation level. 14% membrane association. No palmitoylation and less than 8% membrane association; when associated with S-88 or A-88.|||Disordered|||In isoform 2.|||Interaction with CENPF|||Interaction with ZDHHC17|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine; by PKC and PKA|||S-palmitoyl cysteine|||Synaptosomal-associated protein 25|||t-SNARE coiled-coil homology 1|||t-SNARE coiled-coil homology 2 ^@ http://purl.uniprot.org/annotation/PRO_0000213589|||http://purl.uniprot.org/annotation/VSP_010019 http://togogenome.org/gene/10090:Vmn1r62 ^@ http://purl.uniprot.org/uniprot/Q8R2C0|||http://purl.uniprot.org/uniprot/Q9EPT0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:E030018B13Rik ^@ http://purl.uniprot.org/uniprot/J3QMS9 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Isoc2b ^@ http://purl.uniprot.org/uniprot/Q9DCC7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Isochorismatase domain-containing protein 2B|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000268673 http://togogenome.org/gene/10090:Crtc3 ^@ http://purl.uniprot.org/uniprot/Q91X84 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes phosphorylation at Ser-391. Abolishes interaction with PPP2CA and PPP2R1A.|||Abolishes phosphorylation. Abolishes interaction with PPP2CA and PPP2R1A. Slight increase in phosphorylation at Ser-273 and in the interaction with 14-3-3 proteins.|||CREB-regulated transcription coactivator 3|||Disordered|||Does not affect phosphorylation at Ser-391 or the interaction with PPP2CA and PPP2R1A.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphoserine; by SIK2|||Phosphothreonine|||Polar residues|||Pro residues|||Reduces interaction with 14-3-3 proteins without affecting the interaction with PPP2R1A; when associated with A-329 and A-370.|||Reduces interaction with 14-3-3 proteins without affecting the interaction with PPP2R1A; when associated with A-62 and A-329.|||Reduces interaction with 14-3-3 proteins without affecting the interaction with PPP2R1A; when associated with A-62 and A-370.|||Reduces interaction with 14-3-3 proteins. Abolishes interaction with 14-3-3 proteins without affecting the interaction with PPP2R1A; when associated with A-162.|||Required for interaction with PPP2CA and PPP2R1A|||Up-regulates CREB transcription factor activity. Reduces interaction with 14-3-3 proteins. Abolishes interaction with 14-3-3 proteins without affecting the interaction with PPP2R1A; when associated with A-273. ^@ http://purl.uniprot.org/annotation/PRO_0000318532|||http://purl.uniprot.org/annotation/VSP_031221 http://togogenome.org/gene/10090:Hipk2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J202|||http://purl.uniprot.org/uniprot/A0A0R4J204|||http://purl.uniprot.org/uniprot/Q5D0E9|||http://purl.uniprot.org/uniprot/Q9QZR5 ^@ 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|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Autoinhibitory domain (AID)|||Cleavage; by CASP6|||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 2|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||Inhibits localization to nuclear speckles.|||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|||Localization to nuclear speckles|||No enzymatic activity, but still interacts with TP53 and NLK. Blocks the ability to induce cell growth arrest. Decreases corepressor activity.|||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|||Strongly reduced nuclear localization.|||Transcriptional corepression ^@ http://purl.uniprot.org/annotation/PRO_0000085997|||http://purl.uniprot.org/annotation/VSP_004808|||http://purl.uniprot.org/annotation/VSP_013135|||http://purl.uniprot.org/annotation/VSP_013136|||http://purl.uniprot.org/annotation/VSP_013137|||http://purl.uniprot.org/annotation/VSP_013138|||http://purl.uniprot.org/annotation/VSP_013139 http://togogenome.org/gene/10090:Elf1 ^@ http://purl.uniprot.org/uniprot/A0A2I3BPX9|||http://purl.uniprot.org/uniprot/Q3UQ47|||http://purl.uniprot.org/uniprot/Q3V1H4|||http://purl.uniprot.org/uniprot/Q60775 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||ETS|||ETS-related transcription factor Elf-1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204086 http://togogenome.org/gene/10090:Phkg2 ^@ http://purl.uniprot.org/uniprot/Q9DB30 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Calmodulin-binding (domain-C)|||Calmodulin-binding (domain-N)|||Phosphorylase b kinase gamma catalytic chain, liver/testis isoform|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086513 http://togogenome.org/gene/10090:Qrich1 ^@ http://purl.uniprot.org/uniprot/G3X8R5|||http://purl.uniprot.org/uniprot/Q3UA37 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ CARD|||DUF3504|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Transcriptional regulator QRICH1 ^@ http://purl.uniprot.org/annotation/PRO_0000269854 http://togogenome.org/gene/10090:Or3a10 ^@ http://purl.uniprot.org/uniprot/Q60891 ^@ 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 3A10 ^@ http://purl.uniprot.org/annotation/PRO_0000150816 http://togogenome.org/gene/10090:Unkl ^@ http://purl.uniprot.org/uniprot/E0CYD7|||http://purl.uniprot.org/uniprot/Q5FWH2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||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.|||In isoform 2.|||Polar residues|||Putative E3 ubiquitin-protein ligase UNKL|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000278668|||http://purl.uniprot.org/annotation/VSP_039444|||http://purl.uniprot.org/annotation/VSP_039445|||http://purl.uniprot.org/annotation/VSP_039446|||http://purl.uniprot.org/annotation/VSP_039447 http://togogenome.org/gene/10090:Sned1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0N0|||http://purl.uniprot.org/uniprot/Q70E20 ^@ 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 ^@ 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|||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|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||NIDO|||Sushi|||Sushi, nidogen and EGF-like domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_5000072108|||http://purl.uniprot.org/annotation/PRO_5006451973|||http://purl.uniprot.org/annotation/VSP_027755 http://togogenome.org/gene/10090:1700037C18Rik ^@ http://purl.uniprot.org/uniprot/Q8BT88 ^@ 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 C16orf90 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000343582|||http://purl.uniprot.org/annotation/VSP_034617|||http://purl.uniprot.org/annotation/VSP_034618|||http://purl.uniprot.org/annotation/VSP_034619 http://togogenome.org/gene/10090:Slc39a6 ^@ http://purl.uniprot.org/uniprot/Q8C145 ^@ 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 ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Zinc transporter ZIP6 ^@ http://purl.uniprot.org/annotation/PRO_0000041651 http://togogenome.org/gene/10090:Ly6g5c ^@ http://purl.uniprot.org/uniprot/Q8K1T5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Lymphocyte antigen 6 complex locus protein G5c|||N-linked (GlcNAc...) asparagine|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000323018 http://togogenome.org/gene/10090:Brsk1 ^@ http://purl.uniprot.org/uniprot/Q5RJI5 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Abolishes activation by STK11/LKB1.|||Abolishes kinase activity and ability to regulate centrosome duplication.|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LKB1|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase BRSK1|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000260829|||http://purl.uniprot.org/annotation/VSP_041743|||http://purl.uniprot.org/annotation/VSP_041745 http://togogenome.org/gene/10090:Itgb2l ^@ http://purl.uniprot.org/uniprot/D3YXH8|||http://purl.uniprot.org/uniprot/Q3UV74 ^@ 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.|||In isoform 3.|||In strain: BALB/c and C3H/HeJ.|||Integrin beta|||Integrin beta subunit VWA|||Integrin beta subunit tail|||Integrin beta-2-like protein|||N-linked (GlcNAc...) asparagine|||PSI|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000278124|||http://purl.uniprot.org/annotation/PRO_5003052539|||http://purl.uniprot.org/annotation/VSP_052319|||http://purl.uniprot.org/annotation/VSP_052320|||http://purl.uniprot.org/annotation/VSP_052321|||http://purl.uniprot.org/annotation/VSP_052322 http://togogenome.org/gene/10090:Otor ^@ http://purl.uniprot.org/uniprot/Q548U4|||http://purl.uniprot.org/uniprot/Q9JIE3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Otoraplin|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000019034|||http://purl.uniprot.org/annotation/PRO_5014309629 http://togogenome.org/gene/10090:Mospd2 ^@ http://purl.uniprot.org/uniprot/B1AU74|||http://purl.uniprot.org/uniprot/Q9CWP6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||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|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||CRAL-TRIO|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In strain: FVB/N.|||MSP|||Motile sperm domain-containing protein 2|||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_0000213464|||http://purl.uniprot.org/annotation/VSP_014047|||http://purl.uniprot.org/annotation/VSP_014048|||http://purl.uniprot.org/annotation/VSP_014049|||http://purl.uniprot.org/annotation/VSP_014050|||http://purl.uniprot.org/annotation/VSP_014051|||http://purl.uniprot.org/annotation/VSP_014052 http://togogenome.org/gene/10090:Gnat3 ^@ http://purl.uniprot.org/uniprot/B2RVZ3|||http://purl.uniprot.org/uniprot/Q3V3I2 ^@ 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_0000342672 http://togogenome.org/gene/10090:Dact1 ^@ http://purl.uniprot.org/uniprot/D3Z5V0|||http://purl.uniprot.org/uniprot/Q8R4A3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Bipartite nuclear localization signal|||Dapper homolog 1|||Disordered|||Nuclear export signal|||PDZ-binding|||Phosphoserine; by PKA|||Polar residues|||Required for self-association ^@ http://purl.uniprot.org/annotation/PRO_0000191354 http://togogenome.org/gene/10090:Zcchc12 ^@ http://purl.uniprot.org/uniprot/Q9CZA5 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Zinc Finger ^@ CCHC-type|||Disordered|||Polar residues|||Zinc finger CCHC domain-containing protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000150972 http://togogenome.org/gene/10090:Cmtm8 ^@ http://purl.uniprot.org/uniprot/Q9CZR4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Transmembrane ^@ CKLF-like MARVEL transmembrane domain-containing protein 8|||Helical|||MARVEL ^@ http://purl.uniprot.org/annotation/PRO_0000186113 http://togogenome.org/gene/10090:Lgals3 ^@ http://purl.uniprot.org/uniprot/Q8C253 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Galectin|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Prph2 ^@ http://purl.uniprot.org/uniprot/P15499|||http://purl.uniprot.org/uniprot/Q3UWK3 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Interaction with MREG|||Interchain (with ROM1)|||Lumenal|||N-linked (GlcNAc...) asparagine|||Peripherin-2|||Reduced cone and rod photoreceptor function as a result of outer segment malformation, including disorganization, short outer segments, and elongated disks which affect both rod and cone photoreceptors. Reduced Prph2 and Rom1 protein abundance in the retina in addition to disruption of the formation of large disulfide-linked protein complexes.|||Reduced cone and rod photoreceptor function as a result of outer segment malformation, including disorganization, short outer segments, and elongated disks which affect both rod and cone photoreceptors. Reduced Prph2 protein abundance in the retina. ^@ http://purl.uniprot.org/annotation/PRO_0000168106 http://togogenome.org/gene/10090:Mtbp ^@ http://purl.uniprot.org/uniprot/Q8BJS8 ^@ 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.|||Interaction with MDM2|||Mdm2-binding protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000323746|||http://purl.uniprot.org/annotation/VSP_032105|||http://purl.uniprot.org/annotation/VSP_032106|||http://purl.uniprot.org/annotation/VSP_032107 http://togogenome.org/gene/10090:Cfap299 ^@ http://purl.uniprot.org/uniprot/Q810M1 ^@ Chain|||Molecule Processing ^@ Chain ^@ Cilia- and flagella-associated protein 299 ^@ http://purl.uniprot.org/annotation/PRO_0000301956 http://togogenome.org/gene/10090:Nr4a3 ^@ http://purl.uniprot.org/uniprot/A0A6F8X1J9|||http://purl.uniprot.org/uniprot/Q9QZB6 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Splice Variant|||Zinc Finger ^@ Activation function (AF)-1 domain|||Basic residues|||Disordered|||In isoform 2.|||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|||Required for DNA-PK heterotrimer ^@ http://purl.uniprot.org/annotation/PRO_0000053723|||http://purl.uniprot.org/annotation/VSP_010083|||http://purl.uniprot.org/annotation/VSP_010084 http://togogenome.org/gene/10090:Ctu2 ^@ http://purl.uniprot.org/uniprot/Q3U308 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Cytoplasmic tRNA 2-thiolation protein 2|||Disordered|||N-acetylcysteine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000289176 http://togogenome.org/gene/10090:Sstr5 ^@ http://purl.uniprot.org/uniprot/O08858 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||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; by ZDHHC5|||Somatostatin receptor type 5 ^@ http://purl.uniprot.org/annotation/PRO_0000070131 http://togogenome.org/gene/10090:Igsf9 ^@ http://purl.uniprot.org/uniprot/Q05BQ1 ^@ 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|||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|||Signal Peptide|||Splice Variant|||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.|||Loss of interaction with MAGI2 and SHANK1 and loss of function.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Polar residues|||Pro residues|||Protein turtle homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000306108|||http://purl.uniprot.org/annotation/VSP_028408|||http://purl.uniprot.org/annotation/VSP_028409 http://togogenome.org/gene/10090:Tspyl2 ^@ http://purl.uniprot.org/uniprot/Q7TQI8 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Testis-specific Y-encoded-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000289102 http://togogenome.org/gene/10090:Aip ^@ http://purl.uniprot.org/uniprot/O08915 ^@ Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Repeat|||Strand|||Turn ^@ AH receptor-interacting protein|||PPIase FKBP-type|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000075340 http://togogenome.org/gene/10090:Il1r1 ^@ http://purl.uniprot.org/uniprot/P13504|||http://purl.uniprot.org/uniprot/Q32MH0|||http://purl.uniprot.org/uniprot/Q8C6P3|||http://purl.uniprot.org/uniprot/Q8C833 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||Interleukin-1 receptor type 1|||Interleukin-1 receptor type 1, membrane form|||Interleukin-1 receptor type 1, soluble form|||N-linked (GlcNAc...) asparagine|||Phosphothreonine; by PKC|||Phosphotyrosine|||TIR ^@ http://purl.uniprot.org/annotation/PRO_0000015436|||http://purl.uniprot.org/annotation/PRO_0000415345|||http://purl.uniprot.org/annotation/PRO_5004303921|||http://purl.uniprot.org/annotation/PRO_5014309034|||http://purl.uniprot.org/annotation/PRO_5015099055|||http://purl.uniprot.org/annotation/VSP_058170 http://togogenome.org/gene/10090:Fam107b ^@ http://purl.uniprot.org/uniprot/Q3TGF2 ^@ 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|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Protein FAM107B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000230775 http://togogenome.org/gene/10090:Tmem131l ^@ http://purl.uniprot.org/uniprot/A0A0B4J1F5|||http://purl.uniprot.org/uniprot/Q3U3D7 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Required for Wnt-signaling inhibition and LRP6 degradation|||Transmembrane protein 131-like|||Transmembrane protein 131-like N-terminal|||Transmembrane protein 131-like conserved ^@ http://purl.uniprot.org/annotation/PRO_0000328866|||http://purl.uniprot.org/annotation/PRO_5002094055|||http://purl.uniprot.org/annotation/VSP_032832|||http://purl.uniprot.org/annotation/VSP_032833|||http://purl.uniprot.org/annotation/VSP_032834 http://togogenome.org/gene/10090:Ppie ^@ http://purl.uniprot.org/uniprot/Q9QZH3 ^@ 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|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase E|||Phosphoserine|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000064158 http://togogenome.org/gene/10090:Immp2l ^@ http://purl.uniprot.org/uniprot/Q8BPT6 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Mitochondrial inner membrane protease subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000259578 http://togogenome.org/gene/10090:Csf3 ^@ http://purl.uniprot.org/uniprot/P09920|||http://purl.uniprot.org/uniprot/Q0VB73 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Granulocyte colony-stimulating factor|||O-linked (GalNAc...) threonine ^@ http://purl.uniprot.org/annotation/PRO_0000015571|||http://purl.uniprot.org/annotation/PRO_5014306831 http://togogenome.org/gene/10090:Or5b117 ^@ http://purl.uniprot.org/uniprot/Q7TQQ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lhcgr ^@ http://purl.uniprot.org/uniprot/P30730 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Repeat|||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|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||Lutropin-choriogonadotropic hormone receptor|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000012781 http://togogenome.org/gene/10090:Gm10147 ^@ http://purl.uniprot.org/uniprot/Q62478 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Vmn1r41 ^@ http://purl.uniprot.org/uniprot/A0A0N4SVQ3|||http://purl.uniprot.org/uniprot/Q9EQ44 ^@ 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|||Vomeronasal type-1 receptor 41 ^@ http://purl.uniprot.org/annotation/PRO_0000239981 http://togogenome.org/gene/10090:Snx22 ^@ http://purl.uniprot.org/uniprot/Q8C084 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||PX ^@ http://togogenome.org/gene/10090:Pmpcb ^@ http://purl.uniprot.org/uniprot/Q9CXT8 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Site|||Transit Peptide ^@ Mitochondrial-processing peptidase subunit beta|||Mitochondrion|||Proton acceptor|||Required for the specific determination of the substrate cleavage site ^@ http://purl.uniprot.org/annotation/PRO_0000026778 http://togogenome.org/gene/10090:Ppp2r5b ^@ http://purl.uniprot.org/uniprot/Q6PD28 ^@ 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|||Pro residues|||Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform ^@ http://purl.uniprot.org/annotation/PRO_0000438660 http://togogenome.org/gene/10090:Trp53bp2 ^@ http://purl.uniprot.org/uniprot/E9QJU8|||http://purl.uniprot.org/uniprot/Q8CG79 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||Apoptosis-stimulating of p53 protein 2|||Basic and acidic residues|||Disordered|||Interaction with APPBP1|||Mediates interaction with APC2|||Phosphoserine|||Polar residues|||SH3|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000066965 http://togogenome.org/gene/10090:Cnot8 ^@ http://purl.uniprot.org/uniprot/Q9D8X5 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ CCR4-NOT transcription complex subunit 8 ^@ http://purl.uniprot.org/annotation/PRO_0000212847 http://togogenome.org/gene/10090:Setd7 ^@ http://purl.uniprot.org/uniprot/Q8VHL1 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Site ^@ Abolishes methyltransferase activity.|||Histone H3K4 binding|||Histone-lysine N-methyltransferase SETD7|||MORN 1|||MORN 2|||MORN 3|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000186055 http://togogenome.org/gene/10090:Ms4a6d ^@ http://purl.uniprot.org/uniprot/Q2TVW7|||http://purl.uniprot.org/uniprot/Q99N07 ^@ 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|||Membrane-spanning 4-domains subfamily A member 6D|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000158641 http://togogenome.org/gene/10090:Or52z14 ^@ http://purl.uniprot.org/uniprot/E9PV95 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Shcbp1 ^@ http://purl.uniprot.org/uniprot/Q9Z179 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ N-acetylalanine|||PbH1 1|||PbH1 2|||PbH1 3|||PbH1 4|||PbH1 5|||Phosphoserine|||Removed|||SHC SH2 domain-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000076316 http://togogenome.org/gene/10090:Suclg1 ^@ http://purl.uniprot.org/uniprot/Q9WUM5 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ 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_0000033341 http://togogenome.org/gene/10090:Eme1 ^@ http://purl.uniprot.org/uniprot/Q8BJW7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Crossover junction endonuclease EME1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000223631 http://togogenome.org/gene/10090:Fam209 ^@ http://purl.uniprot.org/uniprot/A2APA5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Protein FAM209 ^@ http://purl.uniprot.org/annotation/PRO_5015086030 http://togogenome.org/gene/10090:Mutyh ^@ http://purl.uniprot.org/uniprot/Q762C9|||http://purl.uniprot.org/uniprot/Q762D1|||http://purl.uniprot.org/uniprot/Q99P21 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ Adenine DNA glycosylase|||Basic residues|||Disordered|||Nudix box|||Nudix hydrolase|||Polar residues|||Proton donor/acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000102240 http://togogenome.org/gene/10090:Gtf2i ^@ http://purl.uniprot.org/uniprot/Q3UHU8|||http://purl.uniprot.org/uniprot/Q9ESZ8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ 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|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5.|||N-acetylalanine|||N6-acetyllysine; alternate|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PKG/PRKG1|||Phosphothreonine|||Phosphotyrosine; by BTK|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000083873|||http://purl.uniprot.org/annotation/VSP_003869|||http://purl.uniprot.org/annotation/VSP_003870|||http://purl.uniprot.org/annotation/VSP_003871|||http://purl.uniprot.org/annotation/VSP_003872 http://togogenome.org/gene/10090:Dhrs7b ^@ http://purl.uniprot.org/uniprot/I7DM66|||http://purl.uniprot.org/uniprot/Q99J47 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dehydrogenase/reductase SDR family member 7B|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000312106|||http://purl.uniprot.org/annotation/VSP_029698 http://togogenome.org/gene/10090:Kera ^@ http://purl.uniprot.org/uniprot/A4FUJ3|||http://purl.uniprot.org/uniprot/O35367 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide ^@ 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_0000032749|||http://purl.uniprot.org/annotation/PRO_5014296879 http://togogenome.org/gene/10090:Vmn1r218 ^@ http://purl.uniprot.org/uniprot/Q8R261 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfand3 ^@ http://purl.uniprot.org/uniprot/Q497H0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Zinc Finger ^@ A20-type|||AN1-type|||AN1-type zinc finger protein 3|||Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000076371|||http://purl.uniprot.org/annotation/VSP_017154 http://togogenome.org/gene/10090:Xylb ^@ http://purl.uniprot.org/uniprot/Q3TMS3|||http://purl.uniprot.org/uniprot/Q3TNA1 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Carbohydrate kinase FGGY C-terminal|||Xylulose kinase ^@ http://purl.uniprot.org/annotation/PRO_0000230986 http://togogenome.org/gene/10090:Or10ac1 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1M2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Chac1 ^@ http://purl.uniprot.org/uniprot/Q8R3J5 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disordered|||Glutathione-specific gamma-glutamylcyclotransferase 1|||Loss of catalytic activity against glutathione.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000239011 http://togogenome.org/gene/10090:Foxa3 ^@ http://purl.uniprot.org/uniprot/P35584 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Disordered|||Fork-head|||Hepatocyte nuclear factor 3-gamma|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000091801 http://togogenome.org/gene/10090:Fermt1 ^@ http://purl.uniprot.org/uniprot/P59113 ^@ 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 ^@ Disordered|||FERM|||Fermitin family homolog 1|||PH|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000219453 http://togogenome.org/gene/10090:Chmp7 ^@ http://purl.uniprot.org/uniprot/Q8R1T1 ^@ 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 ^@ Charged multivesicular body protein 7|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000211517|||http://purl.uniprot.org/annotation/VSP_015343|||http://purl.uniprot.org/annotation/VSP_015344 http://togogenome.org/gene/10090:Psme3 ^@ http://purl.uniprot.org/uniprot/P61290|||http://purl.uniprot.org/uniprot/Q4FK54 ^@ 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|||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_0000161790 http://togogenome.org/gene/10090:Hvcn1 ^@ http://purl.uniprot.org/uniprot/Q3U2S8 ^@ Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Faster channel activation kinetics.|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Impairs gating cooperativity.|||No effect on channel activation kinetics.|||Same activation kinetics as wild-type.|||Slows channel activation.|||Voltage-gated hydrogen channel 1 ^@ http://purl.uniprot.org/annotation/PRO_0000342188 http://togogenome.org/gene/10090:Mcpt4 ^@ http://purl.uniprot.org/uniprot/P21812|||http://purl.uniprot.org/uniprot/Q3UN88 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Mass|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Mass|||Propeptide|||Sequence Variant|||Signal Peptide ^@ Activation peptide|||Charge relay system|||In strain: C57BL/6 and Leaden XA1.|||Mast cell protease 4|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027453|||http://purl.uniprot.org/annotation/PRO_0000027454|||http://purl.uniprot.org/annotation/PRO_5015097489 http://togogenome.org/gene/10090:Gm10413 ^@ http://purl.uniprot.org/uniprot/Q497R9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Nlrp2 ^@ http://purl.uniprot.org/uniprot/Q4PLS0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ NACHT ^@ http://togogenome.org/gene/10090:Tmem182 ^@ http://purl.uniprot.org/uniprot/B2RVY9 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Interaction with ITGB1|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 182 ^@ http://purl.uniprot.org/annotation/PRO_0000369257 http://togogenome.org/gene/10090:Ly6g6d ^@ http://purl.uniprot.org/uniprot/Q9Z1Q3 ^@ 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 ^@ GPI-anchor amidated asparagine|||Lymphocyte antigen 6 complex locus protein G6d|||O-linked (GalNAc...) threonine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000323709|||http://purl.uniprot.org/annotation/PRO_0000323710 http://togogenome.org/gene/10090:Rnf114 ^@ http://purl.uniprot.org/uniprot/Q9ET26 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Modified Residue|||Region|||Zinc Finger ^@ C2HC RNF-type|||Disordered|||E3 ubiquitin-protein ligase RNF114|||N6-acetyllysine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056308 http://togogenome.org/gene/10090:Pla2g12b ^@ http://purl.uniprot.org/uniprot/Q8VC81 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099439 http://togogenome.org/gene/10090:Cyp21a1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J048|||http://purl.uniprot.org/uniprot/P03940|||http://purl.uniprot.org/uniprot/Q3UJ92 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Sequence Conflict|||Signal Peptide ^@ Steroid 21-hydroxylase|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051977|||http://purl.uniprot.org/annotation/PRO_5004230148|||http://purl.uniprot.org/annotation/PRO_5015044308 http://togogenome.org/gene/10090:Sgsh ^@ http://purl.uniprot.org/uniprot/Q3URR4|||http://purl.uniprot.org/uniprot/Q9EQ08 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Non-terminal Residue|||Signal Peptide ^@ N-sulphoglucosamine sulphohydrolase C-terminal|||Sulfatase N-terminal ^@ http://purl.uniprot.org/annotation/PRO_5015099717 http://togogenome.org/gene/10090:Dalrd3 ^@ http://purl.uniprot.org/uniprot/Q6PJN8 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ DALR anticodon-binding domain-containing protein 3|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000315849|||http://purl.uniprot.org/annotation/VSP_030747 http://togogenome.org/gene/10090:Ggt5 ^@ http://purl.uniprot.org/uniprot/Q9Z2A9 ^@ 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 ^@ Cytoplasmic|||Extracellular|||Glutathione hydrolase 5 heavy chain|||Glutathione hydrolase 5 light chain|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000011074|||http://purl.uniprot.org/annotation/PRO_0000011075|||http://purl.uniprot.org/annotation/VSP_008147|||http://purl.uniprot.org/annotation/VSP_008148 http://togogenome.org/gene/10090:Gm10665 ^@ http://purl.uniprot.org/uniprot/K7N6B7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tgfb1 ^@ http://purl.uniprot.org/uniprot/P04202|||http://purl.uniprot.org/uniprot/Q3UNK5 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Site ^@ Arm domain|||Bowtie tail|||Cell attachment site|||Cleavage; by FURIN|||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|||Straightjacket domain|||TGF-beta family profile|||Transforming growth factor beta|||Transforming growth factor beta-1 ^@ http://purl.uniprot.org/annotation/PRO_0000033766|||http://purl.uniprot.org/annotation/PRO_0000033767|||http://purl.uniprot.org/annotation/PRO_5014309152 http://togogenome.org/gene/10090:Snx20 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0D0|||http://purl.uniprot.org/uniprot/Q9D2Y5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes location on endosome membranes. Abolishes binding to membranes enriched in phosphatidylinositol 3-phosphate. Mildly decreases binding to membranes enriched in phosphatidylinositol 4,5-bisphosphate.|||Disordered|||PX|||Phosphoserine|||Sorting nexin-20 ^@ http://purl.uniprot.org/annotation/PRO_0000213869 http://togogenome.org/gene/10090:Ptk2b ^@ http://purl.uniprot.org/uniprot/E9Q2A6|||http://purl.uniprot.org/uniprot/K7QD41|||http://purl.uniprot.org/uniprot/Q3UDE9|||http://purl.uniprot.org/uniprot/Q9QVP9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disordered|||FERM|||Focal adhesion targeting (FAT)|||Interaction with TGFB1I1|||Loss of phosphorylation and interaction with SRC, and inhibition of bone resorption.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||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_0000088082 http://togogenome.org/gene/10090:Tmem125 ^@ http://purl.uniprot.org/uniprot/Q8CHQ6 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 125 ^@ http://purl.uniprot.org/annotation/PRO_0000251717 http://togogenome.org/gene/10090:Ms4a4a ^@ http://purl.uniprot.org/uniprot/A0A087WRT7 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Pycr2 ^@ http://purl.uniprot.org/uniprot/Q3TMZ1|||http://purl.uniprot.org/uniprot/Q922Q4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylserine|||Phosphoserine|||Polar residues|||Pyrroline-5-carboxylate reductase 2|||Pyrroline-5-carboxylate reductase catalytic N-terminal|||Pyrroline-5-carboxylate reductase dimerisation|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000187318 http://togogenome.org/gene/10090:Izumo3 ^@ http://purl.uniprot.org/uniprot/A6PWV3 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Izumo sperm-egg fusion protein 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000342458|||http://purl.uniprot.org/annotation/VSP_034458 http://togogenome.org/gene/10090:Or10j3b ^@ http://purl.uniprot.org/uniprot/Q8VGE1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dlg2 ^@ http://purl.uniprot.org/uniprot/A0A571BEZ4|||http://purl.uniprot.org/uniprot/D3YWU0|||http://purl.uniprot.org/uniprot/Q91XM9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Disks large homolog 2|||Disordered|||Guanylate kinase-like|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphotyrosine|||Polar residues|||S-palmitoyl cysteine|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000094554|||http://purl.uniprot.org/annotation/VSP_012869|||http://purl.uniprot.org/annotation/VSP_012870|||http://purl.uniprot.org/annotation/VSP_012871|||http://purl.uniprot.org/annotation/VSP_015517|||http://purl.uniprot.org/annotation/VSP_015518|||http://purl.uniprot.org/annotation/VSP_015519|||http://purl.uniprot.org/annotation/VSP_015520|||http://purl.uniprot.org/annotation/VSP_015521|||http://purl.uniprot.org/annotation/VSP_015522|||http://purl.uniprot.org/annotation/VSP_015523|||http://purl.uniprot.org/annotation/VSP_015524 http://togogenome.org/gene/10090:Zfp445 ^@ http://purl.uniprot.org/uniprot/Q8CBF5|||http://purl.uniprot.org/uniprot/Q8R2V3 ^@ 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 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)|||KRAB|||SCAN box|||Zinc finger protein 445 ^@ http://purl.uniprot.org/annotation/PRO_0000047595 http://togogenome.org/gene/10090:Armh4 ^@ http://purl.uniprot.org/uniprot/Q8BT18 ^@ 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 ^@ Acidic residues|||Armadillo-like helical domain-containing protein 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000252153 http://togogenome.org/gene/10090:Has2 ^@ http://purl.uniprot.org/uniprot/P70312 ^@ Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||O-linked (GlcNAc) serine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000197174 http://togogenome.org/gene/10090:Dusp7 ^@ http://purl.uniprot.org/uniprot/Q3TY83|||http://purl.uniprot.org/uniprot/Q91Z46 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Dual specificity protein phosphatase 7|||In isoform 2.|||Interaction with MAPK1|||Loss of MAPK1 binding. No effect on nuclear envelope breakdown activity in oocytes.|||No effect on MAPK1 binding. Impairs nuclear envelope breakdown activity in oocytes.|||Phosphocysteine intermediate|||Rhodanese|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094808|||http://purl.uniprot.org/annotation/VSP_041462 http://togogenome.org/gene/10090:Sftpc ^@ http://purl.uniprot.org/uniprot/Q6P8P8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ BRICHOS|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Nxpe3 ^@ http://purl.uniprot.org/uniprot/B9EKK6 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Sprr2a2 ^@ http://purl.uniprot.org/uniprot/Q4KL71|||http://purl.uniprot.org/uniprot/Q9CQK8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||4|||5|||5 X 9 AA approximate tandem repeats|||Small proline-rich protein 2A1|||Small proline-rich protein 2A3 ^@ http://purl.uniprot.org/annotation/PRO_0000150014|||http://purl.uniprot.org/annotation/PRO_0000425580 http://togogenome.org/gene/10090:Arr3 ^@ http://purl.uniprot.org/uniprot/Q9EQP6 ^@ Chain|||Molecule Processing ^@ Chain ^@ Arrestin-C ^@ http://purl.uniprot.org/annotation/PRO_0000205204 http://togogenome.org/gene/10090:Zc3h6 ^@ http://purl.uniprot.org/uniprot/A2AP88 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||C3H1-type|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Adgrl3 ^@ http://purl.uniprot.org/uniprot/D3Z3X6|||http://purl.uniprot.org/uniprot/D3Z634|||http://purl.uniprot.org/uniprot/D3Z6H9|||http://purl.uniprot.org/uniprot/Q80TS3 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes FLRT3 binding.|||Abolishes interaction with FLRT2; when associated with N-292.|||Abolishes interaction with FLRT2; when associated with N-324.|||Abolishes interaction with FLRT2; when associated with T-294.|||Abolishes interaction with FLRT2; when associated with T-326.|||Adhesion G protein-coupled receptor L3|||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 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||Interaction with FLRT3|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Phosphoserine|||SUEL-type lectin|||Strongly reduces FLRT2 binding; when associated with N-244.|||Strongly reduces FLRT2 binding; when associated with N-267.|||Strongly reduces FLRT2 binding; when associated with T-246.|||Strongly reduces FLRT2 binding; when associated with T-269.|||Strongly reduces FLRT3 binding. ^@ http://purl.uniprot.org/annotation/PRO_0000070344|||http://purl.uniprot.org/annotation/PRO_5003052594|||http://purl.uniprot.org/annotation/PRO_5003052634|||http://purl.uniprot.org/annotation/PRO_5003052648|||http://purl.uniprot.org/annotation/VSP_010121|||http://purl.uniprot.org/annotation/VSP_010122|||http://purl.uniprot.org/annotation/VSP_010123|||http://purl.uniprot.org/annotation/VSP_022138|||http://purl.uniprot.org/annotation/VSP_022139|||http://purl.uniprot.org/annotation/VSP_022140|||http://purl.uniprot.org/annotation/VSP_022141|||http://purl.uniprot.org/annotation/VSP_022142 http://togogenome.org/gene/10090:Pgr15l ^@ http://purl.uniprot.org/uniprot/Q80T54 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Mmut ^@ http://purl.uniprot.org/uniprot/P16332|||http://purl.uniprot.org/uniprot/Q9CSI4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Transit Peptide ^@ B12-binding|||Methylmalonyl-CoA mutase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000019295 http://togogenome.org/gene/10090:Rab5a ^@ http://purl.uniprot.org/uniprot/Q9CQD1 ^@ 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 ^@ Disordered|||Effector region|||Induces the formation of larger endosomes. No effect on interaction with INPP5F. Prevents interaction with DYN2 without affecting the interaction with PIK3C3.|||Inhibits endosome localization. Disrupts interaction of RAB5A and OCRL with INPP5F. Prevents its localization to apoptotic cell corpse-containing early phagosomes. Maturation of apoptotic cell-containing phagosome into acidic phagosomes is decreased. Interacts with PIK3C3.|||Phosphoserine|||Ras-related protein Rab-5A|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121106 http://togogenome.org/gene/10090:Gria4 ^@ http://purl.uniprot.org/uniprot/E9PX01|||http://purl.uniprot.org/uniprot/Q8C069|||http://purl.uniprot.org/uniprot/Q9Z2W8 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Glutamate receptor 4|||Helical|||Helical; Name=M4|||Helical; Pore-forming|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Receptor ligand binding region|||Receptor ligand binding region domain-containing protein|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000011539|||http://purl.uniprot.org/annotation/PRO_5003243006|||http://purl.uniprot.org/annotation/PRO_5004304287 http://togogenome.org/gene/10090:Ssty1 ^@ http://purl.uniprot.org/uniprot/P13675 ^@ Chain|||Molecule Processing ^@ Chain ^@ Y-linked testis-specific protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000181372 http://togogenome.org/gene/10090:Atxn2 ^@ http://purl.uniprot.org/uniprot/E9QM77|||http://purl.uniprot.org/uniprot/O70305|||http://purl.uniprot.org/uniprot/Q3UX07 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Asymmetric dimethylarginine; alternate|||Ataxin-2|||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.|||LsmAD|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Sm ^@ http://purl.uniprot.org/annotation/PRO_0000064757|||http://purl.uniprot.org/annotation/VSP_011583|||http://purl.uniprot.org/annotation/VSP_011584 http://togogenome.org/gene/10090:Lamp1 ^@ http://purl.uniprot.org/uniprot/P11438|||http://purl.uniprot.org/uniprot/Q3TA96|||http://purl.uniprot.org/uniprot/Q3TX84|||http://purl.uniprot.org/uniprot/Q9DC13 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||First lumenal domain|||Helical|||Hinge|||Lumenal|||Lysosome-associated membrane glycoprotein 1|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Pro residues|||Second lumenal domain ^@ http://purl.uniprot.org/annotation/PRO_0000017105|||http://purl.uniprot.org/annotation/PRO_5004229670|||http://purl.uniprot.org/annotation/PRO_5010847756|||http://purl.uniprot.org/annotation/PRO_5014309136 http://togogenome.org/gene/10090:Gm14296 ^@ http://purl.uniprot.org/uniprot/A2ARL4|||http://purl.uniprot.org/uniprot/D3YYR3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Rhox12 ^@ http://purl.uniprot.org/uniprot/Q4TU81 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Sec62 ^@ http://purl.uniprot.org/uniprot/Q8BU14 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Phosphoserine|||Phosphothreonine|||Translocation protein SEC62 ^@ http://purl.uniprot.org/annotation/PRO_0000206617 http://togogenome.org/gene/10090:Tex101 ^@ http://purl.uniprot.org/uniprot/Q9JMI7 ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Signal Peptide|||Strand|||Turn ^@ GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Testis-expressed protein 101|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000247623|||http://purl.uniprot.org/annotation/PRO_0000247624 http://togogenome.org/gene/10090:Or5b111 ^@ http://purl.uniprot.org/uniprot/Q7TQR2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gstp2 ^@ http://purl.uniprot.org/uniprot/P46425 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase P 2 ^@ http://purl.uniprot.org/annotation/PRO_0000185904 http://togogenome.org/gene/10090:Zbtb26 ^@ http://purl.uniprot.org/uniprot/Q6P9Q3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB|||Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ube2u ^@ http://purl.uniprot.org/uniprot/B1AUC4|||http://purl.uniprot.org/uniprot/B7ZWG1|||http://purl.uniprot.org/uniprot/Q3V081 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||UBC core ^@ http://togogenome.org/gene/10090:Clec4d ^@ http://purl.uniprot.org/uniprot/Q3UBK0|||http://purl.uniprot.org/uniprot/Q4KL29|||http://purl.uniprot.org/uniprot/Q9Z2H6 ^@ 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|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 4 member D|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046617 http://togogenome.org/gene/10090:Gphn ^@ http://purl.uniprot.org/uniprot/A0JNY3|||http://purl.uniprot.org/uniprot/Q8BUV3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Gephyrin|||Interaction with GABARAP|||MPT Mo-transferase|||MPT adenylyltransferase|||MoaB/Mog|||Phosphoserine|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000269039 http://togogenome.org/gene/10090:Aplp1 ^@ http://purl.uniprot.org/uniprot/Q03157|||http://purl.uniprot.org/uniprot/Q3TUB1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Amyloid beta precursor like protein 1|||Amyloid-like protein 1|||Basolateral sorting signal|||C30|||Cleavage; by caspase-3|||Collagen-binding|||CuBD subdomain|||Cytoplasmic|||Disordered|||E1|||E2|||Extracellular|||GFLD subdomain|||Helical|||Heparin-binding|||Interaction with DAB1|||Interaction with DAB2|||N-linked (GlcNAc...) asparagine|||NPXY motif; contains endocytosis signal|||Polar residues|||Reduced binding of APBB1. ^@ http://purl.uniprot.org/annotation/PRO_0000000205|||http://purl.uniprot.org/annotation/PRO_0000000206|||http://purl.uniprot.org/annotation/PRO_5004229622 http://togogenome.org/gene/10090:Sgpl1 ^@ http://purl.uniprot.org/uniprot/Q8R0X7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 3'-nitrotyrosine|||Cytoplasmic|||Helical; Signal-anchor for type III membrane protein|||Lumenal|||N6-(pyridoxal phosphate)lysine; alternate|||N6-acetyllysine; alternate|||Phosphoserine|||Sphingosine-1-phosphate lyase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000147013 http://togogenome.org/gene/10090:Eif1ax ^@ http://purl.uniprot.org/uniprot/Q8BMJ3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Eukaryotic translation initiation factor 1A, X-chromosomal|||S1-like ^@ http://purl.uniprot.org/annotation/PRO_0000145107 http://togogenome.org/gene/10090:Ly6m ^@ http://purl.uniprot.org/uniprot/Q9CQ11 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_5015099699 http://togogenome.org/gene/10090:Gm7361 ^@ http://purl.uniprot.org/uniprot/D3Z6R1 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Defa40 ^@ http://purl.uniprot.org/uniprot/L7N231 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Mammalian defensins ^@ http://purl.uniprot.org/annotation/PRO_5003982284 http://togogenome.org/gene/10090:Pnma8b ^@ http://purl.uniprot.org/uniprot/G3X9N3 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Basic residues|||Disordered ^@ http://togogenome.org/gene/10090:Marchf5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1H0|||http://purl.uniprot.org/uniprot/A2RTC8|||http://purl.uniprot.org/uniprot/Q3KNM2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ E3 ubiquitin-protein ligase MARCHF5|||Helical|||RING-CH-type ^@ http://purl.uniprot.org/annotation/PRO_0000271770 http://togogenome.org/gene/10090:Or5ac21 ^@ http://purl.uniprot.org/uniprot/A0A1L1SSG9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp560 ^@ http://purl.uniprot.org/uniprot/Q3URI6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ercc6l ^@ http://purl.uniprot.org/uniprot/Q8BHK9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||DEAH box|||DNA excision repair protein ERCC-6-like|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TPR 1|||TPR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000328832 http://togogenome.org/gene/10090:Sult2a5 ^@ http://purl.uniprot.org/uniprot/K7N6K9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Arhgap32 ^@ http://purl.uniprot.org/uniprot/Q811P8 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Does not affect RhoA or CDC42 activity.|||In isoform 2.|||Interaction with FYN|||Interaction with GAB2|||Omega-N-methylarginine|||PX; atypical|||Phosphoserine|||Polar residues|||Rho GTPase-activating protein 32|||Rho-GAP|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000345204|||http://purl.uniprot.org/annotation/VSP_034937 http://togogenome.org/gene/10090:Ereg ^@ http://purl.uniprot.org/uniprot/Q61521 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EGF-like|||Epiregulin|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Proepiregulin|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000007559|||http://purl.uniprot.org/annotation/PRO_0000007560|||http://purl.uniprot.org/annotation/PRO_0000007561|||http://purl.uniprot.org/annotation/PRO_0000302801 http://togogenome.org/gene/10090:Btaf1 ^@ http://purl.uniprot.org/uniprot/E9QAE3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Rbbp6 ^@ http://purl.uniprot.org/uniprot/A0A0R4J165|||http://purl.uniprot.org/uniprot/P97868 ^@ 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 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.|||Interaction with RB1|||Interaction with p53|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000234355|||http://purl.uniprot.org/annotation/VSP_018285|||http://purl.uniprot.org/annotation/VSP_018286|||http://purl.uniprot.org/annotation/VSP_018287 http://togogenome.org/gene/10090:Nanog ^@ http://purl.uniprot.org/uniprot/A2RS90|||http://purl.uniprot.org/uniprot/B7ZN41|||http://purl.uniprot.org/uniprot/Q80Z64 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 1|||10|||10 X repeats starting with a Trp in each unit|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Decreased protein expression and stability.|||Decreased protein expression and stability. Decreased embryonic stem cell self-renewal.|||Decreased protein expression. Decreased embryonic stem cell self-renewal.|||Decreased protein expression. No effect on protein stability.|||Decreased protein stability.|||Decreased protein stability. Decreased embryonic stem cell self-renewal.|||Disordered|||Homeobox|||Homeobox protein NANOG|||In isoform 2.|||Increased protein expression and stability.|||Increased protein expression. Decreased protein stability.|||Increased protein expression. No effect on protein stability.|||Increases affinity for DNA and protein stability; when associated with E-112.|||Increases affinity for DNA and protein stability; when associated with R-147.|||Increases affinity for DNA; when associated with E-137.|||Increases affinity for DNA; when associated with R-126.|||No effect on protein stability.|||No effect on protein stability. Decreased embryonic stem cell self-renewal.|||Polar residues|||Reduced affinity for DNA.|||Required for DNA-binding|||Slightly reduced affinity for DNA.|||Strongly reduced affinity for DNA.|||Sufficient for interaction with SALL4|||Sufficient for strong transactivation activity|||Sufficient for transactivation activity ^@ http://purl.uniprot.org/annotation/PRO_0000261419|||http://purl.uniprot.org/annotation/VSP_021689 http://togogenome.org/gene/10090:Vmn1r126 ^@ http://purl.uniprot.org/uniprot/L7N2C8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Aff2 ^@ http://purl.uniprot.org/uniprot/O55112 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ AF4/FMR2 family member 2|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000215913 http://togogenome.org/gene/10090:Ism1 ^@ http://purl.uniprot.org/uniprot/V9GXR4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ AMOP|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5004776067 http://togogenome.org/gene/10090:Slc15a1 ^@ http://purl.uniprot.org/uniprot/Q14BA3|||http://purl.uniprot.org/uniprot/Q3UWE2|||http://purl.uniprot.org/uniprot/Q9JIP7 ^@ Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Does not affect trypsin-binding.|||Extracellular|||Extracellular domain (ECD)|||Helical|||N-linked (GlcNAc...) asparagine|||Reduced trypsin-binding; when associated with A-550.|||Reduced trypsin-binding; when associated with A-573.|||Solute carrier family 15 member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000064305 http://togogenome.org/gene/10090:Ubl4b ^@ http://purl.uniprot.org/uniprot/Q9CQ84 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||Ubiquitin-like|||Ubiquitin-like protein 4B ^@ http://purl.uniprot.org/annotation/PRO_0000263702 http://togogenome.org/gene/10090:Esr1 ^@ http://purl.uniprot.org/uniprot/E7FJU2|||http://purl.uniprot.org/uniprot/P19785 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger ^@ Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-512.|||Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-515.|||Abolishes DNA-binding, abolishes transcriptional activity and estrogen-dependent NF-kappa B transcriptional repression; when associated with E-512 and E-515.|||Abolishes estrogen binding; impairs repression of NF-kappa activity.|||Abolishes estrogen-dependent NF-kappa B transcriptional repression, abolishes estrogen-induced interaction with NCOA1.|||Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, abolishes estrogen-induced interaction with NCOA1.|||Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, impairs estrogen-induced interaction with NCOA1; when associated with N-542 and N-548.|||Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, impairs estrogen-induced interaction with NCOA1; when associated with N-542 and Q-546.|||Abolishes estrogen-dependent NF-kappa B transcriptional repression, impairs transcriptional activity, impairs estrogen-induced interaction with NCOA1; when associated with Q-546 and N-548.|||Abolishes estrogen-induced interaction with NCOA1.|||Abolishes transcriptional activity and estrogen-induced interaction with NCOA1.|||Asymmetric dimethylarginine; by PRMT1|||Disordered|||Estrogen receptor|||Greatly reduces transcriptional activity and estrogen-induced interaction with NCOA1.|||Hinge|||In strain: SJL/J.|||Interaction with AKAP13|||Interaction with DDX5; self-association|||Loss of ZDHHC7 and ZDHHC21 binding. Loss of palmitoylation.|||Mediates interaction with DNTTIP2|||Modulating (transactivation AF-1); mediates interaction with MACROD1|||NR C4-type|||NR LBD|||No effect on estrogen-dependent NF-kappa B transcriptional repression, greatly impairs transcriptional activity, abolishes estrogen-induced interaction with NCOA1.|||No effect on transcriptional activity and estrogen-induced interaction with NCOA1. Abolishes estrogen-induced interaction with NCOA1; when associated with A-362 and A-376.|||No effect on transcriptional activity and estrogen-induced interaction with NCOA1. Abolishes estrogen-induced interaction with NCOA1; when associated with A-376 and A-380.|||Nuclear receptor|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphoserine; by CK2|||Phosphotyrosine; by Tyr-kinases|||Polar residues|||Reduces DNA-binding, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-512.|||Reduces DNA-binding, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression; when associated with E-508 and E-515.|||Reduces DNA-binding, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression; when associated with E-512 and E-515.|||Reduces DNA-binding,, attenuates transcriptional activity, does not effect estrogen-dependent NF-kappa B transcriptional repression.|||Reduces transcriptional activity and estrogen-induced interaction with NCOA1.|||Reduces transcriptional activity, no effect on estrogen-induced interaction with NCOA1. Abolishes estrogen-induced interaction with NCOA1; when associated with A-362 and A-380.|||Required for interaction with NCOA1|||S-palmitoyl cysteine|||Self-association|||Transactivation AF-2 ^@ http://purl.uniprot.org/annotation/CAR_000137|||http://purl.uniprot.org/annotation/PRO_0000053621 http://togogenome.org/gene/10090:Pah ^@ http://purl.uniprot.org/uniprot/P16331|||http://purl.uniprot.org/uniprot/Q3UEH8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ ACT|||Biopterin-dependent aromatic amino acid hydroxylase family profile|||Mutant mice have features of phenylketonuria.|||Mutant mice have mild features of phenylketonuria.|||N-acetylalanine|||Phenylalanine-4-hydroxylase|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000205549 http://togogenome.org/gene/10090:Tmem80 ^@ http://purl.uniprot.org/uniprot/Q9D3H0 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Transmembrane protein 80 ^@ http://purl.uniprot.org/annotation/PRO_0000287874|||http://purl.uniprot.org/annotation/VSP_025611 http://togogenome.org/gene/10090:Calr4 ^@ http://purl.uniprot.org/uniprot/A2A8Z3|||http://purl.uniprot.org/uniprot/G5CPP0|||http://purl.uniprot.org/uniprot/Q3TQS0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Calreticulin|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5009996794|||http://purl.uniprot.org/annotation/PRO_5015020010 http://togogenome.org/gene/10090:Heatr9 ^@ http://purl.uniprot.org/uniprot/Q5QNV8 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein HEATR9 ^@ http://purl.uniprot.org/annotation/PRO_0000287178 http://togogenome.org/gene/10090:Lrrc27 ^@ http://purl.uniprot.org/uniprot/D3Z4R3|||http://purl.uniprot.org/uniprot/Q80YS5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Leucine-rich repeat-containing protein 27 ^@ http://purl.uniprot.org/annotation/PRO_0000076243 http://togogenome.org/gene/10090:Tigd4 ^@ http://purl.uniprot.org/uniprot/Q8BUZ3 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Region ^@ 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_0000272617 http://togogenome.org/gene/10090:1500009L16Rik ^@ http://purl.uniprot.org/uniprot/P0C913 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Overexpressed in colon carcinoma 1 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000368222 http://togogenome.org/gene/10090:Siglech ^@ http://purl.uniprot.org/uniprot/A0A4W8|||http://purl.uniprot.org/uniprot/A0A4X5|||http://purl.uniprot.org/uniprot/B7ZMQ5|||http://purl.uniprot.org/uniprot/G3X9N0|||http://purl.uniprot.org/uniprot/Q3Y597|||http://purl.uniprot.org/uniprot/Q4QQK7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like|||Ig-like domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5002621971|||http://purl.uniprot.org/annotation/PRO_5004230615|||http://purl.uniprot.org/annotation/PRO_5015087432|||http://purl.uniprot.org/annotation/PRO_5015091876|||http://purl.uniprot.org/annotation/PRO_5015097635 http://togogenome.org/gene/10090:Lancl3 ^@ http://purl.uniprot.org/uniprot/Q8CD19 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||LanC-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000285252|||http://purl.uniprot.org/annotation/VSP_024856 http://togogenome.org/gene/10090:Sumf1 ^@ http://purl.uniprot.org/uniprot/Q8R0F3 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Formylglycine-generating enzyme|||Interaction with sulfatases|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033457 http://togogenome.org/gene/10090:Kdm1b ^@ http://purl.uniprot.org/uniprot/Q8CIG3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||CW-type|||Disordered|||GLYR1-binding|||Histone H3-binding|||In isoform 2.|||In isoform 3.|||Loss of activity.|||Lysine-specific histone demethylase 1B|||Phosphoserine|||SWIRM ^@ http://purl.uniprot.org/annotation/PRO_0000247337|||http://purl.uniprot.org/annotation/VSP_019968|||http://purl.uniprot.org/annotation/VSP_019969 http://togogenome.org/gene/10090:Gm15085 ^@ http://purl.uniprot.org/uniprot/Q62012 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:S100a8 ^@ http://purl.uniprot.org/uniprot/P27005|||http://purl.uniprot.org/uniprot/Q53X15 ^@ 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|||EF-hand 1|||EF-hand 2|||Protein S100-A8|||Removed|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000143994 http://togogenome.org/gene/10090:Vmn1r118 ^@ http://purl.uniprot.org/uniprot/L7N273 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Abcf1 ^@ http://purl.uniprot.org/uniprot/Q6P542 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family F member 1|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphoserine; by CK2 ^@ http://purl.uniprot.org/annotation/PRO_0000093319 http://togogenome.org/gene/10090:Slc25a27 ^@ http://purl.uniprot.org/uniprot/Q9D6D0 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Repeat|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial uncoupling protein 4|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000458774 http://togogenome.org/gene/10090:9930104L06Rik ^@ http://purl.uniprot.org/uniprot/Q499E6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ AFG2-interacting ribosome maturation factor|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000274383|||http://purl.uniprot.org/annotation/VSP_022735|||http://purl.uniprot.org/annotation/VSP_022736 http://togogenome.org/gene/10090:Ankrd26 ^@ http://purl.uniprot.org/uniprot/D3Z482 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ ANK|||Basic and acidic residues|||CCDC144C-like coiled-coil|||DUF3496|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Fbxl5 ^@ http://purl.uniprot.org/uniprot/Q8C2S5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ F-box|||F-box/LRR-repeat protein 5|||Hemerythrin-like|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7 ^@ http://purl.uniprot.org/annotation/PRO_0000119846|||http://purl.uniprot.org/annotation/VSP_008418|||http://purl.uniprot.org/annotation/VSP_008419|||http://purl.uniprot.org/annotation/VSP_008420|||http://purl.uniprot.org/annotation/VSP_038529|||http://purl.uniprot.org/annotation/VSP_038530 http://togogenome.org/gene/10090:Grb2 ^@ http://purl.uniprot.org/uniprot/Q3U1Q4|||http://purl.uniprot.org/uniprot/Q3U5I5|||http://purl.uniprot.org/uniprot/Q60631 ^@ Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Splice Variant|||Strand ^@ Growth factor receptor-bound protein 2|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphothreonine|||SH2|||SH3|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000088199|||http://purl.uniprot.org/annotation/VSP_001841 http://togogenome.org/gene/10090:Dntt ^@ http://purl.uniprot.org/uniprot/P09838|||http://purl.uniprot.org/uniprot/Q3UZ80 ^@ 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 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Almost complete loss of exonuclease activity in TDT-L; when associated with A-170 and A-473. Decreased transferase activity in TDT-S; when associated with A-170 and A-473.|||Almost complete loss of exonuclease activity in TDT-L; when associated with A-29 and A-170. Decreased transferase activity in TDT-S; when associated with A-29 and A-170.|||Almost complete loss of exonuclease activity in TDT-L; when associated with A-29 and A-473. Decreased transferase activity in TDT-S; when associated with A-29 and A-473.|||BRCT|||DNA nucleotidylexotransferase|||Disordered|||In isoform TDT-L.|||Involved in DNA binding|||Mediates interaction with DNTTIP2|||Nearly abolishes enzyme activity.|||Nuclear localization signal|||Phosphoserine|||Reduces enzyme activity. ^@ http://purl.uniprot.org/annotation/PRO_0000218792|||http://purl.uniprot.org/annotation/VSP_059967 http://togogenome.org/gene/10090:Palm ^@ http://purl.uniprot.org/uniprot/Q3TRX4|||http://purl.uniprot.org/uniprot/Q542N8|||http://purl.uniprot.org/uniprot/Q8CB16|||http://purl.uniprot.org/uniprot/Q9Z0P4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||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_0000058219|||http://purl.uniprot.org/annotation/PRO_0000396690|||http://purl.uniprot.org/annotation/VSP_003919 http://togogenome.org/gene/10090:Prickle4 ^@ http://purl.uniprot.org/uniprot/D3Z6Q6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||LIM zinc-binding|||PET|||Polar residues ^@ http://togogenome.org/gene/10090:Prb1 ^@ http://purl.uniprot.org/uniprot/Q91X93 ^@ 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_5015099526 http://togogenome.org/gene/10090:Trpc4 ^@ http://purl.uniprot.org/uniprot/Q0VB97|||http://purl.uniprot.org/uniprot/Q8BNB6|||http://purl.uniprot.org/uniprot/Q8BNT2|||http://purl.uniprot.org/uniprot/Q9QUQ5 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Binds to ITPR1, ITPR2 and ITPR3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform Beta.|||Multimerization domain|||PDZ-binding domain|||Phosphotyrosine; by FYN|||Short transient receptor potential channel 4|||Transient receptor ion channel ^@ http://purl.uniprot.org/annotation/PRO_0000215315|||http://purl.uniprot.org/annotation/VSP_006570 http://togogenome.org/gene/10090:Ift22 ^@ http://purl.uniprot.org/uniprot/Q9DAI2 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Intraflagellar transport protein 22 homolog|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000253735 http://togogenome.org/gene/10090:Ncln ^@ http://purl.uniprot.org/uniprot/D3YU17|||http://purl.uniprot.org/uniprot/Q8VCM8 ^@ 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 ^@ BOS complex subunit NCLN|||Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Peptidase M28 ^@ http://purl.uniprot.org/annotation/PRO_0000019688 http://togogenome.org/gene/10090:Or8b1b ^@ http://purl.uniprot.org/uniprot/Q7TRC9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Steap4 ^@ http://purl.uniprot.org/uniprot/Q923B6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ Ferric oxidoreductase|||Helical|||Metalloreductase STEAP4|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000285175 http://togogenome.org/gene/10090:Gprin3 ^@ http://purl.uniprot.org/uniprot/B2RQZ6|||http://purl.uniprot.org/uniprot/Q8BWS5 ^@ 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|||G protein-regulated inducer of neurite outgrowth 3|||G protein-regulated inducer of neurite outgrowth C-terminal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000251951 http://togogenome.org/gene/10090:Gpld1 ^@ http://purl.uniprot.org/uniprot/Q8R432|||http://purl.uniprot.org/uniprot/Q8VCU2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Domain Extent|||Repeat|||Signal Peptide ^@ FG-GAP|||Phosphatidylinositol-glycan-specific phospholipase D|||Phospholipase C/D ^@ http://purl.uniprot.org/annotation/PRO_5004313014|||http://purl.uniprot.org/annotation/PRO_5015099431 http://togogenome.org/gene/10090:Catsper4 ^@ http://purl.uniprot.org/uniprot/B3VNK5|||http://purl.uniprot.org/uniprot/Q8BVN3 ^@ Chain|||Domain Extent|||Helix|||INTRAMEM|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Helix|||INTRAMEM|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cation channel sperm-associated protein 4|||Cytoplasmic|||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|||Ion transport ^@ http://purl.uniprot.org/annotation/PRO_0000295682 http://togogenome.org/gene/10090:Mbd2 ^@ http://purl.uniprot.org/uniprot/Q9Z2E1 ^@ 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 residues|||Disordered|||In isoform 2.|||MBD|||Methyl-CpG-binding domain protein 2|||Phosphoserine|||Required for interaction with DHX9 and PRMT5 ^@ http://purl.uniprot.org/annotation/PRO_0000096261|||http://purl.uniprot.org/annotation/VSP_011079|||http://purl.uniprot.org/annotation/VSP_011080 http://togogenome.org/gene/10090:Crhr1 ^@ http://purl.uniprot.org/uniprot/K9J9G1|||http://purl.uniprot.org/uniprot/P35347|||http://purl.uniprot.org/uniprot/Q0VGH2|||http://purl.uniprot.org/uniprot/Q3ZAT0 ^@ 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 ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKA ^@ http://purl.uniprot.org/annotation/PRO_0000012815|||http://purl.uniprot.org/annotation/PRO_5003931449|||http://purl.uniprot.org/annotation/PRO_5014309266 http://togogenome.org/gene/10090:Vmn2r94 ^@ http://purl.uniprot.org/uniprot/E9PZK8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://togogenome.org/gene/10090:Brf2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0C6|||http://purl.uniprot.org/uniprot/Q3UAW9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ 1|||2|||Cysteine sulfenic acid (-SOH)|||Disordered|||Interaction with target DNA|||Phosphoserine|||Polar residues|||Pro residues|||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_0000337189 http://togogenome.org/gene/10090:Fbrsl1 ^@ http://purl.uniprot.org/uniprot/E9PUB6|||http://purl.uniprot.org/uniprot/E9Q9T0|||http://purl.uniprot.org/uniprot/Q8CCX0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Ninj1 ^@ http://purl.uniprot.org/uniprot/O70131|||http://purl.uniprot.org/uniprot/Q3TXT8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Abolished ability to induce plasma membrane rupture in response to death stimuli.|||Cleavage; by MMP9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Helix alpha3|||Helical;Name=Helix alpha4|||Helix alpha1|||Helix alpha2|||Impaired N-glycosylation and reduced homooligomerization.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||N-terminal adhesion motif|||Ninjurin-1|||Phosphoserine|||Required to induce plasma membrane rupture|||Secreted ninjurin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000159644|||http://purl.uniprot.org/annotation/PRO_0000452825 http://togogenome.org/gene/10090:Mfhas1 ^@ http://purl.uniprot.org/uniprot/Q3V1N1 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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|||Malignant fibrous histiocytoma-amplified sequence 1 homolog|||N-acetylalanine|||N6-acetyllysine|||Removed|||Required for interaction with PJA2|||Required for interaction with PPP2R2A|||Roc ^@ http://purl.uniprot.org/annotation/PRO_0000308610 http://togogenome.org/gene/10090:Ccl21d ^@ http://purl.uniprot.org/uniprot/P86792|||http://purl.uniprot.org/uniprot/P86793 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Region|||Sequence Conflict|||Signal Peptide ^@ C-C motif chemokine 21b|||C-C motif chemokine 21c|||C-terminal basic extension|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000005222|||http://purl.uniprot.org/annotation/PRO_0000403422 http://togogenome.org/gene/10090:Nccrp1 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ97|||http://purl.uniprot.org/uniprot/G3X9C2 ^@ 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|||F-box only protein 50|||FBA|||Phosphoserine|||Phosphothreonine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000421450 http://togogenome.org/gene/10090:4933412E24Rik ^@ http://purl.uniprot.org/uniprot/Q9D454 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Polar residues|||Uncharacterized protein CXorf49 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000343896 http://togogenome.org/gene/10090:Aknad1 ^@ http://purl.uniprot.org/uniprot/E9Q8N6|||http://purl.uniprot.org/uniprot/Q3TPF6|||http://purl.uniprot.org/uniprot/Q3UXF3|||http://purl.uniprot.org/uniprot/Q8BI23 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ AKNA|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Npy4r ^@ http://purl.uniprot.org/uniprot/Q61041 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||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|||Neuropeptide Y receptor type 4|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069936 http://togogenome.org/gene/10090:Alx3 ^@ http://purl.uniprot.org/uniprot/O70137|||http://purl.uniprot.org/uniprot/Q3UQX2 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Homeobox protein aristaless-like 3|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000048813 http://togogenome.org/gene/10090:Hhipl2 ^@ http://purl.uniprot.org/uniprot/Q9D2G9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ Basic residues|||Disordered|||HHIP-like protein 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314965|||http://purl.uniprot.org/annotation/VSP_030459 http://togogenome.org/gene/10090:Abcb11 ^@ http://purl.uniprot.org/uniprot/Q9QY30 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||Basic and acidic residues|||Bile salt export pump|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with HAX1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000093297 http://togogenome.org/gene/10090:Eif4e1b ^@ http://purl.uniprot.org/uniprot/E9PVZ9|||http://purl.uniprot.org/uniprot/E9Q929|||http://purl.uniprot.org/uniprot/Q3UTA9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||EIF4EBP1/2/3 binding|||Eukaryotic translation initiation factor 4E type 1B|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000342514|||http://purl.uniprot.org/annotation/VSP_034476|||http://purl.uniprot.org/annotation/VSP_034477 http://togogenome.org/gene/10090:Zmat5 ^@ http://purl.uniprot.org/uniprot/Q9CQR5 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Zinc Finger ^@ C3H1-type|||Zinc finger matrin-type protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000254115 http://togogenome.org/gene/10090:Atp6v1h ^@ http://purl.uniprot.org/uniprot/A0A0A6YX18|||http://purl.uniprot.org/uniprot/Q8BVE3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ ATPase V1 complex subunit H C-terminal|||Phosphoserine|||V-type proton ATPase subunit H ^@ http://purl.uniprot.org/annotation/PRO_0000124194 http://togogenome.org/gene/10090:Tceal7 ^@ http://purl.uniprot.org/uniprot/A3KGA4 ^@ 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_0000404650 http://togogenome.org/gene/10090:St3gal4 ^@ http://purl.uniprot.org/uniprot/Q91Y74 ^@ 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 ^@ CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149263 http://togogenome.org/gene/10090:Or4k77 ^@ http://purl.uniprot.org/uniprot/Q7TQY4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bnip3l ^@ http://purl.uniprot.org/uniprot/Q9Z2F7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Transmembrane ^@ BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like|||BH3|||Disordered|||Helical|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064958 http://togogenome.org/gene/10090:Gdpd4 ^@ http://purl.uniprot.org/uniprot/Q3TT99 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||GP-PDE|||Glycerophosphodiester phosphodiesterase domain-containing protein 4|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000251940 http://togogenome.org/gene/10090:Kif1a ^@ http://purl.uniprot.org/uniprot/E9Q9G6|||http://purl.uniprot.org/uniprot/E9QAN4|||http://purl.uniprot.org/uniprot/G3UW47|||http://purl.uniprot.org/uniprot/Q3UH16|||http://purl.uniprot.org/uniprot/Q6P5H4|||http://purl.uniprot.org/uniprot/Q6TA13 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||FHA|||Kinesin motor|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Frk ^@ http://purl.uniprot.org/uniprot/Q922K9 ^@ 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|||Strand|||Turn ^@ Phosphothreonine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SH2|||SH3|||Tyrosine-protein kinase FRK ^@ http://purl.uniprot.org/annotation/PRO_0000260826 http://togogenome.org/gene/10090:Spice1 ^@ http://purl.uniprot.org/uniprot/Q8C804 ^@ 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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Spindle and centriole-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000282414 http://togogenome.org/gene/10090:Lce1f ^@ http://purl.uniprot.org/uniprot/B9EJP6|||http://purl.uniprot.org/uniprot/Q9D1I4 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Prkra ^@ http://purl.uniprot.org/uniprot/Q9WTX2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ DRBM 1|||DRBM 2|||DRBM 3|||Disordered|||Interferon-inducible double-stranded RNA-dependent protein kinase activator A|||Phosphoserine|||Sufficient for self-association and interaction with TARBP2 ^@ http://purl.uniprot.org/annotation/PRO_0000223610 http://togogenome.org/gene/10090:Slc25a1 ^@ http://purl.uniprot.org/uniprot/Q8JZU2 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Phosphoserine|||Removed in mature form|||Solcar 1|||Solcar 2|||Solcar 3|||Tricarboxylate transport protein, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000430571|||http://purl.uniprot.org/annotation/PRO_0000456576 http://togogenome.org/gene/10090:Ermap ^@ http://purl.uniprot.org/uniprot/A2A7P7|||http://purl.uniprot.org/uniprot/Q9JLN5 ^@ 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 ^@ B30.2/SPRY|||Cytoplasmic|||Erythroid membrane-associated protein|||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_0000226089|||http://purl.uniprot.org/annotation/VSP_017425|||http://purl.uniprot.org/annotation/VSP_017426|||http://purl.uniprot.org/annotation/VSP_017427 http://togogenome.org/gene/10090:Pld3 ^@ http://purl.uniprot.org/uniprot/O35405 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 5'-3' exonuclease PLD3|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000280328 http://togogenome.org/gene/10090:Gatad1 ^@ http://purl.uniprot.org/uniprot/Q920S3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Splice 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 isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288910|||http://purl.uniprot.org/annotation/VSP_025823|||http://purl.uniprot.org/annotation/VSP_025824 http://togogenome.org/gene/10090:Vcp ^@ http://purl.uniprot.org/uniprot/Q01853 ^@ Binding 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with UBXN6|||Loss of phospholipid-binding.|||N-acetylalanine|||N6,N6,N6-trimethyllysine; by VCPKMT|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||PIM motif|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Transitional endoplasmic reticulum ATPase ^@ http://purl.uniprot.org/annotation/PRO_0000084573 http://togogenome.org/gene/10090:Cyp39a1 ^@ http://purl.uniprot.org/uniprot/A0A3B2WCK5|||http://purl.uniprot.org/uniprot/Q544S6|||http://purl.uniprot.org/uniprot/Q9JKJ9 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ 24-hydroxycholesterol 7-alpha-hydroxylase|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051993 http://togogenome.org/gene/10090:Pgpep1 ^@ http://purl.uniprot.org/uniprot/Q9ESW8 ^@ Active Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Chain ^@ Pyroglutamyl-peptidase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000184762 http://togogenome.org/gene/10090:Or51f23b ^@ http://purl.uniprot.org/uniprot/A0A1B0GSU5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wnt3a ^@ http://purl.uniprot.org/uniprot/P27467 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Signal Peptide|||Site ^@ Abolishes palmitoleoylation, promoting formation of disulfide bonds and oligomerization.|||Cleavage; by TIKI1 and TIKI2|||Completely resistant to proteolysis by TIKI1 and TIKI2; when associated with 25-D-D-26.|||Does not affect palmitoleoylation.|||Forms oxidized oligomers regardless of TIKI2. Does not affect palmitoleoylation.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Partially resistant to proteolysis by TIKI1 and TIKI2. Completely resistant to proteolysis by TIKI1 and TIKI2; when associated with 33-D-D-34.|||Protein Wnt-3a ^@ http://purl.uniprot.org/annotation/PRO_0000041419 http://togogenome.org/gene/10090:Vmn2r21 ^@ http://purl.uniprot.org/uniprot/K7N6Y7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908816 http://togogenome.org/gene/10090:Nol4l ^@ http://purl.uniprot.org/uniprot/Q3TZG8|||http://purl.uniprot.org/uniprot/Q3UH85|||http://purl.uniprot.org/uniprot/Q52KQ8 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Clec12a ^@ http://purl.uniprot.org/uniprot/A0A0R4J0T2|||http://purl.uniprot.org/uniprot/Q504P2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 12 member A|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||ITIM motif|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000313579 http://togogenome.org/gene/10090:Atp5g2 ^@ http://purl.uniprot.org/uniprot/P56383 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide|||Transmembrane ^@ Chain|||Modified Residue|||Site|||Transit Peptide|||Transmembrane ^@ ATP synthase F(0) complex subunit C2, mitochondrial|||Helical|||Mitochondrion|||N6,N6,N6-trimethyllysine|||Reversibly protonated during proton transport ^@ http://purl.uniprot.org/annotation/PRO_0000002563 http://togogenome.org/gene/10090:Creg1 ^@ http://purl.uniprot.org/uniprot/O88668 ^@ 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|||N-linked (GlcNAc...) asparagine|||Protein CREG1 ^@ http://purl.uniprot.org/annotation/PRO_0000006204 http://togogenome.org/gene/10090:Trmt12 ^@ http://purl.uniprot.org/uniprot/Q8BG71 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ tRNA wybutosine-synthesizing protein 2 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000281838 http://togogenome.org/gene/10090:Myorg ^@ http://purl.uniprot.org/uniprot/Q69ZQ1 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Myogenesis-regulating glycosidase|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000295753 http://togogenome.org/gene/10090:Lztfl1 ^@ http://purl.uniprot.org/uniprot/Q9JHQ5 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict ^@ Interaction with BSS9|||Leucine zipper transcription factor-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000318760 http://togogenome.org/gene/10090:H2al1e ^@ http://purl.uniprot.org/uniprot/Q810S6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Histone H2A/H2B/H3 ^@ http://togogenome.org/gene/10090:Zfp865 ^@ http://purl.uniprot.org/uniprot/H9KUY5|||http://purl.uniprot.org/uniprot/Q3U3I9 ^@ 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|||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_0000404595 http://togogenome.org/gene/10090:Igfbp3 ^@ http://purl.uniprot.org/uniprot/P47878|||http://purl.uniprot.org/uniprot/Q3UR87 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||IGFBP N-terminal|||Insulin-like growth factor-binding protein 3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000014379 http://togogenome.org/gene/10090:Ecd ^@ http://purl.uniprot.org/uniprot/Q9CS74 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Acidic region required for transactivation activity|||Acidic residues|||Basic and acidic residues|||Disordered|||Involved in nuclear export|||Phosphoserine|||Protein ecdysoneless homolog|||Transcription activation ^@ http://purl.uniprot.org/annotation/PRO_0000220845 http://togogenome.org/gene/10090:Bmp8a ^@ http://purl.uniprot.org/uniprot/P34821|||http://purl.uniprot.org/uniprot/Q3TZB2|||http://purl.uniprot.org/uniprot/Q80VZ0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Bone morphogenetic protein 8A|||Disordered|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile|||TGF-beta family profile domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000033884|||http://purl.uniprot.org/annotation/PRO_0000033885|||http://purl.uniprot.org/annotation/PRO_5004229696|||http://purl.uniprot.org/annotation/PRO_5015098943|||http://purl.uniprot.org/annotation/VSP_046527 http://togogenome.org/gene/10090:Ina ^@ http://purl.uniprot.org/uniprot/P46660 ^@ 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 ^@ Alpha-internexin|||Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Linker 1|||Linker 2|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063784 http://togogenome.org/gene/10090:Kcnb2 ^@ http://purl.uniprot.org/uniprot/A6H8H5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Potassium voltage-gated channel subfamily B member 2|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000320104 http://togogenome.org/gene/10090:Niban1 ^@ http://purl.uniprot.org/uniprot/Q3UW53 ^@ 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|||Polar residues|||Protein Niban 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000355583 http://togogenome.org/gene/10090:Tmf1 ^@ http://purl.uniprot.org/uniprot/B9EKI3 ^@ 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|||Disordered|||Interaction with Elongin BC complex|||Phosphoserine|||Phosphothreonine|||Polar residues|||TATA element modulatory factor ^@ http://purl.uniprot.org/annotation/PRO_0000376797 http://togogenome.org/gene/10090:Caml ^@ http://purl.uniprot.org/uniprot/P49070 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Guided entry of tail-anchored proteins factor CAMLG|||Helical|||Impaired tail-anchored protein insertion and a shift from GET1-CAMLG heterotetramerization to formation of heterodimers but does not affect recruitment of GET3 to the endoplasmic reticulum; when associated with A-202.|||Impaired tail-anchored protein insertion and a shift from GET1-CAMLG heterotetramerization to formation of heterodimers but does not affect recruitment of GET3 to the endoplasmic reticulum; when associated with A-207.|||Lumenal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000089292 http://togogenome.org/gene/10090:Rpl35a ^@ http://purl.uniprot.org/uniprot/O55142 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Large ribosomal subunit protein eL33|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000192798 http://togogenome.org/gene/10090:Rala ^@ http://purl.uniprot.org/uniprot/P63321 ^@ 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|||Phosphoserine|||Ras-related protein Ral-A|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000082694|||http://purl.uniprot.org/annotation/PRO_0000281345 http://togogenome.org/gene/10090:Aqr ^@ http://purl.uniprot.org/uniprot/A2AQA7|||http://purl.uniprot.org/uniprot/Q8CFQ3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ DNA2/NAM7 helicase helicase|||DNA2/NAM7 helicase-like C-terminal|||Disordered|||Helical region with structural similarity to ARM repeat domains|||Intron-binding protein aquarius N-terminal|||N6-acetyllysine|||Polar residues|||RNA helicase aquarius|||Required for assembly of the IB complex ^@ http://purl.uniprot.org/annotation/PRO_0000252390 http://togogenome.org/gene/10090:Kcnj8 ^@ http://purl.uniprot.org/uniprot/A0A0J9YMM3|||http://purl.uniprot.org/uniprot/P97794|||http://purl.uniprot.org/uniprot/Q3U118 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ ATP-sensitive inward rectifier potassium channel 8|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Inward rectifier potassium channel C-terminal|||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_0000154948 http://togogenome.org/gene/10090:Fkbp7 ^@ http://purl.uniprot.org/uniprot/O54998|||http://purl.uniprot.org/uniprot/Q3UU11 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide ^@ Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||N-linked (GlcNAc...) asparagine|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP7|||Prevents secretion from ER|||peptidylprolyl isomerase ^@ http://purl.uniprot.org/annotation/PRO_0000025514|||http://purl.uniprot.org/annotation/PRO_5014309170 http://togogenome.org/gene/10090:Scp2 ^@ http://purl.uniprot.org/uniprot/P32020 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Site|||Splice Variant ^@ Cleavage|||In isoform SCP2.|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||SCP2|||Sterol carrier protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000034093|||http://purl.uniprot.org/annotation/VSP_018895 http://togogenome.org/gene/10090:Rnd1 ^@ http://purl.uniprot.org/uniprot/Q8BLR7 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Splice Variant ^@ Cysteine methyl ester|||Effector region|||In isoform 2.|||In isoform 3.|||Removed in mature form|||Rho-related GTP-binding protein Rho6|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000198875|||http://purl.uniprot.org/annotation/PRO_0000281227|||http://purl.uniprot.org/annotation/VSP_012768|||http://purl.uniprot.org/annotation/VSP_012769 http://togogenome.org/gene/10090:Rpl5 ^@ http://purl.uniprot.org/uniprot/P47962|||http://purl.uniprot.org/uniprot/Q3TKR5|||http://purl.uniprot.org/uniprot/Q58EU6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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|||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_0000131433 http://togogenome.org/gene/10090:Tex38 ^@ http://purl.uniprot.org/uniprot/A2A8T7|||http://purl.uniprot.org/uniprot/D2D552 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Testis-expressed protein 38 ^@ http://purl.uniprot.org/annotation/PRO_0000322539 http://togogenome.org/gene/10090:Ppp2r5d ^@ http://purl.uniprot.org/uniprot/Q91V89 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rundc1 ^@ http://purl.uniprot.org/uniprot/Q0VDN7 ^@ 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|||Phosphoserine|||RUN|||RUN domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000284512 http://togogenome.org/gene/10090:Magi3 ^@ http://purl.uniprot.org/uniprot/G5E8T6|||http://purl.uniprot.org/uniprot/Q9EQJ9 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Guanylate kinase-like|||In 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|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||Phosphoserine|||Polar residues|||WW|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000341408|||http://purl.uniprot.org/annotation/VSP_034288|||http://purl.uniprot.org/annotation/VSP_034289 http://togogenome.org/gene/10090:Gm21379 ^@ http://purl.uniprot.org/uniprot/Q9D3U4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ RRM ^@ http://togogenome.org/gene/10090:Or6c219 ^@ http://purl.uniprot.org/uniprot/Q8VG46 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Adam29 ^@ http://purl.uniprot.org/uniprot/G3X9B5 ^@ Binding Site|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Site|||Transmembrane ^@ Binding Site|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Disintegrin|||Disordered|||Helical|||Peptidase M12B|||Polar residues ^@ http://togogenome.org/gene/10090:Pemt ^@ http://purl.uniprot.org/uniprot/Q61907 ^@ Binding Site|||Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||INTRAMEM|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Phosphatidylethanolamine N-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000193921|||http://purl.uniprot.org/annotation/VSP_053224 http://togogenome.org/gene/10090:Gla ^@ http://purl.uniprot.org/uniprot/Q3UM38|||http://purl.uniprot.org/uniprot/Q8BGZ6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Alpha galactosidase A C-terminal beta-sandwich ^@ http://togogenome.org/gene/10090:Rgs14 ^@ http://purl.uniprot.org/uniprot/P97492 ^@ 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 ^@ Disordered|||Does not affect subcellular location; when associated with A-261.|||Does not affect subcellular location; when associated with A-497.|||Does not reduce interaction with RAP2A. Strongly reduces interaction with RAP2A; when associated with L-336.|||GoLoco|||Inhibits GAP activity. Does not inhibit interaction with GNAI1 in the centrosomes. Reduces the down-regulation of G(i)-dependent signaling. Does not affect subcellular location and does not promote gene transcription activation. Inhibits strongly the down-regulation of G(i)-dependent signaling; when associated with F-519. Inhibits the interaction with GNAI1 in the centrosomes; when associated with A-518.|||Inhibits GDI activity. Does not inhibit interaction with GNAI1 in the centrosomes, does not affect subcellular location and does not promote gene transcription activation. Inhibits interaction with GNAI1 in the centrosomes; when associated with A-92-93-A.|||Necessary for interaction with RABGEF1|||Phosphoserine|||Phosphothreonine|||Polar residues|||RBD 1|||RBD 2|||RGS|||Reduces interaction with GNAI1 and GNAI2. Inhibits strongly the down-regulation of G(i)-dependent signaling; when associated with A-92-93-A.|||Reduces interaction with RABGEF1 and RAP2A. Strongly reduces interaction with RAP2A; when associated with L-409.|||Regulator of G-protein signaling 14|||Strongly expressed in the nucleus, mainly associated with PML nuclear bodies but not with centrosomes. Promotes gene transcription activation. ^@ http://purl.uniprot.org/annotation/PRO_0000204218 http://togogenome.org/gene/10090:Or1n1b ^@ http://purl.uniprot.org/uniprot/Q8VGK0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wipf1 ^@ http://purl.uniprot.org/uniprot/Q8K1I7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Asymmetric dimethylarginine|||Binds actin|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||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_0000065942 http://togogenome.org/gene/10090:Cuedc2 ^@ http://purl.uniprot.org/uniprot/A0A494BAT2|||http://purl.uniprot.org/uniprot/A0A494BB93|||http://purl.uniprot.org/uniprot/Q9CVB0|||http://purl.uniprot.org/uniprot/Q9CXX9 ^@ 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 ^@ Basic and acidic residues|||CUE|||CUE domain-containing protein 2|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000282993 http://togogenome.org/gene/10090:Tpp1 ^@ http://purl.uniprot.org/uniprot/O89023 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Peptidase S53|||Premature lethality from 3 months of age, with no survival beyond 6 months. Progressive defects in motor coordination and balance from age 3 months, accompanied by a twitching phenotype. Marked degeneration of astrocytes in the cerebrum. Significant loss of peptidase activity, leading to accumulation of the TPP1 substrate ATP5MC1 in lysosomes.|||Removed in mature form|||Tripeptidyl-peptidase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000027378|||http://purl.uniprot.org/annotation/PRO_0000027379 http://togogenome.org/gene/10090:Bms1 ^@ http://purl.uniprot.org/uniprot/Q6PGF5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Bms1-type G|||Disordered ^@ http://togogenome.org/gene/10090:Dok2 ^@ http://purl.uniprot.org/uniprot/O70469|||http://purl.uniprot.org/uniprot/Q3TX09 ^@ 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 ^@ Disordered|||Docking protein 2|||IRS-type PTB|||No loss of binding to SH2 domain of RASGAP or NCK. Complete loss of binding to SH2 domain of RASGAP; when associated with F-304.|||No loss of binding to SH2 domain of RASGAP. Complete loss of binding to SH2 domain of NCK.|||No loss of binding to SH2 domain of RASGAP. Complete loss of binding to SH2 domain of RASGAP; when associated with F-276.|||PH|||Phosphotyrosine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000187271 http://togogenome.org/gene/10090:Atp13a5 ^@ http://purl.uniprot.org/uniprot/D3YU82|||http://purl.uniprot.org/uniprot/Q3TYU2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||P5B-type ATPase N-terminal|||Probable cation-transporting ATPase 13A5 ^@ http://purl.uniprot.org/annotation/PRO_0000337123|||http://purl.uniprot.org/annotation/VSP_033924 http://togogenome.org/gene/10090:Hmgb4 ^@ http://purl.uniprot.org/uniprot/Q6P8W9 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Region|||Sequence Conflict ^@ Disordered|||HMG box 1|||HMG box 2|||High mobility group protein B4 ^@ http://purl.uniprot.org/annotation/PRO_0000269181 http://togogenome.org/gene/10090:Mrpl11 ^@ http://purl.uniprot.org/uniprot/Q9CQF0 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Large ribosomal subunit protein uL11m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000030444 http://togogenome.org/gene/10090:Nherf2 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZX2|||http://purl.uniprot.org/uniprot/A0A0R4J006|||http://purl.uniprot.org/uniprot/Q9JHL1 ^@ 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.|||Na(+)/H(+) exchange regulatory cofactor NHE-RF2|||PDZ|||PDZ 1|||PDZ 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096806|||http://purl.uniprot.org/annotation/VSP_009379|||http://purl.uniprot.org/annotation/VSP_009380 http://togogenome.org/gene/10090:Hps5 ^@ http://purl.uniprot.org/uniprot/E9Q3X4|||http://purl.uniprot.org/uniprot/P59438|||http://purl.uniprot.org/uniprot/Q640Q9 ^@ 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 ^@ BLOC-2 complex member HPS5|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084055|||http://purl.uniprot.org/annotation/VSP_007036|||http://purl.uniprot.org/annotation/VSP_007037|||http://purl.uniprot.org/annotation/VSP_007038 http://togogenome.org/gene/10090:Slmap ^@ http://purl.uniprot.org/uniprot/D3Z7V3|||http://purl.uniprot.org/uniprot/H7BX64|||http://purl.uniprot.org/uniprot/Q3URD3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||FHA|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 5.|||Necessary for targeting to centrosomes|||Phosphoserine|||Sarcolemmal membrane-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000259663|||http://purl.uniprot.org/annotation/VSP_021514|||http://purl.uniprot.org/annotation/VSP_021515|||http://purl.uniprot.org/annotation/VSP_021516|||http://purl.uniprot.org/annotation/VSP_021517|||http://purl.uniprot.org/annotation/VSP_021518 http://togogenome.org/gene/10090:E2f2 ^@ http://purl.uniprot.org/uniprot/P56931 ^@ Chain|||DNA Binding|||Molecule Processing|||Motif|||Region ^@ Chain|||DNA Binding|||Motif|||Region ^@ Cyclin A/CDK2 binding|||DEF box|||Dimerization|||Disordered|||Leucine-zipper|||Retinoblastoma protein binding|||Transactivation|||Transcription factor E2F2 ^@ http://purl.uniprot.org/annotation/PRO_0000219465 http://togogenome.org/gene/10090:Tas2r135 ^@ http://purl.uniprot.org/uniprot/B9EII2|||http://purl.uniprot.org/uniprot/Q7TQA9 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||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 135 ^@ http://purl.uniprot.org/annotation/PRO_0000082270 http://togogenome.org/gene/10090:P4ha1 ^@ http://purl.uniprot.org/uniprot/E9Q7B0|||http://purl.uniprot.org/uniprot/Q3TTT2|||http://purl.uniprot.org/uniprot/Q3UF16|||http://purl.uniprot.org/uniprot/Q60715 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||Fe2OG dioxygenase|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prolyl 4-hydroxylase subunit alpha-1|||TPR|||procollagen-proline 4-dioxygenase ^@ http://purl.uniprot.org/annotation/PRO_0000022724|||http://purl.uniprot.org/annotation/PRO_5003245967|||http://purl.uniprot.org/annotation/PRO_5004229735|||http://purl.uniprot.org/annotation/PRO_5004229940|||http://purl.uniprot.org/annotation/VSP_004505 http://togogenome.org/gene/10090:Zfp949 ^@ http://purl.uniprot.org/uniprot/B2RU83|||http://purl.uniprot.org/uniprot/E9Q732|||http://purl.uniprot.org/uniprot/Q9CUP6 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Hoxc8 ^@ http://purl.uniprot.org/uniprot/P09025 ^@ 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_0000200181 http://togogenome.org/gene/10090:Taok1 ^@ http://purl.uniprot.org/uniprot/B2RX66|||http://purl.uniprot.org/uniprot/Q5F2E8 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase TAO1 ^@ http://purl.uniprot.org/annotation/PRO_0000086729 http://togogenome.org/gene/10090:Insl3 ^@ http://purl.uniprot.org/uniprot/Q5RL10 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Insulin-like|||Insulin-like 3 ^@ http://purl.uniprot.org/annotation/PRO_5015098012 http://togogenome.org/gene/10090:Ccnb1ip1 ^@ http://purl.uniprot.org/uniprot/D3Z3K2 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Coiled-Coil|||Mutagenesis Site|||Zinc Finger ^@ E3 ubiquitin-protein ligase CCNB1IP1|||In mei4; Sterility in both sexes due to meiotic defects.|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000425901 http://togogenome.org/gene/10090:Mgat2 ^@ http://purl.uniprot.org/uniprot/Q921V5 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000080518 http://togogenome.org/gene/10090:Gm5935 ^@ http://purl.uniprot.org/uniprot/Q497S0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Scd3 ^@ http://purl.uniprot.org/uniprot/Q99PL7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acyl-CoA desaturase 3|||Changes substrate specificity so that stearate becomes a good substrate.|||Cytoplasmic|||Disordered|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In isoform 2.|||Lumenal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000433871|||http://purl.uniprot.org/annotation/VSP_057848 http://togogenome.org/gene/10090:Ceacam13 ^@ http://purl.uniprot.org/uniprot/Q9DAT7|||http://purl.uniprot.org/uniprot/Q9DAY4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Immunoglobulin V-set ^@ http://togogenome.org/gene/10090:Krt76 ^@ http://purl.uniprot.org/uniprot/Q3UV17 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type II cytoskeletal 2 oral|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000361693 http://togogenome.org/gene/10090:Zfp318 ^@ http://purl.uniprot.org/uniprot/Q99PP2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000191808|||http://purl.uniprot.org/annotation/VSP_016594|||http://purl.uniprot.org/annotation/VSP_016595 http://togogenome.org/gene/10090:Rab42 ^@ http://purl.uniprot.org/uniprot/Q0PD08 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Region ^@ Disordered|||Polar residues|||Ras-related protein Rab-42|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000442580 http://togogenome.org/gene/10090:Gata1 ^@ http://purl.uniprot.org/uniprot/P17679 ^@ Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn|||Zinc Finger ^@ Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn|||Zinc Finger ^@ Abolishes DNA-binding.|||Abolishes sumoylation. No change in PIAS4 binding nor on transcriptional activity.|||Binds to DNA with reduced affinity.|||Disordered|||Disrupts interaction with ZFPM1 and binding to DNA.|||Disrupts interaction with ZFPM1.|||Disrupts interaction with ZFPM1. Binds normally to DNA.|||Erythroid transcription factor|||GATA-type 1|||GATA-type 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||Interaction with CALCOCO1|||Interaction with MED1 and CCAR1|||Loss of phosphorylation of the chymotryptic peptide.|||N6-acetyllysine|||N6-acetyllysine; by CREBBP|||N6-acetyllysine; by EP300|||No effect on DNA binding.|||No effect on DNA binding. Reduces acetylation. Reduces ability to induce erythroid differentiation. Abrogates acetylation; when associated with 312-A--A-316. Abrogates ability to induce erythroid differentiation; when associated with 312-A--A-316. Reduces binding to CREBBP; when associated with 312-A--A-316. Disrupts stable association with chromatin; when associated with 312-A--A-316.|||No effect on DNA binding. Reduces acetylation. Reduces binding to CREBBP. Reduces ability to induce erythroid differentiation. Abrogates acetylation; when associated with 245-A-A-246. Abrogates ability to induce erythroid differentiation; when associated with 245-A-A-246. Reduces binding to CREBBP; when associated with 245-A-A-246. Disrupts stable association with chromatin; when associated with 245-A-A-246.|||No effect on interaction with ZFPM1.|||Phosphoserine|||Required for interaction with ZFPM1|||Stability of binding to DNA reduced. ^@ http://purl.uniprot.org/annotation/PRO_0000083398|||http://purl.uniprot.org/annotation/VSP_041452 http://togogenome.org/gene/10090:Rpusd1 ^@ http://purl.uniprot.org/uniprot/A0A494BAK7|||http://purl.uniprot.org/uniprot/Q8VCZ8 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Pro residues|||Pseudouridine synthase RsuA/RluA-like|||RNA pseudouridylate synthase domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000300817 http://togogenome.org/gene/10090:Stk24 ^@ http://purl.uniprot.org/uniprot/Q3U335|||http://purl.uniprot.org/uniprot/Q99KH8 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Site ^@ Bipartite nuclear localization signal|||Cleavage; by caspase-3, caspase-7 and caspase-8|||Disordered|||N-acetylalanine|||Nuclear export signal (NES)|||Phosphoserine|||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 35 kDa subunit ^@ http://purl.uniprot.org/annotation/PRO_0000086712|||http://purl.uniprot.org/annotation/PRO_0000413620|||http://purl.uniprot.org/annotation/PRO_0000413621 http://togogenome.org/gene/10090:Ninj2 ^@ http://purl.uniprot.org/uniprot/F8WIJ3|||http://purl.uniprot.org/uniprot/Q3TQA7|||http://purl.uniprot.org/uniprot/Q9JL89 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Helical; Name=Helix alpha3|||Helical;Name=Helix alpha4|||Helix alpha1|||Helix alpha2|||Ninjurin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000159647 http://togogenome.org/gene/10090:Dock3 ^@ http://purl.uniprot.org/uniprot/F8VPQ1|||http://purl.uniprot.org/uniprot/Q3UHH9 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Disordered|||Polar residues|||Pro residues|||SH3 ^@ http://togogenome.org/gene/10090:Hs3st4 ^@ http://purl.uniprot.org/uniprot/D3YVV6 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Site ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region ^@ Disordered|||For sulfotransferase activity|||Pro residues|||Sulfotransferase ^@ http://togogenome.org/gene/10090:Tanc2 ^@ http://purl.uniprot.org/uniprot/A2A690 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||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|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues|||Protein TANC2|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000333812|||http://purl.uniprot.org/annotation/VSP_033551 http://togogenome.org/gene/10090:Trim32 ^@ http://purl.uniprot.org/uniprot/Q3TLR3|||http://purl.uniprot.org/uniprot/Q8CH72 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ B box-type|||B box-type; atypical|||Disordered|||E3 ubiquitin-protein ligase TRIM32|||NHL|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||Phosphoserine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056247 http://togogenome.org/gene/10090:Meis3 ^@ http://purl.uniprot.org/uniprot/P97368 ^@ 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 protein Meis3|||Homeobox; TALE-type|||In isoform 2.|||MEIS N-terminal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049111|||http://purl.uniprot.org/annotation/VSP_012894 http://togogenome.org/gene/10090:Sav1 ^@ http://purl.uniprot.org/uniprot/Q8VEB2 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ Phosphoserine|||Phosphothreonine|||Protein salvador homolog 1|||SARAH|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000076061 http://togogenome.org/gene/10090:A4gnt ^@ http://purl.uniprot.org/uniprot/Q14BT6 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||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_0000439855 http://togogenome.org/gene/10090:Slc25a45 ^@ http://purl.uniprot.org/uniprot/A0A494BAQ4|||http://purl.uniprot.org/uniprot/Q8CFJ7 ^@ 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.|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 45 ^@ http://purl.uniprot.org/annotation/PRO_0000291827|||http://purl.uniprot.org/annotation/VSP_026250|||http://purl.uniprot.org/annotation/VSP_026251 http://togogenome.org/gene/10090:Il17rb ^@ http://purl.uniprot.org/uniprot/Q543U7|||http://purl.uniprot.org/uniprot/Q9JIP3 ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Interleukin-17 receptor B|||N-linked (GlcNAc...) asparagine|||SEFIR|||SEFIR domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000011033|||http://purl.uniprot.org/annotation/PRO_5004249149|||http://purl.uniprot.org/annotation/VSP_001742|||http://purl.uniprot.org/annotation/VSP_001743 http://togogenome.org/gene/10090:Myo1d ^@ http://purl.uniprot.org/uniprot/Q3UG58|||http://purl.uniprot.org/uniprot/Q5SYD0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant ^@ Actin-binding|||IQ 1|||IQ 2|||In isoform 2.|||Myosin motor|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Removed|||TH1|||Unconventional myosin-Id ^@ http://purl.uniprot.org/annotation/PRO_0000123448|||http://purl.uniprot.org/annotation/VSP_051938|||http://purl.uniprot.org/annotation/VSP_051939 http://togogenome.org/gene/10090:Pfdn5 ^@ http://purl.uniprot.org/uniprot/Q9WU28 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Prefoldin subunit 5|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000153662 http://togogenome.org/gene/10090:Pgam5 ^@ http://purl.uniprot.org/uniprot/Q8BX10 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cleavage; by PARL|||Helical|||In isoform 2.|||Interaction with KEAP1|||Mitochondrial intermembrane|||Mitochondrial matrix|||N6-acetyllysine|||Phosphoserine|||Serine/threonine-protein phosphatase PGAM5, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000288783|||http://purl.uniprot.org/annotation/VSP_025762 http://togogenome.org/gene/10090:Lonp2 ^@ http://purl.uniprot.org/uniprot/Q8BK80|||http://purl.uniprot.org/uniprot/Q9DBN5 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||Lon N-terminal|||Lon protease homolog 2, peroxisomal|||Lon proteolytic|||Microbody targeting signal|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000287641|||http://purl.uniprot.org/annotation/VSP_025576|||http://purl.uniprot.org/annotation/VSP_025577|||http://purl.uniprot.org/annotation/VSP_025578 http://togogenome.org/gene/10090:Gbp10 ^@ http://purl.uniprot.org/uniprot/Q000W5 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ GB1/RHD3-type G ^@ http://togogenome.org/gene/10090:Or2ak6 ^@ http://purl.uniprot.org/uniprot/L7MTY4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Calhm6 ^@ http://purl.uniprot.org/uniprot/Q8C9E8 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Calcium homeostasis modulator protein 6|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000283782 http://togogenome.org/gene/10090:Piwil2 ^@ http://purl.uniprot.org/uniprot/Q8CDG1 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes interaction with TDRD1; when associated with K-39; K-45 and K-74.|||Abolishes interaction with TDRD1; when associated with K-9; K-39 and K-45.|||Abolishes interaction with TDRD1; when associated with K-9; K-39 and K-74.|||Abolishes interaction with TDRD1; when associated with K-9; K-45 and K-74.|||Disordered|||In DAH mutant; leads to arrest in meiotic prophase due to a failure of transposon piRNA amplification, resulting in the marked reduction of piRNA-bound within PIWIL4.|||Omega-N-methylarginine; alternate|||Omega-N-methylarginine; by PRMT5; alternate|||PAZ|||Piwi|||Piwi-like protein 2|||Symmetric dimethylarginine|||Symmetric dimethylarginine; alternate|||Symmetric dimethylarginine; by PRMT5|||Symmetric dimethylarginine; by PRMT5; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000234570 http://togogenome.org/gene/10090:Psg22 ^@ http://purl.uniprot.org/uniprot/Q810J1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Ig-like C2-type|||Ig-like V-type 1|||Ig-like V-type 2|||Ig-like V-type 3|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific glycoprotein 22 ^@ http://purl.uniprot.org/annotation/PRO_0000440673 http://togogenome.org/gene/10090:Rnasel ^@ http://purl.uniprot.org/uniprot/B2RQP1|||http://purl.uniprot.org/uniprot/Q05921 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Repeat|||Zinc Finger ^@ 2-5A binding (P-loop) 1|||2-5A binding (P-loop) 2|||2-5A-dependent ribonuclease|||ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Binding to TMEV Leader protein|||C6-type|||Disordered|||KEN|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000067052 http://togogenome.org/gene/10090:Tyrp1 ^@ http://purl.uniprot.org/uniprot/P07147|||http://purl.uniprot.org/uniprot/Q3UFS3 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 5,6-dihydroxyindole-2-carboxylic acid oxidase|||Cytoplasmic|||Helical|||In brown.|||Lumenal, melanosome|||N-linked (GlcNAc...) asparagine|||Tyrosinase copper-binding ^@ http://purl.uniprot.org/annotation/PRO_0000035890|||http://purl.uniprot.org/annotation/PRO_5014309210 http://togogenome.org/gene/10090:Mroh6 ^@ http://purl.uniprot.org/uniprot/V9GX81 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Med18 ^@ http://purl.uniprot.org/uniprot/Q9CZ82 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Mediator of RNA polymerase II transcription subunit 18|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000304743 http://togogenome.org/gene/10090:Vps18 ^@ http://purl.uniprot.org/uniprot/Q8R307 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Zinc Finger ^@ CHCR|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||RING-type|||Removed|||Vacuolar protein sorting-associated protein 18 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000055907 http://togogenome.org/gene/10090:Or4g16 ^@ http://purl.uniprot.org/uniprot/Q8VF38 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pex6 ^@ http://purl.uniprot.org/uniprot/Q99LC9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Omega-N-methylarginine|||Peroxisomal ATPase PEX6 ^@ http://purl.uniprot.org/annotation/PRO_0000084608 http://togogenome.org/gene/10090:Edc4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Q0|||http://purl.uniprot.org/uniprot/G5E896|||http://purl.uniprot.org/uniprot/Q3UJB9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||Enhancer of mRNA-decapping protein 4|||Enhancer of mRNA-decapping protein 4 WD40 repeat region|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000278963|||http://purl.uniprot.org/annotation/VSP_023413 http://togogenome.org/gene/10090:Bcl11a ^@ http://purl.uniprot.org/uniprot/Q3US10|||http://purl.uniprot.org/uniprot/Q5STS9|||http://purl.uniprot.org/uniprot/Q9QYE3 ^@ 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. No effect on nuclear body location.|||Acidic residues|||Asymmetric dimethylarginine|||B-cell lymphoma/leukemia 11A|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||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 and isoform 8.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6.|||In isoform 7.|||No effect on sumoylation.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for nuclear body formation and for SUMO1 recruitment ^@ http://purl.uniprot.org/annotation/PRO_0000047103|||http://purl.uniprot.org/annotation/VSP_009556|||http://purl.uniprot.org/annotation/VSP_009557|||http://purl.uniprot.org/annotation/VSP_009558|||http://purl.uniprot.org/annotation/VSP_009559|||http://purl.uniprot.org/annotation/VSP_009560|||http://purl.uniprot.org/annotation/VSP_009561|||http://purl.uniprot.org/annotation/VSP_009562|||http://purl.uniprot.org/annotation/VSP_009563|||http://purl.uniprot.org/annotation/VSP_009564 http://togogenome.org/gene/10090:Tgif1 ^@ http://purl.uniprot.org/uniprot/G3UWC5|||http://purl.uniprot.org/uniprot/P70284|||http://purl.uniprot.org/uniprot/Q3TVD4 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ CTBP-binding motif|||Disordered|||Homeobox|||Homeobox protein TGIF1|||Homeobox; TALE-type|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000049320|||http://purl.uniprot.org/annotation/VSP_002297 http://togogenome.org/gene/10090:Krt18 ^@ http://purl.uniprot.org/uniprot/P05784 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ 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 SUMO2)|||Head|||IF rod|||Interaction with DNAJB6|||Interaction with TRADD|||Keratin, type I cytoskeletal 18|||Linker 1|||Linker 12|||N-acetylserine|||N6-acetyllysine|||Necessary for interaction with PNN|||O-linked (GlcNAc) serine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by MAPKAPK2 and MAPKAPK3|||Phosphothreonine|||Phosphotyrosine|||Removed|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063667 http://togogenome.org/gene/10090:Mrps35 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0L6|||http://purl.uniprot.org/uniprot/Q8BJZ4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||Mitochondrion|||Small ribosomal subunit protein mS35|||Small ribosomal subunit protein mS35 mitochondrial conserved ^@ http://purl.uniprot.org/annotation/PRO_0000046056 http://togogenome.org/gene/10090:Gpr161 ^@ http://purl.uniprot.org/uniprot/A0A140T8Q9|||http://purl.uniprot.org/uniprot/B2RPY5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||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 mut1; abolishes localization to primary cilia.|||In mut2; weakly affects localization to primary cilia.|||In mut3; does not affect localization to primary cilia; when associated with 243-A-A-244.|||In mut3; does not affect localization to primary cilia; when associated with A-251.|||In mut4; does not affect localization to primary cilia.|||In mut5; does not affect localization to primary cilia.|||Inactive mutant unable to increase cAMP upon induction.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000379073|||http://purl.uniprot.org/annotation/VSP_037635|||http://purl.uniprot.org/annotation/VSP_046300 http://togogenome.org/gene/10090:Scn2a ^@ http://purl.uniprot.org/uniprot/A0A5H1ZRM8|||http://purl.uniprot.org/uniprot/B1AWN6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Site|||Transmembrane ^@ 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|||Disordered|||Gain of function mutation. Mutant mice display enhanced persistent sodium current, have seizures and behavioral abnormalities. Half of the mice die before four months of age, and only 10% survive to nine months. Epilepsy severity in this model is strain-dependent. Mutation in a C57BL/6J background exhibit a mild disorder, whereas animals intercrossed with SJL7/j mice show a severe phenotype.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||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|||Important for channel closure|||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|||Phosphothreonine|||Polar residues|||Pore-forming|||Sodium channel protein type 2 subunit alpha|||Sodium ion transport-associated|||Voltage-gated Na+ ion channel cytoplasmic ^@ http://purl.uniprot.org/annotation/PRO_0000446659 http://togogenome.org/gene/10090:Nudcd1 ^@ http://purl.uniprot.org/uniprot/A0A2K6EDK3|||http://purl.uniprot.org/uniprot/Q6PIP5 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ CS|||NudC domain-containing protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000307705 http://togogenome.org/gene/10090:Gm14461 ^@ http://purl.uniprot.org/uniprot/Q8BRI5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Secreted protein ^@ http://purl.uniprot.org/annotation/PRO_5004303752 http://togogenome.org/gene/10090:Speer4c ^@ http://purl.uniprot.org/uniprot/G3UXD1|||http://purl.uniprot.org/uniprot/Q9CVY0 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Inka2 ^@ http://purl.uniprot.org/uniprot/Q80VY2 ^@ 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.|||Inka box|||PAK4-inhibitor INKA2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000304995|||http://purl.uniprot.org/annotation/VSP_028174 http://togogenome.org/gene/10090:Pkdrej ^@ http://purl.uniprot.org/uniprot/F8VQF3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||PLAT|||Polar residues|||REJ ^@ http://purl.uniprot.org/annotation/PRO_5003379248 http://togogenome.org/gene/10090:Cds1 ^@ http://purl.uniprot.org/uniprot/P98191 ^@ 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|||Omega-N-methylarginine|||Phosphatidate cytidylyltransferase 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000090714 http://togogenome.org/gene/10090:Abhd17c ^@ http://purl.uniprot.org/uniprot/Q8VCV1 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Region ^@ Alpha/beta hydrolase domain-containing protein 17C|||Charge relay system|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000297514 http://togogenome.org/gene/10090:Adamts18 ^@ http://purl.uniprot.org/uniprot/Q4VC17 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ A disintegrin and metalloproteinase with thrombospondin motifs 18|||Disordered|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||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_0000042164|||http://purl.uniprot.org/annotation/PRO_0000437534 http://togogenome.org/gene/10090:Pcdhb5 ^@ http://purl.uniprot.org/uniprot/Q8CEA8|||http://purl.uniprot.org/uniprot/Q91XZ5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Cadherin domain-containing protein|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5004307393|||http://purl.uniprot.org/annotation/PRO_5015099517 http://togogenome.org/gene/10090:Tomm20 ^@ http://purl.uniprot.org/uniprot/Q4KL41|||http://purl.uniprot.org/uniprot/Q9DCC8 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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_0000051539 http://togogenome.org/gene/10090:Fam78a ^@ http://purl.uniprot.org/uniprot/Q8C552 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein FAM78A ^@ http://purl.uniprot.org/annotation/PRO_0000265113 http://togogenome.org/gene/10090:Prss29 ^@ http://purl.uniprot.org/uniprot/E9QLD5|||http://purl.uniprot.org/uniprot/Q99MS4 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 29 ^@ http://purl.uniprot.org/annotation/PRO_0000349226|||http://purl.uniprot.org/annotation/PRO_5003243335 http://togogenome.org/gene/10090:Pcyox1l ^@ http://purl.uniprot.org/uniprot/Q8C7K6 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prenylcysteine oxidase-like ^@ http://purl.uniprot.org/annotation/PRO_0000280287 http://togogenome.org/gene/10090:Maob ^@ http://purl.uniprot.org/uniprot/Q8BW75 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Amine oxidase [flavin-containing] B|||Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Important for catalytic activity|||Mitochondrial intermembrane|||N-acetylserine|||N6-acetyllysine|||Removed|||S-8alpha-FAD cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000099860 http://togogenome.org/gene/10090:Ndufs2 ^@ http://purl.uniprot.org/uniprot/Q91WD5 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Mitochondrion|||N6-acetyllysine|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial|||Symmetric dimethylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000019982 http://togogenome.org/gene/10090:Rfx4 ^@ http://purl.uniprot.org/uniprot/Q7TNK1 ^@ 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 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_0000314238|||http://purl.uniprot.org/annotation/VSP_030247|||http://purl.uniprot.org/annotation/VSP_030248|||http://purl.uniprot.org/annotation/VSP_030249|||http://purl.uniprot.org/annotation/VSP_030250|||http://purl.uniprot.org/annotation/VSP_030251 http://togogenome.org/gene/10090:Fezf2 ^@ http://purl.uniprot.org/uniprot/Q9ESP5 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||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|||Engrailed homology 1 repressor|||Fez family zinc finger protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000295121 http://togogenome.org/gene/10090:Or51v14 ^@ http://purl.uniprot.org/uniprot/E9PZ66 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or10al2 ^@ http://purl.uniprot.org/uniprot/Q7TRJ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Chl1 ^@ http://purl.uniprot.org/uniprot/P70232 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||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 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||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.|||Inhibition of migration potentiation.|||N-linked (GlcNAc...) asparagine|||Neural cell adhesion molecule L1-like protein|||Phosphoserine|||Processed neural cell adhesion molecule L1-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000247897|||http://purl.uniprot.org/annotation/PRO_0000314778|||http://purl.uniprot.org/annotation/VSP_020083|||http://purl.uniprot.org/annotation/VSP_020084|||http://purl.uniprot.org/annotation/VSP_020085 http://togogenome.org/gene/10090:Zswim6 ^@ http://purl.uniprot.org/uniprot/Q80TB7 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Region|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform 2.|||SWIM-type|||Zinc finger SWIM domain-containing protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000223106|||http://purl.uniprot.org/annotation/VSP_009238|||http://purl.uniprot.org/annotation/VSP_009239|||http://purl.uniprot.org/annotation/VSP_009240 http://togogenome.org/gene/10090:Sox10 ^@ http://purl.uniprot.org/uniprot/Q04888 ^@ 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|||Dimerization (DIM)|||Disordered|||HMG box|||Phosphoserine|||Polar residues|||Transactivation domain (TAC)|||Transactivation domain (TAM)|||Transcription factor SOX-10 ^@ http://purl.uniprot.org/annotation/PRO_0000048747 http://togogenome.org/gene/10090:Vamp1 ^@ http://purl.uniprot.org/uniprot/Q62442 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ (Microbial infection) Cleavage; by C.botulinum neurotoxin type X (BoNT/X)|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In lew.|||Phosphoserine|||Vesicle-associated membrane protein 1|||Vesicular|||v-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000206720|||http://purl.uniprot.org/annotation/VSP_029186 http://togogenome.org/gene/10090:Clcn2 ^@ http://purl.uniprot.org/uniprot/Q9R0A1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CBS 1|||CBS 2|||Chloride channel protein 2|||Cytoplasmic|||Disordered|||Helical|||Note=Loop between two helices|||Phosphoserine|||Phosphothreonine|||Polar residues|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3 ^@ http://purl.uniprot.org/annotation/PRO_0000094434 http://togogenome.org/gene/10090:Ndufa8 ^@ http://purl.uniprot.org/uniprot/Q9DCJ5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Motif|||Strand|||Turn ^@ CHCH 1|||CHCH 2|||Cx9C motif 1|||Cx9C motif 2|||Cx9C motif 3|||Cx9C motif 4|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118735 http://togogenome.org/gene/10090:Proser3 ^@ http://purl.uniprot.org/uniprot/Q7TSA6 ^@ 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|||Proline and serine-rich protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000299483|||http://purl.uniprot.org/annotation/VSP_027704|||http://purl.uniprot.org/annotation/VSP_027705|||http://purl.uniprot.org/annotation/VSP_027706 http://togogenome.org/gene/10090:Mn1 ^@ http://purl.uniprot.org/uniprot/D3YWE6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||Transcriptional activator MN1 ^@ http://purl.uniprot.org/annotation/PRO_0000435338 http://togogenome.org/gene/10090:Or8h8 ^@ http://purl.uniprot.org/uniprot/A2AVB0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccdc169 ^@ http://purl.uniprot.org/uniprot/Q8BXX9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant ^@ Coiled-coil domain-containing protein 169|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000341367|||http://purl.uniprot.org/annotation/VSP_035638 http://togogenome.org/gene/10090:Trappc3l ^@ http://purl.uniprot.org/uniprot/Q4KL14 ^@ Chain|||Lipid Binding|||Modification|||Molecule Processing ^@ Chain|||Lipid Binding ^@ S-palmitoyl cysteine|||Trafficking protein particle complex subunit 3-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000305084 http://togogenome.org/gene/10090:Eef2 ^@ http://purl.uniprot.org/uniprot/P58252 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ 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|||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|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000091002 http://togogenome.org/gene/10090:Ccdc115 ^@ http://purl.uniprot.org/uniprot/Q8VE99 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Coiled-coil domain-containing protein 115|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000279404 http://togogenome.org/gene/10090:Apol7e ^@ http://purl.uniprot.org/uniprot/Q3UZ24 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Rgs2 ^@ http://purl.uniprot.org/uniprot/O08849 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Necessary for membrane association|||Necessary to inhibit protein synthesis|||RGS|||Regulator of G-protein signaling 2 ^@ http://purl.uniprot.org/annotation/PRO_0000204179 http://togogenome.org/gene/10090:Pdcd11 ^@ http://purl.uniprot.org/uniprot/Q6NS46 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||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 1|||S1 motif 10|||S1 motif 11|||S1 motif 12|||S1 motif 13|||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_0000364200 http://togogenome.org/gene/10090:Ipo11 ^@ http://purl.uniprot.org/uniprot/Q8K2V6 ^@ 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 ^@ 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|||Importin N-terminal|||Importin-11|||In isoform 2.|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000120757|||http://purl.uniprot.org/annotation/VSP_010935 http://togogenome.org/gene/10090:Iigp1c ^@ http://purl.uniprot.org/uniprot/Q3UED7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ IRG-type G ^@ http://togogenome.org/gene/10090:Acnat1 ^@ http://purl.uniprot.org/uniprot/A2AKK5 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant ^@ Acyl-coenzyme A amino acid N-acyltransferase 1|||Charge relay system|||In isoform 2.|||Microbody targeting signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000352774|||http://purl.uniprot.org/annotation/VSP_052953 http://togogenome.org/gene/10090:Slc8a1 ^@ http://purl.uniprot.org/uniprot/A0A3Q4EBU5|||http://purl.uniprot.org/uniprot/G3X9J1|||http://purl.uniprot.org/uniprot/P70414|||http://purl.uniprot.org/uniprot/Q27PY9|||http://purl.uniprot.org/uniprot/Q68FL0 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Alpha-1|||Alpha-2|||Calx-beta 1|||Calx-beta 2|||Cytoplasmic|||Extracellular|||Helical|||J|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Putative calmodulin-binding region|||Sodium/calcium exchanger 1 ^@ http://purl.uniprot.org/annotation/PRO_0000019380|||http://purl.uniprot.org/annotation/PRO_5004203681|||http://purl.uniprot.org/annotation/PRO_5015091828|||http://purl.uniprot.org/annotation/PRO_5015098148|||http://purl.uniprot.org/annotation/PRO_5030082066 http://togogenome.org/gene/10090:Or2n1 ^@ http://purl.uniprot.org/uniprot/Q8VG95 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tenm3 ^@ http://purl.uniprot.org/uniprot/B7ZNJ5|||http://purl.uniprot.org/uniprot/G3X907 ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||EGF-like|||Helical|||Polar residues|||Teneurin N-terminal ^@ http://togogenome.org/gene/10090:Ldlr ^@ http://purl.uniprot.org/uniprot/A0A1L1SRE8|||http://purl.uniprot.org/uniprot/P35951 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Clustered O-linked oligosaccharides|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3|||Extracellular|||Helical|||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|||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|||N-linked (GlcNAc...) asparagine|||NPXY motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for MYLIP-triggered down-regulation of LDLR ^@ http://purl.uniprot.org/annotation/PRO_0000017313|||http://purl.uniprot.org/annotation/PRO_5009681963 http://togogenome.org/gene/10090:Ear2 ^@ http://purl.uniprot.org/uniprot/P97425|||http://purl.uniprot.org/uniprot/W0UVF7 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Eosinophil cationic protein 2|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Proton donor|||Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_0000030868|||http://purl.uniprot.org/annotation/PRO_5014206141 http://togogenome.org/gene/10090:Slirp ^@ http://purl.uniprot.org/uniprot/Q14AR0|||http://purl.uniprot.org/uniprot/Q9D8T7 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Mitochondrion|||Phosphoserine|||Phosphothreonine|||RRM|||SRA stem-loop-interacting RNA-binding protein, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000247052|||http://purl.uniprot.org/annotation/VSP_019907 http://togogenome.org/gene/10090:Dnajc24 ^@ http://purl.uniprot.org/uniprot/Q91ZF0 ^@ 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 ^@ DPH-type MB|||DnaJ homolog subfamily C member 24|||J ^@ http://purl.uniprot.org/annotation/PRO_0000082623 http://togogenome.org/gene/10090:Gaa ^@ http://purl.uniprot.org/uniprot/P70699 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Lysosomal alpha-glucosidase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||P-type ^@ http://purl.uniprot.org/annotation/PRO_0000018569|||http://purl.uniprot.org/annotation/PRO_0000018570 http://togogenome.org/gene/10090:Sbno2 ^@ http://purl.uniprot.org/uniprot/Q7TNB8 ^@ 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.|||In isoform 3.|||Protein strawberry notch homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000314561|||http://purl.uniprot.org/annotation/VSP_030305|||http://purl.uniprot.org/annotation/VSP_030306|||http://purl.uniprot.org/annotation/VSP_030307|||http://purl.uniprot.org/annotation/VSP_030308|||http://purl.uniprot.org/annotation/VSP_030309 http://togogenome.org/gene/10090:Or10j3 ^@ http://purl.uniprot.org/uniprot/E9PWV2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Yipf4 ^@ http://purl.uniprot.org/uniprot/Q8C407 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Protein YIPF4 ^@ http://purl.uniprot.org/annotation/PRO_0000242633|||http://purl.uniprot.org/annotation/VSP_019457 http://togogenome.org/gene/10090:Qsox2 ^@ http://purl.uniprot.org/uniprot/Q3TMX7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||ERV/ALR sulfhydryl oxidase|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Redox-active|||Sulfhydryl oxidase 2|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000249539|||http://purl.uniprot.org/annotation/VSP_020500|||http://purl.uniprot.org/annotation/VSP_020501|||http://purl.uniprot.org/annotation/VSP_020502 http://togogenome.org/gene/10090:Snx33 ^@ http://purl.uniprot.org/uniprot/Q4VAA7 ^@ 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 ^@ BAR|||Disordered|||PX|||Phosphoserine|||Polar residues|||SH3|||Sorting nexin-33 ^@ http://purl.uniprot.org/annotation/PRO_0000311949 http://togogenome.org/gene/10090:Upp2 ^@ http://purl.uniprot.org/uniprot/A2APN2|||http://purl.uniprot.org/uniprot/Q3UEN1|||http://purl.uniprot.org/uniprot/Q8BLN7|||http://purl.uniprot.org/uniprot/Q8CGR7|||http://purl.uniprot.org/uniprot/Q8R093 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region ^@ Disordered|||Nucleoside phosphorylase|||Polar residues|||Redox-active|||Uridine phosphorylase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000063194 http://togogenome.org/gene/10090:Sptbn1 ^@ http://purl.uniprot.org/uniprot/Q3TTX2|||http://purl.uniprot.org/uniprot/Q3TZN6|||http://purl.uniprot.org/uniprot/Q62261|||http://purl.uniprot.org/uniprot/Q8BQ35|||http://purl.uniprot.org/uniprot/Q8R1C2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Actin-binding|||Basic and acidic residues|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||In isoform 2.|||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_0000073462|||http://purl.uniprot.org/annotation/VSP_026057|||http://purl.uniprot.org/annotation/VSP_026058|||http://purl.uniprot.org/annotation/VSP_026059 http://togogenome.org/gene/10090:1700122O11Rik ^@ http://purl.uniprot.org/uniprot/J3QPW6|||http://purl.uniprot.org/uniprot/Q9D996 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Bid ^@ http://purl.uniprot.org/uniprot/P70444 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand ^@ 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|||Disordered|||Loss of proteolytical cleavage leading to the production of p11 BID.|||N-acetylmethionine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000143102|||http://purl.uniprot.org/annotation/PRO_0000223234|||http://purl.uniprot.org/annotation/PRO_0000223235|||http://purl.uniprot.org/annotation/PRO_0000223236 http://togogenome.org/gene/10090:Slc5a4a ^@ http://purl.uniprot.org/uniprot/Q9ET37 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Confers sodium-dependent sugar transport activity not found in the wild type protein.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Solute carrier family 5 member 4A ^@ http://purl.uniprot.org/annotation/PRO_0000105377 http://togogenome.org/gene/10090:Wnt11 ^@ http://purl.uniprot.org/uniprot/P48615 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-11 ^@ http://purl.uniprot.org/annotation/PRO_0000041466 http://togogenome.org/gene/10090:Akap14 ^@ http://purl.uniprot.org/uniprot/Q3V0I7 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Hpx ^@ http://purl.uniprot.org/uniprot/Q91X72 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Hemopexin 5|||Hemopexin 6|||Hemopexin 7|||Hemopexin 8|||N-linked (GlcNAc...) asparagine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000021407 http://togogenome.org/gene/10090:Mpdz ^@ http://purl.uniprot.org/uniprot/B2RQR2|||http://purl.uniprot.org/uniprot/Q3TUR5|||http://purl.uniprot.org/uniprot/Q8VBX6 ^@ 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 isoform 2.|||In isoform 3.|||In isoform 4.|||In strain: DBA/2J and DBA1/J.|||In strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J.|||L27|||Multiple PDZ domain protein|||Omega-N-methylarginine|||PDZ|||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_0000094595|||http://purl.uniprot.org/annotation/VSP_014201|||http://purl.uniprot.org/annotation/VSP_014202|||http://purl.uniprot.org/annotation/VSP_058771 http://togogenome.org/gene/10090:Cdin1 ^@ http://purl.uniprot.org/uniprot/Q3U4G0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ CDAN1-interacting nuclease 1|||In isoform 2.|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000271045|||http://purl.uniprot.org/annotation/VSP_022272 http://togogenome.org/gene/10090:Dap3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1B9|||http://purl.uniprot.org/uniprot/G3X9M0|||http://purl.uniprot.org/uniprot/Q9ER88 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Small ribosomal subunit protein mS29 ^@ http://purl.uniprot.org/annotation/PRO_0000087718|||http://purl.uniprot.org/annotation/VSP_008916 http://togogenome.org/gene/10090:Zcchc24 ^@ http://purl.uniprot.org/uniprot/B2RVL6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Modified Residue|||Zinc Finger ^@ CCHC-type|||Phosphoserine|||Zinc finger CCHC domain-containing protein 24 ^@ http://purl.uniprot.org/annotation/PRO_0000351149 http://togogenome.org/gene/10090:Gfpt1 ^@ http://purl.uniprot.org/uniprot/P47856 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ For GATase activity|||Glutamine amidotransferase type-2|||Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1|||In isoform 2.|||Isomerase|||Phosphoserine|||Removed|||SIS 1|||SIS 2 ^@ http://purl.uniprot.org/annotation/PRO_0000135281|||http://purl.uniprot.org/annotation/VSP_007498 http://togogenome.org/gene/10090:Cnn3 ^@ http://purl.uniprot.org/uniprot/Q9DAW9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||Calponin-3|||Calponin-homology (CH)|||Calponin-like 1|||Calponin-like 2|||Calponin-like 3|||Disordered|||N6-acetyllysine|||N6-methyllysine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204777 http://togogenome.org/gene/10090:Lypd4 ^@ http://purl.uniprot.org/uniprot/Q8BVP6 ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated alanine|||Ly6/PLAUR domain-containing protein 4|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000226761|||http://purl.uniprot.org/annotation/PRO_0000226762 http://togogenome.org/gene/10090:Cyp2ab1 ^@ http://purl.uniprot.org/uniprot/B9EHK4 ^@ Binding Site|||Site ^@ Binding Site ^@ ^@ http://togogenome.org/gene/10090:Ssxb6 ^@ http://purl.uniprot.org/uniprot/A2BI74|||http://purl.uniprot.org/uniprot/Q6XAS1 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ KRAB|||KRAB-related ^@ http://togogenome.org/gene/10090:Bcl7c ^@ http://purl.uniprot.org/uniprot/A0A0U1RNX8|||http://purl.uniprot.org/uniprot/O08664 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ B-cell CLL/lymphoma 7 protein family member C|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000239834 http://togogenome.org/gene/10090:Thap3 ^@ http://purl.uniprot.org/uniprot/A2A8D4|||http://purl.uniprot.org/uniprot/Q52KE1|||http://purl.uniprot.org/uniprot/Q8BJ25 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||HCFC1-binding motif (HBM)|||Phosphoserine|||THAP domain-containing protein 3|||THAP-type ^@ http://purl.uniprot.org/annotation/PRO_0000068645 http://togogenome.org/gene/10090:Rell1 ^@ http://purl.uniprot.org/uniprot/Q8K2J7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Phosphoserine|||Pro residues|||RELT-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000323591|||http://purl.uniprot.org/annotation/VSP_032026 http://togogenome.org/gene/10090:Cdk6 ^@ http://purl.uniprot.org/uniprot/Q0VBK8|||http://purl.uniprot.org/uniprot/Q64261 ^@ 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 ^@ Cyclin-dependent kinase 6|||Enhanced kinase activity. Over-production of thymocytes and hematopoietic stem cells and progenitor cells.|||In strain: SPRET/Ei.|||Loss of kinase activity. Pronounced reduction in thymocytes and hematopoietic stem cells and progenitor cells.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085790 http://togogenome.org/gene/10090:Il1rl2 ^@ http://purl.uniprot.org/uniprot/Q149G7|||http://purl.uniprot.org/uniprot/Q9ERS7 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Interleukin-1 receptor-like 2|||N-linked (GlcNAc...) asparagine|||TIR ^@ http://purl.uniprot.org/annotation/PRO_0000015446|||http://purl.uniprot.org/annotation/PRO_5014306922 http://togogenome.org/gene/10090:Ak2 ^@ http://purl.uniprot.org/uniprot/Q9WTP6 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Adenylate kinase 2, mitochondrial|||In isoform 2.|||LID|||N-acetylmethionine|||N6-acetyllysine|||N6-succinyllysine|||NMP|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000158918|||http://purl.uniprot.org/annotation/VSP_036504 http://togogenome.org/gene/10090:Wdr74 ^@ http://purl.uniprot.org/uniprot/Q8R3V4|||http://purl.uniprot.org/uniprot/Q8VCG3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Region|||Repeat ^@ Disordered|||N6-methyllysine|||Phosphoserine|||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_0000051429 http://togogenome.org/gene/10090:Fam114a2 ^@ http://purl.uniprot.org/uniprot/Q8VE88 ^@ 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|||Protein FAM114A2 ^@ http://purl.uniprot.org/annotation/PRO_0000274565|||http://purl.uniprot.org/annotation/VSP_022796 http://togogenome.org/gene/10090:Neurod6 ^@ http://purl.uniprot.org/uniprot/P48986|||http://purl.uniprot.org/uniprot/Q3UN97|||http://purl.uniprot.org/uniprot/Q5M8T7 ^@ 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_0000127394 http://togogenome.org/gene/10090:Tmem135 ^@ http://purl.uniprot.org/uniprot/Q9CYV5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 135 ^@ http://purl.uniprot.org/annotation/PRO_0000284623 http://togogenome.org/gene/10090:Ppm1m ^@ http://purl.uniprot.org/uniprot/A0A8I4Q8Y8|||http://purl.uniprot.org/uniprot/F8WGF9|||http://purl.uniprot.org/uniprot/Q8BU27 ^@ 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 ^@ Disordered|||In isoform 1.|||In isoform 2.|||PPM-type phosphatase|||Pro residues|||Protein phosphatase 1M ^@ http://purl.uniprot.org/annotation/PRO_0000057757|||http://purl.uniprot.org/annotation/VSP_061128|||http://purl.uniprot.org/annotation/VSP_061129 http://togogenome.org/gene/10090:Tubgcp5 ^@ http://purl.uniprot.org/uniprot/Q8BKN5 ^@ 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|||Gamma-tubulin complex component 5|||In isoform 2.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000323605|||http://purl.uniprot.org/annotation/VSP_032040|||http://purl.uniprot.org/annotation/VSP_032041 http://togogenome.org/gene/10090:Krt82 ^@ http://purl.uniprot.org/uniprot/Q99M74 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ 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_0000063698 http://togogenome.org/gene/10090:Or5b123 ^@ http://purl.uniprot.org/uniprot/Q8VFQ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lhx6 ^@ http://purl.uniprot.org/uniprot/E9QN32|||http://purl.uniprot.org/uniprot/H9H9T0|||http://purl.uniprot.org/uniprot/Q9R1R0 ^@ 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|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx6|||Polar residues|||Required for interaction with LDB1 ^@ http://purl.uniprot.org/annotation/PRO_0000075795|||http://purl.uniprot.org/annotation/VSP_003110 http://togogenome.org/gene/10090:Gm10256 ^@ http://purl.uniprot.org/uniprot/B2RWR6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||RRM ^@ http://togogenome.org/gene/10090:Serpinb8 ^@ http://purl.uniprot.org/uniprot/O08800|||http://purl.uniprot.org/uniprot/Q8C871 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Chain|||Domain Extent|||Site ^@ Reactive bond|||Serpin|||Serpin B8 ^@ http://purl.uniprot.org/annotation/PRO_0000094112 http://togogenome.org/gene/10090:Oscp1 ^@ http://purl.uniprot.org/uniprot/A2A8Y5|||http://purl.uniprot.org/uniprot/Q8BHW2 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue ^@ Chain|||Non-terminal Residue ^@ Protein OSCP1 ^@ http://purl.uniprot.org/annotation/PRO_0000251966 http://togogenome.org/gene/10090:Zfp808 ^@ http://purl.uniprot.org/uniprot/B8JJZ4|||http://purl.uniprot.org/uniprot/Q6P8L0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Dusp9 ^@ http://purl.uniprot.org/uniprot/Q7TNL7 ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Phosphocysteine intermediate|||Polar residues|||Rhodanese|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://togogenome.org/gene/10090:Flrt2 ^@ http://purl.uniprot.org/uniprot/Q8BLU0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||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|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes homooligomerization and FLRT2-mediated cell-cell adhesion; when associated with N-186.|||Abolishes homooligomerization and FLRT2-mediated cell-cell adhesion; when associated with T-188.|||Abolishes interaction with UNC5D.|||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|||No effect on interaction with UNC5D; when associated with N-248.|||No effect on interaction with UNC5D; when associated with T-250.|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000434523 http://togogenome.org/gene/10090:Gm10778 ^@ http://purl.uniprot.org/uniprot/A0A087WNP5|||http://purl.uniprot.org/uniprot/Q6PFY2 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Siah2 ^@ http://purl.uniprot.org/uniprot/Q06986|||http://purl.uniprot.org/uniprot/Q3UEV2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase SIAH2|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphoserine; by DYRK2 and MAPK14|||Phosphothreonine; by DYRK2|||Phosphothreonine; by MAPK14|||Pro residues|||RING-type|||SBD|||SIAH-type ^@ http://purl.uniprot.org/annotation/PRO_0000056169 http://togogenome.org/gene/10090:Cnpy4 ^@ http://purl.uniprot.org/uniprot/Q8BQ47 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Region|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||Disordered|||Protein canopy homolog 4 ^@ http://purl.uniprot.org/annotation/PRO_0000314019 http://togogenome.org/gene/10090:Tspan15 ^@ http://purl.uniprot.org/uniprot/F7BWT7 ^@ 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|||Tetraspanin-15 ^@ http://purl.uniprot.org/annotation/PRO_0000415812|||http://purl.uniprot.org/annotation/VSP_042389 http://togogenome.org/gene/10090:L2hgdh ^@ http://purl.uniprot.org/uniprot/Q91YP0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ L-2-hydroxyglutarate dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000228130 http://togogenome.org/gene/10090:Ddit3 ^@ http://purl.uniprot.org/uniprot/P35639|||http://purl.uniprot.org/uniprot/Q3V405 ^@ 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 ^@ BZIP|||Basic and acidic residues|||Basic motif|||DNA damage-inducible transcript 3 protein|||Disordered|||Interaction with TRIB3|||Leucine-zipper|||Loss of phosphorylation.|||N-terminal|||Phosphoserine; by CK2|||Phosphoserine; by MAPK14|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076643 http://togogenome.org/gene/10090:Apaf1 ^@ http://purl.uniprot.org/uniprot/G3XA09|||http://purl.uniprot.org/uniprot/O88879|||http://purl.uniprot.org/uniprot/Q5DU30 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Apoptotic protease-activating factor 1|||CARD|||In isoform 2.|||Interpropeller linker|||NB-ARC|||No stimulation of CASP9 activity.|||WD|||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_0000050845|||http://purl.uniprot.org/annotation/VSP_006763 http://togogenome.org/gene/10090:Spata19 ^@ http://purl.uniprot.org/uniprot/Q9DAQ9 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant|||Transit Peptide ^@ Chain|||Modified Residue|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Mitochondrion|||Phosphoserine|||Spermatogenesis-associated protein 19, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000251610|||http://purl.uniprot.org/annotation/VSP_020764|||http://purl.uniprot.org/annotation/VSP_020765 http://togogenome.org/gene/10090:Krt85 ^@ http://purl.uniprot.org/uniprot/Q9Z2T6 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict ^@ Coil 1A|||Coil 1B|||Coil 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Head|||IF rod|||Keratin, type II cuticular Hb5|||Linker 1|||Linker 12|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063703 http://togogenome.org/gene/10090:Gne ^@ http://purl.uniprot.org/uniprot/Q3TCI8|||http://purl.uniprot.org/uniprot/Q3UW64|||http://purl.uniprot.org/uniprot/Q91WG8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase|||N-acetylmannosamine kinase|||UDP-N-acetylglucosamine 2-epimerase ^@ http://purl.uniprot.org/annotation/PRO_0000095717 http://togogenome.org/gene/10090:Dhx30 ^@ http://purl.uniprot.org/uniprot/A0A0G2JGL8|||http://purl.uniprot.org/uniprot/Q99PU8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ ATP-dependent RNA helicase DHX30|||DEAH box|||DRBM|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000245539|||http://purl.uniprot.org/annotation/VSP_019746|||http://purl.uniprot.org/annotation/VSP_019747 http://togogenome.org/gene/10090:Epha5 ^@ http://purl.uniprot.org/uniprot/E9PUQ0|||http://purl.uniprot.org/uniprot/Q60629 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Eph LBD|||Ephrin type-A receptor 5|||Extracellular|||Fibronectin type-III|||Helical|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM|||Strongly reduced binding affinity for SAMD5 SAM domain. ^@ http://purl.uniprot.org/annotation/PRO_0000016813 http://togogenome.org/gene/10090:Pkib ^@ http://purl.uniprot.org/uniprot/F7D7A9|||http://purl.uniprot.org/uniprot/Q3TZU5|||http://purl.uniprot.org/uniprot/Q6P8N5|||http://purl.uniprot.org/uniprot/Q8BNE5 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region|||Site ^@ Compositionally Biased Region|||Non-terminal Residue|||Region|||Site ^@ Basic and acidic residues|||Disordered|||Important for inhibition|||Polar residues ^@ http://togogenome.org/gene/10090:Mdk ^@ http://purl.uniprot.org/uniprot/P12025|||http://purl.uniprot.org/uniprot/Q2LEK5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Signal Peptide|||Site ^@ Decreases affinity binding to PTPRZ1. Decreases affinity binding to PTPRZ1; when associated with Q-105 and Q-106. Decreases neuron migration. Decreases neuron migration; when associated with Q-105 and Q-106.|||Does not affect binding with PTPRZ1. Does not affect binding with PTPRZ1; when associated with Q-105. Does not affect positive regulation of neuron migration.|||Does not affect binding with PTPRZ1. Does not affect binding with PTPRZ1; when associated with Q-106. Does not affect positive regulation of neuron migration.|||Midkine|||Pleiotrophin/Midkine N-terminal|||Required for high affinity binding to PTRZ1 by interacting with the chondroitin sulfate chains of PTRZ1 ^@ http://purl.uniprot.org/annotation/PRO_0000024663|||http://purl.uniprot.org/annotation/PRO_5004212070 http://togogenome.org/gene/10090:Traf1 ^@ http://purl.uniprot.org/uniprot/P39428 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Cleavage; by CASP8|||Decreased interaction with FBXL2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Loss of phosphorylation site. Reduces global phosphorylation.|||MATH|||Phosphoserine|||TNF receptor-associated factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000056398 http://togogenome.org/gene/10090:Or4k38 ^@ http://purl.uniprot.org/uniprot/Q7TQY5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfhx2 ^@ http://purl.uniprot.org/uniprot/Q2MHN3 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 10; degenerate|||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|||Disordered|||Homeobox 1|||Homeobox 2|||Homeobox 3|||Polar residues|||Pro residues|||Results in hyposensitivity to noxious heat.|||Zinc finger homeobox protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000443288 http://togogenome.org/gene/10090:Or10ag59 ^@ http://purl.uniprot.org/uniprot/A2AV41 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fgd5 ^@ http://purl.uniprot.org/uniprot/E9QKY4|||http://purl.uniprot.org/uniprot/Q80UZ0 ^@ 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 ^@ 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|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080951|||http://purl.uniprot.org/annotation/VSP_013089 http://togogenome.org/gene/10090:Foxd3 ^@ http://purl.uniprot.org/uniprot/A2BDY3|||http://purl.uniprot.org/uniprot/Q61060 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Fork-head|||Forkhead box protein D3|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000091818 http://togogenome.org/gene/10090:CK137956 ^@ http://purl.uniprot.org/uniprot/B1AYM9|||http://purl.uniprot.org/uniprot/B2RW37 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Cisd1 ^@ http://purl.uniprot.org/uniprot/Q91WS0 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Modified Residue|||Topological Domain|||Transmembrane ^@ CDGSH iron-sulfur domain-containing protein 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; Signal-anchor for type III membrane protein|||N6-acetyllysine; alternate|||Schiff-base intermediate with pyridoxal 5'-phosphate ^@ http://purl.uniprot.org/annotation/PRO_0000089804 http://togogenome.org/gene/10090:Vmn1r79 ^@ http://purl.uniprot.org/uniprot/Q8R285 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Arl4d ^@ http://purl.uniprot.org/uniprot/Q99PE9 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Sequence Conflict ^@ ADP-ribosylation factor-like protein 4D|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207465 http://togogenome.org/gene/10090:Tmsb4x ^@ http://purl.uniprot.org/uniprot/P20065|||http://purl.uniprot.org/uniprot/Q6ZWX2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Peptide|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Hemoregulatory peptide AcSDKP|||In isoform Short.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Thymosin beta-4 ^@ http://purl.uniprot.org/annotation/PRO_0000034297|||http://purl.uniprot.org/annotation/PRO_0000045923|||http://purl.uniprot.org/annotation/VSP_006424 http://togogenome.org/gene/10090:Meox1 ^@ http://purl.uniprot.org/uniprot/P32442 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Mutagenesis Site|||Region ^@ Abolishes DNA-binding. Does not affect ability to activate expression of CDKN2A.|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein MOX-1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049196 http://togogenome.org/gene/10090:Chuk ^@ http://purl.uniprot.org/uniprot/E9Q605|||http://purl.uniprot.org/uniprot/E9QNL4|||http://purl.uniprot.org/uniprot/Q3TPN9|||http://purl.uniprot.org/uniprot/Q3UDK0|||http://purl.uniprot.org/uniprot/Q8CBT3 ^@ Binding Site|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Domain Extent|||Non-terminal Residue ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Myef2 ^@ http://purl.uniprot.org/uniprot/A2ATP5|||http://purl.uniprot.org/uniprot/A7UQY4|||http://purl.uniprot.org/uniprot/Q8C854 ^@ 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.|||In isoform 3.|||In isoform 4.|||Myelin expression factor 2|||Omega-N-methylarginine|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000081656|||http://purl.uniprot.org/annotation/VSP_013455|||http://purl.uniprot.org/annotation/VSP_013456|||http://purl.uniprot.org/annotation/VSP_013457|||http://purl.uniprot.org/annotation/VSP_013458|||http://purl.uniprot.org/annotation/VSP_013459|||http://purl.uniprot.org/annotation/VSP_013460|||http://purl.uniprot.org/annotation/VSP_013461 http://togogenome.org/gene/10090:B4gat1 ^@ http://purl.uniprot.org/uniprot/Q8BWP8 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Beta-1,4-glucuronyltransferase 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||Mild muscular dystrophy phenotype of variable penetrance due to defects in axon guidance. Mislocalization to the endoplasmic reticulum.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000080556|||http://purl.uniprot.org/annotation/VSP_014004|||http://purl.uniprot.org/annotation/VSP_014005 http://togogenome.org/gene/10090:Gucy1a2 ^@ http://purl.uniprot.org/uniprot/F8VQK3|||http://purl.uniprot.org/uniprot/Q3TNN8|||http://purl.uniprot.org/uniprot/Q3UH83 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Guanylate cyclase|||Haem NO binding associated|||Heme NO-binding|||Polar residues ^@ http://togogenome.org/gene/10090:Ly6i ^@ http://purl.uniprot.org/uniprot/Q9WU67 ^@ 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 glycine|||In Ly-6I.1.|||Lymphocyte antigen 6I|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036152|||http://purl.uniprot.org/annotation/PRO_0000036153 http://togogenome.org/gene/10090:Tmem185a ^@ http://purl.uniprot.org/uniprot/Q3TYW3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Rnf128 ^@ http://purl.uniprot.org/uniprot/A2AGL8|||http://purl.uniprot.org/uniprot/Q9D304 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNF128|||Helical|||Loss of ubiquitination activity.|||N-linked (GlcNAc...) asparagine|||PA|||RING-type|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000261413|||http://purl.uniprot.org/annotation/PRO_5002642489 http://togogenome.org/gene/10090:Shank3 ^@ http://purl.uniprot.org/uniprot/Q4ACU6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Splice Variant|||Strand|||Turn ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In isoform 10.|||In isoform 2 and isoform 5.|||In isoform 2 and isoform 9.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8 and isoform 9.|||Intramolecular interaction with the ANK repeats|||PDZ|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Required for interaction with ABI1|||SAM|||SH3|||SH3 and multiple ankyrin repeat domains protein 3|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000291257|||http://purl.uniprot.org/annotation/VSP_053606|||http://purl.uniprot.org/annotation/VSP_053607|||http://purl.uniprot.org/annotation/VSP_053608|||http://purl.uniprot.org/annotation/VSP_053609|||http://purl.uniprot.org/annotation/VSP_053610|||http://purl.uniprot.org/annotation/VSP_053611|||http://purl.uniprot.org/annotation/VSP_053612|||http://purl.uniprot.org/annotation/VSP_053613|||http://purl.uniprot.org/annotation/VSP_053614|||http://purl.uniprot.org/annotation/VSP_053615 http://togogenome.org/gene/10090:Dyrk1b ^@ http://purl.uniprot.org/uniprot/Q9Z188 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Bipartite nuclear localization signal|||Disordered|||Dual specificity tyrosine-phosphorylation-regulated kinase 1B|||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_0000085935|||http://purl.uniprot.org/annotation/VSP_022954|||http://purl.uniprot.org/annotation/VSP_022955 http://togogenome.org/gene/10090:Hepacam ^@ http://purl.uniprot.org/uniprot/B2RSY3|||http://purl.uniprot.org/uniprot/Q640R3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hepatic and glial cell adhesion molecule|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000298778|||http://purl.uniprot.org/annotation/PRO_5015087153 http://togogenome.org/gene/10090:Tgm3 ^@ http://purl.uniprot.org/uniprot/Q08189 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Cleavage; by CTSL|||Disordered|||Phosphothreonine|||Phosphotyrosine|||Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain|||Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain ^@ http://purl.uniprot.org/annotation/PRO_0000033654|||http://purl.uniprot.org/annotation/PRO_0000033655 http://togogenome.org/gene/10090:Ncbp3 ^@ http://purl.uniprot.org/uniprot/Q8BZR9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||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 SUMO2)|||In isoform 2.|||In isoform 3.|||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_0000308583|||http://purl.uniprot.org/annotation/VSP_029000|||http://purl.uniprot.org/annotation/VSP_029001|||http://purl.uniprot.org/annotation/VSP_029002|||http://purl.uniprot.org/annotation/VSP_029003 http://togogenome.org/gene/10090:P2rx2 ^@ http://purl.uniprot.org/uniprot/Q8K3P1 ^@ 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.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 2|||Polar residues|||Pore-forming motif ^@ http://purl.uniprot.org/annotation/PRO_0000425905|||http://purl.uniprot.org/annotation/VSP_053887|||http://purl.uniprot.org/annotation/VSP_053888|||http://purl.uniprot.org/annotation/VSP_053889|||http://purl.uniprot.org/annotation/VSP_053890 http://togogenome.org/gene/10090:Ifnlr1 ^@ http://purl.uniprot.org/uniprot/Q3URN4|||http://purl.uniprot.org/uniprot/Q8CGK5 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III domain-containing protein|||Helical|||Interferon lambda receptor 1|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000011020|||http://purl.uniprot.org/annotation/PRO_5009970840 http://togogenome.org/gene/10090:Kazald1 ^@ http://purl.uniprot.org/uniprot/Q8BJ66 ^@ 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 ^@ Disordered|||IGFBP N-terminal|||Ig-like C2-type|||Kazal-like|||Kazal-type serine protease inhibitor domain-containing protein 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015077 http://togogenome.org/gene/10090:Fga ^@ http://purl.uniprot.org/uniprot/E9PV24 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Peptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ 4-hydroxyproline; by P4HA1|||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 isoform 2.|||Interchain|||Interchain (with C-213 in beta chain)|||Interchain (with beta chain)|||Interchain (with gamma chain)|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000430789|||http://purl.uniprot.org/annotation/PRO_0000430790|||http://purl.uniprot.org/annotation/VSP_057097|||http://purl.uniprot.org/annotation/VSP_057098 http://togogenome.org/gene/10090:Mbip ^@ http://purl.uniprot.org/uniprot/Q99LQ1 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Modified Residue|||Region ^@ 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 MAP3K12|||Leucine-zipper 1|||Leucine-zipper 2|||MAP3K12-binding inhibitory protein 1|||N6-acetyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000096270 http://togogenome.org/gene/10090:Ppfia4 ^@ http://purl.uniprot.org/uniprot/B8QI36 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||SAM ^@ http://togogenome.org/gene/10090:Plscr2 ^@ http://purl.uniprot.org/uniprot/Q9DCW2 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phospholipid scramblase 2|||Phosphothreonine; by PKC|||Proline-rich domain (PRD)|||S-palmitoyl cysteine|||SH3-binding 1|||SH3-binding 2 ^@ http://purl.uniprot.org/annotation/PRO_0000100788 http://togogenome.org/gene/10090:Rgs13 ^@ http://purl.uniprot.org/uniprot/Q8K443 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ RGS|||Regulator of G-protein signaling 13 ^@ http://purl.uniprot.org/annotation/PRO_0000204216 http://togogenome.org/gene/10090:Jkampl ^@ http://purl.uniprot.org/uniprot/Q9CR05 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Pcdha7 ^@ http://purl.uniprot.org/uniprot/Q91Y13 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||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|||Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself.|||Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself; when associated with L-284.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||No effect on homophilic interaction. Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself; when associated with Q-138.|||O-linked (Man) serine|||O-linked (Man) threonine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||Polar residues|||Protocadherin alpha-7 ^@ http://purl.uniprot.org/annotation/PRO_5008429382 http://togogenome.org/gene/10090:Or5p70 ^@ http://purl.uniprot.org/uniprot/Q8VF12 ^@ 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 5P70 ^@ http://purl.uniprot.org/annotation/PRO_0000150850 http://togogenome.org/gene/10090:Hbb-bt ^@ http://purl.uniprot.org/uniprot/A8DUK4|||http://purl.uniprot.org/uniprot/P02088 ^@ 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 ^@ Asymmetric dimethylarginine|||Globin family profile|||Hemoglobin subunit beta-1|||In allele S and allele W1.|||In allele S.|||In allele W1.|||N-acetylvaline|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||distal binding residue|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000053024 http://togogenome.org/gene/10090:Lrrc55 ^@ http://purl.uniprot.org/uniprot/A0A3B2WBQ3|||http://purl.uniprot.org/uniprot/Q3UY51 ^@ 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_0000232914|||http://purl.uniprot.org/annotation/PRO_5039987890 http://togogenome.org/gene/10090:Thrsp ^@ http://purl.uniprot.org/uniprot/Q543J4|||http://purl.uniprot.org/uniprot/Q62264|||http://purl.uniprot.org/uniprot/Q8BPB6 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Strand ^@ Chain|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Strand ^@ Disordered|||Phosphoserine|||Thyroid hormone-inducible hepatic protein ^@ http://purl.uniprot.org/annotation/PRO_0000123774 http://togogenome.org/gene/10090:Wdr26 ^@ http://purl.uniprot.org/uniprot/Q8C6G8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ CTLH|||Disordered|||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_0000051374 http://togogenome.org/gene/10090:Or13c7b ^@ http://purl.uniprot.org/uniprot/Q8VGA9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Acsl5 ^@ http://purl.uniprot.org/uniprot/Q3UC67|||http://purl.uniprot.org/uniprot/Q8JZR0 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Topological Domain|||Transmembrane ^@ AMP-dependent synthetase/ligase|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type III membrane protein|||Long-chain-fatty-acid--CoA ligase 5|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000193113 http://togogenome.org/gene/10090:Get1 ^@ http://purl.uniprot.org/uniprot/Q8K0D7 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Guided entry of tail-anchored proteins factor 1|||Helical|||Interaction with GET3/TRC40|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000065980 http://togogenome.org/gene/10090:Neto1 ^@ http://purl.uniprot.org/uniprot/Q8R4I7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ CUB 1|||CUB 2|||Cytoplasmic|||Extracellular|||Helical|||LDL-receptor class A|||N-linked (GlcNAc...) asparagine|||Neuropilin and tolloid-like protein 1|||PDZ-binding|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000021800 http://togogenome.org/gene/10090:Zdhhc19 ^@ http://purl.uniprot.org/uniprot/Q810M5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ DHHC|||Disordered|||Helical|||Palmitoyltransferase ZDHHC19|||Pro residues|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000448574 http://togogenome.org/gene/10090:Agpat4 ^@ http://purl.uniprot.org/uniprot/Q8K4X7 ^@ Chain|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Motif|||Transmembrane ^@ 1-acyl-sn-glycerol-3-phosphate acyltransferase delta|||HXXXXD motif|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000208198 http://togogenome.org/gene/10090:Slc6a5 ^@ http://purl.uniprot.org/uniprot/B2RQX9|||http://purl.uniprot.org/uniprot/B2RXV9 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Hnf4g ^@ http://purl.uniprot.org/uniprot/Q059V1|||http://purl.uniprot.org/uniprot/Q3UP48|||http://purl.uniprot.org/uniprot/Q9WUU6 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ Disordered|||Hepatocyte nuclear factor 4-gamma|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053563 http://togogenome.org/gene/10090:Mpg ^@ http://purl.uniprot.org/uniprot/Q04841 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ DNA-3-methyladenine glycosylase|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000100066 http://togogenome.org/gene/10090:4930512M02Rik ^@ http://purl.uniprot.org/uniprot/Q5SQK8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Grik3 ^@ http://purl.uniprot.org/uniprot/B1AS29 ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Glutamate receptor ionotropic, kainate 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000416793 http://togogenome.org/gene/10090:Stard3 ^@ http://purl.uniprot.org/uniprot/Q544C3|||http://purl.uniprot.org/uniprot/Q61542 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||FFAT|||Helical|||MENTAL|||Phosphoserine|||START|||StAR-related lipid transfer protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000220654 http://togogenome.org/gene/10090:Dcaf7 ^@ http://purl.uniprot.org/uniprot/P61963|||http://purl.uniprot.org/uniprot/Q80ZU1 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ DDB1- and CUL4-associated factor 7|||WD|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000051426 http://togogenome.org/gene/10090:Seh1l ^@ http://purl.uniprot.org/uniprot/Q8R2U0 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Nucleoporin SEH1|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000373806|||http://purl.uniprot.org/annotation/VSP_037232 http://togogenome.org/gene/10090:H1f10 ^@ http://purl.uniprot.org/uniprot/Q80ZM5 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||H15 ^@ http://togogenome.org/gene/10090:Klra17 ^@ http://purl.uniprot.org/uniprot/Q8BJS9|||http://purl.uniprot.org/uniprot/Q9JMA4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Gabrq ^@ http://purl.uniprot.org/uniprot/B1AUQ5|||http://purl.uniprot.org/uniprot/Q0VEX8|||http://purl.uniprot.org/uniprot/Q3TP00|||http://purl.uniprot.org/uniprot/Q9JLF1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Disordered|||Extracellular|||Gamma-aminobutyric acid receptor subunit theta|||Helical|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000496|||http://purl.uniprot.org/annotation/PRO_5014306843|||http://purl.uniprot.org/annotation/PRO_5022262050 http://togogenome.org/gene/10090:Apoc4 ^@ http://purl.uniprot.org/uniprot/Q61268 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ Apolipoprotein C-IV|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000002037 http://togogenome.org/gene/10090:Slc22a13 ^@ http://purl.uniprot.org/uniprot/Q6A4L0 ^@ 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 strain: FVB/N.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 13 ^@ http://purl.uniprot.org/annotation/PRO_0000230783 http://togogenome.org/gene/10090:Ppp1r27 ^@ http://purl.uniprot.org/uniprot/Q9D119 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ ANK 1|||ANK 2|||Protein phosphatase 1 regulatory subunit 27 ^@ http://purl.uniprot.org/annotation/PRO_0000264470 http://togogenome.org/gene/10090:C1galt1c1 ^@ http://purl.uniprot.org/uniprot/Q9JMG2 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ C1GALT1-specific chaperone 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000285075 http://togogenome.org/gene/10090:Lysmd2 ^@ http://purl.uniprot.org/uniprot/G3X915|||http://purl.uniprot.org/uniprot/Q9D7V2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||LysM|||LysM and putative peptidoglycan-binding domain-containing protein 2|||N-acetylalanine|||Phosphoserine|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000248003|||http://purl.uniprot.org/annotation/VSP_020124 http://togogenome.org/gene/10090:Rab24 ^@ http://purl.uniprot.org/uniprot/P35290 ^@ 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|||Sequence Conflict ^@ Accumulates in punctate structures in both cytoplasmic and nuclear compartments.|||Accumulates in punctate structures in both cytoplasmic and nuclear compartments. Disrupts the integrity of the nuclear envelope.|||Effector region|||Increase in GTPase activity. No effect neither on prenylation, nor on subcellular location.|||Predominantly in the GTP-bound state. No effect on subcellular location.|||Ras-related protein Rab-24|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121214 http://togogenome.org/gene/10090:Pof1b ^@ http://purl.uniprot.org/uniprot/Q8K4L4 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Sequence Conflict ^@ Protein POF1B ^@ http://purl.uniprot.org/annotation/PRO_0000253912 http://togogenome.org/gene/10090:Rap1b ^@ http://purl.uniprot.org/uniprot/Q99JI6 ^@ 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|||Region|||Sequence Conflict ^@ ADP-ribosylserine; by botulinum toxin|||Cysteine methyl ester|||Effector region|||Interaction with KRIT1|||Phosphoserine; by PKA|||Ras-related protein Rap-1b|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000030211|||http://purl.uniprot.org/annotation/PRO_0000030212 http://togogenome.org/gene/10090:Pnpla2 ^@ http://purl.uniprot.org/uniprot/Q8BJ56 ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DGA/G|||Disordered|||Extracellular|||GXGXXG|||GXSXG|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||In isoform 3.|||Loss of triacylglycerol hydrolysis activity.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PNPLA|||Patatin-like phospholipase domain-containing protein 2|||Phosphoserine; by PKA|||Phosphoserine; in vitro|||Proton acceptor|||Reduced TG hydrolase activity.|||Slightly reduced TG hydrolase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000292528|||http://purl.uniprot.org/annotation/VSP_026422|||http://purl.uniprot.org/annotation/VSP_026423|||http://purl.uniprot.org/annotation/VSP_026424 http://togogenome.org/gene/10090:Fabp7 ^@ http://purl.uniprot.org/uniprot/P51880 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ Fatty acid-binding protein, brain|||N-acetylvaline|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067374 http://togogenome.org/gene/10090:Marf1 ^@ http://purl.uniprot.org/uniprot/Q8BJ34 ^@ 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 and isoform 3.|||In isoform 2, isoform 3 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5 and isoform 6.|||In isoform 5.|||Meiosis regulator and mRNA stability factor 1|||NYN|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000276847|||http://purl.uniprot.org/annotation/VSP_022991|||http://purl.uniprot.org/annotation/VSP_022992|||http://purl.uniprot.org/annotation/VSP_022993|||http://purl.uniprot.org/annotation/VSP_022994|||http://purl.uniprot.org/annotation/VSP_022995|||http://purl.uniprot.org/annotation/VSP_022996|||http://purl.uniprot.org/annotation/VSP_022997|||http://purl.uniprot.org/annotation/VSP_022998|||http://purl.uniprot.org/annotation/VSP_022999|||http://purl.uniprot.org/annotation/VSP_023000|||http://purl.uniprot.org/annotation/VSP_023001|||http://purl.uniprot.org/annotation/VSP_023002 http://togogenome.org/gene/10090:Zp3r ^@ http://purl.uniprot.org/uniprot/G3X970|||http://purl.uniprot.org/uniprot/Q0VET1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Sushi ^@ http://purl.uniprot.org/annotation/PRO_5014306854|||http://purl.uniprot.org/annotation/PRO_5015091841 http://togogenome.org/gene/10090:Tssk3 ^@ http://purl.uniprot.org/uniprot/Q9D2E1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent ^@ Protein kinase|||Proton acceptor|||Testis-specific serine/threonine-protein kinase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000086771 http://togogenome.org/gene/10090:Or5af2 ^@ http://purl.uniprot.org/uniprot/Q5NC55 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fam83c ^@ http://purl.uniprot.org/uniprot/A2ARK0 ^@ 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 FAM83C ^@ http://purl.uniprot.org/annotation/PRO_0000434566 http://togogenome.org/gene/10090:Btbd3 ^@ http://purl.uniprot.org/uniprot/P58545|||http://purl.uniprot.org/uniprot/Q3TSN9|||http://purl.uniprot.org/uniprot/Q8CHC1 ^@ 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 ^@ BACK|||BTB|||BTB/POZ domain-containing protein 3|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000186212 http://togogenome.org/gene/10090:Rbfox3 ^@ http://purl.uniprot.org/uniprot/Q8BIF2 ^@ 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 ^@ Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 5.|||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_0000349208|||http://purl.uniprot.org/annotation/VSP_035219|||http://purl.uniprot.org/annotation/VSP_035220|||http://purl.uniprot.org/annotation/VSP_043949 http://togogenome.org/gene/10090:Napepld ^@ http://purl.uniprot.org/uniprot/Q8BH82 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000318160 http://togogenome.org/gene/10090:Vmn1r131 ^@ http://purl.uniprot.org/uniprot/D3YTY2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdca3 ^@ http://purl.uniprot.org/uniprot/Q99M54 ^@ 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|||Cell division cycle-associated protein 3|||Disordered|||F-box-like|||In isoform 2.|||KEN box|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000287709|||http://purl.uniprot.org/annotation/VSP_025606|||http://purl.uniprot.org/annotation/VSP_025607 http://togogenome.org/gene/10090:Btbd35f1 ^@ http://purl.uniprot.org/uniprot/A0A571BEF3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Adamts2 ^@ http://purl.uniprot.org/uniprot/Q8C9W3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Signal Peptide ^@ A disintegrin and metalloproteinase with thrombospondin motifs 2|||Cell attachment site|||Disintegrin|||Disordered|||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_0000029160|||http://purl.uniprot.org/annotation/PRO_0000029161 http://togogenome.org/gene/10090:Vmn1r199 ^@ http://purl.uniprot.org/uniprot/Q8R280 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp707 ^@ http://purl.uniprot.org/uniprot/D3Z445|||http://purl.uniprot.org/uniprot/Q8R0U9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Arl6 ^@ http://purl.uniprot.org/uniprot/O88848 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Splice Variant ^@ ADP-ribosylation factor-like protein 6|||In isoform 2.|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207473|||http://purl.uniprot.org/annotation/VSP_040512 http://togogenome.org/gene/10090:Magea14 ^@ http://purl.uniprot.org/uniprot/Q9D9G4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Nckap1 ^@ http://purl.uniprot.org/uniprot/A1L0U6|||http://purl.uniprot.org/uniprot/A2AS98|||http://purl.uniprot.org/uniprot/P28660 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||N-acetylserine|||Nck-associated protein 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000216173|||http://purl.uniprot.org/annotation/VSP_016261|||http://purl.uniprot.org/annotation/VSP_016262 http://togogenome.org/gene/10090:Cfap91 ^@ http://purl.uniprot.org/uniprot/Q8BRC6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant ^@ Cilia- and flagella-associated protein 91|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064419|||http://purl.uniprot.org/annotation/VSP_045751|||http://purl.uniprot.org/annotation/VSP_045752 http://togogenome.org/gene/10090:Muc19 ^@ http://purl.uniprot.org/uniprot/Q6PZE0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ 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|||4|||5|||6|||7|||8|||9|||Approximate repeats|||CTCK|||Disordered|||Mucin-19|||Polar residues|||TIL|||VWFC 1|||VWFC 2|||VWFD 1|||VWFD 2|||VWFD 3 ^@ http://purl.uniprot.org/annotation/PRO_5000093121 http://togogenome.org/gene/10090:Hecw2 ^@ http://purl.uniprot.org/uniprot/A3KPB7|||http://purl.uniprot.org/uniprot/Q6I6G8 ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||C2|||Disordered|||E3 ubiquitin-protein ligase HECW2|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||Interaction with TP73|||Phosphoserine|||Polar residues|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000277668|||http://purl.uniprot.org/annotation/VSP_023078 http://togogenome.org/gene/10090:Jazf1 ^@ http://purl.uniprot.org/uniprot/Q80ZQ5 ^@ 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 ^@ Acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; degenerate|||Disordered|||In isoform 2.|||Juxtaposed with another zinc finger protein 1|||Phosphothreonine|||Polar residues|||Required for interaction with NR2C2 ^@ http://purl.uniprot.org/annotation/PRO_0000046986|||http://purl.uniprot.org/annotation/VSP_007756 http://togogenome.org/gene/10090:St6gal2 ^@ http://purl.uniprot.org/uniprot/Q76K27 ^@ 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|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Beta-galactoside alpha-2,6-sialyltransferase 2|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000314786|||http://purl.uniprot.org/annotation/VSP_030357|||http://purl.uniprot.org/annotation/VSP_030358 http://togogenome.org/gene/10090:Slc35e2 ^@ http://purl.uniprot.org/uniprot/Q8C811 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||Solute carrier family 35 member E2A ^@ http://purl.uniprot.org/annotation/PRO_0000305058 http://togogenome.org/gene/10090:Ugt3a1 ^@ http://purl.uniprot.org/uniprot/Q3UP75 ^@ 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 3A1 ^@ http://purl.uniprot.org/annotation/PRO_0000299151 http://togogenome.org/gene/10090:Sin3a ^@ http://purl.uniprot.org/uniprot/Q60520 ^@ 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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Greatly reduced binding to MAD; when associated with A-329.|||Greatly reduced binding to MAD; when associated with A-332.|||Greatly reduced binding to MAD; when associated with D-308 and A-311.|||Greatly reduced binding to MAD; when associated with V-307 and A-311.|||Greatly reduced binding to MAD; when associated with V-307 and D-308.|||In isoform 2.|||Interaction with HCFC1|||Interaction with NCOR1|||Interaction with OGT|||Interaction with REST|||Interaction with SAP30|||Interactions with HDAC1 and ARID4B|||Interactions with SUDS3 and SAP130|||N6-acetyllysine|||No effect on binding to MAD.|||PAH 1|||PAH 2|||PAH 3|||Paired amphipathic helix protein Sin3a|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000121538|||http://purl.uniprot.org/annotation/VSP_039918 http://togogenome.org/gene/10090:Or5g23 ^@ http://purl.uniprot.org/uniprot/Q7TR99 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lefty2 ^@ http://purl.uniprot.org/uniprot/P57785 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Left-right determination factor 2|||N-linked (GlcNAc...) asparagine|||Or 135 ^@ http://purl.uniprot.org/annotation/PRO_0000033812|||http://purl.uniprot.org/annotation/PRO_0000033813 http://togogenome.org/gene/10090:Sun3 ^@ http://purl.uniprot.org/uniprot/E9LV81|||http://purl.uniprot.org/uniprot/Q5SS91 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Splice Variant|||Topological Domain|||Transmembrane ^@ Helical|||In isoform 2.|||Nuclear|||Perinuclear space|||SUN|||SUN domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000312222|||http://purl.uniprot.org/annotation/VSP_029750 http://togogenome.org/gene/10090:Kdm4a ^@ http://purl.uniprot.org/uniprot/A2A8L9|||http://purl.uniprot.org/uniprot/Q8BW72 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||Histone H3K4me3 binding|||In isoform 2.|||Interaction with NCOR1|||JmjC|||JmjN|||Lysine-specific demethylase 4A|||N-acetylalanine|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues|||Removed|||Tudor 1|||Tudor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000183173|||http://purl.uniprot.org/annotation/VSP_016144|||http://purl.uniprot.org/annotation/VSP_016145 http://togogenome.org/gene/10090:Gsx2 ^@ http://purl.uniprot.org/uniprot/P31316 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||GS homeobox 2|||Homeobox ^@ http://purl.uniprot.org/annotation/PRO_0000048897 http://togogenome.org/gene/10090:Rita1 ^@ http://purl.uniprot.org/uniprot/Q9D1H0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Motif|||Region ^@ Disordered|||Interaction with RBPJ/RBPSUH|||Interaction with tubulin|||Nuclear localization signal|||Polar residues|||Pro residues|||RBPJ-interacting and tubulin-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000294430 http://togogenome.org/gene/10090:Ankrd33 ^@ http://purl.uniprot.org/uniprot/Q8BXP5 ^@ 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 2.|||Photoreceptor ankyrin repeat protein|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000243909|||http://purl.uniprot.org/annotation/VSP_059268 http://togogenome.org/gene/10090:Ciao3 ^@ http://purl.uniprot.org/uniprot/Q7TMW6 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Cytosolic iron-sulfur assembly component 3|||Disordered|||In isoform 2.|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000288486|||http://purl.uniprot.org/annotation/VSP_025696 http://togogenome.org/gene/10090:Fbxo16 ^@ http://purl.uniprot.org/uniprot/Q14BG9|||http://purl.uniprot.org/uniprot/Q9QZM9 ^@ 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|||F-box|||F-box only protein 16|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000119897 http://togogenome.org/gene/10090:Rnf146 ^@ http://purl.uniprot.org/uniprot/Q9CTM5|||http://purl.uniprot.org/uniprot/Q9CZW6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF146|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Loss of PAR-binding and of protection against DNA damage; when associated with A-156.|||Loss of PAR-binding and of protection against DNA damage; when associated with A-157.|||Loss of ubiquitination activity.|||Loss of ubiquitination activity. Loss of protection against DNA damage. No effect on PAR-binding.|||Phosphoserine|||Polar residues|||RING-type|||WWE ^@ http://purl.uniprot.org/annotation/PRO_0000056108 http://togogenome.org/gene/10090:Scp2d1 ^@ http://purl.uniprot.org/uniprot/Q9DAH1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ SCP2|||SCP2 sterol-binding domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000079445 http://togogenome.org/gene/10090:Noxa1 ^@ http://purl.uniprot.org/uniprot/Q8CJ00 ^@ 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 ^@ Disordered|||In isoform 2.|||Mediates interaction with RAC1|||NADPH oxidase activator 1|||PB1|||Polar residues|||SH3|||TPR 1|||TPR 2|||TPR 3|||TPR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000314610|||http://purl.uniprot.org/annotation/VSP_030337 http://togogenome.org/gene/10090:Cntf ^@ http://purl.uniprot.org/uniprot/P51642 ^@ Chain|||Molecule Processing ^@ Chain ^@ Ciliary neurotrophic factor ^@ http://purl.uniprot.org/annotation/PRO_0000149520 http://togogenome.org/gene/10090:Tmem222 ^@ http://purl.uniprot.org/uniprot/Q8BVA2 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Transmembrane protein 222 ^@ http://purl.uniprot.org/annotation/PRO_0000247964 http://togogenome.org/gene/10090:Prkaca ^@ http://purl.uniprot.org/uniprot/P05132 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ AGC-kinase C-terminal|||Deamidated asparagine; partial|||Does not affect interaction with SMO; when associated with Q-88.|||Does not affect interaction with SMO; when associated with R-197.|||Impaired inhibition by the R-subunit.|||In isoform 2.|||N-myristoyl glycine|||No phosphorylation by PDPK1.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Reduced catalytic activity and impaired inhibition by the R-subunit.|||Reduced interaction with SMO.|||Removed|||cAMP-dependent protein kinase catalytic subunit alpha ^@ http://purl.uniprot.org/annotation/PRO_0000086053|||http://purl.uniprot.org/annotation/VSP_004760 http://togogenome.org/gene/10090:Prlhr ^@ http://purl.uniprot.org/uniprot/Q6VMN6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||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|||Prolactin-releasing peptide receptor|||Required for interaction with GRIP1, GRIP2 and PICK1 ^@ http://purl.uniprot.org/annotation/PRO_0000069525 http://togogenome.org/gene/10090:Trpm1 ^@ http://purl.uniprot.org/uniprot/Q2TV84 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transient receptor potential cation channel subfamily M member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000328931|||http://purl.uniprot.org/annotation/VSP_052751|||http://purl.uniprot.org/annotation/VSP_052752|||http://purl.uniprot.org/annotation/VSP_052753|||http://purl.uniprot.org/annotation/VSP_052754|||http://purl.uniprot.org/annotation/VSP_052755|||http://purl.uniprot.org/annotation/VSP_052756|||http://purl.uniprot.org/annotation/VSP_052757|||http://purl.uniprot.org/annotation/VSP_052758 http://togogenome.org/gene/10090:Rreb1 ^@ http://purl.uniprot.org/uniprot/Q3UH06 ^@ 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 ^@ Acidic residues|||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|||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.|||Phosphoserine|||Polar residues|||Pro residues|||Ras-responsive element-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000295155|||http://purl.uniprot.org/annotation/VSP_026765|||http://purl.uniprot.org/annotation/VSP_026766|||http://purl.uniprot.org/annotation/VSP_026767|||http://purl.uniprot.org/annotation/VSP_026768 http://togogenome.org/gene/10090:Cntnap2 ^@ http://purl.uniprot.org/uniprot/E9QNF7|||http://purl.uniprot.org/uniprot/Q3SYI6|||http://purl.uniprot.org/uniprot/Q9CPW0 ^@ 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 ^@ Contactin-associated protein-like 2|||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|||Neurexin/syndecan/glycophorin C|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000019507|||http://purl.uniprot.org/annotation/PRO_5003243345|||http://purl.uniprot.org/annotation/VSP_014977 http://togogenome.org/gene/10090:Or8b39 ^@ http://purl.uniprot.org/uniprot/Q9EQA6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sirpb1b ^@ http://purl.uniprot.org/uniprot/Q3U390 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Ig-like ^@ http://togogenome.org/gene/10090:Pbk ^@ http://purl.uniprot.org/uniprot/Q9JJ78 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Lymphokine-activated killer T-cell-originated protein kinase|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086764 http://togogenome.org/gene/10090:Lhfpl4 ^@ http://purl.uniprot.org/uniprot/Q5U4E0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||LHFPL tetraspan subfamily member 4 protein ^@ http://purl.uniprot.org/annotation/PRO_0000285962 http://togogenome.org/gene/10090:Catsperz ^@ http://purl.uniprot.org/uniprot/Q9CQP8 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict ^@ Chain|||Helix|||Sequence Conflict ^@ Cation channel sperm-associated auxiliary subunit zeta ^@ http://purl.uniprot.org/annotation/PRO_0000349323 http://togogenome.org/gene/10090:Gtpbp3 ^@ http://purl.uniprot.org/uniprot/Q923K4 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Mitochondrion|||TrmE-type G|||tRNA modification GTPase GTPBP3, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000280266|||http://purl.uniprot.org/annotation/VSP_023585|||http://purl.uniprot.org/annotation/VSP_023586 http://togogenome.org/gene/10090:Crisp4 ^@ http://purl.uniprot.org/uniprot/E9PVG4|||http://purl.uniprot.org/uniprot/G5E862|||http://purl.uniprot.org/uniprot/Q9D259 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||ShKT ^@ http://purl.uniprot.org/annotation/PRO_5015099675 http://togogenome.org/gene/10090:Vmn2r99 ^@ http://purl.uniprot.org/uniprot/H3BK37 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003580908 http://togogenome.org/gene/10090:Dip2a ^@ http://purl.uniprot.org/uniprot/F8WI56|||http://purl.uniprot.org/uniprot/Q8BWT5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ DMAP1-binding|||Disco-interacting protein 2 homolog A|||Disordered|||PXXP motif; required for interaction with CTTN|||Phosphothreonine|||Polar residues|||Significantly reduced interaction with CTTN; when associated with 235-AKRA-238.|||Significantly reduced interaction with CTTN; when associated with 259-ANQA-262. ^@ http://purl.uniprot.org/annotation/PRO_0000079907 http://togogenome.org/gene/10090:Pclo ^@ http://purl.uniprot.org/uniprot/Q9QYX7 ^@ 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|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||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 2.|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein piccolo ^@ http://purl.uniprot.org/annotation/PRO_0000058251|||http://purl.uniprot.org/annotation/VSP_003928|||http://purl.uniprot.org/annotation/VSP_003929 http://togogenome.org/gene/10090:Lcn6 ^@ http://purl.uniprot.org/uniprot/A2AJB9|||http://purl.uniprot.org/uniprot/G8XSM1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5003518870|||http://purl.uniprot.org/annotation/PRO_5015086015 http://togogenome.org/gene/10090:Or11g7 ^@ http://purl.uniprot.org/uniprot/E9PV79 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Myg1 ^@ http://purl.uniprot.org/uniprot/Q9JK81 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ MYG1 exonuclease|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000213484 http://togogenome.org/gene/10090:Aldh8a1 ^@ http://purl.uniprot.org/uniprot/Q8BH00 ^@ 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 ^@ 2-aminomuconic semialdehyde dehydrogenase|||In strain: FVB/N.|||Nucleophile|||Phosphoserine|||Proton acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000312955 http://togogenome.org/gene/10090:Arsk ^@ http://purl.uniprot.org/uniprot/A0A0R4J1N2|||http://purl.uniprot.org/uniprot/Q9D2L1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 3-oxoalanine (Cys)|||Arylsulfatase K|||Disordered|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Sulfatase N-terminal|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000356286|||http://purl.uniprot.org/annotation/PRO_5006452017 http://togogenome.org/gene/10090:Taar2 ^@ http://purl.uniprot.org/uniprot/Q5QD17 ^@ 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|||Trace amine-associated receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000070147 http://togogenome.org/gene/10090:Prkcg ^@ http://purl.uniprot.org/uniprot/P63318|||http://purl.uniprot.org/uniprot/Q2NKI4|||http://purl.uniprot.org/uniprot/Q3UN66 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Zinc Finger ^@ AGC-kinase C-terminal|||C2|||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_0000055690 http://togogenome.org/gene/10090:Tmprss11f ^@ http://purl.uniprot.org/uniprot/Q8BHM9 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||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_0000299323 http://togogenome.org/gene/10090:Mipol1 ^@ http://purl.uniprot.org/uniprot/E9Q8Z7 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Amd1 ^@ http://purl.uniprot.org/uniprot/P0DMN7 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Site ^@ Cleavage (non-hydrolytic); by autolysis|||Phosphoserine|||Proton acceptor; for processing activity|||Proton donor; for catalytic activity|||Pyruvic acid (Ser); by autocatalysis|||S-adenosylmethionine decarboxylase 1 alpha chain|||S-adenosylmethionine decarboxylase 1 beta chain|||Schiff-base intermediate with substrate; via pyruvic acid ^@ http://purl.uniprot.org/annotation/PRO_0000029963|||http://purl.uniprot.org/annotation/PRO_0000029964 http://togogenome.org/gene/10090:Abcc9 ^@ http://purl.uniprot.org/uniprot/E9PUE8|||http://purl.uniprot.org/uniprot/P70170 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 9|||Acidic residues|||Cytoplasmic|||Disordered|||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=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform SUR2B.|||In isoform SUR2C.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000093403|||http://purl.uniprot.org/annotation/VSP_000059|||http://purl.uniprot.org/annotation/VSP_000060 http://togogenome.org/gene/10090:Or8b48 ^@ http://purl.uniprot.org/uniprot/A0A1L1SSS5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zmym3 ^@ http://purl.uniprot.org/uniprot/B1AXS5|||http://purl.uniprot.org/uniprot/B1AXS6|||http://purl.uniprot.org/uniprot/B1AXS7|||http://purl.uniprot.org/uniprot/Q32P02|||http://purl.uniprot.org/uniprot/Q8CG95|||http://purl.uniprot.org/uniprot/Q9JLM4 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000191379 http://togogenome.org/gene/10090:Grin2c ^@ http://purl.uniprot.org/uniprot/A2A6S2|||http://purl.uniprot.org/uniprot/Q01098 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||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|||Polar residues|||Pore-forming|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000011581|||http://purl.uniprot.org/annotation/PRO_5014296793 http://togogenome.org/gene/10090:Tcf19 ^@ http://purl.uniprot.org/uniprot/G3XA31|||http://purl.uniprot.org/uniprot/Q99KJ5 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||FHA|||Phosphoserine|||Transcription factor 19-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000059330 http://togogenome.org/gene/10090:Atp8b2 ^@ http://purl.uniprot.org/uniprot/E9QAL4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||P-type ATPase C-terminal|||P-type ATPase N-terminal ^@ http://togogenome.org/gene/10090:Cblc ^@ http://purl.uniprot.org/uniprot/G3X9U0|||http://purl.uniprot.org/uniprot/Q80XL1 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 4H|||Cbl-PTB|||Disordered|||E3 ubiquitin-protein ligase CBL-C|||EF-hand-like|||In isoform 2.|||Interaction with RET|||Linker|||Phosphotyrosine; by SRC|||RING-type|||SH2-like ^@ http://purl.uniprot.org/annotation/PRO_0000055867|||http://purl.uniprot.org/annotation/VSP_014946|||http://purl.uniprot.org/annotation/VSP_014947 http://togogenome.org/gene/10090:Tor1aip1 ^@ http://purl.uniprot.org/uniprot/E9PWW2|||http://purl.uniprot.org/uniprot/Q921T2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||In isoform 2.|||In isoform 3.|||Interaction with TOR1A|||N-linked (GlcNAc...) asparagine|||Nuclear|||Perinuclear space|||Phosphoserine|||Phosphothreonine|||Polar residues|||Torsin-1A-interacting protein 1|||Torsin-1A-interacting protein 1/2 AAA+ activator|||Torsin-1A-interacting protein 1/2 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000228836|||http://purl.uniprot.org/annotation/VSP_042952|||http://purl.uniprot.org/annotation/VSP_042953 http://togogenome.org/gene/10090:Qpctl ^@ http://purl.uniprot.org/uniprot/Q8BH73 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Glutaminyl-peptide cyclotransferase-like protein|||Helical|||In isoform 2.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000302004|||http://purl.uniprot.org/annotation/VSP_027904 http://togogenome.org/gene/10090:Kif21b ^@ http://purl.uniprot.org/uniprot/F8VQE2|||http://purl.uniprot.org/uniprot/Q9QXL1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Abolishes processive activity.|||Acidic residues|||Basic and acidic residues|||Disordered|||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_0000125465 http://togogenome.org/gene/10090:Frmd6 ^@ http://purl.uniprot.org/uniprot/Q8C0V9 ^@ 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 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000219449|||http://purl.uniprot.org/annotation/VSP_008024|||http://purl.uniprot.org/annotation/VSP_008025|||http://purl.uniprot.org/annotation/VSP_008026|||http://purl.uniprot.org/annotation/VSP_008027|||http://purl.uniprot.org/annotation/VSP_008028 http://togogenome.org/gene/10090:S100z ^@ http://purl.uniprot.org/uniprot/B9EJL3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ EF-hand ^@ http://togogenome.org/gene/10090:Odf2 ^@ http://purl.uniprot.org/uniprot/A3KGV1|||http://purl.uniprot.org/uniprot/A3KGW0|||http://purl.uniprot.org/uniprot/Q3UFG2 ^@ Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Crosslink|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 6.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 7.|||Outer dense fiber protein 2|||Phosphoserine|||Phosphoserine; by TSSK4|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000299458|||http://purl.uniprot.org/annotation/VSP_027671|||http://purl.uniprot.org/annotation/VSP_027672|||http://purl.uniprot.org/annotation/VSP_027673|||http://purl.uniprot.org/annotation/VSP_027674|||http://purl.uniprot.org/annotation/VSP_027675|||http://purl.uniprot.org/annotation/VSP_027676 http://togogenome.org/gene/10090:Zc3h12c ^@ http://purl.uniprot.org/uniprot/E9Q1I3|||http://purl.uniprot.org/uniprot/Q5DTV4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Zinc Finger ^@ Basic and acidic residues|||C3H1-type|||Disordered|||Phosphoserine|||Polar residues|||Probable ribonuclease ZC3H12C|||RNase NYN ^@ http://purl.uniprot.org/annotation/PRO_0000337844 http://togogenome.org/gene/10090:Fam171a2 ^@ http://purl.uniprot.org/uniprot/A2A699 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protein FAM171A2 ^@ http://purl.uniprot.org/annotation/PRO_0000328772|||http://purl.uniprot.org/annotation/VSP_032783 http://togogenome.org/gene/10090:Slc25a32 ^@ http://purl.uniprot.org/uniprot/Q3UM21|||http://purl.uniprot.org/uniprot/Q8BMG8 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Repeat|||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 32 ^@ http://purl.uniprot.org/annotation/PRO_0000090643 http://togogenome.org/gene/10090:Calhm2 ^@ http://purl.uniprot.org/uniprot/Q3V3G1|||http://purl.uniprot.org/uniprot/Q4VA34|||http://purl.uniprot.org/uniprot/Q8VEC4 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Non-terminal Residue|||Sequence Conflict|||Transmembrane ^@ Calcium homeostasis modulator protein 2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000186721 http://togogenome.org/gene/10090:Prm1 ^@ http://purl.uniprot.org/uniprot/P02319 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing ^@ Chain|||Disulfide Bond ^@ Interchain (with C-22)|||Interchain (with C-37)|||Interchain (with C-6)|||Sperm protamine P1 ^@ http://purl.uniprot.org/annotation/PRO_0000191498 http://togogenome.org/gene/10090:Cstf2 ^@ http://purl.uniprot.org/uniprot/A2AEK1|||http://purl.uniprot.org/uniprot/Q8BIQ5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 10|||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|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081532|||http://purl.uniprot.org/annotation/VSP_014844|||http://purl.uniprot.org/annotation/VSP_014845 http://togogenome.org/gene/10090:Abhd12 ^@ http://purl.uniprot.org/uniprot/Q99LR1 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Charge relay system|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Lysophosphatidylserine lipase ABHD12|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000079414|||http://purl.uniprot.org/annotation/VSP_057493 http://togogenome.org/gene/10090:Slc45a1 ^@ http://purl.uniprot.org/uniprot/Q8BIV7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Phosphothreonine|||Proton-associated sugar transporter A ^@ http://purl.uniprot.org/annotation/PRO_0000122515 http://togogenome.org/gene/10090:Tex47 ^@ http://purl.uniprot.org/uniprot/Q9D5W8 ^@ Chain|||Molecule Processing ^@ Chain ^@ Testis-expressed protein 47 ^@ http://purl.uniprot.org/annotation/PRO_0000321828 http://togogenome.org/gene/10090:Gbx1 ^@ http://purl.uniprot.org/uniprot/P82976 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein GBX-1|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000048879 http://togogenome.org/gene/10090:Ofd1 ^@ http://purl.uniprot.org/uniprot/A2AEG2|||http://purl.uniprot.org/uniprot/Q3URP3|||http://purl.uniprot.org/uniprot/Q80Z25 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Centriole and centriolar satellite protein OFD1|||Disordered|||Induces centriole elongation. Impaired CEP164 and IFT88 recruitment. Impaired ciliogenesis.|||Induces centriole elongation. Impaired IFT88 recruitment. Impaired ciliogenesis.|||Induces centriole elongation. Impaired IFT88 recruitment. Reduced ciliogenesis.|||Induces centriole elongation. Reduced ciliogenesis.|||LisH|||Mediates homooligomerization|||Phosphoserine|||Polar residues|||Shortened centrioles. Reduced ciliogenesis. ^@ http://purl.uniprot.org/annotation/PRO_0000278573 http://togogenome.org/gene/10090:Vil1 ^@ http://purl.uniprot.org/uniprot/Q62468|||http://purl.uniprot.org/uniprot/Q8CEJ4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Core|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||Gelsolin-like 6|||HP|||Headpiece|||LPA/PIP2-binding site 1|||LPA/PIP2-binding site 2|||LPA/PIP2-binding site 3|||Necessary for homodimerization|||Phosphoserine|||Villin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000218728 http://togogenome.org/gene/10090:Cyp4a30b ^@ http://purl.uniprot.org/uniprot/A0A087WS15 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Dusp13a ^@ http://purl.uniprot.org/uniprot/Q6B8I0 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ Dual specificity protein phosphatase 13A|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000381974 http://togogenome.org/gene/10090:Pigo ^@ http://purl.uniprot.org/uniprot/A2AG36|||http://purl.uniprot.org/uniprot/Q562G0 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Lrrfip2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J169|||http://purl.uniprot.org/uniprot/E9QN52|||http://purl.uniprot.org/uniprot/Q91WK0 ^@ 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-rich repeat flightless-interacting protein 2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000245247|||http://purl.uniprot.org/annotation/VSP_019678 http://togogenome.org/gene/10090:Or4c105 ^@ http://purl.uniprot.org/uniprot/Q8VF98 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Xcl1 ^@ http://purl.uniprot.org/uniprot/P47993|||http://purl.uniprot.org/uniprot/Q542T1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide ^@ Chemokine interleukin-8-like|||Disordered|||Lymphotactin|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000005249|||http://purl.uniprot.org/annotation/PRO_5014309595 http://togogenome.org/gene/10090:Cry1 ^@ http://purl.uniprot.org/uniprot/P97784 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Abolishes transcriptional repression of target genes. Abolishes interaction with PER2.|||Cryptochrome-1|||Decreases affinity for FBXL3. Slightly increases affinity for PER2.|||Decreases transcriptional repression of target genes. Decreases FBXL3 binding. Increases PER2 binding.|||Disordered|||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|||Lengthen circadian period. No effect on repressive activity. Increases protein stability.|||Loss of interaction with MAP1LC3B and significant decrease in its autophagy-mediated degradation; when associated with A-494.|||Loss of interaction with MAP1LC3B and significant decrease in its autophagy-mediated degradation; when associated with A-497.|||Loss of ubiquitination. No loss of interaction with DDB1-CUL4A complex.|||No effect on circadian period length and protein stability.|||No effect on its interaction with MAP1LC3B and moderate decrease in its autophagy-mediated degradation; when associated with A-287.|||No effect on its interaction with MAP1LC3B and moderate decrease in its autophagy-mediated degradation; when associated with A-290.|||No effect on its interaction with MAP1LC3B and moderate decrease in its autophagy-mediated degradation; when associated with A-488.|||No effect on its interaction with MAP1LC3B and moderate decrease in its autophagy-mediated degradation; when associated with A-491.|||Phosphomimetic mutant that leads to destabilization of the protein and abolishes ability to bind PER2; when associated with D-280.|||Phosphomimetic mutant that leads to destabilization of the protein and abolishes ability to bind PER2; when associated with D-71.|||Phosphomimetic mutant that leads to stabilization of the protein; when associated with A-280.|||Phosphomimetic mutant that leads to stabilization of the protein; when associated with A-71.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by MAPK|||Photolyase/cryptochrome alpha/beta|||Reduced MAPK-catalyzed in vitro phosphorylation. No effect on inhibition of CLOCK-BMAL1-mediated transcriptional activity.|||Reduced inhibition of CLOCK-BMAL1-mediated transcriptional activity.|||Reduced interaction with MAP1LC3B and significant decrease in its autophagy-mediated degradation; when associated with A-273.|||Reduced interaction with MAP1LC3B and significant decrease in its autophagy-mediated degradation; when associated with A-276.|||Reduces affinity for FBXL3.|||Required for inhibition of CLOCK-BMAL1-mediated transcription|||Sensitive to FBXL3-ediated degradation but noz affected by expression of FBXL21.|||Strongly reduces FBXL3 binding. Reduces PER2 binding. ^@ http://purl.uniprot.org/annotation/PRO_0000261142 http://togogenome.org/gene/10090:Hdac1 ^@ http://purl.uniprot.org/uniprot/O09106|||http://purl.uniprot.org/uniprot/Q58E49 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||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 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|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methylated lysine; by EHMT2|||Phosphoserine|||Proton acceptor|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000114688 http://togogenome.org/gene/10090:BC049762 ^@ http://purl.uniprot.org/uniprot/Q8C601 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Glyr1 ^@ http://purl.uniprot.org/uniprot/D3YYT1|||http://purl.uniprot.org/uniprot/Q922P9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ A.T hook|||Basic and acidic residues|||Cytokine-like nuclear factor N-PAC|||Dehydrogenase domain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with KDM1B|||Interaction with histone H3|||Mutant animals are born at expected Mendelian ratios. 54% mutants display postnatal lethality between days 0 and 1. They show centricular septal defects.|||PWWP|||Phosphoserine|||Required to promote KDM1B demethylase activity toward histone H3K4me1 and H3K4me2 ^@ http://purl.uniprot.org/annotation/PRO_0000312122 http://togogenome.org/gene/10090:Ptprt ^@ http://purl.uniprot.org/uniprot/B1AQN2|||http://purl.uniprot.org/uniprot/Q99M80 ^@ 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|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||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_0000025464|||http://purl.uniprot.org/annotation/PRO_5002761906|||http://purl.uniprot.org/annotation/VSP_007803|||http://purl.uniprot.org/annotation/VSP_007804|||http://purl.uniprot.org/annotation/VSP_007805|||http://purl.uniprot.org/annotation/VSP_007806 http://togogenome.org/gene/10090:Uck2 ^@ http://purl.uniprot.org/uniprot/Q543C2|||http://purl.uniprot.org/uniprot/Q99PM9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylalanine|||Phosphoribulokinase/uridine kinase|||Phosphoserine|||Polar residues|||Removed|||Uridine-cytidine kinase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000164456 http://togogenome.org/gene/10090:Ropn1l ^@ http://purl.uniprot.org/uniprot/Q9EQ00 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ RIIa|||Ropporin-1-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000307400 http://togogenome.org/gene/10090:Ikzf3 ^@ http://purl.uniprot.org/uniprot/O08900 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Mediates homodimerization and heterodimerization|||No effect on protein abundance. Changed DNA-binding transcription factor 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. Profound B cell development defects observed in homozygous or heterozygous animals. Impairs the differentiation of cells in adaptive immunity.|||Phosphoserine|||Phosphothreonine|||Zinc finger protein Aiolos ^@ http://purl.uniprot.org/annotation/PRO_0000047091 http://togogenome.org/gene/10090:Osr1 ^@ http://purl.uniprot.org/uniprot/Q9WVG7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Modified Residue|||Zinc Finger ^@ Asymmetric dimethylarginine|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Protein odd-skipped-related 1 ^@ http://purl.uniprot.org/annotation/PRO_0000047005 http://togogenome.org/gene/10090:Mmd2 ^@ http://purl.uniprot.org/uniprot/Q3V1Z9|||http://purl.uniprot.org/uniprot/Q8R189 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Monocyte to macrophage differentiation factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000218858 http://togogenome.org/gene/10090:Cd99l2 ^@ http://purl.uniprot.org/uniprot/Q8BIF0 ^@ 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 ^@ Basic and acidic residues|||CD99 antigen-like protein 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||O-linked (Xyl...) (chondroitin sulfate) serine ^@ http://purl.uniprot.org/annotation/PRO_0000340093|||http://purl.uniprot.org/annotation/VSP_034186 http://togogenome.org/gene/10090:Tmpo ^@ http://purl.uniprot.org/uniprot/Q3TNH0|||http://purl.uniprot.org/uniprot/Q3TXQ1|||http://purl.uniprot.org/uniprot/Q61029|||http://purl.uniprot.org/uniprot/Q61033 ^@ 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|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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 Delta.|||In isoform Epsilon.|||In isoform Gamma.|||In isoform Zeta.|||LEM|||LEM-like|||Lamina-associated polypeptide 2, isoforms alpha/zeta|||Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gamma|||Linker|||Lumenal|||N6-acetyllysine|||NAKAP95-binding C|||NAKAP95-binding N|||Nuclear localization signal|||Nucleoplasmic|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000206145|||http://purl.uniprot.org/annotation/PRO_0000206146|||http://purl.uniprot.org/annotation/VSP_010128|||http://purl.uniprot.org/annotation/VSP_010129|||http://purl.uniprot.org/annotation/VSP_010130|||http://purl.uniprot.org/annotation/VSP_010131|||http://purl.uniprot.org/annotation/VSP_010132 http://togogenome.org/gene/10090:Rpn2 ^@ http://purl.uniprot.org/uniprot/Q9DBG6 ^@ Chain|||Crosslink|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000022248 http://togogenome.org/gene/10090:Atrx ^@ http://purl.uniprot.org/uniprot/Q61687 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ ADD|||Acidic residues|||Basic and acidic residues|||Basic residues|||Citrulline|||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|||Interaction with DAXX|||Interaction with MECP2|||Omega-N-methylarginine|||PHD-type; atypical|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||PxVxL motif|||Reduces pericentromeric localization. Abolishes pericentromeric localization; when associated with E-580.|||Reduces pericentromeric localization. Abolishes pericentromeric localization; when associated with G-239.|||Transcriptional regulator ATRX ^@ http://purl.uniprot.org/annotation/PRO_0000074303 http://togogenome.org/gene/10090:Srp54a ^@ http://purl.uniprot.org/uniprot/P14576 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||M-domain|||NG-domain|||Signal recognition particle subunit SRP54 ^@ http://purl.uniprot.org/annotation/PRO_0000101194|||http://purl.uniprot.org/annotation/VSP_014953|||http://purl.uniprot.org/annotation/VSP_014954 http://togogenome.org/gene/10090:Gm14459 ^@ http://purl.uniprot.org/uniprot/A2BI73 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB|||KRAB-related ^@ http://togogenome.org/gene/10090:Nsmce3 ^@ http://purl.uniprot.org/uniprot/Q9CPR8 ^@ 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|||Interaction with NSMCE1|||MAGE|||Non-structural maintenance of chromosomes element 3 homolog|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000156734 http://togogenome.org/gene/10090:Vmn1r64 ^@ http://purl.uniprot.org/uniprot/Q8R2B8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Agap3 ^@ http://purl.uniprot.org/uniprot/A0A0G2JDW1|||http://purl.uniprot.org/uniprot/F8VQE9|||http://purl.uniprot.org/uniprot/Q8BV81 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat ^@ ANK|||Arf-GAP|||Disordered|||PH|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Igfbp7 ^@ http://purl.uniprot.org/uniprot/F8WH23|||http://purl.uniprot.org/uniprot/Q61581 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ IGFBP N-terminal|||Ig-like|||Ig-like C2-type|||In RNA edited version.|||Insulin-like growth factor-binding protein 7|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000014393|||http://purl.uniprot.org/annotation/PRO_5003385584 http://togogenome.org/gene/10090:Ccr2 ^@ http://purl.uniprot.org/uniprot/P51683|||http://purl.uniprot.org/uniprot/Q3TRK1|||http://purl.uniprot.org/uniprot/Q543S8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-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|||Phosphotyrosine; by JAK2 ^@ http://purl.uniprot.org/annotation/PRO_0000069234 http://togogenome.org/gene/10090:Exoc3l ^@ http://purl.uniprot.org/uniprot/Q8BI71 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Exocyst complex component 3-like protein|||Mediates interaction with EXOC2, EXOC4 and EXOC5 ^@ http://purl.uniprot.org/annotation/PRO_0000309475 http://togogenome.org/gene/10090:Aldh1a3 ^@ http://purl.uniprot.org/uniprot/Q3UIA4|||http://purl.uniprot.org/uniprot/Q9JHW9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Aldehyde dehydrogenase|||Disordered|||N-acetylalanine|||Nucleophile|||Proton acceptor|||Removed|||Retinaldehyde dehydrogenase 3|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000056479 http://togogenome.org/gene/10090:Slc26a1 ^@ http://purl.uniprot.org/uniprot/G5E8U1|||http://purl.uniprot.org/uniprot/P58735|||http://purl.uniprot.org/uniprot/Q3UPH6 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Transmembrane ^@ Decreased sulfate-hydrogencarbonate exchange activity. Does not affect localization to plasma membrane.|||Decreased sulfate-hydrogencarbonate exchange activity. Increased accumulation of protein in ER.|||Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||STAS|||Sulfate anion transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000080156 http://togogenome.org/gene/10090:Glipr2 ^@ http://purl.uniprot.org/uniprot/Q9CYL5 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict ^@ Golgi-associated plant pathogenesis-related protein 1|||Interaction with CAV1|||N-myristoyl glycine|||Removed|||SCP ^@ http://purl.uniprot.org/annotation/PRO_0000211525 http://togogenome.org/gene/10090:Mc1r ^@ http://purl.uniprot.org/uniprot/A0A0B6VTJ4|||http://purl.uniprot.org/uniprot/Q01727 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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|||Melanocyte-stimulating hormone receptor|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069834 http://togogenome.org/gene/10090:Or1o1 ^@ http://purl.uniprot.org/uniprot/Q7TRK4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or2a12 ^@ http://purl.uniprot.org/uniprot/Q8VEV0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dop1a ^@ http://purl.uniprot.org/uniprot/H7BWZ9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Dopey N-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Atp2a2 ^@ http://purl.uniprot.org/uniprot/O55143|||http://purl.uniprot.org/uniprot/Q5DTI2 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 isoform 2.|||Interaction with HAX1|||Interaction with PLN|||Interaction with TMEM64 and PDIA3|||Lumenal|||Phosphoserine|||Phosphothreonine|||Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000046197|||http://purl.uniprot.org/annotation/VSP_000359 http://togogenome.org/gene/10090:Styxl1 ^@ http://purl.uniprot.org/uniprot/D3YZ02|||http://purl.uniprot.org/uniprot/Q9DAG7|||http://purl.uniprot.org/uniprot/Q9DAR2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Tyrosine-protein phosphatase ^@ http://togogenome.org/gene/10090:Krtap24-1 ^@ http://purl.uniprot.org/uniprot/Q8CAZ5 ^@ Experimental Information|||Non-terminal Residue ^@ Non-terminal Residue ^@ ^@ http://togogenome.org/gene/10090:Sema3c ^@ http://purl.uniprot.org/uniprot/Q62181 ^@ 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 ^@ Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3C ^@ http://purl.uniprot.org/annotation/PRO_0000032312 http://togogenome.org/gene/10090:Mrpl17 ^@ http://purl.uniprot.org/uniprot/Q9D8P4 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant|||Transit Peptide ^@ Chain|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Large ribosomal subunit protein bL17m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000237332|||http://purl.uniprot.org/annotation/VSP_018590|||http://purl.uniprot.org/annotation/VSP_018591 http://togogenome.org/gene/10090:Ppt2 ^@ http://purl.uniprot.org/uniprot/O35448 ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Lysosomal thioesterase PPT2|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000025555 http://togogenome.org/gene/10090:Mettl22 ^@ http://purl.uniprot.org/uniprot/Q8R1C6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Methyltransferase-like protein 22|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000286592 http://togogenome.org/gene/10090:U2af1 ^@ http://purl.uniprot.org/uniprot/G3UW94|||http://purl.uniprot.org/uniprot/Q14C24|||http://purl.uniprot.org/uniprot/Q9D883 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||Disordered|||N-acetylalanine|||N6-methyllysine|||Omega-N-methylarginine|||Phosphoserine|||RRM|||Removed|||Splicing factor U2AF 35 kDa subunit ^@ http://purl.uniprot.org/annotation/PRO_0000081995 http://togogenome.org/gene/10090:Alb ^@ http://purl.uniprot.org/uniprot/P07724|||http://purl.uniprot.org/uniprot/Q546G4 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Albumin|||Albumin 1|||Albumin 2|||Albumin 3|||Aspirin-acetylated lysine|||N6-methyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000001073|||http://purl.uniprot.org/annotation/PRO_0000001074|||http://purl.uniprot.org/annotation/PRO_5015097767 http://togogenome.org/gene/10090:Vps26a ^@ http://purl.uniprot.org/uniprot/P40336 ^@ 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 ^@ Decreases interaction with SNX27.|||Disordered|||Disrupts interaction with VPS35:VPS29 dimer; no endosomal localization.|||In isoform 2.|||Phosphoserine|||Polar residues|||Vacuolar protein sorting-associated protein 26A ^@ http://purl.uniprot.org/annotation/PRO_0000073008|||http://purl.uniprot.org/annotation/VSP_019926 http://togogenome.org/gene/10090:Irs1 ^@ http://purl.uniprot.org/uniprot/P35569|||http://purl.uniprot.org/uniprot/Q543V3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||GRB2-binding|||IRS-type PTB|||Insulin receptor substrate 1|||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 ROCK2|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by INSR|||Polar 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_0000084237 http://togogenome.org/gene/10090:Ccne2 ^@ http://purl.uniprot.org/uniprot/A2API1|||http://purl.uniprot.org/uniprot/Q544H6|||http://purl.uniprot.org/uniprot/Q9Z238 ^@ 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 ^@ Cyclin N-terminal|||Disordered|||G1/S-specific cyclin-E2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080462 http://togogenome.org/gene/10090:Gm6121 ^@ http://purl.uniprot.org/uniprot/L7MUF1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Wrap53 ^@ http://purl.uniprot.org/uniprot/Q8VC51 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Region|||Repeat ^@ Disordered|||Phosphoserine|||Phosphothreonine|||Telomerase Cajal body protein 1|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000242697 http://togogenome.org/gene/10090:Fbxl6 ^@ http://purl.uniprot.org/uniprot/Q9QXW0 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Repeat|||Splice Variant ^@ Disordered|||F-box|||F-box/LRR-repeat protein 6|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000119848|||http://purl.uniprot.org/annotation/VSP_008499|||http://purl.uniprot.org/annotation/VSP_008500 http://togogenome.org/gene/10090:Cemip ^@ http://purl.uniprot.org/uniprot/Q5M9P4|||http://purl.uniprot.org/uniprot/Q8BI06 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Cell migration-inducing and hyaluronan-binding protein|||G8|||GG-type lectin 1|||GG-type lectin 2|||ILEI/PANDER|||In isoform 2.|||In isoform 3.|||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_0000021539|||http://purl.uniprot.org/annotation/VSP_009816|||http://purl.uniprot.org/annotation/VSP_009817 http://togogenome.org/gene/10090:Zfp398 ^@ http://purl.uniprot.org/uniprot/E9Q569|||http://purl.uniprot.org/uniprot/Q8BV16|||http://purl.uniprot.org/uniprot/Q8BVH0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||KRAB-related ^@ http://togogenome.org/gene/10090:Cpsf1 ^@ http://purl.uniprot.org/uniprot/A0A2R8VK76|||http://purl.uniprot.org/uniprot/Q9EPU4 ^@ 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|||Cleavage and polyadenylation specificity factor subunit 1|||Cleavage/polyadenylation specificity factor A subunit C-terminal|||Cleavage/polyadenylation specificity factor A subunit N-terminal|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000074388 http://togogenome.org/gene/10090:Nipsnap3b ^@ http://purl.uniprot.org/uniprot/B1AWZ5|||http://purl.uniprot.org/uniprot/Q9CQE1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ N6-succinyllysine|||NIPSNAP|||Protein NipSnap homolog 3B ^@ http://purl.uniprot.org/annotation/PRO_0000221155 http://togogenome.org/gene/10090:Dpy19l3 ^@ http://purl.uniprot.org/uniprot/Q71B07 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Probable C-mannosyltransferase DPY19L3 ^@ http://purl.uniprot.org/annotation/PRO_0000311902 http://togogenome.org/gene/10090:Hscb ^@ http://purl.uniprot.org/uniprot/A0A0R4J0T0|||http://purl.uniprot.org/uniprot/Q8K3A0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ Co-chaperone HscB C-terminal oligomerisation|||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_0000007263|||http://purl.uniprot.org/annotation/PRO_0000446243|||http://purl.uniprot.org/annotation/PRO_5006451988 http://togogenome.org/gene/10090:Tcfl5 ^@ http://purl.uniprot.org/uniprot/Q32NY8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rangap1 ^@ http://purl.uniprot.org/uniprot/P46061 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site ^@ Abolishes accumulation in the nucleus.|||Absence of sumoylation. Not targeted to the nuclear envelope rim nor to nuclear pore complexes. Disrupted sumoylation. No interaction with SUMO1; when associated with A-564 and with or without SUMO1 A-97.|||Acidic residues|||Disordered|||Disrupted binding to UBE2I, and no sumoylation.|||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 phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-444.|||Hydrophobic interaction with UBE2I|||Important for accumulation in the nucleus|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Little change in phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-411.|||N-acetylalanine|||N6-acetyllysine; alternate|||No UBE2I binding nor sumoylation.|||No UBE2I binding nor sumoylation. Not targeted to nuclear pore complexes; when associated with R-526.|||No effect on UBE2I binding nor on sumoylation.|||No effect on accumulation in the nucleus.|||No sumoylation.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK2|||Ran GTPase-activating protein 1|||Removed|||SUMO conjugation ^@ http://purl.uniprot.org/annotation/PRO_0000056738 http://togogenome.org/gene/10090:Ocstamp ^@ http://purl.uniprot.org/uniprot/Q9D611 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Osteoclast stimulatory transmembrane protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000342122 http://togogenome.org/gene/10090:A630095N17Rik ^@ http://purl.uniprot.org/uniprot/J3KMM7|||http://purl.uniprot.org/uniprot/J3QMK5 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Pcdhga1 ^@ http://purl.uniprot.org/uniprot/Q91XZ0 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (Man...) serine ^@ http://purl.uniprot.org/annotation/PRO_5015099502 http://togogenome.org/gene/10090:Abhd2 ^@ http://purl.uniprot.org/uniprot/Q9QXM0 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||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_0000280782 http://togogenome.org/gene/10090:Trim41 ^@ http://purl.uniprot.org/uniprot/Q5NCC3 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ 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)|||Phosphoserine|||Phosphothreonine|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000386643 http://togogenome.org/gene/10090:Erh ^@ http://purl.uniprot.org/uniprot/P84089 ^@ 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_0000219352 http://togogenome.org/gene/10090:Myo5b ^@ http://purl.uniprot.org/uniprot/G5E8G6 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Actin-binding|||Dilute|||Disordered|||Myosin N-terminal SH3-like|||Myosin motor|||Polar residues ^@ http://togogenome.org/gene/10090:Fsbp ^@ http://purl.uniprot.org/uniprot/Q8BKE5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Region|||Splice Variant ^@ Disordered|||Fibrinogen silencer-binding protein|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087353|||http://purl.uniprot.org/annotation/VSP_010775 http://togogenome.org/gene/10090:Pgam1 ^@ http://purl.uniprot.org/uniprot/Q3U7Z6|||http://purl.uniprot.org/uniprot/Q9DBJ1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site ^@ N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoglycerate mutase 1|||Phosphoserine|||Phosphotyrosine|||Proton donor/acceptor|||Tele-phosphohistidine intermediate|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000179826 http://togogenome.org/gene/10090:Cep55 ^@ http://purl.uniprot.org/uniprot/Q8BT07 ^@ 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 ^@ Centrosomal protein of 55 kDa|||Disordered|||In isoform 2.|||Interaction with PDCD6IP|||Interaction with TSG101|||Phosphoserine|||Phosphoserine; by PLK1|||Polar residues|||Required for localization to the interphase centrosome and to the midbody during cytokinesis ^@ http://purl.uniprot.org/annotation/PRO_0000238665|||http://purl.uniprot.org/annotation/VSP_018630 http://togogenome.org/gene/10090:Sdr9c7 ^@ http://purl.uniprot.org/uniprot/Q8K3P0 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ Phosphoserine|||Proton acceptor|||Short-chain dehydrogenase/reductase family 9C member 7 ^@ http://purl.uniprot.org/annotation/PRO_0000316886 http://togogenome.org/gene/10090:Pgbd1 ^@ http://purl.uniprot.org/uniprot/E9Q2C6|||http://purl.uniprot.org/uniprot/E9Q492|||http://purl.uniprot.org/uniprot/Q3V0V1|||http://purl.uniprot.org/uniprot/Q5FWH8 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||PiggyBac transposable element-derived protein ^@ http://togogenome.org/gene/10090:Nhlh2 ^@ http://purl.uniprot.org/uniprot/Q64221 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Helix-loop-helix protein 2|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127200 http://togogenome.org/gene/10090:Loxl4 ^@ http://purl.uniprot.org/uniprot/E9Q600|||http://purl.uniprot.org/uniprot/Q8CEU1|||http://purl.uniprot.org/uniprot/Q924C6 ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 2',4',5'-topaquinone|||Lysine tyrosylquinone (Lys-Tyr)|||Lysyl oxidase homolog|||Lysyl oxidase homolog 4|||Lysyl-oxidase like|||N-linked (GlcNAc...) asparagine|||SRCR|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000018536|||http://purl.uniprot.org/annotation/PRO_5004306303|||http://purl.uniprot.org/annotation/PRO_5005674915 http://togogenome.org/gene/10090:Ctsr ^@ http://purl.uniprot.org/uniprot/Q497X4|||http://purl.uniprot.org/uniprot/Q9JIA9 ^@ 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|||Cathepsin R|||Cathepsin propeptide inhibitor|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000026283|||http://purl.uniprot.org/annotation/PRO_0000026284|||http://purl.uniprot.org/annotation/PRO_5014205845 http://togogenome.org/gene/10090:Gcdh ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ68|||http://purl.uniprot.org/uniprot/Q60759|||http://purl.uniprot.org/uniprot/Q8BVD4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Transit Peptide ^@ Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA dehydrogenase/oxidase N-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||Glutaryl-CoA dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000000528 http://togogenome.org/gene/10090:Syngr2 ^@ http://purl.uniprot.org/uniprot/O55101 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transmembrane ^@ Helical|||MARVEL|||N-acetylmethionine|||Phosphoserine|||Synaptogyrin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000183994 http://togogenome.org/gene/10090:Or2b6 ^@ http://purl.uniprot.org/uniprot/Q60890 ^@ 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 2B6 ^@ http://purl.uniprot.org/annotation/PRO_0000150810 http://togogenome.org/gene/10090:Cyp3a25 ^@ http://purl.uniprot.org/uniprot/O09158 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Cytochrome P450 3A25|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051805 http://togogenome.org/gene/10090:Psma4 ^@ http://purl.uniprot.org/uniprot/Q9R1P0 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Disordered|||N6-acetyllysine|||Phosphoserine|||Proteasome subunit alpha type-4 ^@ http://purl.uniprot.org/annotation/PRO_0000124105 http://togogenome.org/gene/10090:Tbcc ^@ http://purl.uniprot.org/uniprot/A0A0R4J0M1|||http://purl.uniprot.org/uniprot/Q8VCN9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ C-CAP/cofactor C-like|||Disordered|||N-acetylmethionine|||Phosphoserine|||Tubulin-specific chaperone C ^@ http://purl.uniprot.org/annotation/PRO_0000285107 http://togogenome.org/gene/10090:Vasp ^@ http://purl.uniprot.org/uniprot/P70460 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant ^@ 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|||KLKR|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by PKA and PKG|||Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK1|||Phosphothreonine|||Phosphothreonine; by PKA, PKG/PRKG1 and AMPK|||Phosphotyrosine|||Polar residues|||Pro residues|||Reduced binding to monomeric actin. No VASP-induced actin polymerization.|||Reduces actin polymerization to a lesser extent than wild-type.|||Reduces actin polymerization to a lesser extent than wild-type. Greater effect on actin polymerization; when associated with D-235 and E-274.|||Removed|||Vasodilator-stimulated phosphoprotein|||WH1 ^@ http://purl.uniprot.org/annotation/PRO_0000065768 http://togogenome.org/gene/10090:Mrpl15 ^@ http://purl.uniprot.org/uniprot/A0A0A6YVP4|||http://purl.uniprot.org/uniprot/Q9CPR5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Basic residues|||Disordered|||In isoform 2.|||Large ribosomal subunit protein uL15/eL18|||Large ribosomal subunit protein uL15m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000257839|||http://purl.uniprot.org/annotation/VSP_021370|||http://purl.uniprot.org/annotation/VSP_021371 http://togogenome.org/gene/10090:Rock2 ^@ http://purl.uniprot.org/uniprot/F8VPK5|||http://purl.uniprot.org/uniprot/P70336|||http://purl.uniprot.org/uniprot/Q3TR46 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Zinc Finger ^@ AGC-kinase C-terminal|||Cleavage; by granzyme B|||Disordered|||In isoform 2.|||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_0000086626|||http://purl.uniprot.org/annotation/VSP_041818|||http://purl.uniprot.org/annotation/VSP_041819 http://togogenome.org/gene/10090:Pilrb1 ^@ http://purl.uniprot.org/uniprot/Q2YFS2 ^@ 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|||Paired immunoglobulin-like type 2 receptor beta ^@ http://purl.uniprot.org/annotation/PRO_0000226824 http://togogenome.org/gene/10090:Zbtb1 ^@ http://purl.uniprot.org/uniprot/Q5YB37|||http://purl.uniprot.org/uniprot/Q91VL9 ^@ 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|||Basic and acidic residues|||C2H2-type|||C2H2-type 1; atypical|||C2H2-type 2; atypical|||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|||Polar residues|||UBZ-type|||Zinc finger and BTB domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000047708 http://togogenome.org/gene/10090:Ces2b ^@ http://purl.uniprot.org/uniprot/Q6PDB7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Carboxylesterase type B|||Carboxylic ester hydrolase ^@ http://purl.uniprot.org/annotation/PRO_5015020078 http://togogenome.org/gene/10090:Ing5 ^@ http://purl.uniprot.org/uniprot/Q9D8Y8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Histone H3K4me3 binding|||In isoform 2.|||In isoform 3.|||Inhibitor of growth protein 5|||Omega-N-methylarginine|||PHD-type|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000212672|||http://purl.uniprot.org/annotation/VSP_012529|||http://purl.uniprot.org/annotation/VSP_012530 http://togogenome.org/gene/10090:Mrto4 ^@ http://purl.uniprot.org/uniprot/A2AMU9|||http://purl.uniprot.org/uniprot/A2AMV1|||http://purl.uniprot.org/uniprot/Q9D0I8 ^@ 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 ^@ Acidic residues|||Disordered|||Large ribosomal subunit protein uL10-like insertion|||Phosphoserine|||mRNA turnover protein 4 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000154817 http://togogenome.org/gene/10090:Gpr179 ^@ http://purl.uniprot.org/uniprot/E9PY61 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Cache-like region|||Disordered|||G-protein coupled receptor 179|||Helical; 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_5003245698 http://togogenome.org/gene/10090:Zfp280d ^@ http://purl.uniprot.org/uniprot/Q68FE8|||http://purl.uniprot.org/uniprot/V9GWW1|||http://purl.uniprot.org/uniprot/V9GXP2 ^@ 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 ^@ Basic and acidic residues|||C2H2-type|||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.|||Phosphoserine|||Polar residues|||Zinc finger protein 280D ^@ http://purl.uniprot.org/annotation/PRO_0000227978|||http://purl.uniprot.org/annotation/VSP_017629|||http://purl.uniprot.org/annotation/VSP_017630|||http://purl.uniprot.org/annotation/VSP_017631|||http://purl.uniprot.org/annotation/VSP_017632|||http://purl.uniprot.org/annotation/VSP_017633 http://togogenome.org/gene/10090:Ifi27l2a ^@ http://purl.uniprot.org/uniprot/Q8R412 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||Interferon alpha-inducible protein 27-like protein 2A ^@ http://purl.uniprot.org/annotation/PRO_0000416107 http://togogenome.org/gene/10090:Eif1ad8 ^@ http://purl.uniprot.org/uniprot/Q3UTA4 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||S1-like ^@ http://togogenome.org/gene/10090:Birc6 ^@ http://purl.uniprot.org/uniprot/O88738|||http://purl.uniprot.org/uniprot/Q3UYZ6 ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ BIR|||Baculoviral IAP repeat-containing protein 6|||Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||UBC core ^@ http://purl.uniprot.org/annotation/PRO_0000416247|||http://purl.uniprot.org/annotation/VSP_042536|||http://purl.uniprot.org/annotation/VSP_042537 http://togogenome.org/gene/10090:Lpp ^@ http://purl.uniprot.org/uniprot/Q8BFW7 ^@ 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 SUMO1)|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Lipoma-preferred partner homolog|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000075833|||http://purl.uniprot.org/annotation/VSP_016350|||http://purl.uniprot.org/annotation/VSP_016351|||http://purl.uniprot.org/annotation/VSP_016352|||http://purl.uniprot.org/annotation/VSP_016353|||http://purl.uniprot.org/annotation/VSP_016354|||http://purl.uniprot.org/annotation/VSP_016355|||http://purl.uniprot.org/annotation/VSP_016356 http://togogenome.org/gene/10090:Pld4 ^@ http://purl.uniprot.org/uniprot/Q8BG07 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 5'-3' exonuclease PLD4|||Cytoplasmic|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2|||Signal-anchor for type II membrane protein ^@ http://purl.uniprot.org/annotation/PRO_0000280334|||http://purl.uniprot.org/annotation/VSP_023630 http://togogenome.org/gene/10090:Kcnn3 ^@ http://purl.uniprot.org/uniprot/P58391 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||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|||Phosphoserine|||Polar residues|||Pore-forming; Name=Segment H5|||Pro residues|||Small conductance calcium-activated potassium channel protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000155014 http://togogenome.org/gene/10090:Nudt12 ^@ http://purl.uniprot.org/uniprot/Q9DCN1 ^@ Binding Site|||Chain|||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 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ ANK 1|||ANK 2|||ANK 3|||Abolished deNADding activity.|||In isoform 2.|||Microbody targeting signal|||N6-succinyllysine|||NAD-capped RNA hydrolase NUDT12|||Nudix box|||Nudix hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000056957|||http://purl.uniprot.org/annotation/VSP_014280|||http://purl.uniprot.org/annotation/VSP_014281 http://togogenome.org/gene/10090:Inpp5a ^@ http://purl.uniprot.org/uniprot/Q7TNC9 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Splice Variant ^@ Chain|||Lipid Binding|||Propeptide|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Inositol polyphosphate-5-phosphatase A|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000451144|||http://purl.uniprot.org/annotation/PRO_0000451145|||http://purl.uniprot.org/annotation/VSP_060756 http://togogenome.org/gene/10090:Speg ^@ http://purl.uniprot.org/uniprot/A0A0R4J1J0|||http://purl.uniprot.org/uniprot/E9QQ25|||http://purl.uniprot.org/uniprot/Q62407 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Ig-like|||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 isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Striated muscle-specific serine/threonine-protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000072667|||http://purl.uniprot.org/annotation/VSP_018264|||http://purl.uniprot.org/annotation/VSP_018265|||http://purl.uniprot.org/annotation/VSP_018266|||http://purl.uniprot.org/annotation/VSP_018267|||http://purl.uniprot.org/annotation/VSP_018268 http://togogenome.org/gene/10090:Ackr4 ^@ http://purl.uniprot.org/uniprot/B2RU75|||http://purl.uniprot.org/uniprot/Q924I3 ^@ 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 ^@ Atypical chemokine 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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069297 http://togogenome.org/gene/10090:Tlr6 ^@ http://purl.uniprot.org/uniprot/Q3UV88|||http://purl.uniprot.org/uniprot/Q9EPW9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Dominant negative mutant, blocks response to Gram-positive pathogens.|||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|||N-linked (GlcNAc...) asparagine|||TIR|||Toll-like receptor 6 ^@ http://purl.uniprot.org/annotation/PRO_0000034732 http://togogenome.org/gene/10090:Wdfy2 ^@ http://purl.uniprot.org/uniprot/Q8BUB4 ^@ 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_0000051337 http://togogenome.org/gene/10090:Pnma1 ^@ http://purl.uniprot.org/uniprot/Q8C1C8 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Paraneoplastic antigen Ma1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000155200 http://togogenome.org/gene/10090:Adamts8 ^@ http://purl.uniprot.org/uniprot/F8VQ15 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Peptidase M12B ^@ http://purl.uniprot.org/annotation/PRO_5003379445 http://togogenome.org/gene/10090:Gjd2 ^@ http://purl.uniprot.org/uniprot/O54851 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Gap junction delta-2 protein|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000057836 http://togogenome.org/gene/10090:Rasl10b ^@ http://purl.uniprot.org/uniprot/Q5SSG5 ^@ 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|||Ras-like protein family member 10B|||Removed in mature form|||S-geranylgeranyl cysteine|||Small GTPase-like ^@ http://purl.uniprot.org/annotation/PRO_0000280801|||http://purl.uniprot.org/annotation/PRO_0000281363 http://togogenome.org/gene/10090:Nadk ^@ http://purl.uniprot.org/uniprot/P58058 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ NAD kinase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000120714 http://togogenome.org/gene/10090:Acp7 ^@ http://purl.uniprot.org/uniprot/B2RRA7|||http://purl.uniprot.org/uniprot/Q8BX37 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Acid phosphatase type 7|||Calcineurin-like phosphoesterase|||Iron/zinc purple acid phosphatase-like C-terminal|||N-linked (GlcNAc...) asparagine|||Purple acid phosphatase N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000316825 http://togogenome.org/gene/10090:Gpr62 ^@ http://purl.uniprot.org/uniprot/Q80UC6 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 62|||Helical; 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 constitutive activity; No effect on protein level; Does not affect homooligomerization.|||Strong decreases on constitutive activity; No effect on protein level; Does not affect homooligomerization. ^@ http://purl.uniprot.org/annotation/PRO_0000305584 http://togogenome.org/gene/10090:Ric8a ^@ http://purl.uniprot.org/uniprot/Q3TIR3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Phosphothreonine|||Synembryn-A ^@ http://purl.uniprot.org/annotation/PRO_0000235892 http://togogenome.org/gene/10090:Spcs3 ^@ http://purl.uniprot.org/uniprot/Q6ZWQ7 ^@ 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_0000438396 http://togogenome.org/gene/10090:Gm12886 ^@ http://purl.uniprot.org/uniprot/B1AZM5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5002761498 http://togogenome.org/gene/10090:Rfxank ^@ http://purl.uniprot.org/uniprot/Q53X17|||http://purl.uniprot.org/uniprot/Q543F0|||http://purl.uniprot.org/uniprot/Q9Z205 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Region|||Repeat|||Splice Variant ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||DNA-binding protein RFXANK|||Disordered|||In isoform Short. ^@ http://purl.uniprot.org/annotation/PRO_0000067050|||http://purl.uniprot.org/annotation/VSP_000285 http://togogenome.org/gene/10090:Grin3b ^@ http://purl.uniprot.org/uniprot/Q91ZU9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Glutamate receptor ionotropic, NMDA 3B|||Helical|||Involved in the trafficking and surface expression of NMDARs|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000011571 http://togogenome.org/gene/10090:Scrib ^@ http://purl.uniprot.org/uniprot/Q80U72 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 4.|||Interaction with ARHGEF7|||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|||Omega-N-methylarginine|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein scribble homolog|||Sufficient for targeting to adherens junction and to inhibit cell proliferation ^@ http://purl.uniprot.org/annotation/PRO_0000188304|||http://purl.uniprot.org/annotation/VSP_010909|||http://purl.uniprot.org/annotation/VSP_010910|||http://purl.uniprot.org/annotation/VSP_010911 http://togogenome.org/gene/10090:Rps3a1 ^@ http://purl.uniprot.org/uniprot/P97351|||http://purl.uniprot.org/uniprot/Q564F3 ^@ Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region ^@ ADP-ribosyltyrosine|||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_0000153525 http://togogenome.org/gene/10090:Zfp985 ^@ http://purl.uniprot.org/uniprot/A2A7A5|||http://purl.uniprot.org/uniprot/Q5U4F7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Or4k42 ^@ http://purl.uniprot.org/uniprot/Q7TQX8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Col27a1 ^@ http://purl.uniprot.org/uniprot/Q5QNQ9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ 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 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|||Interchain (with C-1268)|||Interchain (with C-1285)|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide|||Polar residues|||Pro residues|||Triple-helical ^@ http://purl.uniprot.org/annotation/PRO_0000314669|||http://purl.uniprot.org/annotation/PRO_0000314670|||http://purl.uniprot.org/annotation/PRO_0000314671 http://togogenome.org/gene/10090:Gpat3 ^@ http://purl.uniprot.org/uniprot/Q8C0N2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Motif|||Transmembrane ^@ Glycerol-3-phosphate acyltransferase 3|||HXXXXD motif|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000291571 http://togogenome.org/gene/10090:Sox15 ^@ http://purl.uniprot.org/uniprot/P43267|||http://purl.uniprot.org/uniprot/Q5F2B2 ^@ 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|||HMG box|||In strain: various strains.|||Interaction with FHL3|||Phosphoserine|||Polar residues|||Protein SOX-15|||Required to promote HAND1 transcriptional activator activity ^@ http://purl.uniprot.org/annotation/PRO_0000048763 http://togogenome.org/gene/10090:Clcnka ^@ http://purl.uniprot.org/uniprot/Q9WUB7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CBS 1|||CBS 2|||Chloride channel protein ClC-Ka|||Cytoplasmic|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000094456 http://togogenome.org/gene/10090:Vsig4 ^@ http://purl.uniprot.org/uniprot/F6TUL9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5006466957 http://togogenome.org/gene/10090:Ercc3 ^@ http://purl.uniprot.org/uniprot/P49135 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||DEVH box|||Disordered|||General transcription and DNA repair factor IIH helicase subunit XPB|||Helicase ATP-binding|||Helicase C-terminal|||Nuclear localization signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000101989 http://togogenome.org/gene/10090:Dennd2b ^@ http://purl.uniprot.org/uniprot/Q924W7 ^@ 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|||DENN domain-containing protein 2B|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000247449|||http://purl.uniprot.org/annotation/VSP_019989|||http://purl.uniprot.org/annotation/VSP_019990 http://togogenome.org/gene/10090:Or5ac23 ^@ http://purl.uniprot.org/uniprot/Q7TS37 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kctd18 ^@ http://purl.uniprot.org/uniprot/E0CZ26|||http://purl.uniprot.org/uniprot/E9Q945|||http://purl.uniprot.org/uniprot/Q6DI85 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB/POZ|||Disordered|||Polar residues|||Potassium channel tetramerisation-type BTB ^@ http://togogenome.org/gene/10090:Gdf10 ^@ http://purl.uniprot.org/uniprot/P97737|||http://purl.uniprot.org/uniprot/Q8C991 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Growth/differentiation factor 10|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033846|||http://purl.uniprot.org/annotation/PRO_0000033847 http://togogenome.org/gene/10090:Lonrf3 ^@ http://purl.uniprot.org/uniprot/Q9D4H7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||LON peptidase N-terminal domain and RING finger protein 3|||Lon N-terminal|||Polar residues|||RING-type 1|||RING-type 2|||TPR 1|||TPR 2|||TPR 3|||TPR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000277673 http://togogenome.org/gene/10090:Ankrd11 ^@ http://purl.uniprot.org/uniprot/E9Q4F7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ 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 Yoda; protein degradation is impaired. Homozygotes are embryonic lethal. Heterozygotes have reduced body size, craniofacial abnormalities, and reduced bone mineral density.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000436376 http://togogenome.org/gene/10090:Pln ^@ http://purl.uniprot.org/uniprot/P61014 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes palmitoylation.|||Cardiac phospholamban|||Cleaved by SPPL2c.|||Cytoplasmic|||Does not affect palmitoylation.|||Helical|||N-acetylmethionine|||Nearly abolishes inhibition of ATP2A1-mediated calcium uptake.|||No effect on inhibition of ATP2A1-mediated calcium uptake.|||Not cleaved by SPPL2c.|||Phosphoserine; by PKA|||Phosphothreonine; by CaMK2|||Reduces inhibition of ATP2A1-mediated calcium uptake.|||S-palmitoyl cysteine|||Strongly reduces inhibition of ATP2A1-mediated calcium uptake. ^@ http://purl.uniprot.org/annotation/PRO_0000191245 http://togogenome.org/gene/10090:Serpinb1b ^@ http://purl.uniprot.org/uniprot/Q8VHP7 ^@ Chain|||Molecule Processing|||Region|||Site ^@ Chain|||Region|||Site ^@ CARD-binding motif (CBM)|||Leukocyte elastase inhibitor B|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000289121 http://togogenome.org/gene/10090:Map3k15 ^@ http://purl.uniprot.org/uniprot/A2AQW0 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Mitogen-activated protein kinase kinase kinase 15|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000307633 http://togogenome.org/gene/10090:Or52e19b ^@ http://purl.uniprot.org/uniprot/L7N1Y4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Egfr ^@ http://purl.uniprot.org/uniprot/Q01279|||http://purl.uniprot.org/uniprot/Q3TQS6|||http://purl.uniprot.org/uniprot/Q9EP98|||http://purl.uniprot.org/uniprot/Q9WVF5 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Approximate|||Cytoplasmic|||Disordered|||Epidermal growth factor receptor|||Extracellular|||Furin-like cysteine-rich|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Growth factor receptor|||Helical|||Important for dimerization, phosphorylation and activation|||Important for interaction with PIK3C2B|||N-linked (GlcNAc...) asparagine|||N6-(2-hydroxyisobutyryl)lysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKC and PKD/PRKD1|||Phosphothreonine; by PKD/PRKD1|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Receptor L-domain|||Receptor protein-tyrosine kinase|||S-palmitoyl cysteine|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000016666|||http://purl.uniprot.org/annotation/PRO_5010147969|||http://purl.uniprot.org/annotation/PRO_5015100977 http://togogenome.org/gene/10090:Apoo ^@ http://purl.uniprot.org/uniprot/Q9DCZ4 ^@ 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.|||MICOS complex subunit Mic26|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000254647|||http://purl.uniprot.org/annotation/VSP_057812|||http://purl.uniprot.org/annotation/VSP_057813 http://togogenome.org/gene/10090:Bpifa3 ^@ http://purl.uniprot.org/uniprot/Q80X83|||http://purl.uniprot.org/uniprot/Q9D9J8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ BPI fold-containing family A member 3|||Lipid-binding serum glycoprotein N-terminal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017188|||http://purl.uniprot.org/annotation/PRO_5015098925 http://togogenome.org/gene/10090:Mafg ^@ http://purl.uniprot.org/uniprot/O54790 ^@ 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 ^@ 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_0000076501 http://togogenome.org/gene/10090:Pdcl3 ^@ http://purl.uniprot.org/uniprot/Q8BVF2 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ N-acetylmethionine|||Phosducin-like protein 3|||Phosphoserine|||Thioredoxin fold ^@ http://purl.uniprot.org/annotation/PRO_0000163759 http://togogenome.org/gene/10090:Tas2r144 ^@ http://purl.uniprot.org/uniprot/Q7TQB8 ^@ 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 40 ^@ http://purl.uniprot.org/annotation/PRO_0000082314 http://togogenome.org/gene/10090:Rab18 ^@ http://purl.uniprot.org/uniprot/P35293 ^@ 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|||N-acetylmethionine|||Phosphoserine|||Ras-related protein Rab-18|||Removed in mature form|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121194|||http://purl.uniprot.org/annotation/PRO_0000370762 http://togogenome.org/gene/10090:Tubgcp3 ^@ http://purl.uniprot.org/uniprot/P58854 ^@ 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 ^@ Disordered|||Gamma-tubulin complex component 3|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000078119 http://togogenome.org/gene/10090:Hap1 ^@ http://purl.uniprot.org/uniprot/O35668 ^@ 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|||Basic and acidic residues|||Disordered|||HAP1 N-terminal|||Huntingtin-associated protein 1|||In isoform A.|||Interaction with TBP|||Phosphothreonine|||Polar residues|||Sufficient for interaction with KIF5B|||Sufficient for self-association and interaction with HD ^@ http://purl.uniprot.org/annotation/PRO_0000083895|||http://purl.uniprot.org/annotation/VSP_004279 http://togogenome.org/gene/10090:Sh3tc1 ^@ http://purl.uniprot.org/uniprot/G3X9F6|||http://purl.uniprot.org/uniprot/Q3TXV8|||http://purl.uniprot.org/uniprot/Q3UDI4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||SH3 ^@ http://togogenome.org/gene/10090:Kcng3 ^@ http://purl.uniprot.org/uniprot/P59053 ^@ 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_0000054078|||http://purl.uniprot.org/annotation/VSP_001027 http://togogenome.org/gene/10090:Donson ^@ http://purl.uniprot.org/uniprot/Q9QXP4 ^@ 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 downstream neighbor of Son ^@ http://purl.uniprot.org/annotation/PRO_0000079980 http://togogenome.org/gene/10090:Scaf1 ^@ http://purl.uniprot.org/uniprot/Q5U4C3 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||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_0000299407|||http://purl.uniprot.org/annotation/VSP_027636|||http://purl.uniprot.org/annotation/VSP_027637 http://togogenome.org/gene/10090:Or11g2 ^@ http://purl.uniprot.org/uniprot/Q7TRM0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ywhag ^@ http://purl.uniprot.org/uniprot/A8IP69|||http://purl.uniprot.org/uniprot/P61982 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site ^@ 14-3-3|||14-3-3 protein gamma|||14-3-3 protein gamma, N-terminally processed|||Interaction with phosphoserine on interacting protein|||N-acetylmethionine|||N-acetylvaline; in 14-3-3 protein gamma, N-terminally processed|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000058607|||http://purl.uniprot.org/annotation/PRO_0000367908 http://togogenome.org/gene/10090:Cplx3 ^@ http://purl.uniprot.org/uniprot/Q8R1B5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Propeptide|||Region ^@ Basic and acidic residues|||Complexin-3|||Cysteine methyl ester|||Disordered|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000239273|||http://purl.uniprot.org/annotation/PRO_0000240234 http://togogenome.org/gene/10090:Cwf19l1 ^@ http://purl.uniprot.org/uniprot/Q8CI33 ^@ 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|||CWF19-like protein 1|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000315642|||http://purl.uniprot.org/annotation/VSP_030589 http://togogenome.org/gene/10090:Arrdc2 ^@ http://purl.uniprot.org/uniprot/Q9D668 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Arrestin domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000244348 http://togogenome.org/gene/10090:Hs6st3 ^@ http://purl.uniprot.org/uniprot/Q149R8|||http://purl.uniprot.org/uniprot/Q3UTM4|||http://purl.uniprot.org/uniprot/Q9QYK4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Acidic residues|||Cytoplasmic|||Disordered|||Helical|||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_0000190810 http://togogenome.org/gene/10090:Or6z6 ^@ http://purl.uniprot.org/uniprot/Q8VF33 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gimap1 ^@ http://purl.uniprot.org/uniprot/Q3TFI6 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ AIG1-type G|||Basic and acidic residues|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Tbl1x ^@ http://purl.uniprot.org/uniprot/Q9QXE7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Affects recruitment to heterochromatin by MECP2.|||Affects recruitment to heterochromatin by MECP2. Does not interact with MECP2. Is efficiently incorporated in N-Cor repressor complex.|||Disordered|||Does not affect recruitment to heterochromatin by MECP2.|||Does not interact with MECP2. Affects recruitment to heterochromatin by MECP2. Is efficiently incorporated in N-Cor repressor complex.|||F-box-like|||F-box-like/WD repeat-containing protein TBL1X|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||LisH|||N-acetylserine|||N6-acetyllysine|||Polar residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8 ^@ http://purl.uniprot.org/annotation/PRO_0000051265 http://togogenome.org/gene/10090:Caprin2 ^@ http://purl.uniprot.org/uniprot/E4NKG5|||http://purl.uniprot.org/uniprot/Q05A80 ^@ 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 ^@ C1q|||Caprin-2|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000302083|||http://purl.uniprot.org/annotation/VSP_052540 http://togogenome.org/gene/10090:Lyrm1 ^@ http://purl.uniprot.org/uniprot/Q9CQB7 ^@ Chain|||Molecule Processing ^@ Chain ^@ LYR motif-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000174311 http://togogenome.org/gene/10090:Mapre2 ^@ http://purl.uniprot.org/uniprot/E9Q6X0|||http://purl.uniprot.org/uniprot/Q8R001 ^@ 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 ^@ APC-binding|||Basic and acidic residues|||Calponin-homology (CH)|||DCTN1-binding|||Disordered|||EB1 C-terminal|||In isoform 2.|||Microtubule-associated protein RP/EB family member 2|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000213425|||http://purl.uniprot.org/annotation/VSP_012946 http://togogenome.org/gene/10090:Bco2 ^@ http://purl.uniprot.org/uniprot/Q3KNZ2|||http://purl.uniprot.org/uniprot/Q99NF1 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Carotenoid-cleaving dioxygenase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000143939 http://togogenome.org/gene/10090:Themis ^@ http://purl.uniprot.org/uniprot/Q8BGW0 ^@ 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 ^@ Basic and acidic residues|||CABIT 1|||CABIT 2|||Decreased levels of protein expression in thymocytes. Reduced numbers of CD4 and CD8 single-positive thymocytes as well as reduced numbers of peripheral CD4 and CD8 T-cells.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Protein THEMIS ^@ http://purl.uniprot.org/annotation/PRO_0000252379|||http://purl.uniprot.org/annotation/VSP_020919|||http://purl.uniprot.org/annotation/VSP_020920|||http://purl.uniprot.org/annotation/VSP_020921|||http://purl.uniprot.org/annotation/VSP_020922|||http://purl.uniprot.org/annotation/VSP_020923|||http://purl.uniprot.org/annotation/VSP_020924 http://togogenome.org/gene/10090:Reps1 ^@ http://purl.uniprot.org/uniprot/E9Q632|||http://purl.uniprot.org/uniprot/O54916 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||EF-hand|||EH|||EH 1|||EH 2|||In isoform 2.|||In isoform 3 and isoform 4.|||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_0000073830|||http://purl.uniprot.org/annotation/VSP_007956|||http://purl.uniprot.org/annotation/VSP_007957|||http://purl.uniprot.org/annotation/VSP_038336|||http://purl.uniprot.org/annotation/VSP_038337|||http://purl.uniprot.org/annotation/VSP_038338 http://togogenome.org/gene/10090:Mup18 ^@ http://purl.uniprot.org/uniprot/A2BIM8|||http://purl.uniprot.org/uniprot/P04938 ^@ 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 ^@ Major urinary protein 11|||Major urinary protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000201023|||http://purl.uniprot.org/annotation/PRO_5005334073 http://togogenome.org/gene/10090:2310002L09Rik ^@ http://purl.uniprot.org/uniprot/Q14C20|||http://purl.uniprot.org/uniprot/Q9D7L5|||http://purl.uniprot.org/uniprot/Q9D7M6 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Wnt9a ^@ http://purl.uniprot.org/uniprot/Q8R5M2 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-9a ^@ http://purl.uniprot.org/annotation/PRO_0000041456 http://togogenome.org/gene/10090:Nfe2l3 ^@ http://purl.uniprot.org/uniprot/Q3UZC1|||http://purl.uniprot.org/uniprot/Q9WTM4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ BZIP|||Basic and acidic residues|||Basic motif|||Disordered|||Leucine-zipper|||Nuclear factor erythroid 2-related factor 3|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076453 http://togogenome.org/gene/10090:Micu3 ^@ http://purl.uniprot.org/uniprot/Q9CTY5 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Transmembrane ^@ Calcium uptake protein 3, mitochondrial|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000251231 http://togogenome.org/gene/10090:Tulp2 ^@ http://purl.uniprot.org/uniprot/A0A1B0GRN6|||http://purl.uniprot.org/uniprot/D3Z0R4|||http://purl.uniprot.org/uniprot/P46686 ^@ 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, isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Tubby C-terminal|||Tubby-related protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000186469|||http://purl.uniprot.org/annotation/VSP_022197|||http://purl.uniprot.org/annotation/VSP_022198|||http://purl.uniprot.org/annotation/VSP_022199|||http://purl.uniprot.org/annotation/VSP_022200 http://togogenome.org/gene/10090:Adcy1 ^@ http://purl.uniprot.org/uniprot/O88444 ^@ 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 ^@ Adenylate cyclase type 1|||Cytoplasmic|||Disordered|||Helical|||Interaction with calmodulin|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000195683 http://togogenome.org/gene/10090:Insr ^@ http://purl.uniprot.org/uniprot/M4TKR7|||http://purl.uniprot.org/uniprot/P15208|||http://purl.uniprot.org/uniprot/Q3TPM5 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||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|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes interaction with IRS1 but not with IRS2.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||Important for interaction with IRS1, SHC1 and STAT5B|||Insulin receptor subunit alpha|||Insulin receptor subunit beta|||Insulin-binding|||Interchain|||N-linked (GlcNAc...) asparagine|||PIK3R1 binding|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton donor/acceptor|||Tyrosine-protein kinase receptor ^@ http://purl.uniprot.org/annotation/PRO_0000016693|||http://purl.uniprot.org/annotation/PRO_0000016695|||http://purl.uniprot.org/annotation/PRO_5004058829 http://togogenome.org/gene/10090:Fam229b ^@ http://purl.uniprot.org/uniprot/B2RVF6|||http://purl.uniprot.org/uniprot/Q8CF36 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Protein FAM229B ^@ http://purl.uniprot.org/annotation/PRO_0000335818 http://togogenome.org/gene/10090:Serpine3 ^@ http://purl.uniprot.org/uniprot/E9Q6A2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Polar residues|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_5003243109 http://togogenome.org/gene/10090:Or5w12 ^@ http://purl.uniprot.org/uniprot/Q7TR42 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp82 ^@ http://purl.uniprot.org/uniprot/Q6P9Y7|||http://purl.uniprot.org/uniprot/S4R1G9 ^@ 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 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)|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 82 ^@ http://purl.uniprot.org/annotation/PRO_0000233165|||http://purl.uniprot.org/annotation/VSP_018083|||http://purl.uniprot.org/annotation/VSP_046230|||http://purl.uniprot.org/annotation/VSP_046231 http://togogenome.org/gene/10090:Osmr ^@ http://purl.uniprot.org/uniprot/A0A0R4J268|||http://purl.uniprot.org/uniprot/G3X8V6|||http://purl.uniprot.org/uniprot/O70458|||http://purl.uniprot.org/uniprot/Q3TRK8 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Oncostatin-M-specific receptor subunit beta|||Polar residues|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000259760|||http://purl.uniprot.org/annotation/PRO_5006452027|||http://purl.uniprot.org/annotation/PRO_5015091873|||http://purl.uniprot.org/annotation/VSP_021530 http://togogenome.org/gene/10090:Prss56 ^@ http://purl.uniprot.org/uniprot/F2YMG0 ^@ 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|||Region|||Signal Peptide ^@ Charge relay system|||Disordered|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 56 ^@ http://purl.uniprot.org/annotation/PRO_0000422245 http://togogenome.org/gene/10090:Foxe1 ^@ http://purl.uniprot.org/uniprot/Q8R2I0 ^@ Chain|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Region ^@ Disordered|||Fork-head|||Forkhead box protein E1 ^@ http://purl.uniprot.org/annotation/PRO_0000091827 http://togogenome.org/gene/10090:Dynlt3 ^@ http://purl.uniprot.org/uniprot/P56387 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ 3'-nitrotyrosine|||Dynein light chain Tctex-type 3 ^@ http://purl.uniprot.org/annotation/PRO_0000195159 http://togogenome.org/gene/10090:Lars ^@ http://purl.uniprot.org/uniprot/Q7TSZ3|||http://purl.uniprot.org/uniprot/Q8BMJ2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict ^@ 'HIGH' region|||'KMSKS' region|||Aminoacyl-tRNA synthetase class Ia|||Leucine--tRNA ligase, cytoplasmic|||Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000152151 http://togogenome.org/gene/10090:Pdhx ^@ http://purl.uniprot.org/uniprot/Q8BKZ9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Transit Peptide ^@ Disordered|||Lipoyl-binding|||Mitochondrion|||N6-acetyllysine|||N6-lipoyllysine|||N6-succinyllysine|||Peripheral subunit-binding (PSBD)|||Phosphoserine|||Pro residues|||Pyruvate dehydrogenase protein X component, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000020485 http://togogenome.org/gene/10090:Ddx11 ^@ http://purl.uniprot.org/uniprot/A0A2Y9CZM3|||http://purl.uniprot.org/uniprot/Q6AXC6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ ATP-dependent DNA helicase DDX11|||Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000055137 http://togogenome.org/gene/10090:Ccn4 ^@ http://purl.uniprot.org/uniprot/O54775|||http://purl.uniprot.org/uniprot/Q3UFJ5 ^@ 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 ^@ CCN family member 4|||CTCK|||IGFBP N-terminal|||N-linked (GlcNAc...) asparagine|||TSP type-1|||VWFC|||WNT1-inducible-signaling pathway protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000014407|||http://purl.uniprot.org/annotation/PRO_5009970835 http://togogenome.org/gene/10090:Spata31d1b ^@ http://purl.uniprot.org/uniprot/E9QA57 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues|||SPATA31 ^@ http://togogenome.org/gene/10090:Akap7 ^@ http://purl.uniprot.org/uniprot/O55074|||http://purl.uniprot.org/uniprot/Q7TN79 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict ^@ A-kinase anchor protein 7 isoform alpha|||A-kinase anchor protein 7 isoform gamma|||Abolishes PKA-RI-alpha binding; when associated with P-265.|||Abolishes PKA-RI-alpha binding; when associated with P-269.|||Abolishes nuclear localization; when associated with E-41.|||Abolishes nuclear localization; when associated with E-43.|||Basic and acidic residues|||Disordered|||N-myristoyl glycine|||PKA-RII-alpha subunit binding domain|||RI-alpha-binding|||RII-binding|||Removed|||Required for membrane localization|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000064532|||http://purl.uniprot.org/annotation/PRO_0000419634 http://togogenome.org/gene/10090:Polr1d ^@ http://purl.uniprot.org/uniprot/P97304|||http://purl.uniprot.org/uniprot/Q545W2|||http://purl.uniprot.org/uniprot/Q9D1M1 ^@ 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|||DNA-directed RNA polymerase RBP11-like dimerisation|||DNA-directed RNA polymerases I and III subunit RPAC2|||Disordered|||N-acetylmethionine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000149317 http://togogenome.org/gene/10090:Krtap26-1 ^@ http://purl.uniprot.org/uniprot/Q9D7N2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Keratin-associated protein 26-1 ^@ http://purl.uniprot.org/annotation/PRO_0000358599 http://togogenome.org/gene/10090:Coprs ^@ http://purl.uniprot.org/uniprot/Q9CQ13 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Coordinator of PRMT5 and differentiation stimulator|||Disordered|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000336078 http://togogenome.org/gene/10090:Nfasc ^@ http://purl.uniprot.org/uniprot/E9PW06|||http://purl.uniprot.org/uniprot/E9Q171|||http://purl.uniprot.org/uniprot/Q6P6Q1|||http://purl.uniprot.org/uniprot/Q6ZQ54|||http://purl.uniprot.org/uniprot/Q810U3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||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|||N-linked (GlcNAc...) asparagine|||Neurofascin|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000015050|||http://purl.uniprot.org/annotation/PRO_5003242989|||http://purl.uniprot.org/annotation/PRO_5003245599 http://togogenome.org/gene/10090:Ephb6 ^@ http://purl.uniprot.org/uniprot/O08644 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Eph LBD|||Ephrin type-B receptor 6|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Protein kinase|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000016838|||http://purl.uniprot.org/annotation/VSP_003020|||http://purl.uniprot.org/annotation/VSP_003021|||http://purl.uniprot.org/annotation/VSP_003022|||http://purl.uniprot.org/annotation/VSP_003023 http://togogenome.org/gene/10090:Pkn1 ^@ http://purl.uniprot.org/uniprot/P70268 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Site|||Splice Variant ^@ AGC-kinase C-terminal|||C2|||Cleavage; by caspase-3|||Disordered|||In isoform 2.|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000055720|||http://purl.uniprot.org/annotation/VSP_039223 http://togogenome.org/gene/10090:Foxo4 ^@ http://purl.uniprot.org/uniprot/B1AUT3|||http://purl.uniprot.org/uniprot/Q4KL34|||http://purl.uniprot.org/uniprot/Q9WVH3 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Fork-head|||Forkhead box protein O4|||Phosphoserine; by PKB/AKT1|||Phosphothreonine; by PKB/AKT1|||Polar residues|||Required for interaction with FOXK1 ^@ http://purl.uniprot.org/annotation/PRO_0000091876 http://togogenome.org/gene/10090:Trafd1 ^@ http://purl.uniprot.org/uniprot/Q3UDK1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||No effect on TRAF6-induced NF-kappa-B activation.|||Phosphoserine|||Polar residues|||Removed|||TRAF-type|||TRAF-type zinc finger domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000278459|||http://purl.uniprot.org/annotation/VSP_023294 http://togogenome.org/gene/10090:Me1 ^@ http://purl.uniprot.org/uniprot/P06801|||http://purl.uniprot.org/uniprot/Q3TQP6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site ^@ Important for activity|||Malic enzyme N-terminal|||Malic enzyme NAD-binding|||N-acetylmethionine|||NADP-dependent malic enzyme|||Phosphoserine|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000160193 http://togogenome.org/gene/10090:Or4k49 ^@ http://purl.uniprot.org/uniprot/Q7TQX5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vegfd ^@ http://purl.uniprot.org/uniprot/P97946 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ 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|||Vascular endothelial growth factor D ^@ http://purl.uniprot.org/annotation/PRO_0000023411|||http://purl.uniprot.org/annotation/PRO_0000023412|||http://purl.uniprot.org/annotation/PRO_0000023413 http://togogenome.org/gene/10090:4931406C07Rik ^@ http://purl.uniprot.org/uniprot/Q91V76 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Ester hydrolase C11orf54 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000246030 http://togogenome.org/gene/10090:Slc22a15 ^@ http://purl.uniprot.org/uniprot/Q504N2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 15 ^@ http://purl.uniprot.org/annotation/PRO_0000338620|||http://purl.uniprot.org/annotation/VSP_034061|||http://purl.uniprot.org/annotation/VSP_034064 http://togogenome.org/gene/10090:Krtap19-5 ^@ http://purl.uniprot.org/uniprot/O08632 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ 14 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 19-5 ^@ http://purl.uniprot.org/annotation/PRO_0000361663 http://togogenome.org/gene/10090:Cables2 ^@ http://purl.uniprot.org/uniprot/Q8K3M5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ CDK5 and ABL1 enzyme substrate 2|||Disordered|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000080513 http://togogenome.org/gene/10090:Vamp2 ^@ http://purl.uniprot.org/uniprot/P63044|||http://purl.uniprot.org/uniprot/Q8CHR4 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ (Microbial infection) Cleavage; by C.botulinum neurotoxin type B (BoNT/B, botB)|||(Microbial infection) Cleavage; by C.tetani neurotoxin (tetX)|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||N-acetylserine|||Removed|||Required for interaction with SEPT8|||V-SNARE coiled-coil homology|||Vesicle-associated membrane protein 2|||Vesicular|||v-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000206725 http://togogenome.org/gene/10090:Vmn1r94 ^@ http://purl.uniprot.org/uniprot/K7N6X3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Col10a1 ^@ http://purl.uniprot.org/uniprot/Q05306 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide ^@ C1q|||Collagen alpha-1(X) chain|||Disordered|||Nonhelical region (NC1)|||Nonhelical region (NC2)|||Pro residues|||Triple-helical region ^@ http://purl.uniprot.org/annotation/PRO_0000005771 http://togogenome.org/gene/10090:Arl8a ^@ http://purl.uniprot.org/uniprot/Q8VEH3 ^@ Binding Site|||Chain|||INTRAMEM|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||INTRAMEM ^@ ADP-ribosylation factor-like protein 8A|||Note=Mediates targeting to membranes ^@ http://purl.uniprot.org/annotation/PRO_0000232917 http://togogenome.org/gene/10090:Tnfaip8l2 ^@ http://purl.uniprot.org/uniprot/Q9D8Y7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Phosphoserine|||Tumor necrosis factor alpha-induced protein 8-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000285772 http://togogenome.org/gene/10090:Zfp345 ^@ http://purl.uniprot.org/uniprot/A2AQA1|||http://purl.uniprot.org/uniprot/Q3UML8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Stk32c ^@ http://purl.uniprot.org/uniprot/E9PXK4|||http://purl.uniprot.org/uniprot/Q8QZV4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 32C ^@ http://purl.uniprot.org/annotation/PRO_0000232416 http://togogenome.org/gene/10090:Or8c11 ^@ http://purl.uniprot.org/uniprot/E9Q891 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Myh2 ^@ http://purl.uniprot.org/uniprot/G3UW82 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Actin-binding|||Basic and acidic residues|||Disordered|||Myosin N-terminal SH3-like|||Myosin motor ^@ http://togogenome.org/gene/10090:Cib4 ^@ http://purl.uniprot.org/uniprot/Q9D9N5 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Calcium and integrin-binding family member 4|||EF-hand 1|||EF-hand 2|||EF-hand 3 ^@ http://purl.uniprot.org/annotation/PRO_0000289291 http://togogenome.org/gene/10090:Baiap2l2 ^@ http://purl.uniprot.org/uniprot/Q80Y61 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand ^@ Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2|||Deficient in oligomerization (dimerization maintained). Inefficient formation of planar membrane structures. No effect on lipid-binding.|||Disordered|||IMD|||Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-109.|||Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-116.|||Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-127.|||Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-135.|||Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-145 and A-146.|||Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-145 and A-147.|||Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-146 and A-147.|||In isoform 2.|||No effect on lipid-binding.|||No effect on lipid-binding; when associated with A-149 and A-152.|||No effect on lipid-binding; when associated with A-149 and A-155.|||No effect on lipid-binding; when associated with A-152 and A-155.|||Partially impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering.|||Phosphoserine|||Polar residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000256131|||http://purl.uniprot.org/annotation/VSP_021325|||http://purl.uniprot.org/annotation/VSP_021326 http://togogenome.org/gene/10090:Gucy2f ^@ http://purl.uniprot.org/uniprot/Q5SDA5 ^@ 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|||Guanylate cyclase|||Helical|||Interchain|||Protein kinase|||Retinal guanylyl cyclase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000280445 http://togogenome.org/gene/10090:Stx18 ^@ http://purl.uniprot.org/uniprot/Q8VDS8 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||Syntaxin-18|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000210232|||http://purl.uniprot.org/annotation/VSP_017902|||http://purl.uniprot.org/annotation/VSP_017903|||http://purl.uniprot.org/annotation/VSP_017904 http://togogenome.org/gene/10090:Prr7 ^@ http://purl.uniprot.org/uniprot/B2RSG4|||http://purl.uniprot.org/uniprot/Q3V0I2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||PDZ-binding|||Phosphoserine|||Proline-rich protein 7|||Required for apoptosis induction|||Required for interaction with NMDA receptors|||Required for internalization|||Required for membrane localization ^@ http://purl.uniprot.org/annotation/PRO_0000328650 http://togogenome.org/gene/10090:Mpp1 ^@ http://purl.uniprot.org/uniprot/P70290|||http://purl.uniprot.org/uniprot/Q542P4 ^@ 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 ^@ 55 kDa erythrocyte membrane protein|||Disordered|||Guanylate kinase-like|||Interaction with PALS1|||N-acetylthreonine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000094566 http://togogenome.org/gene/10090:4930524B15Rik ^@ http://purl.uniprot.org/uniprot/Q24JP4 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Uncharacterized protein C5orf47 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000321822 http://togogenome.org/gene/10090:Or9e1 ^@ http://purl.uniprot.org/uniprot/Q5NC59 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dzank1 ^@ http://purl.uniprot.org/uniprot/B2RUH8|||http://purl.uniprot.org/uniprot/Q8C008 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Zinc Finger ^@ ANK 1|||ANK 2|||DZANK-type|||DZANK-type 1|||DZANK-type 2|||Double zinc ribbon and ankyrin repeat-containing protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000235912 http://togogenome.org/gene/10090:Hoatz ^@ http://purl.uniprot.org/uniprot/Q80Y73 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Cilia- and flagella-associated protein HOATZ|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000328996 http://togogenome.org/gene/10090:Fam98c ^@ http://purl.uniprot.org/uniprot/E9PYD1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Cacna1d ^@ http://purl.uniprot.org/uniprot/A0A286YD72|||http://purl.uniprot.org/uniprot/A0A589Q4M7|||http://purl.uniprot.org/uniprot/Q99246 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phenylalkylamine binding|||Polar residues|||Voltage-dependent L-type calcium channel subunit alpha-1D|||Voltage-dependent calcium channel alpha-1 subunit IQ ^@ http://purl.uniprot.org/annotation/PRO_0000053935|||http://purl.uniprot.org/annotation/VSP_027090|||http://purl.uniprot.org/annotation/VSP_027091|||http://purl.uniprot.org/annotation/VSP_027092 http://togogenome.org/gene/10090:Tmem268 ^@ http://purl.uniprot.org/uniprot/Q8R239 ^@ 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.|||In isoform 3.|||Transmembrane protein 268 ^@ http://purl.uniprot.org/annotation/PRO_0000279426|||http://purl.uniprot.org/annotation/VSP_023428|||http://purl.uniprot.org/annotation/VSP_023429|||http://purl.uniprot.org/annotation/VSP_023430 http://togogenome.org/gene/10090:Rnpep ^@ http://purl.uniprot.org/uniprot/E9PYF1|||http://purl.uniprot.org/uniprot/Q8BMH2|||http://purl.uniprot.org/uniprot/Q8VCT3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site ^@ Aminopeptidase B|||N6-acetyllysine|||Peptidase M1 leukotriene A4 hydrolase/aminopeptidase C-terminal|||Proton acceptor|||Proton donor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000095089 http://togogenome.org/gene/10090:Ptprcap ^@ http://purl.uniprot.org/uniprot/Q542J3|||http://purl.uniprot.org/uniprot/Q64697 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Polar residues|||Protein tyrosine phosphatase receptor type C-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000097088|||http://purl.uniprot.org/annotation/PRO_5014309538 http://togogenome.org/gene/10090:Apc ^@ http://purl.uniprot.org/uniprot/B2RUG9|||http://purl.uniprot.org/uniprot/Q8BNP7 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat ^@ ARM|||Adenomatous polyposis coli N-terminal dimerisation|||Adenomatous polyposis coli protein basic|||Basic and acidic residues|||Disordered|||EB-1 binding|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Kbtbd4 ^@ http://purl.uniprot.org/uniprot/Q8R179 ^@ 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 repeat and BTB domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000119082|||http://purl.uniprot.org/annotation/VSP_010221 http://togogenome.org/gene/10090:Fgf13 ^@ http://purl.uniprot.org/uniprot/A0A7U3JW69|||http://purl.uniprot.org/uniprot/P70377 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Fibroblast growth factor 13|||In isoform 2.|||In isoform 3.|||Mediates interaction with sodium channels|||Mediates targeting to the nucleus|||Phosphoserine|||Tubulin-binding domain necessary and sufficient for tubulin-binding ^@ http://purl.uniprot.org/annotation/PRO_0000147608|||http://purl.uniprot.org/annotation/VSP_044130|||http://purl.uniprot.org/annotation/VSP_044131 http://togogenome.org/gene/10090:Med9 ^@ http://purl.uniprot.org/uniprot/Q8VCS6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Mediator of RNA polymerase II transcription subunit 9|||N-acetylalanine|||Phosphoserine|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000304148 http://togogenome.org/gene/10090:Nsmce1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0C0|||http://purl.uniprot.org/uniprot/Q9D720 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Interaction with NSMCE3|||Non-structural maintenance of chromosomes element 1 homolog|||Phorbol-ester/DAG-type|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000270945 http://togogenome.org/gene/10090:Ppig ^@ http://purl.uniprot.org/uniprot/A2AR02 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase G|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000282597 http://togogenome.org/gene/10090:Pcsk1 ^@ http://purl.uniprot.org/uniprot/P63239|||http://purl.uniprot.org/uniprot/Q32MU0 ^@ Active Site|||Chain|||Compositionally Biased Region|||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|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Charge relay system|||Disordered|||N-linked (GlcNAc...) asparagine|||Neuroendocrine convertase 1|||P/Homo B|||Peptidase S8|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000027059|||http://purl.uniprot.org/annotation/PRO_0000027060|||http://purl.uniprot.org/annotation/PRO_5014309030 http://togogenome.org/gene/10090:Rhox3a ^@ http://purl.uniprot.org/uniprot/Q4TU90 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Spink1 ^@ http://purl.uniprot.org/uniprot/P09036 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Signal Peptide|||Site ^@ Abolishes trypsin inhibitor activity. No effect on sperm binding.|||Fails to bind sperm. No effect on trypsin inhibitor activity.|||Kazal-like|||Necessary for sperm binding|||No effect on trypsin inhibitor activity or sperm binding.|||Reactive bond for trypsin|||Serine protease inhibitor Kazal-type 1|||Severely impairs sperm binding. No effect on trypsin inhibitor activity. ^@ http://purl.uniprot.org/annotation/PRO_0000016568 http://togogenome.org/gene/10090:Cpeb2 ^@ http://purl.uniprot.org/uniprot/A0A0H2UH22|||http://purl.uniprot.org/uniprot/E9Q5X2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Pro residues|||RRM ^@ http://togogenome.org/gene/10090:Or5p80 ^@ http://purl.uniprot.org/uniprot/Q8VG42 ^@ 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 5P80 ^@ http://purl.uniprot.org/annotation/PRO_0000150855 http://togogenome.org/gene/10090:A530016L24Rik ^@ http://purl.uniprot.org/uniprot/A0A0R4J0P8|||http://purl.uniprot.org/uniprot/Q8BNX7 ^@ 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|||Nutritionally-regulated adipose and cardiac-enriched protein ^@ http://purl.uniprot.org/annotation/PRO_0000326053 http://togogenome.org/gene/10090:Actmap ^@ http://purl.uniprot.org/uniprot/J3QPC3 ^@ Active Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Actin maturation protease|||Disordered|||In isoform 2.|||Peptidase C39-like|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000457346|||http://purl.uniprot.org/annotation/VSP_061770|||http://purl.uniprot.org/annotation/VSP_061771 http://togogenome.org/gene/10090:Pdgfc ^@ http://purl.uniprot.org/uniprot/Q8CI19 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ CUB|||Cleavage|||Disordered|||Interchain (with C-274)|||Interchain (with C-286)|||N-linked (GlcNAc...) asparagine|||Platelet-derived growth factor C, latent form|||Platelet-derived growth factor C, receptor-binding form|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000343873|||http://purl.uniprot.org/annotation/PRO_0000343874 http://togogenome.org/gene/10090:Galnt14 ^@ http://purl.uniprot.org/uniprot/Q08EC9|||http://purl.uniprot.org/uniprot/Q8BVG5 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||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|||Polypeptide N-acetylgalactosaminyltransferase 14|||Ricin B lectin|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059134|||http://purl.uniprot.org/annotation/VSP_011225|||http://purl.uniprot.org/annotation/VSP_011226 http://togogenome.org/gene/10090:Timm44 ^@ http://purl.uniprot.org/uniprot/O35857 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Transit Peptide ^@ Abolished interaction with SLC25A4/ANT1.|||Mitochondrial import inner membrane translocase subunit TIM44|||Mitochondrion|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000034315 http://togogenome.org/gene/10090:Ctag2l1 ^@ http://purl.uniprot.org/uniprot/A3KG45 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or1a1b ^@ http://purl.uniprot.org/uniprot/Q7TRX1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dnajc13 ^@ http://purl.uniprot.org/uniprot/G3X922|||http://purl.uniprot.org/uniprot/Q3TNE7|||http://purl.uniprot.org/uniprot/Q8BNL1|||http://purl.uniprot.org/uniprot/Q8CHD7 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||DnaJ homologue subfamily C GRV2/DNAJC13 N-terminal|||J ^@ http://togogenome.org/gene/10090:Mtmr11 ^@ http://purl.uniprot.org/uniprot/Q3V1L6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||Myotubularin phosphatase|||Myotubularin-related protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000337099 http://togogenome.org/gene/10090:Klrh1 ^@ http://purl.uniprot.org/uniprot/Q58A37 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ C-type lectin|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Astn1 ^@ http://purl.uniprot.org/uniprot/Q3UHD7|||http://purl.uniprot.org/uniprot/Q61137 ^@ 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 ^@ Astrotactin-1|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Extracellular|||Fibronectin type-III|||Helical|||In isoform 2.|||MACPF|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000007482|||http://purl.uniprot.org/annotation/PRO_5004230121|||http://purl.uniprot.org/annotation/VSP_014917 http://togogenome.org/gene/10090:H2-Ab1 ^@ http://purl.uniprot.org/uniprot/P14483|||http://purl.uniprot.org/uniprot/Q3TD53|||http://purl.uniprot.org/uniprot/Q8BPA0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Beta-1|||Beta-2|||Connecting peptide|||Cytoplasmic|||Extracellular|||H-2 class II histocompatibility antigen, A beta chain|||Helical|||Ig-like|||Ig-like C1-type|||Ig-like domain-containing protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000018993|||http://purl.uniprot.org/annotation/PRO_5004303786|||http://purl.uniprot.org/annotation/PRO_5010843273 http://togogenome.org/gene/10090:Neurl1a ^@ http://purl.uniprot.org/uniprot/Q499W5|||http://purl.uniprot.org/uniprot/Q923S6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase NEURL1|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||NHR|||NHR 1|||NHR 2|||Polar residues|||RING-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000181256|||http://purl.uniprot.org/annotation/VSP_013152|||http://purl.uniprot.org/annotation/VSP_013153|||http://purl.uniprot.org/annotation/VSP_013154 http://togogenome.org/gene/10090:Cdh5 ^@ http://purl.uniprot.org/uniprot/P55284 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes interaction with PALS1.|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-5|||Cytoplasmic|||Extracellular|||Helical|||Impairs PARD3 binding.|||N-linked (GlcNAc...) asparagine|||No effect on PARD3 binding.|||Required for interaction with PALS1 ^@ http://purl.uniprot.org/annotation/PRO_0000003757|||http://purl.uniprot.org/annotation/PRO_0000003758 http://togogenome.org/gene/10090:Hnrnpab ^@ http://purl.uniprot.org/uniprot/Q20BD0|||http://purl.uniprot.org/uniprot/Q544Z3|||http://purl.uniprot.org/uniprot/Q99020 ^@ 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 ^@ Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein A/B|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||RRM|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081493 http://togogenome.org/gene/10090:Glb1 ^@ http://purl.uniprot.org/uniprot/P23780|||http://purl.uniprot.org/uniprot/Q3TAW7 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Beta-galactosidase|||Beta-galactosidase jelly roll|||Glycoside hydrolase 35 catalytic|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000012190|||http://purl.uniprot.org/annotation/PRO_0000012191|||http://purl.uniprot.org/annotation/PRO_5009970779 http://togogenome.org/gene/10090:Tbc1d22b ^@ http://purl.uniprot.org/uniprot/Q80VE5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Rab-GAP TBC ^@ http://togogenome.org/gene/10090:Atl3 ^@ http://purl.uniprot.org/uniprot/E9PYT3|||http://purl.uniprot.org/uniprot/Q91YH5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Atlastin-3|||Cytoplasmic|||Disordered|||GB1/RHD3-type G|||Helical|||In isoform 2.|||Lumenal|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000287110|||http://purl.uniprot.org/annotation/VSP_025314 http://togogenome.org/gene/10090:Ssxb10 ^@ http://purl.uniprot.org/uniprot/Q6XAR7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB|||KRAB-related ^@ http://togogenome.org/gene/10090:Hdgfl3 ^@ http://purl.uniprot.org/uniprot/Q9JMG7 ^@ 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|||Basic residues|||Disordered|||Hepatoma-derived growth factor-related protein 3|||In isoform 2.|||Nuclear localization signal|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000191704|||http://purl.uniprot.org/annotation/VSP_014188 http://togogenome.org/gene/10090:Fmr1nb ^@ http://purl.uniprot.org/uniprot/B7ZNB2|||http://purl.uniprot.org/uniprot/B7ZW84|||http://purl.uniprot.org/uniprot/Q80ZA7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Fmr1 neighbor protein|||Helical|||In isoform 2.|||P-type ^@ http://purl.uniprot.org/annotation/PRO_0000281736|||http://purl.uniprot.org/annotation/VSP_024024 http://togogenome.org/gene/10090:Psat1 ^@ http://purl.uniprot.org/uniprot/Q3U6K9|||http://purl.uniprot.org/uniprot/Q543K5|||http://purl.uniprot.org/uniprot/Q99K85 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Aminotransferase class V|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine aminotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000150136 http://togogenome.org/gene/10090:Ccdc71 ^@ http://purl.uniprot.org/uniprot/Q8VEG0 ^@ 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|||Coiled-coil domain-containing protein 71|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000234422 http://togogenome.org/gene/10090:Pbxip1 ^@ http://purl.uniprot.org/uniprot/Q3TVI8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pre-B-cell leukemia transcription factor-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000306116 http://togogenome.org/gene/10090:Rnase10 ^@ http://purl.uniprot.org/uniprot/E9QPU5|||http://purl.uniprot.org/uniprot/G3UWD1|||http://purl.uniprot.org/uniprot/Q9D5A9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Helical|||Inactive ribonuclease-like protein 10|||N-linked (GlcNAc...) asparagine|||Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_0000045964|||http://purl.uniprot.org/annotation/PRO_5015091593 http://togogenome.org/gene/10090:Rpl22 ^@ http://purl.uniprot.org/uniprot/P67984 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Large ribosomal subunit protein eL22|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000215502 http://togogenome.org/gene/10090:Ppp2cb ^@ http://purl.uniprot.org/uniprot/P62715|||http://purl.uniprot.org/uniprot/Q8BN07 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue ^@ Leucine methyl ester|||Loss of binding to PP2AB-alpha regulatory subunit.|||Loss of trimeric subunit ABC assembly.|||Phosphotyrosine|||Proton donor|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform ^@ http://purl.uniprot.org/annotation/PRO_0000058846 http://togogenome.org/gene/10090:Defb50 ^@ http://purl.uniprot.org/uniprot/Q6TU36 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 50 ^@ http://purl.uniprot.org/annotation/PRO_0000006954 http://togogenome.org/gene/10090:C2cd6 ^@ http://purl.uniprot.org/uniprot/Q8C639 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rad23b ^@ http://purl.uniprot.org/uniprot/P54728|||http://purl.uniprot.org/uniprot/Q3UQN3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||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_0000114907 http://togogenome.org/gene/10090:Twf2 ^@ http://purl.uniprot.org/uniprot/Q9Z0P5 ^@ 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|||Region|||Sequence Conflict|||Splice Variant ^@ ADF-H 1|||ADF-H 2|||Disordered|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed|||Twinfilin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000233137|||http://purl.uniprot.org/annotation/VSP_018053 http://togogenome.org/gene/10090:Bche ^@ http://purl.uniprot.org/uniprot/Q03311 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Acyl-ester intermediate|||Charge relay system|||Cholinesterase|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000008614 http://togogenome.org/gene/10090:Stmn2 ^@ http://purl.uniprot.org/uniprot/P55821|||http://purl.uniprot.org/uniprot/Q545S4 ^@ Chain|||Coiled-Coil|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent|||Lipid Binding|||Modified Residue|||Region ^@ Membrane attachment|||Phosphoserine|||Regulatory/phosphorylation domain|||S-palmitoyl cysteine|||SLD|||Stathmin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000182397 http://togogenome.org/gene/10090:Epb41l1 ^@ http://purl.uniprot.org/uniprot/A2AUK5|||http://purl.uniprot.org/uniprot/A2AUK7|||http://purl.uniprot.org/uniprot/A2AUK8|||http://purl.uniprot.org/uniprot/Q9Z2H5 ^@ 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 ^@ Band 4.1-like protein 1|||Basic and acidic residues|||C-terminal (CTD)|||Disordered|||FERM|||Hydrophilic|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Spectrin--actin-binding ^@ http://purl.uniprot.org/annotation/PRO_0000219396|||http://purl.uniprot.org/annotation/VSP_023964|||http://purl.uniprot.org/annotation/VSP_023965 http://togogenome.org/gene/10090:Fam110c ^@ http://purl.uniprot.org/uniprot/Q8VE94 ^@ 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_0000293462 http://togogenome.org/gene/10090:Pdzk1ip1 ^@ http://purl.uniprot.org/uniprot/G3UW41|||http://purl.uniprot.org/uniprot/Q9CQH0 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||PDZK1-interacting protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000058283 http://togogenome.org/gene/10090:Farsa ^@ http://purl.uniprot.org/uniprot/Q8C0C7 ^@ 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-acetylalanine|||N6-acetyllysine|||Phenylalanine--tRNA ligase alpha subunit|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000280447 http://togogenome.org/gene/10090:Lipa ^@ http://purl.uniprot.org/uniprot/Q3TEL5|||http://purl.uniprot.org/uniprot/Q9Z0M5 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ AB hydrolase-1|||Charge relay system|||Lipase|||Lysosomal acid lipase/cholesteryl ester hydrolase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000017800|||http://purl.uniprot.org/annotation/PRO_0000450227|||http://purl.uniprot.org/annotation/PRO_5004229517 http://togogenome.org/gene/10090:Or1j18 ^@ http://purl.uniprot.org/uniprot/Q8VGK2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Diras2 ^@ http://purl.uniprot.org/uniprot/Q5PR73 ^@ 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|||GTP-binding protein Di-Ras2|||Phosphoserine|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000191652|||http://purl.uniprot.org/annotation/PRO_0000370779 http://togogenome.org/gene/10090:Zfp715 ^@ http://purl.uniprot.org/uniprot/G3X9T1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Hspa4 ^@ http://purl.uniprot.org/uniprot/Q3U2G2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Armc3 ^@ http://purl.uniprot.org/uniprot/A2AU71|||http://purl.uniprot.org/uniprot/A2AU72|||http://purl.uniprot.org/uniprot/B7ZN53 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||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|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284404|||http://purl.uniprot.org/annotation/VSP_024502|||http://purl.uniprot.org/annotation/VSP_024503|||http://purl.uniprot.org/annotation/VSP_024504 http://togogenome.org/gene/10090:Magea6 ^@ http://purl.uniprot.org/uniprot/O89010 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Rasa3 ^@ http://purl.uniprot.org/uniprot/Q60790 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Zinc Finger ^@ Btk-type|||C2 1|||C2 2|||N-acetylalanine|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Ras GTPase-activating protein 3|||Ras-GAP|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056643 http://togogenome.org/gene/10090:Kif3b ^@ http://purl.uniprot.org/uniprot/Q3UHC4|||http://purl.uniprot.org/uniprot/Q61771|||http://purl.uniprot.org/uniprot/Q6P1D3 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Globular|||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_0000125396|||http://purl.uniprot.org/annotation/PRO_0000424496 http://togogenome.org/gene/10090:St7l ^@ http://purl.uniprot.org/uniprot/Q8CDC5|||http://purl.uniprot.org/uniprot/Q8K4P7 ^@ 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.|||In isoform 3.|||Polar residues|||Suppressor of tumorigenicity 7 protein-like ^@ http://purl.uniprot.org/annotation/PRO_0000339228|||http://purl.uniprot.org/annotation/VSP_034137|||http://purl.uniprot.org/annotation/VSP_034138 http://togogenome.org/gene/10090:Jmjd1c ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ98|||http://purl.uniprot.org/uniprot/G3UZM1|||http://purl.uniprot.org/uniprot/Q69ZK6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C6-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||JmjC|||LXXLL motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable JmjC domain-containing histone demethylation protein 2C ^@ http://purl.uniprot.org/annotation/PRO_0000234375 http://togogenome.org/gene/10090:Was ^@ http://purl.uniprot.org/uniprot/P70315|||http://purl.uniprot.org/uniprot/Q53WY0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Acidic residues|||Actin nucleation-promoting factor WAS|||CRIB|||Disordered|||GRSGPLPPXP motif 1|||GRSGPLPPXP motif 2|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||WH1|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000188991 http://togogenome.org/gene/10090:Slc36a1 ^@ http://purl.uniprot.org/uniprot/Q5F227|||http://purl.uniprot.org/uniprot/Q8K4D3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Amino acid transporter transmembrane|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Proton-coupled amino acid transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000093826 http://togogenome.org/gene/10090:Mrgprx2 ^@ http://purl.uniprot.org/uniprot/Q3UFT2|||http://purl.uniprot.org/uniprot/Q3UG50 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||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|||Mas-related G-protein coupled receptor member X2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000303886 http://togogenome.org/gene/10090:H2ap ^@ http://purl.uniprot.org/uniprot/Q9CR04 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Huntingtin-interacting protein M ^@ http://purl.uniprot.org/annotation/PRO_0000254088 http://togogenome.org/gene/10090:Tmem160 ^@ http://purl.uniprot.org/uniprot/Q9D938 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Transit Peptide|||Transmembrane ^@ Disordered|||Helical|||Mitochondrion|||Phosphoserine|||Transmembrane protein 160 ^@ http://purl.uniprot.org/annotation/PRO_0000277811 http://togogenome.org/gene/10090:Rnase2b ^@ http://purl.uniprot.org/uniprot/O35292|||http://purl.uniprot.org/uniprot/W0UVC5 ^@ 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|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Proton acceptor|||Proton donor|||Ribonuclease 2B|||Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_0000030870|||http://purl.uniprot.org/annotation/PRO_5007751497 http://togogenome.org/gene/10090:Cisd2 ^@ http://purl.uniprot.org/uniprot/Q9CQB5 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CDGSH iron-sulfur domain-containing protein 2|||Cytoplasmic|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000316006 http://togogenome.org/gene/10090:Rnf167 ^@ http://purl.uniprot.org/uniprot/Q91XF4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane|||Zinc Finger ^@ Acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF167|||Helical|||N-linked (GlcNAc...) asparagine|||PA|||Polar residues|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000245594 http://togogenome.org/gene/10090:Naa40 ^@ http://purl.uniprot.org/uniprot/Q8VE10 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Site|||Splice Variant ^@ Essential for catalytic activity|||In isoform 2.|||In isoform 3.|||N-acetyltransferase|||N-alpha-acetyltransferase 40|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000284898|||http://purl.uniprot.org/annotation/VSP_024744|||http://purl.uniprot.org/annotation/VSP_024745|||http://purl.uniprot.org/annotation/VSP_024746 http://togogenome.org/gene/10090:Npb ^@ http://purl.uniprot.org/uniprot/A2ABY0|||http://purl.uniprot.org/uniprot/A2ABY2|||http://purl.uniprot.org/uniprot/Q3UR83|||http://purl.uniprot.org/uniprot/Q8K4P1 ^@ Chain|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Chain|||Peptide|||Propeptide|||Signal Peptide ^@ Neuropeptide B|||Neuropeptide B-29 ^@ http://purl.uniprot.org/annotation/PRO_0000019839|||http://purl.uniprot.org/annotation/PRO_0000019840|||http://purl.uniprot.org/annotation/PRO_5002642638|||http://purl.uniprot.org/annotation/PRO_5002642648|||http://purl.uniprot.org/annotation/PRO_5010843464 http://togogenome.org/gene/10090:Coa5 ^@ http://purl.uniprot.org/uniprot/Q99M07 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif ^@ CHCH|||Cx10C motif|||Cx9C motif|||Cytochrome c oxidase assembly factor 5|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000325877 http://togogenome.org/gene/10090:Hes5 ^@ http://purl.uniprot.org/uniprot/P70120|||http://purl.uniprot.org/uniprot/Q499J8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ BHLH|||Disordered|||Orange|||Pro residues|||Transcription factor HES-5|||WRPW motif|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127212 http://togogenome.org/gene/10090:Tmem254 ^@ http://purl.uniprot.org/uniprot/P0DN89 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Transmembrane protein 254 ^@ http://purl.uniprot.org/annotation/PRO_0000089797|||http://purl.uniprot.org/annotation/VSP_058265 http://togogenome.org/gene/10090:Hspbap1 ^@ http://purl.uniprot.org/uniprot/Q8BK58 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||HSPB1-associated protein 1|||Interaction with HSPB1|||JmjC ^@ http://purl.uniprot.org/annotation/PRO_0000284114 http://togogenome.org/gene/10090:Gm2411 ^@ http://purl.uniprot.org/uniprot/A0A571BDF8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Pcdhb17 ^@ http://purl.uniprot.org/uniprot/Q91VD8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099500 http://togogenome.org/gene/10090:Sirt3 ^@ http://purl.uniprot.org/uniprot/Q4FJK3|||http://purl.uniprot.org/uniprot/Q8R104 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Deacetylase sirtuin-type|||In isoform S.|||Mitochondrion|||N6-succinyllysine|||NAD-dependent protein deacetylase sirtuin-3|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000110263|||http://purl.uniprot.org/annotation/VSP_053760 http://togogenome.org/gene/10090:Pbx3 ^@ http://purl.uniprot.org/uniprot/O35317 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||DNA Binding|||Domain Extent|||Region|||Splice Variant ^@ Disordered|||Homeobox; TALE-type|||In isoform PBX3b.|||PBC|||PBC-A|||PBC-B|||Pre-B-cell leukemia transcription factor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000049240|||http://purl.uniprot.org/annotation/VSP_008615|||http://purl.uniprot.org/annotation/VSP_008616 http://togogenome.org/gene/10090:H1f1 ^@ http://purl.uniprot.org/uniprot/P43275 ^@ 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 ^@ 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|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000195914 http://togogenome.org/gene/10090:Lmln ^@ http://purl.uniprot.org/uniprot/Q8BMN4 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Leishmanolysin-like peptidase ^@ http://purl.uniprot.org/annotation/PRO_0000303077 http://togogenome.org/gene/10090:Fgfr3 ^@ http://purl.uniprot.org/uniprot/E9QNJ9|||http://purl.uniprot.org/uniprot/F6TK14|||http://purl.uniprot.org/uniprot/Q61563|||http://purl.uniprot.org/uniprot/Q7TSI8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Fibroblast growth factor receptor|||Helical|||Ig-like|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_5003342556|||http://purl.uniprot.org/annotation/PRO_5015090380|||http://purl.uniprot.org/annotation/PRO_5015098103|||http://purl.uniprot.org/annotation/PRO_5015098860 http://togogenome.org/gene/10090:Or10d4b ^@ http://purl.uniprot.org/uniprot/Q8VET5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ttc17 ^@ http://purl.uniprot.org/uniprot/A2AFY7|||http://purl.uniprot.org/uniprot/E9PVB5|||http://purl.uniprot.org/uniprot/Q8C1H7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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_0000426010|||http://purl.uniprot.org/annotation/VSP_053920 http://togogenome.org/gene/10090:Cdc42 ^@ http://purl.uniprot.org/uniprot/P60766 ^@ 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 ^@ Cell division control protein 42 homolog|||Constitutively activated. Enhances interaction with DOCK11.|||Constitutively inactivated. Abolishes interaction with PARD6 and DOCK11. Inhibits filopodia formation.|||Cysteine methyl ester|||Effector region|||In isoform 1.|||No effect on filopodia formation.|||Phosphotyrosine; by SRC|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000030427|||http://purl.uniprot.org/annotation/PRO_0000030428|||http://purl.uniprot.org/annotation/VSP_040585|||http://purl.uniprot.org/annotation/VSP_040586 http://togogenome.org/gene/10090:Rnf138rt1 ^@ http://purl.uniprot.org/uniprot/Q9D9M9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2HC RNF-type|||Disordered|||Polar residues|||RING-type ^@ http://togogenome.org/gene/10090:Pcnt ^@ http://purl.uniprot.org/uniprot/A0A1W2P737|||http://purl.uniprot.org/uniprot/F8VPV0|||http://purl.uniprot.org/uniprot/P48725|||http://purl.uniprot.org/uniprot/Q3TQR8|||http://purl.uniprot.org/uniprot/Q80U10|||http://purl.uniprot.org/uniprot/Q8CDL2 ^@ 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 ^@ Basic and acidic residues|||Calmodulin-binding|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with CDK5RAP2|||Interaction with NEK2|||Pericentrin|||Pericentrin/AKAP-450 centrosomal targeting|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000058258|||http://purl.uniprot.org/annotation/VSP_038927|||http://purl.uniprot.org/annotation/VSP_038928|||http://purl.uniprot.org/annotation/VSP_038929 http://togogenome.org/gene/10090:Dusp26 ^@ http://purl.uniprot.org/uniprot/Q9D700 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ Dual specificity protein phosphatase 26|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000292220 http://togogenome.org/gene/10090:Cldn1 ^@ http://purl.uniprot.org/uniprot/O88551|||http://purl.uniprot.org/uniprot/Q4FJV3 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Region|||Topological Domain|||Transmembrane ^@ Claudin-1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interactions with TJP1, TJP2, TJP3 and PATJ ^@ http://purl.uniprot.org/annotation/PRO_0000144730 http://togogenome.org/gene/10090:Ldaf1 ^@ http://purl.uniprot.org/uniprot/Q922Z1 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lipid droplet assembly factor 1|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000279536 http://togogenome.org/gene/10090:Slc32a1 ^@ http://purl.uniprot.org/uniprot/O35633|||http://purl.uniprot.org/uniprot/Q49S98 ^@ 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 ^@ 3'-nitrotyrosine|||Amino acid transporter transmembrane|||Cytoplasmic|||Helical|||In isoform 2.|||Lumenal, vesicle|||Vesicular inhibitory amino acid transporter ^@ http://purl.uniprot.org/annotation/PRO_0000093822|||http://purl.uniprot.org/annotation/VSP_007063 http://togogenome.org/gene/10090:Med14 ^@ http://purl.uniprot.org/uniprot/A2ABV5 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||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_0000304585|||http://purl.uniprot.org/annotation/VSP_028033|||http://purl.uniprot.org/annotation/VSP_028034|||http://purl.uniprot.org/annotation/VSP_028035|||http://purl.uniprot.org/annotation/VSP_028036|||http://purl.uniprot.org/annotation/VSP_028037|||http://purl.uniprot.org/annotation/VSP_028038 http://togogenome.org/gene/10090:Myo18b ^@ http://purl.uniprot.org/uniprot/E9PV66 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Myosin motor|||Polar residues ^@ http://togogenome.org/gene/10090:Or11l3 ^@ http://purl.uniprot.org/uniprot/Q5NCD0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Arv1 ^@ http://purl.uniprot.org/uniprot/Q0VBH5|||http://purl.uniprot.org/uniprot/Q9D0U9 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Protein ARV1 ^@ http://purl.uniprot.org/annotation/PRO_0000228660 http://togogenome.org/gene/10090:Taar7a ^@ http://purl.uniprot.org/uniprot/Q5QD12 ^@ 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|||Trace amine-associated receptor 7a ^@ http://purl.uniprot.org/annotation/PRO_0000070162 http://togogenome.org/gene/10090:Prkd1 ^@ http://purl.uniprot.org/uniprot/Q62101 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||High basal kinase activity, loss of phorbol ester-stimulated kinase activity; when associated with D-744.|||High basal kinase activity, loss of phorbol ester-stimulated kinase activity; when associated with D-748.|||Loss of basal kinase activity and phorbol ester-stimulated kinase activity; when associated with A-744.|||Loss of basal kinase activity and phorbol ester-stimulated kinase activity; when associated with A-748.|||PH|||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_0000055715 http://togogenome.org/gene/10090:Tnfrsf14 ^@ http://purl.uniprot.org/uniprot/A0A1W2P7D5|||http://purl.uniprot.org/uniprot/Q80WM9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Signal Peptide|||Strand|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 14 ^@ http://purl.uniprot.org/annotation/PRO_5010723555|||http://purl.uniprot.org/annotation/PRO_5015098926 http://togogenome.org/gene/10090:Mix23 ^@ http://purl.uniprot.org/uniprot/Q8R3Q6 ^@ 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_0000239442 http://togogenome.org/gene/10090:Or8b55 ^@ http://purl.uniprot.org/uniprot/Q8VG50 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sorbs1 ^@ http://purl.uniprot.org/uniprot/A0A286YCQ0|||http://purl.uniprot.org/uniprot/A0A286YDN0|||http://purl.uniprot.org/uniprot/D3Z5J3|||http://purl.uniprot.org/uniprot/E9PYX6|||http://purl.uniprot.org/uniprot/E9Q6A3|||http://purl.uniprot.org/uniprot/E9QNA7|||http://purl.uniprot.org/uniprot/Q62417 ^@ 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, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 2, isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||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_0000072186|||http://purl.uniprot.org/annotation/VSP_050885|||http://purl.uniprot.org/annotation/VSP_050886|||http://purl.uniprot.org/annotation/VSP_050887|||http://purl.uniprot.org/annotation/VSP_050888|||http://purl.uniprot.org/annotation/VSP_050889|||http://purl.uniprot.org/annotation/VSP_050890|||http://purl.uniprot.org/annotation/VSP_050891|||http://purl.uniprot.org/annotation/VSP_050892|||http://purl.uniprot.org/annotation/VSP_050893|||http://purl.uniprot.org/annotation/VSP_050894 http://togogenome.org/gene/10090:Xlr5c ^@ http://purl.uniprot.org/uniprot/A2AIE6|||http://purl.uniprot.org/uniprot/Q9JJR2 ^@ 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|||X-linked lymphocyte-regulated protein 5C|||XLR/SYCP3/FAM9 ^@ http://purl.uniprot.org/annotation/PRO_0000443090 http://togogenome.org/gene/10090:Cbx3 ^@ http://purl.uniprot.org/uniprot/Q32P00|||http://purl.uniprot.org/uniprot/Q9DCC5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Chromo|||Disordered ^@ http://togogenome.org/gene/10090:Tpbg ^@ http://purl.uniprot.org/uniprot/Q9Z0L0 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Trophoblast glycoprotein ^@ http://purl.uniprot.org/annotation/PRO_0000019593 http://togogenome.org/gene/10090:Oxt ^@ http://purl.uniprot.org/uniprot/P35454|||http://purl.uniprot.org/uniprot/Q545V4 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Peptide|||Signal Peptide ^@ Glycine amide|||Neurophysin 1|||Oxytocin ^@ http://purl.uniprot.org/annotation/PRO_0000020497|||http://purl.uniprot.org/annotation/PRO_0000020498|||http://purl.uniprot.org/annotation/PRO_5014309645 http://togogenome.org/gene/10090:Kif11 ^@ http://purl.uniprot.org/uniprot/Q6P9P6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Kinesin motor|||Kinesin-like protein KIF11|||N6-acetyllysine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000253343 http://togogenome.org/gene/10090:Gm8765 ^@ http://purl.uniprot.org/uniprot/B7ZWJ3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||SPATA31 ^@ http://togogenome.org/gene/10090:Hnrnpl ^@ http://purl.uniprot.org/uniprot/Q3UMT7|||http://purl.uniprot.org/uniprot/Q8R081|||http://purl.uniprot.org/uniprot/Q9CVU5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein L|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CaMK4|||Polar residues|||Pro residues|||RRM|||RRM 1|||RRM 2|||RRM 3|||RRM 4 ^@ http://purl.uniprot.org/annotation/PRO_0000081863 http://togogenome.org/gene/10090:En2 ^@ http://purl.uniprot.org/uniprot/P09066|||http://purl.uniprot.org/uniprot/Q3TZM2 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Homeobox protein engrailed-2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000196068 http://togogenome.org/gene/10090:Pik3r1 ^@ http://purl.uniprot.org/uniprot/P26450|||http://purl.uniprot.org/uniprot/Q3TP23|||http://purl.uniprot.org/uniprot/Q80UI5|||http://purl.uniprot.org/uniprot/Q8C7P2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||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_0000080759 http://togogenome.org/gene/10090:Sae1 ^@ http://purl.uniprot.org/uniprot/Q9R1T2 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Splice Variant ^@ In isoform 2.|||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_0000194967|||http://purl.uniprot.org/annotation/PRO_0000423291|||http://purl.uniprot.org/annotation/VSP_022004 http://togogenome.org/gene/10090:Or4c11c ^@ http://purl.uniprot.org/uniprot/A2ATJ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Odr4 ^@ http://purl.uniprot.org/uniprot/Q4PJX1 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||In isoform 3.|||Protein odr-4 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000304684|||http://purl.uniprot.org/annotation/VSP_028101|||http://purl.uniprot.org/annotation/VSP_028102 http://togogenome.org/gene/10090:Pacc1 ^@ http://purl.uniprot.org/uniprot/Q9D771 ^@ 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|||Phosphotyrosine|||Proton-activated chloride channel ^@ http://purl.uniprot.org/annotation/PRO_0000279472 http://togogenome.org/gene/10090:Fam20a ^@ http://purl.uniprot.org/uniprot/Q8CID3 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Not secreted; nuclear localization.|||Pseudokinase FAM20A ^@ http://purl.uniprot.org/annotation/PRO_0000008744 http://togogenome.org/gene/10090:Ifit1bl2 ^@ http://purl.uniprot.org/uniprot/Q3U687 ^@ Region|||Repeat ^@ Repeat ^@ TPR ^@ http://togogenome.org/gene/10090:Micos13 ^@ http://purl.uniprot.org/uniprot/Q8R404 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Helical|||MICOS complex subunit MIC13|||Mitochondrial intermembrane|||Mitochondrial matrix ^@ http://purl.uniprot.org/annotation/PRO_0000289987 http://togogenome.org/gene/10090:Tab2 ^@ http://purl.uniprot.org/uniprot/Q99K90 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Turn|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Turn|||Zinc Finger ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||CUE|||Confers ability to bind monoubiquitin and polyubiquitin, irrespective of the type of linkage.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with polyubiquitin|||Loss of interaction with 'Lys-63'-linked ubiquitin.|||Phosphoserine|||RanBP2-type|||TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000225696 http://togogenome.org/gene/10090:Card14 ^@ http://purl.uniprot.org/uniprot/Q99KF0 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ CARD|||Caspase recruitment domain-containing protein 14|||Guanylate kinase-like|||Maintains the protein in an inactive state|||PDZ|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000144089 http://togogenome.org/gene/10090:Pus1 ^@ http://purl.uniprot.org/uniprot/H7BX59|||http://purl.uniprot.org/uniprot/Q9WU56 ^@ 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|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Pseudouridine synthase I TruA alpha/beta|||Pseudouridylate synthase 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000057518|||http://purl.uniprot.org/annotation/VSP_020114|||http://purl.uniprot.org/annotation/VSP_021791|||http://purl.uniprot.org/annotation/VSP_021792 http://togogenome.org/gene/10090:Pcdh12 ^@ http://purl.uniprot.org/uniprot/O55134|||http://purl.uniprot.org/uniprot/Q8C883 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin domain-containing protein|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protocadherin-12|||Protocadherin-12, secreted form ^@ http://purl.uniprot.org/annotation/PRO_0000003997|||http://purl.uniprot.org/annotation/PRO_0000444042|||http://purl.uniprot.org/annotation/PRO_5004306217 http://togogenome.org/gene/10090:Togaram2 ^@ http://purl.uniprot.org/uniprot/Q3TYG6 ^@ 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.|||TOG array regulator of axonemal microtubules protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000325939|||http://purl.uniprot.org/annotation/VSP_032496|||http://purl.uniprot.org/annotation/VSP_032497 http://togogenome.org/gene/10090:Abhd18 ^@ http://purl.uniprot.org/uniprot/Q8C1A9 ^@ 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.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Protein ABHD18 ^@ http://purl.uniprot.org/annotation/PRO_0000301961|||http://purl.uniprot.org/annotation/VSP_027895|||http://purl.uniprot.org/annotation/VSP_027896 http://togogenome.org/gene/10090:Slc49a3 ^@ http://purl.uniprot.org/uniprot/Q8CE47 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Solute carrier family 49 member A3 ^@ http://purl.uniprot.org/annotation/PRO_0000273409 http://togogenome.org/gene/10090:Anapc4 ^@ http://purl.uniprot.org/uniprot/Q3TM92|||http://purl.uniprot.org/uniprot/Q91W96 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ Anaphase-promoting complex subunit 4|||Anaphase-promoting complex subunit 4 long|||Anaphase-promoting complex subunit 4-like WD40|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000064596 http://togogenome.org/gene/10090:Scrt1 ^@ http://purl.uniprot.org/uniprot/Q99M85 ^@ 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 1 ^@ http://purl.uniprot.org/annotation/PRO_0000047037 http://togogenome.org/gene/10090:Oog1 ^@ http://purl.uniprot.org/uniprot/E9Q5G7 ^@ 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|||Oogenesin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000437074 http://togogenome.org/gene/10090:Galnt1 ^@ http://purl.uniprot.org/uniprot/O08912|||http://purl.uniprot.org/uniprot/Q3UFE4 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Induces a decrease in activity.|||Induces a slight decrease in activity.|||Induces a strong decrease in activity.|||Little or no effect.|||Little or no effect. Induces a slight decrease in activity; when associated with A-465.|||Little or no effect. Induces a slight decrease in activity; when associated with A-466.|||Loss of enzyme activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect.|||No effect; specificity not affected.|||Polypeptide N-acetylgalactosaminyltransferase 1|||Polypeptide N-acetylgalactosaminyltransferase 1 soluble form|||Ricin B lectin|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000012259|||http://purl.uniprot.org/annotation/PRO_0000223388 http://togogenome.org/gene/10090:Chdh ^@ http://purl.uniprot.org/uniprot/Q8BJ64 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Choline dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000012330 http://togogenome.org/gene/10090:Slc25a30 ^@ http://purl.uniprot.org/uniprot/Q9CR58 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Kidney mitochondrial carrier protein 1|||N-acetylserine|||Removed|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000288918 http://togogenome.org/gene/10090:Derl1 ^@ http://purl.uniprot.org/uniprot/Q99J56 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Derlin-1|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Lumenal|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||SHP-box ^@ http://purl.uniprot.org/annotation/PRO_0000219043 http://togogenome.org/gene/10090:Or4c110 ^@ http://purl.uniprot.org/uniprot/A3KGY3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ttpal ^@ http://purl.uniprot.org/uniprot/Q9D3D0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Alpha-tocopherol transfer protein-like|||CRAL-TRIO|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000210773|||http://purl.uniprot.org/annotation/VSP_006032|||http://purl.uniprot.org/annotation/VSP_006033 http://togogenome.org/gene/10090:Gm45935 ^@ http://purl.uniprot.org/uniprot/B4XVP7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||MBD|||PHD-type|||Polar residues|||Pre-SET|||SET ^@ http://togogenome.org/gene/10090:Samd11 ^@ http://purl.uniprot.org/uniprot/J3QN61|||http://purl.uniprot.org/uniprot/Q1RNF8 ^@ 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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SAM|||Sterile alpha motif domain-containing protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000279501 http://togogenome.org/gene/10090:Oip5 ^@ http://purl.uniprot.org/uniprot/A2AQ14 ^@ 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 ^@ Mis18|||Phosphoserine|||Phosphothreonine|||Protein Mis18-beta ^@ http://purl.uniprot.org/annotation/PRO_0000359883 http://togogenome.org/gene/10090:Bace1 ^@ http://purl.uniprot.org/uniprot/P56818|||http://purl.uniprot.org/uniprot/Q8C4F4 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Beta-secretase 1|||Completely abolishes S-palmitoylation; when associated with A-478; A-482 and A-485. Doesn't affect trans-Golgi network and endosome localization; when associated with A-478; A-482 and A-485. Reduces membrane raft association; when associated with A-478; A-482 and A-485. Doesn't affect APP processing; when associated with A-478; A-482 and A-485.|||Cytoplasmic|||DXXLL|||Decreases bisecting N-acetylglucosamine levels. Almost abolishes bisecting N-acetylglucosamine levels but has no effect on surface expression; when associated with S-153.|||Decreases bisecting N-acetylglucosamine levels. Almost abolishes bisecting N-acetylglucosamine levels but has no effect on surface expression; when associated with S-223.|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Interaction with RTN3|||Loss of catalytic activity.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Peptidase A1|||Phosphoserine|||S-palmitoyl cysteine|||Significantly reduces S-palmitoylation; when associated with A-478 and A-482. Completely abolishes S-palmitoylation; when associated with A-474; A-478 and A-482. Doesn't affect trans-Golgi network and endosome localization; when associated with A-474; A-478 and A-482. Reduces membrane raft association; when associated with A-474; A-478 and A-482. Doesn't affect APP processing; when associated with A-474; A-478 and A-482.|||Significantly reduces S-palmitoylation; when associated with A-478 and A-485. Completely abolishes S-palmitoylation; when associated with A-474; A-478 and A-485. Doesn't affect trans-Golgi network and endosome localization; when associated with A-474; A-478 and A-485. Reduces membrane raft association; when associated with A-474; A-478 and A-485. Doesn't affect APP processing; when associated with A-474; A-478 and A-485.|||Significantly reduces S-palmitoylation; when associated with A-482 and A-485. Completely abolishes S-palmitoylation; when associated with A-474; A-482 and A-485. Doesn't affect trans-Golgi network and endosome localization; when associated with A-474; A-482 and A-485. Reduces membrane raft association; when associated with A-474; A-482 and A-485. Doesn't affect APP processing; when associated with A-474; A-482 and A-485.|||Slightly decreases bisecting N-acetylglucosamine levels. ^@ http://purl.uniprot.org/annotation/PRO_0000025941|||http://purl.uniprot.org/annotation/PRO_0000025942|||http://purl.uniprot.org/annotation/PRO_5015099023 http://togogenome.org/gene/10090:Pts ^@ http://purl.uniprot.org/uniprot/Q9R1Z7 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ 6-pyruvoyl tetrahydrobiopterin synthase|||Charge relay system|||Phosphoserine|||Phosphotyrosine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000057915 http://togogenome.org/gene/10090:Ccdc25 ^@ http://purl.uniprot.org/uniprot/A0PK78|||http://purl.uniprot.org/uniprot/Q78PG9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 25|||Cytoplasmic|||DNA-binding|||Disordered|||Extracellular|||Helical|||N6-acetyllysine|||NFACT RNA-binding|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000233405 http://togogenome.org/gene/10090:Uevld ^@ http://purl.uniprot.org/uniprot/Q3U1V6 ^@ 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 ^@ In isoform 2.|||UEV|||Ubiquitin-conjugating enzyme E2 variant 3 ^@ http://purl.uniprot.org/annotation/PRO_0000278652|||http://purl.uniprot.org/annotation/VSP_023352|||http://purl.uniprot.org/annotation/VSP_023353 http://togogenome.org/gene/10090:Rrp9 ^@ http://purl.uniprot.org/uniprot/Q91WM3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000051314 http://togogenome.org/gene/10090:Wdr54 ^@ http://purl.uniprot.org/uniprot/Q9R0D8 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ WD 1|||WD 2|||WD 3|||WD 4|||WD repeat-containing protein 54 ^@ http://purl.uniprot.org/annotation/PRO_0000051416 http://togogenome.org/gene/10090:Ctdspl2 ^@ http://purl.uniprot.org/uniprot/Q8BG15 ^@ 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|||CTD small phosphatase-like protein 2|||Disordered|||FCP1 homology|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000331465|||http://purl.uniprot.org/annotation/VSP_033219|||http://purl.uniprot.org/annotation/VSP_033220|||http://purl.uniprot.org/annotation/VSP_033221|||http://purl.uniprot.org/annotation/VSP_033222|||http://purl.uniprot.org/annotation/VSP_033223|||http://purl.uniprot.org/annotation/VSP_033224 http://togogenome.org/gene/10090:Cyp3a11 ^@ http://purl.uniprot.org/uniprot/Q3UEN8|||http://purl.uniprot.org/uniprot/Q64459 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Cytochrome P450 3A11|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051794 http://togogenome.org/gene/10090:Jade3 ^@ http://purl.uniprot.org/uniprot/A0A140T8R5|||http://purl.uniprot.org/uniprot/Q6IE82 ^@ 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|||C2HC pre-PHD-type|||Disordered|||N6-acetyllysine|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues|||Protein Jade-3 ^@ http://purl.uniprot.org/annotation/PRO_0000253534 http://togogenome.org/gene/10090:Agrn ^@ http://purl.uniprot.org/uniprot/M0QWP1 ^@ 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 ^@ Agrin|||Disordered|||EGF-like|||Kazal-like|||Laminin EGF-like|||Laminin G|||NtA|||Polar residues|||SEA ^@ http://purl.uniprot.org/annotation/PRO_5004005268 http://togogenome.org/gene/10090:Uba7 ^@ http://purl.uniprot.org/uniprot/Q9DBK7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ubiquitin-activating enzyme E1 C-terminal ^@ http://togogenome.org/gene/10090:Cdc16 ^@ http://purl.uniprot.org/uniprot/Q3TI84|||http://purl.uniprot.org/uniprot/Q8R349 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Cell division cycle protein 16 homolog|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||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_0000106268 http://togogenome.org/gene/10090:Mmp19 ^@ http://purl.uniprot.org/uniprot/Q2KHP2|||http://purl.uniprot.org/uniprot/Q3UW97|||http://purl.uniprot.org/uniprot/Q9JHI0 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Motif|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Cysteine switch|||Disordered|||GPI-anchor amidated aspartate|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Matrix metalloproteinase-19|||N-linked (GlcNAc...) asparagine|||Peptidase metallopeptidase|||Removed in mature form|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028828|||http://purl.uniprot.org/annotation/PRO_0000028829|||http://purl.uniprot.org/annotation/PRO_0000028830|||http://purl.uniprot.org/annotation/PRO_5014308660 http://togogenome.org/gene/10090:Spag8 ^@ http://purl.uniprot.org/uniprot/Q3V0Q6 ^@ 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|||Sperm-associated antigen 8 ^@ http://purl.uniprot.org/annotation/PRO_0000436205|||http://purl.uniprot.org/annotation/VSP_058322|||http://purl.uniprot.org/annotation/VSP_058323 http://togogenome.org/gene/10090:Polr3d ^@ http://purl.uniprot.org/uniprot/Q91WD1 ^@ 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|||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_0000073968 http://togogenome.org/gene/10090:Pygb ^@ http://purl.uniprot.org/uniprot/Q8CI94 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Site ^@ 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|||Phosphoserine; by PHK; in form phosphorylase A|||Phosphotyrosine|||Pyridoxal 5'-phosphate|||Removed|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000188536 http://togogenome.org/gene/10090:Lsm2 ^@ http://purl.uniprot.org/uniprot/G3UZ96|||http://purl.uniprot.org/uniprot/O35900|||http://purl.uniprot.org/uniprot/O35901|||http://purl.uniprot.org/uniprot/Q3U9X2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Phosphothreonine|||Sm|||U6 snRNA-associated Sm-like protein LSm2 ^@ http://purl.uniprot.org/annotation/PRO_0000125557 http://togogenome.org/gene/10090:Or5h19 ^@ http://purl.uniprot.org/uniprot/E9QNM5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Baiap3 ^@ http://purl.uniprot.org/uniprot/Q80TT2 ^@ 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 ^@ BAI1-associated protein 3|||C2 1|||C2 2|||Disordered|||In isoform 1.|||MHD1|||MHD2 ^@ http://purl.uniprot.org/annotation/PRO_0000064820|||http://purl.uniprot.org/annotation/VSP_061750 http://togogenome.org/gene/10090:Tex37 ^@ http://purl.uniprot.org/uniprot/Q9DAG4 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||Protein SPMIP9 ^@ http://purl.uniprot.org/annotation/PRO_0000304990|||http://purl.uniprot.org/annotation/VSP_028172 http://togogenome.org/gene/10090:Rbms3 ^@ http://purl.uniprot.org/uniprot/Q8BWL5 ^@ 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 4.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 6.|||In isoform 5.|||RNA-binding motif, single-stranded-interacting protein 3|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000274907|||http://purl.uniprot.org/annotation/VSP_022932|||http://purl.uniprot.org/annotation/VSP_022933|||http://purl.uniprot.org/annotation/VSP_022934|||http://purl.uniprot.org/annotation/VSP_022935 http://togogenome.org/gene/10090:Zfp689 ^@ http://purl.uniprot.org/uniprot/Q8BKK5 ^@ 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 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_0000234009 http://togogenome.org/gene/10090:Nubpl ^@ http://purl.uniprot.org/uniprot/Q9CWD8 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Sequence Conflict|||Transit Peptide ^@ Iron-sulfur protein NUBPL|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000184951 http://togogenome.org/gene/10090:Zfp870 ^@ http://purl.uniprot.org/uniprot/Q6NZJ3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Cct3 ^@ http://purl.uniprot.org/uniprot/P80318|||http://purl.uniprot.org/uniprot/Q3U4U6 ^@ Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||Disulfide Bond|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||T-complex protein 1 subunit gamma ^@ http://purl.uniprot.org/annotation/PRO_0000128322 http://togogenome.org/gene/10090:Igsf10 ^@ http://purl.uniprot.org/uniprot/Q3V1M1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ 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|||Immunoglobulin superfamily member 10|||LRR 1|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000286818 http://togogenome.org/gene/10090:Agbl5 ^@ http://purl.uniprot.org/uniprot/Q09M02 ^@ 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 ^@ Abolishes deglutamylase activity; when associated with Q-255.|||Abolishes deglutamylase activity; when associated with S-252.|||Basic and acidic residues|||Cytosolic carboxypeptidase-like protein 5|||Disordered|||In isoform 2 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 7.|||In isoform 5.|||In isoform 6.|||Nucleophile|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000305922|||http://purl.uniprot.org/annotation/VSP_040427|||http://purl.uniprot.org/annotation/VSP_040428|||http://purl.uniprot.org/annotation/VSP_040429|||http://purl.uniprot.org/annotation/VSP_040430|||http://purl.uniprot.org/annotation/VSP_040431|||http://purl.uniprot.org/annotation/VSP_040432|||http://purl.uniprot.org/annotation/VSP_040433|||http://purl.uniprot.org/annotation/VSP_040434 http://togogenome.org/gene/10090:Vmn1r233 ^@ http://purl.uniprot.org/uniprot/Q8R294 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Exog ^@ http://purl.uniprot.org/uniprot/Q8C163 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||Nuclease EXOG, mitochondrial|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000342610 http://togogenome.org/gene/10090:Rec8 ^@ http://purl.uniprot.org/uniprot/Q8C5S7 ^@ 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|||Meiotic recombination protein REC8 homolog|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000097879 http://togogenome.org/gene/10090:Cela1 ^@ http://purl.uniprot.org/uniprot/Q91X79 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Chymotrypsin-like elastase family member 1|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000416103|||http://purl.uniprot.org/annotation/PRO_0000416104 http://togogenome.org/gene/10090:Vmn1r80 ^@ http://purl.uniprot.org/uniprot/L7N1Z3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mcm3 ^@ http://purl.uniprot.org/uniprot/P25206|||http://purl.uniprot.org/uniprot/Q3UI57 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Arginine finger|||Basic and acidic residues|||DNA replication licensing factor MCM3|||Disordered|||MCM|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194094 http://togogenome.org/gene/10090:Chst1 ^@ http://purl.uniprot.org/uniprot/Q3UY35|||http://purl.uniprot.org/uniprot/Q9EQC0 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 1|||Cell attachment site|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Sulfotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000085183|||http://purl.uniprot.org/annotation/PRO_5014309252 http://togogenome.org/gene/10090:2010315B03Rik ^@ http://purl.uniprot.org/uniprot/J3QK55|||http://purl.uniprot.org/uniprot/Q05C34 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Sepsecs ^@ http://purl.uniprot.org/uniprot/Q6P6M7 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ 30% of wild-type activity.|||50% of wild-type 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|||Tetramerization|||Virtually inactive. ^@ http://purl.uniprot.org/annotation/PRO_0000219876 http://togogenome.org/gene/10090:Or7d11 ^@ http://purl.uniprot.org/uniprot/Q7TRF3 ^@ 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 7D11 ^@ http://purl.uniprot.org/annotation/PRO_0000280220 http://togogenome.org/gene/10090:Zfp672 ^@ http://purl.uniprot.org/uniprot/Q99LH4 ^@ 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_0000233992 http://togogenome.org/gene/10090:Cwc25 ^@ http://purl.uniprot.org/uniprot/Q9DBF7 ^@ 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.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pre-mRNA-splicing factor CWC25 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000288866|||http://purl.uniprot.org/annotation/VSP_025798|||http://purl.uniprot.org/annotation/VSP_025799 http://togogenome.org/gene/10090:Ier3 ^@ http://purl.uniprot.org/uniprot/P46694 ^@ 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; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Radiation-inducible immediate-early gene IEX-1 ^@ http://purl.uniprot.org/annotation/PRO_0000084160 http://togogenome.org/gene/10090:Sephs2 ^@ http://purl.uniprot.org/uniprot/P97364 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non standard residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Non standard residue|||Region|||Site ^@ Disordered|||Important for catalytic activity|||N-acetylalanine|||Phosphoserine|||Removed|||Selenide, water dikinase 2|||Selenocysteine|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000127651 http://togogenome.org/gene/10090:Dcdc2a ^@ http://purl.uniprot.org/uniprot/Q5DU00|||http://purl.uniprot.org/uniprot/R4GML1 ^@ 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|||Doublecortin|||Doublecortin 1|||Doublecortin 2|||Doublecortin domain-containing protein 2|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079805|||http://purl.uniprot.org/annotation/VSP_014672|||http://purl.uniprot.org/annotation/VSP_014673 http://togogenome.org/gene/10090:Nuggc ^@ http://purl.uniprot.org/uniprot/D3YWJ0|||http://purl.uniprot.org/uniprot/D3YY21 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent ^@ Dynamin N-terminal|||Nuclear GTPase SLIP-GC ^@ http://purl.uniprot.org/annotation/PRO_0000436145 http://togogenome.org/gene/10090:Ano2 ^@ http://purl.uniprot.org/uniprot/Q8CFW1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Anoctamin-2|||Basic and acidic residues|||Cytoplasmic|||DLG4 binding (PDZ)|||Disordered|||Extracellular|||Helical|||Impaired interaction with DLG4.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000353187 http://togogenome.org/gene/10090:Ift70b ^@ http://purl.uniprot.org/uniprot/Q9CY00 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Repeat|||Sequence Conflict ^@ 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_0000333204 http://togogenome.org/gene/10090:Alox5 ^@ http://purl.uniprot.org/uniprot/P48999 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Decreases (5S)-lipoxygenase activity. Forms 9-hydroperoxyicosatetraenoic acid (9-HPETE) as the major arachidonic acid oxygenation product. Loss of arachidonate (5S)-lipoxygenase activity; when associated with W-360; I-425 and M-426. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with W-360; I-425 and M-426.|||Decreases arachidonate (5S)-lipoxygenase activity.|||Decreases arachidonate (5S)-lipoxygenase activity. Decreases arachidonate 5 lipoxygenase activity; when associated with A-604. Exhibits a (8S)-lipoxygenase activity; when associated with W-360. Exhibits a (15S)-lipoxygenase activity; when associated with W-360 and M-426. Loss of arachidonate (5S)-lipoxygenase activity; when associated with W-360; G-411 and M-426. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with W-360; G-411 and M-426. Does not oxygenate arachidonic acid into 5-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of arachidonic acid into a major product (15S)-HETE followed by 12-HETE and 8-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of linoleic acid, gamma-linolenic acid, arachidonic acid, eicosapentaenoic acid and docosahexaenoic acid; when associated with I-425 and M-426. Catalyzes oxygenation of anandamide to 15-OH-ANA. Knockin mice are viable, fertile, and develop normally; when associated with I-425 and M-426. Mice convert arachidonic to 15-HETE, 12-HETE, and 8-HETE; when associated with I-425 and M-426. Mice cannot synthesize pro-inflammatory leukotrienes but show significantly attenuated plasma levels of lipolytic endocannabinoids; when associated with I-425 and M-426. When aging, animals gain significantly more body weight probably due to higher levels of 13-HODE in the adipose tissue; when associated with I-425 and M-426.|||Essential for stabilizing binding to COTL1|||Increases formation of (8S)-hydroperoxyicosatetraenoic acid ((8S)-HPETE) and (12S)-hydroperoxyicosatetraenoic acid ((12S)-HPETE). Exhibits a (15S)-lipoxygenase activity; when associated with W-360 and I-425. Loss of arachidonate (5S)-lipoxygenase activity; when associated with W-360; G-411 and I-425. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with W-360; G-411 and I-425.|||Increases formation of (8S)-hydroperoxyicosatetraenoic acid ((8S)-HPETE). Exhibits a (8S)-lipoxygenase activity; when associated with I-425. Exhibits a (15S)-lipoxygenase activity; when associated with I-425 and M-426. Loss of arachidonate (5S)-lipoxygenase activity; when associated with G-411; I-425 and M-426. Forms 11(R)-hydroperoxyicosatetraenoic acid (11(R)-HPETE) as the major arachidonic acid oxygenation product; when associated with G-411; I-425 and M-426. Does not oxygenate arachidonic acid into 5-HETE; when associated with I-425 and M-426. Catalyzes oxygenation of arachidonic acid into a major product (15S)-HETE followed by 12-HETE and 8-HETE;when associated with I-425 and M-426. Catalyzes oxygenation of linoleic acid, gamma-linolenic acid, arachidonic acid, eicosapentaenoic acid and docosahexaenoic acid; when associated with I-425 and M-426. Catalyzes oxygenation of anandamide to 15-OH-ANA. Knockin mice are viable, fertile, and develop normally; when associated with I-425 and M-426. Mice convert arachidonic to 15-HETE, 12-HETE, and 8-HETE; when associated with I-425 and M-426. Mice cannot synthesize pro-inflammatory leukotrienes but show significantly attenuated plasma levels of lipolytic endocannabinoids; when associated with I-425 and M-426. When aging, animals gain significantly more body weight probably due to higher levels of 13-HODE in the adipose tissue; when associated with I-425 and M-426.|||Lipoxygenase|||Loss of activity.|||PLAT|||Phosphoserine|||Polyunsaturated fatty acid 5-lipoxygenase ^@ http://purl.uniprot.org/annotation/PRO_0000220695 http://togogenome.org/gene/10090:Vps37c ^@ http://purl.uniprot.org/uniprot/Q8R105 ^@ 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.|||Phosphoserine|||Pro residues|||VPS37 C-terminal|||Vacuolar protein sorting-associated protein 37C ^@ http://purl.uniprot.org/annotation/PRO_0000312199|||http://purl.uniprot.org/annotation/VSP_029730 http://togogenome.org/gene/10090:Dld ^@ http://purl.uniprot.org/uniprot/O08749 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ Dihydrolipoyl dehydrogenase, mitochondrial|||Important for interaction with PDHX and activity of pyruvate dehydrogenase complex|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Proton acceptor|||Redox-active ^@ http://purl.uniprot.org/annotation/PRO_0000030297 http://togogenome.org/gene/10090:Adcy5 ^@ http://purl.uniprot.org/uniprot/P84309 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Adenylate cyclase type 5|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Guanylate cyclase 1|||Guanylate cyclase 2|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000195695|||http://purl.uniprot.org/annotation/VSP_022224 http://togogenome.org/gene/10090:Mbd6 ^@ http://purl.uniprot.org/uniprot/E9Q572|||http://purl.uniprot.org/uniprot/Q3TY92|||http://purl.uniprot.org/uniprot/Q4VBD6|||http://purl.uniprot.org/uniprot/Q5XJH3 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Disordered|||MBD|||Methyl-CpG-binding domain protein 6|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000406941 http://togogenome.org/gene/10090:Tomm40l ^@ http://purl.uniprot.org/uniprot/Q9CZR3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Mitochondrial import receptor subunit TOM40B|||Required for mitochondrial targeting ^@ http://purl.uniprot.org/annotation/PRO_0000051537 http://togogenome.org/gene/10090:Fcnb ^@ http://purl.uniprot.org/uniprot/O70497 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide ^@ Collagen-like|||Disordered|||Fibrinogen C-terminal|||Ficolin-2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009140 http://togogenome.org/gene/10090:Spns1 ^@ http://purl.uniprot.org/uniprot/Q8R0G7 ^@ 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|||Phosphoserine|||Protein spinster homolog 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000305040 http://togogenome.org/gene/10090:Klf5 ^@ http://purl.uniprot.org/uniprot/Q9Z0Z7 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ 9aaTAD|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with WWP1|||Krueppel-like factor 5 ^@ http://purl.uniprot.org/annotation/PRO_0000047170 http://togogenome.org/gene/10090:Btg4 ^@ http://purl.uniprot.org/uniprot/O70552 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict ^@ Chain|||Mutagenesis Site|||Sequence Conflict ^@ Loss of interaction with CNOT7 and CNOT8. No effect on interaction with EIF4E.|||Loss of interaction with CNOT7.|||No effect on interaction with CNOT7.|||Protein BTG4 ^@ http://purl.uniprot.org/annotation/PRO_0000143811 http://togogenome.org/gene/10090:Tcl1b5 ^@ http://purl.uniprot.org/uniprot/P56845 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein TCL1B5 ^@ http://purl.uniprot.org/annotation/PRO_0000184495 http://togogenome.org/gene/10090:Rap2c ^@ http://purl.uniprot.org/uniprot/Q8BU31 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Conflict ^@ Cysteine methyl ester|||Effector region|||Loss of association with membranes.|||Loss of association with the recycling endosome membranes and loss of TNIK activation; when associated with C-176.|||Loss of association with the recycling endosome membranes and loss of TNIK activation; when associated with C-177.|||Ras-related protein Rap-2c|||Removed in mature form|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000030223|||http://purl.uniprot.org/annotation/PRO_0000030224 http://togogenome.org/gene/10090:Ola1 ^@ http://purl.uniprot.org/uniprot/Q9CZ30 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||N6-acetyllysine|||Nuclear export signal|||OBG-type G|||Obg-like ATPase 1|||TGS ^@ http://purl.uniprot.org/annotation/PRO_0000122457|||http://purl.uniprot.org/annotation/VSP_002054|||http://purl.uniprot.org/annotation/VSP_002055 http://togogenome.org/gene/10090:Ttc1 ^@ http://purl.uniprot.org/uniprot/Q91Z38 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000106377 http://togogenome.org/gene/10090:Fsip1 ^@ http://purl.uniprot.org/uniprot/Q9D3V5 ^@ 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|||Fibrous sheath-interacting protein 1|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314920|||http://purl.uniprot.org/annotation/VSP_030430|||http://purl.uniprot.org/annotation/VSP_030431 http://togogenome.org/gene/10090:Lrrc17 ^@ http://purl.uniprot.org/uniprot/Q9CXD9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Repeat|||Signal Peptide ^@ Disordered|||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_0000021609 http://togogenome.org/gene/10090:Trp53i11 ^@ http://purl.uniprot.org/uniprot/Q4QQM4 ^@ 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_0000395041 http://togogenome.org/gene/10090:Cep85l ^@ http://purl.uniprot.org/uniprot/A0A1W2P884|||http://purl.uniprot.org/uniprot/E9QA61|||http://purl.uniprot.org/uniprot/Q3V3K0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region ^@ Centrosomal protein of 85 kDa-like|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000452321 http://togogenome.org/gene/10090:Scgb3a2 ^@ http://purl.uniprot.org/uniprot/Q920H1 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Mutagenesis Site|||Signal Peptide|||Splice Variant ^@ Fails to homodimerize.|||In isoform B.|||In isoform C.|||Interchain|||Secretoglobin family 3A member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000036382|||http://purl.uniprot.org/annotation/VSP_059182|||http://purl.uniprot.org/annotation/VSP_059183 http://togogenome.org/gene/10090:Sec61b ^@ http://purl.uniprot.org/uniprot/Q9CQS8 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||N-acetylproline|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein transport protein Sec61 subunit beta|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000157255 http://togogenome.org/gene/10090:Gm5799 ^@ http://purl.uniprot.org/uniprot/E9Q2M1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:T ^@ http://purl.uniprot.org/uniprot/P20293|||http://purl.uniprot.org/uniprot/Q78ZW9 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent ^@ T-box|||T-box transcription factor T ^@ http://purl.uniprot.org/annotation/PRO_0000184415 http://togogenome.org/gene/10090:Plgrkt ^@ http://purl.uniprot.org/uniprot/Q9D3P8 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disrupts binding to plasminogen.|||Extracellular|||Helical|||Plasminogen receptor (KT) ^@ http://purl.uniprot.org/annotation/PRO_0000089696 http://togogenome.org/gene/10090:Or4q3 ^@ http://purl.uniprot.org/uniprot/Q7TRM4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cysrt1 ^@ http://purl.uniprot.org/uniprot/Q9D1E4 ^@ 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_0000332288 http://togogenome.org/gene/10090:Pias2 ^@ http://purl.uniprot.org/uniprot/F8WHS8|||http://purl.uniprot.org/uniprot/G3UWE3|||http://purl.uniprot.org/uniprot/Q3V3U5|||http://purl.uniprot.org/uniprot/Q8C5D8 ^@ 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|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||E3 SUMO-protein ligase PIAS2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4.|||LXXLL motif|||Nuclear localization signal|||PINIT|||Phosphoserine|||Polar residues|||SAP|||SP-RING-type|||SUMO1-binding ^@ http://purl.uniprot.org/annotation/PRO_0000218977|||http://purl.uniprot.org/annotation/VSP_012198|||http://purl.uniprot.org/annotation/VSP_012199|||http://purl.uniprot.org/annotation/VSP_012200|||http://purl.uniprot.org/annotation/VSP_012201|||http://purl.uniprot.org/annotation/VSP_012202 http://togogenome.org/gene/10090:Exd2 ^@ http://purl.uniprot.org/uniprot/Q8VEG4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 3'-5' exonuclease|||Cytoplasmic|||Disordered|||Exonuclease 3'-5' domain-containing protein 2|||Helical|||In isoform 2.|||Mitochondrial intermembrane|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000089925|||http://purl.uniprot.org/annotation/VSP_058326 http://togogenome.org/gene/10090:Tmc5 ^@ http://purl.uniprot.org/uniprot/Q32NZ6 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Polar residues|||Transmembrane channel-like protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000289967|||http://purl.uniprot.org/annotation/VSP_026047|||http://purl.uniprot.org/annotation/VSP_026048 http://togogenome.org/gene/10090:Cyren ^@ http://purl.uniprot.org/uniprot/Q8BHZ5 ^@ 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|||Cell cycle regulator of non-homologous end joining|||Disordered|||In isoform 2.|||KBM|||N-acetylmethionine|||Polar residues|||XLM ^@ http://purl.uniprot.org/annotation/PRO_0000320949|||http://purl.uniprot.org/annotation/VSP_031769 http://togogenome.org/gene/10090:Zbtb18 ^@ http://purl.uniprot.org/uniprot/H7BX69|||http://purl.uniprot.org/uniprot/Q9WUK6 ^@ 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|||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)|||Interaction with DNMT3A|||Phosphoserine|||Zinc finger and BTB domain-containing protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000047478 http://togogenome.org/gene/10090:Chchd10 ^@ http://purl.uniprot.org/uniprot/Q7TNL9 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Fzd8 ^@ http://purl.uniprot.org/uniprot/Q61091 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||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|||Reduces interaction with GOPC.|||Wnt-binding ^@ http://purl.uniprot.org/annotation/PRO_0000013001 http://togogenome.org/gene/10090:Plekha4 ^@ http://purl.uniprot.org/uniprot/D3Z3Y7 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PH|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Or52z1 ^@ http://purl.uniprot.org/uniprot/F8VPJ8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ins1 ^@ http://purl.uniprot.org/uniprot/P01325 ^@ Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ C peptide|||Insulin-1 A chain|||Insulin-1 B chain|||Interchain (between B and A chains) ^@ http://purl.uniprot.org/annotation/PRO_0000015842|||http://purl.uniprot.org/annotation/PRO_0000015843|||http://purl.uniprot.org/annotation/PRO_0000015844 http://togogenome.org/gene/10090:Or51h5 ^@ http://purl.uniprot.org/uniprot/Q8VGZ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tlx1 ^@ http://purl.uniprot.org/uniprot/Q9QX99 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Eif2b4 ^@ http://purl.uniprot.org/uniprot/Q61749 ^@ 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.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||Translation initiation factor eIF-2B subunit delta ^@ http://purl.uniprot.org/annotation/PRO_0000156068|||http://purl.uniprot.org/annotation/VSP_001434 http://togogenome.org/gene/10090:Plekho2 ^@ http://purl.uniprot.org/uniprot/Q8K124 ^@ 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 ^@ Disordered|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology domain-containing family O member 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000309484 http://togogenome.org/gene/10090:Lrch2 ^@ http://purl.uniprot.org/uniprot/Q3UMG5 ^@ 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|||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 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000253483|||http://purl.uniprot.org/annotation/VSP_021041|||http://purl.uniprot.org/annotation/VSP_021042 http://togogenome.org/gene/10090:Blnk ^@ http://purl.uniprot.org/uniprot/Q9QUN3 ^@ 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 ^@ Abolishes binding to CD79A and SYK.|||Acidic residues|||B-cell linker protein|||Disordered|||Fails to induce pre-BCR down-regulation, leading to splenomegaly and leukemia.|||No effect on pre-BCR down-regulation.|||Phosphotyrosine; by SYK|||Polar residues|||SH2 ^@ http://purl.uniprot.org/annotation/PRO_0000064941 http://togogenome.org/gene/10090:Mthfd1l ^@ http://purl.uniprot.org/uniprot/Q3V3R1 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Disordered|||Formyltetrahydrofolate synthetase|||Methylenetetrahydrofolate dehydrogenase and cyclohydrolase|||Mitochondrion|||Monofunctional C1-tetrahydrofolate synthase, mitochondrial|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000343178 http://togogenome.org/gene/10090:Uhmk1 ^@ http://purl.uniprot.org/uniprot/D3YUF5|||http://purl.uniprot.org/uniprot/P97343 ^@ 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|||RRM|||Serine/threonine-protein kinase Kist ^@ http://purl.uniprot.org/annotation/PRO_0000086778 http://togogenome.org/gene/10090:Shisa7 ^@ http://purl.uniprot.org/uniprot/Q8C3Q5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes the colocalization with GPHN.|||Cytoplasmic|||Disordered|||Extracellular|||GRID|||Helical|||In isoform 2.|||Loss of interaction with PDZ-domain of DLG4.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein shisa-7 ^@ http://purl.uniprot.org/annotation/PRO_0000344473|||http://purl.uniprot.org/annotation/VSP_034790 http://togogenome.org/gene/10090:Tm4sf19 ^@ http://purl.uniprot.org/uniprot/B2RWD4|||http://purl.uniprot.org/uniprot/E9Q9H8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Wdr25 ^@ http://purl.uniprot.org/uniprot/E9Q349 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Splice Variant ^@ Disordered|||In isoform 2.|||Polar residues|||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_0000415827|||http://purl.uniprot.org/annotation/VSP_042397|||http://purl.uniprot.org/annotation/VSP_042398 http://togogenome.org/gene/10090:Acadvl ^@ http://purl.uniprot.org/uniprot/P50544 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Catalytic|||Disordered|||Membrane-anchoring|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Polar residues|||Proton acceptor|||S-nitrosocysteine|||Very long-chain specific acyl-CoA dehydrogenase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000000517 http://togogenome.org/gene/10090:Deptor ^@ http://purl.uniprot.org/uniprot/B2ZRS3|||http://purl.uniprot.org/uniprot/B2ZRS7|||http://purl.uniprot.org/uniprot/Q570Y9 ^@ 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 ^@ BetaTrCP degron motif|||DDEX motif|||DEP|||DEP 1|||DEP 2|||DEP domain-containing mTOR-interacting protein|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||PDZ|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284785|||http://purl.uniprot.org/annotation/VSP_024648|||http://purl.uniprot.org/annotation/VSP_024649 http://togogenome.org/gene/10090:Sptssb ^@ http://purl.uniprot.org/uniprot/Q925E8 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Mutant mice develop early onset ataxia, exhibit reduced body weight and usually die around 10 weeks after birth. Increases SPT affininity toward C18-CoA substrate by twofold and elevates C20 long chain base production in the brain and eye. Produces neurodegenerative effects such as aberrant membrane strucutres, accumulation of ubiquitinated protein on membranes and axon degeneration.|||Serine palmitoyltransferase small subunit B ^@ http://purl.uniprot.org/annotation/PRO_0000239720 http://togogenome.org/gene/10090:Glb1l2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0L1|||http://purl.uniprot.org/uniprot/E0CYE1|||http://purl.uniprot.org/uniprot/Q3UPY5|||http://purl.uniprot.org/uniprot/Q8BZW3 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Beta-galactosidase-1-like protein 2|||Glycoside hydrolase 35 catalytic|||In isoform 2.|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000317514|||http://purl.uniprot.org/annotation/VSP_031000 http://togogenome.org/gene/10090:Rassf5 ^@ http://purl.uniprot.org/uniprot/D3Z6G2|||http://purl.uniprot.org/uniprot/Q5EBH1 ^@ 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|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Pro residues|||Ras association domain-containing protein 5|||Ras-associating|||Reduced interaction with HRAS.|||Reduced specificity for HRAS and diminished discrimination between HRAS and RAP1A.|||SARAH|||Strongly reduced interaction with HRAS.|||Very strong reduction of the interaction with HRAS. ^@ http://purl.uniprot.org/annotation/PRO_0000240402|||http://purl.uniprot.org/annotation/VSP_019368|||http://purl.uniprot.org/annotation/VSP_019369 http://togogenome.org/gene/10090:Mrps7 ^@ http://purl.uniprot.org/uniprot/Q80X85 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||N6-acetyllysine|||Small ribosomal subunit protein uS7m ^@ http://purl.uniprot.org/annotation/PRO_0000273057 http://togogenome.org/gene/10090:Actl9 ^@ http://purl.uniprot.org/uniprot/Q8CG27 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Actin-like protein 9|||Disordered|||Homozygous knockin male mice are infertile. Testis size, sperm concentration, viability and motility are normal. However the acrosome is detached from the nuclear envelope in sperm. Proacrosomal vesicles in the Golgi phase are atypical and separated in testis and they failed to fuse in the cap phase. ^@ http://purl.uniprot.org/annotation/PRO_0000332298 http://togogenome.org/gene/10090:Gpr85 ^@ http://purl.uniprot.org/uniprot/P60894|||http://purl.uniprot.org/uniprot/Q6ZWR2 ^@ 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 85 ^@ http://purl.uniprot.org/annotation/PRO_0000069592 http://togogenome.org/gene/10090:Vmn1r188 ^@ http://purl.uniprot.org/uniprot/Q8K3N2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Speer4d ^@ http://purl.uniprot.org/uniprot/L7N216|||http://purl.uniprot.org/uniprot/Q9D3W2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Fam83g ^@ http://purl.uniprot.org/uniprot/Q5SWY7|||http://purl.uniprot.org/uniprot/Q8C1M8 ^@ 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|||Phosphoserine|||Polar residues|||Protein FAM83G|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000330818 http://togogenome.org/gene/10090:Prc1 ^@ http://purl.uniprot.org/uniprot/G3UW86|||http://purl.uniprot.org/uniprot/G3UY19|||http://purl.uniprot.org/uniprot/Q99K43 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Dimerization|||Disordered|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphothreonine; by PLK1|||Polar residues|||Protein regulator of cytokinesis 1|||Spectrin-fold|||Tubulin binding|||Unstructured, Arg/Lys rich ^@ http://purl.uniprot.org/annotation/PRO_0000229738 http://togogenome.org/gene/10090:Sctr ^@ http://purl.uniprot.org/uniprot/H7BX37|||http://purl.uniprot.org/uniprot/Q5FWI2 ^@ 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|||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_0000043222|||http://purl.uniprot.org/annotation/PRO_5003608417 http://togogenome.org/gene/10090:Or7e173 ^@ http://purl.uniprot.org/uniprot/Q8VFI7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gphb5 ^@ http://purl.uniprot.org/uniprot/B2RTN6|||http://purl.uniprot.org/uniprot/Q812B2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Glycoprotein hormone beta-5|||Glycoprotein hormone subunit beta|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000011762|||http://purl.uniprot.org/annotation/PRO_5014298340 http://togogenome.org/gene/10090:Extl3 ^@ http://purl.uniprot.org/uniprot/Q6P1H4 ^@ Coiled-Coil|||Domain Extent|||Region|||Transmembrane ^@ Coiled-Coil|||Domain Extent|||Transmembrane ^@ Exostosin GT47|||Glycosyl transferase 64|||Helical ^@ http://togogenome.org/gene/10090:Or10al7 ^@ http://purl.uniprot.org/uniprot/Q7TRI9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tnfrsf25 ^@ http://purl.uniprot.org/uniprot/B1AWN9|||http://purl.uniprot.org/uniprot/Q8VD70 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Death|||Disordered|||Helical|||TNFR-Cys ^@ http://purl.uniprot.org/annotation/PRO_5015087030|||http://purl.uniprot.org/annotation/PRO_5015099443 http://togogenome.org/gene/10090:Card9 ^@ http://purl.uniprot.org/uniprot/A2AIV8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Basic and acidic residues|||CARD|||Caspase recruitment domain-containing protein 9|||Disordered|||Does not affect phosphorylation by PKC/PRKCD.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Linker|||Phosphoserine|||Phosphothreonine; by CK2|||Phosphothreonine; by PKC/PRKCD|||Polar residues|||Reduced phosphorylation by PKC/PRKCD, leading to impaired interaction with BCL10 and decreased activation of NF-kappa-B and MAP kinase p38 pathways. ^@ http://purl.uniprot.org/annotation/PRO_0000428725 http://togogenome.org/gene/10090:Rhox3h ^@ http://purl.uniprot.org/uniprot/L7MU37 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Pole3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J091|||http://purl.uniprot.org/uniprot/Q9JKP7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||DNA polymerase epsilon subunit 3|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||Transcription factor CBF/NF-Y/archaeal histone ^@ http://purl.uniprot.org/annotation/PRO_0000208342 http://togogenome.org/gene/10090:Or5al5 ^@ http://purl.uniprot.org/uniprot/A2ARY0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dennd4b ^@ http://purl.uniprot.org/uniprot/A0A0R4J172|||http://purl.uniprot.org/uniprot/Q3U1Y4 ^@ 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 ^@ DENN domain-containing protein 4B|||Disordered|||In isoform 2.|||In isoform 3.|||MABP|||PPR|||PPR 1|||PPR 2|||Phosphoserine|||Polar residues|||Pro residues|||UDENN|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000304679|||http://purl.uniprot.org/annotation/VSP_028093|||http://purl.uniprot.org/annotation/VSP_028094|||http://purl.uniprot.org/annotation/VSP_028095|||http://purl.uniprot.org/annotation/VSP_028096|||http://purl.uniprot.org/annotation/VSP_028097 http://togogenome.org/gene/10090:Bcl7a ^@ http://purl.uniprot.org/uniprot/Q9CXE2 ^@ 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 ^@ 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_0000239824|||http://purl.uniprot.org/annotation/VSP_019272|||http://purl.uniprot.org/annotation/VSP_019273 http://togogenome.org/gene/10090:Kctd6 ^@ http://purl.uniprot.org/uniprot/A2RS47|||http://purl.uniprot.org/uniprot/Q8BNL5 ^@ 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 Mu7|||Interaction with CUL3|||Interaction with USP21 ^@ http://purl.uniprot.org/annotation/PRO_0000251249 http://togogenome.org/gene/10090:Gldc ^@ http://purl.uniprot.org/uniprot/Q91W43 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Transit Peptide ^@ Disordered|||Glycine dehydrogenase (decarboxylating), mitochondrial|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000010741 http://togogenome.org/gene/10090:Lratd1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J012|||http://purl.uniprot.org/uniprot/Q9D650 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ LRAT|||Phosphoserine|||Protein LRATD1 ^@ http://purl.uniprot.org/annotation/PRO_0000234426 http://togogenome.org/gene/10090:Glmn ^@ http://purl.uniprot.org/uniprot/Q8BZM1 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Alpha-helical region with structural similarity to HEAT repeats|||Glomulin|||Important for interaction with RBX1|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087514 http://togogenome.org/gene/10090:Clk3 ^@ http://purl.uniprot.org/uniprot/O35492 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||Dual specificity protein kinase CLK3|||Phosphoserine|||Phosphotyrosine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085871 http://togogenome.org/gene/10090:Ankrd16 ^@ http://purl.uniprot.org/uniprot/A2AS55 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant ^@ Chain|||Mutagenesis Site|||Repeat|||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 ANKRD16(3XR); abolished ability to enhance hydrolysis of Ser-mischarged tRNA(Ala); when associated with R-102 and R-135.|||In ANKRD16(3XR); abolished ability to enhance hydrolysis of Ser-mischarged tRNA(Ala); when associated with R-102 and R-165.|||In ANKRD16(3XR); abolished ability to enhance hydrolysis of Ser-mischarged tRNA(Ala); when associated with R-135 and R-165.|||In isoform 2.|||Required to capture Ser that is misactivated by AARS/AlaRS ^@ http://purl.uniprot.org/annotation/PRO_0000320068|||http://purl.uniprot.org/annotation/VSP_031593|||http://purl.uniprot.org/annotation/VSP_031594 http://togogenome.org/gene/10090:Plpp4 ^@ http://purl.uniprot.org/uniprot/Q0VBU9 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Region|||Site|||Transmembrane ^@ Disordered|||Helical|||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_0000286944 http://togogenome.org/gene/10090:Map4 ^@ http://purl.uniprot.org/uniprot/A0A0G2JDN7|||http://purl.uniprot.org/uniprot/E9PZ43|||http://purl.uniprot.org/uniprot/P27546|||http://purl.uniprot.org/uniprot/Q78TF3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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 3 and isoform 4.|||In isoform 4.|||Microtubule-associated protein 4|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Tau/MAP 1|||Tau/MAP 2|||Tau/MAP 3|||Tau/MAP 4 ^@ http://purl.uniprot.org/annotation/PRO_0000072752|||http://purl.uniprot.org/annotation/VSP_026089|||http://purl.uniprot.org/annotation/VSP_026090|||http://purl.uniprot.org/annotation/VSP_026091|||http://purl.uniprot.org/annotation/VSP_026092|||http://purl.uniprot.org/annotation/VSP_026093|||http://purl.uniprot.org/annotation/VSP_026094|||http://purl.uniprot.org/annotation/VSP_026095|||http://purl.uniprot.org/annotation/VSP_026096|||http://purl.uniprot.org/annotation/VSP_026097 http://togogenome.org/gene/10090:Or52h1 ^@ http://purl.uniprot.org/uniprot/Q8VG19 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r20 ^@ http://purl.uniprot.org/uniprot/K7N778 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Muc4 ^@ http://purl.uniprot.org/uniprot/Q8JZM8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane ^@ AMOP|||Cleavage|||Disordered|||EGF-like 1|||EGF-like 2|||Helical|||Mucin-4|||Mucin-4 alpha chain|||Mucin-4 beta chain|||N-linked (GlcNAc...) asparagine|||NIDO|||O-linked (GalNAc...) threonine|||VWFD|||Variable number of tandem repeats (VNTR) ^@ http://purl.uniprot.org/annotation/PRO_0000274227|||http://purl.uniprot.org/annotation/PRO_0000274228|||http://purl.uniprot.org/annotation/PRO_0000274229 http://togogenome.org/gene/10090:Aadacl2 ^@ http://purl.uniprot.org/uniprot/B2RWD2 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Signal Peptide ^@ Alpha/beta hydrolase fold-3 ^@ http://purl.uniprot.org/annotation/PRO_5015087164 http://togogenome.org/gene/10090:Slc35b1 ^@ http://purl.uniprot.org/uniprot/P97858 ^@ Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Motif|||Splice Variant|||Transmembrane ^@ Di-lysine motif|||Helical|||In isoform 2.|||Solute carrier family 35 member B1 ^@ http://purl.uniprot.org/annotation/PRO_0000213367|||http://purl.uniprot.org/annotation/VSP_016192 http://togogenome.org/gene/10090:Bpifb9b ^@ http://purl.uniprot.org/uniprot/A2AJD1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Lipid-binding serum glycoprotein N-terminal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015086020 http://togogenome.org/gene/10090:Evc ^@ http://purl.uniprot.org/uniprot/P57680 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||EvC complex member EVC|||Extracellular|||Helical|||In isoform Short.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087103|||http://purl.uniprot.org/annotation/VSP_004247 http://togogenome.org/gene/10090:Man1a2 ^@ http://purl.uniprot.org/uniprot/P39098 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB|||N-acetylthreonine|||N-linked (GlcNAc...) asparagine|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000210313|||http://purl.uniprot.org/annotation/VSP_018615 http://togogenome.org/gene/10090:Gsk3a ^@ http://purl.uniprot.org/uniprot/Q2NL51 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||Glycogen synthase kinase-3 alpha|||Loss of phosphorylation; No inhibition of activity and constitutively active.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000280395 http://togogenome.org/gene/10090:Dram1 ^@ http://purl.uniprot.org/uniprot/Q9DC58 ^@ 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_0000287437|||http://purl.uniprot.org/annotation/VSP_025461 http://togogenome.org/gene/10090:Zfp606 ^@ http://purl.uniprot.org/uniprot/Q3UTP2|||http://purl.uniprot.org/uniprot/Q69Z88|||http://purl.uniprot.org/uniprot/Q7TSV0 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Arhgdib ^@ http://purl.uniprot.org/uniprot/Q61599 ^@ 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|||Disordered|||N-acetylthreonine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed|||Rho GDP-dissociation inhibitor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000219017 http://togogenome.org/gene/10090:Crh ^@ http://purl.uniprot.org/uniprot/Q8CIT0 ^@ Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Compositionally Biased Region|||Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Basic and acidic residues|||Corticoliberin|||Disordered|||Isoleucine amide|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000006214|||http://purl.uniprot.org/annotation/PRO_0000006215 http://togogenome.org/gene/10090:Nagk ^@ http://purl.uniprot.org/uniprot/Q3U2G9|||http://purl.uniprot.org/uniprot/Q9D997|||http://purl.uniprot.org/uniprot/Q9QZ08 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ ATPase BadF/BadG/BcrA/BcrD type|||N-acetyl-D-glucosamine kinase|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000096697 http://togogenome.org/gene/10090:Haus1 ^@ http://purl.uniprot.org/uniprot/Q8BHX1 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Sequence Conflict ^@ HAUS augmin-like complex subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000089396 http://togogenome.org/gene/10090:H2bc18 ^@ http://purl.uniprot.org/uniprot/Q64525 ^@ 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 2-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-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_0000244835 http://togogenome.org/gene/10090:Srsf10 ^@ http://purl.uniprot.org/uniprot/Q3TFP0|||http://purl.uniprot.org/uniprot/Q3UA07|||http://purl.uniprot.org/uniprot/Q9R0U0 ^@ 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.|||Phosphoserine|||Polar residues|||RRM|||Serine/arginine-rich splicing factor 10 ^@ http://purl.uniprot.org/annotation/PRO_0000081594|||http://purl.uniprot.org/annotation/VSP_010426|||http://purl.uniprot.org/annotation/VSP_010427|||http://purl.uniprot.org/annotation/VSP_010428 http://togogenome.org/gene/10090:Itga8 ^@ http://purl.uniprot.org/uniprot/A2ARA8 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cell attachment site|||Cytoplasmic|||Extracellular|||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-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_0000297709|||http://purl.uniprot.org/annotation/PRO_0000297710|||http://purl.uniprot.org/annotation/PRO_0000297711|||http://purl.uniprot.org/annotation/VSP_027364|||http://purl.uniprot.org/annotation/VSP_027365 http://togogenome.org/gene/10090:Pter ^@ http://purl.uniprot.org/uniprot/Q60866 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Phosphotriesterase-related protein ^@ http://purl.uniprot.org/annotation/PRO_0000205365|||http://purl.uniprot.org/annotation/VSP_038343|||http://purl.uniprot.org/annotation/VSP_038344 http://togogenome.org/gene/10090:Sh3pxd2b ^@ http://purl.uniprot.org/uniprot/A0A5F8MPP7|||http://purl.uniprot.org/uniprot/A2AAY5 ^@ 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 ^@ Basic and acidic residues|||Disordered|||PX|||Phosphoserine|||Phosphotyrosine|||Pro residues|||Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-25 and F-373.|||Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-25 and F-508.|||Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-373 and F-508.|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||SH3 and PX domain-containing protein 2B ^@ http://purl.uniprot.org/annotation/PRO_0000312202 http://togogenome.org/gene/10090:Krtap7-1 ^@ http://purl.uniprot.org/uniprot/Q9D3I6 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ 8 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 7-1 ^@ http://purl.uniprot.org/annotation/PRO_0000185183 http://togogenome.org/gene/10090:Shc1 ^@ http://purl.uniprot.org/uniprot/P98083 ^@ 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 ^@ CH1|||Disordered|||In isoform p47Shc.|||In isoform p52Shc.|||N-acetylmethionine|||N6-acetyllysine|||PID|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SH2|||SHC-transforming protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000022339|||http://purl.uniprot.org/annotation/VSP_018791|||http://purl.uniprot.org/annotation/VSP_018792 http://togogenome.org/gene/10090:Psmd2 ^@ http://purl.uniprot.org/uniprot/Q3TKV1|||http://purl.uniprot.org/uniprot/Q8VDM4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ 26S proteasome non-ATPase regulatory subunit 2|||26S proteasome non-ATPase regulatory subunit RPN1 C-terminal|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||N6-acetyllysine|||PC 1|||PC 2|||PC 3|||PC 4|||PC 5|||PC 6|||PC 7|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RPN1 N-terminal|||Required for interaction with UBLCP1 ^@ http://purl.uniprot.org/annotation/PRO_0000173811 http://togogenome.org/gene/10090:Kctd11 ^@ http://purl.uniprot.org/uniprot/Q8K485 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ BTB|||BTB/POZ domain-containing protein KCTD11 ^@ http://purl.uniprot.org/annotation/PRO_0000248592 http://togogenome.org/gene/10090:Fbxw24 ^@ http://purl.uniprot.org/uniprot/E9PXM9|||http://purl.uniprot.org/uniprot/Q66JY5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Ntn3 ^@ http://purl.uniprot.org/uniprot/Q52KG2|||http://purl.uniprot.org/uniprot/Q9R1A3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide ^@ Cell attachment site; atypical|||Laminin EGF-like|||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_0000017086|||http://purl.uniprot.org/annotation/PRO_5014309502 http://togogenome.org/gene/10090:Miga1 ^@ http://purl.uniprot.org/uniprot/B2RRB9|||http://purl.uniprot.org/uniprot/Q4QQM5 ^@ 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.|||Mitoguardin 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000285647|||http://purl.uniprot.org/annotation/VSP_024880|||http://purl.uniprot.org/annotation/VSP_024881|||http://purl.uniprot.org/annotation/VSP_024882 http://togogenome.org/gene/10090:Cd200r3 ^@ http://purl.uniprot.org/uniprot/Q5UKY4 ^@ 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 ^@ Cell surface glycoprotein CD200 receptor 3|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2 and isoform 7.|||In isoform 3 and isoform 8.|||In isoform 4 and isoform 9.|||In isoform 5.|||In isoform 6, isoform 7, isoform 8 and isoform 9.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000346453|||http://purl.uniprot.org/annotation/VSP_035003|||http://purl.uniprot.org/annotation/VSP_035004|||http://purl.uniprot.org/annotation/VSP_035005|||http://purl.uniprot.org/annotation/VSP_035006|||http://purl.uniprot.org/annotation/VSP_035007|||http://purl.uniprot.org/annotation/VSP_035008 http://togogenome.org/gene/10090:Rec114 ^@ http://purl.uniprot.org/uniprot/Q9CWH4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Disordered|||Meiotic recombination protein REC114|||Polar residues|||Strongly reduced interaction with ANKRD31.|||Strongly reduced interaction with ANKRD31; when associated with A-104.|||Strongly reduced interaction with ANKRD31; when associated with A-28.|||Strongly reduced interaction with ANKRD31; when associated with A-74.|||Strongly reduced interaction with ANKRD31; when associated with A-81. ^@ http://purl.uniprot.org/annotation/PRO_0000321519 http://togogenome.org/gene/10090:Cfap53 ^@ http://purl.uniprot.org/uniprot/Q059Q0|||http://purl.uniprot.org/uniprot/Q9D439 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Splice Variant ^@ Cilia- and flagella-associated protein 53|||Disordered|||In isoform 2.|||Trichohyalin-plectin-homology ^@ http://purl.uniprot.org/annotation/PRO_0000089408|||http://purl.uniprot.org/annotation/VSP_057233 http://togogenome.org/gene/10090:Ripor3 ^@ http://purl.uniprot.org/uniprot/A1L3T7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Phosphothreonine|||RIPOR family member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000358907 http://togogenome.org/gene/10090:Nlrx1 ^@ http://purl.uniprot.org/uniprot/Q3TL44 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ 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_0000296191 http://togogenome.org/gene/10090:Arxes2 ^@ http://purl.uniprot.org/uniprot/C0HK79|||http://purl.uniprot.org/uniprot/C0HK80 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Adipocyte-related X-chromosome expressed sequence 1|||Adipocyte-related X-chromosome expressed sequence 2|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000438510|||http://purl.uniprot.org/annotation/PRO_0000438511 http://togogenome.org/gene/10090:Cenpe ^@ http://purl.uniprot.org/uniprot/E9QKK1|||http://purl.uniprot.org/uniprot/Q6RT24 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict ^@ Centromere-associated protein E|||Cysteine methyl ester|||Disordered|||Globular autoinhibitory domain|||Kinesin motor|||Kinetochore binding domain|||Phosphoserine|||Polar residues|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000365106|||http://purl.uniprot.org/annotation/PRO_0000396743 http://togogenome.org/gene/10090:Tbpl1 ^@ http://purl.uniprot.org/uniprot/P62340 ^@ Chain|||Molecule Processing ^@ Chain ^@ TATA box-binding protein-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000153993 http://togogenome.org/gene/10090:Usp8 ^@ http://purl.uniprot.org/uniprot/A2AI52|||http://purl.uniprot.org/uniprot/Q80U87 ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes interaction with the SH3 domain of STAM2.|||Abolishes the interaction with YWHAE and leads to accumulation in the nucleus.|||Basic and acidic residues|||Disordered|||Does not affect interaction with the SH3 domain of STAM2.|||Impairs deubiquitination of EPS15, RNF128 and RNF41.|||MIT|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proton acceptor|||Reduces interaction with the SH3 domain of STAM2.|||Reduces stabilization activity on RNF41.|||Rhodanese|||SH3-binding|||USP|||Ubiquitin carboxyl-terminal hydrolase 8 ^@ http://purl.uniprot.org/annotation/PRO_0000080628 http://togogenome.org/gene/10090:Cmtm6 ^@ http://purl.uniprot.org/uniprot/Q9CZ69 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CKLF-like MARVEL transmembrane domain-containing protein 6|||Cytoplasmic|||Extracellular|||Helical|||MARVEL|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000186108 http://togogenome.org/gene/10090:Or7a40 ^@ http://purl.uniprot.org/uniprot/A2RSZ3|||http://purl.uniprot.org/uniprot/Q9JHB2 ^@ 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 7A40 ^@ http://purl.uniprot.org/annotation/PRO_0000150814 http://togogenome.org/gene/10090:Casp14 ^@ http://purl.uniprot.org/uniprot/O89094|||http://purl.uniprot.org/uniprot/Q542Q1 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Propeptide|||Splice Variant ^@ 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|||Decrease in death-inducing activity.|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000004655|||http://purl.uniprot.org/annotation/PRO_0000004657|||http://purl.uniprot.org/annotation/PRO_0000432797|||http://purl.uniprot.org/annotation/PRO_0000432798|||http://purl.uniprot.org/annotation/PRO_0000432799|||http://purl.uniprot.org/annotation/PRO_0000432800|||http://purl.uniprot.org/annotation/VSP_028925|||http://purl.uniprot.org/annotation/VSP_028926 http://togogenome.org/gene/10090:Adgrf3 ^@ http://purl.uniprot.org/uniprot/Q58Y75 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Adhesion G-protein coupled receptor F3|||Basic and acidic residues|||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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000305305 http://togogenome.org/gene/10090:Car1 ^@ http://purl.uniprot.org/uniprot/P13634 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase 1|||Disordered|||N-acetylalanine|||Proton donor/acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000077413 http://togogenome.org/gene/10090:LTO1 ^@ http://purl.uniprot.org/uniprot/Q3TF33|||http://purl.uniprot.org/uniprot/Q8CH62 ^@ 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 ^@ Essential protein Yae1 N-terminal|||N-acetylalanine|||Protein LTO1 homolog|||Removed|||deca-GX3 motif; required for interaction with YAE1 and the CIA complex ^@ http://purl.uniprot.org/annotation/PRO_0000058076 http://togogenome.org/gene/10090:Or10aa3 ^@ http://purl.uniprot.org/uniprot/E9Q8M2|||http://purl.uniprot.org/uniprot/Q3KPC8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fgf18 ^@ http://purl.uniprot.org/uniprot/A0A7U3JW51|||http://purl.uniprot.org/uniprot/O89101 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Fibroblast growth factor|||Fibroblast growth factor 18|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000008991|||http://purl.uniprot.org/annotation/PRO_5031593759 http://togogenome.org/gene/10090:Stk38l ^@ http://purl.uniprot.org/uniprot/Q7TSE6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ AGC-kinase C-terminal|||In isoform 2.|||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_0000086721|||http://purl.uniprot.org/annotation/VSP_012334 http://togogenome.org/gene/10090:Syk ^@ http://purl.uniprot.org/uniprot/P48025|||http://purl.uniprot.org/uniprot/Q3UPF7|||http://purl.uniprot.org/uniprot/Q6P1E0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand ^@ Constitutively active protein tyrosine kinase activity. Causes an immune dysregulation disorder. Treatment with SYK-specific inhibitor ameliorates the disease phenotype.|||Disordered|||Interdomain A|||Interdomain B|||Loss of interaction with FCER1G and TYROBP; when associated with A-194.|||Loss of interaction with FCER1G and TYROBP; when associated with A-41.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by LYN|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SH2|||SH2 1|||SH2 2|||Tyrosine-protein kinase SYK ^@ http://purl.uniprot.org/annotation/PRO_0000088166 http://togogenome.org/gene/10090:Arid5a ^@ http://purl.uniprot.org/uniprot/D3Z0W0|||http://purl.uniprot.org/uniprot/Q3U108 ^@ 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 ^@ ARID|||AT-rich interactive domain-containing protein 5A|||Abolishes binding to STAT3 3'UTR stem loop structure. Abolishes binding to TNFRSF4/OX40 mRNA.|||Abolishes ubiquitination; largely impairs proteasomal degradation; results in overproduction of IL-6 upon overexpression; in association with A-253 and A-433.|||Abolishes ubiquitination; largely impairs proteasomal degradation; results in overproduction of IL-6 upon overexpression; in association with A-253 and A-458.|||Abolishes ubiquitination; largely impairs proteasomal degradation; results in overproduction of IL-6 upon overexpression; in association with A-433 and A-458.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with SOX9|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288931|||http://purl.uniprot.org/annotation/VSP_025838|||http://purl.uniprot.org/annotation/VSP_025839|||http://purl.uniprot.org/annotation/VSP_025840|||http://purl.uniprot.org/annotation/VSP_025841|||http://purl.uniprot.org/annotation/VSP_025842 http://togogenome.org/gene/10090:Mis12 ^@ http://purl.uniprot.org/uniprot/Q9CY25 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Sequence Conflict ^@ Protein MIS12 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000248235 http://togogenome.org/gene/10090:Timm29 ^@ http://purl.uniprot.org/uniprot/Q8BGX2 ^@ 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_0000271007 http://togogenome.org/gene/10090:Adm ^@ http://purl.uniprot.org/uniprot/P97297 ^@ Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disulfide Bond|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Adrenomedullin|||Arginine amide|||Disordered|||PreproAM C-terminal fragment|||Proadrenomedullin N-20 terminal peptide|||Tyrosine amide ^@ http://purl.uniprot.org/annotation/PRO_0000000965|||http://purl.uniprot.org/annotation/PRO_0000000966|||http://purl.uniprot.org/annotation/PRO_0000000967|||http://purl.uniprot.org/annotation/PRO_0000000968 http://togogenome.org/gene/10090:Ints14 ^@ http://purl.uniprot.org/uniprot/Q8R3P6 ^@ 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 ^@ In isoform 2.|||Integrator complex subunit 14|||N6-acetyllysine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000296268|||http://purl.uniprot.org/annotation/VSP_027182|||http://purl.uniprot.org/annotation/VSP_027183 http://togogenome.org/gene/10090:Ppp1r13l ^@ http://purl.uniprot.org/uniprot/Q3TCU2|||http://purl.uniprot.org/uniprot/Q5I1X5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ ANK|||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_0000066967 http://togogenome.org/gene/10090:Or5w1b ^@ http://purl.uniprot.org/uniprot/Q7TR44 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Psd3 ^@ http://purl.uniprot.org/uniprot/E9PUC5|||http://purl.uniprot.org/uniprot/Q2PFD7 ^@ 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 3 and isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PH|||PH and SEC7 domain-containing protein 3|||Phosphoserine|||Polar residues|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000309454|||http://purl.uniprot.org/annotation/VSP_029157|||http://purl.uniprot.org/annotation/VSP_029158|||http://purl.uniprot.org/annotation/VSP_029159|||http://purl.uniprot.org/annotation/VSP_029160|||http://purl.uniprot.org/annotation/VSP_029161 http://togogenome.org/gene/10090:Perm1 ^@ http://purl.uniprot.org/uniprot/Q149B8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Omega-N-methylarginine|||PGC-1 and ERR-induced regulator in muscle protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000299541 http://togogenome.org/gene/10090:Rtl9 ^@ http://purl.uniprot.org/uniprot/Q32KG4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Polar residues|||Retrotransposon Gag-like protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000259628|||http://purl.uniprot.org/annotation/VSP_021488 http://togogenome.org/gene/10090:Pwwp3a ^@ http://purl.uniprot.org/uniprot/Q6DID5 ^@ 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|||PWWP|||PWWP domain-containing DNA repair factor 3A|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295047 http://togogenome.org/gene/10090:Ccs ^@ http://purl.uniprot.org/uniprot/Q543K2|||http://purl.uniprot.org/uniprot/Q9WU84 ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region ^@ Copper chaperone for superoxide dismutase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HMA|||Phosphoserine|||Superoxide dismutase-like ^@ http://purl.uniprot.org/annotation/PRO_0000213544 http://togogenome.org/gene/10090:Pou2f3 ^@ http://purl.uniprot.org/uniprot/P31362|||http://purl.uniprot.org/uniprot/Q3U5D1 ^@ 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 ^@ Disordered|||Homeobox|||POU domain, class 2, transcription factor 3|||POU-specific|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000100718 http://togogenome.org/gene/10090:Elp4 ^@ http://purl.uniprot.org/uniprot/Q9ER73 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Elongator complex protein 4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284005 http://togogenome.org/gene/10090:Apobr ^@ http://purl.uniprot.org/uniprot/Q8VBT6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Apolipoprotein B receptor|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000327264 http://togogenome.org/gene/10090:Cops7a ^@ http://purl.uniprot.org/uniprot/Q9CZ04 ^@ 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 ^@ COP9 signalosome complex subunit 7a|||Disordered|||In isoform 2.|||N-acetylserine|||PCI|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000120997|||http://purl.uniprot.org/annotation/VSP_011912 http://togogenome.org/gene/10090:Nfatc3 ^@ http://purl.uniprot.org/uniprot/Q3UZ64 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||RHD ^@ http://togogenome.org/gene/10090:Cryz ^@ http://purl.uniprot.org/uniprot/P47199 ^@ 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-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Quinone oxidoreductase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000160908 http://togogenome.org/gene/10090:Tbx21 ^@ http://purl.uniprot.org/uniprot/Q9JKD8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand ^@ 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)|||Loss of interaction with RUNX1 and loss of its ability to inhibit RUNX1 transcriptional activity and suppress TH17 lineage development. Significant loss of ABL1-mediated phosphorylation and loss of transcriptional activator activity; when associated with F-219 and F-225.|||Loss of phosphorylation and its ability to interact with NFATC2. Loss of its ability to suppress IL-2 and Th2 cytokine production. No loss of DNA-binding and no loss its ability to activate IFN-gamma transcription.|||No effect on DNA-binding or its nuclear localization.|||No loss in its ability to induce IFN-gamma.|||No loss in its ability to induce IFN-gamma. Significant reduction in its ability to induce IFN-gamma and reduced ability to promote addition of permissive chromatin-remodeling mark H3K4Me2 to the IFNG promoter region; when associated with A-52 and A-224.|||No loss in its ability to induce IFN-gamma. Significant reduction in its ability to induce IFN-gamma and reduced ability to promote addition of permissive chromatin-remodeling mark H3K4Me2 to the IFNG promoter region; when associated with A-52 and A-76.|||No loss in its ability to induce IFN-gamma. Significant reduction in its ability to induce IFN-gamma and reduced ability to promote addition of permissive chromatin-remodeling mark H3K4Me2 to the IFNG promoter region; when associated with A-76 and A-224.|||No loss of interaction with ITK and GATA3.|||No loss of interaction with RUNX1.|||No loss of interaction with RUNX1. Loss of interaction with ITK and GATA3.|||No loss of interaction with RUNX1. No loss in its ability to induce IFN-gamma.|||No loss of phospshorylation.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Phosphotyrosine; by ITK|||Polar residues|||Significant loss of ABL1-mediated phosphorylation and loss of transcriptional activator activity; when associated with F-219 and F-304.|||Significant loss of ABL1-mediated phosphorylation and loss of transcriptional activator activity; when associated with F-225 and F-304.|||Significant loss of ubiquitination. Loss of phosphorylation at T-302 causing loss of its ability to interact with NFATC2. Loss its ability to activate IFN-gamma transcription due to loss of DNA-binding activity. Loss of its ability to suppress IL-2 and Th2 cytokine production. Increased protein stability. Localization seen in both the nucleus and cytoplasm. No loss of interaction with GATA3 and RELA.|||T-box|||T-box transcription factor TBX21 ^@ http://purl.uniprot.org/annotation/PRO_0000184454 http://togogenome.org/gene/10090:Fstl3 ^@ http://purl.uniprot.org/uniprot/Q542M9|||http://purl.uniprot.org/uniprot/Q9EQC7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Follistatin-like 1|||Follistatin-like 2|||Follistatin-related protein 3|||Kazal-like|||Kazal-like 1|||Kazal-like 2|||N-linked (GlcNAc...) asparagine|||TB ^@ http://purl.uniprot.org/annotation/PRO_0000010116|||http://purl.uniprot.org/annotation/PRO_5014309537 http://togogenome.org/gene/10090:Vgll2 ^@ http://purl.uniprot.org/uniprot/Q8BGW8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Transcription cofactor vestigial-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000191350 http://togogenome.org/gene/10090:Ccnb2 ^@ http://purl.uniprot.org/uniprot/P30276 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||G2/mitotic-specific cyclin-B2|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000080363 http://togogenome.org/gene/10090:Setdb1 ^@ http://purl.uniprot.org/uniprot/D3YYC3|||http://purl.uniprot.org/uniprot/G5E8N3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||MBD|||Polar residues|||Post-SET|||Pre-SET|||Pro residues|||SET ^@ http://togogenome.org/gene/10090:ATP6 ^@ http://purl.uniprot.org/uniprot/P00848|||http://purl.uniprot.org/uniprot/Q7JCY9 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ ATP synthase subunit a|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000082139 http://togogenome.org/gene/10090:4933405L10Rik ^@ http://purl.uniprot.org/uniprot/Q9D4A5 ^@ 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 C16orf86 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000402135|||http://purl.uniprot.org/annotation/VSP_040246 http://togogenome.org/gene/10090:Otud6b ^@ http://purl.uniprot.org/uniprot/A0A0A0MQF5|||http://purl.uniprot.org/uniprot/Q8K2H2 ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Cys-loop|||Deubiquitinase OTUD6B|||His-loop|||N-acetylmethionine|||Nucleophile|||OTU|||Variable-loop ^@ http://purl.uniprot.org/annotation/PRO_0000076280 http://togogenome.org/gene/10090:Vax1 ^@ http://purl.uniprot.org/uniprot/Q2NKI2 ^@ 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|||In isoform 2.|||Polar residues|||Ventral anterior homeobox 1 ^@ http://purl.uniprot.org/annotation/PRO_0000240523|||http://purl.uniprot.org/annotation/VSP_019397 http://togogenome.org/gene/10090:Trim47 ^@ http://purl.uniprot.org/uniprot/B7ZN75|||http://purl.uniprot.org/uniprot/Q497Z1|||http://purl.uniprot.org/uniprot/Q8C0E3 ^@ 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|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ B box-type|||B30.2/SPRY|||Disordered|||E3 ubiquitin-protein ligase TRIM47|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056271|||http://purl.uniprot.org/annotation/VSP_011988 http://togogenome.org/gene/10090:Col1a2 ^@ http://purl.uniprot.org/uniprot/Q01149|||http://purl.uniprot.org/uniprot/Q3TX57 ^@ 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ 5-hydroxylysine; alternate|||Allysine|||C-terminal propeptide|||Collagen alpha-2(I) chain|||Disordered|||Fibrillar collagen NC1|||Fibrillar collagen NC1 domain-containing protein|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide|||O-linked (Gal...) hydroxylysine; alternate|||Pro residues|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000005807|||http://purl.uniprot.org/annotation/PRO_0000005808|||http://purl.uniprot.org/annotation/PRO_0000005809|||http://purl.uniprot.org/annotation/PRO_5014309154 http://togogenome.org/gene/10090:Rwdd1 ^@ http://purl.uniprot.org/uniprot/Q9CQK7 ^@ 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 ^@ Acidic residues|||Disordered|||Interaction with DRG2|||N-acetylthreonine|||Phosphothreonine|||RWD|||RWD domain-containing protein 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000097541 http://togogenome.org/gene/10090:Zfp367 ^@ http://purl.uniprot.org/uniprot/Q0VDT2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||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_0000285298|||http://purl.uniprot.org/annotation/VSP_024866 http://togogenome.org/gene/10090:H2-Aa ^@ http://purl.uniprot.org/uniprot/P14434 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Alpha-1|||Alpha-2|||Connecting peptide|||Cytoplasmic|||Extracellular|||H-2 class II histocompatibility antigen, A-B alpha chain|||Helical|||Ig-like C1-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000018975 http://togogenome.org/gene/10090:Map9 ^@ http://purl.uniprot.org/uniprot/Q3TRR0 ^@ 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.|||Microtubule-associated protein 9|||N-acetylserine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000247754|||http://purl.uniprot.org/annotation/VSP_020039 http://togogenome.org/gene/10090:Stx5a ^@ http://purl.uniprot.org/uniprot/Q8K1E0 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Motif|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||IxM motif; signal for cargo packaging into COPII-coated vesicles|||Syntaxin-5|||Vesicular|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000210206|||http://purl.uniprot.org/annotation/VSP_020118 http://togogenome.org/gene/10090:Tsfm ^@ http://purl.uniprot.org/uniprot/Q9CZR8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ Elongation factor Ts, mitochondrial|||Mitochondrion|||N6-succinyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000007469 http://togogenome.org/gene/10090:Prrg2 ^@ http://purl.uniprot.org/uniprot/Q8R182 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 4-carboxyglutamate|||Cytoplasmic|||Disordered|||Extracellular|||Gla|||Helical|||LPXY motif; mediates binding to WW domain-containing proteins|||No effect on interaction with NEDD4.|||PPXY motif; mediates binding to WW domain-containing proteins|||Transmembrane gamma-carboxyglutamic acid protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000022545|||http://purl.uniprot.org/annotation/PRO_0000022546 http://togogenome.org/gene/10090:Stbd1 ^@ http://purl.uniprot.org/uniprot/Q8C7E7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Topological Domain|||Transmembrane ^@ CBM20|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||LIR|||Phosphoserine|||Starch-binding domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000238961 http://togogenome.org/gene/10090:Or9g8 ^@ http://purl.uniprot.org/uniprot/Q7TR95 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccdc180 ^@ http://purl.uniprot.org/uniprot/J3QNE4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||DUF4455|||DUF4456|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tubb3 ^@ http://purl.uniprot.org/uniprot/Q9ERD7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 5-glutamyl polyglutamate|||Acidic residues|||Brain from homozygous mice shows defects in the guidance of commissural axons and nerves, without evidence of cortical cells migration defects.|||Disordered|||MREI motif|||Phosphoserine|||Phosphoserine; by CDK1|||Tubulin beta-3 chain ^@ http://purl.uniprot.org/annotation/PRO_0000048251 http://togogenome.org/gene/10090:Fancf ^@ http://purl.uniprot.org/uniprot/E9Q5Z5 ^@ Chain|||Molecule Processing ^@ Chain ^@ Fanconi anemia group F protein ^@ http://purl.uniprot.org/annotation/PRO_0000436204 http://togogenome.org/gene/10090:Cacna2d1 ^@ http://purl.uniprot.org/uniprot/A0A411ACY8|||http://purl.uniprot.org/uniprot/O08532|||http://purl.uniprot.org/uniprot/Q14BH8 ^@ 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 2B and isoform 2E.|||In isoform 2C and isoform 2D.|||In isoform 2D and isoform 2E.|||Interchain (between alpha-2-1 and delta-1 chains)|||MIDAS-like motif|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||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_0000005003|||http://purl.uniprot.org/annotation/PRO_0000005004|||http://purl.uniprot.org/annotation/PRO_0000304634|||http://purl.uniprot.org/annotation/PRO_5014306917|||http://purl.uniprot.org/annotation/PRO_5019249572|||http://purl.uniprot.org/annotation/VSP_050444|||http://purl.uniprot.org/annotation/VSP_050445|||http://purl.uniprot.org/annotation/VSP_050446 http://togogenome.org/gene/10090:Tmem276-zftraf1 ^@ http://purl.uniprot.org/uniprot/P0DW86|||http://purl.uniprot.org/uniprot/P0DW87 ^@ 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 6 and isoform 7.|||In isoform 6.|||RING-type; degenerate|||TRAF-type|||Transmembrane protein 276|||Zinc finger TRAF-type-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000328853|||http://purl.uniprot.org/annotation/PRO_0000456484|||http://purl.uniprot.org/annotation/VSP_061641|||http://purl.uniprot.org/annotation/VSP_061642|||http://purl.uniprot.org/annotation/VSP_061643 http://togogenome.org/gene/10090:Ifi35 ^@ http://purl.uniprot.org/uniprot/Q9D8C4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Interferon-induced 35 kDa protein homolog|||Leucine-zipper|||NID 1|||NID 2 ^@ http://purl.uniprot.org/annotation/PRO_0000159705 http://togogenome.org/gene/10090:Robo4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J197|||http://purl.uniprot.org/uniprot/A0A1L1SUF8|||http://purl.uniprot.org/uniprot/Q8C310 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||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 isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Roundabout homolog 4 ^@ http://purl.uniprot.org/annotation/PRO_0000031041|||http://purl.uniprot.org/annotation/PRO_5009682011|||http://purl.uniprot.org/annotation/PRO_5039970675|||http://purl.uniprot.org/annotation/VSP_010662|||http://purl.uniprot.org/annotation/VSP_010663 http://togogenome.org/gene/10090:Efcab14 ^@ http://purl.uniprot.org/uniprot/Q6PCQ6|||http://purl.uniprot.org/uniprot/Q8BGQ6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand calcium-binding domain-containing protein 14|||Helical|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000073883|||http://purl.uniprot.org/annotation/VSP_008512 http://togogenome.org/gene/10090:Gm13277 ^@ http://purl.uniprot.org/uniprot/Q8CD73 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099103 http://togogenome.org/gene/10090:Ptprh ^@ http://purl.uniprot.org/uniprot/E9Q0N2 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Helical|||Impairs phosphatase activity.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphotyrosine|||Receptor-type tyrosine-protein phosphatase H|||Reduces tyrosine phosphorylation. Abolishes tyrosine phosphorylation and interaction with GRB2 and FYN; when associated with A-945.|||Reduces tyrosine phosphorylation. Abolishes tyrosine phosphorylation and interaction with GRB2 and FYN; when associated with A-953.|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_5007654674 http://togogenome.org/gene/10090:Nsun3 ^@ http://purl.uniprot.org/uniprot/Q8CCT7 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Splice Variant ^@ In isoform 2.|||Nucleophile|||tRNA (cytosine(34)-C(5))-methyltransferase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000289231|||http://purl.uniprot.org/annotation/VSP_025970 http://togogenome.org/gene/10090:Nkx6-3 ^@ http://purl.uniprot.org/uniprot/B2RU70|||http://purl.uniprot.org/uniprot/Q3UHX8 ^@ 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 and acidic residues|||Disordered|||Homeobox|||Homeobox protein Nkx-6.3 ^@ http://purl.uniprot.org/annotation/PRO_0000311331 http://togogenome.org/gene/10090:Papss2 ^@ http://purl.uniprot.org/uniprot/A0A494B923|||http://purl.uniprot.org/uniprot/O88428 ^@ 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 ^@ ATP-sulfurylase PUA-like|||Adenylyl-sulfate kinase|||Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2|||In bm; activity abolished.|||Sulfate adenylyltransferase|||Sulphate adenylyltransferase catalytic ^@ http://purl.uniprot.org/annotation/PRO_0000105962 http://togogenome.org/gene/10090:Zfr2 ^@ http://purl.uniprot.org/uniprot/E9Q5M4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DZF|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Kif18b ^@ http://purl.uniprot.org/uniprot/Q6PFD6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Kinesin motor|||Kinesin-like protein KIF18B|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000318970 http://togogenome.org/gene/10090:Prss36 ^@ http://purl.uniprot.org/uniprot/D3YV46|||http://purl.uniprot.org/uniprot/E9QJT0 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Region|||Signal Peptide ^@ Charge relay system|||Disordered|||Peptidase S1|||Polyserase-2 ^@ http://purl.uniprot.org/annotation/PRO_5023984888|||http://purl.uniprot.org/annotation/PRO_5023985294 http://togogenome.org/gene/10090:Nop2 ^@ http://purl.uniprot.org/uniprot/E9QN31 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Nucleophile|||Polar residues|||SAM-dependent MTase RsmB/NOP-type ^@ http://togogenome.org/gene/10090:Cplane2 ^@ http://purl.uniprot.org/uniprot/A2A825 ^@ Binding Site|||Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Region|||Strand|||Turn ^@ Ciliogenesis and planar polarity effector 2|||Small GTPase-like ^@ http://purl.uniprot.org/annotation/PRO_0000284539 http://togogenome.org/gene/10090:Sprr2a1 ^@ http://purl.uniprot.org/uniprot/Q4KL71|||http://purl.uniprot.org/uniprot/Q9CQK8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||4|||5|||5 X 9 AA approximate tandem repeats|||Small proline-rich protein 2A1|||Small proline-rich protein 2A3 ^@ http://purl.uniprot.org/annotation/PRO_0000150014|||http://purl.uniprot.org/annotation/PRO_0000425580 http://togogenome.org/gene/10090:Actr2 ^@ http://purl.uniprot.org/uniprot/P61161 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Actin-related protein 2|||N-acetylmethionine|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000089068 http://togogenome.org/gene/10090:Slc22a22 ^@ http://purl.uniprot.org/uniprot/Q8R0S9 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||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 22 ^@ http://purl.uniprot.org/annotation/PRO_0000440989 http://togogenome.org/gene/10090:Pdia4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Z1|||http://purl.uniprot.org/uniprot/P08003 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Acidic residues|||CXXC|||Disordered|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Prevents secretion from ER|||Protein disulfide-isomerase A4|||Redox-active|||Substrate-trapping mutant.|||Thioredoxin|||Thioredoxin 1|||Thioredoxin 2|||Thioredoxin 3 ^@ http://purl.uniprot.org/annotation/PRO_0000034230|||http://purl.uniprot.org/annotation/PRO_5005967682 http://togogenome.org/gene/10090:Ly86 ^@ http://purl.uniprot.org/uniprot/O88188 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Strand ^@ Lymphocyte antigen 86|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000018615 http://togogenome.org/gene/10090:Galr3 ^@ http://purl.uniprot.org/uniprot/O88853 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||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_0000069470 http://togogenome.org/gene/10090:Scart1 ^@ http://purl.uniprot.org/uniprot/Q8CGY7 ^@ 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 ^@ Acidic residues|||Disordered|||Helical|||SRCR ^@ http://purl.uniprot.org/annotation/PRO_5015099075 http://togogenome.org/gene/10090:Or1ak2 ^@ http://purl.uniprot.org/uniprot/Q8VFP5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Snrpd2 ^@ http://purl.uniprot.org/uniprot/P62317|||http://purl.uniprot.org/uniprot/Q14AF6 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||Sm|||Small nuclear ribonucleoprotein Sm D2 ^@ http://purl.uniprot.org/annotation/PRO_0000122208 http://togogenome.org/gene/10090:Dnajc25 ^@ http://purl.uniprot.org/uniprot/A2ALW5 ^@ 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.|||J ^@ http://purl.uniprot.org/annotation/PRO_0000348570|||http://purl.uniprot.org/annotation/VSP_035183 http://togogenome.org/gene/10090:Kmt2c ^@ http://purl.uniprot.org/uniprot/F8WI37 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||FYR C-terminal|||FYR N-terminal|||PHD-type|||Polar residues|||Post-SET|||Pro residues|||RING-type|||SET ^@ http://togogenome.org/gene/10090:Mga ^@ http://purl.uniprot.org/uniprot/A2AWL7|||http://purl.uniprot.org/uniprot/E9QLG3|||http://purl.uniprot.org/uniprot/H7BX50 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||BHLH|||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.|||MAX gene-associated protein|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||T-box|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000342693|||http://purl.uniprot.org/annotation/VSP_034536|||http://purl.uniprot.org/annotation/VSP_034537|||http://purl.uniprot.org/annotation/VSP_034538|||http://purl.uniprot.org/annotation/VSP_034539|||http://purl.uniprot.org/annotation/VSP_034540|||http://purl.uniprot.org/annotation/VSP_034541|||http://purl.uniprot.org/annotation/VSP_034542 http://togogenome.org/gene/10090:Trmt112 ^@ http://purl.uniprot.org/uniprot/Q9DCG9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Multifunctional methyltransferase subunit TRM112-like protein|||TRM112 ^@ http://purl.uniprot.org/annotation/PRO_0000215798 http://togogenome.org/gene/10090:Glul ^@ http://purl.uniprot.org/uniprot/P15105 ^@ 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 ^@ GS beta-grasp|||GS catalytic|||Glutamine synthetase|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000153141 http://togogenome.org/gene/10090:Atp11c ^@ http://purl.uniprot.org/uniprot/E9QKK8|||http://purl.uniprot.org/uniprot/Q9QZW0 ^@ 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|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cleavage; by CASP3|||Cleavage; by CASP3 and CASP7|||Cleavage; by CASP3, CASP6 and CASP7|||Cytoplasmic|||Di-leucine motif|||Extracellular|||Helical|||Impairs ATPase activity.|||In isoform 2.|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Phospholipid-transporting ATPase 11C|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000046374|||http://purl.uniprot.org/annotation/VSP_022222|||http://purl.uniprot.org/annotation/VSP_022223 http://togogenome.org/gene/10090:Tubb1 ^@ http://purl.uniprot.org/uniprot/A2AQ07 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region ^@ 5-glutamyl polyglutamate|||Acidic residues|||Disordered|||MREI motif|||Phosphoserine|||Phosphoserine; by CDK1|||Tubulin beta-1 chain ^@ http://purl.uniprot.org/annotation/PRO_0000413097 http://togogenome.org/gene/10090:Gm3376 ^@ http://purl.uniprot.org/uniprot/Q60990 ^@ 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|||RNA-binding motif protein, Y chromosome, family 1 member B|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000341541 http://togogenome.org/gene/10090:Vmn2r69 ^@ http://purl.uniprot.org/uniprot/G3XA45 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015091856 http://togogenome.org/gene/10090:Acy3 ^@ http://purl.uniprot.org/uniprot/Q91XE4 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolishes activity.|||Drastically reduced activity.|||Hydrolytic domain|||N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)|||Phosphothreonine|||Shielding domain ^@ http://purl.uniprot.org/annotation/PRO_0000216876 http://togogenome.org/gene/10090:Smarca2 ^@ http://purl.uniprot.org/uniprot/F2Z4A9|||http://purl.uniprot.org/uniprot/H3BK47|||http://purl.uniprot.org/uniprot/Q6DIC0|||http://purl.uniprot.org/uniprot/Q9D007 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Signal Peptide ^@ 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|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||Probable global transcription activator SNF2L2|||QLQ ^@ http://purl.uniprot.org/annotation/PRO_0000391618|||http://purl.uniprot.org/annotation/PRO_5015093545 http://togogenome.org/gene/10090:Fnd3c2 ^@ http://purl.uniprot.org/uniprot/A2AP83|||http://purl.uniprot.org/uniprot/Q3UKF7 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Fibronectin type-III|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Ccdc7a ^@ http://purl.uniprot.org/uniprot/G3X9U4|||http://purl.uniprot.org/uniprot/Q9D4Y1|||http://purl.uniprot.org/uniprot/Q9D541 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 7|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000419668 http://togogenome.org/gene/10090:Gm527 ^@ http://purl.uniprot.org/uniprot/Q4KL13 ^@ Chain|||Molecule Processing ^@ Chain ^@ Uncharacterized protein C14orf28 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000274308 http://togogenome.org/gene/10090:Hbq1b ^@ http://purl.uniprot.org/uniprot/Q3U0A6 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Globin family profile|||distal binding residue|||proximal binding residue ^@ http://togogenome.org/gene/10090:Smim26 ^@ http://purl.uniprot.org/uniprot/Q3V460 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Plcd3 ^@ http://purl.uniprot.org/uniprot/Q8K2J0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3|||Acidic residues|||C2|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Loss of phosphatidylinositol 4,5-bisphosphate hydrolyzing activity. In neurons, generates supernumerary protrusions.|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Substrate binding ^@ http://purl.uniprot.org/annotation/PRO_0000306822 http://togogenome.org/gene/10090:Or51ah3 ^@ http://purl.uniprot.org/uniprot/Q8VGY4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dgkk ^@ http://purl.uniprot.org/uniprot/Q6DIC8 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ DAGKc|||Disordered|||PH|||Phorbol-ester/DAG-type ^@ http://togogenome.org/gene/10090:Eid2b ^@ http://purl.uniprot.org/uniprot/E9Q2Y0 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Bicd2 ^@ http://purl.uniprot.org/uniprot/D3Z390|||http://purl.uniprot.org/uniprot/Q921C5 ^@ 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.|||In isoform 3.|||Interaction with DYNLL1, DYNC1H1, DYNC1I2, DCTN1 and DCTN2|||Interaction with KIF5A|||Interaction with RAB6A|||Interaction with RANBP2|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein bicaudal D homolog 2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000205360|||http://purl.uniprot.org/annotation/VSP_007970|||http://purl.uniprot.org/annotation/VSP_007971|||http://purl.uniprot.org/annotation/VSP_007972 http://togogenome.org/gene/10090:Tbc1d9b ^@ http://purl.uniprot.org/uniprot/Q5SVR0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Arginine finger|||Basic and acidic residues|||Disordered|||EF-hand|||GRAM 1|||GRAM 2|||Glutamine finger|||Helical|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rab-GAP TBC|||TBC1 domain family member 9B ^@ http://purl.uniprot.org/annotation/PRO_0000288502|||http://purl.uniprot.org/annotation/VSP_025700 http://togogenome.org/gene/10090:Rabl3 ^@ http://purl.uniprot.org/uniprot/Q9D4V7 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ In isoform 2.|||In xiamen; reduced Rabl3 expression, reduced interaction with Gpr89, reduced thermal stability, reduced frequency of CD3+ T cells, increased CD4+-to-CD8+ T cell ratio, higher CD44 expression in CD8+ T cells and increased B cell-to-T cell ratio.|||Rab-like protein 3|||Small GTPase-like ^@ http://purl.uniprot.org/annotation/PRO_0000312167|||http://purl.uniprot.org/annotation/VSP_029723 http://togogenome.org/gene/10090:Ube2e1 ^@ http://purl.uniprot.org/uniprot/P52482|||http://purl.uniprot.org/uniprot/Q541Z5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Glycyl thioester intermediate|||N-acetylserine|||Polar residues|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 E1 ^@ http://purl.uniprot.org/annotation/PRO_0000082471 http://togogenome.org/gene/10090:Nradd ^@ http://purl.uniprot.org/uniprot/Q8CJ26 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||Cytoplasmic|||Death|||Death domain-containing membrane protein NRADD|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000415383 http://togogenome.org/gene/10090:4930564C03Rik ^@ http://purl.uniprot.org/uniprot/Q9D4S5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Lyve1 ^@ http://purl.uniprot.org/uniprot/Q8BHC0 ^@ 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 ^@ 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_0000252134 http://togogenome.org/gene/10090:Bcl2a1b ^@ http://purl.uniprot.org/uniprot/Q497M6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Bcl-2 Bcl-2 homology region 1-3 ^@ http://togogenome.org/gene/10090:Tesk2 ^@ http://purl.uniprot.org/uniprot/Q8VCT9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Dual specificity testis-specific protein kinase 2|||Phosphoserine|||Phosphoserine; by autocatalysis|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086750 http://togogenome.org/gene/10090:Epc1 ^@ http://purl.uniprot.org/uniprot/Q3UEV1|||http://purl.uniprot.org/uniprot/Q3UG01|||http://purl.uniprot.org/uniprot/Q6PBH3|||http://purl.uniprot.org/uniprot/Q7TNR8|||http://purl.uniprot.org/uniprot/Q8C9X6 ^@ 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|||Enhancer of polycomb C-terminal|||Enhancer of polycomb homolog 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000214154|||http://purl.uniprot.org/annotation/VSP_012878 http://togogenome.org/gene/10090:Focad ^@ http://purl.uniprot.org/uniprot/A2AKG8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Focadhesin|||In isoform 2.|||In isoform 3.|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000314458|||http://purl.uniprot.org/annotation/VSP_030274|||http://purl.uniprot.org/annotation/VSP_030275|||http://purl.uniprot.org/annotation/VSP_030276 http://togogenome.org/gene/10090:Cebpzos ^@ http://purl.uniprot.org/uniprot/Q8BTE5 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Protein CEBPZOS ^@ http://purl.uniprot.org/annotation/PRO_0000432373 http://togogenome.org/gene/10090:Pecr ^@ http://purl.uniprot.org/uniprot/Q99MZ7 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict ^@ Microbody targeting signal|||N-acetylglycine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Peroxisomal trans-2-enoyl-CoA reductase|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000054741 http://togogenome.org/gene/10090:Myh10 ^@ http://purl.uniprot.org/uniprot/Q3UH59|||http://purl.uniprot.org/uniprot/Q5SV64|||http://purl.uniprot.org/uniprot/Q61879 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Actin-binding|||Basic and acidic residues|||Disordered|||IQ|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-10|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000123422 http://togogenome.org/gene/10090:Lipk ^@ http://purl.uniprot.org/uniprot/Q8BM14 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ AB hydrolase-1|||Charge relay system|||In isoform 2.|||Lipase member K|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000286700|||http://purl.uniprot.org/annotation/VSP_025143 http://togogenome.org/gene/10090:Ppl ^@ http://purl.uniprot.org/uniprot/G5E898|||http://purl.uniprot.org/uniprot/Q3UQD7|||http://purl.uniprot.org/uniprot/Q9R269 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||Interacts with BFSP2 and VIM|||Periplakin|||Phosphoserine|||Plectin 1|||Plectin 2|||SH3|||Spectrin 1|||Spectrin 2|||Spectrin 3 ^@ http://purl.uniprot.org/annotation/PRO_0000078150 http://togogenome.org/gene/10090:Ube2j1 ^@ http://purl.uniprot.org/uniprot/Q9JJZ4 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Glycyl thioester intermediate|||Helical; Anchor for type IV membrane protein|||Lumenal|||Phosphoserine|||Polar residues|||UBC core|||Ubiquitin-conjugating enzyme E2 J1 ^@ http://purl.uniprot.org/annotation/PRO_0000082595 http://togogenome.org/gene/10090:Or1l4 ^@ http://purl.uniprot.org/uniprot/Q8VFT2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cep164 ^@ http://purl.uniprot.org/uniprot/A0A1L1SSA4|||http://purl.uniprot.org/uniprot/D3YVU3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||Pro residues|||WW ^@ http://togogenome.org/gene/10090:Ctnnbl1 ^@ http://purl.uniprot.org/uniprot/Q9CWL8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||Basic and acidic residues|||Beta-catenin-like protein 1|||Disordered|||HEAT 1|||HEAT 2|||N-acetylmethionine|||N6-acetyllysine|||Nuclear export signal (NES)|||Nuclear localization signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000079491 http://togogenome.org/gene/10090:Hspg2 ^@ http://purl.uniprot.org/uniprot/E9PZ16|||http://purl.uniprot.org/uniprot/Q05793|||http://purl.uniprot.org/uniprot/Q2XQV0|||http://purl.uniprot.org/uniprot/Q3UHH3|||http://purl.uniprot.org/uniprot/Q52KG8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand ^@ Basement membrane-specific heparan sulfate proteoglycan core protein|||Cleavage; by BMP1|||Disordered|||EGF-like|||Endorepellin|||Ig-like|||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 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|||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|||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|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin IV type A|||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 (Xyl...) (chondroitin sulfate) serine|||O-linked (Xyl...) (heparan sulfate) serine|||Polar residues|||SEA ^@ http://purl.uniprot.org/annotation/PRO_0000026697|||http://purl.uniprot.org/annotation/PRO_0000391623|||http://purl.uniprot.org/annotation/PRO_0000391624|||http://purl.uniprot.org/annotation/PRO_5003243035|||http://purl.uniprot.org/annotation/PRO_5010843443 http://togogenome.org/gene/10090:Rax ^@ http://purl.uniprot.org/uniprot/O35602 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Homeobox|||Nuclear localization signal|||OAR|||Octapeptide motif|||Pro residues|||Retinal homeobox protein Rx ^@ http://purl.uniprot.org/annotation/PRO_0000049277 http://togogenome.org/gene/10090:Gm7030 ^@ http://purl.uniprot.org/uniprot/Q0WXH6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097016 http://togogenome.org/gene/10090:Cyp1b1 ^@ http://purl.uniprot.org/uniprot/Q64429 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Cytochrome P450 1B1|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051661 http://togogenome.org/gene/10090:Xpo6 ^@ http://purl.uniprot.org/uniprot/Q924Z6 ^@ 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 ^@ Exportin-6|||Importin N-terminal|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000235302|||http://purl.uniprot.org/annotation/VSP_018466|||http://purl.uniprot.org/annotation/VSP_018467|||http://purl.uniprot.org/annotation/VSP_018468 http://togogenome.org/gene/10090:Aldoc ^@ http://purl.uniprot.org/uniprot/P05063 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site ^@ Fructose-bisphosphate aldolase C|||N6-acetyllysine|||Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Removed|||Schiff-base intermediate with dihydroxyacetone-P ^@ http://purl.uniprot.org/annotation/PRO_0000216949 http://togogenome.org/gene/10090:Wdr20rt ^@ http://purl.uniprot.org/uniprot/Q9D5R2 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||N-acetylalanine|||Phosphoserine|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat-containing protein 20 ^@ http://purl.uniprot.org/annotation/PRO_0000051367 http://togogenome.org/gene/10090:Or5m9b ^@ http://purl.uniprot.org/uniprot/Q7TR85 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Col8a1 ^@ http://purl.uniprot.org/uniprot/Q00780 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ 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_0000005763|||http://purl.uniprot.org/annotation/PRO_0000390485 http://togogenome.org/gene/10090:Slc5a12 ^@ http://purl.uniprot.org/uniprot/B9EJ03|||http://purl.uniprot.org/uniprot/Q49B93 ^@ 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|||Sodium-coupled monocarboxylate transporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000337681|||http://purl.uniprot.org/annotation/VSP_033996 http://togogenome.org/gene/10090:Htr1d ^@ http://purl.uniprot.org/uniprot/Q61224 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 5-hydroxytryptamine receptor 1D|||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_0000068928 http://togogenome.org/gene/10090:Habp4 ^@ http://purl.uniprot.org/uniprot/E9QKB2|||http://purl.uniprot.org/uniprot/Q3UJC1|||http://purl.uniprot.org/uniprot/Q9JKS5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||Hyaluronan/mRNA-binding protein|||Intracellular hyaluronan-binding protein 4|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine; by PKC ^@ http://purl.uniprot.org/annotation/PRO_0000257973 http://togogenome.org/gene/10090:Pcdha2 ^@ http://purl.uniprot.org/uniprot/Q05C01|||http://purl.uniprot.org/uniprot/Q91Y17 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5004164627|||http://purl.uniprot.org/annotation/PRO_5015099511 http://togogenome.org/gene/10090:Acss1 ^@ http://purl.uniprot.org/uniprot/Q3UJ89|||http://purl.uniprot.org/uniprot/Q69Z91|||http://purl.uniprot.org/uniprot/Q99NB1 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Transit Peptide ^@ AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Acetyl-coenzyme A synthetase 2-like, mitochondrial|||Acetyl-coenzyme A synthetase N-terminal|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000000597 http://togogenome.org/gene/10090:Dync2h1 ^@ http://purl.uniprot.org/uniprot/Q45VK7 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Cytoplasmic dynein 2 heavy chain 1|||In isoform 2.|||In isoform 3.|||In lln mutant; loss of function.|||Loss of function.|||Stalk|||Stem ^@ http://purl.uniprot.org/annotation/PRO_0000318744|||http://purl.uniprot.org/annotation/VSP_031284|||http://purl.uniprot.org/annotation/VSP_031285|||http://purl.uniprot.org/annotation/VSP_031286 http://togogenome.org/gene/10090:Icam1 ^@ http://purl.uniprot.org/uniprot/P13597|||http://purl.uniprot.org/uniprot/Q3U8M7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cell attachment site|||Cell attachment site; atypical|||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|||Ig-like C2-type 5|||Ig-like domain-containing protein|||In isoform 2.|||Intercellular adhesion molecule 1|||N-linked (GlcNAc...) asparagine|||Not glycosylated ^@ http://purl.uniprot.org/annotation/PRO_0000014785|||http://purl.uniprot.org/annotation/PRO_5010843394|||http://purl.uniprot.org/annotation/VSP_002518 http://togogenome.org/gene/10090:Timm10b ^@ http://purl.uniprot.org/uniprot/Q9WV96 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Disulfide Bond|||Motif|||Sequence Conflict ^@ Mitochondrial import inner membrane translocase subunit Tim10 B|||Twin CX3C motif ^@ http://purl.uniprot.org/annotation/PRO_0000193599 http://togogenome.org/gene/10090:Nap1l2 ^@ http://purl.uniprot.org/uniprot/P51860 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Nuclear localization signal|||Nucleosome assembly protein 1-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000185656 http://togogenome.org/gene/10090:Hykk ^@ http://purl.uniprot.org/uniprot/Q5U5V2 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Sequence Conflict|||Splice Variant ^@ Hydroxylysine kinase|||In isoform 2.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000326045|||http://purl.uniprot.org/annotation/VSP_032521|||http://purl.uniprot.org/annotation/VSP_032522 http://togogenome.org/gene/10090:Gfus ^@ http://purl.uniprot.org/uniprot/P23591|||http://purl.uniprot.org/uniprot/Q5HZI6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Site ^@ GDP-L-fucose synthase|||Important for catalytic activity|||In allele TUM-.|||Lowers pKa of active site Tyr|||NAD-dependent epimerase/dehydratase|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000174351 http://togogenome.org/gene/10090:Ralgps1 ^@ http://purl.uniprot.org/uniprot/A2AR50 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||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_0000333193|||http://purl.uniprot.org/annotation/VSP_033482|||http://purl.uniprot.org/annotation/VSP_033483|||http://purl.uniprot.org/annotation/VSP_033484|||http://purl.uniprot.org/annotation/VSP_033485|||http://purl.uniprot.org/annotation/VSP_033486 http://togogenome.org/gene/10090:Myo5c ^@ http://purl.uniprot.org/uniprot/E9Q1F5 ^@ Binding Site|||Coiled-Coil|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Domain Extent|||Region ^@ Actin-binding|||Dilute|||Myosin N-terminal SH3-like|||Myosin motor ^@ http://togogenome.org/gene/10090:6430571L13Rik ^@ http://purl.uniprot.org/uniprot/Q14AT3|||http://purl.uniprot.org/uniprot/Q8BGK9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Uncharacterized protein C3orf18 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000228842 http://togogenome.org/gene/10090:1110059G10Rik ^@ http://purl.uniprot.org/uniprot/Q8K039 ^@ 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|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Uncharacterized protein KIAA1143 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000248339 http://togogenome.org/gene/10090:Pcdhb21 ^@ http://purl.uniprot.org/uniprot/Q91V48 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099498 http://togogenome.org/gene/10090:Tpr ^@ http://purl.uniprot.org/uniprot/F6ZDS4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||N6-acetyllysine|||Necessary for association to the NPC|||Necessary for interaction with HSF1|||Nucleoprotein TPR|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Sufficient and essential for mediating its nuclear import|||Sufficient for interaction with TPR ^@ http://purl.uniprot.org/annotation/PRO_0000422100 http://togogenome.org/gene/10090:Cd40lg ^@ http://purl.uniprot.org/uniprot/P27548|||http://purl.uniprot.org/uniprot/Q0VEI3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ CD40 ligand, membrane form|||CD40 ligand, soluble form|||Cleavage|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||TNF family profile ^@ http://purl.uniprot.org/annotation/PRO_0000034490|||http://purl.uniprot.org/annotation/PRO_0000034491 http://togogenome.org/gene/10090:Fhip1b ^@ http://purl.uniprot.org/uniprot/A0A1C7CYU5|||http://purl.uniprot.org/uniprot/Q3U2I3 ^@ 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|||FHF complex subunit HOOK-interacting protein 1B|||FHF complex subunit HOOK-interacting protein C-terminal|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000253860|||http://purl.uniprot.org/annotation/VSP_021132|||http://purl.uniprot.org/annotation/VSP_021133|||http://purl.uniprot.org/annotation/VSP_021134 http://togogenome.org/gene/10090:Rpsa ^@ http://purl.uniprot.org/uniprot/P14206 ^@ Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Site ^@ Cleavage; by ST3; site 1|||Cleavage; by ST3; site 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Interaction with PPP1R16B|||Laminin-binding|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||Small ribosomal subunit protein uS2|||[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_0000134359 http://togogenome.org/gene/10090:Ttc33 ^@ http://purl.uniprot.org/uniprot/Q9D6K7 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 33 ^@ http://purl.uniprot.org/annotation/PRO_0000287516|||http://purl.uniprot.org/annotation/VSP_025532|||http://purl.uniprot.org/annotation/VSP_025533 http://togogenome.org/gene/10090:Cdc45 ^@ http://purl.uniprot.org/uniprot/F8WJ72|||http://purl.uniprot.org/uniprot/Q3UI99|||http://purl.uniprot.org/uniprot/Q9Z1X9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Cell division control protein 45 homolog|||Disordered|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000192816 http://togogenome.org/gene/10090:Aass ^@ http://purl.uniprot.org/uniprot/Q3UEQ9|||http://purl.uniprot.org/uniprot/Q99K67 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ 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_0000001053 http://togogenome.org/gene/10090:Rnf187 ^@ http://purl.uniprot.org/uniprot/Q8BFX1 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Crosslink|||Modified Residue|||Zinc Finger ^@ Asymmetric dimethylarginine; by PRMT1|||E3 ubiquitin-protein ligase RNF187|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000278242 http://togogenome.org/gene/10090:Cldn8 ^@ http://purl.uniprot.org/uniprot/Q3UZK2|||http://purl.uniprot.org/uniprot/Q9Z260 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Claudin-8|||Cytoplasmic|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Interactions with TJP1, TJP2 and TJP3|||Resistant to KLHL3-dependent protein degradation. ^@ http://purl.uniprot.org/annotation/PRO_0000144754 http://togogenome.org/gene/10090:Slc4a1 ^@ http://purl.uniprot.org/uniprot/P04919|||http://purl.uniprot.org/uniprot/Q3TZ29|||http://purl.uniprot.org/uniprot/Q53ZN9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Band 3 anion transport protein|||Band 3 cytoplasmic|||Bicarbonate transporter-like transmembrane|||Cytoplasmic|||Dimerization arm|||Discontinuously helical|||Discontinuously helical; Name=10|||Discontinuously helical; Name=3|||Disordered|||Extracellular|||Globular|||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.|||Interaction with ANK1|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000079210|||http://purl.uniprot.org/annotation/VSP_000454 http://togogenome.org/gene/10090:Med22 ^@ http://purl.uniprot.org/uniprot/Q62276 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Mediator of RNA polymerase II transcription subunit 22 ^@ http://purl.uniprot.org/annotation/PRO_0000178839|||http://purl.uniprot.org/annotation/VSP_028993|||http://purl.uniprot.org/annotation/VSP_028994 http://togogenome.org/gene/10090:Defa30 ^@ http://purl.uniprot.org/uniprot/E9QPZ2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Mammalian defensins ^@ http://purl.uniprot.org/annotation/PRO_5003246454 http://togogenome.org/gene/10090:Elovl5 ^@ http://purl.uniprot.org/uniprot/Q8BHI7 ^@ 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|||Elongation of very long chain fatty acids protein 5|||Helical|||N-acetylmethionine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000282840 http://togogenome.org/gene/10090:Tfcp2 ^@ http://purl.uniprot.org/uniprot/Q9ERA0 ^@ 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 ^@ Alpha-globin transcription factor CP2|||Basic and acidic residues|||DNA-binding|||Disordered|||Grh/CP2 DB|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000228002|||http://purl.uniprot.org/annotation/VSP_017649|||http://purl.uniprot.org/annotation/VSP_017650 http://togogenome.org/gene/10090:Wdr72 ^@ http://purl.uniprot.org/uniprot/D3YYM4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Disordered|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 72 ^@ http://purl.uniprot.org/annotation/PRO_0000438188 http://togogenome.org/gene/10090:Amn1 ^@ http://purl.uniprot.org/uniprot/B8JKV0 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein AMN1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000451143 http://togogenome.org/gene/10090:Sort1 ^@ http://purl.uniprot.org/uniprot/Q6PHU5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ BNR 1|||BNR 2|||BNR 3|||BNR 4|||BNR 5|||BNR 6|||BNR 7|||BNR 8|||BNR 9|||Basic and acidic residues|||Cytoplasmic|||DXXLL motif involved in the interaction with GGA1|||Disordered|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Removed in mature form|||S-palmitoyl cysteine|||Sortilin ^@ http://purl.uniprot.org/annotation/PRO_0000045155|||http://purl.uniprot.org/annotation/PRO_0000436377|||http://purl.uniprot.org/annotation/VSP_016650 http://togogenome.org/gene/10090:Agxt ^@ http://purl.uniprot.org/uniprot/O35423|||http://purl.uniprot.org/uniprot/Q3UEN9 ^@ 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|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Alanine--glyoxylate aminotransferase|||Aminotransferase class V|||In isoform Peroxisomal.|||Microbody targeting signal|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000001288|||http://purl.uniprot.org/annotation/VSP_018644 http://togogenome.org/gene/10090:Epha4 ^@ http://purl.uniprot.org/uniprot/Q03137 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 4|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform Short.|||Kinase dead; loss of autophosphorylation and loss of CHN1 phosphorylation. No effect on interaction with NGEF.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000016808|||http://purl.uniprot.org/annotation/VSP_002998 http://togogenome.org/gene/10090:Yae1d1 ^@ http://purl.uniprot.org/uniprot/Q9DAY6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Essential protein Yae1 N-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Kin ^@ http://purl.uniprot.org/uniprot/Q8K339 ^@ 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 ^@ C-terminal subdomain A|||C-terminal subdomain B|||C2H2-type|||DNA/RNA-binding protein KIN17|||Disordered|||N6,N6,N6-trimethyllysine; by METTL22; alternate|||N6-methyllysine; alternate|||Polar residues|||Winged helix-turn-helix (wHTH) ^@ http://purl.uniprot.org/annotation/PRO_0000289135 http://togogenome.org/gene/10090:Homer1 ^@ http://purl.uniprot.org/uniprot/Q3UVL6|||http://purl.uniprot.org/uniprot/Q5D052|||http://purl.uniprot.org/uniprot/Q9Z2Y3 ^@ 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 ^@ Disordered|||Homer protein homolog 1|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||N-acetylglycine|||Phosphoserine|||Polar residues|||Removed|||Required for tetramerization|||WH1 ^@ http://purl.uniprot.org/annotation/PRO_0000191006|||http://purl.uniprot.org/annotation/VSP_009060|||http://purl.uniprot.org/annotation/VSP_009061|||http://purl.uniprot.org/annotation/VSP_009062|||http://purl.uniprot.org/annotation/VSP_009063|||http://purl.uniprot.org/annotation/VSP_009064|||http://purl.uniprot.org/annotation/VSP_009065 http://togogenome.org/gene/10090:Slc35b4 ^@ http://purl.uniprot.org/uniprot/Q8CIA5 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Motif|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Mediates endoplasmic reticulum retention|||Nucleotide sugar transporter SLC35B4 ^@ http://purl.uniprot.org/annotation/PRO_0000213387|||http://purl.uniprot.org/annotation/VSP_016203 http://togogenome.org/gene/10090:Pilrb2 ^@ http://purl.uniprot.org/uniprot/Q2YFS1 ^@ 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|||Paired immunoglobulin-like type 2 receptor beta-2 ^@ http://purl.uniprot.org/annotation/PRO_0000226825 http://togogenome.org/gene/10090:Engase ^@ http://purl.uniprot.org/uniprot/Q8BX80 ^@ 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 ^@ BRCT|||Basic and acidic residues|||Cytosolic endo-beta-N-acetylglucosaminidase|||Disordered|||In isoform 2.|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000328868|||http://purl.uniprot.org/annotation/VSP_039763|||http://purl.uniprot.org/annotation/VSP_039764 http://togogenome.org/gene/10090:Lgals3bp ^@ http://purl.uniprot.org/uniprot/Q07797 ^@ 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 ^@ BACK|||BTB|||Galectin-3-binding protein|||N-linked (GlcNAc...) asparagine|||SRCR ^@ http://purl.uniprot.org/annotation/PRO_0000357035 http://togogenome.org/gene/10090:Supt3 ^@ http://purl.uniprot.org/uniprot/Q8BVY4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Pak1ip1 ^@ http://purl.uniprot.org/uniprot/Q9DCE5 ^@ 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|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||p21-activated protein kinase-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000051126 http://togogenome.org/gene/10090:Or4c123 ^@ http://purl.uniprot.org/uniprot/Q8VG58 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mkx ^@ http://purl.uniprot.org/uniprot/B2RQ30|||http://purl.uniprot.org/uniprot/Q8BIA3 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Homeobox protein Mohawk|||Homeobox; TALE-type|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000268857 http://togogenome.org/gene/10090:Tacc2 ^@ http://purl.uniprot.org/uniprot/E9Q8T1|||http://purl.uniprot.org/uniprot/E9Q9Z4|||http://purl.uniprot.org/uniprot/E9QL08|||http://purl.uniprot.org/uniprot/Q3UL40|||http://purl.uniprot.org/uniprot/Q9JJG0 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 4.|||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_0000179989|||http://purl.uniprot.org/annotation/VSP_022159|||http://purl.uniprot.org/annotation/VSP_022160|||http://purl.uniprot.org/annotation/VSP_022161|||http://purl.uniprot.org/annotation/VSP_022162|||http://purl.uniprot.org/annotation/VSP_022163|||http://purl.uniprot.org/annotation/VSP_022164|||http://purl.uniprot.org/annotation/VSP_022165 http://togogenome.org/gene/10090:Klhl41 ^@ http://purl.uniprot.org/uniprot/A2AUC9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict ^@ BACK|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch-like protein 41|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000421252 http://togogenome.org/gene/10090:Tpgs1 ^@ http://purl.uniprot.org/uniprot/Q99MS8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Phosphoserine|||Tubulin polyglutamylase complex subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000249317 http://togogenome.org/gene/10090:Pcolce2 ^@ http://purl.uniprot.org/uniprot/Q8R4W6 ^@ 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 ^@ CUB 1|||CUB 2|||N-linked (GlcNAc...) asparagine|||NTR|||Procollagen C-endopeptidase enhancer 2 ^@ http://purl.uniprot.org/annotation/PRO_0000022021 http://togogenome.org/gene/10090:Ankrd1 ^@ http://purl.uniprot.org/uniprot/Q9CR42 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 1|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000240480 http://togogenome.org/gene/10090:Sec14l4 ^@ http://purl.uniprot.org/uniprot/Q8R0F9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ CRAL-TRIO|||GOLD|||SEC14-like protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000210761 http://togogenome.org/gene/10090:Zfp143 ^@ http://purl.uniprot.org/uniprot/O70230 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Crosslink|||Modified Residue|||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|||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_0000248071|||http://purl.uniprot.org/annotation/VSP_036979|||http://purl.uniprot.org/annotation/VSP_036980 http://togogenome.org/gene/10090:Dcpp2 ^@ http://purl.uniprot.org/uniprot/E9PYC2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Jacalin-type lectin ^@ http://purl.uniprot.org/annotation/PRO_5015090358 http://togogenome.org/gene/10090:Cptp ^@ http://purl.uniprot.org/uniprot/Q8BS40 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Turn ^@ Binding Site|||Chain|||Helix|||Sequence Conflict|||Turn ^@ Ceramide-1-phosphate transfer protein ^@ http://purl.uniprot.org/annotation/PRO_0000317157 http://togogenome.org/gene/10090:Galnt7 ^@ http://purl.uniprot.org/uniprot/Q3U8I4|||http://purl.uniprot.org/uniprot/Q80VA0 ^@ Binding 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 3.|||Lumenal|||N-acetylgalactosaminyltransferase 7|||Ricin B lectin|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059117|||http://purl.uniprot.org/annotation/VSP_011204|||http://purl.uniprot.org/annotation/VSP_011205 http://togogenome.org/gene/10090:Ptpn18 ^@ http://purl.uniprot.org/uniprot/Q61152 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphocysteine intermediate|||Phosphotyrosine|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 18 ^@ http://purl.uniprot.org/annotation/PRO_0000094774 http://togogenome.org/gene/10090:Mup1 ^@ http://purl.uniprot.org/uniprot/A2CEL0|||http://purl.uniprot.org/uniprot/A2CEL1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5002642946|||http://purl.uniprot.org/annotation/PRO_5015086047 http://togogenome.org/gene/10090:Klhl35 ^@ http://purl.uniprot.org/uniprot/Q9CZ49 ^@ 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 35 ^@ http://purl.uniprot.org/annotation/PRO_0000344467 http://togogenome.org/gene/10090:Chid1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J058|||http://purl.uniprot.org/uniprot/A0A0R4J242|||http://purl.uniprot.org/uniprot/Q922Q9 ^@ 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 ^@ Chitinase domain-containing protein 1|||GH18|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000280609|||http://purl.uniprot.org/annotation/PRO_5006451947|||http://purl.uniprot.org/annotation/PRO_5015044306|||http://purl.uniprot.org/annotation/VSP_023827 http://togogenome.org/gene/10090:Slc25a54 ^@ http://purl.uniprot.org/uniprot/B1AUS6 ^@ Domain Extent|||Region|||Repeat ^@ Domain Extent|||Repeat ^@ EF-hand|||Solcar ^@ http://togogenome.org/gene/10090:Nt5c3 ^@ http://purl.uniprot.org/uniprot/Q9D020 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Cytosolic 5'-nucleotidase 3A|||In isoform 1.|||Nucleophile|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000064388|||http://purl.uniprot.org/annotation/VSP_021566 http://togogenome.org/gene/10090:Dhodh ^@ http://purl.uniprot.org/uniprot/O35435 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Dihydroorotate dehydrogenase (quinone), mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion; not cleaved|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000029885 http://togogenome.org/gene/10090:Dio3 ^@ http://purl.uniprot.org/uniprot/Q91ZI8 ^@ Active Site|||Chain|||Helix|||Modification|||Molecule Processing|||Non standard residue|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Chain|||Helix|||Non standard residue|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Selenocysteine|||Thyroxine 5-deiodinase ^@ http://purl.uniprot.org/annotation/PRO_0000154324 http://togogenome.org/gene/10090:Gm4787 ^@ http://purl.uniprot.org/uniprot/B2RUD9 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Disintegrin|||EGF-like|||Helical|||Peptidase M12B ^@ http://purl.uniprot.org/annotation/PRO_5015087155 http://togogenome.org/gene/10090:Samd4 ^@ http://purl.uniprot.org/uniprot/A0A2D0VMX2|||http://purl.uniprot.org/uniprot/Q8CBY1 ^@ 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.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein Smaug homolog 1|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000097572|||http://purl.uniprot.org/annotation/VSP_037781|||http://purl.uniprot.org/annotation/VSP_037782|||http://purl.uniprot.org/annotation/VSP_037783 http://togogenome.org/gene/10090:Olfml2b ^@ http://purl.uniprot.org/uniprot/Q3V1G4|||http://purl.uniprot.org/uniprot/Q8BY24 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Olfactomedin-like protein 2B|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000311427|||http://purl.uniprot.org/annotation/PRO_5004307255 http://togogenome.org/gene/10090:C1d ^@ http://purl.uniprot.org/uniprot/O35473 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Region|||Sequence Conflict ^@ 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_0000316301 http://togogenome.org/gene/10090:Tmem209 ^@ http://purl.uniprot.org/uniprot/Q8BRG8|||http://purl.uniprot.org/uniprot/Q8C214 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Transmembrane protein 209 ^@ http://purl.uniprot.org/annotation/PRO_0000331633|||http://purl.uniprot.org/annotation/VSP_033284|||http://purl.uniprot.org/annotation/VSP_033285|||http://purl.uniprot.org/annotation/VSP_033286 http://togogenome.org/gene/10090:Cd209e ^@ http://purl.uniprot.org/uniprot/Q3KNN8|||http://purl.uniprot.org/uniprot/Q91ZW7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Topological Domain|||Transmembrane ^@ C-type lectin|||CD209 antigen-like protein E|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein ^@ http://purl.uniprot.org/annotation/PRO_0000046608 http://togogenome.org/gene/10090:Prr29 ^@ http://purl.uniprot.org/uniprot/A0A087WQH2|||http://purl.uniprot.org/uniprot/B1ARI9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ DUF4587|||Disordered|||In isoform 2.|||Pro residues|||Proline-rich protein 29 ^@ http://purl.uniprot.org/annotation/PRO_0000344469|||http://purl.uniprot.org/annotation/VSP_034786 http://togogenome.org/gene/10090:Ctla2b ^@ http://purl.uniprot.org/uniprot/A0A0R4J245|||http://purl.uniprot.org/uniprot/P12400 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||2 X 3 AA tandem repeats of E-W-K|||Cathepsin propeptide inhibitor|||Protein CTLA-2-beta ^@ http://purl.uniprot.org/annotation/PRO_0000026486 http://togogenome.org/gene/10090:Anxa1 ^@ http://purl.uniprot.org/uniprot/P10107 ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Peptide|||Repeat|||Sequence Conflict|||Site ^@ 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|||Phosphoserine|||Phosphoserine; by PKC|||Phosphoserine; by TRPM7|||Phosphothreonine|||Phosphotyrosine|||Removed|||Strongly decreased sumoylation. ^@ http://purl.uniprot.org/annotation/PRO_0000067461|||http://purl.uniprot.org/annotation/PRO_0000454557 http://togogenome.org/gene/10090:Jakmip1 ^@ http://purl.uniprot.org/uniprot/Q8BVL9 ^@ 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|||Janus kinase and microtubule-interacting protein 1|||Mediates association with microtubules|||Mediates interaction with TYK2 and GABBR1|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000323009 http://togogenome.org/gene/10090:Ano7 ^@ http://purl.uniprot.org/uniprot/Q14AT5 ^@ 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 ^@ Anoctamin-7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000289327|||http://purl.uniprot.org/annotation/VSP_026009|||http://purl.uniprot.org/annotation/VSP_026010 http://togogenome.org/gene/10090:Cyp4a14 ^@ http://purl.uniprot.org/uniprot/O35728 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Propeptide|||Sequence Conflict ^@ Cytochrome P450 4A14|||Phosphoserine|||Removed in mature form|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000046058|||http://purl.uniprot.org/annotation/PRO_0000046059 http://togogenome.org/gene/10090:Llcfc1 ^@ http://purl.uniprot.org/uniprot/Q9D9P8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Sperm-egg fusion protein LLCFC1 ^@ http://purl.uniprot.org/annotation/PRO_0000352881 http://togogenome.org/gene/10090:Gm11545 ^@ http://purl.uniprot.org/uniprot/Q3TDT7 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 92 ^@ http://purl.uniprot.org/annotation/PRO_5010843262 http://togogenome.org/gene/10090:Uroc1 ^@ http://purl.uniprot.org/uniprot/Q3UEL5|||http://purl.uniprot.org/uniprot/Q8VC12 ^@ 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 ^@ N6-succinyllysine|||Urocanase C-terminal|||Urocanase N-terminal|||Urocanase Rossmann-like|||Urocanate hydratase ^@ http://purl.uniprot.org/annotation/PRO_0000207375 http://togogenome.org/gene/10090:Spart ^@ http://purl.uniprot.org/uniprot/Q3TVW1|||http://purl.uniprot.org/uniprot/Q8R1X6 ^@ 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 ubiquitin)|||In isoform 2.|||MIT|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||Senescence|||Spartin ^@ http://purl.uniprot.org/annotation/PRO_0000072120|||http://purl.uniprot.org/annotation/VSP_010934 http://togogenome.org/gene/10090:Sycn ^@ http://purl.uniprot.org/uniprot/Q8VCK7 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Sequence Conflict|||Signal Peptide ^@ Syncollin ^@ http://purl.uniprot.org/annotation/PRO_0000072357 http://togogenome.org/gene/10090:Pom121l12 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSJ4 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Rab11fip4 ^@ http://purl.uniprot.org/uniprot/Q8BQP8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||EF-hand|||FIP-RBD|||Necessary for interaction with RAB11A, subcellular location, homo- or heterooligomerization|||Polar residues|||Rab11 family-interacting protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000073881 http://togogenome.org/gene/10090:Or5j3 ^@ http://purl.uniprot.org/uniprot/Q8VGR8 ^@ 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 5J3 ^@ http://purl.uniprot.org/annotation/PRO_0000150865 http://togogenome.org/gene/10090:Mprip ^@ http://purl.uniprot.org/uniprot/P97434|||http://purl.uniprot.org/uniprot/Q5SWZ5 ^@ 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 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with F-actin|||Interaction with PPP1R12A|||Interaction with RHOA|||Loss of interaction with PPP1R12C and PPP1R12A.|||Myosin phosphatase Rho-interacting protein|||No effect.|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000223870|||http://purl.uniprot.org/annotation/VSP_017290|||http://purl.uniprot.org/annotation/VSP_017291|||http://purl.uniprot.org/annotation/VSP_017292|||http://purl.uniprot.org/annotation/VSP_017293 http://togogenome.org/gene/10090:Upk3b ^@ http://purl.uniprot.org/uniprot/A0A0R4J0S8|||http://purl.uniprot.org/uniprot/Q80YF6 ^@ 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|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Uroplakin-3b ^@ http://purl.uniprot.org/annotation/PRO_0000022641|||http://purl.uniprot.org/annotation/PRO_5006451987|||http://purl.uniprot.org/annotation/VSP_035890 http://togogenome.org/gene/10090:Gnptg ^@ http://purl.uniprot.org/uniprot/A0A0R4J0H5|||http://purl.uniprot.org/uniprot/A0A140T8R4|||http://purl.uniprot.org/uniprot/Q6S5C2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Signal Peptide|||Splice Variant ^@ Abolishes homodimerization. Abolishes homodimerization; when associated with S-84 and S-157.|||Abolishes homodimerization; when associated with S-157 and S-245. Does not affect homodimerization; when associated with S-157.|||Abolishes homodimerization; when associated with S-84 S-245.|||Abolishes localization to the Golgi apparatus; when associated with Q-115.|||Abolishes localization to the Golgi apparatus; when associated with Q-88.|||DMAP1-binding|||Does not affect homodimerization.|||In isoform 2.|||Interchain|||MRH|||N-acetylglucosamine-1-phosphotransferase subunit gamma|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000019578|||http://purl.uniprot.org/annotation/PRO_5006451975|||http://purl.uniprot.org/annotation/PRO_5007305379|||http://purl.uniprot.org/annotation/VSP_014758 http://togogenome.org/gene/10090:Serinc2 ^@ http://purl.uniprot.org/uniprot/B2KFY0|||http://purl.uniprot.org/uniprot/E9Q7Q6|||http://purl.uniprot.org/uniprot/Q8C6D8|||http://purl.uniprot.org/uniprot/Q8K0E7 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||Serine incorporator 2 ^@ http://purl.uniprot.org/annotation/PRO_0000218969|||http://purl.uniprot.org/annotation/PRO_5004307327 http://togogenome.org/gene/10090:Tas2r105 ^@ http://purl.uniprot.org/uniprot/Q53Z46|||http://purl.uniprot.org/uniprot/Q9JKT4 ^@ 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|||In strain: BALB/c, C3H/He, CBA/Ca and DBA/2J.|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 105 ^@ http://purl.uniprot.org/annotation/PRO_0000082359 http://togogenome.org/gene/10090:Fndc5 ^@ http://purl.uniprot.org/uniprot/Q8K4Z2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type III domain-containing protein 5|||Fibronectin type-III|||Helical|||Irisin|||Microbody targeting signal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000328972|||http://purl.uniprot.org/annotation/PRO_0000415858 http://togogenome.org/gene/10090:Barhl1 ^@ http://purl.uniprot.org/uniprot/P63157 ^@ 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_0000048827 http://togogenome.org/gene/10090:Rbpj ^@ http://purl.uniprot.org/uniprot/A0A0J9YTV5|||http://purl.uniprot.org/uniprot/E9Q7W0|||http://purl.uniprot.org/uniprot/P31266|||http://purl.uniprot.org/uniprot/Q3U6F1|||http://purl.uniprot.org/uniprot/Q3UM17 ^@ 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 ^@ Beta-trefoil DNA-binding|||DNA-binding|||Decreased interaction with L3MBTL3.|||Disordered|||IPT/TIG|||In isoform 2.|||Loss of interaction with L3MBTL3.|||N6-acetyllysine|||No effect on interaction with L3MBTL3.|||RBP-J/Cbf11/Cbf12 DNA binding|||Recombining binding protein suppressor of hairless ^@ http://purl.uniprot.org/annotation/PRO_0000208568|||http://purl.uniprot.org/annotation/VSP_008392|||http://purl.uniprot.org/annotation/VSP_008393 http://togogenome.org/gene/10090:Zfp770 ^@ http://purl.uniprot.org/uniprot/Q8BIQ8 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 770 ^@ http://purl.uniprot.org/annotation/PRO_0000280437 http://togogenome.org/gene/10090:Gpatch4 ^@ http://purl.uniprot.org/uniprot/Q3TFK5 ^@ 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|||G patch domain-containing protein 4|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000287463|||http://purl.uniprot.org/annotation/VSP_025482 http://togogenome.org/gene/10090:Vmn1r24 ^@ http://purl.uniprot.org/uniprot/Q8R2D6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dmkn ^@ http://purl.uniprot.org/uniprot/E9Q2P1|||http://purl.uniprot.org/uniprot/E9QLW7|||http://purl.uniprot.org/uniprot/E9QLW8|||http://purl.uniprot.org/uniprot/Q6P253 ^@ 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 ^@ Dermokine|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000330765|||http://purl.uniprot.org/annotation/PRO_5003243338|||http://purl.uniprot.org/annotation/PRO_5003244801|||http://purl.uniprot.org/annotation/PRO_5003245829|||http://purl.uniprot.org/annotation/VSP_033107|||http://purl.uniprot.org/annotation/VSP_033108|||http://purl.uniprot.org/annotation/VSP_033109|||http://purl.uniprot.org/annotation/VSP_033110 http://togogenome.org/gene/10090:Mcm3ap ^@ http://purl.uniprot.org/uniprot/Q9WUU9 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||DNA primase|||Disordered|||FG-repeats|||Germinal-center associated nuclear protein|||N6-acetyllysine|||PCI|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096285 http://togogenome.org/gene/10090:Vmn1r85 ^@ http://purl.uniprot.org/uniprot/Q8VIB8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or2aj4 ^@ http://purl.uniprot.org/uniprot/Q7TS53 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gatd1 ^@ http://purl.uniprot.org/uniprot/Q8BFQ8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Glutamine amidotransferase-like class 1 domain-containing protein 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000305095 http://togogenome.org/gene/10090:Il7 ^@ http://purl.uniprot.org/uniprot/P10168|||http://purl.uniprot.org/uniprot/Q544C8 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Interleukin-7|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015624|||http://purl.uniprot.org/annotation/PRO_5014309616 http://togogenome.org/gene/10090:Fam149b ^@ http://purl.uniprot.org/uniprot/Q6NSV7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Polar residues|||Primary cilium assembly protein FAM149B1 ^@ http://purl.uniprot.org/annotation/PRO_0000319934|||http://purl.uniprot.org/annotation/VSP_031535|||http://purl.uniprot.org/annotation/VSP_031536|||http://purl.uniprot.org/annotation/VSP_031537|||http://purl.uniprot.org/annotation/VSP_031538|||http://purl.uniprot.org/annotation/VSP_031539|||http://purl.uniprot.org/annotation/VSP_031540|||http://purl.uniprot.org/annotation/VSP_031541|||http://purl.uniprot.org/annotation/VSP_031542 http://togogenome.org/gene/10090:Porcn ^@ http://purl.uniprot.org/uniprot/Q9JJJ7 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolished acyltransferase activity.|||Abolished acyltransferase activity. Impaired ability to interact with WNT3A.|||Cytoplasmic|||Does not affect acyltransferase activity.|||Extracellular|||Helical|||Impaired acyltransferase activity.|||Impaired acyltransferase activity. Impaired ability to interact with WNT3A.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Protein-serine O-palmitoleoyltransferase porcupine ^@ http://purl.uniprot.org/annotation/PRO_0000213138|||http://purl.uniprot.org/annotation/VSP_015889|||http://purl.uniprot.org/annotation/VSP_015890|||http://purl.uniprot.org/annotation/VSP_015891|||http://purl.uniprot.org/annotation/VSP_015892|||http://purl.uniprot.org/annotation/VSP_015893 http://togogenome.org/gene/10090:Diras1 ^@ http://purl.uniprot.org/uniprot/Q91Z61 ^@ 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|||GTP-binding protein Di-Ras1|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000191649|||http://purl.uniprot.org/annotation/PRO_0000370776 http://togogenome.org/gene/10090:Septin3 ^@ http://purl.uniprot.org/uniprot/Q9Z1S5 ^@ 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 ^@ Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform 2.|||Neuronal-specific septin-3|||Phosphoserine|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173518|||http://purl.uniprot.org/annotation/VSP_025400 http://togogenome.org/gene/10090:Or5l14 ^@ http://purl.uniprot.org/uniprot/A2AVC4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp692 ^@ http://purl.uniprot.org/uniprot/Q3U381 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Phosphoserine|||Polar residues|||Zinc finger protein 692 ^@ http://purl.uniprot.org/annotation/PRO_0000234015 http://togogenome.org/gene/10090:Or8b37 ^@ http://purl.uniprot.org/uniprot/Q7TRE1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or5v1 ^@ http://purl.uniprot.org/uniprot/A2RT31 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gsdmd ^@ http://purl.uniprot.org/uniprot/A0A679AXP3|||http://purl.uniprot.org/uniprot/Q9D8T2 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Transmembrane|||Turn ^@ Abolished ability to form a pore, leading to educed ability to induce pyroptosis.|||Abolished cleavage by CASP3 and CASP7.|||Abolished generation of the Gasdermin-D, p40 chain and ability to promote secretion of IL33.|||Beta stranded|||Cleavage; by CASP3 or CASP7|||Cleavage; by caspases CASP1, CASP4/CASP11 and CASP8|||Cleavage; by papain|||Complete loss of homooligomerization, lipid-binding, relocalization of Gasdermin-D, N-terminal to the plasma membrane and pyroptosis, as well as loss of bactericidal activity; when associated with A-138 or with S-138; A-146 and A-152. Partial loss of homooligomerization and pyroptosis; when associated with A-152 or with A-146 and A-152.|||Complete loss of homooligomerization, lipid-binding, relocalization of Gasdermin-D, N-terminal to the plasma membrane and pyroptosis, as well as loss of bactericidal activity; when associated with A-138 or with S-138; A-146 and A-154. Partial loss of homooligomerization and pyroptosis; when associated with A-146 or with A-154, or with A-146 and A-154.|||Complete loss of homooligomerization, lipid-binding, relocalization of Gasdermin-D, N-terminal to the plasma membrane and pyroptosis, as well as loss of bactericidal activity; when associated with A-138 or with S-138; A-152 and A-154. Partial loss of homooligomerization and pyroptosis; when associated with A-138, with A-152 or with A-152 and A-154.|||Complete loss of homooligomerization, lipid-binding, relocalization of Gasdermin-D, N-terminal to the plasma membrane and pyroptosis, as well as loss of bactericidal activity; when associated with A-146; A-152 and A-154. Partial loss of homooligomerization and pyroptosis; when associated with A-146.|||Disrupts intramolecular interactions and autoinhibition, leading to spontaneous pyroptosis-inducing activity.|||Gasdermin PUB|||Gasdermin pore forming|||Gasdermin-D|||Gasdermin-D, C-terminal|||Gasdermin-D, N-terminal|||Gasdermin-D, p13|||Gasdermin-D, p40|||Impaired interaction and cleavage by CASP1.|||In 5A mutant; abolished interaction with CASP1; when associated with 306-L--L310.|||In 5A mutant; abolished interaction with CASP1; when associated with 361-L--L370.|||Linker helix loop|||Loss of CASP1-induced cleavage, pyroptosis and IL1B release. Does not impair interaction with CASP1. Loss of CASP4/CASP11-induced cleavage. Abolished ability to induce pyroptosis following inactivation of MAP3K7/TAK1 by Yersinia toxin YopJ.|||Loss of oligomerization of Gasdermin-D, N-terminal.|||No effect on oligomerization.|||No effect on pyroptosis; when associated with A-237 or with A-237; A-248 and A-249.|||No effect on pyroptosis; when associated with A-237; A-239 and A-248.|||No effect on pyroptosis; when associated with A-237; A-239 and A-249.|||No effect on pyroptosis; when associated with A-239 or with A-239; A-248 and A-249.|||Phosphotyrosine|||Reduced ability to induce pyroptosis.|||Reduced ability to induce pyroptosis. No effect on protein expression. No effect on cleavage by CASP4.|||Reduced ability to induct pyroptosis.|||Reduced homoolimerization, leading to reduced ability to induce pyroptosis.|||Renders Gsdmd susceptible to ubiquitination by S.flexneri IpaH7.8.|||S-(2-succinyl)cysteine|||Spontaneous pyroptosis-inducing activity. ^@ http://purl.uniprot.org/annotation/PRO_0000148176|||http://purl.uniprot.org/annotation/PRO_0000437528|||http://purl.uniprot.org/annotation/PRO_0000437529|||http://purl.uniprot.org/annotation/PRO_0000459019|||http://purl.uniprot.org/annotation/PRO_0000459020 http://togogenome.org/gene/10090:Il17d ^@ http://purl.uniprot.org/uniprot/A0A0B4J1G4|||http://purl.uniprot.org/uniprot/Q8K4C4 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Region|||Signal Peptide ^@ Disordered ^@ http://purl.uniprot.org/annotation/PRO_5002105529|||http://purl.uniprot.org/annotation/PRO_5004309113 http://togogenome.org/gene/10090:Ccdc157 ^@ http://purl.uniprot.org/uniprot/Q5SPX1 ^@ 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 157|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000319421|||http://purl.uniprot.org/annotation/VSP_031476 http://togogenome.org/gene/10090:Mt3 ^@ http://purl.uniprot.org/uniprot/P28184|||http://purl.uniprot.org/uniprot/Q3USP9 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Modified Residue|||Region|||Strand|||Turn ^@ Alpha|||Beta|||Metallothionein-3|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000197251 http://togogenome.org/gene/10090:Dclk1 ^@ http://purl.uniprot.org/uniprot/A3KN70|||http://purl.uniprot.org/uniprot/A8IP62|||http://purl.uniprot.org/uniprot/H7BX36|||http://purl.uniprot.org/uniprot/Q80VB6|||http://purl.uniprot.org/uniprot/Q8BRN4|||http://purl.uniprot.org/uniprot/Q8CCN4|||http://purl.uniprot.org/uniprot/Q9JLM6|||http://purl.uniprot.org/uniprot/Q9JLM8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Doublecortin|||Doublecortin 1|||Doublecortin 2|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase DCLK1 ^@ http://purl.uniprot.org/annotation/PRO_0000085920|||http://purl.uniprot.org/annotation/VSP_019593|||http://purl.uniprot.org/annotation/VSP_019594 http://togogenome.org/gene/10090:Cavin3 ^@ http://purl.uniprot.org/uniprot/Q91VJ2 ^@ 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 ^@ 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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000331413 http://togogenome.org/gene/10090:Mageb11 ^@ http://purl.uniprot.org/uniprot/G3UW88 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Tmem255b ^@ http://purl.uniprot.org/uniprot/G3UWB7|||http://purl.uniprot.org/uniprot/G5E908|||http://purl.uniprot.org/uniprot/Q5FW56 ^@ 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|||Polar residues|||Transmembrane protein 255B ^@ http://purl.uniprot.org/annotation/PRO_0000266043 http://togogenome.org/gene/10090:Rnf43 ^@ http://purl.uniprot.org/uniprot/A3KMI3|||http://purl.uniprot.org/uniprot/Q5NCP0 ^@ 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|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Basic residues|||Cytoplasmic|||Disordered|||E3 ubiquitin-protein ligase RNF43|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||RING-type|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000278240|||http://purl.uniprot.org/annotation/VSP_023203|||http://purl.uniprot.org/annotation/VSP_023204|||http://purl.uniprot.org/annotation/VSP_023205 http://togogenome.org/gene/10090:Coa8 ^@ http://purl.uniprot.org/uniprot/Q9CQW7 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant|||Transit Peptide ^@ Chain|||Splice Variant|||Transit Peptide ^@ Cytochrome c oxidase assembly factor 8|||In isoform 2.|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000353108|||http://purl.uniprot.org/annotation/VSP_041973 http://togogenome.org/gene/10090:Nebl ^@ http://purl.uniprot.org/uniprot/Q9DC07 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Modified Residue|||Repeat ^@ LIM zinc-binding|||LIM zinc-binding domain-containing Nebulette|||Nebulin 1|||Nebulin 2|||Nebulin 3|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000417585 http://togogenome.org/gene/10090:Dlx5 ^@ http://purl.uniprot.org/uniprot/P70396|||http://purl.uniprot.org/uniprot/Q3TYA7 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Homeobox|||Homeobox protein DLX-5|||In isoform 2.|||In isoform 3.|||Inhibits its transcriptional activity; when associated with A-217.|||Inhibits its transcriptional activity; when associated with A-34.|||Phosphoserine; by MAPK14; in vitro|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049032|||http://purl.uniprot.org/annotation/VSP_002237|||http://purl.uniprot.org/annotation/VSP_002238|||http://purl.uniprot.org/annotation/VSP_002239 http://togogenome.org/gene/10090:Mboat1 ^@ http://purl.uniprot.org/uniprot/Q8BH98 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Lysophospholipid acyltransferase 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000273019 http://togogenome.org/gene/10090:Usp4 ^@ http://purl.uniprot.org/uniprot/A0A0A6YW28|||http://purl.uniprot.org/uniprot/P35123|||http://purl.uniprot.org/uniprot/Q3TPN5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ DUSP|||Disordered|||Interacts with DUSP and ubiquitin-like 1 domains and is required for USP4 activation|||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|||Polar residues|||Proton acceptor|||Reduces nuclear localization.|||Reduces the interaction with RB1.|||Regulates ubiquitin dissociation|||Required for USP4 activation by providing conformational flexibility between the DUSP and catalytic domains|||USP|||Ubiquitin carboxyl-terminal hydrolase 4|||Ubiquitin-like 1|||Ubiquitin-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000080622 http://togogenome.org/gene/10090:Arsb ^@ http://purl.uniprot.org/uniprot/A0A0R4J138|||http://purl.uniprot.org/uniprot/P50429 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 3-oxoalanine (Cys)|||Arylsulfatase B|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Sulfatase N-terminal|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000033423|||http://purl.uniprot.org/annotation/PRO_5006452007|||http://purl.uniprot.org/annotation/VSP_007881|||http://purl.uniprot.org/annotation/VSP_022249 http://togogenome.org/gene/10090:Slamf6 ^@ http://purl.uniprot.org/uniprot/Q18PG5|||http://purl.uniprot.org/uniprot/Q18PJ0|||http://purl.uniprot.org/uniprot/Q9ET39 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreases inhibitory signaling in germinal center formation (absence of SH2D1A/SAP); when associated with F-295 and F-319.|||Decreases inhibitory signaling in germinal center formation (absence of SH2D1A/SAP); when associated with F-295 and F-349.|||Decreases inhibitory signaling in germinal center formation (absence of SH2D1A/SAP); when associated with F-319 and F-349.|||Disordered|||Extracellular|||Helical|||ITSM 1|||ITSM 2|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||SLAM family member 6|||Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP); when associated with F-295 and F-335.|||Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP); when associated with F-295 and F-349.|||Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP); when associated with F-319 and F-335.|||Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP); when associated with F-319 and F-349.|||Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP); when associated with F-335 and F-349. ^@ http://purl.uniprot.org/annotation/PRO_0000014962|||http://purl.uniprot.org/annotation/PRO_5015097041|||http://purl.uniprot.org/annotation/PRO_5015097042|||http://purl.uniprot.org/annotation/VSP_010404|||http://purl.uniprot.org/annotation/VSP_010405|||http://purl.uniprot.org/annotation/VSP_058034 http://togogenome.org/gene/10090:2610528J11Rik ^@ http://purl.uniprot.org/uniprot/Q9CQM1 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ 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_0000271011 http://togogenome.org/gene/10090:Spryd4 ^@ http://purl.uniprot.org/uniprot/Q91WK1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ B30.2/SPRY|||N6-acetyllysine|||N6-succinyllysine|||SPRY domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000240857 http://togogenome.org/gene/10090:Klk1b21 ^@ http://purl.uniprot.org/uniprot/Q3UNG6|||http://purl.uniprot.org/uniprot/Q61759 ^@ 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|||Kallikrein 1-related peptidase b21|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027987|||http://purl.uniprot.org/annotation/PRO_0000027988|||http://purl.uniprot.org/annotation/PRO_5014309220 http://togogenome.org/gene/10090:Gm2030 ^@ http://purl.uniprot.org/uniprot/D3Z7C4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:H2-T22 ^@ http://purl.uniprot.org/uniprot/Q31615|||http://purl.uniprot.org/uniprot/Q9BCZ1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097384|||http://purl.uniprot.org/annotation/PRO_5015099646 http://togogenome.org/gene/10090:Or13p8 ^@ http://purl.uniprot.org/uniprot/Q3KPC7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dnajb11 ^@ http://purl.uniprot.org/uniprot/Q99KV1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ DnaJ homolog subfamily B member 11|||J|||N-linked (GlcNAc...) asparagine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000007261 http://togogenome.org/gene/10090:Fads6 ^@ http://purl.uniprot.org/uniprot/Q80UG1 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Motif|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Fatty acid desaturase 6|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000341547|||http://purl.uniprot.org/annotation/VSP_034321 http://togogenome.org/gene/10090:Stim1 ^@ http://purl.uniprot.org/uniprot/P70302 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EF-hand|||Extracellular|||Helical|||Microtubule tip localization signal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM|||SOAR/CAD|||Stromal interaction molecule 1 ^@ http://purl.uniprot.org/annotation/PRO_0000033327 http://togogenome.org/gene/10090:Proc ^@ http://purl.uniprot.org/uniprot/P33587 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||Activation peptide|||Charge relay system|||Cleavage; by thrombin|||EGF-like 1|||EGF-like 2|||Gla|||In strain: BALB/c.|||Interchain (between light and heavy chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||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_0000028112|||http://purl.uniprot.org/annotation/PRO_0000028113|||http://purl.uniprot.org/annotation/PRO_0000028114|||http://purl.uniprot.org/annotation/PRO_0000028115|||http://purl.uniprot.org/annotation/PRO_0000028116 http://togogenome.org/gene/10090:Lrrc46 ^@ http://purl.uniprot.org/uniprot/Q9DAP0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Leucine-rich repeat-containing protein 46|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000223921 http://togogenome.org/gene/10090:Or8g36 ^@ http://purl.uniprot.org/uniprot/Q9EQB7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fam20c ^@ http://purl.uniprot.org/uniprot/Q5MJS3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Abrogates kinase activity without affecting subcellular location.|||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|||Interchain|||Kinase domain|||Lumenal|||Mislocalization of the protein from Golgi apparatus to endoplasmic reticulum.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000297978|||http://purl.uniprot.org/annotation/PRO_0000433884 http://togogenome.org/gene/10090:Eva1a ^@ http://purl.uniprot.org/uniprot/Q91WM6 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Protein eva-1 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000278672 http://togogenome.org/gene/10090:Plrg1 ^@ http://purl.uniprot.org/uniprot/Q922V4 ^@ 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|||N-acetylmethionine|||Phosphoserine|||Pleiotropic regulator 1|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051134 http://togogenome.org/gene/10090:Pidd1 ^@ http://purl.uniprot.org/uniprot/Q9ERV7 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Site ^@ Cleavage; by autolysis|||Death|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||N-acetylalanine|||PIDD-C|||PIDD-CC|||PIDD-N|||Peptidase S68|||Phosphoserine|||Polar residues|||Removed|||UPA domain|||ZU5 1|||ZU5 2|||p53-induced death domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000245244|||http://purl.uniprot.org/annotation/PRO_0000445718|||http://purl.uniprot.org/annotation/PRO_0000445719|||http://purl.uniprot.org/annotation/PRO_0000445720 http://togogenome.org/gene/10090:Napsa ^@ http://purl.uniprot.org/uniprot/O09043|||http://purl.uniprot.org/uniprot/Q3U7H1 ^@ 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|||Region|||Signal Peptide ^@ Activation peptide|||Disordered|||N-linked (GlcNAc...) asparagine|||Napsin-A|||Peptidase A1|||Peptidase A1 domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000025998|||http://purl.uniprot.org/annotation/PRO_0000025999|||http://purl.uniprot.org/annotation/PRO_5009970820 http://togogenome.org/gene/10090:Tmco1 ^@ http://purl.uniprot.org/uniprot/Q3V4A0|||http://purl.uniprot.org/uniprot/Q921L3 ^@ Chain|||Coiled-Coil|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||INTRAMEM|||Modified Residue|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Calcium load-activated calcium channel|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000244077 http://togogenome.org/gene/10090:Nr3c1 ^@ http://purl.uniprot.org/uniprot/P06537 ^@ 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|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Chain|||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. 1-B.|||Abolishes glucocorticoid-mediated degradation and enhances transcription trans-activation.|||Abolishes transactivation activity.|||Abolishes transcriptional activity. Does not impair ligand binding.|||Disordered|||Does not change transactivation activity.|||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); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hinge|||In isoform 1-B and isoform 2-B.|||In isoform 2 and isoform 2-B.|||In isoform 3.|||Interaction with CLOCK|||Interaction with CRY1|||Modulating|||N6-acetyllysine|||NR C4-type|||NR LBD|||Nuclear receptor|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000019939|||http://purl.uniprot.org/annotation/VSP_003704|||http://purl.uniprot.org/annotation/VSP_018774|||http://purl.uniprot.org/annotation/VSP_058320|||http://purl.uniprot.org/annotation/VSP_058321 http://togogenome.org/gene/10090:Diaph3 ^@ http://purl.uniprot.org/uniprot/Q9Z207 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Abolished accumulation in the nucleus.|||Accumulation in the nucleus due to defects in nuclear export.|||Basic and acidic residues|||DAD|||Decreased accumulation in the nucleus.|||Disordered|||Does not affect subcellular location.|||FH1|||FH2|||GBD/FH3|||Impaired ability to release autoinhibition, leading to defects in actin nucleation and elongation factor activity in the nucleus.|||No loss of ubiquitination; when associated with R-118, R-119 and R-493.|||No loss of ubiquitination; when associated with R-118, R-119 and R-494.|||No loss of ubiquitination; when associated with R-118, R-493 and R-494.|||No loss of ubiquitination; when associated with R-119, R-493 and R-494.|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein diaphanous homolog 3 ^@ http://purl.uniprot.org/annotation/PRO_0000194898 http://togogenome.org/gene/10090:Orc1 ^@ http://purl.uniprot.org/uniprot/Q3TPY7|||http://purl.uniprot.org/uniprot/Q3UR71|||http://purl.uniprot.org/uniprot/Q9Z1N2 ^@ 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|||Site|||Strand|||Turn ^@ Acidic residues|||BAH|||Disordered|||Histone H4K20me2 binding|||Necessary and sufficient for ORC complex assembly|||Origin recognition complex subunit 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000127068 http://togogenome.org/gene/10090:Slfn3 ^@ http://purl.uniprot.org/uniprot/Q9Z0I5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Schlafen AlbA-2 ^@ http://togogenome.org/gene/10090:Commd1 ^@ http://purl.uniprot.org/uniprot/A2RSF1|||http://purl.uniprot.org/uniprot/Q8K4M5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ COMM|||COMM domain-containing protein 1|||Required for binding to PtdIns(4,5)P2|||Sufficient for interaction with SLC12A2 ^@ http://purl.uniprot.org/annotation/PRO_0000077385 http://togogenome.org/gene/10090:Ace3 ^@ http://purl.uniprot.org/uniprot/D0G895 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Angiotensin-converting enzyme-like protein Ace3|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M2 ^@ http://purl.uniprot.org/annotation/PRO_5008952182 http://togogenome.org/gene/10090:Tm7sf3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0K4|||http://purl.uniprot.org/uniprot/Q9CRG1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ DUF4203|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane 7 superfamily member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000022538|||http://purl.uniprot.org/annotation/PRO_5006451966 http://togogenome.org/gene/10090:Mtif2 ^@ http://purl.uniprot.org/uniprot/Q91YJ5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Transit Peptide ^@ G1|||G2|||G3|||G4|||G5|||Mitochondrion|||Phosphothreonine|||Translation initiation factor IF-2, mitochondrial|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000014481 http://togogenome.org/gene/10090:Ulk1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0B3|||http://purl.uniprot.org/uniprot/O70405|||http://purl.uniprot.org/uniprot/Q6PB82 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ C-terminal domain; mediates interaction with SESN2|||Disordered|||Does not affect phosphorylation by AMPK in vitro.|||Impairs interaction with AMPK and subsequent phosphorylation by AMPK.|||Impairs phosphorylation by AMPK and ability to promote autophagy; when associated with A-317.|||Impairs phosphorylation by AMPK and ability to promote autophagy; when associated with A-777.|||In K2R; abolished acetylation by KAT5/TIP60 and decreased kinase activity; when associated with R-162.|||In K2R; abolished acetylation by KAT5/TIP60 and decreased kinase activity; when associated with R-606.|||Interaction with GABARAP and GABARAPL2|||Loss of kinase activity and autophosphorylation.|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by MTOR|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase ULK1 ^@ http://purl.uniprot.org/annotation/PRO_0000086781 http://togogenome.org/gene/10090:Baat ^@ http://purl.uniprot.org/uniprot/Q91X34 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Bile acid-CoA:amino acid N-acyltransferase|||Charge relay system|||N6-succinyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000202160 http://togogenome.org/gene/10090:Shld1 ^@ http://purl.uniprot.org/uniprot/B2RR16|||http://purl.uniprot.org/uniprot/Q9D112 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Shieldin complex subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000286613 http://togogenome.org/gene/10090:Hrg ^@ http://purl.uniprot.org/uniprot/A0A0R4J039|||http://purl.uniprot.org/uniprot/Q9ESB3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Basic and acidic residues|||Basic residues|||Cleavage; by plasmin|||Cystatin|||Cystatin 1|||Cystatin 2|||Disordered|||Histidine-rich glycoprotein|||Interaction with ATP5F1A|||N-linked (GlcNAc...) asparagine|||Necessary for endothelial cell focal adhesions and anti-angiogenic activities|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000408507|||http://purl.uniprot.org/annotation/PRO_5006451934 http://togogenome.org/gene/10090:Ccnk ^@ http://purl.uniprot.org/uniprot/Q3U3M5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Cyclin C-terminal|||Cyclin-like|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Rflnb ^@ http://purl.uniprot.org/uniprot/Q5SVD0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Refilin-B ^@ http://purl.uniprot.org/annotation/PRO_0000264632 http://togogenome.org/gene/10090:Zbtb43 ^@ http://purl.uniprot.org/uniprot/G3X9N4|||http://purl.uniprot.org/uniprot/Q9DAI4 ^@ 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|||Basic and acidic residues|||C2H2-type|||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_0000047520 http://togogenome.org/gene/10090:Galr1 ^@ http://purl.uniprot.org/uniprot/P56479 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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_0000069464 http://togogenome.org/gene/10090:Srarp ^@ http://purl.uniprot.org/uniprot/Q3ULG3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Steroid receptor-associated and regulated protein ^@ http://purl.uniprot.org/annotation/PRO_0000442318 http://togogenome.org/gene/10090:Aspa ^@ http://purl.uniprot.org/uniprot/Q8R3P0 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Aspartoacylase ^@ http://purl.uniprot.org/annotation/PRO_0000216873 http://togogenome.org/gene/10090:Ms4a4b ^@ http://purl.uniprot.org/uniprot/Q9ES61 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Dnph1 ^@ http://purl.uniprot.org/uniprot/Q80VJ3 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ 2'-deoxynucleoside 5'-phosphate N-hydrolase 1|||N-acetylalanine|||Phosphoserine|||Removed|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000097201 http://togogenome.org/gene/10090:Faxc ^@ http://purl.uniprot.org/uniprot/Q3UMF9 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Failed axon connections homolog|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000417443 http://togogenome.org/gene/10090:Tmed3 ^@ http://purl.uniprot.org/uniprot/Q78IS1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||Dimethylated arginine|||GOLD|||Helical|||Lumenal|||Transmembrane emp24 domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000010385 http://togogenome.org/gene/10090:Prdm12 ^@ http://purl.uniprot.org/uniprot/A2AJ77 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||PR domain zinc finger protein 12|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000416114 http://togogenome.org/gene/10090:Rcc1 ^@ http://purl.uniprot.org/uniprot/Q3U6D2|||http://purl.uniprot.org/uniprot/Q6PFB2|||http://purl.uniprot.org/uniprot/Q8VE37 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||N,N-dimethylproline; alternate|||N-methylproline; alternate|||Phosphoserine|||Polar residues|||RCC1|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||RCC1 7|||Regulator of chromosome condensation|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000206630 http://togogenome.org/gene/10090:Or7e178 ^@ http://purl.uniprot.org/uniprot/Q0VAX9 ^@ 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 7E178 ^@ http://purl.uniprot.org/annotation/PRO_0000269660 http://togogenome.org/gene/10090:Vmn1r246 ^@ http://purl.uniprot.org/uniprot/K9J7H2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ndel1 ^@ http://purl.uniprot.org/uniprot/Q9ERR1 ^@ 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 ^@ Disordered|||Impairs interaction with DISC1.|||In isoform 2.|||Interaction with CENPF|||Interaction with DISC1|||Interaction with KATNA1|||Interaction with KATNB1|||Interaction with NEFL|||Interaction with YWHAE|||Nuclear distribution protein nudE-like 1|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Phosphothreonine; by CDK1 and MAPK1|||Reduces phosphorylation by CDK5 and impairs interaction with YWHAE. Impairs interaction with KATNA1; when associated with A-198 and A-219.|||Reduces phosphorylation by CDK5 and impairs interaction with YWHAE. Impairs interaction with KATNA1; when associated with A-198 and A-231.|||Reduces phosphorylation by CDK5 and impairs interaction with YWHAE. Impairs interaction with KATNA1; when associated with A-219 and A-231.|||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_0000240212|||http://purl.uniprot.org/annotation/VSP_019311 http://togogenome.org/gene/10090:Ankrd34b ^@ http://purl.uniprot.org/uniprot/Q3UUF8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 34B|||Disordered|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000319103 http://togogenome.org/gene/10090:Ezh1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1C0|||http://purl.uniprot.org/uniprot/P70351 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Motif|||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.|||Nuclear localization signal|||Polar residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000213991|||http://purl.uniprot.org/annotation/VSP_036388 http://togogenome.org/gene/10090:Or10q1b ^@ http://purl.uniprot.org/uniprot/Q8VEZ5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tnik ^@ http://purl.uniprot.org/uniprot/B2RQ80|||http://purl.uniprot.org/uniprot/B9EKN8|||http://purl.uniprot.org/uniprot/E9PUL9|||http://purl.uniprot.org/uniprot/P83510 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||CNH|||Disordered|||In isoform 2.|||Mediates interaction with NEDD4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Traf2 and NCK-interacting protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000086762|||http://purl.uniprot.org/annotation/VSP_007351 http://togogenome.org/gene/10090:Carmil3 ^@ http://purl.uniprot.org/uniprot/Q3UFQ8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Capping protein, Arp2/3 and myosin-I linker protein 3|||Disordered|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000324609 http://togogenome.org/gene/10090:Pik3c2g ^@ http://purl.uniprot.org/uniprot/O70167 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Splice Variant ^@ Activation loop|||C2|||C2 PI3K-type|||Catalytic loop|||Disordered|||G-loop|||In isoform 2.|||PI3K-RBD|||PI3K/PI4K catalytic|||PIK helical|||PX|||Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma ^@ http://purl.uniprot.org/annotation/PRO_0000088800|||http://purl.uniprot.org/annotation/VSP_004706|||http://purl.uniprot.org/annotation/VSP_004707 http://togogenome.org/gene/10090:Rhox4g ^@ http://purl.uniprot.org/uniprot/Q2MDF7 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Polr2g ^@ http://purl.uniprot.org/uniprot/P62488 ^@ Chain|||Molecule Processing ^@ Chain ^@ DNA-directed RNA polymerase II subunit RPB7 ^@ http://purl.uniprot.org/annotation/PRO_0000073987 http://togogenome.org/gene/10090:Bex1 ^@ http://purl.uniprot.org/uniprot/Q9R224 ^@ 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|||His cluster|||Phosphoserine|||Protein BEX1 ^@ http://purl.uniprot.org/annotation/PRO_0000229774 http://togogenome.org/gene/10090:Glra3 ^@ http://purl.uniprot.org/uniprot/G5E811|||http://purl.uniprot.org/uniprot/Q91XP5 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Phosphoserine|||Phosphoserine; by PKA ^@ http://purl.uniprot.org/annotation/PRO_0000000420 http://togogenome.org/gene/10090:Tnp1 ^@ http://purl.uniprot.org/uniprot/P10856|||http://purl.uniprot.org/uniprot/Q545L6 ^@ 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_0000191418 http://togogenome.org/gene/10090:Cln6 ^@ http://purl.uniprot.org/uniprot/Q3U466 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Or8k21 ^@ http://purl.uniprot.org/uniprot/L7MU59 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kifc1 ^@ http://purl.uniprot.org/uniprot/Q9QWT9 ^@ 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 ^@ Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Kinesin motor|||Kinesin-like protein KIFC1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000302089|||http://purl.uniprot.org/annotation/VSP_052526|||http://purl.uniprot.org/annotation/VSP_052527 http://togogenome.org/gene/10090:Syngr1 ^@ http://purl.uniprot.org/uniprot/O55100|||http://purl.uniprot.org/uniprot/Q3U6D7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||In isoform 1B.|||Lumenal|||MARVEL|||N-acetylmethionine|||Synaptogyrin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000183991|||http://purl.uniprot.org/annotation/VSP_006333 http://togogenome.org/gene/10090:Itfg2 ^@ http://purl.uniprot.org/uniprot/Q91WI7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified 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_0000289293|||http://purl.uniprot.org/annotation/VSP_026003 http://togogenome.org/gene/10090:Vmn1r223 ^@ http://purl.uniprot.org/uniprot/Q5SSA0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cndp2 ^@ http://purl.uniprot.org/uniprot/Q9D1A2 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Strand|||Turn ^@ Cytosolic non-specific dipeptidase|||Important for catalytic activity|||Loss of activity.|||Loss of threonyl dipeptidase activity.|||Phosphoserine|||Proton acceptor|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000185273 http://togogenome.org/gene/10090:Serpinb9b ^@ http://purl.uniprot.org/uniprot/Q9DAV6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Afp ^@ http://purl.uniprot.org/uniprot/P02772 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Albumin 1|||Albumin 2|||Albumin 3|||Alpha-fetoprotein|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000001098 http://togogenome.org/gene/10090:Slc35d2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J181|||http://purl.uniprot.org/uniprot/A0A1Y7VL74|||http://purl.uniprot.org/uniprot/Q762D5 ^@ 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|||Extracellular|||Helical|||In isoform 2.|||Nucleotide sugar transporter SLC35D2|||Sugar phosphate transporter ^@ http://purl.uniprot.org/annotation/PRO_0000313081|||http://purl.uniprot.org/annotation/VSP_030007|||http://purl.uniprot.org/annotation/VSP_030008 http://togogenome.org/gene/10090:Aadacl4fm2 ^@ http://purl.uniprot.org/uniprot/A2A752 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Alpha/beta hydrolase fold-3 ^@ http://togogenome.org/gene/10090:Anxa7 ^@ http://purl.uniprot.org/uniprot/A0A2C9F2D2|||http://purl.uniprot.org/uniprot/Q07076|||http://purl.uniprot.org/uniprot/Q3UYL7|||http://purl.uniprot.org/uniprot/Q8CCV9 ^@ 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 ^@ 3 X 5 AA tandem repeats of G-Y-P-P-X|||Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A7|||Disordered|||N6-acetyllysine|||Polar residues|||Pro residues|||Repeat-rich region ^@ http://purl.uniprot.org/annotation/PRO_0000067500 http://togogenome.org/gene/10090:F13b ^@ http://purl.uniprot.org/uniprot/Q07968|||http://purl.uniprot.org/uniprot/Q3UER0 ^@ 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 ^@ Coagulation factor XIII B chain|||N-linked (GlcNAc...) asparagine|||Sushi|||Sushi 1|||Sushi 10|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9|||Sushi domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000021223|||http://purl.uniprot.org/annotation/PRO_5004230103 http://togogenome.org/gene/10090:Tnnt3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1A8|||http://purl.uniprot.org/uniprot/A0A0R4J1B0|||http://purl.uniprot.org/uniprot/A0A0R4J1B1|||http://purl.uniprot.org/uniprot/A2A6H6|||http://purl.uniprot.org/uniprot/A2A6I0|||http://purl.uniprot.org/uniprot/A2A6I3|||http://purl.uniprot.org/uniprot/A2A6I5|||http://purl.uniprot.org/uniprot/A2A6I8|||http://purl.uniprot.org/uniprot/A2A6J0|||http://purl.uniprot.org/uniprot/A2A6J1|||http://purl.uniprot.org/uniprot/Q9QZ47|||http://purl.uniprot.org/uniprot/Z4YJU0|||http://purl.uniprot.org/uniprot/Z4YKD9|||http://purl.uniprot.org/uniprot/Z4YKF8|||http://purl.uniprot.org/uniprot/Z4YKG3|||http://purl.uniprot.org/uniprot/Z4YKG8|||http://purl.uniprot.org/uniprot/Z4YNB2 ^@ 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 isoform A2e17, isoform A4e17 and isoform A6e17.|||In isoform A3e17, isoform B2e17 and isoform B2e16.|||In isoform A4e17, isoform B3e17, isoform B3e16, isoform B4e17 and isoform B4e16.|||In isoform A5e17, isoform A6e17, isoform B2e17 and isoform B2e16.|||In isoform B1e16, isoform B2e16, isoform B3e16, isoform B4e16 and isoform 14.|||In isoform B1e16, isoform B3e17 and isoform B3e16.|||In isoform B4e17 and isoform B4e16.|||N-acetylserine|||Phosphoserine|||Phosphotyrosine|||Removed|||Troponin T, fast skeletal muscle ^@ http://purl.uniprot.org/annotation/PRO_0000186179|||http://purl.uniprot.org/annotation/VSP_050338|||http://purl.uniprot.org/annotation/VSP_050339|||http://purl.uniprot.org/annotation/VSP_050340|||http://purl.uniprot.org/annotation/VSP_050341|||http://purl.uniprot.org/annotation/VSP_050342|||http://purl.uniprot.org/annotation/VSP_050343|||http://purl.uniprot.org/annotation/VSP_050344 http://togogenome.org/gene/10090:Gsta3 ^@ http://purl.uniprot.org/uniprot/P30115 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Mass|||Modified Residue ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase A3|||N-acetylalanine|||N6-succinyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000185790 http://togogenome.org/gene/10090:Sfxn1 ^@ http://purl.uniprot.org/uniprot/Q99JR1 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Topological Domain|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylserine|||Removed|||Sideroflexin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000177033 http://togogenome.org/gene/10090:Zfp618 ^@ http://purl.uniprot.org/uniprot/F8WIU3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Det1 ^@ http://purl.uniprot.org/uniprot/Q9D0A0 ^@ Chain|||Molecule Processing ^@ Chain ^@ DET1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000129027 http://togogenome.org/gene/10090:Hoxb6 ^@ http://purl.uniprot.org/uniprot/P09023 ^@ Chain|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Modified Residue|||Motif|||Sequence Conflict ^@ Antp-type hexapeptide|||Homeobox|||Homeobox protein Hox-B6|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000200136 http://togogenome.org/gene/10090:Arhgef12 ^@ http://purl.uniprot.org/uniprot/F8VQN6 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DH|||Disordered|||PDZ|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Rab9b ^@ http://purl.uniprot.org/uniprot/Q8BHH2 ^@ 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-9B|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121143 http://togogenome.org/gene/10090:Runx2 ^@ http://purl.uniprot.org/uniprot/E0CZ12|||http://purl.uniprot.org/uniprot/F8WHN7|||http://purl.uniprot.org/uniprot/Q08775|||http://purl.uniprot.org/uniprot/Q9Z2T9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||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|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||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, isoform 6, isoform 7, isoform 8 and isoform 9.|||In isoform 6 and isoform 9.|||In isoform 7.|||In isoform 8 and isoform 9.|||Interaction with IFI204|||Interaction with KAT6A|||Interaction with KAT6B|||Phosphoserine; by CDK1|||Polar residues|||Pro residues|||Required for interaction with FOXO1|||Runt|||Runt-related transcription factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000174660|||http://purl.uniprot.org/annotation/VSP_005939|||http://purl.uniprot.org/annotation/VSP_005940|||http://purl.uniprot.org/annotation/VSP_005941|||http://purl.uniprot.org/annotation/VSP_005942|||http://purl.uniprot.org/annotation/VSP_005943|||http://purl.uniprot.org/annotation/VSP_005944|||http://purl.uniprot.org/annotation/VSP_005945|||http://purl.uniprot.org/annotation/VSP_005946|||http://purl.uniprot.org/annotation/VSP_005947|||http://purl.uniprot.org/annotation/VSP_005948 http://togogenome.org/gene/10090:Fgf7 ^@ http://purl.uniprot.org/uniprot/P36363|||http://purl.uniprot.org/uniprot/Q544I6 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ Fibroblast growth factor|||Fibroblast growth factor 7|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000008966|||http://purl.uniprot.org/annotation/PRO_5014205868 http://togogenome.org/gene/10090:Srsf7 ^@ http://purl.uniprot.org/uniprot/A0A3Q4L393|||http://purl.uniprot.org/uniprot/Q3THA6|||http://purl.uniprot.org/uniprot/Q8BL97 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 1|||2|||3|||4|||5; approximate|||6 X 8 AA repeats of R-R-S-R-S-X-S-X|||6; approximate|||Basic residues|||CCHC-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2, isoform 3 and isoform 4.|||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_0000081933|||http://purl.uniprot.org/annotation/VSP_013654|||http://purl.uniprot.org/annotation/VSP_013655|||http://purl.uniprot.org/annotation/VSP_013656|||http://purl.uniprot.org/annotation/VSP_013657 http://togogenome.org/gene/10090:Itgam ^@ http://purl.uniprot.org/uniprot/E9Q604|||http://purl.uniprot.org/uniprot/G5E8F1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Repeat|||Signal Peptide|||Transmembrane ^@ FG-GAP|||Helical|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5006524986|||http://purl.uniprot.org/annotation/PRO_5015019565 http://togogenome.org/gene/10090:H2bc9 ^@ http://purl.uniprot.org/uniprot/Q64478 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 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-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-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_0000244832 http://togogenome.org/gene/10090:Uqcr11 ^@ http://purl.uniprot.org/uniprot/Q9CPX8 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Topological Domain|||Transmembrane ^@ Chain|||Helix|||Topological Domain|||Transmembrane ^@ Cytochrome b-c1 complex subunit 10|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix ^@ http://purl.uniprot.org/annotation/PRO_0000193561 http://togogenome.org/gene/10090:Ptgr2 ^@ http://purl.uniprot.org/uniprot/Q8VDQ1 ^@ 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 ^@ In isoform 2.|||Prostaglandin reductase 2|||Significant reduction in catalytic efficiency. ^@ http://purl.uniprot.org/annotation/PRO_0000218071|||http://purl.uniprot.org/annotation/VSP_013528|||http://purl.uniprot.org/annotation/VSP_013529 http://togogenome.org/gene/10090:Shisa4 ^@ http://purl.uniprot.org/uniprot/Q8CA71 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Protein shisa-4 ^@ http://purl.uniprot.org/annotation/PRO_0000254091 http://togogenome.org/gene/10090:Pth2r ^@ http://purl.uniprot.org/uniprot/Q91V95 ^@ 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 ^@ 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|||Parathyroid hormone 2 receptor ^@ http://purl.uniprot.org/annotation/PRO_0000012850 http://togogenome.org/gene/10090:Vwc2l ^@ http://purl.uniprot.org/uniprot/Q505H4 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Signal Peptide|||Splice Variant ^@ In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||VWFC 1|||VWFC 2|||von Willebrand factor C domain-containing protein 2-like ^@ http://purl.uniprot.org/annotation/PRO_0000348062|||http://purl.uniprot.org/annotation/VSP_035090|||http://purl.uniprot.org/annotation/VSP_035091|||http://purl.uniprot.org/annotation/VSP_035092|||http://purl.uniprot.org/annotation/VSP_035093|||http://purl.uniprot.org/annotation/VSP_044591|||http://purl.uniprot.org/annotation/VSP_044592 http://togogenome.org/gene/10090:Csn1s1 ^@ http://purl.uniprot.org/uniprot/P19228|||http://purl.uniprot.org/uniprot/Q91VV1|||http://purl.uniprot.org/uniprot/Q99JM6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Signal Peptide ^@ 1|||10|||11|||12|||13|||14|||15|||15 X 6 AA tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Alpha-S1-casein|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000004457|||http://purl.uniprot.org/annotation/PRO_5013243536|||http://purl.uniprot.org/annotation/PRO_5015099522 http://togogenome.org/gene/10090:Zfp954 ^@ http://purl.uniprot.org/uniprot/Q7TNU5|||http://purl.uniprot.org/uniprot/Q8BIA9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Slc37a4 ^@ http://purl.uniprot.org/uniprot/Q9D1F9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:Fbxw7 ^@ http://purl.uniprot.org/uniprot/D3YUA8|||http://purl.uniprot.org/uniprot/Q8VBV4 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||F-box|||F-box/WD repeat-containing protein 7|||In isoform 2.|||Phosphoserine|||Phosphoserine; by SGK1|||Phosphothreonine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000050995|||http://purl.uniprot.org/annotation/VSP_059530 http://togogenome.org/gene/10090:Gpx2 ^@ http://purl.uniprot.org/uniprot/Q9JHC0 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Molecule Processing|||Non standard residue|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Non standard residue|||Sequence Conflict ^@ Glutathione peroxidase 2|||Selenocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000066622 http://togogenome.org/gene/10090:Mindy2 ^@ http://purl.uniprot.org/uniprot/Q6PDI6 ^@ 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|||Site|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||Ubiquitin carboxyl-terminal hydrolase MINDY-2|||Ubiquitin-binding|||Ubiquitin-binding domain (UBD) ^@ http://purl.uniprot.org/annotation/PRO_0000344043|||http://purl.uniprot.org/annotation/VSP_034720|||http://purl.uniprot.org/annotation/VSP_034721|||http://purl.uniprot.org/annotation/VSP_034722 http://togogenome.org/gene/10090:Cd27 ^@ http://purl.uniprot.org/uniprot/B7ZW87|||http://purl.uniprot.org/uniprot/D3Z7W5|||http://purl.uniprot.org/uniprot/P41272|||http://purl.uniprot.org/uniprot/Q3U4X0 ^@ 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 ^@ CD27 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Pro residues|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3 ^@ http://purl.uniprot.org/annotation/PRO_0000034572|||http://purl.uniprot.org/annotation/PRO_5003052667|||http://purl.uniprot.org/annotation/PRO_5015087457|||http://purl.uniprot.org/annotation/PRO_5015097465 http://togogenome.org/gene/10090:Rep15 ^@ http://purl.uniprot.org/uniprot/Q9D7T1 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Lipid Binding|||Sequence Conflict ^@ N-myristoyl glycine|||Rab15 effector protein|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000323588 http://togogenome.org/gene/10090:Arl5a ^@ http://purl.uniprot.org/uniprot/Q80ZU0 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding ^@ ADP-ribosylation factor-like protein 5A|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207468 http://togogenome.org/gene/10090:Gstt3 ^@ http://purl.uniprot.org/uniprot/G3UX05|||http://purl.uniprot.org/uniprot/Q99L20 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase theta-3 ^@ http://purl.uniprot.org/annotation/PRO_0000437667 http://togogenome.org/gene/10090:Dscaml1 ^@ http://purl.uniprot.org/uniprot/E9QPR7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Fibronectin type-III|||Ig-like|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Znrf3 ^@ http://purl.uniprot.org/uniprot/Q5SSZ7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger ^@ 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_0000277807|||http://purl.uniprot.org/annotation/VSP_023089|||http://purl.uniprot.org/annotation/VSP_023090|||http://purl.uniprot.org/annotation/VSP_023091 http://togogenome.org/gene/10090:Rlbp1 ^@ http://purl.uniprot.org/uniprot/Q544Y3|||http://purl.uniprot.org/uniprot/Q9Z275 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ CRAL-TRIO|||N-acetylserine|||Removed|||Retinaldehyde-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000079331 http://togogenome.org/gene/10090:Nme6 ^@ http://purl.uniprot.org/uniprot/O88425 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Nucleoside diphosphate kinase 6|||Pros-phosphohistidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000137128 http://togogenome.org/gene/10090:Cep162 ^@ http://purl.uniprot.org/uniprot/Q6ZQ06 ^@ 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|||Centrosomal protein of 162 kDa|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295629 http://togogenome.org/gene/10090:Zyx ^@ http://purl.uniprot.org/uniprot/Q62523|||http://purl.uniprot.org/uniprot/Q7TQE2|||http://purl.uniprot.org/uniprot/Q8CBM0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Disordered|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Zyxin ^@ http://purl.uniprot.org/annotation/PRO_0000075914 http://togogenome.org/gene/10090:H4c1 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Teddm1b ^@ http://purl.uniprot.org/uniprot/Q8CC62 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:B3gnt4 ^@ http://purl.uniprot.org/uniprot/Q1RLK6 ^@ 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-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000289208 http://togogenome.org/gene/10090:Tbx6 ^@ http://purl.uniprot.org/uniprot/P70327 ^@ 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|||In isoform 2.|||T-box|||T-box transcription factor TBX6 ^@ http://purl.uniprot.org/annotation/PRO_0000184439|||http://purl.uniprot.org/annotation/VSP_043221 http://togogenome.org/gene/10090:Cav3 ^@ http://purl.uniprot.org/uniprot/P51637 ^@ Chain|||Crosslink|||Experimental Information|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain ^@ Chain|||Crosslink|||INTRAMEM|||Mutagenesis Site|||Region|||Topological Domain ^@ Caveolin-3|||Cytoplasmic|||Dominant-negative mutant that induces defects in membrane repair.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)|||Helical|||Required for interaction with DAG1|||Results in aberrent localization of TRIM72 and defects in membrane repair. ^@ http://purl.uniprot.org/annotation/PRO_0000144141 http://togogenome.org/gene/10090:Klhl15 ^@ http://purl.uniprot.org/uniprot/A2AAX3 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Splice Variant ^@ BACK|||BTB|||In isoform 2.|||In isoform 3.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch-like protein 15 ^@ http://purl.uniprot.org/annotation/PRO_0000438648|||http://purl.uniprot.org/annotation/VSP_058695|||http://purl.uniprot.org/annotation/VSP_058696|||http://purl.uniprot.org/annotation/VSP_058697|||http://purl.uniprot.org/annotation/VSP_058698 http://togogenome.org/gene/10090:Fchsd2 ^@ http://purl.uniprot.org/uniprot/Q3USJ8 ^@ 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|||F-BAR|||F-BAR and double SH3 domains protein 2|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues|||Required and sufficient for location at clathrin-coated pits|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000278215|||http://purl.uniprot.org/annotation/VSP_023170|||http://purl.uniprot.org/annotation/VSP_023171 http://togogenome.org/gene/10090:Cd300lg ^@ http://purl.uniprot.org/uniprot/Q1ERP8 ^@ 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 ^@ Basic and acidic residues|||CMRF35-like molecule 9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000306113|||http://purl.uniprot.org/annotation/VSP_028413|||http://purl.uniprot.org/annotation/VSP_028414|||http://purl.uniprot.org/annotation/VSP_028415|||http://purl.uniprot.org/annotation/VSP_028416|||http://purl.uniprot.org/annotation/VSP_028417 http://togogenome.org/gene/10090:Tsbp1 ^@ http://purl.uniprot.org/uniprot/A2CG24|||http://purl.uniprot.org/uniprot/Q3V0M8|||http://purl.uniprot.org/uniprot/Q80XD0|||http://purl.uniprot.org/uniprot/Q8BHP1 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Drd1 ^@ http://purl.uniprot.org/uniprot/Q61616 ^@ 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|||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|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069375 http://togogenome.org/gene/10090:Pax3 ^@ http://purl.uniprot.org/uniprot/P24610|||http://purl.uniprot.org/uniprot/Q3TZM4|||http://purl.uniprot.org/uniprot/Q3UGH9|||http://purl.uniprot.org/uniprot/Q8BRF1 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Homeobox|||In Spd.|||PAI subdomain|||Paired|||Paired box protein Pax-3|||Phosphoserine|||RED subdomain ^@ http://purl.uniprot.org/annotation/PRO_0000050179 http://togogenome.org/gene/10090:Lama3 ^@ http://purl.uniprot.org/uniprot/Q61789 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||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 isoform A.|||Interchain|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 11|||Laminin EGF-like 12; first part|||Laminin EGF-like 12; second part|||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-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_0000017059|||http://purl.uniprot.org/annotation/VSP_003038|||http://purl.uniprot.org/annotation/VSP_003039 http://togogenome.org/gene/10090:Or10ag58 ^@ http://purl.uniprot.org/uniprot/A2AT86 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mcc ^@ http://purl.uniprot.org/uniprot/E9PWI3|||http://purl.uniprot.org/uniprot/G3UW40|||http://purl.uniprot.org/uniprot/Q3TYX4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||EF-hand|||Harmonin-binding protein USHBP1 PDZ-binding|||Polar residues ^@ http://togogenome.org/gene/10090:Smim7 ^@ http://purl.uniprot.org/uniprot/Q5RKS2 ^@ 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_0000342614 http://togogenome.org/gene/10090:Sec31a ^@ http://purl.uniprot.org/uniprot/Q3UPL0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ALG-2-binding site motif-2 (ABS-2),|||Asymmetric dimethylarginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||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_0000295148|||http://purl.uniprot.org/annotation/VSP_026752|||http://purl.uniprot.org/annotation/VSP_026753 http://togogenome.org/gene/10090:Arl14ep ^@ http://purl.uniprot.org/uniprot/Q8BIX3 ^@ 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 ^@ ARL14 effector protein|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000251893|||http://purl.uniprot.org/annotation/VSP_020776|||http://purl.uniprot.org/annotation/VSP_020777 http://togogenome.org/gene/10090:Syna ^@ http://purl.uniprot.org/uniprot/Q5G5D5 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ CX6CC|||CXXC|||Cleavage|||Cytoplasmic|||Extracellular|||Fusion peptide|||Helical|||Interchain (between SU and TM chains, or C-47 with C-505); in linked form|||N-linked (GlcNAc...) asparagine|||No effect on fusogenic activity. Confers immunosuppressive activity not found in the wild type protein.|||Surface protein|||Syncytin-A|||Transmembrane protein ^@ http://purl.uniprot.org/annotation/PRO_0000440573|||http://purl.uniprot.org/annotation/PRO_0000440574|||http://purl.uniprot.org/annotation/PRO_5009343953 http://togogenome.org/gene/10090:H2-M3 ^@ http://purl.uniprot.org/uniprot/Q31093 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_5015097374 http://togogenome.org/gene/10090:Tmc7 ^@ http://purl.uniprot.org/uniprot/Q8C428 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Transmembrane channel-like protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000287167|||http://purl.uniprot.org/annotation/VSP_025348 http://togogenome.org/gene/10090:Dab2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J104|||http://purl.uniprot.org/uniprot/E9PX84|||http://purl.uniprot.org/uniprot/E9QL31|||http://purl.uniprot.org/uniprot/P98078|||http://purl.uniprot.org/uniprot/Q3TN55|||http://purl.uniprot.org/uniprot/Q3TRE6|||http://purl.uniprot.org/uniprot/Q3TRI2 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Abolishes LDLR endocytosis.|||Abolishes binding to PtdIns(4,5)P2.|||Abolishes interaction with EPS15 and impairs interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-589 and V-736. Abolishes interaction with ITSN1; when associated with V-255, V-398, V-589 and V-736.|||Abolishes interaction with EPS15 and impairs interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-589 and V-765. Abolishes interaction with ITSN1; when associated with V-255, V-398, V-589, and V-765.|||Abolishes interaction with EPS15 and impairs interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-736 and V-765. Abolishes interaction with ITSN1; when associated with V-255, V-398, V-736 and V-765.|||Abolishes interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-255, V-589, V-736 and V-765.|||Abolishes interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-398, V-589, V-736 and V-765.|||Basic and acidic residues|||DPF 1|||DPF 2|||Disabled homolog 2|||Disordered|||Impairs LDLR endocytosis.|||In isoform p67.|||In isoform p93.|||Loss of interaction with FCHO2; when associated with A-294.|||Loss of interaction with FCHO2; when associated with A-299.|||N-acetylserine|||PID|||Phosphoserine|||Phosphoserine; in mitosis|||Phosphothreonine|||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_0000079771|||http://purl.uniprot.org/annotation/VSP_004182|||http://purl.uniprot.org/annotation/VSP_004183 http://togogenome.org/gene/10090:Snapc4 ^@ http://purl.uniprot.org/uniprot/Q8BP86 ^@ 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 ^@ Disordered|||H-T-H motif|||HTH myb-type 1|||HTH myb-type 2|||HTH myb-type 3|||In isoform 2 and isoform 3.|||In isoform 3.|||Myb-like 1|||Myb-like 2|||Phosphoserine|||Polar residues|||SNAPC2-binding|||SNAPC5-binding|||snRNA-activating protein complex subunit 4 ^@ http://purl.uniprot.org/annotation/PRO_0000197121|||http://purl.uniprot.org/annotation/VSP_051855|||http://purl.uniprot.org/annotation/VSP_051857 http://togogenome.org/gene/10090:Vpreb1b ^@ http://purl.uniprot.org/uniprot/P13373 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Region|||Signal Peptide ^@ Complementarity-determining-1|||Complementarity-determining-2|||Framework-1|||Framework-2|||Framework-3|||Immunoglobulin omega chain ^@ http://purl.uniprot.org/annotation/PRO_0000015002 http://togogenome.org/gene/10090:Itm2a ^@ http://purl.uniprot.org/uniprot/Q61500 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ BRICHOS|||Helical; Signal-anchor for type II membrane protein|||Integral membrane protein 2A|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000154819 http://togogenome.org/gene/10090:Nxn ^@ http://purl.uniprot.org/uniprot/P97346 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Splice Variant ^@ In isoform 2.|||Loss of function and interaction with DVL1; when associated with S-205.|||Loss of function and interaction with DVL1; when associated with S-208.|||N-acetylserine|||Nucleoredoxin|||Removed|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000332934|||http://purl.uniprot.org/annotation/VSP_033396|||http://purl.uniprot.org/annotation/VSP_033397 http://togogenome.org/gene/10090:Rhox3a2 ^@ http://purl.uniprot.org/uniprot/Q4TU90 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Csrnp2 ^@ http://purl.uniprot.org/uniprot/Q8BGQ2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Cysteine/serine-rich nuclear protein 2|||Disordered|||N-acetylmethionine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000114791 http://togogenome.org/gene/10090:Hk3 ^@ http://purl.uniprot.org/uniprot/E9Q3Z4|||http://purl.uniprot.org/uniprot/E9Q8S8|||http://purl.uniprot.org/uniprot/Q3TRM8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ 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-3 ^@ http://purl.uniprot.org/annotation/PRO_0000197591 http://togogenome.org/gene/10090:Elfn1 ^@ http://purl.uniprot.org/uniprot/Q8C8T7 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues|||Protein ELFN1 ^@ http://purl.uniprot.org/annotation/PRO_0000343739 http://togogenome.org/gene/10090:Phpt1 ^@ http://purl.uniprot.org/uniprot/Q9DAK9 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ 14 kDa phosphohistidine phosphatase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000206153 http://togogenome.org/gene/10090:Or4a15 ^@ http://purl.uniprot.org/uniprot/A2AVK5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Emilin3 ^@ http://purl.uniprot.org/uniprot/A2A4B4|||http://purl.uniprot.org/uniprot/P59900 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||EMI|||EMILIN-3|||N-linked (GlcNAc...) asparagine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000007820|||http://purl.uniprot.org/annotation/PRO_5002642605 http://togogenome.org/gene/10090:Zfp971 ^@ http://purl.uniprot.org/uniprot/A2BFG8|||http://purl.uniprot.org/uniprot/Q3V498 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Itm2b ^@ http://purl.uniprot.org/uniprot/O89051 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Peptide|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Peptide|||Region|||Site|||Topological Domain|||Transmembrane ^@ BRI2 intracellular domain|||BRI2, membrane form|||BRI2C, soluble form|||BRICHOS|||Bri23 peptide|||Cleavage; by furin|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Integral membrane protein 2B|||Interchain|||Lumenal|||N-linked (GlcNAc...) asparagine|||Necessary for interaction with APP and inhibitor effects on APP processing ^@ http://purl.uniprot.org/annotation/PRO_0000154822|||http://purl.uniprot.org/annotation/PRO_0000417471|||http://purl.uniprot.org/annotation/PRO_0000417472|||http://purl.uniprot.org/annotation/PRO_0000417473|||http://purl.uniprot.org/annotation/PRO_0000417474 http://togogenome.org/gene/10090:Mab21l3 ^@ http://purl.uniprot.org/uniprot/Q8CI17 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Protein mab-21-like 3 ^@ http://purl.uniprot.org/annotation/PRO_0000286585 http://togogenome.org/gene/10090:Entpd8 ^@ http://purl.uniprot.org/uniprot/Q8K0L2 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||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_0000306883|||http://purl.uniprot.org/annotation/VSP_028560|||http://purl.uniprot.org/annotation/VSP_028561 http://togogenome.org/gene/10090:Bsg ^@ http://purl.uniprot.org/uniprot/P18572 ^@ 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 ^@ Basic and acidic residues|||Basigin|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000014519|||http://purl.uniprot.org/annotation/VSP_011502 http://togogenome.org/gene/10090:Mogat1 ^@ http://purl.uniprot.org/uniprot/Q91ZV4 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ 2-acylglycerol O-acyltransferase 1|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000249059 http://togogenome.org/gene/10090:Gpr183 ^@ http://purl.uniprot.org/uniprot/Q3U6B2 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||Interaction with G proteins|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000303231 http://togogenome.org/gene/10090:Fyco1 ^@ http://purl.uniprot.org/uniprot/Q8VDC1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||FYVE and coiled-coil domain-containing protein 1|||FYVE-type|||GOLD|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RUN|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000245838 http://togogenome.org/gene/10090:Prss30 ^@ http://purl.uniprot.org/uniprot/D6REI2|||http://purl.uniprot.org/uniprot/Q9QYZ9 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Charge relay system|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Removed in mature form|||Serine protease 30 ^@ http://purl.uniprot.org/annotation/PRO_0000027861|||http://purl.uniprot.org/annotation/PRO_0000027862|||http://purl.uniprot.org/annotation/PRO_0000027863 http://togogenome.org/gene/10090:Mtdh ^@ http://purl.uniprot.org/uniprot/Q80WJ7 ^@ 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 ^@ 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|||Polar residues|||Protein LYRIC ^@ http://purl.uniprot.org/annotation/PRO_0000084534 http://togogenome.org/gene/10090:Cfap54 ^@ http://purl.uniprot.org/uniprot/Q8C6S9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant ^@ Cilia- and flagella-associated protein 54|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000324607|||http://purl.uniprot.org/annotation/VSP_058120 http://togogenome.org/gene/10090:Ptgdr ^@ http://purl.uniprot.org/uniprot/P70263 ^@ 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|||Prostaglandin D2 receptor ^@ http://purl.uniprot.org/annotation/PRO_0000070048 http://togogenome.org/gene/10090:Tssk4 ^@ http://purl.uniprot.org/uniprot/Q9D411 ^@ 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|||Sequence Conflict|||Splice Variant ^@ In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Loss of kinase activity and no phosphorylation of ODF2. No effect on interaction with ODF2.|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Testis-specific serine/threonine-protein kinase 4 ^@ http://purl.uniprot.org/annotation/PRO_0000086773|||http://purl.uniprot.org/annotation/VSP_023561|||http://purl.uniprot.org/annotation/VSP_059881|||http://purl.uniprot.org/annotation/VSP_059882|||http://purl.uniprot.org/annotation/VSP_059883|||http://purl.uniprot.org/annotation/VSP_059884 http://togogenome.org/gene/10090:Trim6 ^@ http://purl.uniprot.org/uniprot/Q8BGE7 ^@ 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 6 ^@ http://purl.uniprot.org/annotation/PRO_0000056203 http://togogenome.org/gene/10090:S100a11 ^@ http://purl.uniprot.org/uniprot/P50543 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue ^@ EF-hand 1|||EF-hand 2|||Interchain|||N6-acetyllysine|||Phosphothreonine|||Protein S100-A11 ^@ http://purl.uniprot.org/annotation/PRO_0000144010 http://togogenome.org/gene/10090:Cdan1 ^@ http://purl.uniprot.org/uniprot/Q8CC12 ^@ 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 ^@ Codanin-1|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Interaction with ASF1A/B|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089440|||http://purl.uniprot.org/annotation/VSP_027099|||http://purl.uniprot.org/annotation/VSP_027100 http://togogenome.org/gene/10090:Mapk15 ^@ http://purl.uniprot.org/uniprot/Q80Y86 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Mitogen-activated protein kinase 15|||Necessary to interact with ESRRA, to regulate its subcellular localization and to inhibit its transcriptional activity|||Omega-N-methylarginine|||PXXXP motif|||PXXXP motif; regulates binding with chromatin and interaction with PCNA|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Requires for interaction with GABARAP, MAP1LC3B AND GABARAPL1|||TXY|||Ubiquitin-conjugating ^@ http://purl.uniprot.org/annotation/PRO_0000232638 http://togogenome.org/gene/10090:Zan ^@ http://purl.uniprot.org/uniprot/E9PWQ7 ^@ 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 ^@ Disordered|||EGF-like|||Helical|||MAM|||Polar residues|||VWFD ^@ http://purl.uniprot.org/annotation/PRO_5015090356 http://togogenome.org/gene/10090:Cst8 ^@ http://purl.uniprot.org/uniprot/P32766 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Cystatin-8|||N-linked (GlcNAc...) asparagine|||Secondary area of contact ^@ http://purl.uniprot.org/annotation/PRO_0000006654 http://togogenome.org/gene/10090:Isx ^@ http://purl.uniprot.org/uniprot/A1A546|||http://purl.uniprot.org/uniprot/B1Q2M1 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Homeobox|||In isoform 2.|||Intestine-specific homeobox|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288603|||http://purl.uniprot.org/annotation/VSP_025717 http://togogenome.org/gene/10090:Tspan11 ^@ http://purl.uniprot.org/uniprot/Q9D1D1 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-11 ^@ http://purl.uniprot.org/annotation/PRO_0000311906 http://togogenome.org/gene/10090:Ccdc42 ^@ http://purl.uniprot.org/uniprot/Q5SV66 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Splice Variant ^@ Coiled-coil domain-containing protein 42|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000234499|||http://purl.uniprot.org/annotation/VSP_018334|||http://purl.uniprot.org/annotation/VSP_018335 http://togogenome.org/gene/10090:Vmn1r47 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Y0|||http://purl.uniprot.org/uniprot/Q9EQ51 ^@ 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|||Vomeronasal type-1 receptor 47 ^@ http://purl.uniprot.org/annotation/PRO_0000239959 http://togogenome.org/gene/10090:Tusc2 ^@ http://purl.uniprot.org/uniprot/Q542N4|||http://purl.uniprot.org/uniprot/Q9WVF8 ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region ^@ Disordered|||N-myristoyl glycine|||Phosphoserine|||Removed|||Tumor suppressor candidate 2 ^@ http://purl.uniprot.org/annotation/PRO_0000148171 http://togogenome.org/gene/10090:Ifitm3 ^@ http://purl.uniprot.org/uniprot/Q9CQW9 ^@ Chain|||Crosslink|||Experimental Information|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||INTRAMEM|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Accumulates at the plasma membrane. No effect on anti-SARS-CoV-2 activity.|||Cytoplasmic|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Interaction with SPP1|||Interaction with VAPA|||Interferon-induced transmembrane protein 3|||No effect on SARS-CoV-2 infection; when associated with 71-A-A-72.|||No effect on SARS-CoV-2 infection; when associated with A-105.|||Phosphotyrosine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000398567 http://togogenome.org/gene/10090:Or56b2 ^@ http://purl.uniprot.org/uniprot/Q99NH4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Smc1b ^@ http://purl.uniprot.org/uniprot/A1L2Z0|||http://purl.uniprot.org/uniprot/Q920F6 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N6-acetyllysine|||SMC hinge|||Structural maintenance of chromosomes protein 1B ^@ http://purl.uniprot.org/annotation/PRO_0000118994 http://togogenome.org/gene/10090:Msn ^@ http://purl.uniprot.org/uniprot/P26041 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Diminishes the number of microvilli-like structures.|||Disordered|||FERM|||Moesin|||N6-acetyllysine|||N6-succinyllysine|||No effect on microvilli-like structures.|||Phosphoserine|||Phosphothreonine; by ROCK2 and STK10|||Phosphotyrosine|||S-nitrosocysteine|||[IL]-x-C-x-x-[DE] motif ^@ http://purl.uniprot.org/annotation/PRO_0000219417 http://togogenome.org/gene/10090:Hcfc2 ^@ http://purl.uniprot.org/uniprot/Q9D968 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Strand ^@ Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Host cell factor 2|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000119073 http://togogenome.org/gene/10090:Efcc1 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ84|||http://purl.uniprot.org/uniprot/Q9JJF6 ^@ 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 ^@ Basic and acidic residues|||Disordered|||EF-hand|||EF-hand and coiled-coil domain-containing protein 1|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000342342|||http://purl.uniprot.org/annotation/VSP_039450 http://togogenome.org/gene/10090:Tas2r104 ^@ http://purl.uniprot.org/uniprot/Q7M723 ^@ 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 104 ^@ http://purl.uniprot.org/annotation/PRO_0000248248 http://togogenome.org/gene/10090:Nmrk2 ^@ http://purl.uniprot.org/uniprot/Q9D7C9 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Nicotinamide riboside kinase 2|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000215895 http://togogenome.org/gene/10090:Paqr8 ^@ http://purl.uniprot.org/uniprot/Q80ZE5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||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|||Membrane progestin receptor beta ^@ http://purl.uniprot.org/annotation/PRO_0000218841 http://togogenome.org/gene/10090:Zfyve19 ^@ http://purl.uniprot.org/uniprot/Q4KL52|||http://purl.uniprot.org/uniprot/Q9DAZ9 ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger ^@ Abscission/NoCut checkpoint regulator|||Disordered|||FYVE-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In strain: C57BL/6.|||In strain: FVB/N.|||MIM1-A|||MIM1-B|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000098719 http://togogenome.org/gene/10090:Klf11 ^@ http://purl.uniprot.org/uniprot/Q8K1S5 ^@ 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|||Disordered|||Krueppel-like factor 11 ^@ http://purl.uniprot.org/annotation/PRO_0000047189 http://togogenome.org/gene/10090:Kcnrg ^@ http://purl.uniprot.org/uniprot/Q2TUM3 ^@ 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_0000238946|||http://purl.uniprot.org/annotation/VSP_019023|||http://purl.uniprot.org/annotation/VSP_019024 http://togogenome.org/gene/10090:Flywch1 ^@ http://purl.uniprot.org/uniprot/Q8CI03 ^@ 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|||Basic 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.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314461|||http://purl.uniprot.org/annotation/VSP_030282|||http://purl.uniprot.org/annotation/VSP_030283 http://togogenome.org/gene/10090:Nup155 ^@ http://purl.uniprot.org/uniprot/Q6ZQ45|||http://purl.uniprot.org/uniprot/Q8BUA6|||http://purl.uniprot.org/uniprot/Q99P88 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region ^@ Disordered|||Nuclear pore complex protein Nup155|||Nucleoporin Nup133/Nup155-like C-terminal|||Nucleoporin Nup133/Nup155-like N-terminal|||O-linked (GlcNAc) serine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000204845 http://togogenome.org/gene/10090:Ndufb4b ^@ http://purl.uniprot.org/uniprot/Q9CQC7 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Transmembrane|||Turn ^@ Helical|||N-acetylserine|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118801 http://togogenome.org/gene/10090:Ormdl1 ^@ http://purl.uniprot.org/uniprot/Q921I0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||ORM1-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000215631 http://togogenome.org/gene/10090:Yes1 ^@ http://purl.uniprot.org/uniprot/Q04736|||http://purl.uniprot.org/uniprot/Q3TJI7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Strand|||Turn ^@ N-myristoyl glycine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||S-palmitoyl cysteine; in membrane form|||SH2|||SH3|||Tyrosine-protein kinase Yes ^@ http://purl.uniprot.org/annotation/PRO_0000088182 http://togogenome.org/gene/10090:Chia1 ^@ http://purl.uniprot.org/uniprot/Q91XA9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Acidic mammalian chitinase|||Chitin-binding type-2|||Disordered|||GH18|||Polar residues|||Proton donor|||Strongly reduced activity at low pH, with minor effect on activity at neutral pH. ^@ http://purl.uniprot.org/annotation/PRO_0000011945 http://togogenome.org/gene/10090:Sdad1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0B7|||http://purl.uniprot.org/uniprot/Q80UZ2 ^@ 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|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Protein SDA1 homolog|||SDA1 C-terminal|||SDA1 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000287483|||http://purl.uniprot.org/annotation/VSP_025506|||http://purl.uniprot.org/annotation/VSP_025507|||http://purl.uniprot.org/annotation/VSP_025508 http://togogenome.org/gene/10090:Ccdc92b ^@ http://purl.uniprot.org/uniprot/Q5SUE3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||CCDC92/74 N-terminal|||Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Sgcg ^@ http://purl.uniprot.org/uniprot/P82348|||http://purl.uniprot.org/uniprot/Q9EQ83 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Gamma-sarcoglycan|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000175250 http://togogenome.org/gene/10090:Nms ^@ http://purl.uniprot.org/uniprot/A0A250SH12|||http://purl.uniprot.org/uniprot/Q5H8A1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Chain|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide ^@ Asparagine amide|||Neuromedin-S ^@ http://purl.uniprot.org/annotation/PRO_0000262485|||http://purl.uniprot.org/annotation/PRO_0000262486|||http://purl.uniprot.org/annotation/PRO_0000262487|||http://purl.uniprot.org/annotation/PRO_0000262488|||http://purl.uniprot.org/annotation/PRO_0000262489|||http://purl.uniprot.org/annotation/PRO_5011694470 http://togogenome.org/gene/10090:Crebrf ^@ http://purl.uniprot.org/uniprot/Q8CDG5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Acidic residues|||Basic motif|||CREB3 regulatory factor|||Disordered|||Leucine-zipper|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000299307 http://togogenome.org/gene/10090:Hycc2 ^@ http://purl.uniprot.org/uniprot/Q8C729 ^@ 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|||Hyccin 2|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000278095|||http://purl.uniprot.org/annotation/VSP_035078 http://togogenome.org/gene/10090:Gna14 ^@ http://purl.uniprot.org/uniprot/P30677|||http://purl.uniprot.org/uniprot/Q8CBT5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict ^@ 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_0000203753 http://togogenome.org/gene/10090:Trmt6 ^@ http://purl.uniprot.org/uniprot/Q8CE96 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 3 and isoform 4.|||In isoform 4.|||Phosphothreonine|||Substrate|||tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6 ^@ http://purl.uniprot.org/annotation/PRO_0000233099|||http://purl.uniprot.org/annotation/VSP_018026|||http://purl.uniprot.org/annotation/VSP_018027|||http://purl.uniprot.org/annotation/VSP_018028 http://togogenome.org/gene/10090:Mgat4e ^@ http://purl.uniprot.org/uniprot/A6H684 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4E|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000325757|||http://purl.uniprot.org/annotation/VSP_054935 http://togogenome.org/gene/10090:Scgb2b17 ^@ http://purl.uniprot.org/uniprot/A0A089N3E7|||http://purl.uniprot.org/uniprot/S4R2V3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5001847728|||http://purl.uniprot.org/annotation/PRO_5015101141 http://togogenome.org/gene/10090:Ntan1 ^@ http://purl.uniprot.org/uniprot/Q64311|||http://purl.uniprot.org/uniprot/Q8BRX4 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue ^@ Chain|||Non-terminal Residue ^@ Protein N-terminal asparagine amidohydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000057972 http://togogenome.org/gene/10090:Noc4l ^@ http://purl.uniprot.org/uniprot/Q8BHY2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Nucleolar complex protein 4 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000173485 http://togogenome.org/gene/10090:Plbd2 ^@ http://purl.uniprot.org/uniprot/Q3TCN2 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ In isoform 2.|||N-linked (GlcNAc...) asparagine|||Putative phospholipase B-like 2|||Putative phospholipase B-like 2 15 kDa form|||Putative phospholipase B-like 2 28 kDa form|||Putative phospholipase B-like 2 40 kDa form ^@ http://purl.uniprot.org/annotation/PRO_0000286111|||http://purl.uniprot.org/annotation/PRO_0000314076|||http://purl.uniprot.org/annotation/PRO_0000314077|||http://purl.uniprot.org/annotation/PRO_0000314078|||http://purl.uniprot.org/annotation/VSP_024998|||http://purl.uniprot.org/annotation/VSP_024999 http://togogenome.org/gene/10090:Cyp2b10 ^@ http://purl.uniprot.org/uniprot/Q9WUD0 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Cytochrome P450 ^@ http://purl.uniprot.org/annotation/PRO_5015100996 http://togogenome.org/gene/10090:Smarcc2 ^@ http://purl.uniprot.org/uniprot/Q3UID0|||http://purl.uniprot.org/uniprot/Q6PDG5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolished mono-ADP-ribosylation by SIRT6 and recruitment to the enhancer region of the Heme oxygenase-1 (HO-1) locus.|||BRCT; C-terminus|||BRCT; N-terminus|||Basic and acidic residues|||Chromo|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||MarR-like|||MarR-like, BRCT and chromo domains module|||Myb-like|||N6-(ADP-ribosyl)lysine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||SANT|||SWI/SNF complex subunit SMARCC2|||SWIRM ^@ http://purl.uniprot.org/annotation/PRO_0000197118|||http://purl.uniprot.org/annotation/VSP_012492 http://togogenome.org/gene/10090:Adam15 ^@ http://purl.uniprot.org/uniprot/O88839 ^@ 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|||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|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cleavage; by furin|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 15|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphotyrosine; by HCK and LCK|||Polar residues|||Pro residues|||Reduced binding to CHO cells expressing ITAG9-ITGB1.|||SH3-binding|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029084|||http://purl.uniprot.org/annotation/PRO_0000029085|||http://purl.uniprot.org/annotation/VSP_008879|||http://purl.uniprot.org/annotation/VSP_008880|||http://purl.uniprot.org/annotation/VSP_008881 http://togogenome.org/gene/10090:Lancl1 ^@ http://purl.uniprot.org/uniprot/O89112 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site ^@ Does not increase glutathione transferase activity and reduces cellular protection.|||Glutathione S-transferase LANCL1|||N-acetylalanine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000191269 http://togogenome.org/gene/10090:Ghitm ^@ http://purl.uniprot.org/uniprot/Q91VC9 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Growth hormone-inducible transmembrane protein|||Helical|||Impaired protein stability. Skeletal muscle mitochondria are swollen, exhibiting a disrupted cristae structure.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000320076 http://togogenome.org/gene/10090:Htr7 ^@ http://purl.uniprot.org/uniprot/B6VJS3|||http://purl.uniprot.org/uniprot/P32304 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 5-hydroxytryptamine receptor 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|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000068980 http://togogenome.org/gene/10090:Soga3 ^@ http://purl.uniprot.org/uniprot/Q6NZL0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Polar residues|||Protein SOGA3 ^@ http://purl.uniprot.org/annotation/PRO_0000271353 http://togogenome.org/gene/10090:Plcxd1 ^@ http://purl.uniprot.org/uniprot/G3X9J3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Phosphatidylinositol-specific phospholipase C X ^@ http://togogenome.org/gene/10090:Ptp4a3 ^@ http://purl.uniprot.org/uniprot/E9PXS4|||http://purl.uniprot.org/uniprot/Q9D658 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict ^@ Cysteine methyl ester|||Loss of enzymatic activity; reduced migration-promoting activity.|||Phosphocysteine intermediate|||Protein tyrosine phosphatase type IVA 3|||Proton donor|||Removed in mature form|||S-farnesyl cysteine|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094789|||http://purl.uniprot.org/annotation/PRO_0000396655 http://togogenome.org/gene/10090:Antxr1 ^@ http://purl.uniprot.org/uniprot/Q9CZ52 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Anthrax toxin receptor 1|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000002693|||http://purl.uniprot.org/annotation/VSP_000450 http://togogenome.org/gene/10090:Or51f1d ^@ http://purl.uniprot.org/uniprot/Q8VG25 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tmem154 ^@ http://purl.uniprot.org/uniprot/Q8C4Q9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Transmembrane protein 154 ^@ http://purl.uniprot.org/annotation/PRO_0000284504|||http://purl.uniprot.org/annotation/VSP_024546|||http://purl.uniprot.org/annotation/VSP_024547 http://togogenome.org/gene/10090:Rab31 ^@ http://purl.uniprot.org/uniprot/Q3TXV4|||http://purl.uniprot.org/uniprot/Q921E2 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Effector region|||Phosphoserine|||Ras-related protein Rab-31|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121233 http://togogenome.org/gene/10090:Eif1ad3 ^@ http://purl.uniprot.org/uniprot/Q3TQZ4 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||S1-like ^@ http://togogenome.org/gene/10090:Eif3f ^@ http://purl.uniprot.org/uniprot/Q3U8X1|||http://purl.uniprot.org/uniprot/Q3UVY8|||http://purl.uniprot.org/uniprot/Q9DCH4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Eukaryotic translation initiation factor 3 subunit F|||MPN|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK11; in vitro|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213965 http://togogenome.org/gene/10090:Tbkbp1 ^@ http://purl.uniprot.org/uniprot/A2A9T0|||http://purl.uniprot.org/uniprot/Z4YKN2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||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_0000324655|||http://purl.uniprot.org/annotation/VSP_032344|||http://purl.uniprot.org/annotation/VSP_052716 http://togogenome.org/gene/10090:Bin2 ^@ http://purl.uniprot.org/uniprot/S4R270 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||BAR|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rad17 ^@ http://purl.uniprot.org/uniprot/Q3UYY2|||http://purl.uniprot.org/uniprot/Q6NXW6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ AAA+ ATPase|||Acidic residues|||Basic and acidic residues|||Cell cycle checkpoint protein RAD17|||Disordered|||Interaction with MCM7|||Phosphoserine|||Phosphoserine; by ATR|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000209949 http://togogenome.org/gene/10090:Nrk ^@ http://purl.uniprot.org/uniprot/Q9R0G8 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||CNH|||Disordered|||Kinase inactivation.|||Nik-related protein kinase|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000250512 http://togogenome.org/gene/10090:Rsph1 ^@ http://purl.uniprot.org/uniprot/Q3YEA4|||http://purl.uniprot.org/uniprot/Q8VIG3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Strand ^@ Acidic residues|||Basic and acidic residues|||Disordered|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||Polar residues|||Radial spoke head 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000065663 http://togogenome.org/gene/10090:Tmc2 ^@ http://purl.uniprot.org/uniprot/Q8R4P4 ^@ 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|||Polar residues|||Transmembrane channel-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000185383 http://togogenome.org/gene/10090:Zfp455 ^@ http://purl.uniprot.org/uniprot/Q7M6X9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:E2f4 ^@ http://purl.uniprot.org/uniprot/Q8R0K9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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_0000322638 http://togogenome.org/gene/10090:Foxa2 ^@ http://purl.uniprot.org/uniprot/G5E8P5|||http://purl.uniprot.org/uniprot/P35583 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Fork-head|||Hepatocyte nuclear factor 3-beta|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transactivation domain 1|||Transactivation domain 2 ^@ http://purl.uniprot.org/annotation/PRO_0000091796 http://togogenome.org/gene/10090:Lce3b ^@ http://purl.uniprot.org/uniprot/Q9CQM7 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Myof ^@ http://purl.uniprot.org/uniprot/A0A286YDF5|||http://purl.uniprot.org/uniprot/Q69ZN7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ C2|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||C2 6|||C2 7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Myoferlin|||N6-acetyllysine|||Necessary for interaction with EHD2|||Phosphoserine|||Reduces calcium-sensitive phospholipid binding. ^@ http://purl.uniprot.org/annotation/PRO_0000281646|||http://purl.uniprot.org/annotation/VSP_024013|||http://purl.uniprot.org/annotation/VSP_024014|||http://purl.uniprot.org/annotation/VSP_024015|||http://purl.uniprot.org/annotation/VSP_024016|||http://purl.uniprot.org/annotation/VSP_024017|||http://purl.uniprot.org/annotation/VSP_035934 http://togogenome.org/gene/10090:Celf3 ^@ http://purl.uniprot.org/uniprot/A0A0G2JDL2|||http://purl.uniprot.org/uniprot/A0A0G2JGX2|||http://purl.uniprot.org/uniprot/Q8CIN6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ CUGBP Elav-like family member 3|||Disordered|||In isoform 2.|||Polar residues|||Pro residues|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000295199|||http://purl.uniprot.org/annotation/VSP_026826|||http://purl.uniprot.org/annotation/VSP_026827 http://togogenome.org/gene/10090:Iqgap3 ^@ http://purl.uniprot.org/uniprot/F8VQ29 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Calponin-homology (CH)|||Ras-GAP|||WW ^@ http://togogenome.org/gene/10090:Spryd3 ^@ http://purl.uniprot.org/uniprot/E9Q9B3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||B30.2/SPRY|||Disordered ^@ http://togogenome.org/gene/10090:Ppp1r13b ^@ http://purl.uniprot.org/uniprot/Q62415 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ 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_0000066963 http://togogenome.org/gene/10090:Atp13a1 ^@ http://purl.uniprot.org/uniprot/Q9EPE9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||A-domain; part 1|||A-domain; part 2|||Arm-like|||Cytoplasmic|||Disordered|||Endoplasmic reticulum transmembrane helix translocase|||Extracellular|||Helical|||Loss of ATPase activity.|||N-domain|||N-linked (GlcNAc...) asparagine|||P-domain; part 1|||P-domain; part 2|||P-domain; part 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000046422 http://togogenome.org/gene/10090:Cep290 ^@ http://purl.uniprot.org/uniprot/E9Q9M0|||http://purl.uniprot.org/uniprot/Q6A078 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Centrosomal localization retained.|||Centrosomal protein of 290 kDa|||Centrosomal protein of 290kDa coiled-coil region|||Disordered|||In isoform 2.|||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_0000258013|||http://purl.uniprot.org/annotation/VSP_052188|||http://purl.uniprot.org/annotation/VSP_052189 http://togogenome.org/gene/10090:Or2d2b ^@ http://purl.uniprot.org/uniprot/E9Q725 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Adipor2 ^@ http://purl.uniprot.org/uniprot/Q53YY3|||http://purl.uniprot.org/uniprot/Q8BQS5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Adiponectin receptor protein 2|||Basic and acidic residues|||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. ^@ http://purl.uniprot.org/annotation/PRO_0000218830|||http://purl.uniprot.org/annotation/VSP_008887|||http://purl.uniprot.org/annotation/VSP_008888 http://togogenome.org/gene/10090:Phaf1 ^@ http://purl.uniprot.org/uniprot/Q922R1 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Phagosome assembly factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000221084 http://togogenome.org/gene/10090:Dnai4 ^@ http://purl.uniprot.org/uniprot/E9PYY5 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Region|||Repeat|||Splice Variant ^@ Disordered|||Dynein axonemal intermediate chain 4|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000415828|||http://purl.uniprot.org/annotation/VSP_042399|||http://purl.uniprot.org/annotation/VSP_042400|||http://purl.uniprot.org/annotation/VSP_042401|||http://purl.uniprot.org/annotation/VSP_042402|||http://purl.uniprot.org/annotation/VSP_042403 http://togogenome.org/gene/10090:Tjap1 ^@ http://purl.uniprot.org/uniprot/Q9DCD5 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Tight junction-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072551|||http://purl.uniprot.org/annotation/VSP_060915 http://togogenome.org/gene/10090:Upk2 ^@ http://purl.uniprot.org/uniprot/Q3SXK0 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015097428 http://togogenome.org/gene/10090:Xrcc6 ^@ http://purl.uniprot.org/uniprot/A0A0R4J187|||http://purl.uniprot.org/uniprot/P23475 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||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)|||Interaction with DEAF1|||Ku|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PRKDC|||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_0000210180 http://togogenome.org/gene/10090:Cyp2b23 ^@ http://purl.uniprot.org/uniprot/E9Q593 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Cytochrome P450 ^@ http://purl.uniprot.org/annotation/PRO_5003243103 http://togogenome.org/gene/10090:Or2p2 ^@ http://purl.uniprot.org/uniprot/Q8VFG4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clec3b ^@ http://purl.uniprot.org/uniprot/Q8CFZ6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ C-type lectin ^@ http://purl.uniprot.org/annotation/PRO_5015099104 http://togogenome.org/gene/10090:Alg3 ^@ http://purl.uniprot.org/uniprot/Q8K2A8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000080567 http://togogenome.org/gene/10090:Atxn7l3 ^@ http://purl.uniprot.org/uniprot/A2AWT3 ^@ 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 ^@ Ataxin-7-like protein 3|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||SCA7|||SGF11-type ^@ http://purl.uniprot.org/annotation/PRO_0000367516|||http://purl.uniprot.org/annotation/VSP_036728 http://togogenome.org/gene/10090:Lrrc38 ^@ http://purl.uniprot.org/uniprot/A2VDH3 ^@ 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|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 38|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000312419 http://togogenome.org/gene/10090:Gm14326 ^@ http://purl.uniprot.org/uniprot/A2BFG4|||http://purl.uniprot.org/uniprot/A2BFG5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Rhox2d ^@ http://purl.uniprot.org/uniprot/W4VSN9 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Or6c204 ^@ http://purl.uniprot.org/uniprot/F6VS78 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Coro1c ^@ http://purl.uniprot.org/uniprot/Q9WUM4 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict ^@ Coronin-1C|||Decreased actin-binding. Loss of actin binding; when associated with 418-E-E-419 and 427-E-E-428.|||Decreased actin-binding. Loss of actin binding; when associated with D-28 and 418-E-E-419.|||Decreased actin-binding. Loss of actin binding; when associated with D-28 and 427-E-E-428.|||N6-acetyllysine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000050927 http://togogenome.org/gene/10090:Tex19.1 ^@ http://purl.uniprot.org/uniprot/Q99MV2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Does not affect interaction with UBR2.|||Important for interaction with piRNA|||Interaction with LIRE1|||Testis-expressed protein 19.1 ^@ http://purl.uniprot.org/annotation/PRO_0000325963 http://togogenome.org/gene/10090:Pcsk9 ^@ http://purl.uniprot.org/uniprot/Q80W65 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ C-terminal domain|||Cell attachment site|||Charge relay system|||Cleavage; by autolysis|||Cleavage; by furin and PCSK5|||N-linked (GlcNAc...) asparagine|||Peptidase S8|||Phosphoserine|||Proprotein convertase subtilisin/kexin type 9|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000027122|||http://purl.uniprot.org/annotation/PRO_0000027123 http://togogenome.org/gene/10090:Zc2hc1c ^@ http://purl.uniprot.org/uniprot/Q8CB75|||http://purl.uniprot.org/uniprot/Q8CCG1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2HC/C3H-type 1|||C2HC/C3H-type 2|||Disordered|||Polar residues|||Zinc finger C2HC domain-containing protein 1C ^@ http://purl.uniprot.org/annotation/PRO_0000089942 http://togogenome.org/gene/10090:Ube3b ^@ http://purl.uniprot.org/uniprot/Q9ES34 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue ^@ Glycyl thioester intermediate|||HECT|||IQ|||N-acetylmethionine|||Phosphoserine|||Ubiquitin-protein ligase E3B ^@ http://purl.uniprot.org/annotation/PRO_0000281883 http://togogenome.org/gene/10090:Msantd3 ^@ http://purl.uniprot.org/uniprot/Q9CR78 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Myb-like|||Myb/SANT-like DNA-binding domain-containing protein 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000292591 http://togogenome.org/gene/10090:Clgn ^@ http://purl.uniprot.org/uniprot/P52194 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 1-1|||1-2|||1-3|||1-4|||2-1|||2-2|||2-3|||2-4|||Basic and acidic residues|||Calmegin|||Cytoplasmic|||Disordered|||Helical|||Interaction with PPIB|||Lumenal|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000004211 http://togogenome.org/gene/10090:Sgta ^@ http://purl.uniprot.org/uniprot/Q3TN35|||http://purl.uniprot.org/uniprot/Q8BJU0 ^@ 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|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||SGTA homodimerisation|||Small glutamine-rich tetratricopeptide repeat-containing protein alpha|||TPR|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000106366|||http://purl.uniprot.org/annotation/VSP_009300 http://togogenome.org/gene/10090:Slc35g3 ^@ http://purl.uniprot.org/uniprot/B2RQF0 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Ier2 ^@ http://purl.uniprot.org/uniprot/P17950 ^@ 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|||Immediate early response gene 2 protein|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000190436 http://togogenome.org/gene/10090:Timm9 ^@ http://purl.uniprot.org/uniprot/Q9WV98 ^@ Chain|||Disulfide Bond|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Disulfide Bond|||Initiator Methionine|||Modified Residue|||Motif ^@ Mitochondrial import inner membrane translocase subunit Tim9|||N-acetylalanine|||Removed|||Twin CX3C motif ^@ http://purl.uniprot.org/annotation/PRO_0000193596 http://togogenome.org/gene/10090:Gm7694 ^@ http://purl.uniprot.org/uniprot/J3QNH8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Defb21 ^@ http://purl.uniprot.org/uniprot/Q8C5Z4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Beta-defensin ^@ http://purl.uniprot.org/annotation/PRO_5015020116 http://togogenome.org/gene/10090:Pank1 ^@ http://purl.uniprot.org/uniprot/Q8K4K6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of nuclear localization.|||Nucleolar localization signal|||Pantothenate kinase 1|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000161803|||http://purl.uniprot.org/annotation/VSP_004522|||http://purl.uniprot.org/annotation/VSP_004523 http://togogenome.org/gene/10090:Ggnbp1 ^@ http://purl.uniprot.org/uniprot/D3Z3W4|||http://purl.uniprot.org/uniprot/Q6K1E7 ^@ 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|||Gametogenetin-binding protein 1|||Interaction with GGN|||Polar residues|||Required for induction of mitochondrial fragmentation|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000239346 http://togogenome.org/gene/10090:Ramp1 ^@ http://purl.uniprot.org/uniprot/A0A087WPC6|||http://purl.uniprot.org/uniprot/E9Q915|||http://purl.uniprot.org/uniprot/Q3TNJ3|||http://purl.uniprot.org/uniprot/Q9WTJ5 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Receptor activity-modifying protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000030169|||http://purl.uniprot.org/annotation/PRO_5001831761|||http://purl.uniprot.org/annotation/PRO_5003243133|||http://purl.uniprot.org/annotation/PRO_5014309108 http://togogenome.org/gene/10090:Nherf4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0D4|||http://purl.uniprot.org/uniprot/Q99MJ6 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ Loss of phosphorylation. Significant increase in interaction with SLC26A3.|||Na(+)/H(+) exchange regulatory cofactor NHE-RF4|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphomimetic mutant. Significant decrease in interaction with SLC26A3.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000058293 http://togogenome.org/gene/10090:Mri1 ^@ http://purl.uniprot.org/uniprot/Q9CQT1 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Site ^@ Methylthioribose-1-phosphate isomerase|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Proton donor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000317326 http://togogenome.org/gene/10090:Trhr2 ^@ http://purl.uniprot.org/uniprot/Q9ERT2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Evx1 ^@ http://purl.uniprot.org/uniprot/P23683 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Disordered|||Homeobox|||Homeobox even-skipped homolog protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048871 http://togogenome.org/gene/10090:Esyt3 ^@ http://purl.uniprot.org/uniprot/Q5DTI8 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ C2 1|||C2 2|||C2 3|||Cytoplasmic|||Disordered|||Extended synaptotagmin-3|||Helical|||In isoform 2.|||Lumenal|||Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane|||SMP-LTD ^@ http://purl.uniprot.org/annotation/PRO_0000314900|||http://purl.uniprot.org/annotation/VSP_030426 http://togogenome.org/gene/10090:Arhgap40 ^@ http://purl.uniprot.org/uniprot/E9Q6X9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Rho GTPase-activating protein 40|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000415822 http://togogenome.org/gene/10090:Ppp4c ^@ http://purl.uniprot.org/uniprot/P97470|||http://purl.uniprot.org/uniprot/Q3UNF2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Leucine methyl ester|||N-acetylalanine|||Proton donor|||Removed|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase 4 catalytic subunit ^@ http://purl.uniprot.org/annotation/PRO_0000058884 http://togogenome.org/gene/10090:Rsu1 ^@ http://purl.uniprot.org/uniprot/A2AUR7|||http://purl.uniprot.org/uniprot/Q9D031 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Abcb4 ^@ http://purl.uniprot.org/uniprot/P21440 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||Cytoplasmic|||Extracellular|||Helical|||Interaction with HAX1|||N-linked (GlcNAc...) asparagine|||Phosphatidylcholine translocator ABCB4|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000093337 http://togogenome.org/gene/10090:Or6c38 ^@ http://purl.uniprot.org/uniprot/Q8VGC4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Spred2 ^@ http://purl.uniprot.org/uniprot/Q924S7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||KBD|||Phosphotyrosine|||Polar residues|||SPR|||Sprouty-related, EVH1 domain-containing protein 2|||WH1 ^@ http://purl.uniprot.org/annotation/PRO_0000076911 http://togogenome.org/gene/10090:Ess2 ^@ http://purl.uniprot.org/uniprot/O70279|||http://purl.uniprot.org/uniprot/Q3UFM6 ^@ 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|||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_0000079877 http://togogenome.org/gene/10090:Camk2b ^@ http://purl.uniprot.org/uniprot/P28652|||http://purl.uniprot.org/uniprot/Q5SVI2|||http://purl.uniprot.org/uniprot/Q5SVJ0|||http://purl.uniprot.org/uniprot/Q68EG2|||http://purl.uniprot.org/uniprot/Q8BL41 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Autoinhibitory domain|||Blocks calcium/calmodulin binding.|||Calcium/calmodulin-dependent protein kinase type II subunit beta|||Calmodulin-binding|||Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086097 http://togogenome.org/gene/10090:Tmem9 ^@ http://purl.uniprot.org/uniprot/Q9CR23 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||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_0000034375 http://togogenome.org/gene/10090:Pds5b ^@ http://purl.uniprot.org/uniprot/F8WHU5|||http://purl.uniprot.org/uniprot/Q4VA53 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ A.T hook 1|||A.T hook 2|||A.T hook 3|||Basic and acidic residues|||Disordered|||HEAT|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sister chromatid cohesion protein PDS5 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000287425|||http://purl.uniprot.org/annotation/VSP_052403|||http://purl.uniprot.org/annotation/VSP_052404|||http://purl.uniprot.org/annotation/VSP_052405|||http://purl.uniprot.org/annotation/VSP_052406 http://togogenome.org/gene/10090:Lims2 ^@ http://purl.uniprot.org/uniprot/Q91XD2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ LIM and senescent cell antigen-like-containing domain protein 2|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||LIM zinc-binding 5|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000266012 http://togogenome.org/gene/10090:Tfg ^@ http://purl.uniprot.org/uniprot/Q8C2C6|||http://purl.uniprot.org/uniprot/Q9Z1A1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PB1|||Polar residues ^@ http://togogenome.org/gene/10090:Epx ^@ http://purl.uniprot.org/uniprot/P49290|||http://purl.uniprot.org/uniprot/Q3V1J3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ 3'-nitrotyrosine|||Eosinophil peroxidase heavy chain|||Eosinophil peroxidase light chain|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Transition state stabilizer|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000023642|||http://purl.uniprot.org/annotation/PRO_0000023643|||http://purl.uniprot.org/annotation/PRO_0000023644 http://togogenome.org/gene/10090:Garin3 ^@ http://purl.uniprot.org/uniprot/Q5STT6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Basic residues|||Bipartite nuclear localization signal|||Disordered|||Golgi-associated RAB2B interactor protein 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000285644 http://togogenome.org/gene/10090:S1pr4 ^@ http://purl.uniprot.org/uniprot/Q9Z0L1 ^@ Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Lipid Binding|||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|||S-palmitoyl cysteine|||Sphingosine 1-phosphate receptor 4 ^@ http://purl.uniprot.org/annotation/PRO_0000069432 http://togogenome.org/gene/10090:Vmn1r122 ^@ http://purl.uniprot.org/uniprot/K7N726 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:A2ml1 ^@ http://purl.uniprot.org/uniprot/Q3TTY9|||http://purl.uniprot.org/uniprot/Q3UU35 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide ^@ Alpha-2-macroglobulin|||Alpha-macroglobulin receptor-binding|||N-linked (GlcNAc...) asparagine|||Ovostatin homolog ^@ http://purl.uniprot.org/annotation/PRO_0000318967 http://togogenome.org/gene/10090:Slc25a41 ^@ http://purl.uniprot.org/uniprot/Q8BVN7 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane ^@ Chain|||Repeat|||Splice Variant|||Transmembrane ^@ Calcium-independent mitochondrial carrier protein SCaMC-3L|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000319991|||http://purl.uniprot.org/annotation/VSP_052684 http://togogenome.org/gene/10090:Acadm ^@ http://purl.uniprot.org/uniprot/P45952 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Medium-chain specific acyl-CoA dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphothreonine|||Proton acceptor|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000000504 http://togogenome.org/gene/10090:Sys1 ^@ http://purl.uniprot.org/uniprot/Q78S06 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Protein SYS1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000213941 http://togogenome.org/gene/10090:Lhx5 ^@ http://purl.uniprot.org/uniprot/P61375|||http://purl.uniprot.org/uniprot/Q543P4 ^@ 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|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx5|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000075790 http://togogenome.org/gene/10090:Zfp820 ^@ http://purl.uniprot.org/uniprot/E9Q5G8|||http://purl.uniprot.org/uniprot/Q9CSX8 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Synm ^@ http://purl.uniprot.org/uniprot/A0A140LJ61|||http://purl.uniprot.org/uniprot/Q70IV5 ^@ 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|||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_0000364438|||http://purl.uniprot.org/annotation/VSP_053033|||http://purl.uniprot.org/annotation/VSP_053034|||http://purl.uniprot.org/annotation/VSP_053035 http://togogenome.org/gene/10090:Grhpr ^@ http://purl.uniprot.org/uniprot/Q3T9Z2|||http://purl.uniprot.org/uniprot/Q91Z53 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Site ^@ D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding|||D-isomer specific 2-hydroxyacid dehydrogenase catalytic|||Glyoxylate reductase/hydroxypyruvate reductase|||Phosphoserine|||Phosphothreonine|||Proton donor|||Raises pKa of active site His ^@ http://purl.uniprot.org/annotation/PRO_0000075945 http://togogenome.org/gene/10090:Serpina11 ^@ http://purl.uniprot.org/uniprot/E9QK54|||http://purl.uniprot.org/uniprot/E9QLL8|||http://purl.uniprot.org/uniprot/Q3UEP8|||http://purl.uniprot.org/uniprot/Q8CIE0 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Serpin|||Serpin A11|||Serpin domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000041974|||http://purl.uniprot.org/annotation/PRO_5003243333|||http://purl.uniprot.org/annotation/PRO_5003246393|||http://purl.uniprot.org/annotation/PRO_5004229917 http://togogenome.org/gene/10090:Dock6 ^@ http://purl.uniprot.org/uniprot/A0A1L1SQR4|||http://purl.uniprot.org/uniprot/Q8VDR9 ^@ 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 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 6|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000189994|||http://purl.uniprot.org/annotation/VSP_022257|||http://purl.uniprot.org/annotation/VSP_022258|||http://purl.uniprot.org/annotation/VSP_022259|||http://purl.uniprot.org/annotation/VSP_022260|||http://purl.uniprot.org/annotation/VSP_022261 http://togogenome.org/gene/10090:Dctn1 ^@ http://purl.uniprot.org/uniprot/E9Q3M3|||http://purl.uniprot.org/uniprot/E9Q586|||http://purl.uniprot.org/uniprot/O08788|||http://purl.uniprot.org/uniprot/Q3TRF1|||http://purl.uniprot.org/uniprot/Q6NZM3 ^@ 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 ^@ Basic residues|||CAP-Gly|||Disordered|||Dynactin subunit 1|||In isoform 2.|||Interaction with HPS6|||Phosphoserine; by CDK1|||Phosphoserine; by PLK1|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000083519|||http://purl.uniprot.org/annotation/VSP_029584 http://togogenome.org/gene/10090:Zfp180 ^@ http://purl.uniprot.org/uniprot/Q6NZI9|||http://purl.uniprot.org/uniprot/Q6P407|||http://purl.uniprot.org/uniprot/Q8BJI2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Grp ^@ http://purl.uniprot.org/uniprot/Q8R1I2 ^@ Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Gastrin-releasing peptide|||Methionine amide|||Neuromedin-C ^@ http://purl.uniprot.org/annotation/PRO_0000262472|||http://purl.uniprot.org/annotation/PRO_0000262473|||http://purl.uniprot.org/annotation/PRO_0000262474 http://togogenome.org/gene/10090:Gpr37 ^@ http://purl.uniprot.org/uniprot/Q9QY42 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Glycosylation Site|||Region|||Sequence Conflict|||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|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Prosaposin receptor GPR37 ^@ http://purl.uniprot.org/annotation/PRO_0000012800|||http://purl.uniprot.org/annotation/VSP_011762|||http://purl.uniprot.org/annotation/VSP_011763|||http://purl.uniprot.org/annotation/VSP_011764 http://togogenome.org/gene/10090:Klk9 ^@ http://purl.uniprot.org/uniprot/Q32M27 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015097381 http://togogenome.org/gene/10090:Pcnx3 ^@ http://purl.uniprot.org/uniprot/Q8VI59 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pecanex-like protein 3|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000215796|||http://purl.uniprot.org/annotation/VSP_033246 http://togogenome.org/gene/10090:Phf5a ^@ http://purl.uniprot.org/uniprot/P83870 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Site ^@ Interaction with RNA|||Interaction with SF3B1 and SF3B3|||Interaction with SF3B3|||N-acetylalanine|||N6-acetyllysine|||PHD finger-like domain-containing protein 5A|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000218717 http://togogenome.org/gene/10090:Dmrt2 ^@ http://purl.uniprot.org/uniprot/Q8BG36 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict ^@ Acidic residues|||DM|||Disordered|||Doublesex- and mab-3-related transcription factor 2|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000423010 http://togogenome.org/gene/10090:Fbxl18 ^@ http://purl.uniprot.org/uniprot/F8VQK6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box|||F-box/LRR-repeat protein 18 LRR ^@ http://togogenome.org/gene/10090:Nkx1-2 ^@ http://purl.uniprot.org/uniprot/P42580 ^@ 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|||NK1 transcription factor-related protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000049290 http://togogenome.org/gene/10090:Ccm2 ^@ http://purl.uniprot.org/uniprot/F7AVU1|||http://purl.uniprot.org/uniprot/Q8K2Y9 ^@ 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|||Cerebral cavernous malformations 2 harmonin-homology|||Cerebral cavernous malformations protein 2 homolog|||Disordered|||Harmonin homology domain|||In isoform 2.|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089425|||http://purl.uniprot.org/annotation/VSP_024404|||http://purl.uniprot.org/annotation/VSP_024405 http://togogenome.org/gene/10090:5730455P16Rik ^@ http://purl.uniprot.org/uniprot/Q9CYI0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Protein Njmu-R1 ^@ http://purl.uniprot.org/annotation/PRO_0000096866 http://togogenome.org/gene/10090:Mrgpra4 ^@ http://purl.uniprot.org/uniprot/Q91WW2|||http://purl.uniprot.org/uniprot/W8W3F5 ^@ 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|||Mas-related G-protein coupled receptor member A4|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069750 http://togogenome.org/gene/10090:Tmem218 ^@ http://purl.uniprot.org/uniprot/Q9CQ44 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 218 ^@ http://purl.uniprot.org/annotation/PRO_0000321837 http://togogenome.org/gene/10090:C1qtnf6 ^@ http://purl.uniprot.org/uniprot/A0A2R8W6P9|||http://purl.uniprot.org/uniprot/A0A3B0IP29|||http://purl.uniprot.org/uniprot/Q6IR41 ^@ 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 ^@ C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 6|||Disordered|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000320084|||http://purl.uniprot.org/annotation/PRO_5030054822|||http://purl.uniprot.org/annotation/PRO_5030075161 http://togogenome.org/gene/10090:Nr2c1 ^@ http://purl.uniprot.org/uniprot/Q505F1 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger ^@ Abolishes sumoylation.|||Abolishes sumoylation. No effect on activation of OCT4 but activation not suppressed by additional SUMO1. Enhanced interaction with KAT2B; when associated with A-210 or E-210.|||Abolishes sumoylation. No repression of OCT4 gene expression with or without retinoic acid and enhanced interaction with KAT2B and HDAC3. Abolishes interaction with HDAC3 and PML association; when associated with R-238.|||Abolishes sumoylation. Strongly associated with PML nuclear bodies. No effect on activation of OCT4 but activation not suppressed by additional SUMO1. Increased binding to KAT2B and reduced binding to NRIP1. Abolishes PML association; when associated with A-210.|||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 PKC-stimulated protein stability and activation of RARB reporter.|||In isoform 2.|||In strain: CD-1.|||Little effect on PKC-stimulated protein stability nor on activation of RARB reporter.|||NR C4-type|||NR LBD|||No effect on sumoylation and little effect on binding KAT2B. Some reduced DNA-binding. Greatly reduced DNA-binding, binding to KAT2B and activation of the RARB promoter; when associated with A-170.|||No effect on sumoylation nor on DNA-binding and little effect on binding KAT2B. Greatly reduced DNA-binding, binding to KAT2B and activation of the RARB promoter; when associated with A-185.|||No effect on sumoylation.|||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|||Sumoylated. Repressed OCT4 gene expression. Enhanced interaction with KAT2B; when associated with R-238. ^@ http://purl.uniprot.org/annotation/PRO_0000053587|||http://purl.uniprot.org/annotation/VSP_051921|||http://purl.uniprot.org/annotation/VSP_051922 http://togogenome.org/gene/10090:Ubap1l ^@ http://purl.uniprot.org/uniprot/G3UW59 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Polar residues|||Pro residues|||UMA ^@ http://togogenome.org/gene/10090:Ap3m1 ^@ http://purl.uniprot.org/uniprot/Q9JKC8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ AP-3 complex subunit mu-1|||MHD ^@ http://purl.uniprot.org/annotation/PRO_0000193782 http://togogenome.org/gene/10090:Lman2l ^@ http://purl.uniprot.org/uniprot/D3Z4P2|||http://purl.uniprot.org/uniprot/P59481 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endoplasmic reticulum retention signal|||Helical|||L-type lectin-like|||Lumenal|||N-linked (GlcNAc...) asparagine|||VIP36-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000017669|||http://purl.uniprot.org/annotation/PRO_5015088521 http://togogenome.org/gene/10090:St8sia3 ^@ http://purl.uniprot.org/uniprot/Q64689|||http://purl.uniprot.org/uniprot/Q9CUJ6 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor|||Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000149290 http://togogenome.org/gene/10090:Ush1c ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Z8|||http://purl.uniprot.org/uniprot/D6RIM8|||http://purl.uniprot.org/uniprot/E9PYX1|||http://purl.uniprot.org/uniprot/E9QMN1|||http://purl.uniprot.org/uniprot/H3BIZ2|||http://purl.uniprot.org/uniprot/Q6XA19|||http://purl.uniprot.org/uniprot/Q9ES64 ^@ 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|||Harmonin|||In isoform 1.|||In isoform 2.|||Mediates interaction with MYO7B|||N-terminal domain|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000065728|||http://purl.uniprot.org/annotation/VSP_050530|||http://purl.uniprot.org/annotation/VSP_050531|||http://purl.uniprot.org/annotation/VSP_050532|||http://purl.uniprot.org/annotation/VSP_050533|||http://purl.uniprot.org/annotation/VSP_050534 http://togogenome.org/gene/10090:Or52j3 ^@ http://purl.uniprot.org/uniprot/E9PYB3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Chrd ^@ http://purl.uniprot.org/uniprot/A6H5Z6|||http://purl.uniprot.org/uniprot/Q9Z0E2 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ CHRD|||CHRD 1|||CHRD 2|||CHRD 3|||CHRD 4|||Chordin|||Disordered|||N-linked (GlcNAc...) asparagine|||VWFC|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4 ^@ http://purl.uniprot.org/annotation/PRO_0000005365|||http://purl.uniprot.org/annotation/PRO_5040101962 http://togogenome.org/gene/10090:Bsn ^@ http://purl.uniprot.org/uniprot/O88737|||http://purl.uniprot.org/uniprot/Q3UXD6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 1|||2|||3|||4|||5|||5 X 2 AA tandem repeats of P-G|||5 X 7 AA tandem repeats of K-A-S-P-Q-[AT]-[AT]|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||C4-type|||Disordered|||In isoform 2.|||N-myristoyl glycine|||O-linked (GlcNAc) serine|||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_0000065003|||http://purl.uniprot.org/annotation/VSP_011375 http://togogenome.org/gene/10090:Usp49 ^@ http://purl.uniprot.org/uniprot/Q6P9L4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Zinc Finger ^@ Nucleophile|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 49 ^@ http://purl.uniprot.org/annotation/PRO_0000080679 http://togogenome.org/gene/10090:Mpz ^@ http://purl.uniprot.org/uniprot/A0A5F8MPM4|||http://purl.uniprot.org/uniprot/E9QK82|||http://purl.uniprot.org/uniprot/P27573 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||Myelin protein P0|||N-linked (GlcNAc...) (complex) asparagine|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000019301|||http://purl.uniprot.org/annotation/PRO_5015090381|||http://purl.uniprot.org/annotation/PRO_5023901379 http://togogenome.org/gene/10090:Golga2 ^@ http://purl.uniprot.org/uniprot/A0A6I8MX07|||http://purl.uniprot.org/uniprot/Q5DTL1|||http://purl.uniprot.org/uniprot/Q921M4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Splice Variant ^@ Dimethylated arginine|||Disordered|||Golgin subfamily A conserved|||Golgin subfamily A member 2|||In isoform 2.|||Interaction with GORASP1/GRASP65|||Interaction with p115/USO1|||Nuclear localization signal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000190055|||http://purl.uniprot.org/annotation/VSP_039027 http://togogenome.org/gene/10090:Slc10a5 ^@ http://purl.uniprot.org/uniprot/Q5PT54 ^@ 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|||Sodium/bile acid cotransporter 5 ^@ http://purl.uniprot.org/annotation/PRO_0000263746 http://togogenome.org/gene/10090:Allc ^@ http://purl.uniprot.org/uniprot/Q32MW4|||http://purl.uniprot.org/uniprot/Q9JHX6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Allantoicase|||Probable inactive allantoicase ^@ http://purl.uniprot.org/annotation/PRO_0000205907 http://togogenome.org/gene/10090:Spindoc ^@ http://purl.uniprot.org/uniprot/Q05AH6 ^@ 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|||Polar residues|||Spindlin interactor and repressor of chromatin-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000321529|||http://purl.uniprot.org/annotation/VSP_031789|||http://purl.uniprot.org/annotation/VSP_031790 http://togogenome.org/gene/10090:Rnf169 ^@ http://purl.uniprot.org/uniprot/E9Q7F2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF169|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||LR motif|||MIU motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type|||UMI motif ^@ http://purl.uniprot.org/annotation/PRO_0000415820 http://togogenome.org/gene/10090:Gpc6 ^@ http://purl.uniprot.org/uniprot/Q3TP69|||http://purl.uniprot.org/uniprot/Q3V1C9|||http://purl.uniprot.org/uniprot/Q8R3X6|||http://purl.uniprot.org/uniprot/Q9R087 ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||GPI-anchor amidated serine|||Glypican-6|||Polar residues|||Removed in mature form|||Secreted glypican-6 ^@ http://purl.uniprot.org/annotation/PRO_0000012325|||http://purl.uniprot.org/annotation/PRO_0000012326|||http://purl.uniprot.org/annotation/PRO_0000333852|||http://purl.uniprot.org/annotation/PRO_5004229660|||http://purl.uniprot.org/annotation/PRO_5010843522|||http://purl.uniprot.org/annotation/PRO_5015099341 http://togogenome.org/gene/10090:Dmrtc1c1 ^@ http://purl.uniprot.org/uniprot/Q14AJ8|||http://purl.uniprot.org/uniprot/Q9D410 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Doublesex- and mab-3-related transcription factor C1/C2 C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Stag1 ^@ http://purl.uniprot.org/uniprot/F8WHU7|||http://purl.uniprot.org/uniprot/Q9D3E6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Cohesin subunit SA-1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||SCD ^@ http://purl.uniprot.org/annotation/PRO_0000120183 http://togogenome.org/gene/10090:Ern2 ^@ http://purl.uniprot.org/uniprot/Q32MS5|||http://purl.uniprot.org/uniprot/Q3UTN5|||http://purl.uniprot.org/uniprot/Q9Z2E3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||KEN|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase/endoribonuclease IRE2|||non-specific serine/threonine protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000024330|||http://purl.uniprot.org/annotation/PRO_5014309036|||http://purl.uniprot.org/annotation/PRO_5015097498 http://togogenome.org/gene/10090:Meak7 ^@ http://purl.uniprot.org/uniprot/Q8K0P3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||MTOR-associated protein MEAK7|||N-myristoyl glycine|||Removed|||TLDc ^@ http://purl.uniprot.org/annotation/PRO_0000313641|||http://purl.uniprot.org/annotation/VSP_030079|||http://purl.uniprot.org/annotation/VSP_030080 http://togogenome.org/gene/10090:Bsnd ^@ http://purl.uniprot.org/uniprot/Q8VIM4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Barttin|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000065000 http://togogenome.org/gene/10090:Gbp9 ^@ http://purl.uniprot.org/uniprot/Q8BTS3 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ GB1/RHD3-type G ^@ http://togogenome.org/gene/10090:Ilf3 ^@ http://purl.uniprot.org/uniprot/A0A1L1STE4|||http://purl.uniprot.org/uniprot/Q45VK5|||http://purl.uniprot.org/uniprot/Q45VK6|||http://purl.uniprot.org/uniprot/Q9Z1X4 ^@ Chain|||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|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||Bipartite nuclear localization signal|||DRBM|||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 3.|||In isoform 2.|||Interaction with PRMT1|||Interleukin enhancer-binding factor 3|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKR|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000126071|||http://purl.uniprot.org/annotation/VSP_013406|||http://purl.uniprot.org/annotation/VSP_013407|||http://purl.uniprot.org/annotation/VSP_013408 http://togogenome.org/gene/10090:Fam166c ^@ http://purl.uniprot.org/uniprot/Q9DAS2 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ Ciliary microtubule inner protein 2C|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000332278|||http://purl.uniprot.org/annotation/VSP_033372|||http://purl.uniprot.org/annotation/VSP_033373 http://togogenome.org/gene/10090:Potefam3b ^@ http://purl.uniprot.org/uniprot/Q8C646 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ ANK|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rgs21 ^@ http://purl.uniprot.org/uniprot/V9GXQ3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ RGS ^@ http://togogenome.org/gene/10090:Or5m3b ^@ http://purl.uniprot.org/uniprot/Q8VFK5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r27 ^@ http://purl.uniprot.org/uniprot/D3YUK6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003053062 http://togogenome.org/gene/10090:Atp6v1c1 ^@ http://purl.uniprot.org/uniprot/Q9Z1G3 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ N-acetylthreonine|||Removed|||V-type proton ATPase subunit C 1 ^@ http://purl.uniprot.org/annotation/PRO_0000209349 http://togogenome.org/gene/10090:Or9q2 ^@ http://purl.uniprot.org/uniprot/Q8VG11 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccdc163 ^@ http://purl.uniprot.org/uniprot/A2AGD7 ^@ Coiled-Coil|||Region ^@ Coiled-Coil ^@ ^@ http://togogenome.org/gene/10090:Mtpn ^@ http://purl.uniprot.org/uniprot/P62774 ^@ Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ ANK 1|||ANK 2|||ANK 3|||Myotrophin|||N-acetylcysteine|||N6-acetyllysine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067032 http://togogenome.org/gene/10090:Prss21 ^@ http://purl.uniprot.org/uniprot/Q54AE4|||http://purl.uniprot.org/uniprot/Q80YD8|||http://purl.uniprot.org/uniprot/Q9JHJ7 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Charge relay system|||GPI-anchor amidated asparagine|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Removed in mature form|||Testisin ^@ http://purl.uniprot.org/annotation/PRO_0000027852|||http://purl.uniprot.org/annotation/PRO_0000027853|||http://purl.uniprot.org/annotation/PRO_0000027854|||http://purl.uniprot.org/annotation/PRO_5014309658 http://togogenome.org/gene/10090:Myt1 ^@ http://purl.uniprot.org/uniprot/B0R0C1|||http://purl.uniprot.org/uniprot/Q8CFC2 ^@ 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 ^@ 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.|||In isoform 3.|||Myelin transcription factor 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096677|||http://purl.uniprot.org/annotation/VSP_015720|||http://purl.uniprot.org/annotation/VSP_015721 http://togogenome.org/gene/10090:Cldn34b3 ^@ http://purl.uniprot.org/uniprot/Q80ZS5 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015098929 http://togogenome.org/gene/10090:Cbx6 ^@ http://purl.uniprot.org/uniprot/Q9DBY5 ^@ 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 ^@ Chromo|||Chromobox protein homolog 6|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080211 http://togogenome.org/gene/10090:H2al1j ^@ http://purl.uniprot.org/uniprot/A2BFR3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic residues|||Disordered|||Histone H2A/H2B/H3 ^@ http://togogenome.org/gene/10090:Dnaaf9 ^@ http://purl.uniprot.org/uniprot/Q7TT23 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Dynein axonemal assembly factor 9 ^@ http://purl.uniprot.org/annotation/PRO_0000236043 http://togogenome.org/gene/10090:Zfp873 ^@ http://purl.uniprot.org/uniprot/A0A1B0GT64|||http://purl.uniprot.org/uniprot/E9PU88|||http://purl.uniprot.org/uniprot/Q3UPB5|||http://purl.uniprot.org/uniprot/Q5BL04 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Eed ^@ http://purl.uniprot.org/uniprot/Q921E6 ^@ Chain|||Compositionally Biased Region|||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|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Strand|||Turn ^@ Abrogates interaction with EZH2.|||Disordered|||Hypomorphic allele. Abrogates interaction with EZH2 and impairs transcriptional repression.|||Impairs 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|||Null allele. Abrogates interaction with EZH2 and impairs transcriptional repression.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Polycomb protein EED|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000343726|||http://purl.uniprot.org/annotation/VSP_034693|||http://purl.uniprot.org/annotation/VSP_034694 http://togogenome.org/gene/10090:Tmem263 ^@ http://purl.uniprot.org/uniprot/Q9DAM7 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 263 ^@ http://purl.uniprot.org/annotation/PRO_0000263630 http://togogenome.org/gene/10090:Magec2 ^@ http://purl.uniprot.org/uniprot/Q9D4D2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||MAGE ^@ http://togogenome.org/gene/10090:Cog3 ^@ http://purl.uniprot.org/uniprot/E9QL65|||http://purl.uniprot.org/uniprot/Q3USH9 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Nedd4l ^@ http://purl.uniprot.org/uniprot/A0A494BAG2|||http://purl.uniprot.org/uniprot/E9PXB7|||http://purl.uniprot.org/uniprot/G3X9H8 ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2|||Disordered|||Glycyl thioester intermediate|||HECT|||Polar residues|||WW ^@ http://togogenome.org/gene/10090:Or2t29 ^@ http://purl.uniprot.org/uniprot/M9MMK5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gimap5 ^@ http://purl.uniprot.org/uniprot/Q8BWF2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ AIG1-type G|||Cytoplasmic|||GTPase IMAP family member 5|||Helical; Anchor for type IV membrane protein|||Mitochondrial intermembrane ^@ http://purl.uniprot.org/annotation/PRO_0000190991 http://togogenome.org/gene/10090:Tarbp1 ^@ http://purl.uniprot.org/uniprot/E9Q368 ^@ Domain Extent|||Region ^@ Domain Extent ^@ tRNA/rRNA methyltransferase SpoU type ^@ http://togogenome.org/gene/10090:Kcnd3 ^@ http://purl.uniprot.org/uniprot/B2RUE0|||http://purl.uniprot.org/uniprot/Q3UH54|||http://purl.uniprot.org/uniprot/Q9Z0V1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ BTB|||BTB domain-containing protein|||Cytoplasmic|||Disordered|||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.|||Interaction with KCNIP2|||Mediates dendritic targeting|||Phosphoserine|||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_0000054069|||http://purl.uniprot.org/annotation/PRO_5010843434|||http://purl.uniprot.org/annotation/PRO_5014298308|||http://purl.uniprot.org/annotation/VSP_008827|||http://purl.uniprot.org/annotation/VSP_008828|||http://purl.uniprot.org/annotation/VSP_008829 http://togogenome.org/gene/10090:Nit2 ^@ http://purl.uniprot.org/uniprot/Q9JHW2 ^@ 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|||Strand|||Turn ^@ CN hydrolase|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Omega-amidase NIT2|||Phosphoserine|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000320254 http://togogenome.org/gene/10090:Usp46 ^@ http://purl.uniprot.org/uniprot/P62069 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site ^@ In CS; shows negligible immobility in the tail suspension test (TST) and forced swimming test (FST). Both male and female CS mice show virtually no immobile posture immobility in the TST and FST.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 46 ^@ http://purl.uniprot.org/annotation/PRO_0000080675 http://togogenome.org/gene/10090:Capza2 ^@ http://purl.uniprot.org/uniprot/P47754 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ F-actin-capping protein subunit alpha-2|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000208628 http://togogenome.org/gene/10090:Atf3 ^@ http://purl.uniprot.org/uniprot/Q4FJW1|||http://purl.uniprot.org/uniprot/Q60765 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ BZIP|||Basic and acidic residues|||Basic motif|||Cyclic AMP-dependent transcription factor ATF-3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Leucine-zipper|||Phosphothreonine|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076582 http://togogenome.org/gene/10090:1700025G04Rik ^@ http://purl.uniprot.org/uniprot/Q3TJL3|||http://purl.uniprot.org/uniprot/Q8K207 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Polar residues|||Uncharacterized protein C1orf21 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089247 http://togogenome.org/gene/10090:3110009E18Rik ^@ http://purl.uniprot.org/uniprot/Q9CRW3 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||UPF0538 protein C2orf76 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000325825|||http://purl.uniprot.org/annotation/VSP_032430 http://togogenome.org/gene/10090:Arel1 ^@ http://purl.uniprot.org/uniprot/Q8CHG5 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ Apoptosis-resistant E3 ubiquitin protein ligase 1|||Disordered|||Filamin|||Glycyl thioester intermediate|||HECT|||Interaction with SOCS2 ^@ http://purl.uniprot.org/annotation/PRO_0000120350 http://togogenome.org/gene/10090:Kcnk2 ^@ http://purl.uniprot.org/uniprot/P97438|||http://purl.uniprot.org/uniprot/Q6P6P9 ^@ 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 ^@ Abolishes formation of a disulfide-linked heterodimer with KCNK1.|||Cytoplasmic|||Disordered|||Essential for chloroform and halothane sensitivity|||Helical|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||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_0000101743|||http://purl.uniprot.org/annotation/VSP_053951 http://togogenome.org/gene/10090:Flad1 ^@ http://purl.uniprot.org/uniprot/Q8R123 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ FAD synthase|||In isoform 2.|||Molybdenum cofactor biosynthesis protein-like|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000302738|||http://purl.uniprot.org/annotation/VSP_027955 http://togogenome.org/gene/10090:Trappc9 ^@ http://purl.uniprot.org/uniprot/Q3U0M1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Trafficking protein particle complex subunit 9 ^@ http://purl.uniprot.org/annotation/PRO_0000341587|||http://purl.uniprot.org/annotation/VSP_034351|||http://purl.uniprot.org/annotation/VSP_034352|||http://purl.uniprot.org/annotation/VSP_034353|||http://purl.uniprot.org/annotation/VSP_034354|||http://purl.uniprot.org/annotation/VSP_034355|||http://purl.uniprot.org/annotation/VSP_034356 http://togogenome.org/gene/10090:Rpp25l ^@ http://purl.uniprot.org/uniprot/Q99JH1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Pro residues|||Ribonuclease P protein subunit p25-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000271033 http://togogenome.org/gene/10090:Fshb ^@ http://purl.uniprot.org/uniprot/A0A0F7RQR1|||http://purl.uniprot.org/uniprot/Q60687 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Follitropin subunit beta|||Glycoprotein hormone subunit beta|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000011713|||http://purl.uniprot.org/annotation/PRO_5014227023 http://togogenome.org/gene/10090:Sall4 ^@ http://purl.uniprot.org/uniprot/Q8BX22|||http://purl.uniprot.org/uniprot/Q9CYI8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||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|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Sal-like protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000261416|||http://purl.uniprot.org/annotation/VSP_021686|||http://purl.uniprot.org/annotation/VSP_021687 http://togogenome.org/gene/10090:Majin ^@ http://purl.uniprot.org/uniprot/Q9D992 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Impaired DNA-binding activity.|||In isoform 2.|||Membrane-anchored junction protein|||Nuclear|||Perinuclear space ^@ http://purl.uniprot.org/annotation/PRO_0000325833|||http://purl.uniprot.org/annotation/VSP_058064 http://togogenome.org/gene/10090:Stk16 ^@ http://purl.uniprot.org/uniprot/O88697|||http://purl.uniprot.org/uniprot/Q8BSV9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Activation loop|||N-myristoyl glycine|||Phosphoserine; by autocatalysis|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||S-palmitoyl cysteine|||Serine/threonine-protein kinase 16 ^@ http://purl.uniprot.org/annotation/PRO_0000086702 http://togogenome.org/gene/10090:Prokr1 ^@ http://purl.uniprot.org/uniprot/Q9JKL1 ^@ 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|||Prokineticin receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000070080 http://togogenome.org/gene/10090:Snrnp200 ^@ http://purl.uniprot.org/uniprot/Q6P4T2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||DEAH box|||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)|||Helicase ATP-binding 1|||Helicase ATP-binding 2|||Helicase C-terminal 1|||Helicase C-terminal 2|||Interaction with C9orf78 and WBP4|||Interaction with TSSC4|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||SEC63 1|||SEC63 2|||U5 small nuclear ribonucleoprotein 200 kDa helicase ^@ http://purl.uniprot.org/annotation/PRO_0000422049 http://togogenome.org/gene/10090:Trappc3 ^@ http://purl.uniprot.org/uniprot/O55013 ^@ Chain|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Lipid Binding|||Strand|||Turn ^@ S-palmitoyl cysteine|||Trafficking protein particle complex subunit 3 ^@ http://purl.uniprot.org/annotation/PRO_0000211573 http://togogenome.org/gene/10090:Wmp ^@ http://purl.uniprot.org/uniprot/Q3V0P9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||WH2 ^@ http://togogenome.org/gene/10090:Cul4b ^@ http://purl.uniprot.org/uniprot/A2A432|||http://purl.uniprot.org/uniprot/Q3TP81 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Cullin protein neddylation|||Cullin-4B|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000394426|||http://purl.uniprot.org/annotation/VSP_039242 http://togogenome.org/gene/10090:Pate4 ^@ http://purl.uniprot.org/uniprot/Q09098 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Mass|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Mass|||Sequence Conflict|||Signal Peptide ^@ Prostate and testis expressed protein 4|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036175 http://togogenome.org/gene/10090:Or8g54 ^@ http://purl.uniprot.org/uniprot/Q8VG89 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bola2 ^@ http://purl.uniprot.org/uniprot/Q8BGS2 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Splice Variant|||Strand|||Turn ^@ BolA-like protein 2|||In isoform 2.|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000201237|||http://purl.uniprot.org/annotation/VSP_010094 http://togogenome.org/gene/10090:Aldh3b1 ^@ http://purl.uniprot.org/uniprot/Q3TX25|||http://purl.uniprot.org/uniprot/Q80VQ0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide ^@ Abolishes palmitoylation.|||Aldehyde dehydrogenase|||Aldehyde dehydrogenase family 3 member B1|||Cysteine methyl ester|||N-acetylmethionine|||Reduces palmitoylation.|||Removed in mature form|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000056482|||http://purl.uniprot.org/annotation/PRO_0000424194 http://togogenome.org/gene/10090:Trp53rkb ^@ http://purl.uniprot.org/uniprot/Q543M9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Fam222a ^@ http://purl.uniprot.org/uniprot/Q6PGH4 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein FAM222A ^@ http://purl.uniprot.org/annotation/PRO_0000274240 http://togogenome.org/gene/10090:Hnrnpu ^@ http://purl.uniprot.org/uniprot/Q8VEK3 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||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|||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 isoform 2.|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RNA-binding RGG-box|||Removed|||SAP ^@ http://purl.uniprot.org/annotation/PRO_0000387947|||http://purl.uniprot.org/annotation/VSP_059004 http://togogenome.org/gene/10090:Nhsl2 ^@ http://purl.uniprot.org/uniprot/B1AXH1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||NHS-like protein 2|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000341356 http://togogenome.org/gene/10090:Cbln4 ^@ http://purl.uniprot.org/uniprot/Q8BME9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ C1q|||Cerebellin-4|||Interchain|||N-linked (GlcNAc...) asparagine|||No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with NRXN1, NRXN3 and DCC. Shows interaction with NEO1, GRID1 and GRID2. Total loss of N-glycosylation; when associated with Q-26.|||No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with NRXN1, NRXN3 and DCC. Shows interaction with NEO1, GRID1 and GRID2. Total loss of N-glycosylation; when associated with Q-85. ^@ http://purl.uniprot.org/annotation/PRO_0000003557 http://togogenome.org/gene/10090:Hrh2 ^@ http://purl.uniprot.org/uniprot/P97292 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Essential for histamine binding|||Essential for tiotidine binding and implicated in histamine binding|||Extracellular|||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|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069685 http://togogenome.org/gene/10090:E330034G19Rik ^@ http://purl.uniprot.org/uniprot/Q3UWX6 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ncan ^@ http://purl.uniprot.org/uniprot/A0A0R4IZX5|||http://purl.uniprot.org/uniprot/P55066 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||C-type lectin|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||Ig-like|||Ig-like V-type|||Link|||Link 1|||Link 2|||N-linked (GlcNAc...) asparagine|||Neurocan core protein|||O-linked (Xyl...) (chondroitin sulfate) serine|||Polar residues|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_0000017517|||http://purl.uniprot.org/annotation/PRO_5006451921 http://togogenome.org/gene/10090:Rngtt ^@ http://purl.uniprot.org/uniprot/O55236|||http://purl.uniprot.org/uniprot/Q3UA94|||http://purl.uniprot.org/uniprot/Q9DCC1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Acidic residues|||Almost complete loss of RNA-binding and loss of GTase activity.|||At least 60% of RNA binding activity and loss of GTase activity.|||At least 60% of RNA-binding activity and loss of GTase activity.|||Decrease of 55-60% of TPase activity.|||Decrease of >90% of TPase activity.|||Disordered|||GTase|||Increases stimulation of GTase activity by POLR2A binding.|||Interaction with POLR2A|||Loss of GTase activity.|||Loss of TPase activity.|||N6-GMP-lysine intermediate|||No effect.|||Phosphocysteine intermediate|||Polar residues|||Pro residues|||TPase|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||mRNA-capping enzyme ^@ http://purl.uniprot.org/annotation/PRO_0000210109 http://togogenome.org/gene/10090:Zfp955b ^@ http://purl.uniprot.org/uniprot/L7N232|||http://purl.uniprot.org/uniprot/Q9CS13 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dkk2 ^@ http://purl.uniprot.org/uniprot/Q9QYZ8 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand ^@ DKK-type Cys-1|||DKK-type Cys-2|||Dickkopf-related protein 2|||Disordered|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000007221 http://togogenome.org/gene/10090:Hoxd12 ^@ http://purl.uniprot.org/uniprot/P23812 ^@ Chain|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Region ^@ Disordered|||Homeobox|||Homeobox protein Hox-D12 ^@ http://purl.uniprot.org/annotation/PRO_0000200239 http://togogenome.org/gene/10090:Ints15 ^@ http://purl.uniprot.org/uniprot/Q8BGA7 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Integrator complex subunit 15 ^@ http://purl.uniprot.org/annotation/PRO_0000089583 http://togogenome.org/gene/10090:Mios ^@ http://purl.uniprot.org/uniprot/Q8BV62|||http://purl.uniprot.org/uniprot/Q8VE19 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Zinc Finger ^@ C4-type|||GATOR complex protein MIO zinc-ribbon like|||GATOR2 complex protein MIOS|||Phosphoserine|||RING-type; atypical|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000329405 http://togogenome.org/gene/10090:Commd8 ^@ http://purl.uniprot.org/uniprot/Q4QQP1|||http://purl.uniprot.org/uniprot/Q9CZG3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ COMM|||COMM domain-containing protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000077402 http://togogenome.org/gene/10090:Ackr2 ^@ http://purl.uniprot.org/uniprot/O08707 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Atypical chemokine receptor 2|||C-terminal cytoplasmic tail|||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_0000069220 http://togogenome.org/gene/10090:Gatad2b ^@ http://purl.uniprot.org/uniprot/Q8VHR5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Splice 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)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Transcriptional repressor p66-beta ^@ http://purl.uniprot.org/annotation/PRO_0000083503|||http://purl.uniprot.org/annotation/VSP_010930|||http://purl.uniprot.org/annotation/VSP_010931 http://togogenome.org/gene/10090:Pex11a ^@ http://purl.uniprot.org/uniprot/Q9Z211 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Peroxisomal membrane protein 11A|||Required for homodimerization, interaction with PEX11G, and peroxisomal localization ^@ http://purl.uniprot.org/annotation/PRO_0000105965 http://togogenome.org/gene/10090:Barx1 ^@ http://purl.uniprot.org/uniprot/Q9ER42 ^@ 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 1 ^@ http://purl.uniprot.org/annotation/PRO_0000048835 http://togogenome.org/gene/10090:Tapbpl ^@ http://purl.uniprot.org/uniprot/Q8VD31 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Ig-like C1-type|||Ig-like V-type|||Lumenal|||N-linked (GlcNAc...) asparagine|||Tapasin-related protein ^@ http://purl.uniprot.org/annotation/PRO_0000014994 http://togogenome.org/gene/10090:Prtg ^@ http://purl.uniprot.org/uniprot/Q2EY15 ^@ 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 ^@ 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_5000141192 http://togogenome.org/gene/10090:Trim37 ^@ http://purl.uniprot.org/uniprot/Q6PCX9 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ B box-type|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase TRIM37|||MATH|||N-acetylmethionine|||Phosphoserine|||Polar residues|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000056255 http://togogenome.org/gene/10090:Met ^@ http://purl.uniprot.org/uniprot/A4FUV6|||http://purl.uniprot.org/uniprot/F8VQL0 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Signal Peptide|||Transmembrane ^@ Helical|||Hepatocyte growth factor receptor|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Sema ^@ http://purl.uniprot.org/annotation/PRO_5002667977|||http://purl.uniprot.org/annotation/PRO_5015091372 http://togogenome.org/gene/10090:Sbk1 ^@ http://purl.uniprot.org/uniprot/Q8QZX0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase SBK1 ^@ http://purl.uniprot.org/annotation/PRO_0000238452 http://togogenome.org/gene/10090:Rhbg ^@ http://purl.uniprot.org/uniprot/Q8BUX5 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Ammonium transporter Rh type B|||Cytoplasmic|||Decreases expression and/or localization at the plasma membrane.|||Disordered|||Extracellular|||Helical|||Impairs targeting to plasma membrane resulting in loss of transporter activity.|||Interaction with ANK3|||N-linked (GlcNAc...) asparagine|||Normal plasma membrane localization.|||Normal plasma membrane localization. Loss of transporter activity. ^@ http://purl.uniprot.org/annotation/PRO_0000283599 http://togogenome.org/gene/10090:Gata5 ^@ http://purl.uniprot.org/uniprot/P97489 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||GATA-type 1|||GATA-type 2|||Polar residues|||Transcription factor GATA-5 ^@ http://purl.uniprot.org/annotation/PRO_0000083419 http://togogenome.org/gene/10090:Tmem100 ^@ http://purl.uniprot.org/uniprot/Q9CQG9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Mutagenesis Site|||Region|||Transmembrane ^@ Abolishes interaction with TRPA1. Increases interaction with TRPV1. Enhances interaction between TRPA1 and TRPV1.|||Disordered|||Helical|||Phosphoserine|||Transmembrane protein 100 ^@ http://purl.uniprot.org/annotation/PRO_0000240847 http://togogenome.org/gene/10090:Rcor2 ^@ http://purl.uniprot.org/uniprot/Q8C796 ^@ 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 ^@ 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_0000226777 http://togogenome.org/gene/10090:Zhx2 ^@ http://purl.uniprot.org/uniprot/Q8C0C0 ^@ 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 ^@ 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|||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_0000049392 http://togogenome.org/gene/10090:Ndrg3 ^@ http://purl.uniprot.org/uniprot/Q544I1|||http://purl.uniprot.org/uniprot/Q8VCV2|||http://purl.uniprot.org/uniprot/Q9QYF9 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein NDRG3 ^@ http://purl.uniprot.org/annotation/PRO_0000159578 http://togogenome.org/gene/10090:Aoc2 ^@ http://purl.uniprot.org/uniprot/Q812C9 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ 2',4',5'-topaquinone|||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_0000035672 http://togogenome.org/gene/10090:Slx4 ^@ http://purl.uniprot.org/uniprot/Q6P1D7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||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)|||Interaction with MUS81|||Interaction with PLK1 and TERF2-TERF2IP|||Interaction with SLX1|||Phosphoserine|||Polar residues|||Structure-specific endonuclease subunit SLX4|||UBZ4-type 1|||UBZ4-type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000383567 http://togogenome.org/gene/10090:Vmn1r66 ^@ http://purl.uniprot.org/uniprot/Q8K4I0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pkd1l3 ^@ http://purl.uniprot.org/uniprot/A2A258|||http://purl.uniprot.org/uniprot/Q2EG98 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||Channel pore-region|||Cytoplasmic|||Disordered|||Extracellular|||GPS|||Helical|||In isoform 2, isoform 6 and isoform 8.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Little or no effect on calcium channel activity.|||N-linked (GlcNAc...) asparagine|||PLAT|||Polar residues|||Polycystin-1-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000322579|||http://purl.uniprot.org/annotation/PRO_5002642390|||http://purl.uniprot.org/annotation/VSP_031952|||http://purl.uniprot.org/annotation/VSP_031953|||http://purl.uniprot.org/annotation/VSP_031954|||http://purl.uniprot.org/annotation/VSP_031955|||http://purl.uniprot.org/annotation/VSP_031956|||http://purl.uniprot.org/annotation/VSP_031957|||http://purl.uniprot.org/annotation/VSP_031958|||http://purl.uniprot.org/annotation/VSP_031959|||http://purl.uniprot.org/annotation/VSP_031960|||http://purl.uniprot.org/annotation/VSP_031961|||http://purl.uniprot.org/annotation/VSP_031962 http://togogenome.org/gene/10090:Med29 ^@ http://purl.uniprot.org/uniprot/Q9DB91 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Mediator of RNA polymerase II transcription subunit 29|||N-acetylalanine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000288059 http://togogenome.org/gene/10090:Or4k15c ^@ http://purl.uniprot.org/uniprot/E9Q8X3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Edrf1 ^@ http://purl.uniprot.org/uniprot/E9Q9F9|||http://purl.uniprot.org/uniprot/Q6GQV7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ Acidic residues|||Disordered|||Erythroid differentiation-related factor 1|||Polar residues|||TPR 1|||TPR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000244261 http://togogenome.org/gene/10090:Zpld2 ^@ http://purl.uniprot.org/uniprot/Q3UU21 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||ZP ^@ http://togogenome.org/gene/10090:Krt4 ^@ http://purl.uniprot.org/uniprot/P07744 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type II cytoskeletal 4|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063723 http://togogenome.org/gene/10090:Bcl2l14 ^@ http://purl.uniprot.org/uniprot/Q9CPT0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Motif|||Sequence Conflict ^@ Apoptosis facilitator Bcl-2-like protein 14|||BH2|||BH3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000143076 http://togogenome.org/gene/10090:Top3a ^@ http://purl.uniprot.org/uniprot/O70157|||http://purl.uniprot.org/uniprot/Q5NCT2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ C4-type|||DNA topoisomerase 3-alpha|||Disordered|||GRF-type|||GRF-type 1|||GRF-type 2|||O-(5'-phospho-DNA)-tyrosine intermediate|||Polar residues|||Toprim ^@ http://purl.uniprot.org/annotation/PRO_0000145191 http://togogenome.org/gene/10090:Or8u10 ^@ http://purl.uniprot.org/uniprot/Q7TR84 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kirrel3 ^@ http://purl.uniprot.org/uniprot/G5E8B6|||http://purl.uniprot.org/uniprot/Q8BR86 ^@ 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|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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.|||In isoform 3 and isoform 4.|||In isoform 3.|||Kin of IRRE-like protein 3|||N-linked (GlcNAc...) asparagine|||Processed kin of IRRE-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000015099|||http://purl.uniprot.org/annotation/PRO_0000296241|||http://purl.uniprot.org/annotation/VSP_011816|||http://purl.uniprot.org/annotation/VSP_011817|||http://purl.uniprot.org/annotation/VSP_011818|||http://purl.uniprot.org/annotation/VSP_011819|||http://purl.uniprot.org/annotation/VSP_011820 http://togogenome.org/gene/10090:Synpo ^@ http://purl.uniprot.org/uniprot/E9Q3E2|||http://purl.uniprot.org/uniprot/Q3TY32|||http://purl.uniprot.org/uniprot/Q3U336|||http://purl.uniprot.org/uniprot/Q3URF1 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Kcnh7 ^@ http://purl.uniprot.org/uniprot/Q9ER47 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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|||Phosphoserine|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 7|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054016 http://togogenome.org/gene/10090:Aoc1l1 ^@ http://purl.uniprot.org/uniprot/Q6IMK7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Amine oxidase|||Copper amine oxidase N2-terminal|||Copper amine oxidase N3-terminal|||Copper amine oxidase catalytic ^@ http://purl.uniprot.org/annotation/PRO_5015098334 http://togogenome.org/gene/10090:Poll ^@ http://purl.uniprot.org/uniprot/Q9QXE2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ BRCT|||DNA polymerase lambda|||DNA-binding|||Disordered|||Involved in primer binding|||Polar residues|||Schiff-base intermediate with DNA ^@ http://purl.uniprot.org/annotation/PRO_0000218785 http://togogenome.org/gene/10090:Plat ^@ http://purl.uniprot.org/uniprot/P11214 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Charge relay system|||EGF-like|||Fibronectin type-I|||Important for binding to LRP1|||Important for binding to annexin A2|||Important for single-chain activity|||Interchain (between A and B chains)|||Kringle 1|||Kringle 2|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Removed by plasmin|||Tissue-type plasminogen activator|||Tissue-type plasminogen activator chain A|||Tissue-type plasminogen activator chain B ^@ http://purl.uniprot.org/annotation/PRO_0000028353|||http://purl.uniprot.org/annotation/PRO_0000028354|||http://purl.uniprot.org/annotation/PRO_0000028355|||http://purl.uniprot.org/annotation/PRO_0000028356|||http://purl.uniprot.org/annotation/PRO_0000285906 http://togogenome.org/gene/10090:Tnrc6c ^@ http://purl.uniprot.org/uniprot/B1ATC3|||http://purl.uniprot.org/uniprot/Q3UHC0 ^@ 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|||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|||Sufficient for interaction with argonaute family proteins|||Sufficient for translational repression when tethered to a target mRNA|||Trinucleotide repeat-containing gene 6C protein|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000278527 http://togogenome.org/gene/10090:Ceacam1 ^@ http://purl.uniprot.org/uniprot/P31809|||http://purl.uniprot.org/uniprot/Q3LFS8|||http://purl.uniprot.org/uniprot/Q3LFS9|||http://purl.uniprot.org/uniprot/Q925P3 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Carcinoembryonic antigen-related cell adhesion molecule 1|||Cytoplasmic|||Disordered|||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 PTPN11 and PTPN6. Doesn't affect phosphorylation.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with FLNA|||Interaction with calmodulin|||N-linked (GlcNAc...) asparagine|||Phosphorylated on tyrosine. Abrogates interaction with PTPN11. Abrogates interaction with PTPN11 and phosphorylation; when associated with F-488. Suppresses T cell proliferation; when associated with F-488. Increases cytokine production; when associated with F-488. Activates JNK cascade; when associated with F-488. Abrogates CEACAM1-L phosphorylation in endothelial cells upon VEGF stimulation. Impairs interaction with and inactivation of SYK; when associated with F-488.|||Phosphorylated on tyrosine. Abrogates interaction with PTPN11. Abrogates interaction with PTPN11 and phosphorylation; when associated with F-515. Reduces endothelial cell migration and differentiation. Suppresses T cell proliferation; when associated with F-515. Increases cytokine production; when associated with F-515. Activates JNK cascade; when associated with F-515. Abrogates CEACAM1-L phosphorylation in endothelial cells and decreases amounts of released nitric oxide upon VEGF stimulation. Impairs interaction with and inactivation of SYK; when associated with F-515.|||Phosphoserine|||Phosphotyrosine; by INSR, SRC and LCK|||Phosphotyrosine; by SRC, LCK, INSR and EGFR|||Polar residues|||Reduces Tyr phosphorylation by at least 50% and almost completely abrogates interaction with PTPN11 and PTPN6.|||Reduces endothelial cell migration and differentiation.|||Required for homophilic binding|||Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level ^@ http://purl.uniprot.org/annotation/PRO_0000014563|||http://purl.uniprot.org/annotation/PRO_5015097416|||http://purl.uniprot.org/annotation/PRO_5015097417|||http://purl.uniprot.org/annotation/PRO_5015099545|||http://purl.uniprot.org/annotation/VSP_002484|||http://purl.uniprot.org/annotation/VSP_002485|||http://purl.uniprot.org/annotation/VSP_036040|||http://purl.uniprot.org/annotation/VSP_036041|||http://purl.uniprot.org/annotation/VSP_058517 http://togogenome.org/gene/10090:Sh2d4a ^@ http://purl.uniprot.org/uniprot/Q9D7V1 ^@ 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|||SH2|||SH2 domain-containing protein 4A ^@ http://purl.uniprot.org/annotation/PRO_0000233134 http://togogenome.org/gene/10090:Hoxc12 ^@ http://purl.uniprot.org/uniprot/Q8K5B8 ^@ 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_0000248840 http://togogenome.org/gene/10090:Tpbpb ^@ http://purl.uniprot.org/uniprot/Q9CQC0 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Region|||Signal Peptide ^@ Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015099700 http://togogenome.org/gene/10090:Gm38666 ^@ http://purl.uniprot.org/uniprot/Q8K491 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Cadherin C-terminal catenin-binding|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ruvbl2 ^@ http://purl.uniprot.org/uniprot/Q3TXT7|||http://purl.uniprot.org/uniprot/Q9WTM5 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ AAA+ ATPase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Phosphoserine|||Removed|||RuvB-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000165645 http://togogenome.org/gene/10090:Slc12a8 ^@ http://purl.uniprot.org/uniprot/Q8VI23 ^@ 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.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Solute carrier family 12 member 8 ^@ http://purl.uniprot.org/annotation/PRO_0000305288|||http://purl.uniprot.org/annotation/VSP_028333|||http://purl.uniprot.org/annotation/VSP_028334|||http://purl.uniprot.org/annotation/VSP_028335|||http://purl.uniprot.org/annotation/VSP_028336 http://togogenome.org/gene/10090:Uqcrh ^@ http://purl.uniprot.org/uniprot/P99028 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Modified Residue|||Region|||Transit Peptide ^@ Basic and acidic residues|||Cytochrome b-c1 complex subunit 6, mitochondrial|||Disordered|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000035992 http://togogenome.org/gene/10090:Pdcd2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0N5|||http://purl.uniprot.org/uniprot/P46718 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger ^@ MYND-type|||MYND-type; atypical|||Programmed cell death protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000218305 http://togogenome.org/gene/10090:Map7d3 ^@ http://purl.uniprot.org/uniprot/A2AEY4 ^@ 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.|||MAP7 domain-containing protein 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000306813|||http://purl.uniprot.org/annotation/VSP_028500 http://togogenome.org/gene/10090:Or11g25 ^@ http://purl.uniprot.org/uniprot/L7N1Y5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r251 ^@ http://purl.uniprot.org/uniprot/K9J7G2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Csnk1a1 ^@ http://purl.uniprot.org/uniprot/Q6PJ87 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Chst4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1C9|||http://purl.uniprot.org/uniprot/Q9R1I1 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 4|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Sulfotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000085194 http://togogenome.org/gene/10090:Slc38a4 ^@ http://purl.uniprot.org/uniprot/Q8R1S9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ 40% decrease in alanine uptake. Significantly decreases alanine transporter activity. Does not affect cell surface expression.|||Abolishes transport activity.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Influences on amino acid transport capacity|||N-linked (GlcNAc...) asparagine|||No significant effect on alanine uptake.|||No significant effect on alanine uptake. Does not affect alanine transport activity.|||Phosphoserine|||Polar residues|||Sodium-coupled neutral amino acid transporter 4 ^@ http://purl.uniprot.org/annotation/PRO_0000247861 http://togogenome.org/gene/10090:Grina ^@ http://purl.uniprot.org/uniprot/Q9ESF4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Pro residues|||Protein lifeguard 1 ^@ http://purl.uniprot.org/annotation/PRO_0000314440 http://togogenome.org/gene/10090:Ndufaf7 ^@ http://purl.uniprot.org/uniprot/Q9CWG8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Disordered|||In isoform 2.|||Mitochondrion|||Polar residues|||Protein arginine methyltransferase NDUFAF7, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000315673|||http://purl.uniprot.org/annotation/VSP_030608 http://togogenome.org/gene/10090:1700034J05Rik ^@ http://purl.uniprot.org/uniprot/Q80W69 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||Uncharacterized protein C12orf71 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000343578|||http://purl.uniprot.org/annotation/VSP_034616 http://togogenome.org/gene/10090:Gtf2e2 ^@ http://purl.uniprot.org/uniprot/Q3UIR2|||http://purl.uniprot.org/uniprot/Q9D902 ^@ 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 ^@ Basic residues|||Disordered|||General transcription factor IIE subunit 2|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||TFIIE beta ^@ http://purl.uniprot.org/annotation/PRO_0000211227 http://togogenome.org/gene/10090:Ascc3 ^@ http://purl.uniprot.org/uniprot/E9PZJ8 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant ^@ Activating signal cointegrator 1 complex subunit 3|||DEIH box|||DEVH box|||Helicase ATP-binding 1|||Helicase ATP-binding 2|||Helicase C-terminal 1|||Helicase C-terminal 2|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||SEC63 1|||SEC63 2 ^@ http://purl.uniprot.org/annotation/PRO_0000416915|||http://purl.uniprot.org/annotation/VSP_042999 http://togogenome.org/gene/10090:Dthd1 ^@ http://purl.uniprot.org/uniprot/E9PZX1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Death|||Disordered|||Polar residues|||ZU5 ^@ http://togogenome.org/gene/10090:Prpf19 ^@ http://purl.uniprot.org/uniprot/Q99KP6 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||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_0000051146|||http://purl.uniprot.org/annotation/VSP_011945|||http://purl.uniprot.org/annotation/VSP_012192 http://togogenome.org/gene/10090:Mob1a ^@ http://purl.uniprot.org/uniprot/Q921Y0 ^@ 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.|||MOB kinase activator 1A|||N-acetylserine|||Phosphothreonine|||Phosphothreonine; by STK3/MST2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000193567|||http://purl.uniprot.org/annotation/VSP_012297 http://togogenome.org/gene/10090:Or8k1 ^@ http://purl.uniprot.org/uniprot/Q7TR79 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H4c2 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Tekt5 ^@ http://purl.uniprot.org/uniprot/G5E8A8 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Repeat|||Splice Variant ^@ 1|||2|||3|||4|||5|||6|||6 X 6 AA approximate tandem repeats of C-[GSK]-G-[GSPH]-A-[SLP]|||In isoform 2.|||Tektin-5 ^@ http://purl.uniprot.org/annotation/PRO_0000436475|||http://purl.uniprot.org/annotation/VSP_058377 http://togogenome.org/gene/10090:B430306N03Rik ^@ http://purl.uniprot.org/uniprot/Q6QX36 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015098475 http://togogenome.org/gene/10090:Hal ^@ http://purl.uniprot.org/uniprot/B2RXW1|||http://purl.uniprot.org/uniprot/P35492|||http://purl.uniprot.org/uniprot/Q8CE60 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Variant ^@ 2,3-didehydroalanine (Ser)|||5-imidazolinone (Ala-Gly)|||Histidine ammonia-lyase|||In His; reduced stability.|||Par3/HAL N-terminal|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000161059 http://togogenome.org/gene/10090:Ccdc177 ^@ http://purl.uniprot.org/uniprot/Q3UHB8 ^@ 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|||Coiled-coil domain-containing protein 177|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000420411 http://togogenome.org/gene/10090:Wbp1l ^@ http://purl.uniprot.org/uniprot/Q8BGW2 ^@ 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 and isoform 3.|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Polar residues|||Pro residues|||WW domain binding protein 1-like ^@ http://purl.uniprot.org/annotation/PRO_0000241451|||http://purl.uniprot.org/annotation/VSP_019442|||http://purl.uniprot.org/annotation/VSP_019443|||http://purl.uniprot.org/annotation/VSP_041951|||http://purl.uniprot.org/annotation/VSP_041952 http://togogenome.org/gene/10090:Ccdc146 ^@ http://purl.uniprot.org/uniprot/E9Q9F7|||http://purl.uniprot.org/uniprot/Q5DTX2|||http://purl.uniprot.org/uniprot/Q9D511 ^@ Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Klhl23 ^@ http://purl.uniprot.org/uniprot/Q6GQU2 ^@ 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 23 ^@ http://purl.uniprot.org/annotation/PRO_0000242158 http://togogenome.org/gene/10090:Fcrl5 ^@ http://purl.uniprot.org/uniprot/Q68SN8 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fc receptor-like protein 5|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000331641|||http://purl.uniprot.org/annotation/VSP_033309 http://togogenome.org/gene/10090:Rida ^@ http://purl.uniprot.org/uniprot/P52760 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ 2-iminobutanoate/2-iminopropanoate deaminase|||N-acetylserine|||N6-succinyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000170309 http://togogenome.org/gene/10090:Tsc22d3 ^@ http://purl.uniprot.org/uniprot/Q9Z2S7 ^@ 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 3.|||In isoform 4.|||Leucine-zipper|||Phosphoserine|||Phosphothreonine|||TSC22 domain family protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000219371|||http://purl.uniprot.org/annotation/VSP_012690|||http://purl.uniprot.org/annotation/VSP_012691|||http://purl.uniprot.org/annotation/VSP_055016 http://togogenome.org/gene/10090:Cd36 ^@ http://purl.uniprot.org/uniprot/Q08857|||http://purl.uniprot.org/uniprot/Q3U6Y9|||http://purl.uniprot.org/uniprot/Q3UAI3|||http://purl.uniprot.org/uniprot/Q3UC79|||http://purl.uniprot.org/uniprot/Q8C6Z4 ^@ Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Site|||Topological Domain|||Transmembrane ^@ Critical for TLR4-TLR6 dimerization and signaling|||Cytoplasmic|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Interaction with PTK2, PXN and LYN|||N-linked (GlcNAc...) asparagine|||Platelet glycoprotein 4|||Required for interaction with thrombospondins, THBS1 and THBS2|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000144153 http://togogenome.org/gene/10090:Ikzf4 ^@ http://purl.uniprot.org/uniprot/A0A571BEH5|||http://purl.uniprot.org/uniprot/Q8C208 ^@ 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 ^@ C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||CTBP-binding motif PEDLG|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with FOXP3|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Zinc finger protein Eos ^@ http://purl.uniprot.org/annotation/PRO_0000299469|||http://purl.uniprot.org/annotation/VSP_027689|||http://purl.uniprot.org/annotation/VSP_027690|||http://purl.uniprot.org/annotation/VSP_027691 http://togogenome.org/gene/10090:Mcm10 ^@ http://purl.uniprot.org/uniprot/Q0VBD2 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000278321 http://togogenome.org/gene/10090:Ttbk2 ^@ http://purl.uniprot.org/uniprot/A2AW15|||http://purl.uniprot.org/uniprot/Q3UVR3 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes serine/threonine-protein kinase activity and ability to initiate ciliogenesis.|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Tau-tubulin kinase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000234343|||http://purl.uniprot.org/annotation/VSP_018276 http://togogenome.org/gene/10090:Acot5 ^@ http://purl.uniprot.org/uniprot/Q6Q2Z6|||http://purl.uniprot.org/uniprot/Q91YQ6 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase|||Acyl-coenzyme A thioesterase 5|||BAAT/Acyl-CoA thioester hydrolase C-terminal|||Charge relay system|||Disordered|||Microbody targeting signal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000202151 http://togogenome.org/gene/10090:Slc9a2 ^@ http://purl.uniprot.org/uniprot/Q3ZAS0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Sodium/hydrogen exchanger 2 ^@ http://purl.uniprot.org/annotation/PRO_5015097548 http://togogenome.org/gene/10090:Or4d10b ^@ http://purl.uniprot.org/uniprot/Q8VFV1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tent5a ^@ http://purl.uniprot.org/uniprot/D3Z5S8 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Mutagenesis Site ^@ Homozygous mice show severe morphological and skeletal abnormalities including short stature along with limb, rib, pelvis, and skull deformities with minimal trabecular bone and reduced cortical bone thickness in long bones.|||Terminal nucleotidyltransferase 5A ^@ http://purl.uniprot.org/annotation/PRO_0000454711 http://togogenome.org/gene/10090:Ldoc1 ^@ http://purl.uniprot.org/uniprot/Q7TPY9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Acidic residues|||Disordered|||Protein LDOC1 ^@ http://purl.uniprot.org/annotation/PRO_0000084392 http://togogenome.org/gene/10090:Gm4565 ^@ http://purl.uniprot.org/uniprot/A0A140LJ87 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Dact3 ^@ http://purl.uniprot.org/uniprot/Q0PHV7 ^@ 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_0000264617 http://togogenome.org/gene/10090:Wars2 ^@ http://purl.uniprot.org/uniprot/Q9CYK1 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||Tryptophan--tRNA ligase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000035829 http://togogenome.org/gene/10090:Edn3 ^@ http://purl.uniprot.org/uniprot/A2APU5|||http://purl.uniprot.org/uniprot/P48299 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide|||Site ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Peptide|||Propeptide|||Region|||Signal Peptide|||Site ^@ Basic and acidic residues|||Cleavage; by KEL|||Disordered|||Endothelin-3|||Endothelin-like|||Endothelin-like toxin ^@ http://purl.uniprot.org/annotation/PRO_0000008114|||http://purl.uniprot.org/annotation/PRO_0000008115|||http://purl.uniprot.org/annotation/PRO_0000008116|||http://purl.uniprot.org/annotation/PRO_5014296789 http://togogenome.org/gene/10090:Snip1 ^@ http://purl.uniprot.org/uniprot/Q8BIZ6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||Phosphoserine|||Smad nuclear-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072010 http://togogenome.org/gene/10090:Adora1 ^@ http://purl.uniprot.org/uniprot/Q3URG8|||http://purl.uniprot.org/uniprot/Q3UYG0|||http://purl.uniprot.org/uniprot/Q60612|||http://purl.uniprot.org/uniprot/Q6AXD8|||http://purl.uniprot.org/uniprot/Q8CAH1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Adenosine receptor A1|||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_0000068992 http://togogenome.org/gene/10090:Asb4 ^@ http://purl.uniprot.org/uniprot/Q9WV71 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Site ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Site ^@ (3S)-3-hydroxyasparagine; by HIF1AN; partial|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Abolishes interaction with HIF1AN.|||Abolishes interaction with HIF1AN. Fails to induce expansion of the hematovascular lineage in embryonic stem cells.|||Ankyrin repeat and SOCS box protein 4|||Essential for interaction with HIF1AN|||Impairs interaction with HIF1AN.|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066929 http://togogenome.org/gene/10090:Gabpa ^@ http://purl.uniprot.org/uniprot/Q00422 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||ETS|||GA-binding protein alpha chain|||PNT|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000204128 http://togogenome.org/gene/10090:Brinp2 ^@ http://purl.uniprot.org/uniprot/Q6DFY8 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ BMP/retinoic acid-inducible neural-specific protein 2|||MACPF|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000045771 http://togogenome.org/gene/10090:Spin2e ^@ http://purl.uniprot.org/uniprot/A0A571BDE3 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Hmbs ^@ http://purl.uniprot.org/uniprot/P22907|||http://purl.uniprot.org/uniprot/Q3UBC6|||http://purl.uniprot.org/uniprot/Q3UPG1 ^@ 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.|||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_0000143035|||http://purl.uniprot.org/annotation/VSP_002068 http://togogenome.org/gene/10090:Elmod1 ^@ http://purl.uniprot.org/uniprot/Q3V1U8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ ELMO|||ELMO domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000225015 http://togogenome.org/gene/10090:Phykpl ^@ http://purl.uniprot.org/uniprot/Q8R1K4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ 5-phosphohydroxy-L-lysine phospho-lyase|||In isoform 2.|||In isoform 3.|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_0000287668|||http://purl.uniprot.org/annotation/VSP_025586|||http://purl.uniprot.org/annotation/VSP_025587|||http://purl.uniprot.org/annotation/VSP_025588 http://togogenome.org/gene/10090:R3hdm4 ^@ http://purl.uniprot.org/uniprot/B2RRK4|||http://purl.uniprot.org/uniprot/Q4VBF2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||R3H|||R3H domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000281432 http://togogenome.org/gene/10090:Sowahc ^@ http://purl.uniprot.org/uniprot/Q8C0J6 ^@ 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|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000274341 http://togogenome.org/gene/10090:Uqcc5 ^@ http://purl.uniprot.org/uniprot/A0A0R3P9C4|||http://purl.uniprot.org/uniprot/Q8C1Q6 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Splice Variant|||Topological Domain|||Transmembrane ^@ Helical|||In isoform 2.|||In isoform 3.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Ubiquinol-cytochrome c reductase complex assembly factor 5 ^@ http://purl.uniprot.org/annotation/PRO_0000349244|||http://purl.uniprot.org/annotation/VSP_035265|||http://purl.uniprot.org/annotation/VSP_035266|||http://purl.uniprot.org/annotation/VSP_035267 http://togogenome.org/gene/10090:Or4a68 ^@ http://purl.uniprot.org/uniprot/Q8VG73 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:1810037I17Rik ^@ http://purl.uniprot.org/uniprot/Q99M08 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||N-acetylmethionine|||Phosphoserine|||Uncharacterized protein C4orf3 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000325785 http://togogenome.org/gene/10090:Slf1 ^@ http://purl.uniprot.org/uniprot/Q8R3P9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||BRCT 1|||BRCT 2|||Disordered|||In isoform 2.|||NSE5-like domain; mediates interaction with SLF2|||SMC5-SMC6 complex localization factor protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000243907|||http://purl.uniprot.org/annotation/VSP_034415|||http://purl.uniprot.org/annotation/VSP_034416 http://togogenome.org/gene/10090:Mamdc2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0J7|||http://purl.uniprot.org/uniprot/Q8CG85 ^@ 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 ^@ Disordered|||MAM|||MAM 1|||MAM 2|||MAM 3|||MAM 4|||MAM domain-containing protein 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014863|||http://purl.uniprot.org/annotation/PRO_5006451974 http://togogenome.org/gene/10090:Jak1 ^@ http://purl.uniprot.org/uniprot/B1ASP2|||http://purl.uniprot.org/uniprot/Q3U8P8|||http://purl.uniprot.org/uniprot/Q3URU8 ^@ Active Site|||Binding Site|||Coiled-Coil|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Coiled-Coil|||Domain Extent ^@ FERM|||Protein kinase|||Proton acceptor|||SH2 ^@ http://togogenome.org/gene/10090:Cdk12 ^@ http://purl.uniprot.org/uniprot/Q14AX6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||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|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||Cyclin-dependent kinase 12|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000314470|||http://purl.uniprot.org/annotation/VSP_030285|||http://purl.uniprot.org/annotation/VSP_030286|||http://purl.uniprot.org/annotation/VSP_030287 http://togogenome.org/gene/10090:Mpig6b ^@ http://purl.uniprot.org/uniprot/D3YVS6|||http://purl.uniprot.org/uniprot/D7PDD4 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Motif|||Signal Peptide|||Transmembrane ^@ Helical|||ITIM motif|||Megakaryocyte and platelet inhibitory receptor G6b|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_5003053081|||http://purl.uniprot.org/annotation/PRO_5009689216 http://togogenome.org/gene/10090:Daw1 ^@ http://purl.uniprot.org/uniprot/A6H6T7 ^@ Region|||Repeat ^@ Repeat ^@ WD ^@ http://togogenome.org/gene/10090:Zdbf2 ^@ http://purl.uniprot.org/uniprot/A0A6I8MWW6|||http://purl.uniprot.org/uniprot/Q5SS00 ^@ 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|||DBF4-type|||DBF4-type zinc finger-containing protein 2 homolog|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314167 http://togogenome.org/gene/10090:Cntd1 ^@ http://purl.uniprot.org/uniprot/Q9D995 ^@ 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 N-terminal domain-containing protein 1|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000313716|||http://purl.uniprot.org/annotation/VSP_061282 http://togogenome.org/gene/10090:G2e3 ^@ http://purl.uniprot.org/uniprot/E9Q7C2|||http://purl.uniprot.org/uniprot/E9Q7E5|||http://purl.uniprot.org/uniprot/Q5RJY2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger ^@ C2HC pre-PHD-type|||G2/M phase-specific E3 ubiquitin-protein ligase|||HECT|||PHD-type|||PHD-type 1|||PHD-type 2; degenerate|||PHD-type 3 ^@ http://purl.uniprot.org/annotation/PRO_0000248345 http://togogenome.org/gene/10090:Cfap70 ^@ http://purl.uniprot.org/uniprot/D3YVL2 ^@ 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 ^@ Basic and acidic residues|||Cilia- and flagella-associated protein 70|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8 ^@ http://purl.uniprot.org/annotation/PRO_0000449347|||http://purl.uniprot.org/annotation/VSP_060549|||http://purl.uniprot.org/annotation/VSP_060550|||http://purl.uniprot.org/annotation/VSP_060551 http://togogenome.org/gene/10090:Mtf2 ^@ http://purl.uniprot.org/uniprot/Q02395 ^@ 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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Metal-response element-binding transcription factor 2|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tudor ^@ http://purl.uniprot.org/annotation/PRO_0000059318|||http://purl.uniprot.org/annotation/VSP_016240 http://togogenome.org/gene/10090:Psma1 ^@ http://purl.uniprot.org/uniprot/Q3TS44|||http://purl.uniprot.org/uniprot/Q9R1P4 ^@ Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||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_0000124062 http://togogenome.org/gene/10090:Nrd1 ^@ http://purl.uniprot.org/uniprot/A2A9Q2|||http://purl.uniprot.org/uniprot/A6PWC3|||http://purl.uniprot.org/uniprot/Q8BHG1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Nardilysin|||Peptidase M16 C-terminal|||Peptidase M16 N-terminal|||Peptidase M16 middle/third|||Phosphoserine|||Polar residues|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000026756 http://togogenome.org/gene/10090:Zfp111 ^@ http://purl.uniprot.org/uniprot/Q99K53|||http://purl.uniprot.org/uniprot/Q9R164 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Bok ^@ http://purl.uniprot.org/uniprot/O35425|||http://purl.uniprot.org/uniprot/Q3TH93 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Transmembrane ^@ BH1|||BH2|||BH3|||BH4|||Bcl-2 Bcl-2 homology region 1-3|||Bcl-2-related ovarian killer protein|||Disrupts homodimerization. Positively regulates intrinsic apoptotic signaling pathway.|||Does not interact with ITPR1.|||Does not interact with ITPR1. Triggers apoptosis.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||Increases protein expression and stability; when associated with R-25, R-160 and R-177. Increases apoptosis; when associated with R-25, R-160 and R-177.|||Increases protein expression and stability; when associated with R-25, R-32 and R-160. Increases apoptosis; when associated with R-25, R-32 and R-160.|||Increases protein expression and stability; when associated with R-25, R-32 and R-177. Increases apoptosis; when associated with R-25, R-32 and R-177.|||Increases protein expression and stability; when associated with R-32, R-160 and R-177. Increases apoptosis; when associated with R-32, R-160 and R-177.|||Interactions with ITPR1|||No change in apoptosis induction; when associated with Q-71 and Q-74.|||No change in apoptosis induction; when associated with Q-71 and Q-78.|||No change in apoptosis induction; when associated with Q-74 and Q-78.|||Nuclear export signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000143087|||http://purl.uniprot.org/annotation/VSP_058600 http://togogenome.org/gene/10090:St3gal3 ^@ http://purl.uniprot.org/uniprot/P97325|||http://purl.uniprot.org/uniprot/Q3UWD5|||http://purl.uniprot.org/uniprot/Q9CZ48|||http://purl.uniprot.org/uniprot/Q9DBB6 ^@ 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 ^@ CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149267 http://togogenome.org/gene/10090:Cyp4a12b ^@ http://purl.uniprot.org/uniprot/A2A974 ^@ Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Signal Peptide ^@ Cytochrome P450 4A12B|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000448898 http://togogenome.org/gene/10090:Ptgfrn ^@ http://purl.uniprot.org/uniprot/Q9WV91 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||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_0000014763 http://togogenome.org/gene/10090:Cdx2 ^@ http://purl.uniprot.org/uniprot/P43241|||http://purl.uniprot.org/uniprot/Q543L9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 4S motif; modulates transactivation activity and protein stability|||Disordered|||Homeobox|||Homeobox protein CDX-2|||Interaction with 5-mCpG DNA|||Interaction with DNA|||Phosphoserine|||Phosphoserine; by CDK2|||Pro residues|||Reduced phosphorylation. Does not affect nuclear localization. ^@ http://purl.uniprot.org/annotation/PRO_0000048851 http://togogenome.org/gene/10090:Il2rg ^@ http://purl.uniprot.org/uniprot/P34902|||http://purl.uniprot.org/uniprot/Q3UPA9|||http://purl.uniprot.org/uniprot/V5SIM2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Box 1 motif|||Cytokine receptor common subunit gamma|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III domain-containing protein|||Helical|||N-linked (GlcNAc...) asparagine|||Type I cytokine receptor cytokine-binding|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010867|||http://purl.uniprot.org/annotation/PRO_5004740773|||http://purl.uniprot.org/annotation/PRO_5014309216 http://togogenome.org/gene/10090:Fam120b ^@ http://purl.uniprot.org/uniprot/Q6RI63 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant ^@ Constitutive coactivator of peroxisome proliferator-activated receptor gamma|||Disordered|||In isoform 2.|||Mediates transactivation of PPARG|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000332991|||http://purl.uniprot.org/annotation/VSP_033417|||http://purl.uniprot.org/annotation/VSP_033418 http://togogenome.org/gene/10090:Btbd35f14 ^@ http://purl.uniprot.org/uniprot/Q1LZI5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Tmem145 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPQ2|||http://purl.uniprot.org/uniprot/E9PUE6|||http://purl.uniprot.org/uniprot/Q8C4U2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||GPR180/TMEM145 transmembrane|||Helical|||N-linked (GlcNAc...) asparagine|||Pro residues|||Transmembrane protein 145 ^@ http://purl.uniprot.org/annotation/PRO_0000280356|||http://purl.uniprot.org/annotation/PRO_5003242979|||http://purl.uniprot.org/annotation/PRO_5023887791 http://togogenome.org/gene/10090:Ppp1r14bl ^@ http://purl.uniprot.org/uniprot/Q14BX6 ^@ Coiled-Coil|||Region ^@ Coiled-Coil|||Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Zfp292 ^@ http://purl.uniprot.org/uniprot/Q9Z2U2 ^@ 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|||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 isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Zinc finger protein 292 ^@ http://purl.uniprot.org/annotation/PRO_0000392944|||http://purl.uniprot.org/annotation/VSP_053207 http://togogenome.org/gene/10090:Ctsb ^@ http://purl.uniprot.org/uniprot/P10605 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cathepsin B|||Cathepsin B heavy chain|||Cathepsin B light chain|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000026148|||http://purl.uniprot.org/annotation/PRO_0000026149|||http://purl.uniprot.org/annotation/PRO_0000026150|||http://purl.uniprot.org/annotation/PRO_0000026151|||http://purl.uniprot.org/annotation/PRO_0000026152 http://togogenome.org/gene/10090:Ankrd27 ^@ http://purl.uniprot.org/uniprot/A0A0R4J2C4|||http://purl.uniprot.org/uniprot/Q3UMR0 ^@ 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 ^@ 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 and RAB38; inhibits peripheral distribution of TYRP1 in melanocytes; no effect on dendrite formation in melanocytes.|||Impairs interaction with RAB32 and RAB38.|||In isoform 2.|||In isoform 3.|||Inhibits dendrite formation.|||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_0000274557|||http://purl.uniprot.org/annotation/VSP_022791|||http://purl.uniprot.org/annotation/VSP_022792 http://togogenome.org/gene/10090:Or5b3 ^@ http://purl.uniprot.org/uniprot/Q8VFW5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lifr ^@ http://purl.uniprot.org/uniprot/P42703|||http://purl.uniprot.org/uniprot/Q3UKU5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 isoform 2.|||Leukemia inhibitory factor receptor|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010903|||http://purl.uniprot.org/annotation/VSP_001686|||http://purl.uniprot.org/annotation/VSP_001687 http://togogenome.org/gene/10090:Gm10334 ^@ http://purl.uniprot.org/uniprot/Q792Y8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015098653 http://togogenome.org/gene/10090:Vmn1r54 ^@ http://purl.uniprot.org/uniprot/Q9EPB8 ^@ 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|||Vomeronasal type-1 receptor 54 ^@ http://purl.uniprot.org/annotation/PRO_0000239966 http://togogenome.org/gene/10090:Svip ^@ http://purl.uniprot.org/uniprot/Q3TYK1|||http://purl.uniprot.org/uniprot/Q3UZP4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal 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_0000280799 http://togogenome.org/gene/10090:Gm1123 ^@ http://purl.uniprot.org/uniprot/Q1RME4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097181 http://togogenome.org/gene/10090:Mtfmt ^@ http://purl.uniprot.org/uniprot/Q3V021|||http://purl.uniprot.org/uniprot/Q9D799 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide ^@ Formyl transferase C-terminal|||Formyl transferase N-terminal|||Methionyl-tRNA formyltransferase, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000010094 http://togogenome.org/gene/10090:Six1 ^@ http://purl.uniprot.org/uniprot/Q3V2C3|||http://purl.uniprot.org/uniprot/Q62231|||http://purl.uniprot.org/uniprot/Q8BSP4 ^@ 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 and acidic residues|||Disordered|||Homeobox|||Homeobox protein SIX1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049296 http://togogenome.org/gene/10090:Tssk5 ^@ http://purl.uniprot.org/uniprot/Q8C1R0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Protein kinase|||Proton acceptor|||Testis-specific serine/threonine-protein kinase 5 ^@ http://purl.uniprot.org/annotation/PRO_0000281894 http://togogenome.org/gene/10090:Strc ^@ http://purl.uniprot.org/uniprot/Q8VIM6 ^@ 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 ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Pro residues|||Stereocilin ^@ http://purl.uniprot.org/annotation/PRO_0000022427 http://togogenome.org/gene/10090:Preb ^@ http://purl.uniprot.org/uniprot/D3Z3S1|||http://purl.uniprot.org/uniprot/Q3UAP1|||http://purl.uniprot.org/uniprot/Q9WUQ2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 3'-nitrotyrosine|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Prolactin regulatory element-binding protein|||WD|||WD 1|||WD 2|||WD 3 ^@ http://purl.uniprot.org/annotation/PRO_0000051155 http://togogenome.org/gene/10090:Irf3 ^@ http://purl.uniprot.org/uniprot/P70671|||http://purl.uniprot.org/uniprot/Q3U9K6 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Site|||Strand|||Turn ^@ Cleavage; by CASP3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||IRF tryptophan pentad repeat|||Interaction with HERC5|||Interferon regulatory factor 3|||Mediates interaction with ZDHHC11|||Phosphoserine|||Phosphoserine; by IKKE|||Phosphoserine; by TBK1|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000154554 http://togogenome.org/gene/10090:Gng4 ^@ http://purl.uniprot.org/uniprot/P50153 ^@ 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-4|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000012623|||http://purl.uniprot.org/annotation/PRO_0000012624 http://togogenome.org/gene/10090:Rbm33 ^@ http://purl.uniprot.org/uniprot/D3Z5I9|||http://purl.uniprot.org/uniprot/Q9CXK9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pro residues|||RNA-binding protein 33|||RRM|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000285045|||http://purl.uniprot.org/annotation/VSP_030148|||http://purl.uniprot.org/annotation/VSP_030149 http://togogenome.org/gene/10090:Dhx9 ^@ http://purl.uniprot.org/uniprot/A0A087WPL5|||http://purl.uniprot.org/uniprot/O70133|||http://purl.uniprot.org/uniprot/Q05BR6|||http://purl.uniprot.org/uniprot/Q3TF92 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ ATP-dependent RNA helicase A|||Asymmetric dimethylarginine|||Basic and acidic residues|||Core helicase|||DEAD-box helicase OB fold|||DEAH box|||DRBM|||DRBM 1|||DRBM 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HA2|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||Interaction with BRCA1|||Interaction with CREBBP|||MTAD|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||NTD region|||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|||siRNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000055158|||http://purl.uniprot.org/annotation/VSP_014778|||http://purl.uniprot.org/annotation/VSP_014779 http://togogenome.org/gene/10090:Or10d4 ^@ http://purl.uniprot.org/uniprot/Q7TRA9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fhod1 ^@ http://purl.uniprot.org/uniprot/Q6P9Q4 ^@ 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|||DAD|||Disordered|||FH1|||FH1/FH2 domain-containing protein 1|||FH2|||GBD/FH3|||Interaction with ROCK1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000194906 http://togogenome.org/gene/10090:Chmp1b2 ^@ http://purl.uniprot.org/uniprot/Q9CQD4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region ^@ Charged multivesicular body protein 1B2|||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_0000211456 http://togogenome.org/gene/10090:Foxl1 ^@ http://purl.uniprot.org/uniprot/Q64731 ^@ 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|||Fork-head|||Forkhead box protein L1 ^@ http://purl.uniprot.org/annotation/PRO_0000091860 http://togogenome.org/gene/10090:Clptm1l ^@ http://purl.uniprot.org/uniprot/Q8BXA5 ^@ 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|||Lipid scramblase CLPTM1L|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000331301 http://togogenome.org/gene/10090:Crx ^@ http://purl.uniprot.org/uniprot/A0A0A0MQN6|||http://purl.uniprot.org/uniprot/O54751|||http://purl.uniprot.org/uniprot/Q543C9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Cone-rod homeobox protein|||Disordered|||Homeobox|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048863 http://togogenome.org/gene/10090:Nnt ^@ http://purl.uniprot.org/uniprot/Q8BGK0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Alanine dehydrogenase/pyridine nucleotide transhydrogenase N-terminal|||Alanine dehydrogenase/pyridine nucleotide transhydrogenase NAD(H)-binding|||Helical ^@ http://togogenome.org/gene/10090:Ica1 ^@ http://purl.uniprot.org/uniprot/P97411 ^@ 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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084131|||http://purl.uniprot.org/annotation/VSP_050425|||http://purl.uniprot.org/annotation/VSP_050426 http://togogenome.org/gene/10090:Mesp1 ^@ http://purl.uniprot.org/uniprot/P97309 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ CPLCP|||Disordered|||Mesoderm posterior protein 1|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000304405 http://togogenome.org/gene/10090:Golgb1 ^@ http://purl.uniprot.org/uniprot/E9PVZ8|||http://purl.uniprot.org/uniprot/E9QAH1 ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Transmembrane ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Cbfa2t2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1D5|||http://purl.uniprot.org/uniprot/O70374|||http://purl.uniprot.org/uniprot/Q3UGB2 ^@ 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|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Disrupts interaction with PRDM14.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with PRDM14|||MYND-type|||Nervy homology region 2 (NHR2)|||Nervy homology region 3 (NHR3)|||Phosphoserine|||Polar residues|||Protein CBFA2T2|||Reduces PRDM14 and OCT14 occupancy on target sites, no effect on interaction with PRDM14, predicted to impair homooligomerization; when associated with R-330; R-342; E-346; E-360; R-363 and R-374.|||Reduces PRDM14 and OCT14 occupancy on target sites, no effect on interaction with PRDM14, predicted to impair homooligomerization; when associated with R-330; R-342; R-345; E-346; E-360 and R-363.|||Reduces PRDM14 and OCT14 occupancy on target sites, no effect on interaction with PRDM14, predicted to impair homooligomerization; when associated with R-330; R-342; R-345; E-346; E-360 and R-374.|||Reduces PRDM14 and OCT14 occupancy on target sites, no effect on interaction with PRDM14, predicted to impair homooligomerization; when associated with R-330; R-342; R-345; E-346; E-360; R-363 and R-374.|||Reduces PRDM14 and OCT14 occupancy on target sites, no effect on interaction with PRDM14, predicted to impair homooligomerization; when associated with R-330; R-342; R-345; R-363 and R-374.|||Reduces PRDM14 and OCT14 occupancy on target sites, no effect on interaction with PRDM14, predicted to impair homooligomerization; when associated with R-330; R-345; E-346; E-360; R-363 and R-374.|||Reduces PRDM14 and OCT14 occupancy on target sites, no effect on interaction with PRDM14, predicted to impair homooligomerization; when associated with R-342; R-345; E-346; E-360; R-363 and R-374.|||TAFH ^@ http://purl.uniprot.org/annotation/PRO_0000218302|||http://purl.uniprot.org/annotation/VSP_030517 http://togogenome.org/gene/10090:Nox3 ^@ http://purl.uniprot.org/uniprot/Q672J9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Defects in otoconia biogenesis.|||Extracellular|||FAD-binding FR-type|||Ferric oxidoreductase|||Helical|||N-linked (GlcNAc...) asparagine|||NADPH oxidase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000227597 http://togogenome.org/gene/10090:Lyn ^@ http://purl.uniprot.org/uniprot/P25911|||http://purl.uniprot.org/uniprot/Q3TCS3|||http://purl.uniprot.org/uniprot/Q3U6Q5|||http://purl.uniprot.org/uniprot/Q8CEI0 ^@ 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 Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Abolishes autoinhibition, leading to increased kinase activity and constitutive phosphorylation of LYN substrates.|||Basic and acidic residues|||Disordered|||In isoform 2.|||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|||Tyrosine-protein kinase Lyn ^@ http://purl.uniprot.org/annotation/PRO_0000088130|||http://purl.uniprot.org/annotation/VSP_005003 http://togogenome.org/gene/10090:Plekha3 ^@ http://purl.uniprot.org/uniprot/Q9ERS4 ^@ 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|||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_0000053879 http://togogenome.org/gene/10090:Cyp2d9 ^@ http://purl.uniprot.org/uniprot/P11714 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Cytochrome P450 2D9|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051734 http://togogenome.org/gene/10090:Sik3 ^@ http://purl.uniprot.org/uniprot/Q6P4S6 ^@ 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 ^@ Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase SIK3|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000252258|||http://purl.uniprot.org/annotation/VSP_020894|||http://purl.uniprot.org/annotation/VSP_020895 http://togogenome.org/gene/10090:Aurkc ^@ http://purl.uniprot.org/uniprot/E9QL04|||http://purl.uniprot.org/uniprot/O88445|||http://purl.uniprot.org/uniprot/Q497X5 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict ^@ Aurora kinase C|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs kinase activity, when associated with A-171.|||Impairs kinase activity, when associated with A-175.|||Phosphothreonine; by PKA|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085661 http://togogenome.org/gene/10090:Larp4b ^@ http://purl.uniprot.org/uniprot/Q6A0A2 ^@ 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|||HTH La-type RNA-binding|||In isoform 2.|||In isoform 3.|||La-related protein 4B|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000281140|||http://purl.uniprot.org/annotation/VSP_023987|||http://purl.uniprot.org/annotation/VSP_023988 http://togogenome.org/gene/10090:Gid8 ^@ http://purl.uniprot.org/uniprot/Q9D7M1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ CTLH|||Glucose-induced degradation protein 8 homolog|||Interaction with CTNNB1|||LisH ^@ http://purl.uniprot.org/annotation/PRO_0000079412 http://togogenome.org/gene/10090:Thbs2 ^@ http://purl.uniprot.org/uniprot/Q03350 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||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_0000035847 http://togogenome.org/gene/10090:Tgif2lx1 ^@ http://purl.uniprot.org/uniprot/Q8K5B9 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Ang5 ^@ http://purl.uniprot.org/uniprot/Q5GAN1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_5015020045 http://togogenome.org/gene/10090:Sost ^@ http://purl.uniprot.org/uniprot/Q99P68 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Basic and acidic residues|||CTCK|||Disordered|||N-linked (GlcNAc...) asparagine|||Sclerostin ^@ http://purl.uniprot.org/annotation/PRO_0000033178 http://togogenome.org/gene/10090:Ptpn2 ^@ http://purl.uniprot.org/uniprot/Q06180 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Catalytically inactive. Unable to restore phosphatase activity toward PDGFRB.|||Endoplasmic reticulum location|||In isoform 2.|||Mediates interaction with STX17|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||S-nitrosocysteine|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000094753|||http://purl.uniprot.org/annotation/VSP_012367 http://togogenome.org/gene/10090:Tmem191 ^@ http://purl.uniprot.org/uniprot/Q9JJB1 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Transmembrane protein 191 ^@ http://purl.uniprot.org/annotation/PRO_0000340718|||http://purl.uniprot.org/annotation/VSP_057637 http://togogenome.org/gene/10090:Micu1 ^@ http://purl.uniprot.org/uniprot/Q8VCX5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Abolishes interaction with MICU2.|||Acts as a dominant negative mutant that reduces the mitochondrial Ca(2+) peaks; when associated with A-233; A-244 and A-423.|||Acts as a dominant negative mutant that reduces the mitochondrial Ca(2+) peaks; when associated with A-233; A-244 and A-434.|||Acts as a dominant negative mutant that reduces the mitochondrial Ca(2+) peaks; when associated with A-233; A-423 and A-434.|||Acts as a dominant negative mutant that reduces the mitochondrial Ca(2+) peaks; when associated with A-244; A-423 and A-434.|||Basic and acidic residues|||C-helix region|||Calcium uptake protein 1, mitochondrial|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Helical|||In isoform 2.|||In isoform 3.|||Interchain (with C-410 in MICU2)|||Mitochondrial intermembrane|||Mitochondrion|||No effect.|||Polybasic region ^@ http://purl.uniprot.org/annotation/PRO_0000322992|||http://purl.uniprot.org/annotation/VSP_031982|||http://purl.uniprot.org/annotation/VSP_031983 http://togogenome.org/gene/10090:Rap1a ^@ http://purl.uniprot.org/uniprot/P62835 ^@ 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|||Ras-related protein Rap-1A|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000030201|||http://purl.uniprot.org/annotation/PRO_0000030202 http://togogenome.org/gene/10090:Elk1 ^@ http://purl.uniprot.org/uniprot/P41969 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||ETS|||ETS domain-containing protein Elk-1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Phosphoserine; by MAPK1|||Phosphoserine; by MAPK1 and MAPK8|||Phosphothreonine; by MAPK1|||Polar residues|||Pro residues|||Sufficient for interaction with MAD2L2 ^@ http://purl.uniprot.org/annotation/PRO_0000204096 http://togogenome.org/gene/10090:Cox19 ^@ http://purl.uniprot.org/uniprot/Q8K0C8 ^@ 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_0000273152 http://togogenome.org/gene/10090:Plxna3 ^@ http://purl.uniprot.org/uniprot/A0A158SIT4|||http://purl.uniprot.org/uniprot/P70208 ^@ 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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes response to semaphorin.|||Almost abolishes response to semaphorin.|||Cytoplasmic|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Plexin-A3|||Sema|||Strongly reduced response to semaphorin. ^@ http://purl.uniprot.org/annotation/PRO_0000411104|||http://purl.uniprot.org/annotation/PRO_5014248912|||http://purl.uniprot.org/annotation/VSP_041609 http://togogenome.org/gene/10090:Jph3 ^@ http://purl.uniprot.org/uniprot/Q9ET77 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||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_0000159851 http://togogenome.org/gene/10090:Rspo2 ^@ http://purl.uniprot.org/uniprot/Q8BFU0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Strand|||Turn ^@ Basic residues|||Disordered|||FU|||N-linked (GlcNAc...) asparagine|||R-spondin-2|||TSP type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000234440 http://togogenome.org/gene/10090:Or52p1 ^@ http://purl.uniprot.org/uniprot/Q8VGX9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp467 ^@ http://purl.uniprot.org/uniprot/B2RU53|||http://purl.uniprot.org/uniprot/G3X9X3|||http://purl.uniprot.org/uniprot/Q3USQ2|||http://purl.uniprot.org/uniprot/Q8JZL0 ^@ 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 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)|||Interaction with STAT3|||Polar residues|||Zinc finger protein 467 ^@ http://purl.uniprot.org/annotation/PRO_0000247518 http://togogenome.org/gene/10090:Defb28 ^@ http://purl.uniprot.org/uniprot/Q3V2L0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Beta-defensin ^@ http://purl.uniprot.org/annotation/PRO_5015020018 http://togogenome.org/gene/10090:Efcab5 ^@ http://purl.uniprot.org/uniprot/A0JP43 ^@ 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|||EF-hand|||EF-hand calcium-binding domain-containing protein 5|||In isoform 2.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315837|||http://purl.uniprot.org/annotation/VSP_030736|||http://purl.uniprot.org/annotation/VSP_030737|||http://purl.uniprot.org/annotation/VSP_030738 http://togogenome.org/gene/10090:Elp2 ^@ http://purl.uniprot.org/uniprot/Q91WG4 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ Elongator complex protein 2|||In isoform 2.|||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_0000051242|||http://purl.uniprot.org/annotation/VSP_016534 http://togogenome.org/gene/10090:Ldhd ^@ http://purl.uniprot.org/uniprot/Q7TNG8 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ FAD-binding PCMH-type|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Probable D-lactate dehydrogenase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000262953 http://togogenome.org/gene/10090:Lrrc7 ^@ http://purl.uniprot.org/uniprot/A0A0G2JDT9|||http://purl.uniprot.org/uniprot/A0A571BEA5|||http://purl.uniprot.org/uniprot/B9EHV0|||http://purl.uniprot.org/uniprot/E9Q6L9|||http://purl.uniprot.org/uniprot/Q80TE7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Disordered|||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 7|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000188299 http://togogenome.org/gene/10090:Brd8dc ^@ http://purl.uniprot.org/uniprot/G3X9B4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Bromo|||Disordered ^@ http://togogenome.org/gene/10090:Or4c3 ^@ http://purl.uniprot.org/uniprot/Q9R0K2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Oas2 ^@ http://purl.uniprot.org/uniprot/E9Q9A9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||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|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ 2'-5'-oligoadenylate synthase 2|||Abolished 2'-5'-oligoadenylate synthase activity.|||Disordered|||In isoform 2.|||In strain: C3H/He.|||Mice display postpartum failure of lactation and strongly reduced milk protein synthesis. Otherwise, mice develop normally and mammary glands are normal. The mutation causes an activation of the OAS2 pathway, characterized by a strong increase of Ribonuclease L (RNASEL) activity.|||N-myristoyl glycine|||N6-acetyllysine|||OAS domain 1|||OAS domain 2|||Polar residues|||Removed|||Strongly reduced 2'-5'-oligoadenylate synthase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000418628|||http://purl.uniprot.org/annotation/VSP_044068 http://togogenome.org/gene/10090:Actl6a ^@ http://purl.uniprot.org/uniprot/Q9Z2N8 ^@ Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Actin-like protein 6A|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylserine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089134 http://togogenome.org/gene/10090:Sptan1 ^@ http://purl.uniprot.org/uniprot/A3KGU5|||http://purl.uniprot.org/uniprot/A3KGU7|||http://purl.uniprot.org/uniprot/A3KGU9|||http://purl.uniprot.org/uniprot/B2RXX6|||http://purl.uniprot.org/uniprot/B7ZWK3|||http://purl.uniprot.org/uniprot/B9EKJ1|||http://purl.uniprot.org/uniprot/Q3V1V5 ^@ Coiled-Coil|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Domain Extent|||Non-terminal Residue ^@ EF-hand|||SH3 ^@ http://togogenome.org/gene/10090:Irag2 ^@ http://purl.uniprot.org/uniprot/G5E880|||http://purl.uniprot.org/uniprot/Q3TVR1|||http://purl.uniprot.org/uniprot/Q3V3H7|||http://purl.uniprot.org/uniprot/Q60664 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||Inositol 1,4,5-triphosphate receptor associated 2|||Lumenal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Processed inositol 1,4,5-triphosphate receptor associated 2|||Results in cytosolic distribution. ^@ http://purl.uniprot.org/annotation/PRO_0000084484|||http://purl.uniprot.org/annotation/PRO_0000296245 http://togogenome.org/gene/10090:Erv3 ^@ http://purl.uniprot.org/uniprot/Q9DAX3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099679 http://togogenome.org/gene/10090:B3gnt7 ^@ http://purl.uniprot.org/uniprot/Q8K0J2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7 ^@ http://purl.uniprot.org/annotation/PRO_0000264619 http://togogenome.org/gene/10090:Zfp263 ^@ http://purl.uniprot.org/uniprot/Q8CF60 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||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|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||SCAN box|||Zinc finger protein 263 ^@ http://purl.uniprot.org/annotation/PRO_0000452087 http://togogenome.org/gene/10090:Ak6 ^@ http://purl.uniprot.org/uniprot/Q8VCP8 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Region ^@ Adenylate kinase isoenzyme 6|||LID|||NMP ^@ http://purl.uniprot.org/annotation/PRO_0000153897 http://togogenome.org/gene/10090:Pheta1 ^@ http://purl.uniprot.org/uniprot/Q8BH49 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Disordered|||F&H|||PH|||Phosphoserine|||Pro residues|||Sesquipedalian-1 ^@ http://purl.uniprot.org/annotation/PRO_0000406046 http://togogenome.org/gene/10090:Mrpl40 ^@ http://purl.uniprot.org/uniprot/Q3UKS6|||http://purl.uniprot.org/uniprot/Q9Z2Q5 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transit Peptide ^@ Chain|||Coiled-Coil|||Region|||Sequence Variant|||Transit Peptide ^@ Disordered|||Large ribosomal subunit protein mL40|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000030559 http://togogenome.org/gene/10090:Tkfc ^@ http://purl.uniprot.org/uniprot/Q8VC30 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ DhaK|||DhaL|||Phosphoserine|||Tele-hemiaminal-histidine intermediate|||Triokinase/FMN cyclase ^@ http://purl.uniprot.org/annotation/PRO_0000121526 http://togogenome.org/gene/10090:Lrrn1 ^@ http://purl.uniprot.org/uniprot/Q61809 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||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 neuronal protein 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014848 http://togogenome.org/gene/10090:Cfb ^@ http://purl.uniprot.org/uniprot/B8JJM5|||http://purl.uniprot.org/uniprot/B8JJM6|||http://purl.uniprot.org/uniprot/Q3UEG8 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ C3/C5 convertase|||Charge relay system|||Peptidase S1|||Sushi|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5002875128|||http://purl.uniprot.org/annotation/PRO_5002875339|||http://purl.uniprot.org/annotation/PRO_5014309148 http://togogenome.org/gene/10090:Or2t26 ^@ http://purl.uniprot.org/uniprot/Q8VGD7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Grip1 ^@ http://purl.uniprot.org/uniprot/H7BX09|||http://purl.uniprot.org/uniprot/H7BX90|||http://purl.uniprot.org/uniprot/Q6GQT7|||http://purl.uniprot.org/uniprot/Q925T6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Disordered|||Glutamate receptor-interacting protein 1|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||PDZ 7|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000083850|||http://purl.uniprot.org/annotation/VSP_009744|||http://purl.uniprot.org/annotation/VSP_009745|||http://purl.uniprot.org/annotation/VSP_009746|||http://purl.uniprot.org/annotation/VSP_009747|||http://purl.uniprot.org/annotation/VSP_009748|||http://purl.uniprot.org/annotation/VSP_009749|||http://purl.uniprot.org/annotation/VSP_009750 http://togogenome.org/gene/10090:Stfa3 ^@ http://purl.uniprot.org/uniprot/P35173 ^@ Chain|||Molecule Processing|||Motif|||Region|||Site ^@ Chain|||Motif|||Site ^@ Reactive site|||Secondary area of contact|||Stefin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000207146 http://togogenome.org/gene/10090:Dctn5 ^@ http://purl.uniprot.org/uniprot/Q9QZB9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Dynactin subunit 5|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000079828 http://togogenome.org/gene/10090:Lrrc49 ^@ http://purl.uniprot.org/uniprot/D3YUD9|||http://purl.uniprot.org/uniprot/D3YWN5|||http://purl.uniprot.org/uniprot/E9Q8C9|||http://purl.uniprot.org/uniprot/E9QM16|||http://purl.uniprot.org/uniprot/G5E8R5|||http://purl.uniprot.org/uniprot/Q91YK0 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||Leucine-rich repeat-containing protein 49|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000233035|||http://purl.uniprot.org/annotation/VSP_018023|||http://purl.uniprot.org/annotation/VSP_020408|||http://purl.uniprot.org/annotation/VSP_020409 http://togogenome.org/gene/10090:Rhox3c ^@ http://purl.uniprot.org/uniprot/A2AWM0 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Selenos ^@ http://purl.uniprot.org/uniprot/Q9BCZ4 ^@ Chain|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane ^@ Chain|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane ^@ Disordered|||Helical|||In allele H47b.|||Selenocysteine|||Selenoprotein S|||VCP/p97-interacting motif (VIM) ^@ http://purl.uniprot.org/annotation/PRO_0000097673 http://togogenome.org/gene/10090:Tex43 ^@ http://purl.uniprot.org/uniprot/C9W8M4|||http://purl.uniprot.org/uniprot/Q9D9I1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Sperm-associated microtubule inner protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000321825 http://togogenome.org/gene/10090:H2-M10.5 ^@ http://purl.uniprot.org/uniprot/Q85ZW7|||http://purl.uniprot.org/uniprot/Q860W5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5004300506|||http://purl.uniprot.org/annotation/PRO_5015098985 http://togogenome.org/gene/10090:Irf7 ^@ http://purl.uniprot.org/uniprot/D3Z4U9|||http://purl.uniprot.org/uniprot/P70434|||http://purl.uniprot.org/uniprot/Q3TW14|||http://purl.uniprot.org/uniprot/Q542T3 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand ^@ Almost complete loss of transcriptional activation; when associated with A-437.|||Almost complete loss of transcriptional activation; when associated with A-438.|||Almost no effect on transcriptional activation in response to viral infection.|||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|||Increased transcriptional activation; when associated with D-437.|||Increased transcriptional activation; when associated with D-438.|||Interferon regulatory factor 7|||N6-acetyllysine; by KAT2A and KAT2B|||Necessary for the interaction with NMI|||No effect on transcriptional activation in response to viral infection.|||Phosphoserine|||Phosphoserine; by TBK1 and IKKE|||Strongly decreased transcriptional activation in response to viral infection.|||Strongly decreased transcriptional activation in response to viral infection; when associated with A-425.|||Strongly decreased transcriptional activation in response to viral infection; when associated with A-426.|||Strongly decreased transcriptional activation in response to viral infection; when associated with D-425.|||Strongly decreased transcriptional activation in response to viral infection; when associated with D-426.|||Strongly increased transcriptional activation in response to viral infection. ^@ http://purl.uniprot.org/annotation/PRO_0000154563 http://togogenome.org/gene/10090:Zc3hav1l ^@ http://purl.uniprot.org/uniprot/B9EHM1|||http://purl.uniprot.org/uniprot/Q8BFR1 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Splice Variant|||Zinc Finger ^@ C3H1-type|||C3H1-type 1|||C3H1-type 2|||In isoform 2.|||N-acetylalanine|||Removed|||Zinc finger CCCH-type antiviral protein 1-like ^@ http://purl.uniprot.org/annotation/PRO_0000331460|||http://purl.uniprot.org/annotation/VSP_033212 http://togogenome.org/gene/10090:Ubl5b ^@ http://purl.uniprot.org/uniprot/A0A1Y7VKT9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ubiquitin-like ^@ http://togogenome.org/gene/10090:Msh4 ^@ http://purl.uniprot.org/uniprot/A0A087WQN0|||http://purl.uniprot.org/uniprot/A6H6D5|||http://purl.uniprot.org/uniprot/Q7TNA7|||http://purl.uniprot.org/uniprot/Q99MT2 ^@ 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 ^@ DNA mismatch repair proteins mutS family|||Disordered|||MutS protein homolog 4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000115198 http://togogenome.org/gene/10090:Aqp5 ^@ http://purl.uniprot.org/uniprot/Q9WTY4 ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Motif|||Topological Domain|||Transmembrane ^@ Aquaporin-5|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000063952 http://togogenome.org/gene/10090:Sh2d1a ^@ http://purl.uniprot.org/uniprot/B2RWI0|||http://purl.uniprot.org/uniprot/O88890|||http://purl.uniprot.org/uniprot/Q544F1|||http://purl.uniprot.org/uniprot/W0BZ77 ^@ 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 ^@ Disordered|||Disrupts interaction with FYNSH3 domain.|||In isoform Short.|||Interaction with FYN SH3 domain|||N6-acetyllysine|||No effect on NK cell development, impairs promotion of NK cell cytotoxicity and IFN-gamma production in response to hematopoietic cells.|||No effect on interaction with FYNSH3 domain.|||SH2|||SH2 domain-containing protein 1A ^@ http://purl.uniprot.org/annotation/PRO_0000097723|||http://purl.uniprot.org/annotation/VSP_004391 http://togogenome.org/gene/10090:Sntb2 ^@ http://purl.uniprot.org/uniprot/Q542S9|||http://purl.uniprot.org/uniprot/Q61235 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Beta-2-syntrophin|||Calmodulin-binding|||Disordered|||PDZ|||PH|||PH 1|||PH 2|||Phosphoserine|||Polar residues|||Pro residues|||SU ^@ http://purl.uniprot.org/annotation/PRO_0000184012 http://togogenome.org/gene/10090:Fbxo27 ^@ http://purl.uniprot.org/uniprot/Q6DIA9 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ F-box|||F-box only protein 27|||FBA|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000119916|||http://purl.uniprot.org/annotation/VSP_013054 http://togogenome.org/gene/10090:Pon2 ^@ http://purl.uniprot.org/uniprot/Q62086 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Not cleaved|||Proton acceptor|||Serum paraoxonase/arylesterase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000223288 http://togogenome.org/gene/10090:Mad2l1bp ^@ http://purl.uniprot.org/uniprot/Q9DCX1 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Interaction with MAD2L1|||MAD2L1-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000096311 http://togogenome.org/gene/10090:Rasip1 ^@ http://purl.uniprot.org/uniprot/Q3U0S6|||http://purl.uniprot.org/uniprot/Q8CCF1 ^@ 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 ^@ Dilute|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Ras-associating|||Ras-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000097164 http://togogenome.org/gene/10090:Dok5 ^@ http://purl.uniprot.org/uniprot/Q91ZM9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Motif|||Sequence Conflict ^@ DKFBH motif|||Docking protein 5|||IRS-type PTB|||PH ^@ http://purl.uniprot.org/annotation/PRO_0000187278 http://togogenome.org/gene/10090:Podnl1 ^@ http://purl.uniprot.org/uniprot/Q6P3Y9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide ^@ 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|||N-linked (GlcNAc...) asparagine|||Podocan-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000311188 http://togogenome.org/gene/10090:Nlrp6 ^@ http://purl.uniprot.org/uniprot/Q91WS2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||Does not affect formation of liquid-liquid phase separation (LLPS).|||Impaired formation of liquid-liquid phase separation (LLPS), leading to reduced formation of the NLRP6 inflammasome and GSDMD-dependent release of IL18.|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||NACHT|||NACHT, LRR and PYD domains-containing protein 6|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000080893|||http://purl.uniprot.org/annotation/VSP_042301|||http://purl.uniprot.org/annotation/VSP_057971 http://togogenome.org/gene/10090:Mars1 ^@ http://purl.uniprot.org/uniprot/E9QB02|||http://purl.uniprot.org/uniprot/Q68FL6 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif ^@ 'HIGH' region|||'KMSKS' region|||GST C-terminal|||Methionine--tRNA ligase, cytoplasmic|||Phosphoserine|||Phosphothreonine|||WHEP-TRS ^@ http://purl.uniprot.org/annotation/PRO_0000139263 http://togogenome.org/gene/10090:Or5al7 ^@ http://purl.uniprot.org/uniprot/Q8VFK4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp358 ^@ http://purl.uniprot.org/uniprot/E9Q8M1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Exoc6 ^@ http://purl.uniprot.org/uniprot/A0A5F8MP92|||http://purl.uniprot.org/uniprot/Q3U9D6|||http://purl.uniprot.org/uniprot/Q8C670 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Exocyst complex subunit Sec15 C-terminal ^@ http://togogenome.org/gene/10090:Arhgap6 ^@ http://purl.uniprot.org/uniprot/O54834|||http://purl.uniprot.org/uniprot/Q8C8B2 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Rho GTPase-activating protein 6|||Rho-GAP|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000056705|||http://purl.uniprot.org/annotation/VSP_001643|||http://purl.uniprot.org/annotation/VSP_001644|||http://purl.uniprot.org/annotation/VSP_026051|||http://purl.uniprot.org/annotation/VSP_026052|||http://purl.uniprot.org/annotation/VSP_026053 http://togogenome.org/gene/10090:Ppp5c ^@ http://purl.uniprot.org/uniprot/Q60676 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Catalytic|||Disordered|||N-acetylalanine|||Proton donor/acceptor|||Removed|||Required for autoinhibition|||Serine/threonine-protein phosphatase 5|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000058895 http://togogenome.org/gene/10090:Rbm10 ^@ http://purl.uniprot.org/uniprot/Q99KG3 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||C2H2-type; atypical|||Disordered|||G-patch|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RNA-binding protein 10|||RRM 1|||RRM 2|||RanBP2-type ^@ http://purl.uniprot.org/annotation/PRO_0000345017|||http://purl.uniprot.org/annotation/VSP_034905|||http://purl.uniprot.org/annotation/VSP_034906 http://togogenome.org/gene/10090:Or6c69 ^@ http://purl.uniprot.org/uniprot/Q8VFU2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r139 ^@ http://purl.uniprot.org/uniprot/E9Q8L6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nat2 ^@ http://purl.uniprot.org/uniprot/P50295 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Variant ^@ Acyl-thioester intermediate|||Arylamine N-acetyltransferase 2|||In allele NAT2*9; slow/unstable isoform. ^@ http://purl.uniprot.org/annotation/PRO_0000107909 http://togogenome.org/gene/10090:Sumo1 ^@ http://purl.uniprot.org/uniprot/P63166 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Site ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Propeptide|||Site ^@ 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|||Interaction with PIAS2|||N-acetylserine|||Phosphoserine|||Removed|||Small ubiquitin-related modifier 1|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000035941|||http://purl.uniprot.org/annotation/PRO_0000035942 http://togogenome.org/gene/10090:Tas2r103 ^@ http://purl.uniprot.org/uniprot/Q9JKA3 ^@ 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 103 ^@ http://purl.uniprot.org/annotation/PRO_0000082243 http://togogenome.org/gene/10090:Adck2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1X6|||http://purl.uniprot.org/uniprot/Q6NSR3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ ABC1 atypical kinase-like|||Helical|||Protein kinase|||Proton acceptor|||Uncharacterized aarF domain-containing protein kinase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000271793 http://togogenome.org/gene/10090:Vmn1r205 ^@ http://purl.uniprot.org/uniprot/Q8R276 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Etl4 ^@ http://purl.uniprot.org/uniprot/A2AQ25|||http://purl.uniprot.org/uniprot/B2RY09|||http://purl.uniprot.org/uniprot/D3Z781|||http://purl.uniprot.org/uniprot/E9QAU4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Actin interacting protein 3-like C-terminal|||Basic and acidic residues|||Disordered|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 8 and isoform 9.|||In isoform 2, isoform 5, isoform 6 and isoform 9.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 4 and isoform 9.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Sickle tail protein ^@ http://purl.uniprot.org/annotation/PRO_0000287898|||http://purl.uniprot.org/annotation/VSP_052416|||http://purl.uniprot.org/annotation/VSP_052417|||http://purl.uniprot.org/annotation/VSP_052418|||http://purl.uniprot.org/annotation/VSP_052419|||http://purl.uniprot.org/annotation/VSP_052420|||http://purl.uniprot.org/annotation/VSP_052421|||http://purl.uniprot.org/annotation/VSP_052422|||http://purl.uniprot.org/annotation/VSP_052423|||http://purl.uniprot.org/annotation/VSP_052424|||http://purl.uniprot.org/annotation/VSP_052425|||http://purl.uniprot.org/annotation/VSP_052426 http://togogenome.org/gene/10090:Camkmt ^@ http://purl.uniprot.org/uniprot/B9EHP1|||http://purl.uniprot.org/uniprot/Q3U2J5 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Region|||Splice Variant ^@ Calmodulin-lysine N-methyltransferase|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000300116|||http://purl.uniprot.org/annotation/VSP_027786|||http://purl.uniprot.org/annotation/VSP_027787 http://togogenome.org/gene/10090:Tmigd1 ^@ http://purl.uniprot.org/uniprot/Q9D7L8 ^@ 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|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Transmembrane and immunoglobulin domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000045791 http://togogenome.org/gene/10090:Nlk ^@ http://purl.uniprot.org/uniprot/O54949|||http://purl.uniprot.org/uniprot/Q3TV73 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Abrogates autophosphorylation.|||Abrogates autophosphorylation. Retains ability to homodimerize. Abrogates ability to induce MYB degradation.|||Abrogates homodimerization and intermolecular autophosphorylation, with consequent loss of kinase activity. Loss of nuclear localization.|||Abrogates kinase activity and autophosphorylation. Retains ability to homodimerize. Abrogates ability to induce ubiquitination and degradation of LEF1 and repress canonical Wnt/beta-catenin signaling. Abrogates ability to induce MYB degradation, and reduces ability to repress MYBL1 and MYBL2.|||Basic residues|||Disordered|||Phosphoserine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Required for homodimerization and kinase activation and localization to the nucleus|||Required for interaction with TAB2|||Retains kinase activity.|||Serine/threonine-protein kinase NLK|||Sufficient for interaction with DAPK3|||TQE ^@ http://purl.uniprot.org/annotation/PRO_0000186337 http://togogenome.org/gene/10090:Ncoa2 ^@ http://purl.uniprot.org/uniprot/E9PV80|||http://purl.uniprot.org/uniprot/Q61026|||http://purl.uniprot.org/uniprot/Q8BN74|||http://purl.uniprot.org/uniprot/Q8C961|||http://purl.uniprot.org/uniprot/Q8CAG7|||http://purl.uniprot.org/uniprot/Q8CBM5|||http://purl.uniprot.org/uniprot/Q8CE59 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Abolishes interaction with RORC; when associated with 644-A-A-645 and 689-A--A-694.|||Abolishes interaction with RORC; when associated with 644-A-A-645 and 744-A--A-749.|||Abolishes interaction with RORC; when associated with 689-A--A-694 and 744-A--A-749.|||Asymmetric dimethylarginine|||BHLH|||Basic and acidic residues|||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|||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|||Removed|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000094403 http://togogenome.org/gene/10090:Heph ^@ http://purl.uniprot.org/uniprot/A2AI62|||http://purl.uniprot.org/uniprot/Q9Z0Z4 ^@ Binding Site|||Chain|||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 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Hephaestin|||In isoform 2.|||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_0000002916|||http://purl.uniprot.org/annotation/PRO_5002641927|||http://purl.uniprot.org/annotation/VSP_011628 http://togogenome.org/gene/10090:Vmn1r179 ^@ http://purl.uniprot.org/uniprot/Q8R2B4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:1700013H16Rik ^@ http://purl.uniprot.org/uniprot/Q9DAC5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Sipa1l2 ^@ http://purl.uniprot.org/uniprot/Q80TE4 ^@ 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.|||PDZ|||Phosphoserine|||Polar residues|||Rap-GAP|||Signal-induced proliferation-associated 1-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000056750|||http://purl.uniprot.org/annotation/VSP_016999 http://togogenome.org/gene/10090:Or5m11b ^@ http://purl.uniprot.org/uniprot/A2ATE0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lgr4 ^@ http://purl.uniprot.org/uniprot/A2ARI4|||http://purl.uniprot.org/uniprot/Q8BZR7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Confers constitutive activity.|||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.|||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_0000303240|||http://purl.uniprot.org/annotation/VSP_047137 http://togogenome.org/gene/10090:Supv3l1 ^@ http://purl.uniprot.org/uniprot/Q80YD1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ ATP-dependent RNA helicase SUPV3L1, mitochondrial|||Basic and acidic residues|||Disordered|||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_0000310546 http://togogenome.org/gene/10090:Kdm6a ^@ http://purl.uniprot.org/uniprot/O70546|||http://purl.uniprot.org/uniprot/Q3TNW2|||http://purl.uniprot.org/uniprot/Q3TPN3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||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_0000106410|||http://purl.uniprot.org/annotation/VSP_022196 http://togogenome.org/gene/10090:Sap18 ^@ http://purl.uniprot.org/uniprot/E9Q317|||http://purl.uniprot.org/uniprot/O55128|||http://purl.uniprot.org/uniprot/Q4FZH3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone deacetylase complex subunit SAP18|||Impairs interactions with RNPS1, ACIN1 and PNN; reduces ASAP and PSAP complex assemblies.|||Involved in splicing regulation activity|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000220976 http://togogenome.org/gene/10090:Vmn1r127 ^@ http://purl.uniprot.org/uniprot/K7N6J5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H3c8 ^@ http://purl.uniprot.org/uniprot/P68433 ^@ Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||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|||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; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoarginine|||Phosphoarginine; 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|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000221249 http://togogenome.org/gene/10090:Clip3 ^@ http://purl.uniprot.org/uniprot/B9EHT4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Repeat|||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|||Phosphoserine|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000415670 http://togogenome.org/gene/10090:Acod1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J027|||http://purl.uniprot.org/uniprot/P54987 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Turn ^@ Cis-aconitate decarboxylase|||MmgE/PrpD C-terminal|||MmgE/PrpD N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000084233 http://togogenome.org/gene/10090:A530064D06Rik ^@ http://purl.uniprot.org/uniprot/Q8BNV8|||http://purl.uniprot.org/uniprot/Q8C239 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015099017|||http://purl.uniprot.org/annotation/PRO_5015099065 http://togogenome.org/gene/10090:Ankrd39 ^@ http://purl.uniprot.org/uniprot/A0A0A6YWV1|||http://purl.uniprot.org/uniprot/Q14A32|||http://purl.uniprot.org/uniprot/Q9D2X0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 39|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000244367 http://togogenome.org/gene/10090:Zfy2 ^@ http://purl.uniprot.org/uniprot/P20662 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Motif|||Region|||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|||Disordered|||Nuclear localization signal|||Zinc finger Y-chromosomal protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000047264 http://togogenome.org/gene/10090:Frrs1 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFP4|||http://purl.uniprot.org/uniprot/Q8K385 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Cytochrome b561|||DOMON|||Ferric-chelate reductase 1|||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|||Reelin|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000314844|||http://purl.uniprot.org/annotation/PRO_5015039205 http://togogenome.org/gene/10090:Grid2 ^@ http://purl.uniprot.org/uniprot/Q61625 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Abolishes interaction with SHANK1 and SHANK2.|||Cytoplasmic|||Essential for dimerization|||Extracellular|||Glutamate receptor ionotropic, delta-2|||Helical|||In Lurcher.|||Interaction with AP4M1|||Interaction with CBLN1 homotrimer|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000011565 http://togogenome.org/gene/10090:Sdhaf2 ^@ http://purl.uniprot.org/uniprot/Q8C6I2 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||In isoform 3.|||Mitochondrion|||Succinate dehydrogenase assembly factor 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000294358|||http://purl.uniprot.org/annotation/VSP_026633|||http://purl.uniprot.org/annotation/VSP_026634 http://togogenome.org/gene/10090:Prkar1b ^@ http://purl.uniprot.org/uniprot/P12849|||http://purl.uniprot.org/uniprot/Q3TY04 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Region ^@ 3'-nitrotyrosine|||Cyclic nucleotide-binding|||Dimerization and phosphorylation|||Disordered|||Interchain (with C-18)|||Interchain (with C-39)|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Pseudophosphorylation motif|||cAMP-dependent protein kinase type I-beta regulatory subunit ^@ http://purl.uniprot.org/annotation/PRO_0000205382 http://togogenome.org/gene/10090:Prr11 ^@ http://purl.uniprot.org/uniprot/Q8BHE0 ^@ 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 residues|||D-box|||Disordered|||KEN box|||Phosphodegron|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proline-rich protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000243944 http://togogenome.org/gene/10090:Gm3402 ^@ http://purl.uniprot.org/uniprot/A0A0G2JG26 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Rrp36 ^@ http://purl.uniprot.org/uniprot/A0A0R4J045|||http://purl.uniprot.org/uniprot/Q3UFY0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||Nuclear localization signal|||Phosphoserine|||Ribosomal RNA processing protein 36 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000252158 http://togogenome.org/gene/10090:Or8b43 ^@ http://purl.uniprot.org/uniprot/E9Q6Z7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:F2 ^@ http://purl.uniprot.org/uniprot/P19221|||http://purl.uniprot.org/uniprot/Q3TJ94 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||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|||Gla|||High affinity receptor-binding region which is also known as the TP508 peptide|||Interchain (between light and heavy chains)|||Kringle|||Kringle 1|||Kringle 2|||Loss of protease activity.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Prothrombin|||Thrombin heavy chain|||Thrombin light chain ^@ http://purl.uniprot.org/annotation/PRO_0000028165|||http://purl.uniprot.org/annotation/PRO_0000028166|||http://purl.uniprot.org/annotation/PRO_0000028167|||http://purl.uniprot.org/annotation/PRO_0000028168|||http://purl.uniprot.org/annotation/PRO_0000028169|||http://purl.uniprot.org/annotation/PRO_0000028170|||http://purl.uniprot.org/annotation/PRO_5014309112 http://togogenome.org/gene/10090:Vmn1r49 ^@ http://purl.uniprot.org/uniprot/Q9WUF1 ^@ 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|||Vomeronasal type-1 receptor 49 ^@ http://purl.uniprot.org/annotation/PRO_0000239974 http://togogenome.org/gene/10090:Vps11 ^@ http://purl.uniprot.org/uniprot/Q91W86 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Zinc Finger ^@ CHCR 1|||CHCR 2|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||RING-type|||Removed|||Vacuolar protein sorting-associated protein 11 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000055903 http://togogenome.org/gene/10090:Crlf1 ^@ http://purl.uniprot.org/uniprot/Q9JM58 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Signal Peptide ^@ Cytokine receptor-like factor 1|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000011040 http://togogenome.org/gene/10090:Pi4k2b ^@ http://purl.uniprot.org/uniprot/Q8CBQ5 ^@ 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 ^@ Activation loop|||Catalytic loop|||Disordered|||G-loop|||Important for interaction with membranes|||Important for substrate binding|||In isoform 2.|||PI3K/PI4K catalytic|||Phosphatidylinositol 4-kinase type 2-beta|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000285165|||http://purl.uniprot.org/annotation/VSP_024828 http://togogenome.org/gene/10090:Radil ^@ http://purl.uniprot.org/uniprot/D3YWJ9|||http://purl.uniprot.org/uniprot/Q69Z89 ^@ 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 ^@ Dilute|||Disordered|||FHA|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PDZ|||Phosphoserine|||Polar residues|||Ras-associating|||Ras-associating and dilute domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000050804|||http://purl.uniprot.org/annotation/VSP_016100|||http://purl.uniprot.org/annotation/VSP_016101|||http://purl.uniprot.org/annotation/VSP_016102|||http://purl.uniprot.org/annotation/VSP_016103 http://togogenome.org/gene/10090:Mymx ^@ http://purl.uniprot.org/uniprot/A0A223PZC0|||http://purl.uniprot.org/uniprot/Q2Q5T5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes the ability to mediate myoblast fusion; does not affect interaction with MYMK; does not affect localization to the cell membrane.|||AxLyCxL|||Basic and acidic residues|||Cytoplasmic|||Decreased interaction with MYMK without affecting localization to the cell membrane.|||Disordered|||Extracellular|||Helical|||Homozygous mice die perinatally due to muscle abnormalities.|||In isoform 2.|||Protein myomixer ^@ http://purl.uniprot.org/annotation/PRO_5010681111|||http://purl.uniprot.org/annotation/PRO_5011290048|||http://purl.uniprot.org/annotation/VSP_059105 http://togogenome.org/gene/10090:Amdhd2 ^@ http://purl.uniprot.org/uniprot/Q8JZV7 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ N-acetylglucosamine-6-phosphate deacetylase|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000315777 http://togogenome.org/gene/10090:Nsf ^@ http://purl.uniprot.org/uniprot/P46460 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ Abolishes phosphorylation by CDK16.|||Interferes with oligomerization.|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK16|||Phosphotyrosine|||Vesicle-fusing ATPase ^@ http://purl.uniprot.org/annotation/PRO_0000084564 http://togogenome.org/gene/10090:Ube2a ^@ http://purl.uniprot.org/uniprot/Q3TQ27|||http://purl.uniprot.org/uniprot/Q3UCS1|||http://purl.uniprot.org/uniprot/Q9Z255 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue ^@ Glycyl thioester intermediate|||Phosphoserine; by CDK9|||UBC core|||Ubiquitin-conjugating enzyme E2 A ^@ http://purl.uniprot.org/annotation/PRO_0000082446 http://togogenome.org/gene/10090:Zmynd11 ^@ http://purl.uniprot.org/uniprot/D3YXX1|||http://purl.uniprot.org/uniprot/Q3UKS1|||http://purl.uniprot.org/uniprot/Q6PD13|||http://purl.uniprot.org/uniprot/Q8BJZ0|||http://purl.uniprot.org/uniprot/Q8R5C8 ^@ Binding Site|||Chain|||Coiled-Coil|||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|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Abolished H3.3K36me3 binding.|||Aromatic cage required for H3.3K36me3-specific binding|||Basic and acidic residues|||Bromo|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired H3.3K36me3 binding.|||MYND-type|||No effect on protein folding and histone binding.|||Nuclear localization signal|||PHD-type|||PWWP|||Phosphoserine|||Polar residues|||SAMD1-like winged helix (WH)|||Zinc finger MYND domain-containing protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000211219 http://togogenome.org/gene/10090:Gsr ^@ http://purl.uniprot.org/uniprot/P47791 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Glutathione reductase, mitochondrial|||In isoform Cytoplasmic.|||Interchain|||Mitochondrion|||N6-acetyllysine|||Proton acceptor|||Redox-active ^@ http://purl.uniprot.org/annotation/PRO_0000030278|||http://purl.uniprot.org/annotation/VSP_018973 http://togogenome.org/gene/10090:Tcf4 ^@ http://purl.uniprot.org/uniprot/A0A0J9YTU7|||http://purl.uniprot.org/uniprot/A0A0J9YUG4|||http://purl.uniprot.org/uniprot/A0A0J9YUZ0|||http://purl.uniprot.org/uniprot/Q60722|||http://purl.uniprot.org/uniprot/Q8BPX7|||http://purl.uniprot.org/uniprot/Q91XK1|||http://purl.uniprot.org/uniprot/Q91YV0 ^@ 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 ^@ BHLH|||Basic and acidic residues|||Class A specific domain|||Disordered|||Essential for MYOD1 inhibition|||In isoform 1.|||In isoform 3.|||Leucine-zipper|||Phosphoserine|||Polar residues|||Transcription factor 4|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127257|||http://purl.uniprot.org/annotation/VSP_002113|||http://purl.uniprot.org/annotation/VSP_002114|||http://purl.uniprot.org/annotation/VSP_002115 http://togogenome.org/gene/10090:Cst11 ^@ http://purl.uniprot.org/uniprot/Q9D269 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Cystatin-11|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000006659 http://togogenome.org/gene/10090:Atpaf2 ^@ http://purl.uniprot.org/uniprot/Q91YY4 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ ATP synthase mitochondrial F1 complex assembly factor 2|||Mitochondrion|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000002419 http://togogenome.org/gene/10090:Stc1 ^@ http://purl.uniprot.org/uniprot/O55183|||http://purl.uniprot.org/uniprot/Q3UEW5|||http://purl.uniprot.org/uniprot/Q3UYZ1 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Signal Peptide ^@ Interchain|||N-linked (GlcNAc...) asparagine|||Stanniocalcin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000033299|||http://purl.uniprot.org/annotation/PRO_0000033300|||http://purl.uniprot.org/annotation/PRO_5004230105|||http://purl.uniprot.org/annotation/PRO_5014309237 http://togogenome.org/gene/10090:Or5al6 ^@ http://purl.uniprot.org/uniprot/A2ARY1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Btn1a1 ^@ http://purl.uniprot.org/uniprot/Q3UM26|||http://purl.uniprot.org/uniprot/Q3UQC0|||http://purl.uniprot.org/uniprot/Q62556 ^@ 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 ^@ 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_0000014528|||http://purl.uniprot.org/annotation/PRO_5004230038|||http://purl.uniprot.org/annotation/PRO_5014309226 http://togogenome.org/gene/10090:Rab14 ^@ http://purl.uniprot.org/uniprot/Q50HX4|||http://purl.uniprot.org/uniprot/Q91V41 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region ^@ Cysteine methyl ester|||Disordered|||Effector region|||N-acetylalanine|||Ras-related protein Rab-14|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121186 http://togogenome.org/gene/10090:Kif27 ^@ http://purl.uniprot.org/uniprot/Q7M6Z4 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF27|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000307144|||http://purl.uniprot.org/annotation/VSP_028607|||http://purl.uniprot.org/annotation/VSP_028608 http://togogenome.org/gene/10090:Kcng2 ^@ http://purl.uniprot.org/uniprot/F7A6P6 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ BTB|||Basic and acidic residues|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Alpl ^@ http://purl.uniprot.org/uniprot/P09242|||http://purl.uniprot.org/uniprot/Q3TQ02 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Alkaline phosphatase|||Alkaline phosphatase, tissue-nonspecific isozyme|||GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine intermediate|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000024025|||http://purl.uniprot.org/annotation/PRO_0000024026|||http://purl.uniprot.org/annotation/PRO_5004229673 http://togogenome.org/gene/10090:Spink5 ^@ http://purl.uniprot.org/uniprot/Q148R4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Kazal-like|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015097027 http://togogenome.org/gene/10090:Rnf26 ^@ http://purl.uniprot.org/uniprot/Q8BUH7 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Chain|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ E3 ubiquitin-protein ligase RNF26|||Helical|||In isoform 2.|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000415816|||http://purl.uniprot.org/annotation/VSP_042390|||http://purl.uniprot.org/annotation/VSP_042391 http://togogenome.org/gene/10090:Slc2a12 ^@ http://purl.uniprot.org/uniprot/B2RRB2|||http://purl.uniprot.org/uniprot/Q8BFW9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Solute carrier family 2, facilitated glucose transporter member 12 ^@ http://purl.uniprot.org/annotation/PRO_0000292016 http://togogenome.org/gene/10090:Grem1 ^@ http://purl.uniprot.org/uniprot/O70326|||http://purl.uniprot.org/uniprot/Q3TNY7 ^@ 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 ^@ CTCK|||Disordered|||Gremlin|||Gremlin-1|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000006716|||http://purl.uniprot.org/annotation/PRO_5014212501 http://togogenome.org/gene/10090:Tfip11 ^@ http://purl.uniprot.org/uniprot/Q3TTV6|||http://purl.uniprot.org/uniprot/Q9ERA6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||G-patch|||No effect on nuclear speckled pattern localization; when associated with A-166 and A-168.|||No effect on nuclear speckled pattern localization; when associated with A-166 and R-170.|||No effect on nuclear speckled pattern localization; when associated with A-168 and R-170.|||Nuclear localization signal|||Phosphoserine|||Predominant cytoplasmic localization.|||Required for interaction with DHX15|||Required for nuclear speckle localization|||Tuftelin-interacting protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000072502 http://togogenome.org/gene/10090:Gcsh ^@ http://purl.uniprot.org/uniprot/Q91WK5 ^@ 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 ^@ Glycine cleavage system H protein, mitochondrial|||Lipoyl-binding|||Mitochondrion|||N6-lipoyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000010724 http://togogenome.org/gene/10090:Ceacam3 ^@ http://purl.uniprot.org/uniprot/E9Q6J4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5006724082 http://togogenome.org/gene/10090:Rgs7 ^@ http://purl.uniprot.org/uniprot/A0A0A6YW36|||http://purl.uniprot.org/uniprot/O54829|||http://purl.uniprot.org/uniprot/Q80XD3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ DEP|||Disordered|||G protein gamma|||Phosphoserine|||Phosphothreonine|||RGS|||Regulator of G-protein signaling 7 ^@ http://purl.uniprot.org/annotation/PRO_0000204197 http://togogenome.org/gene/10090:Vmn2r43 ^@ http://purl.uniprot.org/uniprot/Q80Z08 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015098930 http://togogenome.org/gene/10090:Xpc ^@ http://purl.uniprot.org/uniprot/P51612 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||DNA repair protein complementing XP-C cells homolog|||DNA-binding; preference for heteroduplex DNA|||DNA-binding; preference for single stranded DNA; required for formation of stable nucleoprotein complex|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000218294 http://togogenome.org/gene/10090:Atp8a2 ^@ http://purl.uniprot.org/uniprot/P98200 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Abolishes phosphatidylserine translocase activity, abolishes effect on neurite outgrowth.|||Cytoplasmic|||Exoplasmic loop|||Helical|||In wl; abolishes phosphatidylserine translocase activity.|||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 IB|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000046363 http://togogenome.org/gene/10090:Cryge ^@ http://purl.uniprot.org/uniprot/A2RTH4|||http://purl.uniprot.org/uniprot/Q03740 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ 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 E ^@ http://purl.uniprot.org/annotation/PRO_0000057599 http://togogenome.org/gene/10090:4930486L24Rik ^@ http://purl.uniprot.org/uniprot/Q80UB0 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site ^@ Ancestral active site|||N-linked (GlcNAc...) asparagine|||Testin-1|||Testin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000284681|||http://purl.uniprot.org/annotation/PRO_0000284682 http://togogenome.org/gene/10090:Zfp516 ^@ http://purl.uniprot.org/uniprot/Q7TSH3 ^@ 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 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|||Zinc finger protein 516 ^@ http://purl.uniprot.org/annotation/PRO_0000047635 http://togogenome.org/gene/10090:Cldn34d ^@ http://purl.uniprot.org/uniprot/A2AGU5 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:N4bp2 ^@ http://purl.uniprot.org/uniprot/F8VQG7|||http://purl.uniprot.org/uniprot/Q69ZK1 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Smr ^@ http://togogenome.org/gene/10090:Lhpp ^@ http://purl.uniprot.org/uniprot/Q9D7I5 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Binding Site|||Chain|||Splice Variant ^@ In isoform 2.|||Phospholysine phosphohistidine inorganic pyrophosphate phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000305075|||http://purl.uniprot.org/annotation/VSP_028214|||http://purl.uniprot.org/annotation/VSP_028215 http://togogenome.org/gene/10090:Dnah2 ^@ http://purl.uniprot.org/uniprot/D3Z667 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ AAA+ ATPase|||Disordered ^@ http://togogenome.org/gene/10090:Zfp92 ^@ http://purl.uniprot.org/uniprot/Q4VAD4|||http://purl.uniprot.org/uniprot/Q62396 ^@ 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|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; degenerate|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Polar residues|||Zinc finger protein 92 ^@ http://purl.uniprot.org/annotation/PRO_0000047314 http://togogenome.org/gene/10090:Eef1g ^@ http://purl.uniprot.org/uniprot/Q4FZK2|||http://purl.uniprot.org/uniprot/Q9D8N0 ^@ 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|||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)|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000208814 http://togogenome.org/gene/10090:Il17ra ^@ http://purl.uniprot.org/uniprot/Q60943 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interleukin-17 receptor A|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||SEFIR ^@ http://purl.uniprot.org/annotation/PRO_0000011031 http://togogenome.org/gene/10090:Mettl7a3 ^@ http://purl.uniprot.org/uniprot/G3X9G9|||http://purl.uniprot.org/uniprot/Q5I0W6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Methyltransferase type 11 ^@ http://togogenome.org/gene/10090:Or2y1 ^@ http://purl.uniprot.org/uniprot/Q7TQT1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gjd4 ^@ http://purl.uniprot.org/uniprot/A0A654ICD8|||http://purl.uniprot.org/uniprot/Q8BSD4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction delta-4 protein|||Gap junction protein|||Gap junction protein cysteine-rich|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000313011|||http://purl.uniprot.org/annotation/PRO_5025030019 http://togogenome.org/gene/10090:Tas2r122 ^@ http://purl.uniprot.org/uniprot/D3YU55 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Cap1 ^@ http://purl.uniprot.org/uniprot/P40124 ^@ 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 ^@ Adenylyl cyclase-associated protein 1|||C-CAP/cofactor C-like|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||N-acetylalanine|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000205697 http://togogenome.org/gene/10090:Tmprss13 ^@ http://purl.uniprot.org/uniprot/E9QPR6 ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Peptidase S1|||Polar residues|||Pro residues|||SRCR ^@ http://togogenome.org/gene/10090:Efemp1 ^@ http://purl.uniprot.org/uniprot/Q8BPB5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ EGF-containing fibulin-like extracellular matrix protein 1|||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|||Mediates interaction with TIMP3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000007572 http://togogenome.org/gene/10090:Rprml ^@ http://purl.uniprot.org/uniprot/B2RV63|||http://purl.uniprot.org/uniprot/Q3URD2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Transmembrane ^@ Helical|||Phosphoserine|||Reprimo-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000312757 http://togogenome.org/gene/10090:Avpi1 ^@ http://purl.uniprot.org/uniprot/Q9D7H4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Arginine vasopressin-induced protein 1|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000282403 http://togogenome.org/gene/10090:Kcnmb3 ^@ http://purl.uniprot.org/uniprot/E9Q7U0 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Arfgap2 ^@ http://purl.uniprot.org/uniprot/Q3UR67|||http://purl.uniprot.org/uniprot/Q99K28 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ADP-ribosylation factor GTPase-activating protein 2|||Arf-GAP|||C4-type|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||Required for interaction with coatomer ^@ http://purl.uniprot.org/annotation/PRO_0000278469|||http://purl.uniprot.org/annotation/VSP_023305 http://togogenome.org/gene/10090:Flna ^@ http://purl.uniprot.org/uniprot/B7FAU9 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Calponin-homology (CH)|||Disordered|||Filamin|||Polar residues ^@ http://togogenome.org/gene/10090:Prol1 ^@ http://purl.uniprot.org/uniprot/E9PYQ4 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Region|||Signal Peptide ^@ Disordered ^@ http://purl.uniprot.org/annotation/PRO_5003245525 http://togogenome.org/gene/10090:Trem1 ^@ http://purl.uniprot.org/uniprot/Q14DT9|||http://purl.uniprot.org/uniprot/Q9JKE2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Triggering receptor expressed on myeloid cells 1 ^@ http://purl.uniprot.org/annotation/PRO_0000042797|||http://purl.uniprot.org/annotation/PRO_5015097035 http://togogenome.org/gene/10090:Rps20 ^@ http://purl.uniprot.org/uniprot/P60867|||http://purl.uniprot.org/uniprot/Q5BLK2 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ 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-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||Small ribosomal subunit protein uS10 ^@ http://purl.uniprot.org/annotation/PRO_0000146684 http://togogenome.org/gene/10090:Sash1 ^@ http://purl.uniprot.org/uniprot/F8VQK5|||http://purl.uniprot.org/uniprot/P59808 ^@ 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|||Pro residues|||Required for interaction with TRAF6|||SAM|||SAM 1|||SAM 2|||SAM and SH3 domain-containing protein 1|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000097598 http://togogenome.org/gene/10090:Mamdc4 ^@ http://purl.uniprot.org/uniprot/D3YY20 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||MAM ^@ http://purl.uniprot.org/annotation/PRO_5003052357 http://togogenome.org/gene/10090:Slc27a3 ^@ http://purl.uniprot.org/uniprot/G3X8Y7|||http://purl.uniprot.org/uniprot/O88561 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane ^@ AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Disordered|||Helical|||In isoform 2.|||Long-chain fatty acid transport protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000193208|||http://purl.uniprot.org/annotation/PRO_5015091826|||http://purl.uniprot.org/annotation/VSP_016219|||http://purl.uniprot.org/annotation/VSP_016220 http://togogenome.org/gene/10090:Pex11b ^@ http://purl.uniprot.org/uniprot/E9PXK7|||http://purl.uniprot.org/uniprot/Q9Z210 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Helical|||Interaction with PEX19, PEX11G and FIS1 and peroxisome targeting|||N6-acetyllysine|||Peroxisomal membrane protein 11B ^@ http://purl.uniprot.org/annotation/PRO_0000105968 http://togogenome.org/gene/10090:Itgb8 ^@ http://purl.uniprot.org/uniprot/Q0VBD0 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||Integrin beta-8|||N-linked (GlcNAc...) asparagine|||PSI|||VWFA|||in LIMBS binding site|||in MIDAS binding site ^@ http://purl.uniprot.org/annotation/PRO_5015296953 http://togogenome.org/gene/10090:Glra4 ^@ http://purl.uniprot.org/uniprot/Q2TB05|||http://purl.uniprot.org/uniprot/Q61603 ^@ 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|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Glycine receptor subunit alpha-4|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Important for obstruction of the ion pore in the closed conformation|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000422 http://togogenome.org/gene/10090:Or2a51 ^@ http://purl.uniprot.org/uniprot/Q8VFS3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cux1 ^@ http://purl.uniprot.org/uniprot/E9QKE9|||http://purl.uniprot.org/uniprot/H3BJN3|||http://purl.uniprot.org/uniprot/H3BK24|||http://purl.uniprot.org/uniprot/H3BKT0|||http://purl.uniprot.org/uniprot/H3BLS0|||http://purl.uniprot.org/uniprot/P53564|||http://purl.uniprot.org/uniprot/Q5BL05|||http://purl.uniprot.org/uniprot/Q6AXG1|||http://purl.uniprot.org/uniprot/Q9JJB6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||CASP C-terminal|||CDP/Cux p110|||CUT|||CUT 1|||CUT 2|||CUT 3|||Cleavage; by CTSL|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||Homeobox|||Homeobox protein cut-like 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000202394|||http://purl.uniprot.org/annotation/PRO_0000450798|||http://purl.uniprot.org/annotation/VSP_002311|||http://purl.uniprot.org/annotation/VSP_015748|||http://purl.uniprot.org/annotation/VSP_015749|||http://purl.uniprot.org/annotation/VSP_015750|||http://purl.uniprot.org/annotation/VSP_017360 http://togogenome.org/gene/10090:Trim27 ^@ http://purl.uniprot.org/uniprot/Q62158 ^@ 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|||Zinc finger protein RFP ^@ http://purl.uniprot.org/annotation/PRO_0000056241 http://togogenome.org/gene/10090:Bpnt2 ^@ http://purl.uniprot.org/uniprot/Q80V26 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase|||Helical|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000289042 http://togogenome.org/gene/10090:Trpv6 ^@ http://purl.uniprot.org/uniprot/Q91WD2 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane|||Turn ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Abolishes binding of Mg(2+) and increases pore diameter. Impairs intestinal Ca(2+) uptake.|||Abolishes channel activity.|||Abolishes plasma membrane localization and channel activity.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Increases pore diameter.|||Interaction with S100A10|||Interaction with calmodulin|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC|||Pore-forming|||Selectivity filter|||Transient receptor potential cation channel subfamily V member 6 ^@ http://purl.uniprot.org/annotation/PRO_0000215355 http://togogenome.org/gene/10090:Dpep2 ^@ http://purl.uniprot.org/uniprot/Q8C255 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Dipeptidase 2|||Disordered|||GPI-anchor amidated serine|||In isoform 2.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000231605|||http://purl.uniprot.org/annotation/PRO_0000231606|||http://purl.uniprot.org/annotation/VSP_017852|||http://purl.uniprot.org/annotation/VSP_017853|||http://purl.uniprot.org/annotation/VSP_017854|||http://purl.uniprot.org/annotation/VSP_017855 http://togogenome.org/gene/10090:Atp2b4 ^@ http://purl.uniprot.org/uniprot/D1FNM8|||http://purl.uniprot.org/uniprot/D1FNM9|||http://purl.uniprot.org/uniprot/E9Q828|||http://purl.uniprot.org/uniprot/F7AAP4|||http://purl.uniprot.org/uniprot/Q3UPA8|||http://purl.uniprot.org/uniprot/Q6Q477 ^@ 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|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||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 isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine; by PKC|||Plasma membrane calcium-transporting ATPase 4 ^@ http://purl.uniprot.org/annotation/PRO_0000435124|||http://purl.uniprot.org/annotation/VSP_058018|||http://purl.uniprot.org/annotation/VSP_058019 http://togogenome.org/gene/10090:Suco ^@ http://purl.uniprot.org/uniprot/B2RRF3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Polar residues|||SUN ^@ http://purl.uniprot.org/annotation/PRO_5015087150 http://togogenome.org/gene/10090:Hrct1 ^@ http://purl.uniprot.org/uniprot/Q9D6B9 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Histidine-rich carboxyl terminus protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000317639 http://togogenome.org/gene/10090:Mrpl28 ^@ http://purl.uniprot.org/uniprot/Q9D1B9 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Large ribosomal subunit protein bL28m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000030507 http://togogenome.org/gene/10090:Nip7 ^@ http://purl.uniprot.org/uniprot/E9Q109|||http://purl.uniprot.org/uniprot/Q9CXK8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ 60S ribosome subunit biogenesis protein NIP7 homolog|||60S ribosome subunit biogenesis protein NIP7 pre-PUA|||C-terminal domain|||N-terminal domain|||PUA ^@ http://purl.uniprot.org/annotation/PRO_0000218774 http://togogenome.org/gene/10090:Ccdc137 ^@ http://purl.uniprot.org/uniprot/Q8R0K4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 137|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288453 http://togogenome.org/gene/10090:H2al2c ^@ http://purl.uniprot.org/uniprot/A9Z055 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Transcription factor CBF/NF-Y/archaeal histone ^@ http://togogenome.org/gene/10090:Ebag9 ^@ http://purl.uniprot.org/uniprot/Q9D0V7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Receptor-binding cancer antigen expressed on SiSo cells ^@ http://purl.uniprot.org/annotation/PRO_0000097196 http://togogenome.org/gene/10090:Fat2 ^@ http://purl.uniprot.org/uniprot/Q5F226 ^@ 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 ^@ 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|||Extracellular|||Helical|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Protocadherin Fat 2 ^@ http://purl.uniprot.org/annotation/PRO_0000406601 http://togogenome.org/gene/10090:Mrpl3 ^@ http://purl.uniprot.org/uniprot/Q99N95 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Large ribosomal subunit protein uL3m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000077254 http://togogenome.org/gene/10090:Uap1 ^@ http://purl.uniprot.org/uniprot/Q91YN5 ^@ Binding Site|||Chain|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Motif|||Sequence Variant|||Splice Variant|||Strand|||Turn ^@ In isoform 3.|||In isoform AGX1.|||In strain: C57BL/6J.|||Substrate binding|||UDP-N-acetylhexosamine pyrophosphorylase ^@ http://purl.uniprot.org/annotation/PRO_0000185768|||http://purl.uniprot.org/annotation/VSP_014524|||http://purl.uniprot.org/annotation/VSP_014525 http://togogenome.org/gene/10090:Or6d15 ^@ http://purl.uniprot.org/uniprot/Q8VF82 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp961 ^@ http://purl.uniprot.org/uniprot/E9Q4R5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Pabpn1l ^@ http://purl.uniprot.org/uniprot/Q5XFR0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Embryonic polyadenylate-binding protein 2|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000239462 http://togogenome.org/gene/10090:Iqcc ^@ http://purl.uniprot.org/uniprot/A2ADZ8 ^@ 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|||IQ|||IQ domain-containing protein C|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000282546 http://togogenome.org/gene/10090:Hpd ^@ http://purl.uniprot.org/uniprot/P49429 ^@ 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 ^@ 4-hydroxyphenylpyruvate dioxygenase|||In allele F1.|||N-acetylthreonine|||N6-succinyllysine|||Phosphoserine|||Removed|||VOC 1|||VOC 2 ^@ http://purl.uniprot.org/annotation/PRO_0000088389 http://togogenome.org/gene/10090:Mrm1 ^@ http://purl.uniprot.org/uniprot/Q99J25 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||rRNA methyltransferase 1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000273203 http://togogenome.org/gene/10090:Ccnl2 ^@ http://purl.uniprot.org/uniprot/Q9JJA7 ^@ 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|||Cyclin-L2|||Cyclin-like 1|||Cyclin-like 2|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||RS ^@ http://purl.uniprot.org/annotation/PRO_0000080488|||http://purl.uniprot.org/annotation/VSP_016133|||http://purl.uniprot.org/annotation/VSP_016134|||http://purl.uniprot.org/annotation/VSP_016135 http://togogenome.org/gene/10090:Gm6377 ^@ http://purl.uniprot.org/uniprot/Q8BHV4 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Wwox ^@ http://purl.uniprot.org/uniprot/Q91WL8 ^@ 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|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes the TNF-induced nuclear translocation.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with MAPT|||Mediates targeting to the mitochondria|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by TNK2|||Proton acceptor|||WW 1|||WW 2|||WW domain-containing oxidoreductase ^@ http://purl.uniprot.org/annotation/PRO_0000054816|||http://purl.uniprot.org/annotation/VSP_016370|||http://purl.uniprot.org/annotation/VSP_016371|||http://purl.uniprot.org/annotation/VSP_016372|||http://purl.uniprot.org/annotation/VSP_016373|||http://purl.uniprot.org/annotation/VSP_016374|||http://purl.uniprot.org/annotation/VSP_016375 http://togogenome.org/gene/10090:Cenpv ^@ http://purl.uniprot.org/uniprot/Q9CXS4 ^@ 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 ^@ CENP-V/GFA|||Centromere protein V|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000244360|||http://purl.uniprot.org/annotation/VSP_019551 http://togogenome.org/gene/10090:Zfp558 ^@ http://purl.uniprot.org/uniprot/E9Q1J0|||http://purl.uniprot.org/uniprot/Q9DAN2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Phb2 ^@ http://purl.uniprot.org/uniprot/O35129|||http://purl.uniprot.org/uniprot/Q3V235 ^@ 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 ^@ Band 7|||N-acetylalanine|||N6-acetyllysine|||Necessary for transcriptional repression|||Phosphoserine|||Phosphotyrosine|||Prohibitin-2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213885 http://togogenome.org/gene/10090:Cpsf7 ^@ http://purl.uniprot.org/uniprot/Q8BTV2 ^@ 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 ^@ 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|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081528|||http://purl.uniprot.org/annotation/VSP_017195|||http://purl.uniprot.org/annotation/VSP_017196 http://togogenome.org/gene/10090:Nkain4 ^@ http://purl.uniprot.org/uniprot/Q9JMG4 ^@ 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.|||Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000079438|||http://purl.uniprot.org/annotation/VSP_029301|||http://purl.uniprot.org/annotation/VSP_029302 http://togogenome.org/gene/10090:Dsg4 ^@ http://purl.uniprot.org/uniprot/Q7TMD7 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cytoplasmic|||Desmoglein repeat 1|||Desmoglein repeat 2|||Desmoglein-4|||Disordered|||Extracellular|||Helical|||In lah.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000003857|||http://purl.uniprot.org/annotation/PRO_0000003858 http://togogenome.org/gene/10090:Hsd3b2 ^@ http://purl.uniprot.org/uniprot/P26149 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2|||Helical|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000087781 http://togogenome.org/gene/10090:Mettl17 ^@ http://purl.uniprot.org/uniprot/Q3U2U7 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Transit Peptide ^@ Chain|||Mutagenesis Site|||Sequence Conflict|||Transit Peptide ^@ Abolished S-adenosyl-L-methionine-binding and ability to stabilize the small subunits of mitochondrial ribosome.|||Methyltransferase-like protein 17, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000312164 http://togogenome.org/gene/10090:Trim43b ^@ http://purl.uniprot.org/uniprot/P86448 ^@ 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 43B ^@ http://purl.uniprot.org/annotation/PRO_0000392435 http://togogenome.org/gene/10090:Sbp ^@ http://purl.uniprot.org/uniprot/P15501|||http://purl.uniprot.org/uniprot/Q544L5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Jacalin-type lectin|||Jacalin-type lectin domain-containing protein|||N-linked (GlcNAc...) asparagine|||Prostatic spermine-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000022389|||http://purl.uniprot.org/annotation/PRO_5014309556 http://togogenome.org/gene/10090:C3ar1 ^@ http://purl.uniprot.org/uniprot/O09047|||http://purl.uniprot.org/uniprot/Q5U7A4 ^@ 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 ^@ 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|||Phosphoserine|||Phosphothreonine|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000069204 http://togogenome.org/gene/10090:Pcdhga3 ^@ http://purl.uniprot.org/uniprot/Q91XY5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099499 http://togogenome.org/gene/10090:Taf15 ^@ http://purl.uniprot.org/uniprot/Q8BQ46 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||RRM|||RanBP2-type ^@ http://togogenome.org/gene/10090:Erich6 ^@ http://purl.uniprot.org/uniprot/D3Z6S9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glutamate-rich protein 6|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000395103 http://togogenome.org/gene/10090:ND1 ^@ http://purl.uniprot.org/uniprot/P03888|||http://purl.uniprot.org/uniprot/Q4JFN6 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane|||Turn ^@ Chain|||Helix|||Strand|||Transmembrane|||Turn ^@ Helical|||NADH-ubiquinone oxidoreductase chain 1 ^@ http://purl.uniprot.org/annotation/PRO_0000117431 http://togogenome.org/gene/10090:Pgk2 ^@ http://purl.uniprot.org/uniprot/P09041 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ N6-acetyllysine|||Phosphoglycerate kinase 2|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000145836 http://togogenome.org/gene/10090:Pglyrp2 ^@ http://purl.uniprot.org/uniprot/A0A494B9M1|||http://purl.uniprot.org/uniprot/A0A498WFR9|||http://purl.uniprot.org/uniprot/Q8VCS0 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Important for catalytic activity; essential for amidase activity and zinc hydrate coordination|||In isoform 2.|||In isoform 3.|||N-acetylmuramoyl-L-alanine amidase|||N-linked (GlcNAc...) asparagine|||Peptidoglycan recognition protein family|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000023921|||http://purl.uniprot.org/annotation/PRO_5019797169|||http://purl.uniprot.org/annotation/PRO_5020027685|||http://purl.uniprot.org/annotation/VSP_009079|||http://purl.uniprot.org/annotation/VSP_009080|||http://purl.uniprot.org/annotation/VSP_009081 http://togogenome.org/gene/10090:Nipal4 ^@ http://purl.uniprot.org/uniprot/Q8BZF2 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Magnesium transporter NIPA4|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000284448 http://togogenome.org/gene/10090:Gcnt4 ^@ http://purl.uniprot.org/uniprot/E9Q649 ^@ 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 4|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000415825 http://togogenome.org/gene/10090:Or2j6 ^@ http://purl.uniprot.org/uniprot/Q8VGL2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hs3st5 ^@ http://purl.uniprot.org/uniprot/B2RXW6|||http://purl.uniprot.org/uniprot/Q8BSL4 ^@ 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|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||For sulfotransferase activity|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate glucosamine 3-O-sulfotransferase 5|||Lumenal|||N-linked (GlcNAc...) asparagine|||Sulfotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000085223 http://togogenome.org/gene/10090:Psmc2 ^@ http://purl.uniprot.org/uniprot/P46471|||http://purl.uniprot.org/uniprot/Q8BVQ9 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 26S proteasome regulatory subunit 7|||AAA+ ATPase|||Basic and acidic residues|||Disordered|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000084710 http://togogenome.org/gene/10090:Tcp11l1 ^@ http://purl.uniprot.org/uniprot/Q8BTG3 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||T-complex protein 11-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000313748 http://togogenome.org/gene/10090:Meiob ^@ http://purl.uniprot.org/uniprot/Q9D513 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||DNA Binding|||Mutagenesis Site ^@ Impaired DNA-binding and exonuclease activities.|||Impaired exonuclease activity without affecting much the DNA-binding activity.|||Meiosis-specific with OB domain-containing protein|||OB ^@ http://purl.uniprot.org/annotation/PRO_0000337136 http://togogenome.org/gene/10090:Or4k44 ^@ http://purl.uniprot.org/uniprot/Q8VGE5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rpl12 ^@ http://purl.uniprot.org/uniprot/P35979|||http://purl.uniprot.org/uniprot/Q5BLK0 ^@ 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)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Large ribosomal subunit protein uL11|||Large ribosomal subunit protein uL11 C-terminal|||Large ribosomal subunit protein uL11 N-terminal|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000104457 http://togogenome.org/gene/10090:Pla2g4b ^@ http://purl.uniprot.org/uniprot/B7ZCM8|||http://purl.uniprot.org/uniprot/P0C871|||http://purl.uniprot.org/uniprot/Q06G06 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict ^@ C2|||Cytosolic phospholipase A2 beta|||Impairs calcium-dependent binding to phospholipids; when associated with N-24 and N-49.|||Impairs calcium-dependent binding to phospholipids; when associated with N-24 and N-52.|||Impairs calcium-dependent binding to phospholipids; when associated with N-49 and N-52.|||Nucleophile|||PLA2c|||Proton acceptor|||Significantly decreases calcium-dependent binding to phospholipids.|||Significantly decreases calcium-dependent binding to phospholipids; when associated with N-44.|||Significantly decreases calcium-dependent binding to phospholipids; when associated with N-82. ^@ http://purl.uniprot.org/annotation/PRO_0000247022 http://togogenome.org/gene/10090:Eef2k ^@ http://purl.uniprot.org/uniprot/O08796|||http://purl.uniprot.org/uniprot/Q7TPC7|||http://purl.uniprot.org/uniprot/Q8BNP6|||http://purl.uniprot.org/uniprot/Q8CEC8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Alpha-type protein kinase|||Basic and acidic residues|||Calmodulin-binding|||Disordered|||Eukaryotic elongation factor 2 kinase|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by MAPK13 and CDK1|||Phosphoserine; by PKA|||Phosphoserine; by autocatalysis|||Phosphoserine; by autocatalysis, RPS6KA1 and RPS6KB1|||Phosphothreonine; by autocatalysis|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000086937 http://togogenome.org/gene/10090:Bcl9l ^@ http://purl.uniprot.org/uniprot/Q67FY2 ^@ 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 ^@ Asymmetric dimethylarginine|||B-cell CLL/lymphoma 9-like protein|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Necessary for interaction with CTNNB1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000314080|||http://purl.uniprot.org/annotation/VSP_030209 http://togogenome.org/gene/10090:Krtap12-1 ^@ http://purl.uniprot.org/uniprot/Q9Z287 ^@ 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_0000355591 http://togogenome.org/gene/10090:Ms4a15 ^@ http://purl.uniprot.org/uniprot/Q3UPL6 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||Membrane-spanning 4-domains subfamily A member 15 ^@ http://purl.uniprot.org/annotation/PRO_0000320578 http://togogenome.org/gene/10090:Zfp300 ^@ http://purl.uniprot.org/uniprot/A2AE21|||http://purl.uniprot.org/uniprot/Q8C6W5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Nudt17 ^@ http://purl.uniprot.org/uniprot/Q9CWD3 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Splice Variant ^@ In isoform 2.|||Nucleoside diphosphate-linked moiety X motif 17|||Nudix box|||Nudix hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000019954|||http://purl.uniprot.org/annotation/VSP_037799 http://togogenome.org/gene/10090:Ccdc181 ^@ http://purl.uniprot.org/uniprot/Q80ZU5 ^@ 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|||Coiled-coil domain-containing protein 181|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000279467 http://togogenome.org/gene/10090:Sphk1 ^@ http://purl.uniprot.org/uniprot/Q8CI15 ^@ 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|||Splice Variant ^@ DAGKc|||In isoform 2.|||In isoform 3.|||No effect on recruitment to endocytic membrane. No effect on membrane fusion produced by sphingosine.|||Nuclear export signal 1|||Nuclear export signal 2|||Phosphoserine|||Phosphothreonine|||Proton donor/acceptor|||Sphingosine kinase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000333032|||http://purl.uniprot.org/annotation/VSP_033448|||http://purl.uniprot.org/annotation/VSP_033449 http://togogenome.org/gene/10090:Ins2 ^@ http://purl.uniprot.org/uniprot/P01326|||http://purl.uniprot.org/uniprot/Q5EEX1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Propeptide|||Signal Peptide ^@ C peptide|||Insulin|||Insulin-2 A chain|||Insulin-2 B chain|||Insulin-like|||Interchain (between B and A chains) ^@ http://purl.uniprot.org/annotation/PRO_0000015845|||http://purl.uniprot.org/annotation/PRO_0000015846|||http://purl.uniprot.org/annotation/PRO_0000015847|||http://purl.uniprot.org/annotation/PRO_5014309767 http://togogenome.org/gene/10090:Adgra3 ^@ http://purl.uniprot.org/uniprot/Q7TT36 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||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|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000012901 http://togogenome.org/gene/10090:Plg ^@ http://purl.uniprot.org/uniprot/P20918|||http://purl.uniprot.org/uniprot/Q3V1T9 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Angiostatin|||Apple|||Charge relay system|||Disordered|||Interchain (between A and B chains)|||Kringle|||Kringle 1|||Kringle 2|||Kringle 3|||Kringle 4|||Kringle 5|||PAN|||Peptidase S1|||Phosphoserine|||Plasmin heavy chain A|||Plasmin heavy chain A, short form|||Plasmin light chain B|||Plasminogen ^@ http://purl.uniprot.org/annotation/PRO_0000028069|||http://purl.uniprot.org/annotation/PRO_0000028070|||http://purl.uniprot.org/annotation/PRO_0000028071|||http://purl.uniprot.org/annotation/PRO_0000028072|||http://purl.uniprot.org/annotation/PRO_0000028073|||http://purl.uniprot.org/annotation/PRO_0000028074|||http://purl.uniprot.org/annotation/PRO_5004230501 http://togogenome.org/gene/10090:Adar ^@ http://purl.uniprot.org/uniprot/Q3UH31|||http://purl.uniprot.org/uniprot/Q99MU3 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ A to I editase|||Asymmetric dimethylarginine|||Basic and acidic residues|||C-terminal extension of DRBM 3 and constituent of a bi-partite nuclear localization signal|||DRBM|||DRBM 1|||DRBM 2|||DRBM 3|||Disordered|||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 isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 5.|||In strain: Czech II.|||Interaction with Z-DNA|||N-terminal extension of DRBM 3 and constituent of a bi-partite nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton donor|||Z-binding|||Z-binding 1|||Z-binding 2 ^@ http://purl.uniprot.org/annotation/PRO_0000171775|||http://purl.uniprot.org/annotation/VSP_008875|||http://purl.uniprot.org/annotation/VSP_019236|||http://purl.uniprot.org/annotation/VSP_019237 http://togogenome.org/gene/10090:Hmgcs1 ^@ http://purl.uniprot.org/uniprot/Q8JZK9 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region ^@ Acyl-thioester intermediate|||Disordered|||Hydroxymethylglutaryl-CoA synthase, cytoplasmic|||N6-acetyllysine|||Phosphoserine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000213748 http://togogenome.org/gene/10090:Tram1 ^@ http://purl.uniprot.org/uniprot/Q4FK14|||http://purl.uniprot.org/uniprot/Q91V04 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Abolishes glycosylation.|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on glycosylation; when associated with Q-120.|||No effect on glycosylation; when associated with Q-355.|||Phosphoserine|||Polar residues|||TLC|||Translocating chain-associated membrane protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000185531 http://togogenome.org/gene/10090:Fgf16 ^@ http://purl.uniprot.org/uniprot/Q9ESL8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict ^@ Fibroblast growth factor 16|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000147614 http://togogenome.org/gene/10090:Selenom ^@ http://purl.uniprot.org/uniprot/Q8VHC3 ^@ Active Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Non standard residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Crosslink|||Helix|||Non standard residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Cysteinyl-selenocysteine (Cys-Sec)|||Disordered|||Nucleophile|||Selenocysteine|||Selenoprotein M ^@ http://purl.uniprot.org/annotation/PRO_0000022299 http://togogenome.org/gene/10090:Slc15a2 ^@ http://purl.uniprot.org/uniprot/Q80XC0|||http://purl.uniprot.org/uniprot/Q9JM03 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Mbtps2 ^@ http://purl.uniprot.org/uniprot/Q8CHX6 ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Membrane-bound transcription factor site-2 protease|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000261592 http://togogenome.org/gene/10090:Lpgat1 ^@ http://purl.uniprot.org/uniprot/E9QL80|||http://purl.uniprot.org/uniprot/Q3UZK0|||http://purl.uniprot.org/uniprot/Q6A0A4|||http://purl.uniprot.org/uniprot/Q91YX5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Non-terminal Residue|||Region|||Transmembrane ^@ Acyl-CoA:lysophosphatidylglycerol acyltransferase 1|||Disordered|||HXXXXD motif|||Helical|||Phospholipid/glycerol acyltransferase|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000208205 http://togogenome.org/gene/10090:Rgr ^@ http://purl.uniprot.org/uniprot/Q543X1|||http://purl.uniprot.org/uniprot/Q9Z2B3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||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|||N6-(retinylidene)lysine|||RPE-retinal G protein-coupled receptor ^@ http://purl.uniprot.org/annotation/PRO_0000197823 http://togogenome.org/gene/10090:Or14j7 ^@ http://purl.uniprot.org/uniprot/Q7TRJ1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ckm ^@ http://purl.uniprot.org/uniprot/A2RTA0|||http://purl.uniprot.org/uniprot/P07310 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Creatine kinase M-type|||Phosphagen kinase C-terminal|||Phosphagen kinase N-terminal|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000211976 http://togogenome.org/gene/10090:Rrad ^@ http://purl.uniprot.org/uniprot/Q6PGA2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Comp ^@ http://purl.uniprot.org/uniprot/Q9R0G6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||COMP N-terminal|||Cartilage oligomeric matrix protein|||Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||Equivalent to human variant V66E involved in CTS2 disease. Reduces secretion in tendon cells and nhibits oligomerization. Mutant mice develop inflammation and fibrosis in Achilles tendons and carpal tunnel. They show compromised regenerative capability of tendons.|||Interchain (with C-68)|||Interchain (with C-71)|||Mediates cell survival and induction of the IAP family of survival proteins|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||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_0000035858 http://togogenome.org/gene/10090:Ndufb5 ^@ http://purl.uniprot.org/uniprot/D3Z568|||http://purl.uniprot.org/uniprot/Q9CQH3 ^@ Chain|||Coiled-Coil|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transit Peptide|||Transmembrane ^@ Chain|||Coiled-Coil|||Helix|||Strand|||Transit Peptide|||Transmembrane ^@ Helical|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000020053 http://togogenome.org/gene/10090:Cldn19 ^@ http://purl.uniprot.org/uniprot/Q3UNX6|||http://purl.uniprot.org/uniprot/Q9ET38 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes interaction with Clostridium perfringens CPE.|||Claudin-19|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||No effect on interaction with Clostridium perfringens CPE.|||Strongly inhibits interaction with Clostridium perfringens CPE.|||Strongly reduces interaction with Clostridium perfringens CPE. ^@ http://purl.uniprot.org/annotation/PRO_0000144782|||http://purl.uniprot.org/annotation/VSP_010343 http://togogenome.org/gene/10090:Sox8 ^@ http://purl.uniprot.org/uniprot/Q04886|||http://purl.uniprot.org/uniprot/Q543C3 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||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_0000048734 http://togogenome.org/gene/10090:Skic2 ^@ http://purl.uniprot.org/uniprot/Q6NZR5|||http://purl.uniprot.org/uniprot/Q8C2W7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ DEVH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Superkiller complex protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000458136 http://togogenome.org/gene/10090:Prpf40a ^@ http://purl.uniprot.org/uniprot/Q9R1C7 ^@ 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|||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.|||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_0000076086|||http://purl.uniprot.org/annotation/VSP_008049 http://togogenome.org/gene/10090:Mocs3 ^@ http://purl.uniprot.org/uniprot/A2BDX3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region ^@ Adenylyltransferase and sulfurtransferase MOCS3|||Cysteine persulfide|||Cysteine persulfide intermediate; for sulfurtransferase activity|||Glycyl thioester intermediate; for adenylyltransferase activity|||Interaction with NFS1|||Rhodanese ^@ http://purl.uniprot.org/annotation/PRO_0000281918 http://togogenome.org/gene/10090:Or8k23 ^@ http://purl.uniprot.org/uniprot/A2AVY0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hsf2bp ^@ http://purl.uniprot.org/uniprot/A0A3T0ZJB3|||http://purl.uniprot.org/uniprot/Q9D4G2 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Coiled-Coil|||Mutagenesis Site|||Region ^@ Abolishes interaction with BRCA2 and location to double-strand breaks in chromosomes.|||Disordered|||Heat shock factor 2-binding protein|||Interaction with BRCA2|||Interaction with BRME1|||Mutant females show reduced fertility with smaller litter sizes. Produces DNA repair defects during meiotic prophase I. Reduces loading of BRME1 and HSF2BP at the recombination nodules. Males show a slight non-significant reduction in fertility. No effect on interaction with BRCA2 and BRME1. No effect on subcellular location. Reduces BRME1 expression. ^@ http://purl.uniprot.org/annotation/PRO_0000437125 http://togogenome.org/gene/10090:Ccdc192 ^@ http://purl.uniprot.org/uniprot/Q9DAG0 ^@ Coiled-Coil|||Region ^@ Coiled-Coil ^@ ^@ http://togogenome.org/gene/10090:Rnf220 ^@ http://purl.uniprot.org/uniprot/Q6PDX6|||http://purl.uniprot.org/uniprot/Q9D4L6 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase Rnf220|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||RING-type|||Required for targeting to the cytoplasm ^@ http://purl.uniprot.org/annotation/PRO_0000277659|||http://purl.uniprot.org/annotation/VSP_023068|||http://purl.uniprot.org/annotation/VSP_023069|||http://purl.uniprot.org/annotation/VSP_023070|||http://purl.uniprot.org/annotation/VSP_023071|||http://purl.uniprot.org/annotation/VSP_023072|||http://purl.uniprot.org/annotation/VSP_023073 http://togogenome.org/gene/10090:Npy2r ^@ http://purl.uniprot.org/uniprot/P97295|||http://purl.uniprot.org/uniprot/Q3SWR9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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|||N-linked (GlcNAc...) asparagine|||Neuropeptide Y receptor type 2|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069930 http://togogenome.org/gene/10090:Wdhd1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1F8|||http://purl.uniprot.org/uniprot/P59328 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Repeat|||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|||HMG box|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD|||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_0000051339|||http://purl.uniprot.org/annotation/VSP_006757|||http://purl.uniprot.org/annotation/VSP_006758|||http://purl.uniprot.org/annotation/VSP_016898 http://togogenome.org/gene/10090:Cpne7 ^@ http://purl.uniprot.org/uniprot/Q0VE82 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ C2 1|||C2 2|||Copine-7|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000375983 http://togogenome.org/gene/10090:Eif2ak2 ^@ http://purl.uniprot.org/uniprot/Q03963 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ DRBM 1|||DRBM 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Interaction with TRAF5|||Interferon-induced, double-stranded RNA-activated protein kinase|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000085946 http://togogenome.org/gene/10090:Cog6 ^@ http://purl.uniprot.org/uniprot/Q8R3I3 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Conserved oligomeric Golgi complex subunit 6 ^@ http://purl.uniprot.org/annotation/PRO_0000213514 http://togogenome.org/gene/10090:Rnd2 ^@ http://purl.uniprot.org/uniprot/A2A4Q3|||http://purl.uniprot.org/uniprot/Q9QYM5 ^@ 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_0000198877|||http://purl.uniprot.org/annotation/PRO_0000281229 http://togogenome.org/gene/10090:Nelfcd ^@ http://purl.uniprot.org/uniprot/Q922L6 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Negative elongation factor D ^@ http://purl.uniprot.org/annotation/PRO_0000219132 http://togogenome.org/gene/10090:Nrg2 ^@ http://purl.uniprot.org/uniprot/D3YZR2 ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||EGF-like|||Helical|||Ig-like|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:1700018F24Rik ^@ http://purl.uniprot.org/uniprot/B2RW27 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Il11ra1 ^@ http://purl.uniprot.org/uniprot/Q3UIV4|||http://purl.uniprot.org/uniprot/Q64385 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like|||Ig-like C2-type|||Interleukin-11 receptor subunit alpha|||Interleukin-11 receptor subunit alpha-1|||N-linked (GlcNAc...) asparagine|||Soluble interleukin-11 receptor subunit alpha|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010914|||http://purl.uniprot.org/annotation/PRO_0000450689|||http://purl.uniprot.org/annotation/PRO_5004230134 http://togogenome.org/gene/10090:Krba1 ^@ http://purl.uniprot.org/uniprot/A0A0N4SVV3|||http://purl.uniprot.org/uniprot/A0A140T8R3|||http://purl.uniprot.org/uniprot/Q6NXZ1 ^@ 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.|||KRAB|||Phosphoserine|||Polar residues|||Protein KRBA1 ^@ http://purl.uniprot.org/annotation/PRO_0000300112|||http://purl.uniprot.org/annotation/VSP_027781|||http://purl.uniprot.org/annotation/VSP_027782|||http://purl.uniprot.org/annotation/VSP_027783 http://togogenome.org/gene/10090:Tatdn1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1E8|||http://purl.uniprot.org/uniprot/Q6P8M1 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Splice Variant ^@ Deoxyribonuclease TATDN1|||In isoform 2.|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000313591|||http://purl.uniprot.org/annotation/VSP_030046|||http://purl.uniprot.org/annotation/VSP_030047 http://togogenome.org/gene/10090:Uba6 ^@ http://purl.uniprot.org/uniprot/Q8C7R4 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ Glycyl thioester intermediate|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Ubiquitin-like modifier-activating enzyme 6 ^@ http://purl.uniprot.org/annotation/PRO_0000277798 http://togogenome.org/gene/10090:Acox1 ^@ http://purl.uniprot.org/uniprot/Q9R0H0 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Site|||Splice Variant ^@ Cleavage|||In isoform 2.|||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_0000204678|||http://purl.uniprot.org/annotation/PRO_0000447502|||http://purl.uniprot.org/annotation/PRO_0000447503|||http://purl.uniprot.org/annotation/VSP_042477 http://togogenome.org/gene/10090:Slc9b1 ^@ http://purl.uniprot.org/uniprot/G5E8I2 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Cation/H+ exchanger|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Echs1 ^@ http://purl.uniprot.org/uniprot/Q8BH95 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ Enoyl-CoA hydratase, mitochondrial|||Important for catalytic activity|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000007412 http://togogenome.org/gene/10090:Pdcl2 ^@ http://purl.uniprot.org/uniprot/Q78Y63 ^@ 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 ^@ In isoform 2.|||Phosducin-like protein 2|||Thioredoxin fold ^@ http://purl.uniprot.org/annotation/PRO_0000246158|||http://purl.uniprot.org/annotation/VSP_022360 http://togogenome.org/gene/10090:Or5a1 ^@ http://purl.uniprot.org/uniprot/Q8VFV2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tert ^@ http://purl.uniprot.org/uniprot/O70372 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ CP motif|||CTE|||Disordered|||GQ motif|||Linker|||Phosphoserine; by DYRK2|||Phosphotyrosine; by SRC-type Tyr-kinases|||Primer grip sequence|||QFP motif|||RNA-interacting domain 1|||RNA-interacting domain 2|||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|||TFLY; involved in RNA binding|||Telomerase reverse transcriptase ^@ http://purl.uniprot.org/annotation/PRO_0000054926 http://togogenome.org/gene/10090:Leng8 ^@ http://purl.uniprot.org/uniprot/D3YWS8|||http://purl.uniprot.org/uniprot/Q8CBY3 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 3.|||Leukocyte receptor cluster member 8 homolog|||N-acetylalanine|||PCI|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000306392|||http://purl.uniprot.org/annotation/VSP_028464|||http://purl.uniprot.org/annotation/VSP_028465 http://togogenome.org/gene/10090:Or13a27 ^@ http://purl.uniprot.org/uniprot/Q8VGL4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Smarce1 ^@ http://purl.uniprot.org/uniprot/O54941 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region ^@ 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|||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_0000048578 http://togogenome.org/gene/10090:Dppa5a ^@ http://purl.uniprot.org/uniprot/Q9CQS7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Developmental pluripotency-associated protein 5A|||KH; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000311976 http://togogenome.org/gene/10090:Ascl4 ^@ http://purl.uniprot.org/uniprot/M0QW46 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BHLH|||Disordered ^@ http://togogenome.org/gene/10090:Gabra5 ^@ http://purl.uniprot.org/uniprot/Q8BHJ7 ^@ Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Region|||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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000000445 http://togogenome.org/gene/10090:Gm5622 ^@ http://purl.uniprot.org/uniprot/Q810Q0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Scamp2 ^@ http://purl.uniprot.org/uniprot/Q3TAL2|||http://purl.uniprot.org/uniprot/Q3TU28|||http://purl.uniprot.org/uniprot/Q9ERN0 ^@ 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_0000191255 http://togogenome.org/gene/10090:Stk25 ^@ http://purl.uniprot.org/uniprot/Q3U6Y0|||http://purl.uniprot.org/uniprot/Q9Z2W1 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 25 ^@ http://purl.uniprot.org/annotation/PRO_0000086714 http://togogenome.org/gene/10090:Or12d2 ^@ http://purl.uniprot.org/uniprot/B2RT33 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Foxo6 ^@ http://purl.uniprot.org/uniprot/Q70KY4 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||Fork-head|||Forkhead box protein O6|||No IGF1-induced increase in cytoplasmic localization.|||No IGF1-induced increase in cytoplasmic localization. Increased transactivation activity.|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000317414 http://togogenome.org/gene/10090:Zbtb8os ^@ http://purl.uniprot.org/uniprot/B2KGA7|||http://purl.uniprot.org/uniprot/Q505B7 ^@ 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 ^@ Archease|||Disordered|||In isoform 2.|||N-acetylalanine|||Protein archease|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000285951|||http://purl.uniprot.org/annotation/VSP_024927|||http://purl.uniprot.org/annotation/VSP_024928 http://togogenome.org/gene/10090:Rab11fip5 ^@ http://purl.uniprot.org/uniprot/A0A0N4SW73|||http://purl.uniprot.org/uniprot/Q6ZQ33|||http://purl.uniprot.org/uniprot/Q8R361 ^@ 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 ^@ Acidic residues|||C2|||Disordered|||FIP-RBD|||Phosphoserine|||Polar residues|||Pro residues|||Rab11 family-interacting protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000097308 http://togogenome.org/gene/10090:Csdc2 ^@ http://purl.uniprot.org/uniprot/Q91YQ3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ CSD|||Cold shock domain-containing protein C2|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000100352 http://togogenome.org/gene/10090:Urah ^@ http://purl.uniprot.org/uniprot/A0A0A0MQC3|||http://purl.uniprot.org/uniprot/Q9CRB3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site ^@ 5-hydroxyisourate hydrolase|||No effect.|||Reduced enzyme activity.|||Strongly reduced enzyme activity.|||Transthyretin/hydroxyisourate hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000315282 http://togogenome.org/gene/10090:Spata18 ^@ http://purl.uniprot.org/uniprot/Q0P557 ^@ 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.|||Mitochondria-eating protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000408329|||http://purl.uniprot.org/annotation/VSP_041057|||http://purl.uniprot.org/annotation/VSP_041058 http://togogenome.org/gene/10090:Sema3f ^@ http://purl.uniprot.org/uniprot/O88632 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Ig-like C2-type|||In isoform A.|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3F ^@ http://purl.uniprot.org/annotation/PRO_0000032321|||http://purl.uniprot.org/annotation/VSP_006042 http://togogenome.org/gene/10090:Smyd5 ^@ http://purl.uniprot.org/uniprot/Q3TYX3 ^@ 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_0000227789 http://togogenome.org/gene/10090:Cxxc1 ^@ http://purl.uniprot.org/uniprot/Q541B1|||http://purl.uniprot.org/uniprot/Q9CWW7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||CXXC-type|||CXXC-type zinc finger protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079744 http://togogenome.org/gene/10090:Pir ^@ http://purl.uniprot.org/uniprot/Q9D711 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Pirin ^@ http://purl.uniprot.org/annotation/PRO_0000214052 http://togogenome.org/gene/10090:Cdk19 ^@ http://purl.uniprot.org/uniprot/B7ZMT1|||http://purl.uniprot.org/uniprot/G5E8L1|||http://purl.uniprot.org/uniprot/Q8BKC7|||http://purl.uniprot.org/uniprot/Q8BWD8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Cyclin-dependent kinase 19|||Disordered|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085714 http://togogenome.org/gene/10090:Or5b102 ^@ http://purl.uniprot.org/uniprot/Q8VFW2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dbi ^@ http://purl.uniprot.org/uniprot/P31786|||http://purl.uniprot.org/uniprot/Q4VWZ5|||http://purl.uniprot.org/uniprot/Q548W7 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ ACB|||Acyl-CoA-binding protein|||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_0000214005 http://togogenome.org/gene/10090:Zdhhc18 ^@ http://purl.uniprot.org/uniprot/Q5Y5T2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Disordered|||Helical|||Lumenal|||Palmitoyltransferase ZDHHC18|||Phosphoserine|||Pro residues|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212903 http://togogenome.org/gene/10090:Gjb2 ^@ http://purl.uniprot.org/uniprot/Q00977|||http://purl.uniprot.org/uniprot/Q3UJE9 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Topological Domain|||Transmembrane ^@ Connexin N-terminal|||Cytoplasmic|||Extracellular|||Gap junction beta-2 protein|||Gap junction protein cysteine-rich|||Helical|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000057858 http://togogenome.org/gene/10090:Pkp4 ^@ http://purl.uniprot.org/uniprot/Q3UIX3|||http://purl.uniprot.org/uniprot/Q68FH0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ARM|||ARM 1|||ARM 2|||ARM 3|||ARM 4|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Plakophilin-4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064290|||http://purl.uniprot.org/annotation/VSP_012374|||http://purl.uniprot.org/annotation/VSP_012375|||http://purl.uniprot.org/annotation/VSP_012376|||http://purl.uniprot.org/annotation/VSP_012377 http://togogenome.org/gene/10090:Lyzl1 ^@ http://purl.uniprot.org/uniprot/A0A077S9Z4|||http://purl.uniprot.org/uniprot/Q9CPX3 ^@ 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 ^@ C-type lysozyme|||Glycosyl hydrolases family 22 (GH22)|||Lysozyme-like protein 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000240636|||http://purl.uniprot.org/annotation/PRO_5014216947 http://togogenome.org/gene/10090:Or4l15 ^@ http://purl.uniprot.org/uniprot/K7N5X7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or10q3 ^@ http://purl.uniprot.org/uniprot/Q7TQS2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pdha1 ^@ http://purl.uniprot.org/uniprot/P35486|||http://purl.uniprot.org/uniprot/Q3UFJ3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Transit Peptide ^@ Decreases phosphorylation at S-232 and S-300 but does not affect activity or substrate metabolism.|||Dehydrogenase E1 component|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by PDK1|||Phosphoserine; by PDK1, PDK2, PDK3 and PDK4|||Phosphotyrosine|||Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000020442 http://togogenome.org/gene/10090:D630045J12Rik ^@ http://purl.uniprot.org/uniprot/Q68FD9 ^@ 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|||Polar residues|||UPF0606 protein KIAA1549 ^@ http://purl.uniprot.org/annotation/PRO_0000342406 http://togogenome.org/gene/10090:Cops8 ^@ http://purl.uniprot.org/uniprot/Q8VBV7 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ COP9 signalosome complex subunit 8|||PCI|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000121008 http://togogenome.org/gene/10090:Thoc1 ^@ http://purl.uniprot.org/uniprot/Q8R3N6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region ^@ 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|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||THO complex subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072521 http://togogenome.org/gene/10090:Bdh2 ^@ http://purl.uniprot.org/uniprot/Q8JZV9 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Site ^@ Active Site|||Binding Site|||Chain|||Mutagenesis Site ^@ Dehydrogenase/reductase SDR family member 6|||Loss of function.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000042581 http://togogenome.org/gene/10090:Rab2a ^@ http://purl.uniprot.org/uniprot/P53994|||http://purl.uniprot.org/uniprot/Q0PD65 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Constitutively active. Interacts with GARIN1B.|||Constitutively inactive. Loss of interaction with GARIN1B.|||Disordered|||Effector region|||N-acetylalanine|||Polar residues|||Ras-related protein Rab-2A|||Removed|||Required for interaction with PRKCI|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121067 http://togogenome.org/gene/10090:Mup22 ^@ http://purl.uniprot.org/uniprot/Q4FZE8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5015097606 http://togogenome.org/gene/10090:Cela2a ^@ http://purl.uniprot.org/uniprot/P05208 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Chymotrypsin-like elastase family member 2A|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027687|||http://purl.uniprot.org/annotation/PRO_0000027688 http://togogenome.org/gene/10090:Il4i1b ^@ http://purl.uniprot.org/uniprot/D3Z4E0|||http://purl.uniprot.org/uniprot/O09046 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Amine oxidase|||Disordered|||In isoform 2.|||L-amino-acid oxidase|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000001711|||http://purl.uniprot.org/annotation/PRO_5003053046|||http://purl.uniprot.org/annotation/VSP_017174 http://togogenome.org/gene/10090:2310057J18Rik ^@ http://purl.uniprot.org/uniprot/Q8C6C9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Protein LEG1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000252386 http://togogenome.org/gene/10090:Spata4 ^@ http://purl.uniprot.org/uniprot/Q8K3V1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Spermatogenesis-associated protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000072102 http://togogenome.org/gene/10090:Fam135a ^@ http://purl.uniprot.org/uniprot/Q6NS59 ^@ 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 FAM135A ^@ http://purl.uniprot.org/annotation/PRO_0000314169|||http://purl.uniprot.org/annotation/VSP_030231 http://togogenome.org/gene/10090:Btbd35f2 ^@ http://purl.uniprot.org/uniprot/J3QMS5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Tmem151a ^@ http://purl.uniprot.org/uniprot/Q6GQT5 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 151A ^@ http://purl.uniprot.org/annotation/PRO_0000282987 http://togogenome.org/gene/10090:Cdkl5 ^@ http://purl.uniprot.org/uniprot/Q3UTQ8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Cyclin-dependent kinase-like 5|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000275897|||http://purl.uniprot.org/annotation/VSP_022968|||http://purl.uniprot.org/annotation/VSP_022969 http://togogenome.org/gene/10090:Tut7 ^@ http://purl.uniprot.org/uniprot/E9PUA2|||http://purl.uniprot.org/uniprot/Q5BLK4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||CCHC-type|||CCHC-type 1|||CCHC-type 2|||CCHC-type 3|||Disordered|||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_0000150958 http://togogenome.org/gene/10090:Lilrb4a ^@ http://purl.uniprot.org/uniprot/Q64281 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||Leukocyte immunoglobulin-like receptor subfamily B member 4A|||N-linked (GlcNAc...) asparagine|||Partially suppresses inhibition of mast cell activation. Abolishes inhibition of mast cell activation; when associated with F-300.|||Partially suppresses inhibition of mast cell activation. Abolishes inhibition of mast cell activation; when associated with F-322. ^@ http://purl.uniprot.org/annotation/PRO_0000014824|||http://purl.uniprot.org/annotation/VSP_002510|||http://purl.uniprot.org/annotation/VSP_002511 http://togogenome.org/gene/10090:Gm10377 ^@ http://purl.uniprot.org/uniprot/D3YXI8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or10ag56 ^@ http://purl.uniprot.org/uniprot/A0A0J9YUE7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sertad4 ^@ http://purl.uniprot.org/uniprot/A7DTG3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||SERTA|||SERTA domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000314140 http://togogenome.org/gene/10090:Otogl ^@ http://purl.uniprot.org/uniprot/F7A4A7 ^@ 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 ^@ CTCK|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Otogelin-like protein|||TIL 1|||TIL 2|||VWFD 1|||VWFD 2|||VWFD 3|||VWFD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000421106|||http://purl.uniprot.org/annotation/VSP_045177 http://togogenome.org/gene/10090:Zfp839 ^@ http://purl.uniprot.org/uniprot/B2RWW3|||http://purl.uniprot.org/uniprot/E9PUU5|||http://purl.uniprot.org/uniprot/Q9CSB3 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue|||Region ^@ C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Hrh4 ^@ http://purl.uniprot.org/uniprot/B2ZGH2|||http://purl.uniprot.org/uniprot/Q2M2N7|||http://purl.uniprot.org/uniprot/Q91ZY2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||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|||Histamine H4 receptor|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000303238 http://togogenome.org/gene/10090:Ttc29 ^@ http://purl.uniprot.org/uniprot/E9QLU4 ^@ Region|||Repeat ^@ Region|||Repeat ^@ Disordered|||TPR ^@ http://togogenome.org/gene/10090:Lin28a ^@ http://purl.uniprot.org/uniprot/Q8K3Y3 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ CCHC-type 1|||CCHC-type 2|||CSD|||Disordered|||Disrupts 5'-GGAG-3' motif interaction. Binds miRNA but not TUT4.|||Disrupts 5'-GGAG-3' motif interaction. Disrupts oligoU-addition to pre-miRNA pre-let-7 by TUT4.|||Erroneous subcellular location. No positive effect on terminal myogenic differentiation.|||Erroneous subcellular location; when associated with I-81. No positive effect on terminal myogenic differentiation; when associated with I-81.|||Erroneous subcellular location; when associated with Q-85. No positive effect on terminal myogenic differentiation; when associated with Q-85.|||Erroneous subcellular location; when associated with R-119. No positive effect on terminal myogenic differentiation; when associated with R-119.|||Erroneous subcellular location; when associated with S-124. No positive effect on terminal myogenic differentiation; when associated with S-124.|||Flexible linker|||N-acetylglycine|||No effect on subcellular location; when associated with 44-C--F-47. Normal terminal myogenic differentiation; when associated with 44-C--F-47.|||No effect on subcellular location; when associated with S-142. Normal terminal myogenic differentiation; when associated with S-142.|||Phosphoserine|||Protein lin-28 homolog A|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000253788 http://togogenome.org/gene/10090:Skp1 ^@ http://purl.uniprot.org/uniprot/Q5SUR3|||http://purl.uniprot.org/uniprot/Q9WTX5 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Interaction with the F-box domain of F-box proteins|||Phosphothreonine|||S-phase kinase-associated protein 1|||SKP1 component POZ|||SKP1 component dimerisation ^@ http://purl.uniprot.org/annotation/PRO_0000187252 http://togogenome.org/gene/10090:Sirpb1c ^@ http://purl.uniprot.org/uniprot/Q1AN90 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097051 http://togogenome.org/gene/10090:Ddx24 ^@ http://purl.uniprot.org/uniprot/F8WJA0|||http://purl.uniprot.org/uniprot/Q9ESV0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ ATP-dependent RNA helicase DDX24|||Basic and acidic 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|||Phosphoserine|||Polar residues|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000055030 http://togogenome.org/gene/10090:Akr1c18 ^@ http://purl.uniprot.org/uniprot/Q3U538|||http://purl.uniprot.org/uniprot/Q8K023 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Site|||Splice Variant ^@ Aldo-keto reductase family 1 member C18|||Important for substrate specificity|||In isoform 2.|||Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000124649|||http://purl.uniprot.org/annotation/VSP_014039 http://togogenome.org/gene/10090:Spata5 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ80|||http://purl.uniprot.org/uniprot/A0A0G2JFY0|||http://purl.uniprot.org/uniprot/Q3UMC0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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)|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000330584 http://togogenome.org/gene/10090:Vamp8 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0R1|||http://purl.uniprot.org/uniprot/O70404 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Blocks internalization from cell surface; when associated with A-24.|||Blocks internalization from cell surface; when associated with A-27.|||Cytoplasmic|||Helical|||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_0000206737 http://togogenome.org/gene/10090:Rassf10 ^@ http://purl.uniprot.org/uniprot/Q8BL43 ^@ 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 ^@ Disordered|||Polar residues|||Ras association domain-containing protein 10|||Ras-associating ^@ http://purl.uniprot.org/annotation/PRO_0000332285 http://togogenome.org/gene/10090:Irx5 ^@ http://purl.uniprot.org/uniprot/Q9JKQ4 ^@ 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-5|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000049161 http://togogenome.org/gene/10090:Gnmt ^@ http://purl.uniprot.org/uniprot/Q9QXF8 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ Glycine N-methyltransferase|||N-acetylvaline|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087525 http://togogenome.org/gene/10090:Dip2b ^@ http://purl.uniprot.org/uniprot/B2RQC7|||http://purl.uniprot.org/uniprot/Q3UH60 ^@ 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 ^@ AMP-dependent synthetase/ligase|||Basic and acidic residues|||DMAP1-binding|||Disco-interacting protein 2 homolog B|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000318737|||http://purl.uniprot.org/annotation/VSP_031278|||http://purl.uniprot.org/annotation/VSP_031279 http://togogenome.org/gene/10090:Epn1 ^@ http://purl.uniprot.org/uniprot/Q80VP1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||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 D-P-W|||Disordered|||ENTH|||Epsin-1|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Pro residues|||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_0000074514|||http://purl.uniprot.org/annotation/VSP_009153 http://togogenome.org/gene/10090:Ppip5k1 ^@ http://purl.uniprot.org/uniprot/A2ARP1 ^@ 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 ^@ Acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1|||Phosphoserine|||Polar residues|||Polyphosphoinositide-binding domain ^@ http://purl.uniprot.org/annotation/PRO_0000315689|||http://purl.uniprot.org/annotation/VSP_030625|||http://purl.uniprot.org/annotation/VSP_030626|||http://purl.uniprot.org/annotation/VSP_030627|||http://purl.uniprot.org/annotation/VSP_030628|||http://purl.uniprot.org/annotation/VSP_030629|||http://purl.uniprot.org/annotation/VSP_030630|||http://purl.uniprot.org/annotation/VSP_030631|||http://purl.uniprot.org/annotation/VSP_030634 http://togogenome.org/gene/10090:Med1 ^@ http://purl.uniprot.org/uniprot/Q925J9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In strain: ISS and 129/Ola.|||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|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK1 or MAPK3|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000058553|||http://purl.uniprot.org/annotation/VSP_051892|||http://purl.uniprot.org/annotation/VSP_051893|||http://purl.uniprot.org/annotation/VSP_051894|||http://purl.uniprot.org/annotation/VSP_051895|||http://purl.uniprot.org/annotation/VSP_051896 http://togogenome.org/gene/10090:Trappc10 ^@ http://purl.uniprot.org/uniprot/Q3TLI0 ^@ 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|||Trafficking protein particle complex subunit 10 ^@ http://purl.uniprot.org/annotation/PRO_0000331480 http://togogenome.org/gene/10090:Or5t9 ^@ http://purl.uniprot.org/uniprot/Q0VAY0|||http://purl.uniprot.org/uniprot/Q8VF13 ^@ 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 5T9 ^@ http://purl.uniprot.org/annotation/PRO_0000150867 http://togogenome.org/gene/10090:Fn3krp ^@ http://purl.uniprot.org/uniprot/Q8K274 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Ketosamine-3-kinase|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000216340 http://togogenome.org/gene/10090:Fpgs ^@ http://purl.uniprot.org/uniprot/P48760 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Folylpolyglutamate synthase, mitochondrial|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mitochondrion|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000010099|||http://purl.uniprot.org/annotation/VSP_018734|||http://purl.uniprot.org/annotation/VSP_041961|||http://purl.uniprot.org/annotation/VSP_041962|||http://purl.uniprot.org/annotation/VSP_041967 http://togogenome.org/gene/10090:Lag3 ^@ http://purl.uniprot.org/uniprot/Q61790 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 13 X 2 AA tandem repeats of E-X|||Abolished ability to inhibit T-cell activation.|||Connecting peptide|||Cytoplasmic|||Decreased binding to MHC class II.|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||Interaction with FGL1|||KIEELE motif|||Lymphocyte activation gene 3 protein|||N-linked (GlcNAc...) asparagine|||No significant effect on MHC class II-binding.|||Secreted lymphocyte activation gene 3 protein ^@ http://purl.uniprot.org/annotation/PRO_0000014632|||http://purl.uniprot.org/annotation/PRO_0000446643 http://togogenome.org/gene/10090:Cacfd1 ^@ http://purl.uniprot.org/uniprot/Q8BG21 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Calcium channel flower homolog|||Helical|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000089672|||http://purl.uniprot.org/annotation/VSP_012998|||http://purl.uniprot.org/annotation/VSP_012999|||http://purl.uniprot.org/annotation/VSP_013000 http://togogenome.org/gene/10090:Vmn2r101 ^@ http://purl.uniprot.org/uniprot/E9PZS9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003244340 http://togogenome.org/gene/10090:Arpc1b ^@ http://purl.uniprot.org/uniprot/Q9WV32 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ Actin-related protein 2/3 complex subunit 1B|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000050856 http://togogenome.org/gene/10090:Ythdf2 ^@ http://purl.uniprot.org/uniprot/Q91YT7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Interaction with m6A-containing mRNAs|||Localization to mRNA processing bodies (P-bodies)|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||YTH|||YTH domain-containing family protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000425544 http://togogenome.org/gene/10090:Mif ^@ http://purl.uniprot.org/uniprot/P34884 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Strand ^@ Loss of tautomerase activity, reduced activation of intracellular signaling pathways, and reduced interaction with CXCR2 and COPS5.|||Macrophage migration inhibitory factor|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Proton acceptor; via imino nitrogen|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000158066 http://togogenome.org/gene/10090:Cbll1 ^@ http://purl.uniprot.org/uniprot/A0A1X7SB71|||http://purl.uniprot.org/uniprot/Q9JIY2 ^@ 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 ^@ C2H2-type|||Disordered|||E3 ubiquitin-protein ligase Hakai|||HYB domain|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Pro residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000284050|||http://purl.uniprot.org/annotation/VSP_024415|||http://purl.uniprot.org/annotation/VSP_024416|||http://purl.uniprot.org/annotation/VSP_024417|||http://purl.uniprot.org/annotation/VSP_024418|||http://purl.uniprot.org/annotation/VSP_024419 http://togogenome.org/gene/10090:Ciita ^@ http://purl.uniprot.org/uniprot/A0A2R8VHC7|||http://purl.uniprot.org/uniprot/P79621|||http://purl.uniprot.org/uniprot/Q3KNE0|||http://purl.uniprot.org/uniprot/Q3U5G4|||http://purl.uniprot.org/uniprot/Q3UNW8|||http://purl.uniprot.org/uniprot/Q3UU40|||http://purl.uniprot.org/uniprot/Q8HW99 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||MHC class II transactivator|||NACHT|||Polar residues|||Required for acetyltransferase activity ^@ http://purl.uniprot.org/annotation/PRO_0000089242|||http://purl.uniprot.org/annotation/VSP_007214|||http://purl.uniprot.org/annotation/VSP_007215|||http://purl.uniprot.org/annotation/VSP_007216 http://togogenome.org/gene/10090:Myl1 ^@ http://purl.uniprot.org/uniprot/E9PWG4|||http://purl.uniprot.org/uniprot/P05977|||http://purl.uniprot.org/uniprot/Q545G5|||http://purl.uniprot.org/uniprot/Q545T7 ^@ 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 ^@ Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform MLC3.|||Myosin light chain 1/3, skeletal muscle isoform|||N,N,N-trimethylalanine|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000198682|||http://purl.uniprot.org/annotation/VSP_038687 http://togogenome.org/gene/10090:Gvin1 ^@ http://purl.uniprot.org/uniprot/L7N451 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ VLIG-type G ^@ http://togogenome.org/gene/10090:Tspan2 ^@ http://purl.uniprot.org/uniprot/Q922J6|||http://purl.uniprot.org/uniprot/Q9D1X8 ^@ 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-2 ^@ http://purl.uniprot.org/annotation/PRO_0000219237 http://togogenome.org/gene/10090:4930563E22Rik ^@ http://purl.uniprot.org/uniprot/Q8BGJ3 ^@ 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|||Uncharacterized protein C17orf100 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000340709 http://togogenome.org/gene/10090:Sec14l1 ^@ http://purl.uniprot.org/uniprot/A8Y5H7 ^@ 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 ^@ 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_0000435528|||http://purl.uniprot.org/annotation/VSP_058109|||http://purl.uniprot.org/annotation/VSP_058110 http://togogenome.org/gene/10090:Taar8a ^@ http://purl.uniprot.org/uniprot/Q5QD07 ^@ 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|||Trace amine-associated receptor 8a ^@ http://purl.uniprot.org/annotation/PRO_0000070175 http://togogenome.org/gene/10090:Thy1 ^@ http://purl.uniprot.org/uniprot/P01831 ^@ 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|||Sequence Variant|||Signal Peptide ^@ Alternate|||GPI-anchor amidated cysteine; alternate|||Ig-like V-type|||In allele Thy-1.1.|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid|||Removed in mature form|||Thy-1 membrane glycoprotein ^@ http://purl.uniprot.org/annotation/PRO_0000014977|||http://purl.uniprot.org/annotation/PRO_0000014978 http://togogenome.org/gene/10090:Ank3 ^@ http://purl.uniprot.org/uniprot/G3X971|||http://purl.uniprot.org/uniprot/G5E8K2|||http://purl.uniprot.org/uniprot/G5E8K3|||http://purl.uniprot.org/uniprot/G5E8K5|||http://purl.uniprot.org/uniprot/S4R2K9 ^@ 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 ^@ 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|||Ankyrin-3|||Basic and acidic residues|||Death|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 6.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 5.|||Phosphoserine|||Polar residues|||UPA domain|||ZU5|||ZU5 1|||ZU5 2 ^@ http://purl.uniprot.org/annotation/PRO_0000419782|||http://purl.uniprot.org/annotation/VSP_044355|||http://purl.uniprot.org/annotation/VSP_044356|||http://purl.uniprot.org/annotation/VSP_044357|||http://purl.uniprot.org/annotation/VSP_044358|||http://purl.uniprot.org/annotation/VSP_044359 http://togogenome.org/gene/10090:Potegl ^@ http://purl.uniprot.org/uniprot/Q9D4J9 ^@ Region|||Repeat ^@ Region|||Repeat ^@ ANK|||Disordered ^@ http://togogenome.org/gene/10090:Drg1 ^@ http://purl.uniprot.org/uniprot/P32233|||http://purl.uniprot.org/uniprot/Q5NBZ3 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ (3S)-3-hydroxylysine|||Developmentally-regulated GTP-binding protein 1|||N-acetylserine|||OBG-type G|||Phosphothreonine; by STK16|||Removed|||Required for interaction with STK16|||TGS ^@ http://purl.uniprot.org/annotation/PRO_0000205425 http://togogenome.org/gene/10090:Kcna10 ^@ http://purl.uniprot.org/uniprot/B2RQA1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Motif|||Region|||Sequence Conflict|||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|||Polar residues|||Potassium voltage-gated channel subfamily A member 10|||S-palmitoyl cysteine|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000437460 http://togogenome.org/gene/10090:Api5 ^@ http://purl.uniprot.org/uniprot/O35841|||http://purl.uniprot.org/uniprot/Q3UYQ4 ^@ 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 ^@ ARM-like and Heat-like helical repeats|||Apoptosis inhibitor 5|||Disordered|||Leucine-zipper|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064635 http://togogenome.org/gene/10090:Fgfbp1 ^@ http://purl.uniprot.org/uniprot/O70514 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Fibroblast growth factor-binding protein 1|||O-linked (GalNAc...) serine|||Polar residues|||Sufficient for interaction with FGF2 and FGF2-induced effects ^@ http://purl.uniprot.org/annotation/PRO_0000245513 http://togogenome.org/gene/10090:Snx12 ^@ http://purl.uniprot.org/uniprot/O70493|||http://purl.uniprot.org/uniprot/Q3TGS7|||http://purl.uniprot.org/uniprot/Q3V2H3|||http://purl.uniprot.org/uniprot/Q6ZWQ5 ^@ 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|||Region|||Sequence Conflict ^@ Disordered|||N-acetylserine|||PX|||Phosphoserine|||Phosphotyrosine|||Removed|||Sorting nexin-12 ^@ http://purl.uniprot.org/annotation/PRO_0000213859 http://togogenome.org/gene/10090:Pmf1 ^@ http://purl.uniprot.org/uniprot/Q9CPV5 ^@ 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.|||Polyamine-modulated factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000248238|||http://purl.uniprot.org/annotation/VSP_052141 http://togogenome.org/gene/10090:Kbtbd13 ^@ http://purl.uniprot.org/uniprot/Q8C828 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch repeat and BTB domain-containing protein 13 ^@ http://purl.uniprot.org/annotation/PRO_0000393907 http://togogenome.org/gene/10090:Pde6b ^@ http://purl.uniprot.org/uniprot/P23440 ^@ Active Site|||Binding Site|||Chain|||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|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ GAF 1|||GAF 2|||In Rd mouse, causes retinal degeneration.|||In isoform 2.|||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_0000023350|||http://purl.uniprot.org/annotation/PRO_0000023351|||http://purl.uniprot.org/annotation/VSP_004592 http://togogenome.org/gene/10090:Rlig1 ^@ http://purl.uniprot.org/uniprot/Q8BHN7 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||RNA ligase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000305273|||http://purl.uniprot.org/annotation/VSP_028320|||http://purl.uniprot.org/annotation/VSP_028321 http://togogenome.org/gene/10090:Or52s1 ^@ http://purl.uniprot.org/uniprot/Q8VF28 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Emc10 ^@ http://purl.uniprot.org/uniprot/A0A0X1KG67|||http://purl.uniprot.org/uniprot/Q3TAS6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||ER membrane protein complex subunit 10|||Helical|||In isoform 2.|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000315049|||http://purl.uniprot.org/annotation/PRO_5015049263|||http://purl.uniprot.org/annotation/VSP_030475 http://togogenome.org/gene/10090:Brinp3 ^@ http://purl.uniprot.org/uniprot/Q499E0 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ BMP/retinoic acid-inducible neural-specific protein 3|||MACPF|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000045775 http://togogenome.org/gene/10090:Lrrc74b ^@ http://purl.uniprot.org/uniprot/Q14BP6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Splice Variant ^@ 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-containing protein 74B|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000306173|||http://purl.uniprot.org/annotation/VSP_028428|||http://purl.uniprot.org/annotation/VSP_028429|||http://purl.uniprot.org/annotation/VSP_028430 http://togogenome.org/gene/10090:Or55b4 ^@ http://purl.uniprot.org/uniprot/E9PX47 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ctc1 ^@ http://purl.uniprot.org/uniprot/Q5SUQ9 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ CST complex subunit CTC1|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000287183|||http://purl.uniprot.org/annotation/VSP_025354|||http://purl.uniprot.org/annotation/VSP_025355 http://togogenome.org/gene/10090:Tkt ^@ http://purl.uniprot.org/uniprot/P40142 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Modified Residue|||Sequence Conflict|||Site ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Important for catalytic activity|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton donor|||Transketolase ^@ http://purl.uniprot.org/annotation/PRO_0000191896 http://togogenome.org/gene/10090:Actr10 ^@ http://purl.uniprot.org/uniprot/Q9QZB7 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Actin-related protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000089132 http://togogenome.org/gene/10090:Ifna16 ^@ http://purl.uniprot.org/uniprot/Q810G1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015098938 http://togogenome.org/gene/10090:Vmn1r152 ^@ http://purl.uniprot.org/uniprot/E9Q9N3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdk2ap1 ^@ http://purl.uniprot.org/uniprot/O35207 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region ^@ Cyclin-dependent kinase 2-associated protein 1|||Disordered|||Interaction with CDK2AP2|||Interchain|||Phosphoserine; by IKKE|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089454 http://togogenome.org/gene/10090:Akip1 ^@ http://purl.uniprot.org/uniprot/Q9JJR5 ^@ Chain|||Molecule Processing ^@ Chain ^@ A-kinase-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000064858 http://togogenome.org/gene/10090:Msx1 ^@ http://purl.uniprot.org/uniprot/P13297 ^@ Chain|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Crosslink|||DNA Binding|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes interaction with PIAS1.|||Abolishes sumoylation. No effect on interaction with PIAS1.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Homeobox|||Homeobox protein MSX-1|||Required for interaction with EHMT2|||Sumoylated. ^@ http://purl.uniprot.org/annotation/PRO_0000049091 http://togogenome.org/gene/10090:Cfhr4 ^@ http://purl.uniprot.org/uniprot/B2RUG5|||http://purl.uniprot.org/uniprot/E9Q8B5|||http://purl.uniprot.org/uniprot/E9Q8B6|||http://purl.uniprot.org/uniprot/Q0KHD2|||http://purl.uniprot.org/uniprot/Q0KHD3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Sushi ^@ http://purl.uniprot.org/annotation/PRO_5003243112|||http://purl.uniprot.org/annotation/PRO_5003245823|||http://purl.uniprot.org/annotation/PRO_5004174948|||http://purl.uniprot.org/annotation/PRO_5004175193|||http://purl.uniprot.org/annotation/PRO_5014298343 http://togogenome.org/gene/10090:Grk4 ^@ http://purl.uniprot.org/uniprot/O70291|||http://purl.uniprot.org/uniprot/Q8BP13 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ AGC-kinase C-terminal|||G protein-coupled receptor kinase 4|||N-acetylmethionine|||N-terminal|||Phosphoserine|||Protein kinase|||Proton acceptor|||RGS ^@ http://purl.uniprot.org/annotation/PRO_0000085968 http://togogenome.org/gene/10090:Zfp532 ^@ http://purl.uniprot.org/uniprot/Q3TQ12|||http://purl.uniprot.org/uniprot/Q6NXK2 ^@ 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 ^@ Basic and acidic residues|||C2H2-type|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Zinc finger protein 532 ^@ http://purl.uniprot.org/annotation/PRO_0000299553|||http://purl.uniprot.org/annotation/VSP_027745 http://togogenome.org/gene/10090:Hey2 ^@ http://purl.uniprot.org/uniprot/Q0VGJ1|||http://purl.uniprot.org/uniprot/Q9QUS4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abrogates DNA-binding and transcriptional repression.|||Abrogates interaction with GATA4 and repression of GATA4-mediated transcription.|||BHLH|||Disordered|||Hairy/enhancer-of-split related with YRPW motif protein 2|||Orange|||Polar residues|||Transcriptional repression and interaction with NCOR1 and SIN3A|||YQPW motif|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000245516 http://togogenome.org/gene/10090:Ddit4l ^@ http://purl.uniprot.org/uniprot/Q8VHZ5 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ DNA damage-inducible transcript 4-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000307205 http://togogenome.org/gene/10090:Ocln ^@ http://purl.uniprot.org/uniprot/B2RS24|||http://purl.uniprot.org/uniprot/Q61146 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||MARVEL|||OCEL|||Occludin|||Phosphoserine|||Phosphoserine; by PKC; in vitro|||Phosphothreonine|||Phosphothreonine; by PKC/PRKCH|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000146740 http://togogenome.org/gene/10090:H2ac11 ^@ http://purl.uniprot.org/uniprot/B2RVF0|||http://purl.uniprot.org/uniprot/C0HKE1|||http://purl.uniprot.org/uniprot/C0HKE2|||http://purl.uniprot.org/uniprot/C0HKE3|||http://purl.uniprot.org/uniprot/C0HKE4|||http://purl.uniprot.org/uniprot/C0HKE5|||http://purl.uniprot.org/uniprot/C0HKE6|||http://purl.uniprot.org/uniprot/C0HKE7|||http://purl.uniprot.org/uniprot/C0HKE8|||http://purl.uniprot.org/uniprot/C0HKE9 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Histone H2A type 1-C|||Histone H2A type 1-D|||Histone H2A type 1-E|||Histone H2A type 1-G|||Histone H2A type 1-I|||Histone H2A type 1-N|||Histone H2A type 1-O|||Histone H2A type 1-P|||Histone H2A/H2B/H3|||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_0000439715|||http://purl.uniprot.org/annotation/PRO_0000439716|||http://purl.uniprot.org/annotation/PRO_0000439717|||http://purl.uniprot.org/annotation/PRO_0000439718|||http://purl.uniprot.org/annotation/PRO_0000439719|||http://purl.uniprot.org/annotation/PRO_0000439720|||http://purl.uniprot.org/annotation/PRO_0000439721|||http://purl.uniprot.org/annotation/PRO_0000439722|||http://purl.uniprot.org/annotation/PRO_0000439723 http://togogenome.org/gene/10090:Irs2 ^@ http://purl.uniprot.org/uniprot/P81122 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||Disordered|||IRS-type PTB|||Insulin receptor substrate 2|||Omega-N-methylarginine|||PH|||Phosphoserine|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000084240 http://togogenome.org/gene/10090:Tmem170b ^@ http://purl.uniprot.org/uniprot/P86050 ^@ 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_0000354976 http://togogenome.org/gene/10090:Arg1 ^@ http://purl.uniprot.org/uniprot/Q61176 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Arginase-1|||Disordered|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000173694 http://togogenome.org/gene/10090:Rnaseh1 ^@ http://purl.uniprot.org/uniprot/E9QLN8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||RNase H type-1 ^@ http://togogenome.org/gene/10090:Ppp6c ^@ http://purl.uniprot.org/uniprot/Q9CQR6 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ N-acetylmethionine|||Proton donor|||Serine/threonine-protein phosphatase 6 catalytic subunit ^@ http://purl.uniprot.org/annotation/PRO_0000058878 http://togogenome.org/gene/10090:Cacna1f ^@ http://purl.uniprot.org/uniprot/Q7TNI3 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Region|||Site|||Transmembrane ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Voltage-dependent calcium channel alpha-1 subunit IQ ^@ http://togogenome.org/gene/10090:Aff4 ^@ http://purl.uniprot.org/uniprot/Q9ESC8 ^@ 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 ^@ AF4/FMR2 family member 4|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000239394 http://togogenome.org/gene/10090:Fbxo34 ^@ http://purl.uniprot.org/uniprot/E9QM55|||http://purl.uniprot.org/uniprot/Q80XI1 ^@ 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|||F-box|||F-box only protein 34|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000119927|||http://purl.uniprot.org/annotation/VSP_013055 http://togogenome.org/gene/10090:Magea2 ^@ http://purl.uniprot.org/uniprot/Q9R2A2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Ppm1f ^@ http://purl.uniprot.org/uniprot/Q8CGA0 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ PPM-type phosphatase|||Phosphoserine|||Protein phosphatase 1F ^@ http://purl.uniprot.org/annotation/PRO_0000057759 http://togogenome.org/gene/10090:Cnnm3 ^@ http://purl.uniprot.org/uniprot/Q32NY4 ^@ Chain|||Compositionally Biased Region|||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|||Compositionally Biased Region|||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.|||Metal transporter CNNM3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295764|||http://purl.uniprot.org/annotation/VSP_027084 http://togogenome.org/gene/10090:Raver1 ^@ http://purl.uniprot.org/uniprot/A0A158RFV1|||http://purl.uniprot.org/uniprot/Q9CW46 ^@ 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|||In isoform 2.|||Interaction with PTBP1|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||RRM 1|||RRM 2|||RRM 3|||Removed|||Ribonucleoprotein PTB-binding 1 ^@ http://purl.uniprot.org/annotation/PRO_0000081488|||http://purl.uniprot.org/annotation/VSP_017037|||http://purl.uniprot.org/annotation/VSP_017038 http://togogenome.org/gene/10090:Psg25 ^@ http://purl.uniprot.org/uniprot/Q497W1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Stt3b ^@ http://purl.uniprot.org/uniprot/A0A0R4J0D3|||http://purl.uniprot.org/uniprot/Q3TDQ1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DK motif|||DXD motif 1|||DXD motif 2|||Disordered|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B|||Helical|||Important for catalytic activity|||In strain: A.BY, B10.H7 and C3H.SW; correlated with B6dom1-negative phenotype.|||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_0000246002 http://togogenome.org/gene/10090:Pola2 ^@ http://purl.uniprot.org/uniprot/P33611|||http://purl.uniprot.org/uniprot/Q8C2T6 ^@ 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 ^@ DNA polymerase alpha subunit B|||DNA polymerase alpha subunit B N-terminal|||DNA polymerase alpha/delta/epsilon subunit B|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000194036 http://togogenome.org/gene/10090:Prss27 ^@ http://purl.uniprot.org/uniprot/Q8BJR6 ^@ 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_0000027508|||http://purl.uniprot.org/annotation/PRO_0000027509 http://togogenome.org/gene/10090:Mast3 ^@ http://purl.uniprot.org/uniprot/A0A1D5RM97|||http://purl.uniprot.org/uniprot/Q3U214 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ AGC-kinase C-terminal|||Basic and acidic residues|||Basic residues|||Disordered|||Microtubule-associated serine/threonine-protein kinase 3|||PDZ|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000277823 http://togogenome.org/gene/10090:Fam174a ^@ http://purl.uniprot.org/uniprot/Q9D3L0 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Membrane protein FAM174A|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000263651 http://togogenome.org/gene/10090:Or5aq7 ^@ http://purl.uniprot.org/uniprot/Q7TS20 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fbxl20 ^@ http://purl.uniprot.org/uniprot/Q9CZV8 ^@ 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.|||In isoform 3.|||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_0000119871|||http://purl.uniprot.org/annotation/VSP_030770|||http://purl.uniprot.org/annotation/VSP_038354 http://togogenome.org/gene/10090:Rbm18 ^@ http://purl.uniprot.org/uniprot/Q9CR83 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Probable RNA-binding protein 18|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000254123 http://togogenome.org/gene/10090:Zfp3 ^@ http://purl.uniprot.org/uniprot/Q8BLB0 ^@ Chain|||Crosslink|||Modification|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Crosslink|||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)|||Zinc finger protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000233714 http://togogenome.org/gene/10090:Vps28 ^@ http://purl.uniprot.org/uniprot/A0A2R8VKS6|||http://purl.uniprot.org/uniprot/Q8BMZ7|||http://purl.uniprot.org/uniprot/Q9D1C8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ N-acetylmethionine|||VPS28 C-terminal|||VPS28 N-terminal|||Vacuolar protein sorting-associated protein 28 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000120952 http://togogenome.org/gene/10090:Nat8f7 ^@ http://purl.uniprot.org/uniprot/E0CYR6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Transmembrane ^@ Helical|||N-acetyltransferase|||N-acetyltransferase family 8 member 7 ^@ http://purl.uniprot.org/annotation/PRO_0000444045 http://togogenome.org/gene/10090:Surf6 ^@ http://purl.uniprot.org/uniprot/P70279|||http://purl.uniprot.org/uniprot/Q3V1X4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Basic residues|||Citrulline|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ribosomal RNA-processing protein 14/surfeit locus protein 6 C-terminal|||Surfeit locus protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000220970 http://togogenome.org/gene/10090:Adgrg3 ^@ http://purl.uniprot.org/uniprot/Q8R0T6 ^@ 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 ^@ Adhesion G protein-coupled receptor G3|||Cytoplasmic|||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_0000012890 http://togogenome.org/gene/10090:Vmn1r211 ^@ http://purl.uniprot.org/uniprot/Q8R266 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp735 ^@ http://purl.uniprot.org/uniprot/B1ARH2|||http://purl.uniprot.org/uniprot/B2RQK9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Disp3 ^@ http://purl.uniprot.org/uniprot/E9QL24 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||SSD ^@ http://togogenome.org/gene/10090:Armcx2 ^@ http://purl.uniprot.org/uniprot/Q6A058|||http://purl.uniprot.org/uniprot/Q8BJ81|||http://purl.uniprot.org/uniprot/Q8BTE8 ^@ 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|||Cytoplasmic|||Disordered|||Helical; Signal-anchor|||Mitochondrial intermembrane|||Mitochondrion outer membrane (MOM)-targeting sequence|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000191365 http://togogenome.org/gene/10090:Mageb5 ^@ http://purl.uniprot.org/uniprot/Q14AN0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||MAGE ^@ http://togogenome.org/gene/10090:Ncor1 ^@ http://purl.uniprot.org/uniprot/Q5PRE9|||http://purl.uniprot.org/uniprot/Q5RIM6|||http://purl.uniprot.org/uniprot/Q8BK32|||http://purl.uniprot.org/uniprot/Q8CHB6 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||HTH myb-type|||Myb-like|||N-CoR GPS2-interacting|||Polar residues|||Pro residues|||SANT ^@ http://togogenome.org/gene/10090:Herpud1 ^@ http://purl.uniprot.org/uniprot/Q3TMN9|||http://purl.uniprot.org/uniprot/Q9JJK5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein|||Interaction with UBQLN1|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000114921 http://togogenome.org/gene/10090:Zfyve9 ^@ http://purl.uniprot.org/uniprot/A0S860|||http://purl.uniprot.org/uniprot/A2A8R0|||http://purl.uniprot.org/uniprot/A8Y5G5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||FYVE-type|||Polar residues|||Smad anchor for receptor activation-like C-terminal|||Smad anchor for receptor activation-like Smad-binding ^@ http://togogenome.org/gene/10090:Klf1 ^@ http://purl.uniprot.org/uniprot/A0A6I8MWY6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Jph2 ^@ http://purl.uniprot.org/uniprot/Q9ET78 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Site|||Topological Domain|||Transmembrane ^@ Abolishes cleavage by calpain at the C-terminus.|||Abolishes cleavage by calpain at the N-terminus.|||Abolishes nuclear localization of the Junctophilin-2 N-terminal fragment chain.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Cleavage; by calpain|||Cytoplasmic|||Decreased transverse tubule regularity and aberrant calcium handling in septal cardiomyocytes.|||Disordered|||Helical; Anchor for type IV membrane protein|||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|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000159848|||http://purl.uniprot.org/annotation/PRO_0000446376 http://togogenome.org/gene/10090:Slc38a9 ^@ http://purl.uniprot.org/uniprot/Q8BGD6 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CARC motif|||CRAC motif|||Cytoplasmic|||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|||Lumenal|||N-linked (GlcNAc...) asparagine|||Neutral amino acid transporter 9|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000328841 http://togogenome.org/gene/10090:Mau2 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLR7|||http://purl.uniprot.org/uniprot/Q9D2X5 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||MAU2 chromatid cohesion factor homolog|||Sufficient for interaction with NIPBL|||TPR 1|||TPR 2|||TPR 3|||TPR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000254549|||http://purl.uniprot.org/annotation/VSP_037924 http://togogenome.org/gene/10090:1700019D03Rik ^@ http://purl.uniprot.org/uniprot/Q9CPS8 ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region ^@ N-myristoyl glycine|||PKA-RI-binding|||Phosphoserine|||Removed|||S-palmitoyl cysteine|||Small membrane A-kinase anchor protein ^@ http://purl.uniprot.org/annotation/PRO_0000348431 http://togogenome.org/gene/10090:Or5p61 ^@ http://purl.uniprot.org/uniprot/A0A140LJF5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lhfpl6 ^@ http://purl.uniprot.org/uniprot/Q8BM86 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Helical|||LHFPL tetraspan subfamily member 6 protein ^@ http://purl.uniprot.org/annotation/PRO_0000244757 http://togogenome.org/gene/10090:Susd4 ^@ http://purl.uniprot.org/uniprot/Q8BH32 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000251976|||http://purl.uniprot.org/annotation/VSP_020844 http://togogenome.org/gene/10090:Keap1 ^@ http://purl.uniprot.org/uniprot/Q9Z2X8 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Site|||Strand|||Turn ^@ Abolished ability to ubiquitinate NFE2L2/NRF2 without affecting homodimerization.|||Abolishes repression of NFE2L2/NRF2-dependent gene expression.|||Abolishes repression of NFE2L2/NRF2-dependent gene expression. Knockin mice die approximately three weeks after birth because of impaired ability of the BCR(KEAP1) complex to ubiquitinate NFE2L2/NRF2; when associated with A-288.|||Abolishes repression of NFE2L2/NRF2-dependent gene expression. Slows down degradation of NFE2L2/NRF2. Knockin mice die approximately three weeks after birth because of impaired ability of the BCR(KEAP1) complex to ubiquitinate NFE2L2/NRF2; when associated with A-273.|||BACK|||BTB|||Decreases repression of NFE2L2/NRF2-dependent gene expression.|||Does not affect interaction with SQSTM1/p62. Abolished interaction with SQSTM1/p62; when associated with A-380 and A-415.|||Impaired interaction with NFE2L2/NRF2.|||Impaired interaction with SQSTM1/p62.|||Impaired interaction with SQSTM1/p62. Abolished interaction with SQSTM1/p62; when associated with A-380 and A-483.|||Impaired interaction with SQSTM1/p62. Abolished interaction with SQSTM1/p62; when associated with A-415 and A-483.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like ECH-associated protein 1|||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)|||Retains ability to degrade NFE2L2/NRF2; when associated with E-288.|||Retains ability to degrade NFE2L2/NRF2; when associated with W-273. Abolishes ability to be activated by 15-deoxy-delta(12,14)-prostaglandin J2.|||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 small side chain that prevents covalent modification by an electrophile; promotes constitutive ubiquitination of NFE2L2/NRF2 and subsequent repression of phase 2 detoxifying enzymes. Knockin mice are healthy and viable in normal conditions but do not activate NFE2L2/NRF2 in response to oxidative stress. ^@ http://purl.uniprot.org/annotation/PRO_0000119094 http://togogenome.org/gene/10090:Hdhd5 ^@ http://purl.uniprot.org/uniprot/Q91WM2 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Haloacid dehalogenase-like hydrolase domain-containing 5 ^@ http://purl.uniprot.org/annotation/PRO_0000020921 http://togogenome.org/gene/10090:Tpd52l2 ^@ http://purl.uniprot.org/uniprot/Q3TAI4|||http://purl.uniprot.org/uniprot/Q3TUJ9|||http://purl.uniprot.org/uniprot/Q8BKP1|||http://purl.uniprot.org/uniprot/Q9CYZ2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tumor protein D54 ^@ http://purl.uniprot.org/annotation/PRO_0000185745 http://togogenome.org/gene/10090:Rnd3 ^@ http://purl.uniprot.org/uniprot/P61588 ^@ 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_0000198879|||http://purl.uniprot.org/annotation/PRO_0000281231 http://togogenome.org/gene/10090:Ankrd46 ^@ http://purl.uniprot.org/uniprot/Q8BTZ5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Chain|||Repeat|||Sequence Conflict|||Transmembrane ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 46|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000244578 http://togogenome.org/gene/10090:Clasrp ^@ http://purl.uniprot.org/uniprot/Q8CFC7 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||CLK4-associating serine/arginine rich protein|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000081946|||http://purl.uniprot.org/annotation/VSP_008211|||http://purl.uniprot.org/annotation/VSP_008212|||http://purl.uniprot.org/annotation/VSP_008213|||http://purl.uniprot.org/annotation/VSP_008214 http://togogenome.org/gene/10090:Fscb ^@ http://purl.uniprot.org/uniprot/E9QJV1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Rnf183 ^@ http://purl.uniprot.org/uniprot/Q8QZS5 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Mutagenesis Site|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||Decrease in autoubiquitination; when associated with S-13.|||Decrease in autoubiquitination; when associated with S-16.|||E3 ubiquitin-protein ligase RNF183|||Helical; Anchor for type IV membrane protein|||Lumenal|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000247359 http://togogenome.org/gene/10090:Nphp1 ^@ http://purl.uniprot.org/uniprot/A2APS1|||http://purl.uniprot.org/uniprot/Q3TWM5|||http://purl.uniprot.org/uniprot/Q9QY53 ^@ 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|||Disordered|||Nephrocystin-1|||Phosphotyrosine; by FAK2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000159586 http://togogenome.org/gene/10090:Colgalt2 ^@ http://purl.uniprot.org/uniprot/Q6NVG7 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Procollagen galactosyltransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000309542 http://togogenome.org/gene/10090:Hexim2 ^@ http://purl.uniprot.org/uniprot/Q3TVI4 ^@ 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|||Interaction with CCNT1, HEXIM1 and HEXIM2|||Interaction with P-TEFb|||Phosphoserine|||Polar residues|||Protein HEXIM2 ^@ http://purl.uniprot.org/annotation/PRO_0000305268 http://togogenome.org/gene/10090:Abca17 ^@ http://purl.uniprot.org/uniprot/E9PX95 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Transmembrane ^@ ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family A member 17|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000436476 http://togogenome.org/gene/10090:Tmem35a ^@ http://purl.uniprot.org/uniprot/Q9D328 ^@ 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_0000271609 http://togogenome.org/gene/10090:Gm3415 ^@ http://purl.uniprot.org/uniprot/J3QMS8 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Rsf1 ^@ http://purl.uniprot.org/uniprot/E9PWW9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||PHD-type|||Polar residues ^@ http://togogenome.org/gene/10090:Or8b50 ^@ http://purl.uniprot.org/uniprot/E9PW59 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Siva1 ^@ http://purl.uniprot.org/uniprot/O54926 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Apoptosis regulatory protein Siva|||In isoform 2.|||Interaction with BCL2L1 isoform Bcl-x(L) and inhibition of BCL2L1 anti-apoptotic activity|||Phosphoserine|||Phosphotyrosine; by ABL2 ^@ http://purl.uniprot.org/annotation/PRO_0000097775|||http://purl.uniprot.org/annotation/VSP_007526 http://togogenome.org/gene/10090:Pccb ^@ http://purl.uniprot.org/uniprot/E9Q1J7|||http://purl.uniprot.org/uniprot/Q3UYS0|||http://purl.uniprot.org/uniprot/Q99MN9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Acyl-CoA binding|||Carboxyltransferase|||CoA carboxyltransferase C-terminal|||CoA carboxyltransferase N-terminal|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Propionyl-CoA carboxylase beta chain, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000000294 http://togogenome.org/gene/10090:Lrfn4 ^@ http://purl.uniprot.org/uniprot/Q80XU8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||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 4|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000014844 http://togogenome.org/gene/10090:Or10g3 ^@ http://purl.uniprot.org/uniprot/Q8VF72 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Crnn ^@ http://purl.uniprot.org/uniprot/D3YUU6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||EF-hand|||Polar residues ^@ http://togogenome.org/gene/10090:Vnn3 ^@ http://purl.uniprot.org/uniprot/Q9QZ25 ^@ 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 ^@ CN hydrolase|||GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Vascular non-inflammatory molecule 3 ^@ http://purl.uniprot.org/annotation/PRO_0000019722|||http://purl.uniprot.org/annotation/PRO_0000019723 http://togogenome.org/gene/10090:Dvl1 ^@ http://purl.uniprot.org/uniprot/P51141 ^@ 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|||DEP|||DIX|||Disordered|||Loss of oligomerization.|||PDZ|||Phosphoserine|||Polar residues|||Reduces activity in Wnt signaling; when associated with I-449.|||Reduces activity in Wnt signaling; when associated with I-452.|||Segment polarity protein dishevelled homolog DVL-1|||Strongly reduces activity in Wnt signaling. Abolishes location at the cell membrane. ^@ http://purl.uniprot.org/annotation/PRO_0000145743 http://togogenome.org/gene/10090:Pcsk7 ^@ http://purl.uniprot.org/uniprot/Q61139 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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_0000027116|||http://purl.uniprot.org/annotation/PRO_0000027117 http://togogenome.org/gene/10090:Ldc1 ^@ http://purl.uniprot.org/uniprot/B7ZWH9|||http://purl.uniprot.org/uniprot/Q3UNZ2 ^@ Active Site|||Domain Extent|||Modification|||Modified Residue|||Region|||Site ^@ Active Site|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N6-(pyridoxal phosphate)lysine|||Orn/DAP/Arg decarboxylase 2 C-terminal|||Orn/DAP/Arg decarboxylase 2 N-terminal|||Proton donor ^@ http://togogenome.org/gene/10090:Or12e9 ^@ http://purl.uniprot.org/uniprot/L7MTT1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:N4bp1 ^@ http://purl.uniprot.org/uniprot/Q5EBQ4|||http://purl.uniprot.org/uniprot/Q6A037 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||Cleavage|||Cleavage; by CASP8|||Cleavage; by MALT1|||CoCUN|||Disordered|||KH-like|||NEDD4-binding protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Prevents cleavage by CASP8 and subsequent inactivation.|||RNase NYN ^@ http://purl.uniprot.org/annotation/PRO_0000301985 http://togogenome.org/gene/10090:Anapc2 ^@ http://purl.uniprot.org/uniprot/Q8BZQ7 ^@ 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|||Anaphase-promoting complex subunit 2|||Disordered|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000119812 http://togogenome.org/gene/10090:Asap3 ^@ http://purl.uniprot.org/uniprot/Q5U464 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Zinc Finger ^@ ANK 1|||ANK 2|||Arf-GAP|||Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3|||C4-type|||Disordered|||PH|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000232888 http://togogenome.org/gene/10090:Prkx ^@ http://purl.uniprot.org/uniprot/Q922R0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ AGC-kinase C-terminal|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||cAMP-dependent protein kinase catalytic subunit PRKX ^@ http://purl.uniprot.org/annotation/PRO_0000086583 http://togogenome.org/gene/10090:Tnks ^@ http://purl.uniprot.org/uniprot/Q6PFX9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||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 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||PARP catalytic|||Polar residues|||Poly [ADP-ribose] polymerase tankyrase-1|||Pro residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000409511|||http://purl.uniprot.org/annotation/VSP_041320 http://togogenome.org/gene/10090:Or8c13 ^@ http://purl.uniprot.org/uniprot/E9Q843 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gstm3 ^@ http://purl.uniprot.org/uniprot/P19639 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000185828 http://togogenome.org/gene/10090:Atxn2l ^@ http://purl.uniprot.org/uniprot/A0A0U1RPL0|||http://purl.uniprot.org/uniprot/Q3TGG2|||http://purl.uniprot.org/uniprot/Q7TQH0 ^@ 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|||Ataxin-2-like protein|||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.|||Interaction with MPL|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Sm ^@ http://purl.uniprot.org/annotation/PRO_0000064755|||http://purl.uniprot.org/annotation/VSP_011595|||http://purl.uniprot.org/annotation/VSP_011596 http://togogenome.org/gene/10090:Cc2d2a ^@ http://purl.uniprot.org/uniprot/Q8CFW7 ^@ 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|||C2|||Coiled-coil and C2 domain-containing protein 2A|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000317251|||http://purl.uniprot.org/annotation/VSP_030925 http://togogenome.org/gene/10090:Pabpc1 ^@ http://purl.uniprot.org/uniprot/P29341 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine; alternate|||CSDE1-binding|||Dimethylated arginine; alternate|||N-acetylmethionine|||N6-acetyllysine|||N6-methyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Omega-N-methylated arginine; by CARM1|||PABC|||Phosphoserine|||Phosphothreonine|||Polyadenylate-binding protein 1|||RRM 1|||RRM 2|||RRM 3|||RRM 4 ^@ http://purl.uniprot.org/annotation/PRO_0000081699 http://togogenome.org/gene/10090:Gm8978 ^@ http://purl.uniprot.org/uniprot/A0A494BBH0 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Signal Peptide ^@ Charge relay system|||Lipase|||Nucleophile|||Partial AB-hydrolase lipase ^@ http://purl.uniprot.org/annotation/PRO_5019711791 http://togogenome.org/gene/10090:Rab30 ^@ http://purl.uniprot.org/uniprot/Q923S9 ^@ 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 Rab-30|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121231|||http://purl.uniprot.org/annotation/PRO_0000370827 http://togogenome.org/gene/10090:Kif5a ^@ http://purl.uniprot.org/uniprot/P33175|||http://purl.uniprot.org/uniprot/Q3US62 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Disordered|||Globular|||Interaction with BICD2|||Kinesin heavy chain isoform 5A|||Kinesin motor|||Loss of ability to induce formation of neurite-like membrane protrusions in non-neuronal cells.|||Microtubule-binding|||N-acetylalanine|||Necessary for interaction with ZFYVE27|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000125354 http://togogenome.org/gene/10090:Sall2 ^@ http://purl.uniprot.org/uniprot/A0A2I3BQV4|||http://purl.uniprot.org/uniprot/Q8BP69|||http://purl.uniprot.org/uniprot/Q9QX96 ^@ 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 ^@ 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)|||Phosphoserine|||Polar residues|||Pro residues|||Sal-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000047023 http://togogenome.org/gene/10090:Tas2r129 ^@ http://purl.uniprot.org/uniprot/Q7M709 ^@ 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 129 ^@ http://purl.uniprot.org/annotation/PRO_0000248485 http://togogenome.org/gene/10090:Ifitm6 ^@ http://purl.uniprot.org/uniprot/Q3SXF0 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Cbx7 ^@ http://purl.uniprot.org/uniprot/F8WHN2|||http://purl.uniprot.org/uniprot/Q8VDS3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand ^@ Abolishes binding to trimethylated histone H3.|||Basic and acidic residues|||Chromo|||Chromobox protein homolog 7|||Disordered|||Strongly reduced RNA binding.|||Strongly reduced RNA binding. Prevents cellular senescence and promotes continued cell division.|||Strongly reduced binding to methylated histone H3 (H3K27me3). Causes premature cellular senescence. ^@ http://purl.uniprot.org/annotation/PRO_0000080213 http://togogenome.org/gene/10090:Abi2 ^@ http://purl.uniprot.org/uniprot/A0A087WRS3|||http://purl.uniprot.org/uniprot/P62484|||http://purl.uniprot.org/uniprot/Q6AXD2|||http://purl.uniprot.org/uniprot/Q6AXH6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Abl interactor 2|||Acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000191791 http://togogenome.org/gene/10090:Slc4a3 ^@ http://purl.uniprot.org/uniprot/P16283|||http://purl.uniprot.org/uniprot/Q68EG4|||http://purl.uniprot.org/uniprot/Q9ERP4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Anion exchange protein 3|||Band 3 cytoplasmic|||Basic and acidic residues|||Basic residues|||Bicarbonate transporter-like transmembrane|||Cytoplasmic|||Disordered|||Helical|||In isoform 14-AE3.|||In isoform 311-AE3.|||Membrane (anion exchange)|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000079220|||http://purl.uniprot.org/annotation/VSP_000464|||http://purl.uniprot.org/annotation/VSP_000465|||http://purl.uniprot.org/annotation/VSP_000466|||http://purl.uniprot.org/annotation/VSP_000467 http://togogenome.org/gene/10090:Thap2 ^@ http://purl.uniprot.org/uniprot/Q9D305 ^@ Chain|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Motif|||Zinc Finger ^@ HCFC1-binding motif (HBM)|||THAP domain-containing protein 2|||THAP-type ^@ http://purl.uniprot.org/annotation/PRO_0000068643 http://togogenome.org/gene/10090:Gdpd1 ^@ http://purl.uniprot.org/uniprot/Q9CRY7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||GP-PDE|||Helical|||Lysophospholipase D GDPD1 ^@ http://purl.uniprot.org/annotation/PRO_0000251932 http://togogenome.org/gene/10090:Oplah ^@ http://purl.uniprot.org/uniprot/Q8K010 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ 5-oxoprolinase|||Disordered|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000208578 http://togogenome.org/gene/10090:Clec2h ^@ http://purl.uniprot.org/uniprot/Q8C1T8 ^@ 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-type lectin|||C-type lectin domain family 2 member H|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In strain: FVB/N.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000315290 http://togogenome.org/gene/10090:Sh3gl2 ^@ http://purl.uniprot.org/uniprot/Q62420 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ BAR|||Binds and tubulates liposomes|||Disordered|||Endophilin-A1|||Membrane-binding amphipathic helix|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Required for dimerization upon membrane association|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000146748 http://togogenome.org/gene/10090:Pak3 ^@ http://purl.uniprot.org/uniprot/B1GX80|||http://purl.uniprot.org/uniprot/B1GX81|||http://purl.uniprot.org/uniprot/Q61036 ^@ 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 ^@ Acidic residues|||Autoregulatory region|||Basic and acidic residues|||CRIB|||Decreases interaction of PAK3 with CDC42 but increases interaction with RAC1.|||Disordered|||GTPase-binding|||In isoform 2.|||Linker|||Loss of kinase activity.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PAK 3|||When expressed in hippocampal neurons, decreases the number of dendritic spines. Strong decrease in the number of dendritic spines; when associated with L-78 and L-81.|||When expressed in hippocampal neurons, increases the density of both spines and dendritic protrusions.|||When expressed in hippocampal neurons, strongly decreases the number of dendritic spines; when associated with L-78 and R-312.|||When expressed in hippocampal neurons, strongly decreases the number of dendritic spines; when associated with L-81 and R-312. ^@ http://purl.uniprot.org/annotation/PRO_0000086470|||http://purl.uniprot.org/annotation/VSP_010243 http://togogenome.org/gene/10090:Ywhae ^@ http://purl.uniprot.org/uniprot/P62259|||http://purl.uniprot.org/uniprot/Q5SS40 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Site ^@ 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|||Interaction with phosphoserine on interacting protein|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000058619 http://togogenome.org/gene/10090:Csnk2a2 ^@ http://purl.uniprot.org/uniprot/O54833|||http://purl.uniprot.org/uniprot/Q545V8|||http://purl.uniprot.org/uniprot/Q8CDH5 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue ^@ Casein kinase II subunit alpha'|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085892 http://togogenome.org/gene/10090:Cfap141 ^@ http://purl.uniprot.org/uniprot/Q9D9D9 ^@ Chain|||Molecule Processing ^@ Chain ^@ Cilia- and flagella-associated protein 141 ^@ http://purl.uniprot.org/annotation/PRO_0000270967 http://togogenome.org/gene/10090:Pum1 ^@ http://purl.uniprot.org/uniprot/E9Q6M7|||http://purl.uniprot.org/uniprot/Q3TQ21|||http://purl.uniprot.org/uniprot/Q3TTW5|||http://purl.uniprot.org/uniprot/Q80U78 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Adenine-nucleotide binding in RNA target|||Basic and acidic residues|||Disordered|||Guanine-nucleotide binding in RNA target|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||N-acetylserine|||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 1|||Removed|||Uracil-nucleotide binding in RNA target ^@ http://purl.uniprot.org/annotation/PRO_0000075918|||http://purl.uniprot.org/annotation/VSP_009315|||http://purl.uniprot.org/annotation/VSP_009316|||http://purl.uniprot.org/annotation/VSP_009317|||http://purl.uniprot.org/annotation/VSP_009318 http://togogenome.org/gene/10090:Lipt2 ^@ http://purl.uniprot.org/uniprot/Q9D009 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ Acyl-thioester intermediate|||BPL/LPL catalytic|||Lowers pKa of active site Cys|||Mitochondrion|||N6-succinyllysine|||Putative lipoyltransferase 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000332306 http://togogenome.org/gene/10090:Sardh ^@ http://purl.uniprot.org/uniprot/Q3TWI2|||http://purl.uniprot.org/uniprot/Q99LB7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Aminomethyltransferase folate-binding|||FAD dependent oxidoreductase|||FAD dependent oxidoreductase central|||Glycine cleavage T-protein C-terminal barrel|||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_0000010771 http://togogenome.org/gene/10090:Il2ra ^@ http://purl.uniprot.org/uniprot/P01590|||http://purl.uniprot.org/uniprot/Q544I2 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interleukin-2 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sushi|||Sushi 1|||Sushi 2 ^@ http://purl.uniprot.org/annotation/PRO_0000011026|||http://purl.uniprot.org/annotation/PRO_5014309622 http://togogenome.org/gene/10090:Ube2d2a ^@ http://purl.uniprot.org/uniprot/P62838|||http://purl.uniprot.org/uniprot/Q3UT95 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ Glycyl thioester intermediate|||UBC core|||Ubiquitin-conjugating enzyme E2 D2 ^@ http://purl.uniprot.org/annotation/PRO_0000082463 http://togogenome.org/gene/10090:Cdc27 ^@ http://purl.uniprot.org/uniprot/A2A6Q5|||http://purl.uniprot.org/uniprot/Q3TTW1|||http://purl.uniprot.org/uniprot/Q8BYJ1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Cell division cycle protein 27 homolog|||Disordered|||In isoform 2 and isoform 3.|||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_0000390473|||http://purl.uniprot.org/annotation/VSP_038534|||http://purl.uniprot.org/annotation/VSP_038535 http://togogenome.org/gene/10090:Mmp28 ^@ http://purl.uniprot.org/uniprot/Q8BG29|||http://purl.uniprot.org/uniprot/Q8CGV5|||http://purl.uniprot.org/uniprot/Q8CGV8 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Repeat|||Signal Peptide ^@ Hemopexin|||Peptidase metallopeptidase|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_5015099028|||http://purl.uniprot.org/annotation/PRO_5015099093|||http://purl.uniprot.org/annotation/PRO_5015099108 http://togogenome.org/gene/10090:Mfap1b ^@ http://purl.uniprot.org/uniprot/C0HKD8|||http://purl.uniprot.org/uniprot/C0HKD9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Microfibrillar-associated protein 1A|||Microfibrillar-associated protein 1B|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000096459|||http://purl.uniprot.org/annotation/PRO_0000439458 http://togogenome.org/gene/10090:Capn13 ^@ http://purl.uniprot.org/uniprot/Q3UW68 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ Calpain catalytic|||Calpain-13|||EF-hand 1|||EF-hand 2 ^@ http://purl.uniprot.org/annotation/PRO_0000259583 http://togogenome.org/gene/10090:Tmprss9 ^@ http://purl.uniprot.org/uniprot/D3YTR8 ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region ^@ Disordered|||Peptidase S1|||Polar residues|||Pro residues|||SEA ^@ http://togogenome.org/gene/10090:Rps21 ^@ http://purl.uniprot.org/uniprot/Q9CQR2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ N-acetylmethionine|||N6-acetyllysine|||Small ribosomal subunit protein eS21 ^@ http://purl.uniprot.org/annotation/PRO_0000194731 http://togogenome.org/gene/10090:B3gnt3 ^@ http://purl.uniprot.org/uniprot/Q5JCS9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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_0000219173 http://togogenome.org/gene/10090:Prrx2 ^@ http://purl.uniprot.org/uniprot/A2APZ7|||http://purl.uniprot.org/uniprot/Q06348 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Motif|||Region ^@ Disordered|||Homeobox|||OAR|||Paired mesoderm homeobox protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000049256 http://togogenome.org/gene/10090:Nudt2 ^@ http://purl.uniprot.org/uniprot/P56380|||http://purl.uniprot.org/uniprot/Q3V1C8 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict ^@ Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]|||N-acetylalanine|||Nudix box|||Nudix hydrolase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057103 http://togogenome.org/gene/10090:Vmn1r111 ^@ http://purl.uniprot.org/uniprot/D3YTY2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cd14 ^@ http://purl.uniprot.org/uniprot/P10810|||http://purl.uniprot.org/uniprot/Q3UB18|||http://purl.uniprot.org/uniprot/Q3UE54|||http://purl.uniprot.org/uniprot/Q4FJP7 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Signal Peptide|||Strand|||Turn ^@ 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|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Required for response to bacterial lipopolysaccharide (LPS) ^@ http://purl.uniprot.org/annotation/PRO_0000020887|||http://purl.uniprot.org/annotation/PRO_0000020888|||http://purl.uniprot.org/annotation/PRO_5004230087|||http://purl.uniprot.org/annotation/PRO_5014309365 http://togogenome.org/gene/10090:Agmat ^@ http://purl.uniprot.org/uniprot/A2AS89 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Guanidino acid hydrolase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000320072 http://togogenome.org/gene/10090:Pstk ^@ http://purl.uniprot.org/uniprot/Q8BP74 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Binding Site|||Chain|||Splice Variant ^@ In isoform 2.|||L-seryl-tRNA(Sec) kinase ^@ http://purl.uniprot.org/annotation/PRO_0000097081|||http://purl.uniprot.org/annotation/VSP_024860 http://togogenome.org/gene/10090:Slc29a1 ^@ http://purl.uniprot.org/uniprot/Q3TCZ2|||http://purl.uniprot.org/uniprot/Q9JIM1 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Equilibrative nucleoside transporter 1|||Essential for nucleobase transport|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000209338|||http://purl.uniprot.org/annotation/VSP_010471 http://togogenome.org/gene/10090:Satl1 ^@ http://purl.uniprot.org/uniprot/Q9D5N8 ^@ 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 ^@ Disordered|||N-acetyltransferase|||Polar residues|||Spermidine/spermine N(1)-acetyltransferase-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000282929 http://togogenome.org/gene/10090:Pex26 ^@ http://purl.uniprot.org/uniprot/Q8BGI5 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Peroxisomal matrix|||Peroxisome assembly protein 26 ^@ http://purl.uniprot.org/annotation/PRO_0000058342|||http://purl.uniprot.org/annotation/VSP_010444 http://togogenome.org/gene/10090:Mcpt8 ^@ http://purl.uniprot.org/uniprot/P43430|||http://purl.uniprot.org/uniprot/Q3UWB6 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Mast cell protease 8|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027457|||http://purl.uniprot.org/annotation/PRO_0000027458|||http://purl.uniprot.org/annotation/PRO_5014309175 http://togogenome.org/gene/10090:Jchain ^@ http://purl.uniprot.org/uniprot/P01592 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Immunoglobulin J chain|||Interchain (with heavy chain)|||N-linked (GlcNAc...) (complex) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000021486 http://togogenome.org/gene/10090:Gm4836 ^@ http://purl.uniprot.org/uniprot/Q62478 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Slc18a1 ^@ http://purl.uniprot.org/uniprot/Q32XG7|||http://purl.uniprot.org/uniprot/Q8R090 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Chromaffin granule amine transporter|||Cytoplasmic|||Helical|||Lumenal, vesicle|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000127511 http://togogenome.org/gene/10090:Or2a7 ^@ http://purl.uniprot.org/uniprot/P34984|||http://purl.uniprot.org/uniprot/Q0VAZ7 ^@ 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 2A7 ^@ http://purl.uniprot.org/annotation/PRO_0000150812 http://togogenome.org/gene/10090:Dph3 ^@ http://purl.uniprot.org/uniprot/D3YXV3|||http://purl.uniprot.org/uniprot/Q8K0W9 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Strand|||Turn ^@ DPH-type MB|||Diphthamide biosynthesis protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000082621 http://togogenome.org/gene/10090:Arhgap24 ^@ http://purl.uniprot.org/uniprot/D3Z5T4|||http://purl.uniprot.org/uniprot/G3X9N1|||http://purl.uniprot.org/uniprot/Q8BHH3|||http://purl.uniprot.org/uniprot/Q8C4V1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho GTPase-activating protein 24|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000280474|||http://purl.uniprot.org/annotation/VSP_023719|||http://purl.uniprot.org/annotation/VSP_023720|||http://purl.uniprot.org/annotation/VSP_023721 http://togogenome.org/gene/10090:Sulf1 ^@ http://purl.uniprot.org/uniprot/Q8K007 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||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|||N-linked (GlcNAc...) asparagine|||Nucleophile|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000033435|||http://purl.uniprot.org/annotation/PRO_0000457757 http://togogenome.org/gene/10090:Cxcl16 ^@ http://purl.uniprot.org/uniprot/A2CFE9|||http://purl.uniprot.org/uniprot/Q8BSU2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ C-X-C motif chemokine 16|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000005119|||http://purl.uniprot.org/annotation/PRO_5007633832 http://togogenome.org/gene/10090:Serpina1d ^@ http://purl.uniprot.org/uniprot/Q00897 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide|||Site ^@ Alpha-1-antitrypsin 1-4|||N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000032391 http://togogenome.org/gene/10090:Mrpl38 ^@ http://purl.uniprot.org/uniprot/Q8K2M0 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Large ribosomal subunit protein mL38|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000261653|||http://purl.uniprot.org/annotation/VSP_021748 http://togogenome.org/gene/10090:Cyp2j12 ^@ http://purl.uniprot.org/uniprot/G3UXT0 ^@ Binding Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Nup160 ^@ http://purl.uniprot.org/uniprot/Q9Z0W3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Nuclear pore complex protein Nup160|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000204852|||http://purl.uniprot.org/annotation/VSP_018500|||http://purl.uniprot.org/annotation/VSP_018501 http://togogenome.org/gene/10090:Fbh1 ^@ http://purl.uniprot.org/uniprot/Q3UGP2|||http://purl.uniprot.org/uniprot/Q8K2I9 ^@ 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 ^@ APIM motif|||Disordered|||F-box|||F-box DNA helicase 1|||In isoform 2.|||PIP-box|||UvrD-like helicase ATP-binding ^@ http://purl.uniprot.org/annotation/PRO_0000119902|||http://purl.uniprot.org/annotation/VSP_009716|||http://purl.uniprot.org/annotation/VSP_009717 http://togogenome.org/gene/10090:Aldob ^@ http://purl.uniprot.org/uniprot/Q91Y97 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site ^@ Fructose-bisphosphate aldolase B|||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_0000216941 http://togogenome.org/gene/10090:Uba3 ^@ http://purl.uniprot.org/uniprot/Q3TL72|||http://purl.uniprot.org/uniprot/Q66JT6|||http://purl.uniprot.org/uniprot/Q8C878 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Determines specificity for NEDD8|||E2 binding|||Glycyl thioester intermediate|||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|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194942|||http://purl.uniprot.org/annotation/VSP_010787 http://togogenome.org/gene/10090:Mrpl42 ^@ http://purl.uniprot.org/uniprot/Q9CPV3 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Large ribosomal subunit protein mL42|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000087725 http://togogenome.org/gene/10090:Igfbpl1 ^@ http://purl.uniprot.org/uniprot/Q80W15 ^@ 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_0000297688 http://togogenome.org/gene/10090:Or6n1 ^@ http://purl.uniprot.org/uniprot/Q7TRW1|||http://purl.uniprot.org/uniprot/Q8VFZ2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vps52 ^@ http://purl.uniprot.org/uniprot/Q8C754 ^@ 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_0000213316|||http://purl.uniprot.org/annotation/VSP_016234|||http://purl.uniprot.org/annotation/VSP_016235 http://togogenome.org/gene/10090:Adcyap1 ^@ http://purl.uniprot.org/uniprot/O70176|||http://purl.uniprot.org/uniprot/Q3UYH8|||http://purl.uniprot.org/uniprot/Q8BJT8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Glucagon / GIP / secretin / VIP family|||Glucagon / GIP / secretin / VIP family domain-containing protein|||Important for receptor binding|||Leucine amide|||Lysine amide|||PACAP-related peptide|||Pituitary adenylate cyclase-activating polypeptide 27|||Pituitary adenylate cyclase-activating polypeptide 38 ^@ http://purl.uniprot.org/annotation/PRO_0000011491|||http://purl.uniprot.org/annotation/PRO_0000011492|||http://purl.uniprot.org/annotation/PRO_0000011493|||http://purl.uniprot.org/annotation/PRO_0000011494|||http://purl.uniprot.org/annotation/PRO_0000011495|||http://purl.uniprot.org/annotation/PRO_5004303672|||http://purl.uniprot.org/annotation/PRO_5014309238 http://togogenome.org/gene/10090:Smlr1 ^@ http://purl.uniprot.org/uniprot/J3QMJ4 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Ccpg1 ^@ http://purl.uniprot.org/uniprot/D3Z7R9|||http://purl.uniprot.org/uniprot/Q640L3 ^@ 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 ^@ Basic and acidic residues|||Cell cycle progression protein 1|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Interaction with MCF2L and SRC|||Lumenal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000310539|||http://purl.uniprot.org/annotation/VSP_029317|||http://purl.uniprot.org/annotation/VSP_029318 http://togogenome.org/gene/10090:Xiap ^@ http://purl.uniprot.org/uniprot/Q60989 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ BIR 1|||BIR 2|||BIR 3|||E3 ubiquitin-protein ligase XIAP|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with caspase-7|||RING-type|||Required for anti-apoptotic activity|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000122353 http://togogenome.org/gene/10090:Fgf1 ^@ http://purl.uniprot.org/uniprot/P61148 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Propeptide|||Region ^@ Fibroblast growth factor 1|||Heparin-binding|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000008911|||http://purl.uniprot.org/annotation/PRO_0000008912 http://togogenome.org/gene/10090:Cep70 ^@ http://purl.uniprot.org/uniprot/Q6IQY5 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Repeat|||Sequence Conflict|||Splice Variant ^@ Centrosomal protein of 70 kDa|||In isoform 2.|||TPR ^@ http://purl.uniprot.org/annotation/PRO_0000089498|||http://purl.uniprot.org/annotation/VSP_042142|||http://purl.uniprot.org/annotation/VSP_042143 http://togogenome.org/gene/10090:Gm20888 ^@ http://purl.uniprot.org/uniprot/J3QNI1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Zfp688 ^@ http://purl.uniprot.org/uniprot/E9Q5M9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Tcaim ^@ http://purl.uniprot.org/uniprot/G3X983|||http://purl.uniprot.org/uniprot/Q66JZ4 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent ^@ DUF4460|||DUF4461|||T-cell activation inhibitor, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000235341 http://togogenome.org/gene/10090:Cr2 ^@ http://purl.uniprot.org/uniprot/A0A1B0GS59|||http://purl.uniprot.org/uniprot/Q9DC83 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_5008408573|||http://purl.uniprot.org/annotation/PRO_5015099704 http://togogenome.org/gene/10090:Nkpd1 ^@ http://purl.uniprot.org/uniprot/H7BX48|||http://purl.uniprot.org/uniprot/Q0VF94 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||KAP NTPase|||NTPase KAP family P-loop domain-containing protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000294151|||http://purl.uniprot.org/annotation/VSP_026599 http://togogenome.org/gene/10090:Duxbl1 ^@ http://purl.uniprot.org/uniprot/Q7TNE6 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Hsd3b9 ^@ http://purl.uniprot.org/uniprot/E9Q007 ^@ Domain Extent|||Region ^@ Domain Extent ^@ 3-beta hydroxysteroid dehydrogenase/isomerase ^@ http://togogenome.org/gene/10090:Tcp11 ^@ http://purl.uniprot.org/uniprot/B2KF24|||http://purl.uniprot.org/uniprot/Q5FWA2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rapgef5 ^@ http://purl.uniprot.org/uniprot/Q8C0Q9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ DEP|||In isoform 2.|||In isoform 3.|||N-terminal Ras-GEF|||Rap guanine nucleotide exchange factor 5|||Ras-GEF ^@ http://purl.uniprot.org/annotation/PRO_0000068874|||http://purl.uniprot.org/annotation/VSP_007617|||http://purl.uniprot.org/annotation/VSP_007618|||http://purl.uniprot.org/annotation/VSP_007619|||http://purl.uniprot.org/annotation/VSP_007620 http://togogenome.org/gene/10090:Opn1mw ^@ http://purl.uniprot.org/uniprot/O35599|||http://purl.uniprot.org/uniprot/Q3UEX0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||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|||Medium-wave-sensitive opsin 1|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||Required for 11-cis-retinal regeneration ^@ http://purl.uniprot.org/annotation/PRO_0000197786 http://togogenome.org/gene/10090:Cacng1 ^@ http://purl.uniprot.org/uniprot/O70578|||http://purl.uniprot.org/uniprot/Q4KL26 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Voltage-dependent calcium channel gamma-1 subunit ^@ http://purl.uniprot.org/annotation/PRO_0000164670 http://togogenome.org/gene/10090:Pcdhga8 ^@ http://purl.uniprot.org/uniprot/Q91XY0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (Man...) threonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099516 http://togogenome.org/gene/10090:Adck1 ^@ http://purl.uniprot.org/uniprot/Q9D0L4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Signal Peptide|||Splice Variant ^@ AarF domain-containing protein kinase 1|||In isoform 2.|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000252250|||http://purl.uniprot.org/annotation/VSP_020886 http://togogenome.org/gene/10090:Txlnb ^@ http://purl.uniprot.org/uniprot/Q8VBT1 ^@ 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|||Beta-taxilin|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000189424 http://togogenome.org/gene/10090:Ermard ^@ http://purl.uniprot.org/uniprot/E9Q048 ^@ Domain Extent|||Region ^@ Domain Extent ^@ DUF4209 ^@ http://togogenome.org/gene/10090:ND5 ^@ http://purl.uniprot.org/uniprot/P03921|||http://purl.uniprot.org/uniprot/Q9MD82 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ Helical|||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_0000118114 http://togogenome.org/gene/10090:Ftdc1 ^@ http://purl.uniprot.org/uniprot/Q3UWK9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Ferritin-like diiron ^@ http://togogenome.org/gene/10090:Pgpep1l ^@ http://purl.uniprot.org/uniprot/Q9CWB5 ^@ Active Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Chain ^@ Pyroglutamyl-peptidase 1-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000334695 http://togogenome.org/gene/10090:Trp53tg5 ^@ http://purl.uniprot.org/uniprot/Q9D976 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Scmh1 ^@ http://purl.uniprot.org/uniprot/Q8K214 ^@ 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|||In isoform 2.|||MBT 1|||MBT 2|||Polar residues|||Polycomb protein SCMH1|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000114335|||http://purl.uniprot.org/annotation/VSP_051680|||http://purl.uniprot.org/annotation/VSP_051681 http://togogenome.org/gene/10090:Selenoo ^@ http://purl.uniprot.org/uniprot/Q9DBC0 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non standard residue|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Non standard residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||Phosphoserine|||Phosphothreonine|||Protein adenylyltransferase SelO, mitochondrial|||Proton acceptor|||Selenocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121400 http://togogenome.org/gene/10090:Phactr1 ^@ http://purl.uniprot.org/uniprot/B1B1B8|||http://purl.uniprot.org/uniprot/Q2M3X8|||http://purl.uniprot.org/uniprot/Q3TLK1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Turn ^@ Abolishes nuclear import.|||Acidic residues|||Basic and acidic residues|||Constitutively nuclear; when associated with A-431 and A-469. Strongly reduced affinity for actin.|||Constitutively nuclear; when associated with A-431 and A-507. Strongly reduced affinity for actin.|||Constitutively nuclear; when associated with A-469 and A-507. Strongly reduced affinity for actin.|||Disordered|||Does not rescue cortical neuron migration defects in PHACTR1 knocked-down mice.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Increases affinity for actin.|||Nuclear localization signal|||Phosphatase and actin regulator 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||RPEL|||RPEL 1|||RPEL 2|||RPEL 3|||RPEL 4|||Reduces affinity for actin. ^@ http://purl.uniprot.org/annotation/PRO_0000235990|||http://purl.uniprot.org/annotation/VSP_018559|||http://purl.uniprot.org/annotation/VSP_018560 http://togogenome.org/gene/10090:Atp5g1 ^@ http://purl.uniprot.org/uniprot/Q9CR84 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide|||Transmembrane ^@ Chain|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000395412 http://togogenome.org/gene/10090:Krtcap2 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQN1|||http://purl.uniprot.org/uniprot/Q5RL79 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Motif|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Keratinocyte-associated protein 2|||Lumenal|||Phosphothreonine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000226993 http://togogenome.org/gene/10090:Nlrp4f ^@ http://purl.uniprot.org/uniprot/L7N1W9|||http://purl.uniprot.org/uniprot/Q3UX59|||http://purl.uniprot.org/uniprot/Q4G0D0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Non-terminal Residue|||Signal Peptide ^@ NACHT|||NACHT LRR and PYD ^@ http://purl.uniprot.org/annotation/PRO_5004238479 http://togogenome.org/gene/10090:Gdf1 ^@ http://purl.uniprot.org/uniprot/A2RT05|||http://purl.uniprot.org/uniprot/P20863|||http://purl.uniprot.org/uniprot/Q3TRG1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Embryonic growth/differentiation factor 1|||Helical|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile|||TGF-beta family profile domain-containing protein|||TLC ^@ http://purl.uniprot.org/annotation/PRO_0000033900|||http://purl.uniprot.org/annotation/PRO_0000033901|||http://purl.uniprot.org/annotation/PRO_5004229574 http://togogenome.org/gene/10090:Or2m12 ^@ http://purl.uniprot.org/uniprot/Q8VF87 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or51e2 ^@ http://purl.uniprot.org/uniprot/Q8VBV9 ^@ 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 51E2 ^@ http://purl.uniprot.org/annotation/PRO_0000430209 http://togogenome.org/gene/10090:Dapl1 ^@ http://purl.uniprot.org/uniprot/Q9D757 ^@ Chain|||Molecule Processing ^@ Chain ^@ Death-associated protein-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000316836 http://togogenome.org/gene/10090:Psme2 ^@ http://purl.uniprot.org/uniprot/G3X9V0|||http://purl.uniprot.org/uniprot/P97372|||http://purl.uniprot.org/uniprot/Q5SVP3 ^@ 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 ^@ Basic and acidic residues|||Disordered|||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_0000161786 http://togogenome.org/gene/10090:Fam207a ^@ http://purl.uniprot.org/uniprot/P58468 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Ribosome biogenesis protein SLX9 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000079529 http://togogenome.org/gene/10090:Rpl28 ^@ http://purl.uniprot.org/uniprot/P41105|||http://purl.uniprot.org/uniprot/Q5M9J8 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL28|||N-acetylserine|||Phosphoserine|||Removed|||Ribosomal eL28/Mak16 ^@ http://purl.uniprot.org/annotation/PRO_0000122390 http://togogenome.org/gene/10090:Teddm2 ^@ http://purl.uniprot.org/uniprot/Q208S0 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Pomt1 ^@ http://purl.uniprot.org/uniprot/Q8R2R1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ Helical|||MIR 1|||MIR 2|||MIR 3|||N-linked (GlcNAc...) asparagine|||Protein O-mannosyl-transferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000121485 http://togogenome.org/gene/10090:Zbtb25 ^@ http://purl.uniprot.org/uniprot/G3UW50|||http://purl.uniprot.org/uniprot/Q6NV93 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cysltr2 ^@ http://purl.uniprot.org/uniprot/Q920A1 ^@ 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 ^@ Cysteinyl leukotriene 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_0000069304 http://togogenome.org/gene/10090:Chst8 ^@ http://purl.uniprot.org/uniprot/Q8BQ86 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 8|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000189654 http://togogenome.org/gene/10090:Anapc16 ^@ http://purl.uniprot.org/uniprot/Q9CPV2|||http://purl.uniprot.org/uniprot/S4R2B6 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Anaphase-promoting complex subunit 16|||Disordered|||N-acetylalanine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089817 http://togogenome.org/gene/10090:Plekhb2 ^@ http://purl.uniprot.org/uniprot/Q3UFC9|||http://purl.uniprot.org/uniprot/Q9QZC7 ^@ 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.|||In isoform 3.|||PH|||Pleckstrin homology domain-containing family B member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000053890|||http://purl.uniprot.org/annotation/VSP_009785|||http://purl.uniprot.org/annotation/VSP_009786 http://togogenome.org/gene/10090:Ints11 ^@ http://purl.uniprot.org/uniprot/Q9CWS4 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Motif|||Sequence Conflict ^@ HXHXDH motif|||Integrator complex subunit 11 ^@ http://purl.uniprot.org/annotation/PRO_0000259564 http://togogenome.org/gene/10090:Or51l14 ^@ http://purl.uniprot.org/uniprot/Q8VGZ8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp346 ^@ http://purl.uniprot.org/uniprot/Q9R0B7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Matrin-type 1|||Matrin-type 2|||Matrin-type 3|||Matrin-type 4|||N-acetylmethionine|||No loss of dsRNA binding capacity. Binding capacity was reduced 40-60%; when associated with A-203. Binding capacity was reduced to 5-10%; when associated with A-152 and A-203. Loss of binding capacity; when associated with A-152; A-203 and A-257.|||No loss of dsRNA binding capacity. Binding capacity was reduced 40-60%; when associated with A-91. Binding capacity was reduced to 5-10%; when associated with A-91 and A-152. Loss of binding capacity; when associated with A-91; A-152 and A-257.|||No loss of dsRNA binding capacity. Loss of 40-60% dsRNA binding; when associated with A-203. Binding capacity was reduced to 5-10%; when associated with A-91 and A-203. Loss of binding capacity; when associated with A-91; A-203 and A-257.|||No loss of dsRNA binding capacity. Loss of 5-10 % dsRNA binding capacity; when associated with A-152 and A-203. Loss of binding capacity; when associated with A-91; A-152 and A-203.|||Zinc finger protein 346 ^@ http://purl.uniprot.org/annotation/PRO_0000191810 http://togogenome.org/gene/10090:Ddx42 ^@ http://purl.uniprot.org/uniprot/Q810A7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ 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_0000280059|||http://purl.uniprot.org/annotation/VSP_023519 http://togogenome.org/gene/10090:Eif3h ^@ http://purl.uniprot.org/uniprot/Q5M9L0|||http://purl.uniprot.org/uniprot/Q91WK2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ 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_0000213962 http://togogenome.org/gene/10090:Plxnb1 ^@ http://purl.uniprot.org/uniprot/B2RWT9|||http://purl.uniprot.org/uniprot/Q8CJH3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||Important for interaction with RAC1 and RND1|||N-linked (GlcNAc...) asparagine|||Plexin-B1|||Pro residues|||Sema ^@ http://purl.uniprot.org/annotation/PRO_0000024672|||http://purl.uniprot.org/annotation/PRO_5002782180 http://togogenome.org/gene/10090:Lrfn5 ^@ http://purl.uniprot.org/uniprot/Q8BXA0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Ig-like|||In isoform 2.|||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_0000014846|||http://purl.uniprot.org/annotation/VSP_009299 http://togogenome.org/gene/10090:Bmal1 ^@ http://purl.uniprot.org/uniprot/Q3UHZ2|||http://purl.uniprot.org/uniprot/Q9WTL8 ^@ 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|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Abolishes sumoylation.|||BHLH|||Basic and acidic residues|||Basic helix-loop-helix ARNT-like protein 1|||Decreased acetylation, leading to decreased transcription elongation during the activation phase of the circadian cycle.|||Decreases without abolishing O-GlcNAcylation.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impaired nuclear accumulation, decreased interaction with CLOCK and disruption of circadian clock function.|||Important for interaction with CLOCK|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||Interaction with CIART|||Interaction with E-box DNA|||Loss of nuclear localization.|||N6-acetyllysine|||No effect on sumoylation.|||Nuclear export signal 1|||Nuclear export signal 2|||Nuclear localization signal|||PAC|||PAS|||PAS 1|||PAS 2|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by GSK3-beta|||Phosphothreonine; by GSK3-beta|||Polar residues|||Reduced CLOCK binding. Abolishes transcriptional activation by the CLOCK-BMAL1 heterodimer.|||Reduced CLOCK binding. Slightly reduced transcriptional activation by the CLOCK-BMAL1 heterodimer. Impairs regulation of circadian clock. Loss of ability to inhibit the expression of CD274 in macrophages.|||Significant decrease in; transcriptional activity, localization in PML body, ubiquitination and proteasome-mediated proteolysis.|||Significant reduction in nucleocytoplasmic shuttling; when associated with A-154.|||Significant reduction in nucleocytoplasmic shuttling; when associated with A-157.|||Significant reduction in nucleocytoplasmic shuttling; when associated with A-370.|||Significant reduction in nucleocytoplasmic shuttling; when associated with A-374.|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127158|||http://purl.uniprot.org/annotation/VSP_007992|||http://purl.uniprot.org/annotation/VSP_007993|||http://purl.uniprot.org/annotation/VSP_007994|||http://purl.uniprot.org/annotation/VSP_007995|||http://purl.uniprot.org/annotation/VSP_007996 http://togogenome.org/gene/10090:Nudt6 ^@ http://purl.uniprot.org/uniprot/A0A0R4J176|||http://purl.uniprot.org/uniprot/Q3ULU4|||http://purl.uniprot.org/uniprot/Q8CH40|||http://purl.uniprot.org/uniprot/Q8CH41 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Nucleoside diphosphate-linked moiety X motif 6|||Nudix hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000057108 http://togogenome.org/gene/10090:Eif6 ^@ http://purl.uniprot.org/uniprot/O55135|||http://purl.uniprot.org/uniprot/Q545K4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Modified Residue|||Mutagenesis Site ^@ Abolishes insulin-stimulated translation, abrogates tumorigenesis.|||Eukaryotic translation initiation factor 6|||Phosphoserine|||Phosphoserine; by CK1|||Phosphoserine; by PKC|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000153735 http://togogenome.org/gene/10090:Spidr ^@ http://purl.uniprot.org/uniprot/Q8BGX7 ^@ 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|||DNA repair-scaffolding protein|||Disordered|||In isoform 2.|||In isoform 3.|||Necessary for interaction with RAD51|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000251721|||http://purl.uniprot.org/annotation/VSP_020767|||http://purl.uniprot.org/annotation/VSP_020768|||http://purl.uniprot.org/annotation/VSP_020769 http://togogenome.org/gene/10090:Insyn2a ^@ http://purl.uniprot.org/uniprot/E9PZW7 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Inhbb ^@ http://purl.uniprot.org/uniprot/Q04999 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Inhibin beta B chain|||Interchain|||N-linked (GlcNAc...) asparagine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000033724|||http://purl.uniprot.org/annotation/PRO_0000033725 http://togogenome.org/gene/10090:Tm9sf5 ^@ http://purl.uniprot.org/uniprot/A2AFI6 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Adig ^@ http://purl.uniprot.org/uniprot/Q8R400 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Transmembrane ^@ Adipogenin|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000296376 http://togogenome.org/gene/10090:Brca2 ^@ http://purl.uniprot.org/uniprot/P97929 ^@ Chain|||Compositionally Biased Region|||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|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn ^@ BRCA2 1|||BRCA2 2|||BRCA2 3|||BRCA2 4|||BRCA2 5|||BRCA2 6|||BRCA2 7|||Basic and acidic residues|||Breast cancer type 2 susceptibility protein homolog|||Disordered|||In strain: 129/Sv.|||In strain: C57BL/6 and 129/Sv.|||In strain: C57BL/6.|||Interaction with FANCD2|||Interaction with HSF2BP|||Interaction with NPM1|||Interaction with PALB2|||Interaction with RAD51|||Interaction with SEM1|||Nuclear export signal; masked by interaction with SEM1|||Phosphoserine|||Phosphoserine; by CDK1 and CDK2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064985 http://togogenome.org/gene/10090:Wfdc15a ^@ http://purl.uniprot.org/uniprot/Q8BH89 ^@ 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 15A ^@ http://purl.uniprot.org/annotation/PRO_0000343831 http://togogenome.org/gene/10090:Acoxl ^@ http://purl.uniprot.org/uniprot/Q9DBS4 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Binding Site|||Chain|||Splice Variant ^@ Acyl-coenzyme A oxidase-like protein|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000305101|||http://purl.uniprot.org/annotation/VSP_028240 http://togogenome.org/gene/10090:Lamb1 ^@ http://purl.uniprot.org/uniprot/E9QN70|||http://purl.uniprot.org/uniprot/P02469|||http://purl.uniprot.org/uniprot/Q3UHL7 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000017066 http://togogenome.org/gene/10090:Gli2 ^@ http://purl.uniprot.org/uniprot/A5AA27|||http://purl.uniprot.org/uniprot/Q0VGT2|||http://purl.uniprot.org/uniprot/Q8BKI7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type 1|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||N6-acetyllysine; by EP300|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphothreonine|||Polar residues|||Zinc finger protein GLI2 ^@ http://purl.uniprot.org/annotation/PRO_0000406215 http://togogenome.org/gene/10090:Rbbp8 ^@ http://purl.uniprot.org/uniprot/Q80YR6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region ^@ DNA endonuclease RBBP8|||Damage-recruitment motif|||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|||KLHL15-binding|||PXDLS motif|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues|||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_0000417036 http://togogenome.org/gene/10090:Cers2 ^@ http://purl.uniprot.org/uniprot/Q924Z4 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Ceramide synthase 2|||Cytoplasmic|||Disordered|||Helical|||Homeobox-like|||Last loop motif|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||TLC ^@ http://purl.uniprot.org/annotation/PRO_0000185510 http://togogenome.org/gene/10090:Slc45a2 ^@ http://purl.uniprot.org/uniprot/P58355|||http://purl.uniprot.org/uniprot/Q541S3 ^@ 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|||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 UW-dbr.|||Membrane-associated transporter protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000122518 http://togogenome.org/gene/10090:Gprasp2 ^@ http://purl.uniprot.org/uniprot/Q8BUY8 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||G-protein coupled receptor-associated sorting protein 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000239054 http://togogenome.org/gene/10090:Adam6a ^@ http://purl.uniprot.org/uniprot/B2RSY5 ^@ Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Disulfide Bond|||Domain Extent|||Transmembrane ^@ Disintegrin|||EGF-like|||Helical|||Peptidase M12B ^@ http://togogenome.org/gene/10090:Vmn1r193 ^@ http://purl.uniprot.org/uniprot/Q8R258 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Spib ^@ http://purl.uniprot.org/uniprot/O35906 ^@ Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||DNA Binding|||Region|||Splice Variant ^@ ETS|||In isoform IC.|||In isoform IIA.|||TAD1 (Acidic)|||TAD2|||Transcription factor Spi-B ^@ http://purl.uniprot.org/annotation/PRO_0000204137|||http://purl.uniprot.org/annotation/VSP_013907|||http://purl.uniprot.org/annotation/VSP_013908 http://togogenome.org/gene/10090:Lpxn ^@ http://purl.uniprot.org/uniprot/Q99N69 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Disordered|||LD motif 1|||LD motif 2|||LD motif 3|||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_0000075837 http://togogenome.org/gene/10090:Gm13271 ^@ http://purl.uniprot.org/uniprot/B1AYH9 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015087040 http://togogenome.org/gene/10090:Scyl3 ^@ http://purl.uniprot.org/uniprot/Q9DBQ7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||In isoform 2.|||In isoform 3.|||Interaction with EZR|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Protein kinase|||Protein-associating with the carboxyl-terminal domain of ezrin|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000058168|||http://purl.uniprot.org/annotation/VSP_013126|||http://purl.uniprot.org/annotation/VSP_027369|||http://purl.uniprot.org/annotation/VSP_037985 http://togogenome.org/gene/10090:Rrp8 ^@ http://purl.uniprot.org/uniprot/E9PVA2|||http://purl.uniprot.org/uniprot/Q9DB85 ^@ 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 residues|||Disordered|||Phosphoserine|||Polar residues|||Ribosomal RNA-processing protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000084091 http://togogenome.org/gene/10090:Copz2 ^@ http://purl.uniprot.org/uniprot/Q9JHH9 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Coatomer subunit zeta-2|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000193832 http://togogenome.org/gene/10090:Gpr141 ^@ http://purl.uniprot.org/uniprot/Q7TQP0 ^@ 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 141 ^@ http://purl.uniprot.org/annotation/PRO_0000069619 http://togogenome.org/gene/10090:Spink4 ^@ http://purl.uniprot.org/uniprot/O35679 ^@ 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 4 ^@ http://purl.uniprot.org/annotation/PRO_0000016570 http://togogenome.org/gene/10090:Depdc1a ^@ http://purl.uniprot.org/uniprot/D3Z6J1|||http://purl.uniprot.org/uniprot/Q8CIG0 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ DEP|||DEP domain-containing protein 1A|||In isoform 2.|||Interaction with ZNF224|||Phosphoserine|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000284787|||http://purl.uniprot.org/annotation/VSP_024656|||http://purl.uniprot.org/annotation/VSP_024657|||http://purl.uniprot.org/annotation/VSP_024658 http://togogenome.org/gene/10090:Far1 ^@ http://purl.uniprot.org/uniprot/Q922J9 ^@ 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|||Fatty acyl-CoA reductase 1|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Necessary and sufficient for PEX19-mediated localization into peroxisome membrane|||Peroxisomal ^@ http://purl.uniprot.org/annotation/PRO_0000261395|||http://purl.uniprot.org/annotation/VSP_021678|||http://purl.uniprot.org/annotation/VSP_021679|||http://purl.uniprot.org/annotation/VSP_021680|||http://purl.uniprot.org/annotation/VSP_021681 http://togogenome.org/gene/10090:Gpn1 ^@ http://purl.uniprot.org/uniprot/Q4VAB2|||http://purl.uniprot.org/uniprot/Q8VCE2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Site ^@ AAA+ ATPase|||Basic and acidic residues|||Disordered|||GPN-loop GTPase 1|||Gly-Pro-Asn (GPN)-loop; involved in dimer interface|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||Stabilizes the phosphate intermediate; shared with dimeric partner ^@ http://purl.uniprot.org/annotation/PRO_0000066002 http://togogenome.org/gene/10090:Plppr5 ^@ http://purl.uniprot.org/uniprot/Q8BJ52 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Phospholipid phosphatase-related protein type 5 ^@ http://purl.uniprot.org/annotation/PRO_0000321934|||http://purl.uniprot.org/annotation/VSP_031829 http://togogenome.org/gene/10090:Hspb8 ^@ http://purl.uniprot.org/uniprot/Q9JK92 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Asymmetric dimethylarginine|||Disordered|||Heat shock protein beta-8|||Phosphoserine|||Phosphothreonine|||sHSP ^@ http://purl.uniprot.org/annotation/PRO_0000125947 http://togogenome.org/gene/10090:Map6 ^@ http://purl.uniprot.org/uniprot/Q7TSJ2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 4 X approximate tandem repeat Mc|||Basic and acidic residues|||Calmodulin-binding|||Disordered|||In isoform 2.|||In isoform 3.|||Mc-1|||Mc-2|||Mc-3|||Mc-4|||Microtubule-associated protein 6|||Mn 1|||Mn 2|||Mn 3|||Phosphoserine|||Phosphotyrosine|||Pro residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000344045|||http://purl.uniprot.org/annotation/VSP_034724|||http://purl.uniprot.org/annotation/VSP_034725|||http://purl.uniprot.org/annotation/VSP_034726|||http://purl.uniprot.org/annotation/VSP_034727 http://togogenome.org/gene/10090:Nme5 ^@ http://purl.uniprot.org/uniprot/Q3V2L8|||http://purl.uniprot.org/uniprot/Q99MH5 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Nucleoside diphosphate kinase homolog 5|||Nucleoside diphosphate kinase-like|||Pros-phosphohistidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000137126|||http://purl.uniprot.org/annotation/VSP_007773|||http://purl.uniprot.org/annotation/VSP_007774 http://togogenome.org/gene/10090:Or52k2 ^@ http://purl.uniprot.org/uniprot/E9Q545 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:1700014D04Rik ^@ http://purl.uniprot.org/uniprot/J3QMS2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||SPATA31 ^@ http://togogenome.org/gene/10090:Ecscr ^@ http://purl.uniprot.org/uniprot/Q3TZW0 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Endothelial cell-specific chemotaxis regulator|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000365018|||http://purl.uniprot.org/annotation/VSP_036454|||http://purl.uniprot.org/annotation/VSP_053880 http://togogenome.org/gene/10090:Map2k3 ^@ http://purl.uniprot.org/uniprot/O09110|||http://purl.uniprot.org/uniprot/Q5SWN9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Dual specificity mitogen-activated protein kinase kinase 3|||In isoform 1.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086379|||http://purl.uniprot.org/annotation/VSP_004879 http://togogenome.org/gene/10090:Bcas1 ^@ http://purl.uniprot.org/uniprot/E9Q8Q5|||http://purl.uniprot.org/uniprot/Q80YN3 ^@ 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|||Breast carcinoma-amplified sequence 1 homolog|||Disordered|||Interacts with DYNLL1 AND DYNLL2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000235984 http://togogenome.org/gene/10090:Sprr2h ^@ http://purl.uniprot.org/uniprot/O70559 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1|||2|||3|||4|||5|||6|||7|||7 X 9 AA tandem repeats of P-[KQ]-C-[PT]-E-P-C-P-P|||Disordered|||Small proline-rich protein 2H ^@ http://purl.uniprot.org/annotation/PRO_0000150020 http://togogenome.org/gene/10090:Nfic ^@ http://purl.uniprot.org/uniprot/P70255|||http://purl.uniprot.org/uniprot/Q3UHA6 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant ^@ 9aaTAD|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||CTF/NF-I|||Disordered|||In isoform 2.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||N-acetylmethionine|||Nuclear factor 1 C-type|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000100200|||http://purl.uniprot.org/annotation/VSP_003557|||http://purl.uniprot.org/annotation/VSP_007556|||http://purl.uniprot.org/annotation/VSP_007557|||http://purl.uniprot.org/annotation/VSP_007558|||http://purl.uniprot.org/annotation/VSP_007559 http://togogenome.org/gene/10090:Ndrg1 ^@ http://purl.uniprot.org/uniprot/Q545R3|||http://purl.uniprot.org/uniprot/Q62433 ^@ 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 ^@ 1|||2|||3|||3 X 10 AA tandem repeats of G-[PST]-R-S-R-S-H-T-S-E|||Basic and acidic residues|||Disordered|||N-acetylserine|||Phosphoserine|||Phosphoserine; by SGK1|||Phosphothreonine|||Phosphothreonine; by SGK1|||Polar residues|||Protein NDRG1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000159574 http://togogenome.org/gene/10090:Tbc1d1 ^@ http://purl.uniprot.org/uniprot/E9Q6L4|||http://purl.uniprot.org/uniprot/Q3U3T9|||http://purl.uniprot.org/uniprot/Q60949 ^@ 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.|||PID|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by PKB/AKT1|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1|||Phosphotyrosine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000208023|||http://purl.uniprot.org/annotation/VSP_008473 http://togogenome.org/gene/10090:Krt16 ^@ http://purl.uniprot.org/uniprot/Q3SYP5|||http://purl.uniprot.org/uniprot/Q3ZAW8|||http://purl.uniprot.org/uniprot/Q9Z2K1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent|||Region ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type I cytoskeletal 16|||Linker 1|||Linker 12|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063663 http://togogenome.org/gene/10090:Ubl4a ^@ http://purl.uniprot.org/uniprot/P21126|||http://purl.uniprot.org/uniprot/Q3UK94 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Required and sufficient for interaction with BAG6|||Ubiquitin-like|||Ubiquitin-like protein 4A ^@ http://purl.uniprot.org/annotation/PRO_0000114865 http://togogenome.org/gene/10090:Nanos3 ^@ http://purl.uniprot.org/uniprot/P60324 ^@ Binding Site|||Chain|||Molecule Processing|||Motif|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Motif|||Region|||Site|||Zinc Finger ^@ C2HC 1|||C2HC 2|||Disordered|||Involved in RNA binding|||Nanos homolog 3|||Nanos-type ^@ http://purl.uniprot.org/annotation/PRO_0000207690 http://togogenome.org/gene/10090:Hba-a2 ^@ http://purl.uniprot.org/uniprot/Q91VB8 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Globin family profile|||distal binding residue|||proximal binding residue ^@ http://togogenome.org/gene/10090:Ky ^@ http://purl.uniprot.org/uniprot/F8VQF8 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Transglutaminase-like ^@ http://togogenome.org/gene/10090:Adra2b ^@ http://purl.uniprot.org/uniprot/P30545|||http://purl.uniprot.org/uniprot/Q925K6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Alpha-2B adrenergic receptor|||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|||Implicated in catechol agonist binding|||Implicated in ligand binding|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069096 http://togogenome.org/gene/10090:Smdt1 ^@ http://purl.uniprot.org/uniprot/Q9DB10 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Motif|||Mutagenesis Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Abolishes calcium uptake into mitochondria. Abolishes interaction with MCU.|||Essential MCU regulator, mitochondrial|||GXXXX[G/A/S]|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000296321 http://togogenome.org/gene/10090:Drg2 ^@ http://purl.uniprot.org/uniprot/Q9QXB9 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ (3S)-3-hydroxylysine|||Developmentally-regulated GTP-binding protein 2|||OBG-type G|||TGS ^@ http://purl.uniprot.org/annotation/PRO_0000205428 http://togogenome.org/gene/10090:Gm5771 ^@ http://purl.uniprot.org/uniprot/Q792Y9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015098649 http://togogenome.org/gene/10090:Scara5 ^@ http://purl.uniprot.org/uniprot/Q8K299 ^@ 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|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||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.|||N-linked (GlcNAc...) asparagine|||SRCR|||Scavenger receptor class A member 5 ^@ http://purl.uniprot.org/annotation/PRO_0000279519|||http://purl.uniprot.org/annotation/VSP_023476|||http://purl.uniprot.org/annotation/VSP_023477|||http://purl.uniprot.org/annotation/VSP_023478 http://togogenome.org/gene/10090:Or13g1 ^@ http://purl.uniprot.org/uniprot/Q7TS01 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Frey1 ^@ http://purl.uniprot.org/uniprot/Q8CF31 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||Protein Frey ^@ http://purl.uniprot.org/annotation/PRO_0000394236 http://togogenome.org/gene/10090:Zcchc13 ^@ http://purl.uniprot.org/uniprot/Q9D548 ^@ Domain Extent|||Region ^@ Domain Extent ^@ CCHC-type ^@ http://togogenome.org/gene/10090:Cyp2a12 ^@ http://purl.uniprot.org/uniprot/P56593 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict ^@ Cytochrome P450 2A12|||Same as wild-type.|||Stabilizes the protein, 17-fold lower Vmax.|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051675 http://togogenome.org/gene/10090:Asb3 ^@ http://purl.uniprot.org/uniprot/Q9WV72 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 10|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and SOCS box protein 3|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066927 http://togogenome.org/gene/10090:Slfnl1 ^@ http://purl.uniprot.org/uniprot/Q8BHW9 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Polar residues|||Pro residues|||Schlafen-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000283000|||http://purl.uniprot.org/annotation/VSP_024279 http://togogenome.org/gene/10090:Pisd ^@ http://purl.uniprot.org/uniprot/E9PX91|||http://purl.uniprot.org/uniprot/Q505E1|||http://purl.uniprot.org/uniprot/Q8BSF4 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Charge relay system; for autoendoproteolytic cleavage activity|||Cleavage (non-hydrolytic); by autocatalysis|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||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_0000029837|||http://purl.uniprot.org/annotation/PRO_0000029838|||http://purl.uniprot.org/annotation/PRO_0000435572|||http://purl.uniprot.org/annotation/PRO_5023416554|||http://purl.uniprot.org/annotation/PRO_5023416555|||http://purl.uniprot.org/annotation/PRO_5034791803|||http://purl.uniprot.org/annotation/PRO_5034791804 http://togogenome.org/gene/10090:Krtap5-1 ^@ http://purl.uniprot.org/uniprot/Q64507 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 1|||10|||11|||12|||13|||14|||14 X 4 AA repeats of C-C-X-P|||2|||3|||4|||5|||6|||7|||8|||9|||In isoform 2.|||Keratin-associated protein 5-1 ^@ http://purl.uniprot.org/annotation/PRO_0000361657|||http://purl.uniprot.org/annotation/VSP_052994 http://togogenome.org/gene/10090:Ppef2 ^@ http://purl.uniprot.org/uniprot/O35385 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Catalytic|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||IQ|||Proton donor|||Serine/threonine-protein phosphatase with EF-hands 2 ^@ http://purl.uniprot.org/annotation/PRO_0000058902 http://togogenome.org/gene/10090:Or5b112 ^@ http://purl.uniprot.org/uniprot/Q8VFW4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Utp18 ^@ http://purl.uniprot.org/uniprot/Q3U3Q3|||http://purl.uniprot.org/uniprot/Q5SSI6|||http://purl.uniprot.org/uniprot/Q8BHW1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Non-terminal Residue|||Region|||Repeat ^@ 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 18 homolog|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000051406 http://togogenome.org/gene/10090:Smug1 ^@ http://purl.uniprot.org/uniprot/Q6P5C5 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Region|||Sequence Conflict ^@ DNA-binding|||Single-strand selective monofunctional uracil DNA glycosylase ^@ http://purl.uniprot.org/annotation/PRO_0000071993 http://togogenome.org/gene/10090:Pla2g2d ^@ http://purl.uniprot.org/uniprot/Q3TYT9|||http://purl.uniprot.org/uniprot/Q9WVF6 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Signal Peptide|||Splice Variant ^@ Group IID secretory phospholipase A2|||Has no effect on Treg effector functions.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phospholipase A2 ^@ http://purl.uniprot.org/annotation/PRO_0000022756|||http://purl.uniprot.org/annotation/PRO_5014205824|||http://purl.uniprot.org/annotation/VSP_004508 http://togogenome.org/gene/10090:Eprs ^@ http://purl.uniprot.org/uniprot/Q8CGC7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 'HIGH' region|||'KMSKS' region|||3 X 57 AA approximate repeats|||Basic and acidic residues|||Bifunctional glutamate/proline--tRNA ligase|||Constitutively active in translation inhibition (phosphomimetic). Mutant mice have no apparent developmental defect and do not display overt phenotype related to adiposity or lifespan.|||Disordered|||Glutamate--tRNA ligase|||Loss of function in translation inhibition. Loss of interaction with SLC27A1. Mutant mice have no apparent developmental defect but display reduced adiposity associated with decreased insulin levels and adipocytes size. They also display increased lipolysis and fatty acid beta-oxidation and an extended lifespan. Adipocytes display decreased insulin-stimulated long-chain fatty acid uptake.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||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_0000119744 http://togogenome.org/gene/10090:Dusp10 ^@ http://purl.uniprot.org/uniprot/Q9ESS0 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Dual specificity protein phosphatase 10|||Interaction with MAP kinases|||Phosphocysteine intermediate|||Rhodanese|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094814 http://togogenome.org/gene/10090:Lzts1 ^@ http://purl.uniprot.org/uniprot/P60853 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Leucine zipper putative tumor suppressor 1|||N-myristoyl glycine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000182972 http://togogenome.org/gene/10090:Ufd1 ^@ http://purl.uniprot.org/uniprot/P70362 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylmethionine|||Phosphoserine|||Ubiquitin recognition factor in ER-associated degradation protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000194985 http://togogenome.org/gene/10090:Mrps17 ^@ http://purl.uniprot.org/uniprot/Q9CQE3 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||Small ribosomal subunit protein uS17m ^@ http://purl.uniprot.org/annotation/PRO_0000030624 http://togogenome.org/gene/10090:Pdlim1 ^@ http://purl.uniprot.org/uniprot/O70400 ^@ 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|||Region|||Sequence Conflict ^@ Disordered|||LIM zinc-binding|||N-acetylthreonine|||PDZ|||PDZ and LIM domain protein 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000075860 http://togogenome.org/gene/10090:Or4p18 ^@ http://purl.uniprot.org/uniprot/A2AUS6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Becn2 ^@ http://purl.uniprot.org/uniprot/P0DM65 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Beclin-2|||Required for homodimer formation ^@ http://purl.uniprot.org/annotation/PRO_0000424159 http://togogenome.org/gene/10090:Thoc7 ^@ http://purl.uniprot.org/uniprot/Q7TMY4 ^@ 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|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||Interaction with NIF3L1|||Interaction with THOC5|||N-acetylglycine|||N6-acetyllysine|||Phosphothreonine|||Removed|||THO complex subunit 7 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000310755|||http://purl.uniprot.org/annotation/VSP_029326 http://togogenome.org/gene/10090:Rab3c ^@ http://purl.uniprot.org/uniprot/P62823|||http://purl.uniprot.org/uniprot/Q542T7 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Region ^@ Cysteine methyl ester|||Disordered|||Effector region|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-3C|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121086 http://togogenome.org/gene/10090:Mup9 ^@ http://purl.uniprot.org/uniprot/A2CGB6|||http://purl.uniprot.org/uniprot/A9C496|||http://purl.uniprot.org/uniprot/P02762 ^@ 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 ^@ Lipocalin/cytosolic fatty-acid binding|||Major urinary protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000017932|||http://purl.uniprot.org/annotation/PRO_5002736258|||http://purl.uniprot.org/annotation/PRO_5014296800 http://togogenome.org/gene/10090:2410002F23Rik ^@ http://purl.uniprot.org/uniprot/Q3TE80|||http://purl.uniprot.org/uniprot/Q9CWW9 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Sptssa ^@ http://purl.uniprot.org/uniprot/Q8R207 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000089950 http://togogenome.org/gene/10090:Stmnd1 ^@ http://purl.uniprot.org/uniprot/Q6P3A1 ^@ 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_0000421694 http://togogenome.org/gene/10090:Mlana ^@ http://purl.uniprot.org/uniprot/Q2TA50 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Txk ^@ http://purl.uniprot.org/uniprot/A0A0G2JG94|||http://purl.uniprot.org/uniprot/B2RQ20|||http://purl.uniprot.org/uniprot/P42682 ^@ 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|||Splice Variant ^@ Disordered|||In isoform 2.|||Phosphotyrosine; by FYN and autocatalysis|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduces palmitoylation and leads to nuclear localization.|||SH2|||SH3|||Tyrosine-protein kinase TXK ^@ http://purl.uniprot.org/annotation/PRO_0000088176|||http://purl.uniprot.org/annotation/VSP_041923 http://togogenome.org/gene/10090:Cdkn2c ^@ http://purl.uniprot.org/uniprot/Q60772|||http://purl.uniprot.org/uniprot/Q9D153 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Cyclin-dependent kinase 4 inhibitor C ^@ http://purl.uniprot.org/annotation/PRO_0000144187 http://togogenome.org/gene/10090:Resp18 ^@ http://purl.uniprot.org/uniprot/P47939|||http://purl.uniprot.org/uniprot/Q8BT93 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Polar residues|||RESP18|||RESP18 domain-containing protein|||Regulated endocrine-specific protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000022219|||http://purl.uniprot.org/annotation/PRO_5004303775 http://togogenome.org/gene/10090:Gypc ^@ http://purl.uniprot.org/uniprot/G3UXY6|||http://purl.uniprot.org/uniprot/Q78HU7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Glycophorin-C|||Helical|||Helical; Signal-anchor for type III membrane protein|||Neurexin/syndecan/glycophorin C|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000378454 http://togogenome.org/gene/10090:Ints8 ^@ http://purl.uniprot.org/uniprot/Q80V86 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ Integrator complex subunit 8|||Phosphothreonine|||TPR 1|||TPR 2|||TPR 3|||TPR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000259554 http://togogenome.org/gene/10090:Fam47e ^@ http://purl.uniprot.org/uniprot/B2RVF4|||http://purl.uniprot.org/uniprot/E9PYM1|||http://purl.uniprot.org/uniprot/E9Q0Z5|||http://purl.uniprot.org/uniprot/Q3UN37 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Ppp1r18 ^@ http://purl.uniprot.org/uniprot/Q8BQ30 ^@ 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.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phostensin|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000050809|||http://purl.uniprot.org/annotation/VSP_014260 http://togogenome.org/gene/10090:Or10am5 ^@ http://purl.uniprot.org/uniprot/Q7TQV1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Setd2 ^@ http://purl.uniprot.org/uniprot/E9Q5F9 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ AWS|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase SETD2|||In isoform 2.|||Interaction with POLR2A|||Interaction with TUBA1A|||Low charge region|||Phosphoserine|||Phosphothreonine|||Polar residues|||Post-SET|||Pro residues|||SET|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000423553|||http://purl.uniprot.org/annotation/VSP_047946 http://togogenome.org/gene/10090:Or6b2 ^@ http://purl.uniprot.org/uniprot/Q8VGU4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp868 ^@ http://purl.uniprot.org/uniprot/Q3UTQ6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Otud3 ^@ http://purl.uniprot.org/uniprot/B1AZ99 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Cys-loop|||Disordered|||His-loop|||N6-acetyllysine|||Nucleophile|||OTU|||OTU domain-containing protein 3|||UBA-like|||Variable-loop ^@ http://purl.uniprot.org/annotation/PRO_0000424025 http://togogenome.org/gene/10090:Psmd14 ^@ http://purl.uniprot.org/uniprot/O35593 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict ^@ 26S proteasome non-ATPase regulatory subunit 14|||JAMM motif|||MPN|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000213953 http://togogenome.org/gene/10090:Htr2a ^@ http://purl.uniprot.org/uniprot/P35363|||http://purl.uniprot.org/uniprot/Q543D4 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Site|||Topological Domain|||Transmembrane ^@ 5-hydroxytryptamine receptor 2A|||Cytoplasmic|||DRY motif; important for ligand-induced conformation changes|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||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|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling|||PDZ-binding|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000068948 http://togogenome.org/gene/10090:Kank3 ^@ http://purl.uniprot.org/uniprot/Q9Z1P7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Turn ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||KN motif and ankyrin repeat domain-containing protein 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000244583 http://togogenome.org/gene/10090:Phf11d ^@ http://purl.uniprot.org/uniprot/A6H5X4|||http://purl.uniprot.org/uniprot/B4XVQ0 ^@ 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 ^@ Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||In isoform 2.|||In isoform 3.|||PHD finger protein 11|||PHD-type ^@ http://purl.uniprot.org/annotation/PRO_0000385015|||http://purl.uniprot.org/annotation/VSP_038089|||http://purl.uniprot.org/annotation/VSP_038090 http://togogenome.org/gene/10090:Thyn1 ^@ http://purl.uniprot.org/uniprot/Q8BJZ7|||http://purl.uniprot.org/uniprot/Q91YJ3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Basic and acidic residues|||Disordered|||EVE|||Nuclear localization signal|||Thymocyte nuclear protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000262565 http://togogenome.org/gene/10090:Lrrc26 ^@ http://purl.uniprot.org/uniprot/Q91W20 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 26 ^@ http://purl.uniprot.org/annotation/PRO_0000309361 http://togogenome.org/gene/10090:Rfc3 ^@ http://purl.uniprot.org/uniprot/Q3TKD1|||http://purl.uniprot.org/uniprot/Q8R323 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ AAA+ ATPase|||N6-acetyllysine|||Phosphoserine|||Replication factor C subunit 3 ^@ http://purl.uniprot.org/annotation/PRO_0000121762 http://togogenome.org/gene/10090:Pyroxd2 ^@ http://purl.uniprot.org/uniprot/Q3U4I7 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000244072 http://togogenome.org/gene/10090:Akt1 ^@ http://purl.uniprot.org/uniprot/P31750 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ AGC-kinase C-terminal|||Abolishes caspase-3 cleavage and increases cell survival. Does not affect kinase activity.|||Cleavage; by caspase-3|||Disordered|||Does not affect caspase-3 cleavage.|||Does not affect ubiquitination by ZNRF1.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In kinase dead mutant; lacks kinase activity. Overexpression inhibits insulin-stimulated translocation of SLC2A4/GLUT4 in a dominant negative manner.|||N6-acetyllysine|||O-linked (GlcNAc) serine; alternate|||O-linked (GlcNAc) threonine|||PH|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by IKKE, MTOR, PRKDC and TBK1; alternate|||Phosphothreonine|||Phosphothreonine; by IKKE, PDPK1 and TBK1|||Phosphothreonine; by MTOR|||Phosphotyrosine|||Phosphotyrosine; by TNK2|||Protein kinase|||Proton acceptor|||RAC-alpha serine/threonine-protein kinase|||Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. ^@ http://purl.uniprot.org/annotation/PRO_0000085606 http://togogenome.org/gene/10090:Spatc1l ^@ http://purl.uniprot.org/uniprot/Q9D9W0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Phosphoserine|||Speriolin-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000079520 http://togogenome.org/gene/10090:Cd209f ^@ http://purl.uniprot.org/uniprot/G3UVT9|||http://purl.uniprot.org/uniprot/Q4KL16 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||C-type lectin|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Rbm15b ^@ http://purl.uniprot.org/uniprot/Q6PHZ5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Strand ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000081779 http://togogenome.org/gene/10090:Coq10b ^@ http://purl.uniprot.org/uniprot/A0A0R4J066|||http://purl.uniprot.org/uniprot/G5E8J7|||http://purl.uniprot.org/uniprot/Q3THF9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Domain Extent|||Sequence Conflict|||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_0000228648|||http://purl.uniprot.org/annotation/VSP_017686 http://togogenome.org/gene/10090:Nfia ^@ http://purl.uniprot.org/uniprot/B1AUC0|||http://purl.uniprot.org/uniprot/Q02780|||http://purl.uniprot.org/uniprot/Q05B39|||http://purl.uniprot.org/uniprot/Q3UTK6 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant ^@ 9aaTAD|||Asymmetric dimethylarginine|||CTF/NF-I|||Disordered|||In isoform 1, isoform 5 and isoform 7.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Nuclear factor 1 A-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000100192|||http://purl.uniprot.org/annotation/VSP_003537|||http://purl.uniprot.org/annotation/VSP_003538|||http://purl.uniprot.org/annotation/VSP_003539|||http://purl.uniprot.org/annotation/VSP_003540|||http://purl.uniprot.org/annotation/VSP_003541|||http://purl.uniprot.org/annotation/VSP_003542|||http://purl.uniprot.org/annotation/VSP_003543|||http://purl.uniprot.org/annotation/VSP_003544 http://togogenome.org/gene/10090:Tchp ^@ http://purl.uniprot.org/uniprot/Q3TVW5 ^@ 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|||Disordered|||In isoform 2.|||Interaction with keratin proteins|||Trichohyalin/plectin homology domain|||Trichoplein keratin filament-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000292610|||http://purl.uniprot.org/annotation/VSP_052475 http://togogenome.org/gene/10090:Ppp1r10 ^@ http://purl.uniprot.org/uniprot/Q80W00 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C3H1-type|||Disordered|||Essential for PPP1CA inhibition|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with TOX4|||Interaction with WDR82|||Loss of interaction with PPP1CA but no effect on interaction with TOX4 or WDR82. Cell cycle arrest at mitosis and cell death. Exhibits normal association with chromosomes but shows defects in the process of chromosome decondensation at late telophase.|||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_0000071512|||http://purl.uniprot.org/annotation/VSP_013155 http://togogenome.org/gene/10090:Ftsj3 ^@ http://purl.uniprot.org/uniprot/Q9DBE9 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Proton acceptor|||pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3 ^@ http://purl.uniprot.org/annotation/PRO_0000155578 http://togogenome.org/gene/10090:Med15 ^@ http://purl.uniprot.org/uniprot/A0A338P730|||http://purl.uniprot.org/uniprot/E9Q7C1|||http://purl.uniprot.org/uniprot/Q3TE00|||http://purl.uniprot.org/uniprot/Q6KAM1|||http://purl.uniprot.org/uniprot/Q924H2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Disordered|||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_0000058265 http://togogenome.org/gene/10090:Or5w13 ^@ http://purl.uniprot.org/uniprot/Q0VBI4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vip ^@ http://purl.uniprot.org/uniprot/A0A0R4J003|||http://purl.uniprot.org/uniprot/P32648 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Asparagine amide|||Glucagon / GIP / secretin / VIP family|||Intestinal peptide PHI-27|||Intestinal peptide PHI-42|||Isoleucine amide|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Vasoactive intestinal peptide ^@ http://purl.uniprot.org/annotation/PRO_0000011462|||http://purl.uniprot.org/annotation/PRO_0000011463|||http://purl.uniprot.org/annotation/PRO_0000011464|||http://purl.uniprot.org/annotation/PRO_0000011465|||http://purl.uniprot.org/annotation/PRO_0000011466|||http://purl.uniprot.org/annotation/PRO_5006451935 http://togogenome.org/gene/10090:4933430I17Rik ^@ http://purl.uniprot.org/uniprot/F6UZS4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered ^@ http://togogenome.org/gene/10090:Sez6l2 ^@ http://purl.uniprot.org/uniprot/Q4V9Z5 ^@ 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 ^@ CUB 1|||CUB 2|||CUB 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Seizure 6-like protein 2|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5 ^@ http://purl.uniprot.org/annotation/PRO_0000333889|||http://purl.uniprot.org/annotation/VSP_033598|||http://purl.uniprot.org/annotation/VSP_033599 http://togogenome.org/gene/10090:Gpr149 ^@ http://purl.uniprot.org/uniprot/Q3UVY1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||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|||Probable G-protein coupled receptor 149 ^@ http://purl.uniprot.org/annotation/PRO_0000069627 http://togogenome.org/gene/10090:Aadacl2fm1 ^@ http://purl.uniprot.org/uniprot/Q8BUY2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Alpha/beta hydrolase fold-3 ^@ http://togogenome.org/gene/10090:Ovol3 ^@ http://purl.uniprot.org/uniprot/D3YYM0 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Region|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Putative transcription factor ovo-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000415414 http://togogenome.org/gene/10090:Cacna1g ^@ http://purl.uniprot.org/uniprot/E9PWL1|||http://purl.uniprot.org/uniprot/Q27YN9|||http://purl.uniprot.org/uniprot/Q5SUF5|||http://purl.uniprot.org/uniprot/Q5SUF6|||http://purl.uniprot.org/uniprot/Q5SUF7|||http://purl.uniprot.org/uniprot/Q5SUF8|||http://purl.uniprot.org/uniprot/Q5SUF9|||http://purl.uniprot.org/uniprot/Q5SUG0|||http://purl.uniprot.org/uniprot/Q5SUG1|||http://purl.uniprot.org/uniprot/Q5SUG3|||http://purl.uniprot.org/uniprot/Q5SUG4|||http://purl.uniprot.org/uniprot/Q6PFV8|||http://purl.uniprot.org/uniprot/Q6ZPX4|||http://purl.uniprot.org/uniprot/Q9WUT2 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Site|||Transmembrane ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Ion transport|||Polar residues ^@ http://togogenome.org/gene/10090:Retreg2 ^@ http://purl.uniprot.org/uniprot/Q6NS82 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Abolishes interaction with ATG8 family proteins. Does not affect collagen degradation.|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||LIR motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reticulophagy regulator 2 ^@ http://purl.uniprot.org/annotation/PRO_0000089347|||http://purl.uniprot.org/annotation/VSP_014550|||http://purl.uniprot.org/annotation/VSP_014551 http://togogenome.org/gene/10090:Lypd3 ^@ http://purl.uniprot.org/uniprot/Q91YK8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||GPI-anchor amidated serine|||Ly6/PLAUR domain-containing protein 3|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form|||UPAR/Ly6 1|||UPAR/Ly6 2 ^@ http://purl.uniprot.org/annotation/PRO_0000226753|||http://purl.uniprot.org/annotation/PRO_0000226754 http://togogenome.org/gene/10090:Arrdc5 ^@ http://purl.uniprot.org/uniprot/Q497K5 ^@ Chain|||Molecule Processing ^@ Chain ^@ Arrestin domain-containing protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000244357 http://togogenome.org/gene/10090:Zcchc9 ^@ http://purl.uniprot.org/uniprot/Q8R1J3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger ^@ CCHC-type 1|||CCHC-type 2|||CCHC-type 3|||CCHC-type 4|||Disordered|||Polar residues|||Zinc finger CCHC domain-containing protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000150966 http://togogenome.org/gene/10090:Zfp383 ^@ http://purl.uniprot.org/uniprot/A0A087WRR7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ddx60 ^@ http://purl.uniprot.org/uniprot/G3X9F7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Helicase ATP-binding|||Helicase C-terminal ^@ http://togogenome.org/gene/10090:Apod ^@ http://purl.uniprot.org/uniprot/P51910 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Signal Peptide ^@ Apolipoprotein D|||In strain: Swiss Webster.|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000017874 http://togogenome.org/gene/10090:Kncn ^@ http://purl.uniprot.org/uniprot/B7ZNQ4|||http://purl.uniprot.org/uniprot/Q307W7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Kinocilin|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000311266 http://togogenome.org/gene/10090:Myl4 ^@ http://purl.uniprot.org/uniprot/Q9CZ19 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||EF-hand ^@ http://togogenome.org/gene/10090:Stxbp5 ^@ http://purl.uniprot.org/uniprot/D3Z079 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Pro residues|||V-SNARE coiled-coil homology|||WD ^@ http://togogenome.org/gene/10090:Prrt4 ^@ http://purl.uniprot.org/uniprot/B2RU40 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Polar residues|||Proline-rich transmembrane protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000394499 http://togogenome.org/gene/10090:Stpg2 ^@ http://purl.uniprot.org/uniprot/Q8C8J0 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ Disordered|||STPGR 1|||STPGR 10|||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_0000311961 http://togogenome.org/gene/10090:Med6 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZX3|||http://purl.uniprot.org/uniprot/Q921D4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Mediator of RNA polymerase II transcription subunit 6|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000303042 http://togogenome.org/gene/10090:Or9m1b ^@ http://purl.uniprot.org/uniprot/A2AVT0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tab3 ^@ http://purl.uniprot.org/uniprot/B1ASY9|||http://purl.uniprot.org/uniprot/Q571K4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Turn|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Turn|||Zinc Finger ^@ CUE|||Disordered|||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_0000226973 http://togogenome.org/gene/10090:Cacnb3 ^@ http://purl.uniprot.org/uniprot/A0A2U3TZ49|||http://purl.uniprot.org/uniprot/D3Z3Z3|||http://purl.uniprot.org/uniprot/P54285 ^@ 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|||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_0000144057 http://togogenome.org/gene/10090:Tmem39a ^@ http://purl.uniprot.org/uniprot/Q9CYC3 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 39A ^@ http://purl.uniprot.org/annotation/PRO_0000279225|||http://purl.uniprot.org/annotation/VSP_023418 http://togogenome.org/gene/10090:Rorb ^@ http://purl.uniprot.org/uniprot/A0A0R4J1H4|||http://purl.uniprot.org/uniprot/Q8R1B8 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ AF-2|||Basic and acidic residues|||Disordered|||In isoform 1.|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor ROR-beta ^@ http://purl.uniprot.org/annotation/PRO_0000053515|||http://purl.uniprot.org/annotation/VSP_022576 http://togogenome.org/gene/10090:Ppef1 ^@ http://purl.uniprot.org/uniprot/O35655 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Catalytic|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||IQ|||Proton donor|||Serine/threonine-protein phosphatase with EF-hands 1 ^@ http://purl.uniprot.org/annotation/PRO_0000058900 http://togogenome.org/gene/10090:Dusp2 ^@ http://purl.uniprot.org/uniprot/Q05922 ^@ 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|||Sequence Conflict|||Splice Variant ^@ Does not affect interaction with MAPK1.|||Does not affect interaction with MAPK1. Loss of interaction with MAPK1; when associated with A-62.|||Does not affect phosphatase activity. Loss of phosphatase activity; when associated with A-294 and A-295. Does not affect interaction with MAPK1.|||Dual specificity protein phosphatase 2|||In isoform 2.|||Loss of interaction with MAPK1. Loss of interaction with MAPK1; when associated with A-61.|||Loss of phosphatase activity.|||Loss of phosphatase activity. Does not affect interaction with MAPK1.|||Loss of phosphatase activity. Loss of phosphatase activity; when associated with A-292 and A-294. Does not affect interaction with MAPK1.|||Loss of phosphatase activity. Loss of phosphatase activity; when associated with A-292 and A-295. Does not affect interaction with MAPK1.|||Phosphocysteine intermediate|||Rhodanese|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094794|||http://purl.uniprot.org/annotation/VSP_005135|||http://purl.uniprot.org/annotation/VSP_005136 http://togogenome.org/gene/10090:Kcnc1 ^@ http://purl.uniprot.org/uniprot/P15388|||http://purl.uniprot.org/uniprot/Q3TR92|||http://purl.uniprot.org/uniprot/Q3UHB6 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ BTB|||Cytoplasmic|||Disordered|||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.|||Ion transport|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Potassium voltage-gated channel subfamily C member 1|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054052|||http://purl.uniprot.org/annotation/VSP_058604 http://togogenome.org/gene/10090:Apoa2 ^@ http://purl.uniprot.org/uniprot/P09813 ^@ Chain|||Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ Chain|||Mass|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ Apolipoprotein A-II|||In SAM.|||Methionine sulfoxide|||Proapolipoprotein A-II|||Strain BALB/c. With 1 methionine sulfoxide.|||Strain BALB/c. Without methionine sulfoxide.|||Strain C57BL/6. With 1 methionine sulfoxide.|||Strain C57BL/6. With 2 methionine sulfoxides.|||Strain C57BL/6. Without methionine sulfoxide. ^@ http://purl.uniprot.org/annotation/PRO_0000002008|||http://purl.uniprot.org/annotation/PRO_0000425354 http://togogenome.org/gene/10090:Fgfrl1 ^@ http://purl.uniprot.org/uniprot/Q91V87 ^@ 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|||Fibroblast growth factor receptor-like 1|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000021251|||http://purl.uniprot.org/annotation/VSP_013976 http://togogenome.org/gene/10090:Rpl37rt ^@ http://purl.uniprot.org/uniprot/Q9D823 ^@ 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_0000139706 http://togogenome.org/gene/10090:Nt5c ^@ http://purl.uniprot.org/uniprot/Q9JM14 ^@ Active Site|||Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Strand|||Turn ^@ 5'(3')-deoxyribonucleotidase, cytosolic type|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000164372 http://togogenome.org/gene/10090:Rnf113a1 ^@ http://purl.uniprot.org/uniprot/Q8R3P8 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ C3H1-type|||Disordered|||Polar residues|||RING-type ^@ http://togogenome.org/gene/10090:Pdk4 ^@ http://purl.uniprot.org/uniprot/O70571|||http://purl.uniprot.org/uniprot/Q544J2 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Site|||Transit Peptide ^@ Histidine kinase|||Interaction with the other subunit in the homodimer|||Mitochondrion|||[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000023446 http://togogenome.org/gene/10090:Cpne6 ^@ http://purl.uniprot.org/uniprot/Q3UYN2|||http://purl.uniprot.org/uniprot/Q9Z140 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region ^@ C2|||C2 1|||C2 2|||Copine-6|||Does not inhibit calcium-dependent translocation to the cell membrane. Inhibits calcium-dependent translocation to the cell membrane; when associated with G-282 and G-284.|||Does not inhibit calcium-dependent translocation to the cell membrane. Inhibits calcium-dependent translocation to the cell membrane; when associated with G-283 and G-284.|||Does not inhibit calcium-dependent translocation to the cell membrane. Inhibits strongly calcium-dependent translocation to the cell membrane; when associated with N-229. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-167; N-173 and N-229.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with A-272 and A-273.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with A-272 and A-274.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with A-273 and A-274.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with G-286 and G-287.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with G-286 and G-288.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with G-287 and G-288.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-33; N-35 and N-93.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-33; N-35 and N-96.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-33; N-93 and N-96.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-35; N-93 and N-96.|||Inhibits calcium-dependent translocation to the cell membrane; when associated with S-282 and S-283.|||Inhibits calcium-dependent translocation to the cell membrane; when associated with S-282 and S-284.|||Inhibits calcium-dependent translocation to the cell membrane; when associated with S-283 and S-284.|||Inhibits partially calcium-dependent translocation to the cell membrane. Inhibits calcium-dependent translocation to the cell membrane; when associated with G-282 and G-283.|||Inhibits strongly calcium-dependent translocation to the cell membrane. Inhibits strongly calcium-dependent translocation to the cell membrane; when associated with N-167. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-167; N-229 and N-231.|||Inhibits strongly calcium-dependent translocation to the cell membrane. Inhibits strongly calcium-dependent translocation to the cell membrane; when associated with N-173. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-173; N-229 and N-231.|||Inhibits strongly calcium-dependent translocation to the cell membrane; when associated with N-231. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-167; N-173 and N-231.|||Linker region|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000144846 http://togogenome.org/gene/10090:Vmn2r65 ^@ http://purl.uniprot.org/uniprot/G3X931 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015091875 http://togogenome.org/gene/10090:Acvr1c ^@ http://purl.uniprot.org/uniprot/A2AJR5|||http://purl.uniprot.org/uniprot/Q3V348|||http://purl.uniprot.org/uniprot/Q8K348 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Activin receptor type-1C|||Cytoplasmic|||Extracellular|||GS|||Helical|||Protein kinase|||Proton acceptor|||receptor protein serine/threonine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000042629|||http://purl.uniprot.org/annotation/PRO_5002642525 http://togogenome.org/gene/10090:Slc22a30 ^@ http://purl.uniprot.org/uniprot/Q3V3G0|||http://purl.uniprot.org/uniprot/Q96LX3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:Pdlim3 ^@ http://purl.uniprot.org/uniprot/O70209 ^@ Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Strand|||Turn ^@ LIM zinc-binding|||Omega-N-methylarginine|||PDZ|||PDZ and LIM domain protein 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000075868 http://togogenome.org/gene/10090:Fam186a ^@ http://purl.uniprot.org/uniprot/Q9D9R9 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||Protein FAM186A ^@ http://purl.uniprot.org/annotation/PRO_0000332202|||http://purl.uniprot.org/annotation/VSP_036417 http://togogenome.org/gene/10090:Gatc ^@ http://purl.uniprot.org/uniprot/Q8CBY0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000290035 http://togogenome.org/gene/10090:Or1e1f ^@ http://purl.uniprot.org/uniprot/Q8VEZ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tmem165 ^@ http://purl.uniprot.org/uniprot/P52875 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Putative divalent cation/proton antiporter TMEM165 ^@ http://purl.uniprot.org/annotation/PRO_0000212469 http://togogenome.org/gene/10090:Dnajc5g ^@ http://purl.uniprot.org/uniprot/A0A087WQK2|||http://purl.uniprot.org/uniprot/Q8C632 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||J ^@ http://togogenome.org/gene/10090:Atf2 ^@ http://purl.uniprot.org/uniprot/P16951|||http://purl.uniprot.org/uniprot/Q543G2|||http://purl.uniprot.org/uniprot/Q640L6|||http://purl.uniprot.org/uniprot/Q68FE3|||http://purl.uniprot.org/uniprot/Q8CBR9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||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|||Helical|||In isoform 2.|||In isoform 3.|||Leucine-zipper|||N6-acetyllysine|||Nuclear export signal|||Phosphoserine|||Phosphoserine; by ATM|||Phosphoserine; by PKC/PRKCA and PKC/PRKCB|||Phosphothreonine|||Phosphothreonine; by MAPK1, MAPK3, MAPK11, MAPK12, MAPK14 and PLK3|||Phosphothreonine; by MAPK11 and MAPK14|||Phosphothreonine; by PKC/PRKCH|||Phosphothreonine; by VRK1|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076578|||http://purl.uniprot.org/annotation/VSP_000589|||http://purl.uniprot.org/annotation/VSP_000590 http://togogenome.org/gene/10090:Ly6g6c ^@ http://purl.uniprot.org/uniprot/Q545T2|||http://purl.uniprot.org/uniprot/Q9Z1Q4 ^@ 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 ^@ GPI-anchor amidated serine|||Lymphocyte antigen 6 complex locus protein G6c|||N-linked (GlcNAc...) (high mannose) asparagine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036177|||http://purl.uniprot.org/annotation/PRO_0000323020|||http://purl.uniprot.org/annotation/PRO_5014309632 http://togogenome.org/gene/10090:Krt42 ^@ http://purl.uniprot.org/uniprot/Q6IFX2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cytoskeletal 42|||Linker 1|||Linker 12|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000311714 http://togogenome.org/gene/10090:Cdk7 ^@ http://purl.uniprot.org/uniprot/Q03147|||http://purl.uniprot.org/uniprot/Q3THG5 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Cyclin-dependent kinase 7|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by CDK1 and CDK2|||Phosphothreonine; by CDK2|||Protein kinase|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000085792 http://togogenome.org/gene/10090:Zfand2a ^@ http://purl.uniprot.org/uniprot/Q9JII7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Zinc Finger ^@ AN1-type 1|||AN1-type 2|||AN1-type zinc finger protein 2A|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000269889 http://togogenome.org/gene/10090:Gna12 ^@ http://purl.uniprot.org/uniprot/P27600 ^@ 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 palmitoylation and transformation activity.|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein subunit alpha-12|||Phosphothreonine|||Results in myristoylation of G-2, which restores the transformation activity; when associated with G-2.|||Results in myristoylation of G-2, which restores the transformation activity; when associated with S-6.|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000203771 http://togogenome.org/gene/10090:Sstr2 ^@ http://purl.uniprot.org/uniprot/P30875 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||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 B.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||S-palmitoyl cysteine|||Somatostatin receptor type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000070121|||http://purl.uniprot.org/annotation/VSP_001923 http://togogenome.org/gene/10090:Atp1a3 ^@ http://purl.uniprot.org/uniprot/Q6PIC6|||http://purl.uniprot.org/uniprot/Q8R0E8|||http://purl.uniprot.org/uniprot/Q8VCE0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase C-terminal|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with phosphoinositide-3 kinase|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Sodium/potassium-transporting ATPase subunit alpha-3 ^@ http://purl.uniprot.org/annotation/PRO_0000046299 http://togogenome.org/gene/10090:Mpp7 ^@ http://purl.uniprot.org/uniprot/G5E8S8|||http://purl.uniprot.org/uniprot/Q8BVD5 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Guanylate kinase-like|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||L27|||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_0000320028|||http://purl.uniprot.org/annotation/VSP_031574|||http://purl.uniprot.org/annotation/VSP_031575|||http://purl.uniprot.org/annotation/VSP_031576|||http://purl.uniprot.org/annotation/VSP_031577|||http://purl.uniprot.org/annotation/VSP_031578|||http://purl.uniprot.org/annotation/VSP_031579|||http://purl.uniprot.org/annotation/VSP_031580 http://togogenome.org/gene/10090:Tubgcp6 ^@ http://purl.uniprot.org/uniprot/G5E8P0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Disordered|||Gamma-tubulin complex component 6|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000436164|||http://purl.uniprot.org/annotation/VSP_058269|||http://purl.uniprot.org/annotation/VSP_058270 http://togogenome.org/gene/10090:Hivep1 ^@ http://purl.uniprot.org/uniprot/F8VPM9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||C2H2-type|||CCHC HIVEP-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tmem94 ^@ http://purl.uniprot.org/uniprot/A0A668KL57|||http://purl.uniprot.org/uniprot/Q7TSH8 ^@ 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|||Transmembrane protein 94 ^@ http://purl.uniprot.org/annotation/PRO_0000050732 http://togogenome.org/gene/10090:Nefh ^@ http://purl.uniprot.org/uniprot/P19246|||http://purl.uniprot.org/uniprot/Q80TQ3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ 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; approximate|||44|||45|||46|||47|||48|||49|||5|||50|||51|||52|||52 X 6 AA approximate tandem repeats of K-S-P-[AGISV]-[EATK]-[APVQ]|||6|||7|||8|||9|||Acidic residues|||Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2A|||Coil 2B|||Disordered|||Head|||IF rod|||Linker 1|||Linker 12|||Linker 2|||Neurofilament heavy polypeptide|||Phosphoserine|||Phosphothreonine|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063801 http://togogenome.org/gene/10090:Ccdc85b ^@ http://purl.uniprot.org/uniprot/A0A494B9B6|||http://purl.uniprot.org/uniprot/Q6PDY0 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Region ^@ Coiled-coil domain-containing protein 85B|||Disordered|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000079909 http://togogenome.org/gene/10090:Gm5431 ^@ http://purl.uniprot.org/uniprot/A6PWD6|||http://purl.uniprot.org/uniprot/Q3TMS7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ IRG-type G ^@ http://togogenome.org/gene/10090:Tmem178b ^@ http://purl.uniprot.org/uniprot/Q8BNC6 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Rnf111 ^@ http://purl.uniprot.org/uniprot/Q99ML9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Abolishes binding to sumoylated proteins and ubiquitination and degradation of PML; when associated with 300-A--A-303 and 326-A--A-329.|||Abolishes binding to sumoylated proteins and ubiquitination and degradation of PML; when associated with 300-A--A-303 and 382-A--A-385.|||Abolishes binding to sumoylated proteins and ubiquitination and degradation of PML; 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.|||Interaction with AXIN1|||No effect on TGF-beta and BMP signaling.|||Polar 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_0000280691|||http://purl.uniprot.org/annotation/VSP_023842 http://togogenome.org/gene/10090:Prcp ^@ http://purl.uniprot.org/uniprot/Q7TMR0 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Charge relay system|||In isoform 2.|||Lysosomal Pro-X carboxypeptidase|||N-linked (GlcNAc...) asparagine|||SKS domain ^@ http://purl.uniprot.org/annotation/PRO_0000027310|||http://purl.uniprot.org/annotation/PRO_0000027311|||http://purl.uniprot.org/annotation/VSP_039456 http://togogenome.org/gene/10090:Dhx33 ^@ http://purl.uniprot.org/uniprot/Q80VY9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 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|||Loss of stimulation of rRNA synthesis. Loss of protein synthesis promotion. No effect on interaction with DDX3X, EIF3G, EIF3H and RPL27.|||Required for nucleolar location ^@ http://purl.uniprot.org/annotation/PRO_0000055165 http://togogenome.org/gene/10090:Nat8f1 ^@ http://purl.uniprot.org/uniprot/E9PUL7|||http://purl.uniprot.org/uniprot/Q9JIZ0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ Helical|||N-acetyltransferase|||Probable N-acetyltransferase CML1 ^@ http://purl.uniprot.org/annotation/PRO_0000284686 http://togogenome.org/gene/10090:Cnot6l ^@ http://purl.uniprot.org/uniprot/Q8VEG6 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ CCR4-NOT transcription complex subunit 6-like|||In isoform 2 and isoform 3.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||Nuclease domain|||Proton donor/acceptor|||Required for interaction with CNOT1, CNOT3 and CNOT7 ^@ http://purl.uniprot.org/annotation/PRO_0000314588|||http://purl.uniprot.org/annotation/VSP_030324|||http://purl.uniprot.org/annotation/VSP_030325|||http://purl.uniprot.org/annotation/VSP_030326 http://togogenome.org/gene/10090:Mlph ^@ http://purl.uniprot.org/uniprot/A0A0R4J075|||http://purl.uniprot.org/uniprot/Q91V27 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||Disordered|||FYVE-type|||Melanophilin|||Polar residues|||RabBD ^@ http://purl.uniprot.org/annotation/PRO_0000190223 http://togogenome.org/gene/10090:Bcl7b ^@ http://purl.uniprot.org/uniprot/Q921K9 ^@ 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.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000239830|||http://purl.uniprot.org/annotation/VSP_019280|||http://purl.uniprot.org/annotation/VSP_019281 http://togogenome.org/gene/10090:Stx6 ^@ http://purl.uniprot.org/uniprot/Q9JKK1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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_0000210209|||http://purl.uniprot.org/annotation/VSP_016138 http://togogenome.org/gene/10090:Epha7 ^@ http://purl.uniprot.org/uniprot/A2BDQ4|||http://purl.uniprot.org/uniprot/Q61772|||http://purl.uniprot.org/uniprot/Q8CC52 ^@ Active Site|||Binding Site|||Chain|||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 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 7|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||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|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000016819|||http://purl.uniprot.org/annotation/PRO_5015086042|||http://purl.uniprot.org/annotation/PRO_5015099087|||http://purl.uniprot.org/annotation/VSP_003006|||http://purl.uniprot.org/annotation/VSP_003007|||http://purl.uniprot.org/annotation/VSP_003008|||http://purl.uniprot.org/annotation/VSP_003009|||http://purl.uniprot.org/annotation/VSP_003010|||http://purl.uniprot.org/annotation/VSP_003011 http://togogenome.org/gene/10090:Gm30302 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VN40 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues|||SPATA31 ^@ http://togogenome.org/gene/10090:Pcdh17 ^@ http://purl.uniprot.org/uniprot/E9PXF0|||http://purl.uniprot.org/uniprot/Q3UTP0|||http://purl.uniprot.org/uniprot/Q5HZI5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Cadherin|||Cadherin domain-containing protein|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003245482|||http://purl.uniprot.org/annotation/PRO_5004230310|||http://purl.uniprot.org/annotation/PRO_5004257614 http://togogenome.org/gene/10090:Fbxo36 ^@ http://purl.uniprot.org/uniprot/Q9CQ24 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ F-box|||F-box only protein 36 ^@ http://purl.uniprot.org/annotation/PRO_0000119929 http://togogenome.org/gene/10090:Or1n2 ^@ http://purl.uniprot.org/uniprot/Q8VGJ8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tpst2 ^@ http://purl.uniprot.org/uniprot/O88856 ^@ 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|||Helical; Signal-anchor for type II membrane protein|||Interaction with peptide substrate|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein-tyrosine sulfotransferase 2|||Proton donor/acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000189830 http://togogenome.org/gene/10090:Or10j2 ^@ http://purl.uniprot.org/uniprot/A0A140T8J6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dlec1 ^@ http://purl.uniprot.org/uniprot/D3Z6E8|||http://purl.uniprot.org/uniprot/E9Q8C0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Zfp758 ^@ http://purl.uniprot.org/uniprot/E9Q462|||http://purl.uniprot.org/uniprot/E9QAA1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Fem1al ^@ http://purl.uniprot.org/uniprot/Q8C0T1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Region|||Repeat ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Disordered|||Phosphoserine|||Protein fem-1 homolog A-B|||TPR 1|||TPR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000324527 http://togogenome.org/gene/10090:Htr5b ^@ http://purl.uniprot.org/uniprot/G3X9C6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Prickle2 ^@ http://purl.uniprot.org/uniprot/A7YQ68|||http://purl.uniprot.org/uniprot/Q80Y24 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Cysteine methyl ester|||Disordered|||LIM zinc-binding|||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_0000075892|||http://purl.uniprot.org/annotation/PRO_0000396719 http://togogenome.org/gene/10090:Rbp1 ^@ http://purl.uniprot.org/uniprot/Q00915|||http://purl.uniprot.org/uniprot/Q58EU7 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region ^@ Cytosolic fatty-acid binding proteins|||Important for interaction with STRA6|||Retinol-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000067393 http://togogenome.org/gene/10090:Malsu1 ^@ http://purl.uniprot.org/uniprot/Q9CWV0 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Mitochondrial assembly of ribosomal large subunit protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000228109 http://togogenome.org/gene/10090:Or8b12c ^@ http://purl.uniprot.org/uniprot/Q7TRE4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wdr5b ^@ http://purl.uniprot.org/uniprot/Q9D7H2 ^@ Chain|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Motif|||Region|||Repeat ^@ DDB1-binding motif|||Disordered|||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_0000278462 http://togogenome.org/gene/10090:Fam104a ^@ http://purl.uniprot.org/uniprot/A2A6P4|||http://purl.uniprot.org/uniprot/Q9CQP1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Slc66a3 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VLY9|||http://purl.uniprot.org/uniprot/Q3UU83|||http://purl.uniprot.org/uniprot/Q8C6U2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Helical|||Solute carrier family 66 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000232513|||http://purl.uniprot.org/annotation/PRO_5010988203|||http://purl.uniprot.org/annotation/PRO_5015097502 http://togogenome.org/gene/10090:Mb21d2 ^@ http://purl.uniprot.org/uniprot/D3Z742 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Mab-21-like HhH/H2TH-like|||Mab-21-like nucleotidyltransferase|||Polar residues ^@ http://togogenome.org/gene/10090:Catip ^@ http://purl.uniprot.org/uniprot/B9EKE5 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Ciliogenesis-associated TTC17-interacting protein|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000391708|||http://purl.uniprot.org/annotation/VSP_038747|||http://purl.uniprot.org/annotation/VSP_038748 http://togogenome.org/gene/10090:Nell1 ^@ http://purl.uniprot.org/uniprot/Q2VWQ2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Protein kinase C-binding protein NELL1|||VWFC 1|||VWFC 2|||VWFC 3 ^@ http://purl.uniprot.org/annotation/PRO_0000322642 http://togogenome.org/gene/10090:Vmn2r114 ^@ http://purl.uniprot.org/uniprot/E9Q281 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245616 http://togogenome.org/gene/10090:Slc6a15 ^@ http://purl.uniprot.org/uniprot/Q8BG16 ^@ 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; 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|||Sodium-dependent neutral amino acid transporter B(0)AT2 ^@ http://purl.uniprot.org/annotation/PRO_0000214799 http://togogenome.org/gene/10090:Tpm2 ^@ http://purl.uniprot.org/uniprot/A2AIM4|||http://purl.uniprot.org/uniprot/P58774|||http://purl.uniprot.org/uniprot/Q61344|||http://purl.uniprot.org/uniprot/Q6PJ18|||http://purl.uniprot.org/uniprot/Q9D1R6 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes ADRB2 internalization.|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by PIK3CG|||Phosphothreonine|||Phosphotyrosine|||Tropomyosin beta chain ^@ http://purl.uniprot.org/annotation/PRO_0000205628|||http://purl.uniprot.org/annotation/VSP_006597|||http://purl.uniprot.org/annotation/VSP_006598 http://togogenome.org/gene/10090:Rnf148 ^@ http://purl.uniprot.org/uniprot/G3X9R7 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Transmembrane|||Zinc Finger ^@ Helical|||N-linked (GlcNAc...) asparagine|||PA|||RING finger protein 148|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000415818 http://togogenome.org/gene/10090:Calcoco1 ^@ http://purl.uniprot.org/uniprot/Q8CGU1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ C-terminal AD (CTNNB1 binding site); interaction with CCAR1|||Calcium-binding and coiled-coil domain-containing protein 1|||Disordered|||Interaction with GATA1|||Loss of interaction with p300 KIX domain; eliminated the autonomous transactivation function.|||N-terminal AD (CTNNB1 binding site)|||Phosphoserine|||Polar residues|||Reduced binding to p300 KIX domain; severe reduction in the autonomous transactivation function.|||UBZ1-type|||p300 KIX-binding ^@ http://purl.uniprot.org/annotation/PRO_0000308900 http://togogenome.org/gene/10090:H2-K1 ^@ http://purl.uniprot.org/uniprot/P01901|||http://purl.uniprot.org/uniprot/Q3TH01|||http://purl.uniprot.org/uniprot/Q7JJ15 ^@ 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|||Disordered|||Extracellular|||H-2 class I histocompatibility antigen, K-B alpha chain|||Helical|||Ig-like|||Ig-like C1-type|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000018928|||http://purl.uniprot.org/annotation/PRO_5010845657|||http://purl.uniprot.org/annotation/PRO_5015097436 http://togogenome.org/gene/10090:Dynlt1c ^@ http://purl.uniprot.org/uniprot/P51807 ^@ 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 ^@ Dynein light chain Tctex-type 1|||Interaction with GNB1|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000195153 http://togogenome.org/gene/10090:Rnf20 ^@ http://purl.uniprot.org/uniprot/Q5DTM8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase BRE1A|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055837|||http://purl.uniprot.org/annotation/VSP_016679 http://togogenome.org/gene/10090:Pam16 ^@ http://purl.uniprot.org/uniprot/Q9CQV1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ J-like|||Mitochondrial import inner membrane translocase subunit TIM16|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000214079 http://togogenome.org/gene/10090:Abca8a ^@ http://purl.uniprot.org/uniprot/A4PBQ7|||http://purl.uniprot.org/uniprot/F8WGE3|||http://purl.uniprot.org/uniprot/Q8K442 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ ABC transporter|||ABC transporter 1|||ABC transporter 2|||ABC-type organic anion transporter ABCA8A|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000250678 http://togogenome.org/gene/10090:Hgs ^@ http://purl.uniprot.org/uniprot/Q3UMA3|||http://purl.uniprot.org/uniprot/Q99LI8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ 100-fold loss of affinity for PIP3 and accumulation in the cytosol.|||Accumulation in proteinaceous aggregates devoid of membranes and no interaction with PI3P.|||Basic and acidic residues|||Disordered|||FYVE-type|||Hepatocyte growth factor-regulated tyrosine kinase substrate|||Interaction with NF2|||Interaction with SNAP25 and TRAK2|||Interaction with SNX1|||Interaction with STAM|||Loss of protein phosphorylation at Y-329 and Y-334; when associated with A-269.|||Loss of protein phosphorylation at Y-329 and Y-334; when associated with A-270.|||N6-acetyllysine|||N6-succinyllysine|||No change in the phosphorylation level. Loss of protein phosphorylation; when associated with F-329.|||No change in the phosphorylation level. Loss of protein phosphorylation; when associated with F-334.|||No interaction with ubiquitin.|||Phosphotyrosine|||Polar residues|||Pro residues|||UIM|||VHS ^@ http://purl.uniprot.org/annotation/PRO_0000098709 http://togogenome.org/gene/10090:Coro2b ^@ http://purl.uniprot.org/uniprot/Q8BH44 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Repeat|||Sequence Conflict ^@ Coronin-2B|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000050931 http://togogenome.org/gene/10090:Tmem45a ^@ http://purl.uniprot.org/uniprot/Q8BFU6 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Ifi205 ^@ http://purl.uniprot.org/uniprot/Q8CGE8 ^@ 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|||HIN-200|||Interferon-activable protein 205-A|||Polar residues|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000334527 http://togogenome.org/gene/10090:Pwwp4b ^@ http://purl.uniprot.org/uniprot/Q52KH6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Pcdhb6 ^@ http://purl.uniprot.org/uniprot/Q91XZ4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself.|||Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself; when associated with E-141.|||Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself; when associated with N-185.|||Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself;when associated with D-69 and R-368.|||Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself;when associated with V-67 and R-368.|||Changed homophilic interaction; when associated with F-326.|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||No effect on homophilic interaction. Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself; when associated with K-317.|||No effect on homophilic interaction. Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself; when associated with R-323.|||No effect on homophilic interaction. Changed homophilic interaction, being unable to interact with the wild-type protein but able to bind itself; when associated with V-67 and D-69.|||No effect on homophilic interaction. Changed homophilic interaction; when associated with P-143.|||O-linked (Man) serine|||O-linked (Man) threonine|||Protocadherin beta-6 ^@ http://purl.uniprot.org/annotation/PRO_5008429367 http://togogenome.org/gene/10090:Ski ^@ http://purl.uniprot.org/uniprot/B1AUF1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||c-SKI SMAD4-binding ^@ http://togogenome.org/gene/10090:1700003E16Rik ^@ http://purl.uniprot.org/uniprot/Q9DAQ4 ^@ 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.|||Phosphoserine|||Polar residues|||Uncharacterized protein C2orf81 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000328767|||http://purl.uniprot.org/annotation/VSP_032776|||http://purl.uniprot.org/annotation/VSP_032777 http://togogenome.org/gene/10090:Sft2d2 ^@ http://purl.uniprot.org/uniprot/Q8VD57 ^@ 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_0000238611 http://togogenome.org/gene/10090:Lrrc41 ^@ http://purl.uniprot.org/uniprot/Q8K1C9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||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|||No association with Elongin BC complex; when associated with F-50.|||No association with Elongin BC complex; when associated with P-46.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096646 http://togogenome.org/gene/10090:Fhl5 ^@ http://purl.uniprot.org/uniprot/Q9WTX7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Zinc Finger ^@ C4-type|||Four and a half LIM domains protein 5|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3 ^@ http://purl.uniprot.org/annotation/PRO_0000075743 http://togogenome.org/gene/10090:Cdca7 ^@ http://purl.uniprot.org/uniprot/Q9D0M2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Cell division cycle-associated protein 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with MYC|||Mediates transcriptional activity|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000249311 http://togogenome.org/gene/10090:Ttc5 ^@ http://purl.uniprot.org/uniprot/Q8BNN3|||http://purl.uniprot.org/uniprot/Q8C8M9|||http://purl.uniprot.org/uniprot/Q99LG4 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Strand|||Turn ^@ Decreased phosphorylation. No change in subcellular localization in non-stress conditions. No change in nuclear accumulation in response to DNA damage. Impaired stability in response to DNA damage.|||Increased nuclear localization in non-stress conditions. No change in protein accumulation and stability in response to DNA damage. No change in subcellular localization in non-stress conditions; when associated with 13-L--Y-24. No change in protein accumulation and stability in response to DNA damage; when associated with 13-L--Y-24.|||Loss of phosphorylation at S-203; decreased nuclear localization in non-stress conditions; loss of nuclear accumulation and stability in response to DNA damage. No change in subcellular localization in non-stress conditions; when associated with 13-L--Y-24. No change in protein accumulation and stability in response to DNA damage; when associated with 13-L--Y-24.|||Mediates interaction with 28S rRNA of ribosome-coding tubulin|||Mediates interaction with N-terminal MREI motif of beta-tubulin nascent chain|||No change in subcellular localization in non-stress conditions. No change in protein accumulation and stability in response to DNA damage.|||Nuclear export signal|||Phosphoserine; by ATM|||Phosphoserine; by CHEK2|||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_0000106382 http://togogenome.org/gene/10090:S100a4 ^@ http://purl.uniprot.org/uniprot/P07091|||http://purl.uniprot.org/uniprot/Q545V2 ^@ 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|||EF-hand 1|||EF-hand 2|||N-acetylalanine|||N6-acetyllysine|||Protein S100-A4|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000143978 http://togogenome.org/gene/10090:Rom1 ^@ http://purl.uniprot.org/uniprot/P32958|||http://purl.uniprot.org/uniprot/Q3UZZ7 ^@ 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|||Rod outer segment membrane protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000168112 http://togogenome.org/gene/10090:Pcyt1a ^@ http://purl.uniprot.org/uniprot/P49586 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||2; approximate|||3|||3 X 11 AA approximate tandem repeats|||3 X repeats|||Amphipathic|||Basic and acidic residues|||Choline-phosphate cytidylyltransferase A|||Disordered|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000208454 http://togogenome.org/gene/10090:Dym ^@ http://purl.uniprot.org/uniprot/Q8CHY3 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Splice Variant ^@ Dymeclin|||In isoform 2.|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000086884|||http://purl.uniprot.org/annotation/VSP_036444|||http://purl.uniprot.org/annotation/VSP_036445 http://togogenome.org/gene/10090:Clec4g ^@ http://purl.uniprot.org/uniprot/Q8BNX1 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 4 member G|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000223692 http://togogenome.org/gene/10090:Ldlrad1 ^@ http://purl.uniprot.org/uniprot/D3YYZ1 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Slc7a5 ^@ http://purl.uniprot.org/uniprot/Q9Z127 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interchain (with C-210 in SLC3A2)|||Large neutral amino acids transporter small subunit 1|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000054271 http://togogenome.org/gene/10090:Naa80 ^@ http://purl.uniprot.org/uniprot/Q3UVC9|||http://purl.uniprot.org/uniprot/Q9R123 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||N-acetyltransferase|||N-alpha-acetyltransferase 80|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000074537 http://togogenome.org/gene/10090:Or13a1 ^@ http://purl.uniprot.org/uniprot/Q8VGH2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Asb13 ^@ http://purl.uniprot.org/uniprot/Q8VBX0 ^@ 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 13|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066950 http://togogenome.org/gene/10090:Prl3d1 ^@ http://purl.uniprot.org/uniprot/A0A286YC78|||http://purl.uniprot.org/uniprot/Q8BNL4 ^@ Binding Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015076942|||http://purl.uniprot.org/annotation/PRO_5015099044 http://togogenome.org/gene/10090:Tomm22 ^@ http://purl.uniprot.org/uniprot/Q9CPQ3 ^@ 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 ^@ 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_0000076108 http://togogenome.org/gene/10090:Mlh1 ^@ http://purl.uniprot.org/uniprot/Q9JK91 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||DNA mismatch repair protein Mlh1|||Disordered|||Interaction with EXO1|||Nuclear localization signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000178001 http://togogenome.org/gene/10090:Or8c8 ^@ http://purl.uniprot.org/uniprot/F8VQN7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wdr90 ^@ http://purl.uniprot.org/uniprot/H7BX49|||http://purl.uniprot.org/uniprot/Q6ZPG2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Splice Variant ^@ CFA20|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||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|||WD repeat-containing protein 90 ^@ http://purl.uniprot.org/annotation/PRO_0000341413|||http://purl.uniprot.org/annotation/VSP_034309|||http://purl.uniprot.org/annotation/VSP_034310|||http://purl.uniprot.org/annotation/VSP_034311|||http://purl.uniprot.org/annotation/VSP_034312|||http://purl.uniprot.org/annotation/VSP_034313|||http://purl.uniprot.org/annotation/VSP_034314 http://togogenome.org/gene/10090:Ahdc1 ^@ http://purl.uniprot.org/uniprot/Q6PAL7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict ^@ A.T hook 1|||A.T hook 2|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Transcription factor Gibbin ^@ http://purl.uniprot.org/annotation/PRO_0000313825 http://togogenome.org/gene/10090:Sp100 ^@ http://purl.uniprot.org/uniprot/E9Q4Y0|||http://purl.uniprot.org/uniprot/O35892|||http://purl.uniprot.org/uniprot/Q3U876|||http://purl.uniprot.org/uniprot/Q3UKD8|||http://purl.uniprot.org/uniprot/Q6NTA3|||http://purl.uniprot.org/uniprot/Q8BNW8|||http://purl.uniprot.org/uniprot/Q8C405 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||HSR|||In isoform 2.|||Nuclear autoantigen Sp-100|||Phosphoserine|||Phosphothreonine|||Polar residues|||PxVxL motif|||SAND ^@ http://purl.uniprot.org/annotation/PRO_0000074098|||http://purl.uniprot.org/annotation/VSP_005985 http://togogenome.org/gene/10090:Atrip ^@ http://purl.uniprot.org/uniprot/Q8BMG1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ ATR-interacting protein|||Disordered|||EEXXXDL motif|||Interaction with CINP|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064742 http://togogenome.org/gene/10090:Yipf5 ^@ http://purl.uniprot.org/uniprot/Q9EQQ2 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Interaction with Sec23|||Lumenal|||Protein YIPF5 ^@ http://purl.uniprot.org/annotation/PRO_0000234330 http://togogenome.org/gene/10090:Padi4 ^@ http://purl.uniprot.org/uniprot/Q9Z183 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Citrulline|||Protein-arginine deiminase type-4 ^@ http://purl.uniprot.org/annotation/PRO_0000220034 http://togogenome.org/gene/10090:Mnd1 ^@ http://purl.uniprot.org/uniprot/Q8K396 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Meiotic nuclear division protein 1 homolog|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000318082 http://togogenome.org/gene/10090:Ccdc107 ^@ http://purl.uniprot.org/uniprot/Q9DCC3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Coiled-coil domain-containing protein 107|||Disordered|||Helical|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000282408|||http://purl.uniprot.org/annotation/VSP_024134 http://togogenome.org/gene/10090:Hao2 ^@ http://purl.uniprot.org/uniprot/Q9NYQ2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict ^@ 2-Hydroxyacid oxidase 2|||FMN hydroxy acid dehydrogenase|||Microbody targeting signal|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000206321 http://togogenome.org/gene/10090:Hopx ^@ http://purl.uniprot.org/uniprot/Q8R1H0 ^@ Chain|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||DNA Binding|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand ^@ Homeobox; atypical|||Homeodomain-only protein|||In H2; induces a strong reduction in interaction with SRF and subsequent ability to prevent transcription of cardiac-specific genes.|||In H3; does not affect the interaction with SRF and keeps its ability to prevent transcription of cardiac-specific genes. ^@ http://purl.uniprot.org/annotation/PRO_0000049130 http://togogenome.org/gene/10090:Enoph1 ^@ http://purl.uniprot.org/uniprot/Q8BGB7 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Sequence Conflict|||Splice Variant ^@ Enolase-phosphatase E1|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000254008|||http://purl.uniprot.org/annotation/VSP_021161 http://togogenome.org/gene/10090:BC034090 ^@ http://purl.uniprot.org/uniprot/F6T2X5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ 4Fe-4S ferredoxin-type|||Basic and acidic residues|||Disordered|||PDZ|||Polar residues ^@ http://togogenome.org/gene/10090:Tes ^@ http://purl.uniprot.org/uniprot/Q921W7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||LIM zinc-binding|||PET ^@ http://togogenome.org/gene/10090:Npnt ^@ http://purl.uniprot.org/uniprot/D3YTX1|||http://purl.uniprot.org/uniprot/Q3TYB4|||http://purl.uniprot.org/uniprot/Q91V88 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Integrin interaction|||MAM|||Nephronectin|||Polar residues|||Pro residues|||Reduced cell spreading- and survival-promoting activities. ^@ http://purl.uniprot.org/annotation/PRO_0000295685|||http://purl.uniprot.org/annotation/VSP_026989|||http://purl.uniprot.org/annotation/VSP_026990 http://togogenome.org/gene/10090:Ift140 ^@ http://purl.uniprot.org/uniprot/E9PY46|||http://purl.uniprot.org/uniprot/Q3TQ94 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant ^@ Chain|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant ^@ In cauli.|||Intraflagellar transport protein 140 homolog|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000441017 http://togogenome.org/gene/10090:Mms22l ^@ http://purl.uniprot.org/uniprot/B1AUR6 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||Protein MMS22-like ^@ http://purl.uniprot.org/annotation/PRO_0000403772|||http://purl.uniprot.org/annotation/VSP_040445|||http://purl.uniprot.org/annotation/VSP_040446 http://togogenome.org/gene/10090:Taf10 ^@ http://purl.uniprot.org/uniprot/Q8K0H5 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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_0000118898 http://togogenome.org/gene/10090:Klhl8 ^@ http://purl.uniprot.org/uniprot/P59280 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ BACK|||BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 8|||N-acetylalanine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000119109 http://togogenome.org/gene/10090:Rcan2 ^@ http://purl.uniprot.org/uniprot/Q543P2|||http://purl.uniprot.org/uniprot/Q8VIP4|||http://purl.uniprot.org/uniprot/Q9JHG2 ^@ 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|||Calcipressin-2|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000211418 http://togogenome.org/gene/10090:Tpte ^@ http://purl.uniprot.org/uniprot/G5E8H5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C2 tensin-type|||Helical|||Phosphatase tensin-type|||Tyrosine specific protein phosphatases ^@ http://togogenome.org/gene/10090:Mrps22 ^@ http://purl.uniprot.org/uniprot/Q9CXW2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||N6-acetyllysine|||Phosphoserine|||Small ribosomal subunit protein mS22 ^@ http://purl.uniprot.org/annotation/PRO_0000087704 http://togogenome.org/gene/10090:Apex1 ^@ http://purl.uniprot.org/uniprot/P28352|||http://purl.uniprot.org/uniprot/Q544Z7 ^@ 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|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site|||Strand|||Turn ^@ Alternate|||Basic and acidic residues|||Cleavage; by granzyme A|||Confers neuron sensitivity to MPP(+)/MPTP (1-methyl-4-phenylpyridinium).|||DNA-(apurinic or apyrimidinic site) endonuclease|||DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial|||Disordered|||Endonuclease/exonuclease/phosphatase|||Important for catalytic activity|||Important for substrate recognition|||Interaction with DNA substrate|||Mitochondrial targeting sequence (MTS)|||N6-acetyllysine|||N6-acetyllysine; by EP300|||Necessary for interaction with NPM1 and for efficient rRNA binding|||Necessary for interaction with YBX1, binding to RNA, association together with NPM1 to 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|||Reduced CDK5-mediated phosphorylation. Confers neuron resistance to MPP(+)/MPTP (1-methyl-4-phenylpyridinium). Loss of CDK5-mediated phosphorylation; when associated with S-53.|||Reduced CDK5-mediated phosphorylation. Loss of CDK5-mediated phosphorylation; when associated with T-232.|||Removed|||S-nitrosocysteine|||S-nitrosocysteine; alternate|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000200011|||http://purl.uniprot.org/annotation/PRO_0000402573 http://togogenome.org/gene/10090:Slc4a9 ^@ http://purl.uniprot.org/uniprot/A0A494BA31|||http://purl.uniprot.org/uniprot/A0A494BAI0|||http://purl.uniprot.org/uniprot/A0A494BBC3|||http://purl.uniprot.org/uniprot/E9PUP3|||http://purl.uniprot.org/uniprot/Q14CH2|||http://purl.uniprot.org/uniprot/Q14DJ1|||http://purl.uniprot.org/uniprot/Q3UQE1|||http://purl.uniprot.org/uniprot/Q8BUG8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Transmembrane ^@ Anion exchange protein 4|||Band 3 cytoplasmic|||Basic and acidic residues|||Bicarbonate transporter-like transmembrane|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Significantly decreases Cl(-)/HCO3(-) antiporter activity. Does not affect plasma membrane localization. Abolishes PKA-mediated Cl(-)/HCO3(-) antiporter activity.|||Significantly decreases Cl(-)/HCO3(-) antiporter activity. Does not affect plasma membrane localization. Does not affect PKA-mediated Cl(-)/HCO3(-) antiporter activity. ^@ http://purl.uniprot.org/annotation/PRO_0000458413 http://togogenome.org/gene/10090:Abl2 ^@ http://purl.uniprot.org/uniprot/B2RQ57|||http://purl.uniprot.org/uniprot/F8VQH0 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Protein kinase|||SH2|||SH3 ^@ http://togogenome.org/gene/10090:Vmn1r32 ^@ http://purl.uniprot.org/uniprot/Q8R2D9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or10c1 ^@ http://purl.uniprot.org/uniprot/Q8VFE2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ganab ^@ http://purl.uniprot.org/uniprot/A1A4T2|||http://purl.uniprot.org/uniprot/Q8BHN3 ^@ 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|||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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Disrupts interaction with PRKCSH. Nearly abolishes enzyme activity.|||Glycoside hydrolase family 31 N-terminal|||In isoform 2.|||In isoform 3.|||Loss of enzyme activity.|||N-linked (GlcNAc...) asparagine|||Neutral alpha-glucosidase AB|||Nucleophile|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000018572|||http://purl.uniprot.org/annotation/PRO_5014296705|||http://purl.uniprot.org/annotation/VSP_010675|||http://purl.uniprot.org/annotation/VSP_010676 http://togogenome.org/gene/10090:Chm ^@ http://purl.uniprot.org/uniprot/A2AD03|||http://purl.uniprot.org/uniprot/Q3UR39|||http://purl.uniprot.org/uniprot/Q8CBI2|||http://purl.uniprot.org/uniprot/Q9CS14 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Mup14 ^@ http://purl.uniprot.org/uniprot/A2CEK7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5015086057 http://togogenome.org/gene/10090:Pura ^@ http://purl.uniprot.org/uniprot/P42669 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Transcriptional activator protein Pur-alpha ^@ http://purl.uniprot.org/annotation/PRO_0000097108 http://togogenome.org/gene/10090:Cox6c ^@ http://purl.uniprot.org/uniprot/Q9CPQ1 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Topological Domain|||Transmembrane ^@ Chain|||Helix|||Topological Domain|||Transmembrane ^@ Cytochrome c oxidase subunit 6C|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix ^@ http://purl.uniprot.org/annotation/PRO_0000191302 http://togogenome.org/gene/10090:Slc2a2 ^@ http://purl.uniprot.org/uniprot/P14246 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||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|||Solute carrier family 2, facilitated glucose transporter member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000050347 http://togogenome.org/gene/10090:Dhx36 ^@ http://purl.uniprot.org/uniprot/Q8VHK9 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ ATP-dependent DNA/RNA helicase DHX36|||DEAH box|||DSM (DHX36-specific motif)|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||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|||Polar residues|||RecA-like domain 1|||RecA-like domain 2|||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_0000247531 http://togogenome.org/gene/10090:Samt1d ^@ http://purl.uniprot.org/uniprot/A2BEE3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Oma1 ^@ http://purl.uniprot.org/uniprot/Q9D8H7 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Abolished protease activity and ability to cleave OPA1. Abolished autocatalytic processing.|||Cardiolipin-binding|||Helical|||In isoform 2.|||Metalloendopeptidase OMA1, mitochondrial|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Stress-sensor region ^@ http://purl.uniprot.org/annotation/PRO_0000302810|||http://purl.uniprot.org/annotation/PRO_0000450315|||http://purl.uniprot.org/annotation/PRO_0000450316|||http://purl.uniprot.org/annotation/VSP_027959|||http://purl.uniprot.org/annotation/VSP_027960 http://togogenome.org/gene/10090:Cfap298 ^@ http://purl.uniprot.org/uniprot/Q8BL95 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Cilia- and flagella-associated protein 298 ^@ http://purl.uniprot.org/annotation/PRO_0000424911 http://togogenome.org/gene/10090:Fbxo28 ^@ http://purl.uniprot.org/uniprot/Q8BIG4 ^@ 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|||F-box|||F-box only protein 28|||Phosphoserine|||Phosphothreonine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000307725 http://togogenome.org/gene/10090:Pus10 ^@ http://purl.uniprot.org/uniprot/Q9D3U0 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Nucleophile|||Phosphoserine|||RNA binding forefinger loop|||RNA binding thumb loop|||tRNA pseudouridine synthase Pus10 ^@ http://purl.uniprot.org/annotation/PRO_0000299023 http://togogenome.org/gene/10090:Cdc73 ^@ http://purl.uniprot.org/uniprot/Q3U5E6|||http://purl.uniprot.org/uniprot/Q8JZM7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||Interaction with CTNNB1|||Interaction with POLR2A and PAF1|||N-acetylalanine|||Nuclear localization signal|||Parafibromin|||Phosphoserine|||Polar residues|||Removed|||Secreted peptide ^@ http://purl.uniprot.org/annotation/PRO_0000191804|||http://purl.uniprot.org/annotation/PRO_5004229956 http://togogenome.org/gene/10090:Sdcbp2 ^@ http://purl.uniprot.org/uniprot/Q99JZ0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ PDZ 1|||PDZ 2|||Syntenin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000184005 http://togogenome.org/gene/10090:Ctnnbip1 ^@ http://purl.uniprot.org/uniprot/Q9JJN6 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Modified Residue|||Mutagenesis Site ^@ Abolishes CTNNB1 binding.|||Beta-catenin-interacting protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000152883 http://togogenome.org/gene/10090:Dcc ^@ http://purl.uniprot.org/uniprot/P70211|||http://purl.uniprot.org/uniprot/Q3TZP5 ^@ 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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||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|||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 B.|||In isoform C.|||N-linked (GlcNAc...) asparagine|||Netrin receptor DCC|||Phosphoserine; by MAPK1|||Phosphothreonine; by MAPK1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014745|||http://purl.uniprot.org/annotation/VSP_002501|||http://purl.uniprot.org/annotation/VSP_018807 http://togogenome.org/gene/10090:Jcad ^@ http://purl.uniprot.org/uniprot/B7ZN02|||http://purl.uniprot.org/uniprot/Q5DTX6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Junctional cadherin 5-associated protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000314186 http://togogenome.org/gene/10090:Anxa10 ^@ http://purl.uniprot.org/uniprot/Q9QZ10 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A10 ^@ http://purl.uniprot.org/annotation/PRO_0000067508 http://togogenome.org/gene/10090:Klhdc2 ^@ http://purl.uniprot.org/uniprot/Q4G5Y1 ^@ 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 2 ^@ http://purl.uniprot.org/annotation/PRO_0000228993 http://togogenome.org/gene/10090:Cdc42bpa ^@ http://purl.uniprot.org/uniprot/E9PVY0|||http://purl.uniprot.org/uniprot/H7BX44|||http://purl.uniprot.org/uniprot/Q3UU96 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ AGC-kinase C-terminal|||CNH|||CRIB|||Cleavage; by CASP3 in vitro|||Disordered|||In isoform 2.|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase MRCK alpha ^@ http://purl.uniprot.org/annotation/PRO_0000280455|||http://purl.uniprot.org/annotation/VSP_023679|||http://purl.uniprot.org/annotation/VSP_023680 http://togogenome.org/gene/10090:Pin4 ^@ http://purl.uniprot.org/uniprot/Q9CWW6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||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_0000193439 http://togogenome.org/gene/10090:Ltbp1 ^@ http://purl.uniprot.org/uniprot/Q8CG19 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ (3R)-3-hydroxyasparagine|||8-Cys3 region|||C-terminal domain|||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|||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 isoform 3.|||In isoform Short and isoform 3.|||Interchain (with C-33 in TGFB1); in linked form|||Latent-transforming growth factor beta-binding protein 1|||N-linked (GlcNAc...) asparagine|||O-linked (Glc) serine|||Phosphoserine|||TB 1|||TB 2|||TB 3|||TB 4 ^@ http://purl.uniprot.org/annotation/PRO_0000007637|||http://purl.uniprot.org/annotation/VSP_036968|||http://purl.uniprot.org/annotation/VSP_036969|||http://purl.uniprot.org/annotation/VSP_036970 http://togogenome.org/gene/10090:Or4c12b ^@ http://purl.uniprot.org/uniprot/A2AUA4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bbc3 ^@ http://purl.uniprot.org/uniprot/B2RVL4|||http://purl.uniprot.org/uniprot/Q99ML1 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure ^@ Chain|||Helix|||Modified Residue|||Motif|||Region ^@ BH3|||Bcl-2-binding component 3|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000143084 http://togogenome.org/gene/10090:Tceal3 ^@ http://purl.uniprot.org/uniprot/Q8R0A5 ^@ 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|||Transcription elongation factor A protein-like 3 ^@ http://purl.uniprot.org/annotation/PRO_0000239208 http://togogenome.org/gene/10090:Tfap2c ^@ http://purl.uniprot.org/uniprot/A0A023UF19|||http://purl.uniprot.org/uniprot/Q3ULB3|||http://purl.uniprot.org/uniprot/Q61312 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||H-S-H (helix-span-helix), dimerization|||PPxY motif|||Phosphoserine|||Phosphoserine; by PKA|||Polar residues|||Transcription factor AP-2 C-terminal|||Transcription factor AP-2 gamma ^@ http://purl.uniprot.org/annotation/PRO_0000184804 http://togogenome.org/gene/10090:Zfp866 ^@ http://purl.uniprot.org/uniprot/Q6PGD2|||http://purl.uniprot.org/uniprot/Q8BIY7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Nup205 ^@ http://purl.uniprot.org/uniprot/Q6P9L5|||http://purl.uniprot.org/uniprot/Q6PDG0 ^@ Experimental Information|||Non-terminal Residue ^@ Non-terminal Residue ^@ ^@ http://togogenome.org/gene/10090:Cd3d ^@ http://purl.uniprot.org/uniprot/P04235|||http://purl.uniprot.org/uniprot/Q3U4T1|||http://purl.uniprot.org/uniprot/Q3V3B4|||http://purl.uniprot.org/uniprot/Q6P5P1 ^@ 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|||Signal Peptide|||Topological Domain|||Transmembrane ^@ CD3 gamma/delta subunit Ig-like|||CD3 gamma/delta subunit Ig-like domain-containing protein|||Cytoplasmic|||Extracellular|||Helical|||ITAM|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||T-cell surface glycoprotein CD3 delta chain ^@ http://purl.uniprot.org/annotation/PRO_0000016489|||http://purl.uniprot.org/annotation/PRO_5004230499|||http://purl.uniprot.org/annotation/PRO_5004278011|||http://purl.uniprot.org/annotation/PRO_5010843374 http://togogenome.org/gene/10090:Kif19a ^@ http://purl.uniprot.org/uniprot/A9XMT8|||http://purl.uniprot.org/uniprot/Q99PT9 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Kinesin motor|||Kinesin-like protein KIF19|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000278246 http://togogenome.org/gene/10090:Frem3 ^@ http://purl.uniprot.org/uniprot/F8WHZ0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Repeat|||Signal Peptide ^@ CSPG|||Calx-beta|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5003379512 http://togogenome.org/gene/10090:Ptbp3 ^@ http://purl.uniprot.org/uniprot/G8JL74|||http://purl.uniprot.org/uniprot/Q8BHD7 ^@ 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 ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Polypyrimidine tract-binding protein 3|||RRM|||RRM 1|||RRM 2|||RRM 3|||RRM 4 ^@ http://purl.uniprot.org/annotation/PRO_0000081874|||http://purl.uniprot.org/annotation/VSP_010869 http://togogenome.org/gene/10090:Prmt7 ^@ http://purl.uniprot.org/uniprot/Q922X9 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ 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_0000212336 http://togogenome.org/gene/10090:Scd1 ^@ http://purl.uniprot.org/uniprot/P13516|||http://purl.uniprot.org/uniprot/Q547C4 ^@ 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|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Acyl-CoA desaturase 1|||Cytoplasmic|||Disordered|||Fatty acid desaturase|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In ab.|||Lumenal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000185397 http://togogenome.org/gene/10090:Slc23a3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J067|||http://purl.uniprot.org/uniprot/Q60850 ^@ 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.|||In isoform 4.|||Polar residues|||Solute carrier family 23 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000337204|||http://purl.uniprot.org/annotation/VSP_033975|||http://purl.uniprot.org/annotation/VSP_033976|||http://purl.uniprot.org/annotation/VSP_033977 http://togogenome.org/gene/10090:Septin9 ^@ http://purl.uniprot.org/uniprot/A2A6U3|||http://purl.uniprot.org/uniprot/Q80UG5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Septin-9|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173536|||http://purl.uniprot.org/annotation/VSP_012341|||http://purl.uniprot.org/annotation/VSP_012342 http://togogenome.org/gene/10090:Serhl ^@ http://purl.uniprot.org/uniprot/Q80XK9|||http://purl.uniprot.org/uniprot/Q9EPB5 ^@ 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 ^@ AB hydrolase-1|||Phosphoserine|||Serine hydrolase-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000097693 http://togogenome.org/gene/10090:Or8g30 ^@ http://purl.uniprot.org/uniprot/Q9EQ95 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H3c2 ^@ http://purl.uniprot.org/uniprot/B9EI85|||http://purl.uniprot.org/uniprot/P84228 ^@ Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||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 H2A/H2B/H3|||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; 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_0000221250 http://togogenome.org/gene/10090:Cybb ^@ http://purl.uniprot.org/uniprot/Q3U6G0|||http://purl.uniprot.org/uniprot/Q61093 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000210146 http://togogenome.org/gene/10090:Serpina6 ^@ http://purl.uniprot.org/uniprot/Q06770|||http://purl.uniprot.org/uniprot/Q3UKW1 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Site ^@ Conserved cysteine within steroid binding domain|||Corticosteroid-binding globulin|||N-linked (GlcNAc...) asparagine|||Serpin|||Serpin domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000032431|||http://purl.uniprot.org/annotation/PRO_5004230156 http://togogenome.org/gene/10090:Gsto2 ^@ http://purl.uniprot.org/uniprot/Q8BW12|||http://purl.uniprot.org/uniprot/Q8K2Q2|||http://purl.uniprot.org/uniprot/Q9D2S1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase omega-2|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000239141 http://togogenome.org/gene/10090:Il31ra ^@ http://purl.uniprot.org/uniprot/A0A286YDE2|||http://purl.uniprot.org/uniprot/Q8K5B1 ^@ 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 ^@ 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 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interleukin-31 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000274573|||http://purl.uniprot.org/annotation/VSP_022814|||http://purl.uniprot.org/annotation/VSP_022815|||http://purl.uniprot.org/annotation/VSP_022816|||http://purl.uniprot.org/annotation/VSP_022817|||http://purl.uniprot.org/annotation/VSP_022818|||http://purl.uniprot.org/annotation/VSP_022819|||http://purl.uniprot.org/annotation/VSP_022820|||http://purl.uniprot.org/annotation/VSP_022821|||http://purl.uniprot.org/annotation/VSP_022822 http://togogenome.org/gene/10090:Dcn ^@ http://purl.uniprot.org/uniprot/P28654|||http://purl.uniprot.org/uniprot/Q3UKR1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Repeat|||Signal Peptide ^@ Decorin|||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_0000032711|||http://purl.uniprot.org/annotation/PRO_0000032712|||http://purl.uniprot.org/annotation/PRO_5014205833 http://togogenome.org/gene/10090:Nup58 ^@ http://purl.uniprot.org/uniprot/Q8R332 ^@ 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 ^@ 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.|||In isoform 4.|||Nucleoporin p58/p45|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204893|||http://purl.uniprot.org/annotation/VSP_008573|||http://purl.uniprot.org/annotation/VSP_008574|||http://purl.uniprot.org/annotation/VSP_008575 http://togogenome.org/gene/10090:Ube2r2 ^@ http://purl.uniprot.org/uniprot/Q6ZWZ2 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Glycyl thioester intermediate|||Phosphoserine; by CK2|||UBC core|||Ubiquitin-conjugating enzyme E2 R2 ^@ http://purl.uniprot.org/annotation/PRO_0000280514 http://togogenome.org/gene/10090:Angel1 ^@ http://purl.uniprot.org/uniprot/Q8VCU0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Protein angel homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000356223 http://togogenome.org/gene/10090:Ikbke ^@ http://purl.uniprot.org/uniprot/Q9R0T8 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Dominant negative.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Inhibitor of nuclear factor kappa-B kinase subunit epsilon|||Interaction with DDX3X|||Leucine-zipper|||Phosphoserine|||Phosphoserine; by autocatalysis and IKKB|||Phosphothreonine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086018 http://togogenome.org/gene/10090:Vrk1 ^@ http://purl.uniprot.org/uniprot/Q3UWH3|||http://purl.uniprot.org/uniprot/Q80X41 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolished protein serine/threonine kinase activity.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 5.|||Phosphoserine|||Phosphoserine; by PLK3|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase VRK1 ^@ http://purl.uniprot.org/annotation/PRO_0000086804|||http://purl.uniprot.org/annotation/VSP_008528|||http://purl.uniprot.org/annotation/VSP_008529|||http://purl.uniprot.org/annotation/VSP_008532 http://togogenome.org/gene/10090:Dnajb9 ^@ http://purl.uniprot.org/uniprot/Q9QYI6 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Abolishes ability to stimulate ATPase activity of HSPA5/BiP.|||Divergent targeting domain|||DnaJ homolog subfamily B member 9|||J|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000071032 http://togogenome.org/gene/10090:Ckmt2 ^@ http://purl.uniprot.org/uniprot/Q6P8J7 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Transit Peptide ^@ Cardiolipin-binding|||Creatine kinase S-type, mitochondrial|||Mitochondrion|||Phosphagen kinase C-terminal|||Phosphagen kinase N-terminal|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000016595 http://togogenome.org/gene/10090:Or5k1b ^@ http://purl.uniprot.org/uniprot/E9Q8F6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ubxn1 ^@ http://purl.uniprot.org/uniprot/Q922Y1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Turn ^@ Basic and acidic residues|||Disordered|||Interaction with BRCA1|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by MAPK12|||Phosphothreonine|||Removed|||UBA|||UBX|||UBX domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000211024 http://togogenome.org/gene/10090:Fgf2 ^@ http://purl.uniprot.org/uniprot/P15655 ^@ Binding Site|||Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Propeptide|||Region|||Site ^@ Fibroblast growth factor 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Heparin-binding|||Important for interaction with integrin|||Phosphotyrosine; by TEC ^@ http://purl.uniprot.org/annotation/PRO_0000008936|||http://purl.uniprot.org/annotation/PRO_0000008937 http://togogenome.org/gene/10090:Srd5a3 ^@ http://purl.uniprot.org/uniprot/Q9WUP4 ^@ 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.|||Lumenal|||Polyprenol reductase ^@ http://purl.uniprot.org/annotation/PRO_0000317704|||http://purl.uniprot.org/annotation/VSP_039779 http://togogenome.org/gene/10090:Zkscan8 ^@ http://purl.uniprot.org/uniprot/A0A286YCX3|||http://purl.uniprot.org/uniprot/B2RX01|||http://purl.uniprot.org/uniprot/Q78WV9|||http://purl.uniprot.org/uniprot/Q8BSL0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||Polar residues|||SCAN box ^@ http://togogenome.org/gene/10090:Klk1b4 ^@ http://purl.uniprot.org/uniprot/A0A1R3UGK0|||http://purl.uniprot.org/uniprot/P00757 ^@ 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 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand ^@ Activation peptide homolog|||Kallikrein 1-related peptidase-like b4|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027972|||http://purl.uniprot.org/annotation/PRO_5010203531 http://togogenome.org/gene/10090:Bud31 ^@ http://purl.uniprot.org/uniprot/Q6PGH1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Modified Residue|||Motif|||Region|||Splice Variant ^@ In isoform 2.|||Interaction with AR|||N6-acetyllysine|||Nuclear localization signal|||Protein BUD31 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000223627|||http://purl.uniprot.org/annotation/VSP_059351 http://togogenome.org/gene/10090:Tdp1 ^@ http://purl.uniprot.org/uniprot/B8JJC1|||http://purl.uniprot.org/uniprot/Q6P1B8 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Region|||Site ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Region|||Site ^@ Basic and acidic residues|||Disordered|||Interaction with DNA|||Nucleophile|||Polar residues|||Proton donor/acceptor ^@ http://togogenome.org/gene/10090:Rarb ^@ http://purl.uniprot.org/uniprot/P22605|||http://purl.uniprot.org/uniprot/Q6DFX0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Disordered|||Hinge|||In isoform Beta-1.|||In isoform Beta-2.|||In isoform Beta-4.|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine|||Polar residues|||Retinoic acid receptor beta ^@ http://purl.uniprot.org/annotation/PRO_0000053468|||http://purl.uniprot.org/annotation/VSP_003636|||http://purl.uniprot.org/annotation/VSP_003637|||http://purl.uniprot.org/annotation/VSP_003638|||http://purl.uniprot.org/annotation/VSP_003639|||http://purl.uniprot.org/annotation/VSP_003640 http://togogenome.org/gene/10090:Wscd2 ^@ http://purl.uniprot.org/uniprot/D4PHA7 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sialate:O-sulfotransferase 2|||WSC 1|||WSC 2 ^@ http://purl.uniprot.org/annotation/PRO_0000416124|||http://purl.uniprot.org/annotation/VSP_042508|||http://purl.uniprot.org/annotation/VSP_042509 http://togogenome.org/gene/10090:Ube3c ^@ http://purl.uniprot.org/uniprot/Q80U95 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict ^@ 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|||Ubiquitin-protein ligase E3C ^@ http://purl.uniprot.org/annotation/PRO_0000194983 http://togogenome.org/gene/10090:Fam135b ^@ http://purl.uniprot.org/uniprot/Q9DAI6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Polar residues|||Protein FAM135B ^@ http://purl.uniprot.org/annotation/PRO_0000314172 http://togogenome.org/gene/10090:Fthl17f ^@ http://purl.uniprot.org/uniprot/Q3SXD2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ferritin-like diiron ^@ http://togogenome.org/gene/10090:Cd160 ^@ http://purl.uniprot.org/uniprot/E9Q0X3|||http://purl.uniprot.org/uniprot/O88875 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ CD160 antigen|||CD160 antigen, soluble form|||GPI-anchor amidated serine|||Ig-like|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000014545|||http://purl.uniprot.org/annotation/PRO_0000014546|||http://purl.uniprot.org/annotation/PRO_0000446050|||http://purl.uniprot.org/annotation/PRO_5003245591 http://togogenome.org/gene/10090:Trpc2 ^@ http://purl.uniprot.org/uniprot/Q9R244 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ ANK 1|||ANK 2|||ANK 3|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Short transient receptor potential channel 2 ^@ http://purl.uniprot.org/annotation/PRO_0000215307|||http://purl.uniprot.org/annotation/VSP_006562|||http://purl.uniprot.org/annotation/VSP_006563|||http://purl.uniprot.org/annotation/VSP_006564|||http://purl.uniprot.org/annotation/VSP_006565 http://togogenome.org/gene/10090:Lrrk2 ^@ http://purl.uniprot.org/uniprot/Q5S006|||http://purl.uniprot.org/uniprot/Q9CQG8 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||Does not affect kinase activity and decreases sensitivity towards small molecule kinase inhibitors.|||Impaired ability to recruit SEC61A and SEC31A to endoplasmic reticulum exit sites. Impaired ability to regulate ER to Golgi vesicle-mediated transport.|||Increases kinase activity. Causes loss of dopaminergic neurons in the substantia nigra of 20-month old mice due to increased phosphorylation of APP. Reduces primary ciliogenesis.|||Increases kinase activity. Reduces primary ciliogenesis. Causes fragmentation of the trans-Golgi network.|||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|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Roc|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000086239 http://togogenome.org/gene/10090:Scn1a ^@ http://purl.uniprot.org/uniprot/A2APX8 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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|||Homozygous mice display spontaneous generalized seizures and premature death between P16 and P26. Heterozygous mice show infrequent spontaneous seizures, increased susceptibility to chemically and hyperthermia-induced generalized seizures and sleep abnormalities. Heterozygous mice also show deficits in social behavior, spatial memory, cued fear conditioning, pre-pulse inhibition and risk assessment.|||I|||II|||III|||IQ|||IV|||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)|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues|||Pore-forming|||S1-S2 loop of repeat IV|||S3b-S4 loop of repeat IV|||Sodium channel protein type 1 subunit alpha ^@ http://purl.uniprot.org/annotation/PRO_0000437536|||http://purl.uniprot.org/annotation/VSP_058552|||http://purl.uniprot.org/annotation/VSP_058553 http://togogenome.org/gene/10090:Spns3 ^@ http://purl.uniprot.org/uniprot/Q9D232 ^@ 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.|||Polar residues|||Protein spinster homolog 3 ^@ http://purl.uniprot.org/annotation/PRO_0000305047|||http://purl.uniprot.org/annotation/VSP_028199 http://togogenome.org/gene/10090:Evi5l ^@ http://purl.uniprot.org/uniprot/H3BJX1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Rab-GAP TBC ^@ http://togogenome.org/gene/10090:Sdhaf1 ^@ http://purl.uniprot.org/uniprot/Q3U276 ^@ Chain|||Molecule Processing|||Motif|||Region ^@ Chain|||Motif|||Region ^@ Disordered|||Interaction with SDHB|||LYR motif 1; required for interaction with HSC20|||LYR motif 2; not required for interaction with HSC20|||Succinate dehydrogenase assembly factor 1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000327917 http://togogenome.org/gene/10090:Plxnd1 ^@ http://purl.uniprot.org/uniprot/Q3UH93 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||N-linked (GlcNAc...) asparagine|||Plexin-D1|||Sema ^@ http://purl.uniprot.org/annotation/PRO_0000415890 http://togogenome.org/gene/10090:Or52ab2 ^@ http://purl.uniprot.org/uniprot/L7N224 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pifo ^@ http://purl.uniprot.org/uniprot/Q9D9W1 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ Ciliary microtubule-associated protein 3|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000284527|||http://purl.uniprot.org/annotation/VSP_024558 http://togogenome.org/gene/10090:Farp1 ^@ http://purl.uniprot.org/uniprot/F8VPU2|||http://purl.uniprot.org/uniprot/Q8BM51 ^@ 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 ^@ DH|||Disordered|||FERM|||FERM, ARHGEF and pleckstrin domain-containing protein 1|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000422336 http://togogenome.org/gene/10090:Or12d13 ^@ http://purl.uniprot.org/uniprot/Q920Y8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or4b1b ^@ http://purl.uniprot.org/uniprot/Q8VGN8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zbtb38 ^@ http://purl.uniprot.org/uniprot/Q3LR78 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB|||Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cytl1 ^@ http://purl.uniprot.org/uniprot/A1E5L0 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015085905 http://togogenome.org/gene/10090:Wnt2b ^@ http://purl.uniprot.org/uniprot/O70283 ^@ 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|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-2b ^@ http://purl.uniprot.org/annotation/PRO_0000041414 http://togogenome.org/gene/10090:Angpt1 ^@ http://purl.uniprot.org/uniprot/O08538 ^@ 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 ^@ Angiopoietin-1|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009111 http://togogenome.org/gene/10090:Smok3a ^@ http://purl.uniprot.org/uniprot/C0HKC8|||http://purl.uniprot.org/uniprot/C0HKC9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Protein kinase|||Proton acceptor|||Sperm motility kinase 3A|||Sperm motility kinase 3B|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000307871|||http://purl.uniprot.org/annotation/PRO_0000439229 http://togogenome.org/gene/10090:Plekhg4 ^@ http://purl.uniprot.org/uniprot/F8VPS6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ DH|||Disordered|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Otog ^@ http://purl.uniprot.org/uniprot/O55225 ^@ 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 ^@ CTCK|||Disordered|||EGF-like|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Otogelin|||Polar residues|||Pro residues|||TIL|||VWFD 1|||VWFD 2|||VWFD 3|||VWFD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000312149|||http://purl.uniprot.org/annotation/VSP_029715|||http://purl.uniprot.org/annotation/VSP_029716 http://togogenome.org/gene/10090:Iqgap1 ^@ http://purl.uniprot.org/uniprot/Q3TPD2|||http://purl.uniprot.org/uniprot/Q3TU98|||http://purl.uniprot.org/uniprot/Q9JKF1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ C1|||C2|||Calponin-homology (CH)|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||N-acetylserine|||Phosphoserine|||Phosphotyrosine|||Ras GTPase-activating-like protein IQGAP1|||Ras-GAP|||Removed|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000056649 http://togogenome.org/gene/10090:Or51s1 ^@ http://purl.uniprot.org/uniprot/E9Q407 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Krt23 ^@ http://purl.uniprot.org/uniprot/Q544I8|||http://purl.uniprot.org/uniprot/Q99PS0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type I cytoskeletal 23|||Linker 1|||Linker 12|||Polar residues|||Rod-like helical tail ^@ http://purl.uniprot.org/annotation/PRO_0000063678 http://togogenome.org/gene/10090:Tmco5b ^@ http://purl.uniprot.org/uniprot/Q80X59 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane and coiled-coil domain-containing protein 5B ^@ http://purl.uniprot.org/annotation/PRO_0000305156 http://togogenome.org/gene/10090:Eif4a3l1 ^@ http://purl.uniprot.org/uniprot/E9PV04 ^@ Domain Extent|||Motif|||Region ^@ Domain Extent|||Motif ^@ DEAD-box RNA helicase Q|||Helicase ATP-binding|||Helicase C-terminal|||Q motif ^@ http://togogenome.org/gene/10090:Bmp3 ^@ http://purl.uniprot.org/uniprot/A0A0G2JEU2|||http://purl.uniprot.org/uniprot/Q149J9|||http://purl.uniprot.org/uniprot/Q8BHE5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide ^@ Bone morphogenetic protein 3|||Disordered|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033838|||http://purl.uniprot.org/annotation/PRO_0000033839|||http://purl.uniprot.org/annotation/PRO_5014212495|||http://purl.uniprot.org/annotation/PRO_5015039210 http://togogenome.org/gene/10090:Lrit2 ^@ http://purl.uniprot.org/uniprot/Q6PFC5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Fibronectin type-III|||Helical|||Ig-like|||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_0000309345 http://togogenome.org/gene/10090:Mtmr12 ^@ http://purl.uniprot.org/uniprot/Q80TA6 ^@ 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 MTM1|||Myotubularin phosphatase|||Myotubularin-related protein 12|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315826|||http://purl.uniprot.org/annotation/VSP_030723 http://togogenome.org/gene/10090:Unc13a ^@ http://purl.uniprot.org/uniprot/H3BJZ7|||http://purl.uniprot.org/uniprot/Q4KUS2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||C2|||C2 1|||C2 2|||C2 3|||Disordered|||MHD1|||MHD2|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Protein unc-13 homolog A|||Reduces number of fusion-competent vesicles in neurons. ^@ http://purl.uniprot.org/annotation/PRO_0000306285 http://togogenome.org/gene/10090:Shoc2 ^@ http://purl.uniprot.org/uniprot/O88520 ^@ 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|||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_0000097738 http://togogenome.org/gene/10090:Inpp5b ^@ http://purl.uniprot.org/uniprot/Q8K337 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ 5-phosphatase|||ASH|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||In isoform 2.|||In isoform 3.|||PH|||Removed in mature form|||Rho-GAP|||S-farnesyl cysteine|||Type II inositol 1,4,5-trisphosphate 5-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000415365|||http://purl.uniprot.org/annotation/PRO_0000422294|||http://purl.uniprot.org/annotation/VSP_042224|||http://purl.uniprot.org/annotation/VSP_042225|||http://purl.uniprot.org/annotation/VSP_042226|||http://purl.uniprot.org/annotation/VSP_042227 http://togogenome.org/gene/10090:Tmc8 ^@ http://purl.uniprot.org/uniprot/B0QZP6|||http://purl.uniprot.org/uniprot/B0QZP7|||http://purl.uniprot.org/uniprot/B1ATC0|||http://purl.uniprot.org/uniprot/Q7TN58 ^@ 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 ^@ Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||TMC|||Transmembrane channel-like protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000185387|||http://purl.uniprot.org/annotation/VSP_016451 http://togogenome.org/gene/10090:Vldlr ^@ http://purl.uniprot.org/uniprot/F8WGI9|||http://purl.uniprot.org/uniprot/P98156|||http://purl.uniprot.org/uniprot/Q3UVX6|||http://purl.uniprot.org/uniprot/Q91YY0 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Clustered O-linked oligosaccharides|||Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like domain-containing protein|||Endocytosis signal|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||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_0000017344|||http://purl.uniprot.org/annotation/PRO_5003379499|||http://purl.uniprot.org/annotation/PRO_5004230382|||http://purl.uniprot.org/annotation/PRO_5015099515 http://togogenome.org/gene/10090:Ccr3 ^@ http://purl.uniprot.org/uniprot/P51678|||http://purl.uniprot.org/uniprot/Q3U5L7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||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|||Probable C-C chemokine receptor type 3 ^@ http://purl.uniprot.org/annotation/PRO_0000069242 http://togogenome.org/gene/10090:Acsm3 ^@ http://purl.uniprot.org/uniprot/Q3UNX5 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Acyl-coenzyme A synthetase ACSM3, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000306098|||http://purl.uniprot.org/annotation/VSP_028397 http://togogenome.org/gene/10090:Zbtb5 ^@ http://purl.uniprot.org/uniprot/Q7TQG0 ^@ 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|||Basic and acidic residues|||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_0000047714 http://togogenome.org/gene/10090:Ankib1 ^@ http://purl.uniprot.org/uniprot/Q6ZPS6 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Zinc Finger ^@ ANK 1|||ANK 2|||Ankyrin repeat and IBR domain-containing protein 1|||Basic and acidic residues|||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_0000066893 http://togogenome.org/gene/10090:Srek1 ^@ http://purl.uniprot.org/uniprot/Q8BZX4 ^@ 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.|||Phosphoserine|||Phosphothreonine|||RRM|||Splicing regulatory glutamine/lysine-rich protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000081941|||http://purl.uniprot.org/annotation/VSP_008400 http://togogenome.org/gene/10090:Glo1 ^@ http://purl.uniprot.org/uniprot/A5GZX3|||http://purl.uniprot.org/uniprot/Q9CPU0 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ Lactoylglutathione lyase|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphothreonine|||Proton donor/acceptor|||Removed|||S-glutathionyl cysteine|||VOC|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000168078 http://togogenome.org/gene/10090:Ces1b ^@ http://purl.uniprot.org/uniprot/D3Z5G7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Carboxylesterase type B|||Carboxylic ester hydrolase ^@ http://purl.uniprot.org/annotation/PRO_5005126416 http://togogenome.org/gene/10090:Ms4a8a ^@ http://purl.uniprot.org/uniprot/Q99N10 ^@ 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.|||Membrane-spanning 4-domains subfamily A member 8 ^@ http://purl.uniprot.org/annotation/PRO_0000158644|||http://purl.uniprot.org/annotation/VSP_053843 http://togogenome.org/gene/10090:Gps1 ^@ http://purl.uniprot.org/uniprot/B1ATU4|||http://purl.uniprot.org/uniprot/G3UXW9|||http://purl.uniprot.org/uniprot/Q3MIA8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PCI|||Polar residues ^@ http://togogenome.org/gene/10090:Igdcc3 ^@ http://purl.uniprot.org/uniprot/Q8BQC3 ^@ 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|||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|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014921|||http://purl.uniprot.org/annotation/VSP_012321 http://togogenome.org/gene/10090:Ssbp2 ^@ http://purl.uniprot.org/uniprot/Q540I3|||http://purl.uniprot.org/uniprot/Q9CYZ8 ^@ 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|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Single-stranded DNA-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000123827|||http://purl.uniprot.org/annotation/VSP_006259 http://togogenome.org/gene/10090:Prdm2 ^@ http://purl.uniprot.org/uniprot/A2A7B5|||http://purl.uniprot.org/uniprot/B9EKQ3|||http://purl.uniprot.org/uniprot/Q8C2W5 ^@ Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Crosslink|||Domain Extent|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Pro residues|||SET ^@ http://togogenome.org/gene/10090:Or7g22 ^@ http://purl.uniprot.org/uniprot/Q8VFJ4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gpr157 ^@ http://purl.uniprot.org/uniprot/Q148S2|||http://purl.uniprot.org/uniprot/Q8C206 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 157|||G-protein coupled receptors family 1 profile|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000070340 http://togogenome.org/gene/10090:F13a1 ^@ http://purl.uniprot.org/uniprot/Q3V3W7|||http://purl.uniprot.org/uniprot/Q8BH61 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Activation peptide|||Cleavage; by thrombin; to produce active factor XIII-A|||Coagulation factor XIII A chain|||Disordered|||N-acetylserine|||N-linked (GlcNAc...) asparagine|||Removed|||Transglutaminase-like ^@ http://purl.uniprot.org/annotation/PRO_0000033648|||http://purl.uniprot.org/annotation/PRO_0000033649 http://togogenome.org/gene/10090:Cartpt ^@ http://purl.uniprot.org/uniprot/P56388|||http://purl.uniprot.org/uniprot/Q3UYI4 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Modified Residue|||Peptide|||Signal Peptide|||Splice Variant ^@ CART(1-52)|||CART(55-102)|||CART(62-102)|||Cocaine- and amphetamine-regulated transcript protein|||In isoform Short.|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000004436|||http://purl.uniprot.org/annotation/PRO_0000004437|||http://purl.uniprot.org/annotation/PRO_0000004438|||http://purl.uniprot.org/annotation/PRO_0000004439|||http://purl.uniprot.org/annotation/PRO_5004230401|||http://purl.uniprot.org/annotation/VSP_000793 http://togogenome.org/gene/10090:Tmed1 ^@ http://purl.uniprot.org/uniprot/B2RRM5|||http://purl.uniprot.org/uniprot/Q3V009 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Motif|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||Extracellular|||GOLD|||Helical|||In isoform 2.|||Transmembrane emp24 domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000248020|||http://purl.uniprot.org/annotation/PRO_5014298354|||http://purl.uniprot.org/annotation/VSP_020135|||http://purl.uniprot.org/annotation/VSP_020136 http://togogenome.org/gene/10090:Ric3 ^@ http://purl.uniprot.org/uniprot/D3YTZ9|||http://purl.uniprot.org/uniprot/Q8BPM6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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 isoform 2.|||In isoform 3.|||Lumenal|||N6-acetyllysine; alternate|||Protein RIC-3|||Resistance to inhibitors of cholinesterase protein 3 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000302732|||http://purl.uniprot.org/annotation/VSP_027944|||http://purl.uniprot.org/annotation/VSP_027945|||http://purl.uniprot.org/annotation/VSP_027946 http://togogenome.org/gene/10090:Polr3f ^@ http://purl.uniprot.org/uniprot/Q921X6 ^@ Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand ^@ Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Strand ^@ DNA-directed RNA polymerase III subunit RPC6|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073973 http://togogenome.org/gene/10090:Bloc1s1 ^@ http://purl.uniprot.org/uniprot/O55102 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Sequence Conflict ^@ Biogenesis of lysosome-related organelles complex 1 subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000156332 http://togogenome.org/gene/10090:Creb3 ^@ http://purl.uniprot.org/uniprot/Q3UNH6 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ BZIP|||Disordered ^@ http://togogenome.org/gene/10090:Fasl ^@ http://purl.uniprot.org/uniprot/P41047|||http://purl.uniprot.org/uniprot/Q544E9|||http://purl.uniprot.org/uniprot/Q99PH8 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ ADAM10-processed FasL form|||Cleavage; by ADAM10|||Cleavage; by SPPL2A|||Cytoplasmic|||Disordered|||Extracellular|||FasL intracellular domain|||Helical|||Helical; Signal-anchor for type II membrane protein|||In gld; abolishes binding of FASL to its receptor.|||In isoform FasLS.|||In strain: BALB/c, DBA/1 and DBA/2; enhances cytotoxicity.|||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_0000034508|||http://purl.uniprot.org/annotation/PRO_0000034509|||http://purl.uniprot.org/annotation/PRO_0000417159|||http://purl.uniprot.org/annotation/PRO_0000417160|||http://purl.uniprot.org/annotation/VSP_006445 http://togogenome.org/gene/10090:Gls ^@ http://purl.uniprot.org/uniprot/D3Z7P3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ ANK 1|||ANK 2|||Abolishes assembly of dimers into functional tetramers. Loss of enzyme activity. Forms oligomers with full, phosphate-independent activity; when associated with A-325. Forms dimers with full, phosphate-independent activity; when associated with Q-316 and A-325.|||Cleavage; by MPP|||Constitutive enzyme activity that is fully active also in the absence phosphate. Forms oligomers with full, phosphate-independent activity; when associated with K-391. Forms dimers with full, phosphate-independent activity; when associated with Q-316 and K-391.|||Disordered|||Forms dimers with full, phosphate-independent activity; when associated with A-325 and K-391.|||Glutaminase kidney isoform, mitochondrial 65 kDa chain|||Glutaminase kidney isoform, mitochondrial 68 kDa chain|||Highly mobile activation loop|||Impairs tetramerization and promotes formation of homodimers. Impairs activation by phosphate.|||In isoform 2.|||Increased enzyme activity in the absence of phosphate. No effect on stimulation of enzyme activity by phosphate.|||Increased stimulation of enzyme activity by phosphate.|||Loss of enzyme activity.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000417583|||http://purl.uniprot.org/annotation/PRO_0000447413|||http://purl.uniprot.org/annotation/VSP_043804 http://togogenome.org/gene/10090:Clpx ^@ http://purl.uniprot.org/uniprot/Q6P8N8|||http://purl.uniprot.org/uniprot/Q8C4Z5|||http://purl.uniprot.org/uniprot/Q9JHS4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial|||Basic and acidic residues|||ClpX-type ZB|||Disordered|||Loss of ATP hydrolysis.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000005519 http://togogenome.org/gene/10090:Plscr3 ^@ http://purl.uniprot.org/uniprot/Q5F283|||http://purl.uniprot.org/uniprot/Q9JIZ9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Complete loss of palmitoylation, mislocalization from mitochondrial membrane and reduced apoptotic function; when associated with A-159, A-161, A-163 and A-166.|||Complete loss of palmitoylation, mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function; when associated with A-159, A-161, A-163 and A-164.|||Complete loss of palmitoylation, mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function; when associated with A-159, A-161, A-164 and A-166.|||Complete loss of palmitoylation, mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function; when associated with A-159, A-163, A-164 and A-166. Partial loss of palmitoylation; when associated with A-159.|||Complete loss of palmitoylation, mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function; when associated with A-161, A-163, A-164 and A-166. Partial loss of palmitoylation; when associated with A-161.|||Disordered|||Helical|||Mitochondrial intermembrane|||PPxY motif|||Phospholipid scramblase 3|||Pro residues|||Proline-rich domain (PRD)|||S-palmitoyl cysteine|||SH3-binding 1|||SH3-binding 2|||SH3-binding 3 ^@ http://purl.uniprot.org/annotation/PRO_0000100790 http://togogenome.org/gene/10090:Polr1f ^@ http://purl.uniprot.org/uniprot/B2RT77|||http://purl.uniprot.org/uniprot/Q78WZ7 ^@ 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 ^@ DNA-directed RNA polymerase I subunit RPA43|||Disordered|||Phosphoserine|||Polar residues|||RPA43 OB ^@ http://purl.uniprot.org/annotation/PRO_0000288633 http://togogenome.org/gene/10090:Mapk1 ^@ http://purl.uniprot.org/uniprot/P63085 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif ^@ Mitogen-activated protein kinase 1|||N-acetylalanine|||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_0000186248 http://togogenome.org/gene/10090:Serpine2 ^@ http://purl.uniprot.org/uniprot/Q07235|||http://purl.uniprot.org/uniprot/Q543R5 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site ^@ Glia-derived nexin|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Serpin|||Serpin domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000032505|||http://purl.uniprot.org/annotation/PRO_5014309560 http://togogenome.org/gene/10090:Vmn1r242 ^@ http://purl.uniprot.org/uniprot/K9J7G4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pawr ^@ http://purl.uniprot.org/uniprot/Q925B0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Splice Variant ^@ B30.2/SPRY domain-binding motif|||Basic and acidic residues|||Disordered|||In isoform 2.|||Leucine-zipper|||Nuclear localization signal|||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_0000058237|||http://purl.uniprot.org/annotation/VSP_022018 http://togogenome.org/gene/10090:Or52n2c ^@ http://purl.uniprot.org/uniprot/Q8VGW3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cngb1 ^@ http://purl.uniprot.org/uniprot/E1AZ71|||http://purl.uniprot.org/uniprot/E9PXX0|||http://purl.uniprot.org/uniprot/Q80VQ4|||http://purl.uniprot.org/uniprot/Q80XL8|||http://purl.uniprot.org/uniprot/Q91WA8 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cyclic nucleotide-binding|||Disordered|||Helical|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Akp3 ^@ http://purl.uniprot.org/uniprot/F8VQM0|||http://purl.uniprot.org/uniprot/Q1LZM2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Signal Peptide ^@ Alkaline phosphatase|||Disordered|||Phosphoserine intermediate|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003379323|||http://purl.uniprot.org/annotation/PRO_5004193585 http://togogenome.org/gene/10090:Slc36a4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Q3|||http://purl.uniprot.org/uniprot/Q8CH36 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Amino acid transporter transmembrane|||Helical|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Neutral amino acid uniporter 4 ^@ http://purl.uniprot.org/annotation/PRO_0000308319 http://togogenome.org/gene/10090:Aamdc ^@ http://purl.uniprot.org/uniprot/D3YZD8|||http://purl.uniprot.org/uniprot/D3Z1Q3|||http://purl.uniprot.org/uniprot/Q8R0P4 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Region|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||MTH138-like domain|||Mth938 domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000239815|||http://purl.uniprot.org/annotation/PRO_5015088510|||http://purl.uniprot.org/annotation/PRO_5015088523|||http://purl.uniprot.org/annotation/VSP_019270 http://togogenome.org/gene/10090:Fads2 ^@ http://purl.uniprot.org/uniprot/Q9Z0R9 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Acyl-CoA 6-desaturase|||Cytochrome b5 heme-binding|||Cytoplasmic|||Disordered|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000307103 http://togogenome.org/gene/10090:Map3k5 ^@ http://purl.uniprot.org/uniprot/O35099 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Disordered|||Interaction with PPIA/CYPA|||Mitogen-activated protein kinase kinase kinase 5|||Phosphoserine|||Phosphoserine; by PIM1 and PKB/AKT1|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Phosphothreonine; by autocatalysis, MELK and MAP3K6|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086250 http://togogenome.org/gene/10090:Spta1 ^@ http://purl.uniprot.org/uniprot/P08032 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||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_0000073453 http://togogenome.org/gene/10090:Gstm6 ^@ http://purl.uniprot.org/uniprot/O35660 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 6 ^@ http://purl.uniprot.org/annotation/PRO_0000185830 http://togogenome.org/gene/10090:Dgcr6 ^@ http://purl.uniprot.org/uniprot/O35347 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Protein DGCR6 ^@ http://purl.uniprot.org/annotation/PRO_0000070261|||http://purl.uniprot.org/annotation/VSP_001827|||http://purl.uniprot.org/annotation/VSP_001828 http://togogenome.org/gene/10090:Zfp637 ^@ http://purl.uniprot.org/uniprot/Q05CR8|||http://purl.uniprot.org/uniprot/Q80V23 ^@ 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 ^@ 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; degenerate|||Disordered|||In isoform 2.|||Zinc finger protein 32 ^@ http://purl.uniprot.org/annotation/PRO_0000047362|||http://purl.uniprot.org/annotation/VSP_016954 http://togogenome.org/gene/10090:Arhgef19 ^@ http://purl.uniprot.org/uniprot/Q8BWA8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ DH|||Disordered|||PH|||Polar residues|||Rho guanine nucleotide exchange factor 19|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000285132 http://togogenome.org/gene/10090:Napg ^@ http://purl.uniprot.org/uniprot/Q9CWZ7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Gamma-soluble NSF attachment protein|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000219064 http://togogenome.org/gene/10090:Fh1 ^@ http://purl.uniprot.org/uniprot/P97807 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Fumarate hydratase, mitochondrial|||Important for catalytic activity|||In isoform Cytoplasmic.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Proton donor/acceptor|||Removed|||in site B ^@ http://purl.uniprot.org/annotation/PRO_0000010323|||http://purl.uniprot.org/annotation/VSP_018967 http://togogenome.org/gene/10090:Itgb4 ^@ http://purl.uniprot.org/uniprot/A2A863|||http://purl.uniprot.org/uniprot/A2A864 ^@ Binding Site|||Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Calx-beta|||Cell attachment site|||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 isoform 2 and isoform 3.|||In isoform 3.|||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_0000379078|||http://purl.uniprot.org/annotation/PRO_5015086010|||http://purl.uniprot.org/annotation/VSP_037636|||http://purl.uniprot.org/annotation/VSP_037637 http://togogenome.org/gene/10090:Skint9 ^@ http://purl.uniprot.org/uniprot/A7TZG3 ^@ 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|||Helical|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Selection and upkeep of intraepithelial T-cells protein 9 ^@ http://purl.uniprot.org/annotation/PRO_5000270118 http://togogenome.org/gene/10090:Lamtor3 ^@ http://purl.uniprot.org/uniprot/O88653 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Region|||Strand|||Turn ^@ Ragulator complex protein LAMTOR3|||Required for interaction with LAMTOR2 ^@ http://purl.uniprot.org/annotation/PRO_0000221006 http://togogenome.org/gene/10090:Adsl ^@ http://purl.uniprot.org/uniprot/P54822 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Adenylosuccinate lyase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||N-acetylalanine|||N6-acetyllysine|||Proton donor/acceptor|||Removed|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000137894 http://togogenome.org/gene/10090:Pygl ^@ http://purl.uniprot.org/uniprot/Q9ET01 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site ^@ Glycogen phosphorylase, liver form|||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_0000188525 http://togogenome.org/gene/10090:Fcgr2b ^@ http://purl.uniprot.org/uniprot/A0A0B4J1E6|||http://purl.uniprot.org/uniprot/A0A0B4J1G1|||http://purl.uniprot.org/uniprot/P08101 ^@ 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|||Disordered|||Extracellular|||Helical|||ITIM motif|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform IIB1'.|||In isoform IIB2.|||In strain: DBA/2; Ly17.2 allotype.|||In strain: NZB.|||In strain: NZB; Ly17.1 allotype.|||Low affinity immunoglobulin gamma Fc region receptor II|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Phosphotyrosine; by SRC-type Tyr-kinases|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000015143|||http://purl.uniprot.org/annotation/VSP_002640|||http://purl.uniprot.org/annotation/VSP_002641 http://togogenome.org/gene/10090:Cd300lb ^@ http://purl.uniprot.org/uniprot/A0A0R3P9D2|||http://purl.uniprot.org/uniprot/Q3TEQ8|||http://purl.uniprot.org/uniprot/Q3U497 ^@ 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 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ CMRF35-like molecule 7|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||Immunoglobulin subtype|||In strain: C57BL/6.|||Interaction with TYROBP|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000320131 http://togogenome.org/gene/10090:Tnks2 ^@ http://purl.uniprot.org/uniprot/Q3UES3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ (3S)-3-hydroxyasparagine; by HIF1AN|||(3S)-3-hydroxyhistidine; by HIF1AN|||ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||HIF1AN-binding|||PARP catalytic|||Poly [ADP-ribose] polymerase tankyrase-2|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000409512 http://togogenome.org/gene/10090:Pf4 ^@ http://purl.uniprot.org/uniprot/Q3TVN6|||http://purl.uniprot.org/uniprot/Q6P8R3|||http://purl.uniprot.org/uniprot/Q9Z126 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide ^@ C-X-C motif chemokine|||Chemokine interleukin-8-like|||O-linked (GalNAc...) threonine|||Phosphoserine|||Platelet factor 4 ^@ http://purl.uniprot.org/annotation/PRO_0000005069|||http://purl.uniprot.org/annotation/PRO_5005144099|||http://purl.uniprot.org/annotation/PRO_5015020009 http://togogenome.org/gene/10090:Nckap1l ^@ http://purl.uniprot.org/uniprot/Q8K1X4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Nck-associated protein 1-like ^@ http://purl.uniprot.org/annotation/PRO_0000439210 http://togogenome.org/gene/10090:Gm1673 ^@ http://purl.uniprot.org/uniprot/Q3UR78 ^@ Chain|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||NELL2-interacting cell ontogeny regulator 1 ^@ http://purl.uniprot.org/annotation/PRO_0000342195|||http://purl.uniprot.org/annotation/VSP_034397 http://togogenome.org/gene/10090:Rmi1 ^@ http://purl.uniprot.org/uniprot/Q9D4G9 ^@ 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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Polar residues|||RecQ-mediated genome instability protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000227547 http://togogenome.org/gene/10090:Nmnat1 ^@ http://purl.uniprot.org/uniprot/Q3V449|||http://purl.uniprot.org/uniprot/Q9EPA7 ^@ 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|||Region ^@ Cytidyltransferase-like|||Decrease in enzyme activity. Has no axonal protective effect. Does not affect ability to promotze glutamate and aspartate ADP-ribosylation.|||Disordered|||Locates to the cytoplasm. Has no effect on enzyme activity or axonal protection.|||Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1|||Nuclear localization signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000135013 http://togogenome.org/gene/10090:Ces2g ^@ http://purl.uniprot.org/uniprot/E9PV38 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Carboxylesterase type B|||Carboxylic ester hydrolase ^@ http://purl.uniprot.org/annotation/PRO_5005128626 http://togogenome.org/gene/10090:Asic5 ^@ http://purl.uniprot.org/uniprot/D3Z0S5|||http://purl.uniprot.org/uniprot/Q9R0Y1 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Acid-sensing ion channel 5|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000335598 http://togogenome.org/gene/10090:Gfi1b ^@ http://purl.uniprot.org/uniprot/B7ZNH2|||http://purl.uniprot.org/uniprot/O70237 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Abrogates interaction with NCOR1 and KDM1A. Greatly diminished interaction with HDAC2. Loss of ability to promote erythrocyte and granulocyte differentiation.|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Interaction with ARIH2|||Mediates interaction with GATA1|||N6,N6-dimethyllysine|||SNAG domain|||Zinc finger protein Gfi-1b ^@ http://purl.uniprot.org/annotation/PRO_0000306328 http://togogenome.org/gene/10090:Tcl1b1 ^@ http://purl.uniprot.org/uniprot/P56840 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein TCL1B1 ^@ http://purl.uniprot.org/annotation/PRO_0000184491 http://togogenome.org/gene/10090:Uxs1 ^@ http://purl.uniprot.org/uniprot/Q91XL3 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Proton acceptor|||UDP-glucuronic acid decarboxylase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000183270 http://togogenome.org/gene/10090:Clcc1 ^@ http://purl.uniprot.org/uniprot/A2AEM2|||http://purl.uniprot.org/uniprot/Q99LI2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Chloride channel CLIC-like protein 1|||Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000297683|||http://purl.uniprot.org/annotation/PRO_5015086018 http://togogenome.org/gene/10090:Cbx4 ^@ http://purl.uniprot.org/uniprot/O55187 ^@ 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|||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.|||N6-acetyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000080207|||http://purl.uniprot.org/annotation/VSP_022009 http://togogenome.org/gene/10090:Snrnp25 ^@ http://purl.uniprot.org/uniprot/Q8VIK1 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand ^@ U11/U12 small nuclear ribonucleoprotein 25 kDa protein|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000114925 http://togogenome.org/gene/10090:Dusp3 ^@ http://purl.uniprot.org/uniprot/Q9D7X3 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ Dual specificity protein phosphatase 3|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094796 http://togogenome.org/gene/10090:Ugt8a ^@ http://purl.uniprot.org/uniprot/Q64676 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ 2-hydroxyacylsphingosine 1-beta-galactosyltransferase|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000036065 http://togogenome.org/gene/10090:Mrps24 ^@ http://purl.uniprot.org/uniprot/Q9CQV5 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||Small ribosomal subunit protein uS3m ^@ http://purl.uniprot.org/annotation/PRO_0000273067 http://togogenome.org/gene/10090:Drp2 ^@ http://purl.uniprot.org/uniprot/Q05AA6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Dystrophin-related protein 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Spectrin 1|||Spectrin 2|||WW|||ZZ-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000345015 http://togogenome.org/gene/10090:Pbld1 ^@ http://purl.uniprot.org/uniprot/Q9DCG6 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Sequence Conflict ^@ Phenazine biosynthesis-like domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000162385 http://togogenome.org/gene/10090:Lamp2 ^@ http://purl.uniprot.org/uniprot/P17047|||http://purl.uniprot.org/uniprot/Q8C5K0 ^@ 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|||First lumenal domain|||Helical|||Hinge|||Important for binding and subsequent lysosomal degradation of target proteins|||In isoform LAMP-2B.|||In isoform LAMP-2C.|||Lumenal|||Lysosome-associated membrane glycoprotein 2|||N-linked (GlcNAc...) asparagine|||Second lumenal domain ^@ http://purl.uniprot.org/annotation/PRO_0000017111|||http://purl.uniprot.org/annotation/PRO_5015099069|||http://purl.uniprot.org/annotation/VSP_003045|||http://purl.uniprot.org/annotation/VSP_003046 http://togogenome.org/gene/10090:Or10al6 ^@ http://purl.uniprot.org/uniprot/Q7TRJ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp386 ^@ http://purl.uniprot.org/uniprot/Q1WWJ5|||http://purl.uniprot.org/uniprot/Q3TN43 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:H2-T24 ^@ http://purl.uniprot.org/uniprot/F8VQG4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5003379460 http://togogenome.org/gene/10090:Stox2 ^@ http://purl.uniprot.org/uniprot/Q499E5 ^@ 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 residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Polar residues|||Storkhead-box protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000313631|||http://purl.uniprot.org/annotation/VSP_030074|||http://purl.uniprot.org/annotation/VSP_030075|||http://purl.uniprot.org/annotation/VSP_030076 http://togogenome.org/gene/10090:Apol7a ^@ http://purl.uniprot.org/uniprot/B2RT54|||http://purl.uniprot.org/uniprot/Q8BUC6|||http://purl.uniprot.org/uniprot/Q9D2Y0 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Mnx1 ^@ http://purl.uniprot.org/uniprot/A2RSX2 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Ipcef1 ^@ http://purl.uniprot.org/uniprot/Q3UX69|||http://purl.uniprot.org/uniprot/Q5DU31 ^@ 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.|||Interactor protein for cytohesin exchange factors 1|||PH|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000326631|||http://purl.uniprot.org/annotation/VSP_032683|||http://purl.uniprot.org/annotation/VSP_032684|||http://purl.uniprot.org/annotation/VSP_032685 http://togogenome.org/gene/10090:Fam76a ^@ http://purl.uniprot.org/uniprot/Q922G2 ^@ 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|||Disordered|||In isoform 2.|||Polar residues|||Protein FAM76A ^@ http://purl.uniprot.org/annotation/PRO_0000245761|||http://purl.uniprot.org/annotation/VSP_019773 http://togogenome.org/gene/10090:Ppp1r35 ^@ http://purl.uniprot.org/uniprot/Q9D8C8 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic residues|||Disordered|||Phosphoserine|||Pro residues|||Protein phosphatase 1 regulatory subunit 35 ^@ http://purl.uniprot.org/annotation/PRO_0000358929 http://togogenome.org/gene/10090:Ogn ^@ http://purl.uniprot.org/uniprot/Q543C5|||http://purl.uniprot.org/uniprot/Q62000 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000032761|||http://purl.uniprot.org/annotation/PRO_5014309541 http://togogenome.org/gene/10090:Or6c2 ^@ http://purl.uniprot.org/uniprot/Q8VGJ0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Psors1c2 ^@ http://purl.uniprot.org/uniprot/Q3UUY0|||http://purl.uniprot.org/uniprot/Q80ZC9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Disordered|||Pro residues|||Psoriasis susceptibility 1 candidate gene 2 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000022160|||http://purl.uniprot.org/annotation/PRO_5015097503 http://togogenome.org/gene/10090:Phtf2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Q1|||http://purl.uniprot.org/uniprot/Q8C9D2|||http://purl.uniprot.org/uniprot/Q8CB19 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||PHTF|||PHTF1/2 N-terminal|||Polar residues|||Protein PHTF2 ^@ http://purl.uniprot.org/annotation/PRO_0000318510 http://togogenome.org/gene/10090:Tifa ^@ http://purl.uniprot.org/uniprot/I3PQW8|||http://purl.uniprot.org/uniprot/Q793I8 ^@ 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 ^@ Disordered|||FHA|||Phosphothreonine|||Polar residues|||TRAF-interacting protein with FHA domain-containing protein A ^@ http://purl.uniprot.org/annotation/PRO_0000320690 http://togogenome.org/gene/10090:Lnpk ^@ http://purl.uniprot.org/uniprot/A2ASL8|||http://purl.uniprot.org/uniprot/Q7TQ95 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Topological Domain|||Transmembrane|||Zinc Finger ^@ C4-type; plays a role in ER morphology|||Cytoplasmic|||Disordered|||Endoplasmic reticulum junction formation protein lunapark|||Helical|||Lumenal|||Lunapark|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000248311 http://togogenome.org/gene/10090:Rftn2 ^@ http://purl.uniprot.org/uniprot/Q8CHX7 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Raftlin-2|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000089339|||http://purl.uniprot.org/annotation/VSP_015324|||http://purl.uniprot.org/annotation/VSP_015325 http://togogenome.org/gene/10090:Or6k14 ^@ http://purl.uniprot.org/uniprot/E9Q7E7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Qtrt1 ^@ http://purl.uniprot.org/uniprot/Q9JMA2 ^@ Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn ^@ N-acetylalanine|||Nucleophile|||Phosphoserine|||Proton acceptor|||Queuine tRNA-ribosyltransferase catalytic subunit 1|||RNA binding|||RNA binding; important for wobble base 34 recognition|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000135566 http://togogenome.org/gene/10090:Cd5 ^@ http://purl.uniprot.org/uniprot/P13379|||http://purl.uniprot.org/uniprot/Q3UP78 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SRCR|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR domain-containing protein|||T-cell surface glycoprotein CD5 ^@ http://purl.uniprot.org/annotation/PRO_0000033223|||http://purl.uniprot.org/annotation/PRO_5009970838 http://togogenome.org/gene/10090:Zfp979 ^@ http://purl.uniprot.org/uniprot/A2A799 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Epsti1 ^@ http://purl.uniprot.org/uniprot/A0A140T8I6|||http://purl.uniprot.org/uniprot/Q8VDI1|||http://purl.uniprot.org/uniprot/Q9D3Q7 ^@ 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|||Epithelial-stromal interaction protein 1|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314035|||http://purl.uniprot.org/annotation/VSP_030203|||http://purl.uniprot.org/annotation/VSP_030204 http://togogenome.org/gene/10090:Gm13304 ^@ http://purl.uniprot.org/uniprot/P86792|||http://purl.uniprot.org/uniprot/P86793 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Region|||Sequence Conflict|||Signal Peptide ^@ C-C motif chemokine 21b|||C-C motif chemokine 21c|||C-terminal basic extension|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000005222|||http://purl.uniprot.org/annotation/PRO_0000403422 http://togogenome.org/gene/10090:Mov10l1 ^@ http://purl.uniprot.org/uniprot/D3YWG8|||http://purl.uniprot.org/uniprot/G3X8T0|||http://purl.uniprot.org/uniprot/Q99MV5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 1|||2|||3|||4|||5|||5 X 11 AA tandem repeats of [TI]-R-N-[DN]-[GS]-Q-[SP]-I-T-[NK]-[IVN]|||Basic and acidic residues|||Catalytically inactive mutant. Homozygous knockin male mice are sterile and display meiotic arrest at the zygotene-like stage of prophase I. LINE1 retrotransposons are derepressed and piRNA biogenesis is abolished.|||DEAG box|||DNA2/NAM7 helicase helicase|||DNA2/NAM7 helicase-like C-terminal|||Disordered|||In isoform 2.|||In isoform 3.|||Isoform 2: Abolishes the suppressor of cell proliferation activity.|||RNA helicase Mov10l1 ^@ http://purl.uniprot.org/annotation/PRO_0000080707|||http://purl.uniprot.org/annotation/VSP_003392|||http://purl.uniprot.org/annotation/VSP_010949 http://togogenome.org/gene/10090:Nfkb2 ^@ http://purl.uniprot.org/uniprot/Q3UG25|||http://purl.uniprot.org/uniprot/Q3UV15|||http://purl.uniprot.org/uniprot/Q9WTK5 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Site|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Site|||Strand|||Turn ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Cleavage (when cotranslationally processed)|||Death|||Disordered|||GRR|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Nuclear factor NF-kappa-B p100 subunit|||Nuclear factor NF-kappa-B p52 subunit|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by MAP3K14|||Phosphothreonine|||RHD ^@ http://purl.uniprot.org/annotation/PRO_0000030323|||http://purl.uniprot.org/annotation/PRO_0000030324 http://togogenome.org/gene/10090:Coro1a ^@ http://purl.uniprot.org/uniprot/O89053|||http://purl.uniprot.org/uniprot/Q3U1N0 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ Coronin-1A|||DUF1899|||Disordered|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000050921 http://togogenome.org/gene/10090:Tdh ^@ http://purl.uniprot.org/uniprot/Q8K3F7 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Decreased L-threonine 3-dehydrogenase activity.|||Decreased L-threonine 3-dehydrogenase activity. Decreased affinity for L-threonine.|||Decreased L-threonine 3-dehydrogenase activity. No effect on protein NAD(+)-binding. No gross effect on protein folding. No effect on protein stability.|||L-threonine 3-dehydrogenase, mitochondrial|||Mitochondrion|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000298784 http://togogenome.org/gene/10090:Or52s6 ^@ http://purl.uniprot.org/uniprot/E9Q838|||http://purl.uniprot.org/uniprot/Q7TRR0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fxn ^@ http://purl.uniprot.org/uniprot/O35943 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Extramitochondrial frataxin|||Frataxin intermediate form|||Frataxin mature form|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000010132|||http://purl.uniprot.org/annotation/PRO_0000399390|||http://purl.uniprot.org/annotation/PRO_0000456949 http://togogenome.org/gene/10090:Gpr4 ^@ http://purl.uniprot.org/uniprot/Q8BUD0 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000379519 http://togogenome.org/gene/10090:Abca15 ^@ http://purl.uniprot.org/uniprot/Q6XBG2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ ABC transporter|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Sfmbt2 ^@ http://purl.uniprot.org/uniprot/Q3UH07|||http://purl.uniprot.org/uniprot/Q3UH63|||http://purl.uniprot.org/uniprot/Q8BG70 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Basic and acidic residues|||Basic residues|||Disordered|||MBT|||Polar residues|||SAM ^@ http://togogenome.org/gene/10090:Gpr15lg ^@ http://purl.uniprot.org/uniprot/A0A0B4J1N3 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Protein GPR15LG ^@ http://purl.uniprot.org/annotation/PRO_5010906477 http://togogenome.org/gene/10090:Oxsr1 ^@ http://purl.uniprot.org/uniprot/Q6P9R2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Impaired phosphorylation by WNK4 and activation. Knockin mice are unable to activate SLC12A3/NCC.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by WNK1|||Phosphothreonine|||Phosphothreonine; by WNK4|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase OSR1 ^@ http://purl.uniprot.org/annotation/PRO_0000086457 http://togogenome.org/gene/10090:Cchcr1 ^@ http://purl.uniprot.org/uniprot/G3UWS7|||http://purl.uniprot.org/uniprot/Q3TWA2|||http://purl.uniprot.org/uniprot/Q8K2I2 ^@ 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|||Coiled-coil alpha-helical rod protein 1|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089417 http://togogenome.org/gene/10090:Trim68 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSL9|||http://purl.uniprot.org/uniprot/G3X9I6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ B box-type|||B30.2/SPRY|||RING-type ^@ http://togogenome.org/gene/10090:Mat1a ^@ http://purl.uniprot.org/uniprot/Q91X83 ^@ Binding Site|||Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Region ^@ Flexible loop|||S-adenosylmethionine synthase isoform type-1|||S-nitrosocysteine|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000174433 http://togogenome.org/gene/10090:Samt1 ^@ http://purl.uniprot.org/uniprot/A2BED8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Defa17 ^@ http://purl.uniprot.org/uniprot/P28310 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Alpha-defensin 3|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000006821|||http://purl.uniprot.org/annotation/PRO_0000006822 http://togogenome.org/gene/10090:Cdc42ep3 ^@ http://purl.uniprot.org/uniprot/Q9CQC5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ CRIB|||Cdc42 effector protein 3|||Disordered|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000212652 http://togogenome.org/gene/10090:Kntc1 ^@ http://purl.uniprot.org/uniprot/Q8C3Y4 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Kinetochore-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000084313 http://togogenome.org/gene/10090:Atg10 ^@ http://purl.uniprot.org/uniprot/Q8R1P4 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Mutagenesis Site|||Sequence Conflict ^@ Glycyl thioester intermediate|||Instead of the formation of an intermediate complex with a thiol ester bond between ATG10 (E2-like enzyme) and ATG12 (substrate), a stable complex with an O-ester bond is formed. Does not affect ATG12 conjugation to ATG3.|||Ubiquitin-like-conjugating enzyme ATG10 ^@ http://purl.uniprot.org/annotation/PRO_0000096184 http://togogenome.org/gene/10090:Gdi2 ^@ http://purl.uniprot.org/uniprot/Q3UPA3|||http://purl.uniprot.org/uniprot/Q61598 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Non-terminal 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_0000056680|||http://purl.uniprot.org/annotation/VSP_010579 http://togogenome.org/gene/10090:Mapk8 ^@ http://purl.uniprot.org/uniprot/A6P3E4|||http://purl.uniprot.org/uniprot/G3X8U9|||http://purl.uniprot.org/uniprot/Q544A0|||http://purl.uniprot.org/uniprot/Q7TSJ7|||http://purl.uniprot.org/uniprot/Q91Y86 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Disordered|||Mitogen-activated protein kinase 8|||Phosphoserine|||Phosphothreonine; by MAP2K7|||Phosphotyrosine; by MAP2K4|||Polar residues|||Protein kinase|||Proton acceptor|||S-nitrosocysteine|||TXY ^@ http://purl.uniprot.org/annotation/PRO_0000186263 http://togogenome.org/gene/10090:Vmn2r48 ^@ http://purl.uniprot.org/uniprot/E9Q5D8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://togogenome.org/gene/10090:Styxl2 ^@ http://purl.uniprot.org/uniprot/Q148W8 ^@ 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|||Phosphothreonine|||Polar residues|||Serine/threonine/tyrosine-interacting-like protein 2|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000302839 http://togogenome.org/gene/10090:Tspan5 ^@ http://purl.uniprot.org/uniprot/D3Z641|||http://purl.uniprot.org/uniprot/P62080 ^@ 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_0000219244 http://togogenome.org/gene/10090:Prss37 ^@ http://purl.uniprot.org/uniprot/Q9DAA4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ Peptidase S1|||Probable inactive serine protease 37 ^@ http://purl.uniprot.org/annotation/PRO_0000326072 http://togogenome.org/gene/10090:Svopl ^@ http://purl.uniprot.org/uniprot/Q6PDF3 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Putative transporter SVOPL ^@ http://purl.uniprot.org/annotation/PRO_0000294462|||http://purl.uniprot.org/annotation/VSP_026653|||http://purl.uniprot.org/annotation/VSP_026654 http://togogenome.org/gene/10090:Mef2b ^@ http://purl.uniprot.org/uniprot/Q80VR4 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||MADS-box ^@ http://togogenome.org/gene/10090:Or9s15 ^@ http://purl.uniprot.org/uniprot/Q8VFC4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccnb1 ^@ http://purl.uniprot.org/uniprot/P24860|||http://purl.uniprot.org/uniprot/Q3TQW9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Cyclin N-terminal|||G2/mitotic-specific cyclin-B1|||Interaction with CDK2|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by PLK1|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000080352 http://togogenome.org/gene/10090:Slc25a18 ^@ http://purl.uniprot.org/uniprot/Q9DB41 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane ^@ Chain|||Modified Residue|||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.|||Mitochondrial glutamate carrier 2|||Phosphoserine|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090622|||http://purl.uniprot.org/annotation/VSP_022262 http://togogenome.org/gene/10090:Txndc17 ^@ http://purl.uniprot.org/uniprot/Q9CQM5 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site|||Strand ^@ Contributes to redox potential value|||N-acetylalanine|||Nucleophile|||Redox-active|||Removed|||Thioredoxin|||Thioredoxin domain-containing protein 17 ^@ http://purl.uniprot.org/annotation/PRO_0000120023 http://togogenome.org/gene/10090:Cadm1 ^@ http://purl.uniprot.org/uniprot/E9PYN1|||http://purl.uniprot.org/uniprot/Q8R5M8 ^@ 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 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.|||In isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000291969|||http://purl.uniprot.org/annotation/PRO_5015090360|||http://purl.uniprot.org/annotation/VSP_052463|||http://purl.uniprot.org/annotation/VSP_052464|||http://purl.uniprot.org/annotation/VSP_052465|||http://purl.uniprot.org/annotation/VSP_052466|||http://purl.uniprot.org/annotation/VSP_052467|||http://purl.uniprot.org/annotation/VSP_052468|||http://purl.uniprot.org/annotation/VSP_052469|||http://purl.uniprot.org/annotation/VSP_052470 http://togogenome.org/gene/10090:Tmem45a2 ^@ http://purl.uniprot.org/uniprot/B7ZWJ5|||http://purl.uniprot.org/uniprot/Q8CEZ6 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Ift27 ^@ http://purl.uniprot.org/uniprot/Q9D0P8 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Intraflagellar transport protein 27 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000082716 http://togogenome.org/gene/10090:Rpain ^@ http://purl.uniprot.org/uniprot/J3QN46|||http://purl.uniprot.org/uniprot/Q0PL79|||http://purl.uniprot.org/uniprot/Q0PL81|||http://purl.uniprot.org/uniprot/Q0PL82|||http://purl.uniprot.org/uniprot/Q9CWY9 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ Mediates nuclear export|||Phosphoserine|||RIP-type|||RPA-interacting protein|||RPA-interacting protein N-terminal|||RPA-interacting protein central ^@ http://purl.uniprot.org/annotation/PRO_0000076300 http://togogenome.org/gene/10090:Hcrtr2 ^@ http://purl.uniprot.org/uniprot/P58308 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||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|||Important for responses to orexin|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Orexin receptor type 2|||Required for response to orexin-A ^@ http://purl.uniprot.org/annotation/PRO_0000069990|||http://purl.uniprot.org/annotation/VSP_016466 http://togogenome.org/gene/10090:Efna5 ^@ http://purl.uniprot.org/uniprot/O08543 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Disordered|||Ephrin RBD|||Ephrin-A5|||GPI-anchor amidated asparagine|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000008379|||http://purl.uniprot.org/annotation/PRO_0000008380|||http://purl.uniprot.org/annotation/VSP_001449 http://togogenome.org/gene/10090:Rpp38 ^@ http://purl.uniprot.org/uniprot/A2AJG0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic residues|||Disordered|||Ribosomal protein eL8/eL30/eS12/Gadd45 ^@ http://togogenome.org/gene/10090:Nol3 ^@ http://purl.uniprot.org/uniprot/Q53YU5|||http://purl.uniprot.org/uniprot/Q9D1X0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region ^@ Acidic residues|||CARD|||Disordered|||Essential for interaction with BAX|||N-myristoyl glycine|||Nucleolar protein 3|||Phosphothreonine; by CK2|||Removed|||Unable to inhibit TNF-induced necrosis; when associated with F-31. Unable to induce TNF nuclear translocation; when associated with F-31.|||Unable to inhibit TNF-induced necrosis; when associated with R-69. Unable to induce TNF nuclear translocation; when associated with R-69. ^@ http://purl.uniprot.org/annotation/PRO_0000144100 http://togogenome.org/gene/10090:Tas2r115 ^@ http://purl.uniprot.org/uniprot/Q7M719 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Parl ^@ http://purl.uniprot.org/uniprot/Q5XJY4 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Active Site|||Chain|||Modified Residue|||Peptide|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Nucleophile|||P-beta|||Phosphoserine|||Presenilin-associated rhomboid-like protein, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000027388|||http://purl.uniprot.org/annotation/PRO_0000027389 http://togogenome.org/gene/10090:Klhl31 ^@ http://purl.uniprot.org/uniprot/G3X9D8|||http://purl.uniprot.org/uniprot/Q8BWA5 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Transmembrane ^@ BACK|||BTB|||Helical|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 31|||N,N,N-trimethylalanine; by NTM1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000271036 http://togogenome.org/gene/10090:Kcp ^@ http://purl.uniprot.org/uniprot/Q3U492 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||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 17|||VWFC 18|||VWFC 2|||VWFC 3|||VWFC 4|||VWFC 5|||VWFC 6|||VWFC 7|||VWFC 8|||VWFC 9|||VWFD ^@ http://purl.uniprot.org/annotation/PRO_0000318587|||http://purl.uniprot.org/annotation/VSP_031232|||http://purl.uniprot.org/annotation/VSP_031233 http://togogenome.org/gene/10090:Fmnl3 ^@ http://purl.uniprot.org/uniprot/D3Z7A7|||http://purl.uniprot.org/uniprot/Q6ZPF4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn ^@ DAD|||Disordered|||FH2|||Formin-like protein 3|||GBD/FH3|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000289096|||http://purl.uniprot.org/annotation/VSP_025894|||http://purl.uniprot.org/annotation/VSP_025895 http://togogenome.org/gene/10090:Prss54 ^@ http://purl.uniprot.org/uniprot/A6H685 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015086519 http://togogenome.org/gene/10090:Oas1d ^@ http://purl.uniprot.org/uniprot/Q3UXA2|||http://purl.uniprot.org/uniprot/Q8VI95 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict ^@ 2'-5'-oligoadenylate synthetase 1|||Inactive 2'-5'-oligoadenylate synthase 1D ^@ http://purl.uniprot.org/annotation/PRO_0000440962 http://togogenome.org/gene/10090:Cpsf3 ^@ http://purl.uniprot.org/uniprot/Q3UDS1|||http://purl.uniprot.org/uniprot/Q9QXK7 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ Abolishes cleavage of the 5' autoinhibitory fragment of the long primary miRNA transcript, pri-miR-17-92.|||Beta-Casp|||Cleavage and polyadenylation specificity factor subunit 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Metallo-beta-lactamase|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000074401 http://togogenome.org/gene/10090:5730409E04Rik ^@ http://purl.uniprot.org/uniprot/Q8BP99 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||UPF0500 protein C1orf216 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000309179 http://togogenome.org/gene/10090:Slc23a4 ^@ http://purl.uniprot.org/uniprot/A0A0J9YUX7|||http://purl.uniprot.org/uniprot/E9PW54|||http://purl.uniprot.org/uniprot/Q6DIB3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:4933416I08Rik ^@ http://purl.uniprot.org/uniprot/Q3TQ67|||http://purl.uniprot.org/uniprot/Q9D434 ^@ Domain Extent|||Region ^@ Domain Extent ^@ S1-like RNA binding ^@ http://togogenome.org/gene/10090:Otud7a ^@ http://purl.uniprot.org/uniprot/Q8R554 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Zinc Finger ^@ A20-type|||Basic and acidic residues|||Catalytic|||Disordered|||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_0000188790 http://togogenome.org/gene/10090:Pdpk1 ^@ http://purl.uniprot.org/uniprot/F2Z3X6|||http://purl.uniprot.org/uniprot/Q3TRL2|||http://purl.uniprot.org/uniprot/Q3UGN6|||http://purl.uniprot.org/uniprot/Q3UHZ0|||http://purl.uniprot.org/uniprot/Q9Z2A0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 3-phosphoinositide-dependent protein kinase 1|||Disordered|||N6-acetyllysine|||PH|||PIF-pocket|||Phosphoserine|||Phosphoserine; by MAP3K5|||Phosphoserine; by PKC/PRKCQ|||Phosphothreonine; by MELK|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by SRC and INSR|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086501 http://togogenome.org/gene/10090:Sel1l3 ^@ http://purl.uniprot.org/uniprot/Q80TS8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||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_0000321895|||http://purl.uniprot.org/annotation/VSP_031813|||http://purl.uniprot.org/annotation/VSP_031814|||http://purl.uniprot.org/annotation/VSP_031815 http://togogenome.org/gene/10090:Celsr3 ^@ http://purl.uniprot.org/uniprot/Q91ZI0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||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|||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|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000012919 http://togogenome.org/gene/10090:Or1e29 ^@ http://purl.uniprot.org/uniprot/Q7TRX7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dnase1 ^@ http://purl.uniprot.org/uniprot/P49183|||http://purl.uniprot.org/uniprot/Q14BW6 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site ^@ Deoxyribonuclease|||Deoxyribonuclease-1|||Endonuclease/exonuclease/phosphatase|||Essential for enzymatic activity|||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_0000007278|||http://purl.uniprot.org/annotation/PRO_5014306910 http://togogenome.org/gene/10090:Cryba2 ^@ http://purl.uniprot.org/uniprot/Q9JJV1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ 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|||N-terminal arm ^@ http://purl.uniprot.org/annotation/PRO_0000057540 http://togogenome.org/gene/10090:Mgst1 ^@ http://purl.uniprot.org/uniprot/Q53ZD4|||http://purl.uniprot.org/uniprot/Q91VS7 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Microsomal glutathione S-transferase 1|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000217737 http://togogenome.org/gene/10090:Tro ^@ http://purl.uniprot.org/uniprot/E9Q098|||http://purl.uniprot.org/uniprot/E9Q160|||http://purl.uniprot.org/uniprot/E9Q886|||http://purl.uniprot.org/uniprot/Q6DIC6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Scgb2b27 ^@ http://purl.uniprot.org/uniprot/A0A087WRN7|||http://purl.uniprot.org/uniprot/Q8R1E9 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015029555|||http://purl.uniprot.org/annotation/PRO_5015099336 http://togogenome.org/gene/10090:Cyb561d1 ^@ http://purl.uniprot.org/uniprot/A2AE42|||http://purl.uniprot.org/uniprot/Q3TPE5|||http://purl.uniprot.org/uniprot/Q6PAS2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Topological Domain|||Transmembrane ^@ Cytochrome b561|||Cytoplasmic|||Helical|||Lumenal|||Probable transmembrane reductase CYB561D1|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000320295 http://togogenome.org/gene/10090:Ntmt1 ^@ http://purl.uniprot.org/uniprot/Q8R2U4 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ 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|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000119289|||http://purl.uniprot.org/annotation/PRO_0000423229 http://togogenome.org/gene/10090:Gnat1 ^@ http://purl.uniprot.org/uniprot/P20612 ^@ 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 ^@ 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|||Interaction with RHO|||N-myristoyl glycine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000203738 http://togogenome.org/gene/10090:Mpst ^@ http://purl.uniprot.org/uniprot/Q99J99 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand ^@ 3-mercaptopyruvate sulfurtransferase|||Abolishes hydrogen sulfide production. Slightly increased basal levels of bound persulfide.|||Cysteine persulfide intermediate|||Hinge|||Interchain (with C-264); redox-active|||Loss of redox potential. Abolishes bound persulfide and hydrogen sulfide production.|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Reduces hydrogen sulfide production by 50%. No change in basal levels of bound persulfide.|||Removed|||Rhodanese 1|||Rhodanese 2 ^@ http://purl.uniprot.org/annotation/PRO_0000139399 http://togogenome.org/gene/10090:Tulp4 ^@ http://purl.uniprot.org/uniprot/Q3UH13|||http://purl.uniprot.org/uniprot/Q69ZK3|||http://purl.uniprot.org/uniprot/Q9JIL5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Phosphoserine|||SOCS box|||TUB|||Tubby-related protein 4|||WD|||WD 1|||WD 2|||WD 3 ^@ http://purl.uniprot.org/annotation/PRO_0000186473 http://togogenome.org/gene/10090:Vmn2r79 ^@ http://purl.uniprot.org/uniprot/E9Q067 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://togogenome.org/gene/10090:Cma1 ^@ http://purl.uniprot.org/uniprot/A4QPC5|||http://purl.uniprot.org/uniprot/P21844 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Chymase|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027455|||http://purl.uniprot.org/annotation/PRO_0000027456|||http://purl.uniprot.org/annotation/PRO_5015086452 http://togogenome.org/gene/10090:Smc4 ^@ http://purl.uniprot.org/uniprot/Q8CG47 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Disordered|||N6-acetyllysine|||Phosphoserine|||SMC hinge|||Structural maintenance of chromosomes protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000119008 http://togogenome.org/gene/10090:Adam26b ^@ http://purl.uniprot.org/uniprot/Q6IMH6|||http://purl.uniprot.org/uniprot/Q9CUI8 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Non-terminal Residue|||Signal Peptide|||Transmembrane ^@ Disintegrin|||EGF-like|||Helical|||Peptidase M12B|||Peptidase M12B domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5004324998|||http://purl.uniprot.org/annotation/PRO_5015098317 http://togogenome.org/gene/10090:Arl2 ^@ http://purl.uniprot.org/uniprot/Q9D0J4 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn ^@ ADP-ribosylation factor-like protein 2|||Does not reduce affinity fo GTP and GDP. Enhances interaction with PDE6D.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-myristoyl glycine|||Phosphoserine|||Reduces affinity to GTP and GDP. Inhibits interaction with PDE6D.|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207454 http://togogenome.org/gene/10090:Tmprss2 ^@ http://purl.uniprot.org/uniprot/Q9JIQ8 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Charge relay system|||Cleavage|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Interchain (between non-catalytic and catalytic chains)|||LDL-receptor class A|||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_0000027857|||http://purl.uniprot.org/annotation/PRO_0000027858 http://togogenome.org/gene/10090:Ccdc9 ^@ http://purl.uniprot.org/uniprot/G3X927|||http://purl.uniprot.org/uniprot/Q8VC31 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Coiled-coil domain-containing protein 9|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089404 http://togogenome.org/gene/10090:Neurod1 ^@ http://purl.uniprot.org/uniprot/Q60867 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Neurogenic differentiation factor 1|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CaMK2|||Promotes the formation of differentiated late retinal amacrine cells.|||Reduces weakly phosphorylation. Reduces strongly phosphorylation; when associated with A-162 and A-259. Reduces transactivation on the insulin promoter in glucose-stimulated insulinoma cells; when associated with A-259 and A-274.|||Reduces weakly phosphorylation. Reduces strongly phosphorylation; when associated with A-162 and A-266. Reduces transactivation on the insulin promoter in glucose-stimulated insulinoma cells; when associated with A-266 and A-274.|||Reduces weakly phosphorylation. Reduces strongly phosphorylation; when associated with A-259 and A-266.|||Strongly reduces phosphorylation. Reduces transactivation on the insulin promoter in glucose-stimulated insulinoma cells; when associated with A-259 and A-266.|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127383 http://togogenome.org/gene/10090:Hyal1 ^@ http://purl.uniprot.org/uniprot/Q91ZJ9 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ EGF-like|||Hyaluronidase-1|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000042624|||http://purl.uniprot.org/annotation/VSP_015923 http://togogenome.org/gene/10090:Pld5 ^@ http://purl.uniprot.org/uniprot/D3YYN6|||http://purl.uniprot.org/uniprot/Q3UNN8 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Inactive phospholipase D5|||N-linked (GlcNAc...) asparagine|||PLD phosphodiesterase|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288607|||http://purl.uniprot.org/annotation/PRO_5003052367|||http://purl.uniprot.org/annotation/VSP_025728|||http://purl.uniprot.org/annotation/VSP_025729 http://togogenome.org/gene/10090:Mrgprx1 ^@ http://purl.uniprot.org/uniprot/Q8CIP3 ^@ 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|||Mas-related G-protein coupled receptor member X1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000283731 http://togogenome.org/gene/10090:Baalc ^@ http://purl.uniprot.org/uniprot/Q8VHV1 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Region|||Splice Variant ^@ Brain and acute leukemia cytoplasmic protein|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with CAMK2A|||N-myristoyl glycine|||Polar residues|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000248206|||http://purl.uniprot.org/annotation/VSP_020205|||http://purl.uniprot.org/annotation/VSP_020206 http://togogenome.org/gene/10090:Or51f5 ^@ http://purl.uniprot.org/uniprot/Q8VGZ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Eif2a ^@ http://purl.uniprot.org/uniprot/Q8BJW6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 2A|||Eukaryotic translation initiation factor 2A, N-terminally processed|||In isoform 2.|||N-acetylalanine; in Eukaryotic translation initiation factor 2A, N-terminally processed|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed; alternate|||WD 1|||WD 2|||WD 3 ^@ http://purl.uniprot.org/annotation/PRO_0000286077|||http://purl.uniprot.org/annotation/PRO_0000424467|||http://purl.uniprot.org/annotation/VSP_024977|||http://purl.uniprot.org/annotation/VSP_024978 http://togogenome.org/gene/10090:Tbx1 ^@ http://purl.uniprot.org/uniprot/B9EII4|||http://purl.uniprot.org/uniprot/F6ZP09|||http://purl.uniprot.org/uniprot/P70323 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolished nuclear localization.|||Basic and acidic residues|||Disordered|||Does not affect transcription factor activity or nuclear localization.|||In isoform 2.|||Nuclear localization signal|||Pro residues|||T-box|||T-box transcription factor TBX1 ^@ http://purl.uniprot.org/annotation/PRO_0000184424|||http://purl.uniprot.org/annotation/VSP_016760 http://togogenome.org/gene/10090:Rad51ap1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1G4|||http://purl.uniprot.org/uniprot/A0A0R4J1H1|||http://purl.uniprot.org/uniprot/Q8C551 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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 ubiquitin; alternate)|||Interaction with DNA|||Interaction with RAD51|||Phosphoserine|||Polar residues|||RAD51 interacting motif|||RAD51-associated protein 1|||SIM motif|||WVPP motif ^@ http://purl.uniprot.org/annotation/PRO_0000097141 http://togogenome.org/gene/10090:Nt5el ^@ http://purl.uniprot.org/uniprot/Q9D3Z8 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ 5'-Nucleotidase C-terminal|||Calcineurin-like phosphoesterase|||Disordered ^@ http://togogenome.org/gene/10090:Ncapg ^@ http://purl.uniprot.org/uniprot/E9PWG6 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Nuclear condensin complex subunit 3 C-terminal ^@ http://togogenome.org/gene/10090:Bhlha15 ^@ http://purl.uniprot.org/uniprot/Q9QYC3 ^@ 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|||Class A basic helix-loop-helix protein 15|||Disordered|||Phosphothreonine|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127151 http://togogenome.org/gene/10090:Myo1f ^@ http://purl.uniprot.org/uniprot/Q8CG29 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Actin-binding|||Disordered|||Myosin motor|||Polar residues|||SH3|||TH1 ^@ http://togogenome.org/gene/10090:Acyp1 ^@ http://purl.uniprot.org/uniprot/P56376|||http://purl.uniprot.org/uniprot/Q4VAF0 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue ^@ Acylphosphatase-1|||Acylphosphatase-like|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000158536 http://togogenome.org/gene/10090:Tmem123 ^@ http://purl.uniprot.org/uniprot/Q91Z22 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Porimin ^@ http://purl.uniprot.org/annotation/PRO_0000045059 http://togogenome.org/gene/10090:Foxl3 ^@ http://purl.uniprot.org/uniprot/J3QP53 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Fork-head ^@ http://togogenome.org/gene/10090:Riox2 ^@ http://purl.uniprot.org/uniprot/Q8CD15 ^@ 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 ^@ JmjC|||Phosphoserine|||Ribosomal oxygenase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000308378 http://togogenome.org/gene/10090:Ppfia1 ^@ http://purl.uniprot.org/uniprot/B2RXQ2|||http://purl.uniprot.org/uniprot/B2RXW8 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||SAM ^@ http://togogenome.org/gene/10090:Ppy ^@ http://purl.uniprot.org/uniprot/P10601|||http://purl.uniprot.org/uniprot/Q496X5 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Signal Peptide ^@ Chain|||Modified Residue|||Peptide|||Signal Peptide ^@ C-terminal peptide|||Pancreatic polypeptide|||Tyrosine amide ^@ http://purl.uniprot.org/annotation/PRO_0000025368|||http://purl.uniprot.org/annotation/PRO_0000025369|||http://purl.uniprot.org/annotation/PRO_5014309334 http://togogenome.org/gene/10090:Trabd2b ^@ http://purl.uniprot.org/uniprot/B1ATG9 ^@ 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|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000346437 http://togogenome.org/gene/10090:Cep57 ^@ http://purl.uniprot.org/uniprot/B8JJE7|||http://purl.uniprot.org/uniprot/Q8CEE0 ^@ 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|||Centrosomal protein of 57 kDa|||Cep57 centrosome localisation|||Cep57 centrosome microtubule-binding|||Disordered|||In isoform 2.|||In isoform 3.|||Mediates interaction with microtubules|||Phosphoserine|||Polar residues|||centrosome localization domain (CLD) ^@ http://purl.uniprot.org/annotation/PRO_0000189533|||http://purl.uniprot.org/annotation/VSP_012265|||http://purl.uniprot.org/annotation/VSP_012266 http://togogenome.org/gene/10090:Or2h15 ^@ http://purl.uniprot.org/uniprot/Q7TRI8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Icam2 ^@ http://purl.uniprot.org/uniprot/P35330 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Intercellular adhesion molecule 2|||Loss of interaction with EZR, MSN and RDX and co-localization to microvilli.|||N-linked (GlcNAc...) asparagine|||Required for interaction with EZR, MSN and RDX and co-localization to microvilli ^@ http://purl.uniprot.org/annotation/PRO_0000014791 http://togogenome.org/gene/10090:Dph1 ^@ http://purl.uniprot.org/uniprot/Q5NCQ5 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000307883 http://togogenome.org/gene/10090:Rdh16 ^@ http://purl.uniprot.org/uniprot/O54909 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Transmembrane ^@ Helical|||Proton acceptor|||Retinol dehydrogenase 16 ^@ http://purl.uniprot.org/annotation/PRO_0000446674 http://togogenome.org/gene/10090:Usp17lc ^@ http://purl.uniprot.org/uniprot/G5E8I7 ^@ 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 deubiquitinating activity.|||Basic and acidic residues|||Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein C ^@ http://purl.uniprot.org/annotation/PRO_0000442982 http://togogenome.org/gene/10090:Yap1 ^@ http://purl.uniprot.org/uniprot/P46938 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn ^@ Disordered|||In isoform 2.|||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|||Transactivation domain|||Transcriptional coactivator YAP1|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000076072|||http://purl.uniprot.org/annotation/VSP_039056 http://togogenome.org/gene/10090:Cyp2c50 ^@ http://purl.uniprot.org/uniprot/Q91X77 ^@ 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 ^@ Cytochrome P450 2C50|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000282957|||http://purl.uniprot.org/annotation/VSP_052374 http://togogenome.org/gene/10090:Alkbh2 ^@ http://purl.uniprot.org/uniprot/Q6P6J4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ DNA oxidative demethylase ALKBH2|||Disordered|||Fe2OG dioxygenase|||Loss of activity.|||PCNA-binding|||Reduces activity. ^@ http://purl.uniprot.org/annotation/PRO_0000239276 http://togogenome.org/gene/10090:Wdr77 ^@ http://purl.uniprot.org/uniprot/Q99J09 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ Methylosome protein WDR77|||Phosphothreonine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051075 http://togogenome.org/gene/10090:Nepro ^@ http://purl.uniprot.org/uniprot/Q3TS42|||http://purl.uniprot.org/uniprot/Q8R2U2 ^@ 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|||Nuclear localization signal|||Nucleolus and neural progenitor protein|||Nucleolus and neural progenitor protein-like N-terminal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000434895 http://togogenome.org/gene/10090:Vmn2r12 ^@ http://purl.uniprot.org/uniprot/L7N217 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982263 http://togogenome.org/gene/10090:Cox6a2 ^@ http://purl.uniprot.org/uniprot/P43023 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn ^@ Chain|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn ^@ Cytochrome c oxidase subunit 6A2, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000006117 http://togogenome.org/gene/10090:Slc6a20b ^@ http://purl.uniprot.org/uniprot/A0A803YV45|||http://purl.uniprot.org/uniprot/O88575 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||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 transporter XTRP3B ^@ http://purl.uniprot.org/annotation/PRO_0000214813 http://togogenome.org/gene/10090:Pdk3 ^@ http://purl.uniprot.org/uniprot/Q4FJR4|||http://purl.uniprot.org/uniprot/Q922H2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Histidine kinase|||Mitochondrion|||N6-succinyllysine|||[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000023444 http://togogenome.org/gene/10090:4930503L19Rik ^@ http://purl.uniprot.org/uniprot/G8CZ53|||http://purl.uniprot.org/uniprot/Q8CB14 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||Lung adenoma susceptibility protein 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000019563|||http://purl.uniprot.org/annotation/VSP_015086|||http://purl.uniprot.org/annotation/VSP_015087 http://togogenome.org/gene/10090:H2-Q1 ^@ http://purl.uniprot.org/uniprot/O19441 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015096742 http://togogenome.org/gene/10090:Dpm2 ^@ http://purl.uniprot.org/uniprot/Q545R7|||http://purl.uniprot.org/uniprot/Q9Z324 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Dolichol phosphate-mannose biosynthesis regulatory protein|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000220874 http://togogenome.org/gene/10090:Slc44a4 ^@ http://purl.uniprot.org/uniprot/Q3TL93|||http://purl.uniprot.org/uniprot/Q3ULA4|||http://purl.uniprot.org/uniprot/Q91VA1 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Choline transporter-like protein 4|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000191724 http://togogenome.org/gene/10090:Ifna11 ^@ http://purl.uniprot.org/uniprot/A0A7R8C4Y5|||http://purl.uniprot.org/uniprot/Q61716 ^@ 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-11|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000317634|||http://purl.uniprot.org/annotation/PRO_5031142305 http://togogenome.org/gene/10090:Szrd1 ^@ http://purl.uniprot.org/uniprot/Q6NXN1 ^@ 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.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||SUZ|||SUZ domain-containing protein 1|||SUZ-C ^@ http://purl.uniprot.org/annotation/PRO_0000303069|||http://purl.uniprot.org/annotation/VSP_027998 http://togogenome.org/gene/10090:Birc7 ^@ http://purl.uniprot.org/uniprot/A2AWP0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Repeat|||Site|||Zinc Finger ^@ BIR|||Baculoviral IAP repeat-containing protein 7|||Baculoviral IAP repeat-containing protein 7 30 kDa subunit|||Basic and acidic residues|||Cleavage; by CASP3 and CASP7|||Disordered|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000416248|||http://purl.uniprot.org/annotation/PRO_0000416249 http://togogenome.org/gene/10090:Pard6b ^@ http://purl.uniprot.org/uniprot/Q9JK83 ^@ 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 RHOQ, but not the interaction with CDC42; when associated with A-136.|||Abolishes interaction with RHOQ, but not the interaction with CDC42; when associated with A-139.|||Disordered|||Does not abolish interaction with CDC42 and RHOQ.|||In isoform 2.|||Interaction with PARD3 and CDC42|||PB1|||PDZ|||Partitioning defective 6 homolog beta|||Phosphoserine|||Polar residues|||Prevents interaction with PALS1.|||Pseudo-CRIB|||Strongly reduces interaction with PARD3. Does not abolish interaction with CDC42 and RHOQ. ^@ http://purl.uniprot.org/annotation/PRO_0000112517|||http://purl.uniprot.org/annotation/VSP_007460|||http://purl.uniprot.org/annotation/VSP_007461 http://togogenome.org/gene/10090:Ifnk ^@ http://purl.uniprot.org/uniprot/Q4FZL7|||http://purl.uniprot.org/uniprot/Q7TSL0 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Interferon kappa ^@ http://purl.uniprot.org/annotation/PRO_0000016411|||http://purl.uniprot.org/annotation/PRO_5009970952 http://togogenome.org/gene/10090:Ggt6 ^@ http://purl.uniprot.org/uniprot/Q6PDE7 ^@ 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 ^@ Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Glutathione hydrolase 6 heavy chain|||Glutathione hydrolase 6 light chain|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000314956|||http://purl.uniprot.org/annotation/PRO_0000314957|||http://purl.uniprot.org/annotation/VSP_030452 http://togogenome.org/gene/10090:Pxmp2 ^@ http://purl.uniprot.org/uniprot/P42925|||http://purl.uniprot.org/uniprot/Q5D073 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Peroxisomal|||Peroxisomal membrane protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000218930 http://togogenome.org/gene/10090:1700012B09Rik ^@ http://purl.uniprot.org/uniprot/Q9DAE7|||http://purl.uniprot.org/uniprot/Q9DAL1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Uncharacterized protein C11orf97 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000440044 http://togogenome.org/gene/10090:Slc15a4 ^@ http://purl.uniprot.org/uniprot/Q91W98 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Phosphoserine|||Solute carrier family 15 member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000338600 http://togogenome.org/gene/10090:Wfdc6a ^@ http://purl.uniprot.org/uniprot/Q3UW55 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ BPTI/Kunitz inhibitor|||WAP|||WAP four-disulfide core domain protein 6A ^@ http://purl.uniprot.org/annotation/PRO_0000415851 http://togogenome.org/gene/10090:Trip12 ^@ http://purl.uniprot.org/uniprot/G5E870 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase TRIP12|||Glycyl thioester intermediate|||HECT|||K-box|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||WWE ^@ http://purl.uniprot.org/annotation/PRO_0000419689 http://togogenome.org/gene/10090:Fignl1 ^@ http://purl.uniprot.org/uniprot/Q8BPY9 ^@ 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|||Fidgetin-like protein 1|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000302724 http://togogenome.org/gene/10090:S100b ^@ http://purl.uniprot.org/uniprot/P50114|||http://purl.uniprot.org/uniprot/Q3UY00 ^@ 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|||EF-hand 1|||EF-hand 2|||N-acetylserine|||Protein S100-B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000143967 http://togogenome.org/gene/10090:Ttc9 ^@ http://purl.uniprot.org/uniprot/Q3V038 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Disordered|||Phosphoserine|||Pro residues|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 9A ^@ http://purl.uniprot.org/annotation/PRO_0000294470 http://togogenome.org/gene/10090:Cdh12 ^@ http://purl.uniprot.org/uniprot/Q5RJH3 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-12|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000320094|||http://purl.uniprot.org/annotation/PRO_0000320095 http://togogenome.org/gene/10090:Rgma ^@ http://purl.uniprot.org/uniprot/Q6PCX7 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Cleavage; by autolysis|||Disordered|||GPI-anchor amidated alanine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Repulsive guidance molecule A ^@ http://purl.uniprot.org/annotation/PRO_0000030388|||http://purl.uniprot.org/annotation/PRO_0000030389|||http://purl.uniprot.org/annotation/PRO_0000030390|||http://purl.uniprot.org/annotation/VSP_011316 http://togogenome.org/gene/10090:S100a9 ^@ http://purl.uniprot.org/uniprot/P31725|||http://purl.uniprot.org/uniprot/Q3UP42 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Strand|||Turn ^@ EF-hand|||EF-hand 1|||EF-hand 2|||N-acetylalanine|||Pros-methylhistidine|||Protein S100-A9|||Reduced histidine methylation by METTL9.|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000143998 http://togogenome.org/gene/10090:Rpf1 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFR7|||http://purl.uniprot.org/uniprot/Q7TND5 ^@ 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|||Brix|||Disordered|||RNA-binding|||Ribosome production factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000120249 http://togogenome.org/gene/10090:Clxn ^@ http://purl.uniprot.org/uniprot/Q9D3N2 ^@ 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.|||In isoform 3.|||In isoform 4. ^@ http://purl.uniprot.org/annotation/PRO_0000251970|||http://purl.uniprot.org/annotation/VSP_020827|||http://purl.uniprot.org/annotation/VSP_020828|||http://purl.uniprot.org/annotation/VSP_020829|||http://purl.uniprot.org/annotation/VSP_020830|||http://purl.uniprot.org/annotation/VSP_020831 http://togogenome.org/gene/10090:Gm21083 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFD5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cstdc6 ^@ http://purl.uniprot.org/uniprot/L7N257 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Cystatin ^@ http://togogenome.org/gene/10090:Pdzd11 ^@ http://purl.uniprot.org/uniprot/Q9CZG9 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Helix|||Strand ^@ PDZ|||PDZ domain-containing protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000058274 http://togogenome.org/gene/10090:Lin7a ^@ http://purl.uniprot.org/uniprot/Q3TUM0|||http://purl.uniprot.org/uniprot/Q8JZS0 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Motif|||Region ^@ Disordered|||Kinase interacting site|||L27|||PDZ|||Protein lin-7 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000189624 http://togogenome.org/gene/10090:Tfrc ^@ http://purl.uniprot.org/uniprot/Q542D9|||http://purl.uniprot.org/uniprot/Q62351 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cell attachment site|||Cytoplasmic|||Endocytosis signal|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Interchain|||Ligand-binding|||Mediates interaction with SH3BP4|||N-linked (GlcNAc...) asparagine|||Negatively regulates of T and B cell proliferation upon activation. Significantly increases cell surface expression on T and B cells. Impairs internalization.|||O-linked (GalNAc...) threonine|||PA|||Peptidase M28|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||S-palmitoyl cysteine|||Stop-transfer sequence|||Transferrin receptor protein 1|||Transferrin receptor-like dimerisation ^@ http://purl.uniprot.org/annotation/PRO_0000174133 http://togogenome.org/gene/10090:Ctps2 ^@ http://purl.uniprot.org/uniprot/P70303 ^@ 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 ^@ CTP synthase 2|||For GATase activity|||Glutamine amidotransferase type-1|||In isoform 2.|||In isoform 3.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000247034|||http://purl.uniprot.org/annotation/VSP_019893|||http://purl.uniprot.org/annotation/VSP_019894|||http://purl.uniprot.org/annotation/VSP_019895|||http://purl.uniprot.org/annotation/VSP_019896 http://togogenome.org/gene/10090:Wee1 ^@ http://purl.uniprot.org/uniprot/P47810 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Phosphoserine; by BRSK1 and BRSK2|||Phosphoserine; by CDK1|||Phosphoserine; by PLK1|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Wee1-like protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000086811 http://togogenome.org/gene/10090:B4galnt3 ^@ http://purl.uniprot.org/uniprot/A0A1D5RMF7|||http://purl.uniprot.org/uniprot/Q6L8S8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||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_0000252369 http://togogenome.org/gene/10090:Sp6 ^@ http://purl.uniprot.org/uniprot/A2A708|||http://purl.uniprot.org/uniprot/Q9ESX2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Zinc Finger ^@ 9aaTAD|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Polar residues|||Transcription factor Sp6 ^@ http://purl.uniprot.org/annotation/PRO_0000047149 http://togogenome.org/gene/10090:Ahrr ^@ http://purl.uniprot.org/uniprot/A0A0R4J020|||http://purl.uniprot.org/uniprot/A0A0R4J1D3|||http://purl.uniprot.org/uniprot/Q3U1U7 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Aryl hydrocarbon receptor repressor|||BHLH|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Needed for transcriptional repression|||PAS|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000333858|||http://purl.uniprot.org/annotation/VSP_033565|||http://purl.uniprot.org/annotation/VSP_033566 http://togogenome.org/gene/10090:Esr2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Y6|||http://purl.uniprot.org/uniprot/A0A1W2P736|||http://purl.uniprot.org/uniprot/O08537 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||DNA Binding|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Abolishes stimulatory effect of Ras.|||Disordered|||Estrogen receptor beta|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Modulating|||NR C4-type|||NR LBD|||No loss of the stimulatory effect of Ras.|||Nuclear receptor|||O-linked (GlcNAc) serine; alternate|||Phosphoserine; alternate|||Phosphoserine; by MAPK ^@ http://purl.uniprot.org/annotation/CAR_000201|||http://purl.uniprot.org/annotation/PRO_0000053644|||http://purl.uniprot.org/annotation/VSP_003693|||http://purl.uniprot.org/annotation/VSP_003696|||http://purl.uniprot.org/annotation/VSP_042429|||http://purl.uniprot.org/annotation/VSP_042430|||http://purl.uniprot.org/annotation/VSP_042431|||http://purl.uniprot.org/annotation/VSP_042432 http://togogenome.org/gene/10090:Hcar2 ^@ http://purl.uniprot.org/uniprot/Q0VBA6|||http://purl.uniprot.org/uniprot/Q9EP66 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||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|||Hydroxycarboxylic acid receptor 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069605 http://togogenome.org/gene/10090:Atg4b ^@ http://purl.uniprot.org/uniprot/A0A0R4J065|||http://purl.uniprot.org/uniprot/Q8BGE6 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict ^@ Cysteine protease ATG4B|||Interchain (with C-292)|||Interchain (with C-361)|||LIR|||N-acetylmethionine|||Nucleophile|||Peptidase C54 catalytic|||Phosphoserine|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000215845 http://togogenome.org/gene/10090:Sytl1 ^@ http://purl.uniprot.org/uniprot/A2AE94|||http://purl.uniprot.org/uniprot/Q6KAP5 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ C2|||Disordered|||Polar residues|||RabBD ^@ http://togogenome.org/gene/10090:Dynlt5 ^@ http://purl.uniprot.org/uniprot/B7ZNE0|||http://purl.uniprot.org/uniprot/Q9D5I4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Dynein light chain Tctex-type 5|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284886 http://togogenome.org/gene/10090:Lmnb1 ^@ http://purl.uniprot.org/uniprot/P14733 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict ^@ 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|||Interchain|||LTD|||Lamin-B1|||Linker 1|||Linker 2|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||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_0000063817|||http://purl.uniprot.org/annotation/PRO_0000403467 http://togogenome.org/gene/10090:BC048671 ^@ http://purl.uniprot.org/uniprot/Q8C5S3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Uncharacterized protein C3orf22 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000234431 http://togogenome.org/gene/10090:Taf7 ^@ http://purl.uniprot.org/uniprot/Q9R1C0 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Motif|||Region ^@ Disordered|||Phosphoserine|||Transcription initiation factor TFIID subunit 7|||[KR]-[STA]-K motif ^@ http://purl.uniprot.org/annotation/PRO_0000118882 http://togogenome.org/gene/10090:Golga7b ^@ http://purl.uniprot.org/uniprot/Q9D428 ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Region ^@ Disordered|||Golgin subfamily A member 7B|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000244091 http://togogenome.org/gene/10090:Serpina3f ^@ http://purl.uniprot.org/uniprot/Q3UDB3|||http://purl.uniprot.org/uniprot/Q3UTZ5|||http://purl.uniprot.org/uniprot/Q80X76 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond|||Serine protease inhibitor A3F|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_0000094097 http://togogenome.org/gene/10090:Morn4 ^@ http://purl.uniprot.org/uniprot/Q6PGF2 ^@ Chain|||Helix|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Repeat|||Strand|||Turn ^@ MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN repeat-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000279489 http://togogenome.org/gene/10090:Taf4 ^@ http://purl.uniprot.org/uniprot/E9QAP7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Pro residues|||TAFH ^@ http://togogenome.org/gene/10090:Klk6 ^@ http://purl.uniprot.org/uniprot/Q91Y82 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015099534 http://togogenome.org/gene/10090:Hoxa4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J193|||http://purl.uniprot.org/uniprot/P06798 ^@ 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 ^@ Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-A4|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000200049 http://togogenome.org/gene/10090:Rce1 ^@ http://purl.uniprot.org/uniprot/P57791 ^@ Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site|||Transmembrane ^@ CAAX prenyl protease 2|||Helical|||N-acetylalanine|||Proton donor/acceptor|||Removed|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000194831 http://togogenome.org/gene/10090:Trappc14 ^@ http://purl.uniprot.org/uniprot/Q3UTZ3 ^@ 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|||Phosphothreonine|||Polar residues|||Trafficking protein particle complex subunit 14 ^@ http://purl.uniprot.org/annotation/PRO_0000280345 http://togogenome.org/gene/10090:Vmn1r38 ^@ http://purl.uniprot.org/uniprot/Q8R2E1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp2 ^@ http://purl.uniprot.org/uniprot/P08043 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||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|||In isoform 2.|||Zinc finger protein ZFP2 ^@ http://purl.uniprot.org/annotation/PRO_0000047282|||http://purl.uniprot.org/annotation/VSP_026332 http://togogenome.org/gene/10090:Dcun1d1 ^@ http://purl.uniprot.org/uniprot/Q3UT23|||http://purl.uniprot.org/uniprot/Q9QZ73 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site ^@ DCN1-like protein 1|||DCUN1|||Essential for interaction with UBE2M|||N-acetylmethionine|||UBA-like ^@ http://purl.uniprot.org/annotation/PRO_0000129499 http://togogenome.org/gene/10090:Spaca6 ^@ http://purl.uniprot.org/uniprot/E9Q8Q8 ^@ 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|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sperm acrosome membrane-associated protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000434004|||http://purl.uniprot.org/annotation/VSP_057872|||http://purl.uniprot.org/annotation/VSP_057873|||http://purl.uniprot.org/annotation/VSP_057874|||http://purl.uniprot.org/annotation/VSP_057875|||http://purl.uniprot.org/annotation/VSP_057876 http://togogenome.org/gene/10090:Garem2 ^@ http://purl.uniprot.org/uniprot/Q6PAJ3 ^@ 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 ^@ CABIT|||Disordered|||GRB2-associated and regulator of MAPK protein 2|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000340254|||http://purl.uniprot.org/annotation/VSP_034202|||http://purl.uniprot.org/annotation/VSP_034203|||http://purl.uniprot.org/annotation/VSP_034204 http://togogenome.org/gene/10090:Knstrn ^@ http://purl.uniprot.org/uniprot/Q9D9Z1 ^@ 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|||Interaction with SPAG5|||Polar residues|||Small kinetochore-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000274513 http://togogenome.org/gene/10090:Mup19 ^@ http://purl.uniprot.org/uniprot/A2CGB6|||http://purl.uniprot.org/uniprot/A9C496|||http://purl.uniprot.org/uniprot/P02762 ^@ 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 ^@ Lipocalin/cytosolic fatty-acid binding|||Major urinary protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000017932|||http://purl.uniprot.org/annotation/PRO_5002736258|||http://purl.uniprot.org/annotation/PRO_5014296800 http://togogenome.org/gene/10090:Chn2 ^@ http://purl.uniprot.org/uniprot/Q3TVA5|||http://purl.uniprot.org/uniprot/Q3V2R3|||http://purl.uniprot.org/uniprot/Q80XD1 ^@ 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 ^@ Beta-chimaerin|||Disordered|||In isoform 2.|||In isoform 3.|||Phorbol-ester/DAG-type|||Polar residues|||Rho-GAP|||SH2 ^@ http://purl.uniprot.org/annotation/PRO_0000056698|||http://purl.uniprot.org/annotation/VSP_014243|||http://purl.uniprot.org/annotation/VSP_014244|||http://purl.uniprot.org/annotation/VSP_014245|||http://purl.uniprot.org/annotation/VSP_014246 http://togogenome.org/gene/10090:Abcf3 ^@ http://purl.uniprot.org/uniprot/Q8K268 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family F member 3|||Basic and acidic residues|||Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000248043 http://togogenome.org/gene/10090:Slc35d3 ^@ http://purl.uniprot.org/uniprot/B9EI54|||http://purl.uniprot.org/uniprot/Q8BGF8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Solute carrier family 35 member D3 ^@ http://purl.uniprot.org/annotation/PRO_0000307728 http://togogenome.org/gene/10090:Dmxl2 ^@ http://purl.uniprot.org/uniprot/B0V2P5|||http://purl.uniprot.org/uniprot/Q8BPN8 ^@ 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|||DmX-like protein 2|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RAVE complex protein Rav1 C-terminal|||WD|||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_0000223325|||http://purl.uniprot.org/annotation/VSP_026594|||http://purl.uniprot.org/annotation/VSP_026595|||http://purl.uniprot.org/annotation/VSP_026596|||http://purl.uniprot.org/annotation/VSP_026597 http://togogenome.org/gene/10090:Dimt1 ^@ http://purl.uniprot.org/uniprot/Q9D0D4 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Probable dimethyladenosine transferase ^@ http://purl.uniprot.org/annotation/PRO_0000101467 http://togogenome.org/gene/10090:Entpd6 ^@ http://purl.uniprot.org/uniprot/Q3U0P5 ^@ Active Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Ectonucleoside triphosphate diphosphohydrolase 6|||Helical|||Lumenal|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000451958 http://togogenome.org/gene/10090:Gm4952 ^@ http://purl.uniprot.org/uniprot/Q5FW57 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Glycine N-acyltransferase-like protein|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000281878 http://togogenome.org/gene/10090:Sap18b ^@ http://purl.uniprot.org/uniprot/E9Q317 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Oosp3 ^@ http://purl.uniprot.org/uniprot/G5E8D7 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Oocyte-secreted protein 3 ^@ http://purl.uniprot.org/annotation/PRO_5015091897 http://togogenome.org/gene/10090:Fbxw15 ^@ http://purl.uniprot.org/uniprot/L7N1X6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant ^@ F-box|||F-box/WD repeat-containing protein 15|||In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000442736|||http://purl.uniprot.org/annotation/VSP_059276 http://togogenome.org/gene/10090:Mrm3 ^@ http://purl.uniprot.org/uniprot/Q5ND52 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||Polar residues|||rRNA methyltransferase 3, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000311302 http://togogenome.org/gene/10090:Tmem229b ^@ http://purl.uniprot.org/uniprot/Q8BFQ2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Transmembrane protein 229B ^@ http://purl.uniprot.org/annotation/PRO_0000263682 http://togogenome.org/gene/10090:Cep85 ^@ http://purl.uniprot.org/uniprot/Q8BMK0 ^@ 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 ^@ Centrosomal protein of 85 kDa|||Disordered|||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_0000233661 http://togogenome.org/gene/10090:C2cd3 ^@ http://purl.uniprot.org/uniprot/Q52KB6 ^@ 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|||C2 3|||C2 4|||C2 5|||C2 6|||C2 domain-containing protein 3|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000311240|||http://purl.uniprot.org/annotation/VSP_029449|||http://purl.uniprot.org/annotation/VSP_029450|||http://purl.uniprot.org/annotation/VSP_029451|||http://purl.uniprot.org/annotation/VSP_029452 http://togogenome.org/gene/10090:Dcpp3 ^@ http://purl.uniprot.org/uniprot/L7N259 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Jacalin-type lectin ^@ http://purl.uniprot.org/annotation/PRO_5040103590 http://togogenome.org/gene/10090:Ddx25 ^@ http://purl.uniprot.org/uniprot/Q9QY15 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant ^@ ATP-dependent RNA helicase DDX25|||DEAD box|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Nuclear export signal|||Nuclear localization signal|||Phosphothreonine|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000030815|||http://purl.uniprot.org/annotation/VSP_018876 http://togogenome.org/gene/10090:Apln ^@ http://purl.uniprot.org/uniprot/Q544B5|||http://purl.uniprot.org/uniprot/Q9R0R4 ^@ Chain|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Apelin|||Apelin-13|||Apelin-28|||Apelin-31|||Apelin-36|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000001764|||http://purl.uniprot.org/annotation/PRO_0000001765|||http://purl.uniprot.org/annotation/PRO_0000001766|||http://purl.uniprot.org/annotation/PRO_0000001767|||http://purl.uniprot.org/annotation/PRO_0000001768|||http://purl.uniprot.org/annotation/PRO_5014309612 http://togogenome.org/gene/10090:Anxa8 ^@ http://purl.uniprot.org/uniprot/O35640 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Repeat|||Sequence Conflict ^@ Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A8 ^@ http://purl.uniprot.org/annotation/PRO_0000067504 http://togogenome.org/gene/10090:Lmna ^@ http://purl.uniprot.org/uniprot/P48678 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Cleavage; by endoprotease|||Coil 1A|||Coil 1B|||Coil 2|||Cysteine methyl ester|||Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death.|||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|||Head|||Heptad change of phase|||IF rod|||In isoform C and isoform C2.|||In isoform C2.|||Interaction with MLIP|||LTD|||Lamin-A/C|||Linker 1|||Linker 2|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Polar residues|||Prelamin-A/C|||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_0000063811|||http://purl.uniprot.org/annotation/PRO_0000398837|||http://purl.uniprot.org/annotation/PRO_0000398838|||http://purl.uniprot.org/annotation/PRO_0000403443|||http://purl.uniprot.org/annotation/VSP_002471|||http://purl.uniprot.org/annotation/VSP_002472|||http://purl.uniprot.org/annotation/VSP_017064|||http://purl.uniprot.org/annotation/VSP_017065 http://togogenome.org/gene/10090:Gart ^@ http://purl.uniprot.org/uniprot/Q64737 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ AIRS domain|||ATP-grasp|||GART domain|||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_0000074938|||http://purl.uniprot.org/annotation/VSP_005518 http://togogenome.org/gene/10090:Chrm4 ^@ http://purl.uniprot.org/uniprot/P32211|||http://purl.uniprot.org/uniprot/Q0VBU3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||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|||Muscarinic acetylcholine receptor M4|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069038 http://togogenome.org/gene/10090:Usp13 ^@ http://purl.uniprot.org/uniprot/Q5BKP2 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Zinc Finger ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nucleophile|||Phosphoserine|||Proton acceptor|||UBA 1|||UBA 2|||UBP-type; degenerate|||USP|||Ubiquitin carboxyl-terminal hydrolase 13 ^@ http://purl.uniprot.org/annotation/PRO_0000418011 http://togogenome.org/gene/10090:Enpp4 ^@ http://purl.uniprot.org/uniprot/Q8BTJ4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ AMP-threonine intermediate|||Bis(5'-adenosyl)-triphosphatase enpp4|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000324796|||http://purl.uniprot.org/annotation/VSP_032370 http://togogenome.org/gene/10090:Pip4p2 ^@ http://purl.uniprot.org/uniprot/Q9CZX7 ^@ 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_0000235229 http://togogenome.org/gene/10090:Luc7l2 ^@ http://purl.uniprot.org/uniprot/E9Q715|||http://purl.uniprot.org/uniprot/Q05CX5|||http://purl.uniprot.org/uniprot/Q3U5L2|||http://purl.uniprot.org/uniprot/Q3UGK2|||http://purl.uniprot.org/uniprot/Q3USM3|||http://purl.uniprot.org/uniprot/Q3UZ17|||http://purl.uniprot.org/uniprot/Q7TNC4 ^@ 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 ^@ 5-hydroxylysine; by JMJD6|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||Phosphoserine|||Putative RNA-binding protein Luc7-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000187283|||http://purl.uniprot.org/annotation/VSP_010218|||http://purl.uniprot.org/annotation/VSP_010219|||http://purl.uniprot.org/annotation/VSP_010220 http://togogenome.org/gene/10090:Or4d1 ^@ http://purl.uniprot.org/uniprot/Q5SW48 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mrap2 ^@ http://purl.uniprot.org/uniprot/D3Z1Q2 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Melanocortin-2 receptor accessory protein 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000424027 http://togogenome.org/gene/10090:Uts2b ^@ http://purl.uniprot.org/uniprot/Q3V249|||http://purl.uniprot.org/uniprot/Q765I1 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Peptide|||Propeptide|||Signal Peptide ^@ Urotensin-2B ^@ http://purl.uniprot.org/annotation/PRO_0000036359|||http://purl.uniprot.org/annotation/PRO_0000036360|||http://purl.uniprot.org/annotation/PRO_5015097528 http://togogenome.org/gene/10090:Slc12a4 ^@ http://purl.uniprot.org/uniprot/F8WIJ0|||http://purl.uniprot.org/uniprot/Q3TPD4|||http://purl.uniprot.org/uniprot/Q3TWZ6|||http://purl.uniprot.org/uniprot/Q3UDQ8|||http://purl.uniprot.org/uniprot/Q9JIS8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Amino acid permease/ SLC12A|||Basic and acidic residues|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||SLC12A transporter C-terminal|||Solute carrier family 12 member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000178031 http://togogenome.org/gene/10090:Bbs4 ^@ http://purl.uniprot.org/uniprot/A6H669|||http://purl.uniprot.org/uniprot/Q8C1Z7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ Bardet-Biedl syndrome 4 protein homolog|||Disordered|||Interaction with PCM1|||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_0000106264 http://togogenome.org/gene/10090:Tfdp1 ^@ http://purl.uniprot.org/uniprot/Q08639|||http://purl.uniprot.org/uniprot/Q3V3X3|||http://purl.uniprot.org/uniprot/Q9CYZ7|||http://purl.uniprot.org/uniprot/Q9D297 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Acidic residues|||DCB1|||DCB2|||DEF box|||Dimerization|||Disordered|||E2F/DP family winged-helix DNA-binding|||Enhances binding of RB protein to E2F|||Interaction with CEBPA|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Transcription factor DP C-terminal|||Transcription factor Dp-1 ^@ http://purl.uniprot.org/annotation/PRO_0000219476 http://togogenome.org/gene/10090:Klkb1 ^@ http://purl.uniprot.org/uniprot/P26262 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Apple 1|||Apple 2|||Apple 3|||Apple 4|||Charge relay system|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Plasma kallikrein heavy chain|||Plasma kallikrein light chain ^@ http://purl.uniprot.org/annotation/PRO_0000028023|||http://purl.uniprot.org/annotation/PRO_0000028024 http://togogenome.org/gene/10090:Zfp956 ^@ http://purl.uniprot.org/uniprot/Q3UZY6|||http://purl.uniprot.org/uniprot/Q4VA54|||http://purl.uniprot.org/uniprot/Q8BR38 ^@ Coiled-Coil|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Region ^@ C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Gpm6b ^@ http://purl.uniprot.org/uniprot/A2AEG3|||http://purl.uniprot.org/uniprot/A2AEG6|||http://purl.uniprot.org/uniprot/P35803|||http://purl.uniprot.org/uniprot/Q3US81|||http://purl.uniprot.org/uniprot/Q3V0Z9 ^@ Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 8.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Neuronal membrane glycoprotein M6-b|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000159022|||http://purl.uniprot.org/annotation/VSP_007318|||http://purl.uniprot.org/annotation/VSP_007319|||http://purl.uniprot.org/annotation/VSP_007320|||http://purl.uniprot.org/annotation/VSP_007321|||http://purl.uniprot.org/annotation/VSP_007322|||http://purl.uniprot.org/annotation/VSP_007323|||http://purl.uniprot.org/annotation/VSP_007324|||http://purl.uniprot.org/annotation/VSP_007325 http://togogenome.org/gene/10090:Dmxl1 ^@ http://purl.uniprot.org/uniprot/Q6PNC0 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||DmX-like protein 1|||Phosphoserine|||Polar residues|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000223323 http://togogenome.org/gene/10090:Stambpl1 ^@ http://purl.uniprot.org/uniprot/Q76N33 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Site|||Splice Variant ^@ AMSH-like protease|||In isoform 2.|||Indirect zinc-binding|||JAMM motif|||MPN|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000194875|||http://purl.uniprot.org/annotation/VSP_014649 http://togogenome.org/gene/10090:Med19 ^@ http://purl.uniprot.org/uniprot/Q8C1S0 ^@ 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|||Mediator of RNA polymerase II transcription subunit 19|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000304767 http://togogenome.org/gene/10090:Rab1a ^@ http://purl.uniprot.org/uniprot/P62821|||http://purl.uniprot.org/uniprot/Q0PD67 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region ^@ Disordered|||Effector region|||N-acetylserine|||Phosphoserine; by CDK1|||Polar residues|||Ras-related protein Rab-1A|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121057 http://togogenome.org/gene/10090:Gstz1 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VNC1|||http://purl.uniprot.org/uniprot/Q9JJA0|||http://purl.uniprot.org/uniprot/Q9WVL0 ^@ 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 ^@ GST C-terminal|||GST N-terminal|||Maleylacetoacetate isomerase|||N-acetylmethionine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000186023 http://togogenome.org/gene/10090:Gdpgp1 ^@ http://purl.uniprot.org/uniprot/Q3TLS3 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Sequence Conflict ^@ GDP-D-glucose phosphorylase 1|||Tele-GMP-histidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000336752 http://togogenome.org/gene/10090:Immt ^@ http://purl.uniprot.org/uniprot/E9Q800|||http://purl.uniprot.org/uniprot/E9QAY6|||http://purl.uniprot.org/uniprot/Q3TEY5|||http://purl.uniprot.org/uniprot/Q3TVZ5|||http://purl.uniprot.org/uniprot/Q3U7N2|||http://purl.uniprot.org/uniprot/Q8CAQ8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Disordered|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||MICOS complex subunit Mic60|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084185|||http://purl.uniprot.org/annotation/VSP_007003|||http://purl.uniprot.org/annotation/VSP_007004|||http://purl.uniprot.org/annotation/VSP_007005|||http://purl.uniprot.org/annotation/VSP_013222|||http://purl.uniprot.org/annotation/VSP_013223|||http://purl.uniprot.org/annotation/VSP_013224 http://togogenome.org/gene/10090:Fam170a ^@ http://purl.uniprot.org/uniprot/Q66LM6 ^@ 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|||C2H2-type; degenerate|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM170A ^@ http://purl.uniprot.org/annotation/PRO_0000326112|||http://purl.uniprot.org/annotation/VSP_032558 http://togogenome.org/gene/10090:Pou2af3 ^@ http://purl.uniprot.org/uniprot/F8VPY8 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ In isoform 2.|||OCA|||POU Class 2 homeobox-associating factor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000456713|||http://purl.uniprot.org/annotation/VSP_061668 http://togogenome.org/gene/10090:Serinc3 ^@ http://purl.uniprot.org/uniprot/Q9QZI9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Serine incorporator 3 ^@ http://purl.uniprot.org/annotation/PRO_0000218971 http://togogenome.org/gene/10090:Or5p51 ^@ http://purl.uniprot.org/uniprot/Q8VF65 ^@ 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 5P51 ^@ http://purl.uniprot.org/annotation/PRO_0000150831 http://togogenome.org/gene/10090:Gm8104 ^@ http://purl.uniprot.org/uniprot/K7N744 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:Fam234a ^@ http://purl.uniprot.org/uniprot/Q8C0Z1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein FAM234A ^@ http://purl.uniprot.org/annotation/PRO_0000247994 http://togogenome.org/gene/10090:Mug1 ^@ http://purl.uniprot.org/uniprot/P28665 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Bait region|||Basic and acidic residues|||Disordered|||Isoglutamyl cysteine thioester (Cys-Gln)|||Murinoglobulin-1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000000059 http://togogenome.org/gene/10090:Osbpl11 ^@ http://purl.uniprot.org/uniprot/G5E8A0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Gtf3a ^@ http://purl.uniprot.org/uniprot/Q8VHT7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||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|||C2H2-type 9|||Disordered|||Polar residues|||Transcription factor IIIA ^@ http://purl.uniprot.org/annotation/PRO_0000319866 http://togogenome.org/gene/10090:Itgbl1 ^@ http://purl.uniprot.org/uniprot/Q8VDV0 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Cysteine-rich tandem repeats|||I|||II|||III|||IV|||IX|||In isoform 2.|||Integrin beta-like protein 1|||N-linked (GlcNAc...) asparagine|||V|||VI|||VII|||VIII|||X ^@ http://purl.uniprot.org/annotation/PRO_0000323023|||http://purl.uniprot.org/annotation/VSP_032005|||http://purl.uniprot.org/annotation/VSP_032006 http://togogenome.org/gene/10090:Ccdc17 ^@ http://purl.uniprot.org/uniprot/Q8CE13 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 17|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000302853 http://togogenome.org/gene/10090:Prx ^@ http://purl.uniprot.org/uniprot/E9QQ57|||http://purl.uniprot.org/uniprot/O55103 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Splice Variant ^@ 1|||10|||11|||12|||13; approximate|||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|||45 X 5 AA approximate tandem repeats of [LVMGIED]-[PQSKHARMI]-[EDKLVTR]-[LIVMAP]-[AQKHRPEVSD]; that may have a tripeptide spacer of [LVIDEA]-[PMSVI]-[KEATDQ]|||5|||6|||7|||8|||9|||Disordered|||In isoform 2.|||Nuclear export signal|||Nuclear localization signal|||PDZ|||Periaxin|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000058564|||http://purl.uniprot.org/annotation/VSP_004366|||http://purl.uniprot.org/annotation/VSP_004367 http://togogenome.org/gene/10090:Magoh ^@ http://purl.uniprot.org/uniprot/P61327 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ N-acetylmethionine|||Protein mago nashi homolog ^@ http://purl.uniprot.org/annotation/PRO_0000174147 http://togogenome.org/gene/10090:Slc26a2 ^@ http://purl.uniprot.org/uniprot/Q62273 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Loss of sulfate-chloride exchange activity.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Reduced sulfate-chloride exchange activity.|||STAS|||Sulfate transporter ^@ http://purl.uniprot.org/annotation/PRO_0000080159 http://togogenome.org/gene/10090:Nek10 ^@ http://purl.uniprot.org/uniprot/K3W4R8|||http://purl.uniprot.org/uniprot/Q3UGM2 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek10 ^@ http://purl.uniprot.org/annotation/PRO_0000283794|||http://purl.uniprot.org/annotation/VSP_052352|||http://purl.uniprot.org/annotation/VSP_052353 http://togogenome.org/gene/10090:Col12a1 ^@ http://purl.uniprot.org/uniprot/Q60847 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 4-hydroxyproline|||Basic and acidic residues|||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 isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||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_0000005784|||http://purl.uniprot.org/annotation/VSP_001150|||http://purl.uniprot.org/annotation/VSP_001151|||http://purl.uniprot.org/annotation/VSP_001152|||http://purl.uniprot.org/annotation/VSP_023404|||http://purl.uniprot.org/annotation/VSP_023405 http://togogenome.org/gene/10090:Snai2 ^@ http://purl.uniprot.org/uniprot/P97469|||http://purl.uniprot.org/uniprot/Q3UZ96 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; atypical|||Disordered|||Polar residues|||SNAG domain|||Zinc finger protein SNAI2 ^@ http://purl.uniprot.org/annotation/PRO_0000047033 http://togogenome.org/gene/10090:Uchl5 ^@ http://purl.uniprot.org/uniprot/Q9WUP7 ^@ Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand ^@ Active Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand ^@ Important for enzyme activity|||In isoform 2.|||Interaction with ADRM1|||N6-acetyllysine|||N6-succinyllysine|||Nucleophile|||Proton donor|||Ubiquitin carboxyl-terminal hydrolase isozyme L5 ^@ http://purl.uniprot.org/annotation/PRO_0000211067|||http://purl.uniprot.org/annotation/VSP_005255 http://togogenome.org/gene/10090:Usp53 ^@ http://purl.uniprot.org/uniprot/P15975 ^@ 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 ^@ Associated with a progressive hearing loss; outer hair cells degenerate rapidly after the first postnatal week.|||Basic and acidic residues|||Disordered|||In isoform 2.|||Inactive ubiquitin carboxyl-terminal hydrolase 53|||Polar residues|||USP ^@ http://purl.uniprot.org/annotation/PRO_0000080682|||http://purl.uniprot.org/annotation/VSP_058590|||http://purl.uniprot.org/annotation/VSP_058591 http://togogenome.org/gene/10090:4833420G17Rik ^@ http://purl.uniprot.org/uniprot/Q3UJC8 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Uncharacterized protein C5orf34 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000295898|||http://purl.uniprot.org/annotation/VSP_027120|||http://purl.uniprot.org/annotation/VSP_027121 http://togogenome.org/gene/10090:Atp10a ^@ http://purl.uniprot.org/uniprot/O54827|||http://purl.uniprot.org/uniprot/Q3V1Y7|||http://purl.uniprot.org/uniprot/Q6A046 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Exoplasmic loop|||Helical|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Phospholipid-transporting ATPase VA|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000046380 http://togogenome.org/gene/10090:2300002M23Rik ^@ http://purl.uniprot.org/uniprot/Q8BM15 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Uncharacterized protein C6orf15 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000363883 http://togogenome.org/gene/10090:Srpk1 ^@ http://purl.uniprot.org/uniprot/O70551|||http://purl.uniprot.org/uniprot/Q3UB06|||http://purl.uniprot.org/uniprot/Q3URR1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||SRSF protein kinase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000086675 http://togogenome.org/gene/10090:Cyp2s1 ^@ http://purl.uniprot.org/uniprot/Q9DBX6 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Cytochrome P450 2S1|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051781 http://togogenome.org/gene/10090:Mmadhc ^@ http://purl.uniprot.org/uniprot/Q99LS1 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Modified Residue|||Strand|||Transit Peptide|||Turn ^@ Cobalamin trafficking protein CblD|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000019535 http://togogenome.org/gene/10090:Fut4 ^@ http://purl.uniprot.org/uniprot/Q11127|||http://purl.uniprot.org/uniprot/Q544B8 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Alpha-(1,3)-fucosyltransferase 4|||Cytoplasmic|||Fucosyltransferase N-terminal|||Helical; Signal-anchor for type II membrane protein|||In isoform Short.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000221101|||http://purl.uniprot.org/annotation/VSP_001778 http://togogenome.org/gene/10090:Klhl32 ^@ http://purl.uniprot.org/uniprot/A2AJX0|||http://purl.uniprot.org/uniprot/E9Q7Q2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Fam167a ^@ http://purl.uniprot.org/uniprot/Q6P1G6 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Disordered|||Protein FAM167A ^@ http://purl.uniprot.org/annotation/PRO_0000301687 http://togogenome.org/gene/10090:Stk33 ^@ http://purl.uniprot.org/uniprot/Q924X7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 33 ^@ http://purl.uniprot.org/annotation/PRO_0000278477 http://togogenome.org/gene/10090:Prox1 ^@ http://purl.uniprot.org/uniprot/P48437 ^@ 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|||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_0000208881 http://togogenome.org/gene/10090:Lsm5 ^@ http://purl.uniprot.org/uniprot/P62322 ^@ 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 LSm5 ^@ http://purl.uniprot.org/annotation/PRO_0000125573 http://togogenome.org/gene/10090:Snx8 ^@ http://purl.uniprot.org/uniprot/Q8CFD4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||PX|||Phosphoserine|||Phosphothreonine|||Sorting nexin-8 ^@ http://purl.uniprot.org/annotation/PRO_0000236199 http://togogenome.org/gene/10090:Or8h9 ^@ http://purl.uniprot.org/uniprot/Q8VG37 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Paxip1 ^@ http://purl.uniprot.org/uniprot/Q6NZQ4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Acidic residues|||BRCT 1|||BRCT 2|||BRCT 3|||BRCT 4|||BRCT 5|||BRCT 6|||Basic and acidic residues|||Disordered|||Interaction with PAGR1|||Interaction with TP53BP1|||Nuclear localization signal|||PAX-interacting protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000296263 http://togogenome.org/gene/10090:Igfals ^@ http://purl.uniprot.org/uniprot/A0A0R4J0S2|||http://purl.uniprot.org/uniprot/P70389 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide ^@ 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_0000020696|||http://purl.uniprot.org/annotation/PRO_5006451992 http://togogenome.org/gene/10090:Exoc1 ^@ http://purl.uniprot.org/uniprot/Q5PPR2|||http://purl.uniprot.org/uniprot/Q6P1Y9|||http://purl.uniprot.org/uniprot/Q8R3S6 ^@ 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|||Exocyst complex component 1|||Exocyst complex component Sec3 PIP2-binding N-terminal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000118914 http://togogenome.org/gene/10090:Pnlip ^@ http://purl.uniprot.org/uniprot/Q6P8U6 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Charge relay system|||Nucleophile|||PLAT|||Pancreatic triacylglycerol lipase ^@ http://purl.uniprot.org/annotation/PRO_0000401139 http://togogenome.org/gene/10090:Pigg ^@ http://purl.uniprot.org/uniprot/D3Z3Y1|||http://purl.uniprot.org/uniprot/D3Z4I0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ GPI ethanolamine phosphate transferase 2 C-terminal|||Helical ^@ http://togogenome.org/gene/10090:Or14j6 ^@ http://purl.uniprot.org/uniprot/Q8VF25 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rasgrp4 ^@ http://purl.uniprot.org/uniprot/Q8BTM9 ^@ 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 ^@ Disordered|||EF-hand|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-terminal Ras-GEF|||Phorbol-ester/DAG-type|||Polar residues|||RAS guanyl-releasing protein 4|||Ras-GEF ^@ http://purl.uniprot.org/annotation/PRO_0000315214|||http://purl.uniprot.org/annotation/VSP_030483|||http://purl.uniprot.org/annotation/VSP_030484|||http://purl.uniprot.org/annotation/VSP_030485|||http://purl.uniprot.org/annotation/VSP_030486|||http://purl.uniprot.org/annotation/VSP_030487 http://togogenome.org/gene/10090:Or4c102 ^@ http://purl.uniprot.org/uniprot/A2AV11 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bmp15 ^@ http://purl.uniprot.org/uniprot/Q9Z0L4 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Signal Peptide ^@ Bone morphogenetic protein 15|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033894|||http://purl.uniprot.org/annotation/PRO_0000033895 http://togogenome.org/gene/10090:Zfp658 ^@ http://purl.uniprot.org/uniprot/Q5PPQ4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:P2rx1 ^@ http://purl.uniprot.org/uniprot/P51576 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 1|||Phosphoserine|||Phosphothreonine|||Pore-forming motif ^@ http://purl.uniprot.org/annotation/PRO_0000161546 http://togogenome.org/gene/10090:Dmgdh ^@ http://purl.uniprot.org/uniprot/Q9DBT9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Dimethylglycine dehydrogenase, mitochondrial|||Disordered|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Tele-8alpha-FAD histidine ^@ http://purl.uniprot.org/annotation/PRO_0000010768 http://togogenome.org/gene/10090:Tmprss11b ^@ http://purl.uniprot.org/uniprot/Q14C59 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||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-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000299320 http://togogenome.org/gene/10090:Tpsb2 ^@ http://purl.uniprot.org/uniprot/E9QJW9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5040054269 http://togogenome.org/gene/10090:Tmed6 ^@ http://purl.uniprot.org/uniprot/Q9CQG0 ^@ 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|||GOLD|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Transmembrane emp24 domain-containing protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000010394 http://togogenome.org/gene/10090:Eri1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0C8|||http://purl.uniprot.org/uniprot/Q7TMF2|||http://purl.uniprot.org/uniprot/Q8BV98 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ 3'-5' exoribonuclease 1|||Basic and acidic residues|||Disordered|||Exonuclease|||Helical|||Impairs binding to and processing of 5.8S rRNA; when associated with A-107.|||Impairs binding to and processing of 5.8S rRNA; when associated with A-108.|||No effect on binding to 5.8S rRNA; when associated with G-130.|||No effect on binding to 5.8S rRNA; when associated with G-132.|||Phosphoserine|||Proton acceptor|||SAP ^@ http://purl.uniprot.org/annotation/PRO_0000187008 http://togogenome.org/gene/10090:Itsn2 ^@ http://purl.uniprot.org/uniprot/B2RR82|||http://purl.uniprot.org/uniprot/E9QNG1|||http://purl.uniprot.org/uniprot/Q8CD59 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2|||DH|||Disordered|||EF-hand|||EH|||PH|||Polar residues|||SH3 ^@ http://togogenome.org/gene/10090:Kdelr2 ^@ http://purl.uniprot.org/uniprot/Q9CQM2 ^@ Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Site|||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|||Interaction with the K-D-E-L motif on target proteins|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000194156 http://togogenome.org/gene/10090:Unc50 ^@ http://purl.uniprot.org/uniprot/Q9CQ61 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Protein unc-50 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000308962 http://togogenome.org/gene/10090:Mtmr6 ^@ http://purl.uniprot.org/uniprot/Q8VE11 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ GRAM|||In isoform 2.|||Interaction with RAB1B|||Myotubularin phosphatase|||Myotubularin-related protein 6|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Probable loss of catalytic activity. Loss of macropinocytosis. ^@ http://purl.uniprot.org/annotation/PRO_0000367041|||http://purl.uniprot.org/annotation/VSP_060069 http://togogenome.org/gene/10090:Bckdk ^@ http://purl.uniprot.org/uniprot/O55028|||http://purl.uniprot.org/uniprot/Q3UCB5 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Histidine kinase|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by autocatalysis|||[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000023453 http://togogenome.org/gene/10090:Shroom3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1H8|||http://purl.uniprot.org/uniprot/A0A286YDQ8|||http://purl.uniprot.org/uniprot/E9QMY5|||http://purl.uniprot.org/uniprot/Q9QXN0 ^@ 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 ^@ ASD1|||ASD2|||Basic and acidic residues|||Disordered|||Does not affect binding to ROCK1.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Loss of binding to ROCK1 and ability to trigger apical constriction in cells.|||Loss of dimerization, binding to ROCK1 and ability to trigger apical constriction in cells.|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein Shroom3|||Reduces binding to ROCK1 and ability to trigger apical constriction in cells. ^@ http://purl.uniprot.org/annotation/PRO_0000286067|||http://purl.uniprot.org/annotation/VSP_024969|||http://purl.uniprot.org/annotation/VSP_024970 http://togogenome.org/gene/10090:Or5ac15 ^@ http://purl.uniprot.org/uniprot/L7N1Y8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Agr3 ^@ http://purl.uniprot.org/uniprot/Q8R3W7 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Motif|||Sequence Conflict|||Signal Peptide ^@ Anterior gradient protein 3|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000001041 http://togogenome.org/gene/10090:Psmb11 ^@ http://purl.uniprot.org/uniprot/Q8BG41 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Modified Residue|||Propeptide|||Sequence Conflict ^@ Nucleophile|||Phosphoserine|||Proteasome subunit beta type-11|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000300013|||http://purl.uniprot.org/annotation/PRO_0000300014 http://togogenome.org/gene/10090:Gbgt1 ^@ http://purl.uniprot.org/uniprot/Q8VI38 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000157296 http://togogenome.org/gene/10090:Rhox4b ^@ http://purl.uniprot.org/uniprot/Q9JI43 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Zc3h11a ^@ http://purl.uniprot.org/uniprot/Q3UL31|||http://purl.uniprot.org/uniprot/Q6NZF1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger CCCH domain-containing protein 11A ^@ http://purl.uniprot.org/annotation/PRO_0000213906 http://togogenome.org/gene/10090:Gc ^@ http://purl.uniprot.org/uniprot/P21614 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Albumin 1|||Albumin 2|||Albumin 3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Vitamin D-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000001103 http://togogenome.org/gene/10090:Sri ^@ http://purl.uniprot.org/uniprot/Q6P069 ^@ 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 ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||Phosphoserine|||Sorcin ^@ http://purl.uniprot.org/annotation/PRO_0000073726|||http://purl.uniprot.org/annotation/VSP_013448 http://togogenome.org/gene/10090:Ankra2 ^@ http://purl.uniprot.org/uniprot/A0A286YDH7|||http://purl.uniprot.org/uniprot/D3Z4I1|||http://purl.uniprot.org/uniprot/Q3UTL3|||http://purl.uniprot.org/uniprot/Q6AXE4|||http://purl.uniprot.org/uniprot/Q6NZJ1|||http://purl.uniprot.org/uniprot/Q8C4M9|||http://purl.uniprot.org/uniprot/Q99PE2 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat family A protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000066896 http://togogenome.org/gene/10090:Alkbh7 ^@ http://purl.uniprot.org/uniprot/Q9D6Z0 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial|||In isoform 2.|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000239289|||http://purl.uniprot.org/annotation/VSP_019132 http://togogenome.org/gene/10090:Ssh2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J2A0|||http://purl.uniprot.org/uniprot/Q5SW75 ^@ 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 ^@ Abrogates phosphatase activity.|||Basic and acidic residues|||DEK-C|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||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_0000094844|||http://purl.uniprot.org/annotation/VSP_016326|||http://purl.uniprot.org/annotation/VSP_016327|||http://purl.uniprot.org/annotation/VSP_016328|||http://purl.uniprot.org/annotation/VSP_016329 http://togogenome.org/gene/10090:Tmem115 ^@ http://purl.uniprot.org/uniprot/Q543Y8|||http://purl.uniprot.org/uniprot/Q9WUH1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||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_0000058452 http://togogenome.org/gene/10090:Prdx2 ^@ http://purl.uniprot.org/uniprot/Q5M9N9|||http://purl.uniprot.org/uniprot/Q61171 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Cysteine sulfenic acid (-SOH) intermediate|||Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity|||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_0000135081 http://togogenome.org/gene/10090:Rdh11 ^@ http://purl.uniprot.org/uniprot/Q9QYF1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||N6-acetyllysine|||Proton acceptor|||Retinol dehydrogenase 11 ^@ http://purl.uniprot.org/annotation/PRO_0000054764 http://togogenome.org/gene/10090:Znrf2 ^@ http://purl.uniprot.org/uniprot/Q71FD5 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase ZNRF2|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||RING-type; atypical|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000277804 http://togogenome.org/gene/10090:Or7g32 ^@ http://purl.uniprot.org/uniprot/Q8VFF2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Apba1 ^@ http://purl.uniprot.org/uniprot/B2RUJ5 ^@ 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 ^@ Amyloid-beta A4 precursor protein-binding family A member 1|||Autoinhibitory helix linker|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||PDZ 1|||PDZ 2|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000417501|||http://purl.uniprot.org/annotation/VSP_043763|||http://purl.uniprot.org/annotation/VSP_043764|||http://purl.uniprot.org/annotation/VSP_053519 http://togogenome.org/gene/10090:Vmn1r72 ^@ http://purl.uniprot.org/uniprot/Q8K3N7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Faap20 ^@ http://purl.uniprot.org/uniprot/Q3UN58 ^@ 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|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||Fanconi anemia core complex-associated protein 20|||In isoform 2.|||In isoform 3.|||Phosphoserine|||UBZ2-type ^@ http://purl.uniprot.org/annotation/PRO_0000316883|||http://purl.uniprot.org/annotation/VSP_030817|||http://purl.uniprot.org/annotation/VSP_030818 http://togogenome.org/gene/10090:Gsc2 ^@ http://purl.uniprot.org/uniprot/A0A8Q0LQJ1|||http://purl.uniprot.org/uniprot/P56916 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Homeobox protein goosecoid-2 ^@ http://purl.uniprot.org/annotation/PRO_0000048892 http://togogenome.org/gene/10090:Tmem102 ^@ http://purl.uniprot.org/uniprot/Q3UPR7 ^@ 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|||Transmembrane protein 102 ^@ http://purl.uniprot.org/annotation/PRO_0000263649 http://togogenome.org/gene/10090:Casp3 ^@ http://purl.uniprot.org/uniprot/P70677 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Modified Residue|||Propeptide|||Sequence Conflict ^@ Caspase-3 subunit p12|||Caspase-3 subunit p17|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||S-nitrosocysteine; in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000004573|||http://purl.uniprot.org/annotation/PRO_0000004574|||http://purl.uniprot.org/annotation/PRO_0000004575|||http://purl.uniprot.org/annotation/PRO_0000004576 http://togogenome.org/gene/10090:Rilpl1 ^@ http://purl.uniprot.org/uniprot/Q9JJC6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||RH1|||RH2|||RILP-like protein 1|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000299311 http://togogenome.org/gene/10090:Pop1 ^@ http://purl.uniprot.org/uniprot/Q8K205|||http://purl.uniprot.org/uniprot/Q9D4G5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||POPLD|||Polar residues|||Pop1 N-terminal ^@ http://togogenome.org/gene/10090:Zscan18 ^@ http://purl.uniprot.org/uniprot/E9PUD6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues|||SCAN box ^@ http://togogenome.org/gene/10090:H2aj ^@ http://purl.uniprot.org/uniprot/Q8R1M2 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Histone H2A.J|||N5-methylglutamine|||N6-acetyllysine|||N6-lactoyllysine; alternate|||Phosphothreonine; by DCAF1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000344249 http://togogenome.org/gene/10090:Glycam1 ^@ http://purl.uniprot.org/uniprot/A0A2I3BPT0|||http://purl.uniprot.org/uniprot/Q02596 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Glycosylation-dependent cell adhesion molecule 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000025406|||http://purl.uniprot.org/annotation/PRO_5015081072 http://togogenome.org/gene/10090:Mtor ^@ http://purl.uniprot.org/uniprot/Q9JLN9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Abolishes interaction with the FKBP1A-rapamycin complex.|||Activation loop|||Catalytic loop|||Disordered|||FAT|||FATC|||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 isoform 2.|||Interaction with MLST8|||Interaction with NBN|||Knockin macrophages display reduced mTORC1 activity.|||N-acetylmethionine|||N6-acetyllysine|||PI3K/PI4K catalytic|||Phosphoserine|||Phosphoserine; by RPS6KB1|||Phosphoserine; by TBK1|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1|||Phosphothreonine; by RPS6KB1|||Serine/threonine-protein kinase mTOR|||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_0000088809|||http://purl.uniprot.org/annotation/VSP_011909|||http://purl.uniprot.org/annotation/VSP_011910 http://togogenome.org/gene/10090:Nmt2 ^@ http://purl.uniprot.org/uniprot/A2AJH3|||http://purl.uniprot.org/uniprot/F7APP3|||http://purl.uniprot.org/uniprot/O70311|||http://purl.uniprot.org/uniprot/Q3THR4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic 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_0000064227 http://togogenome.org/gene/10090:Clstn3 ^@ http://purl.uniprot.org/uniprot/D3Z601|||http://purl.uniprot.org/uniprot/Q99JH7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 2|||Calsyntenin-3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform CLSTN3beta.|||Increased KLC1-binding.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000004027|||http://purl.uniprot.org/annotation/VSP_061881 http://togogenome.org/gene/10090:Orc3 ^@ http://purl.uniprot.org/uniprot/Q9JK30 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Origin recognition complex subunit 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000127084|||http://purl.uniprot.org/annotation/VSP_026407 http://togogenome.org/gene/10090:Kiz ^@ http://purl.uniprot.org/uniprot/Q3UXL4 ^@ 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|||Centrosomal protein kizuna|||Disordered|||Phosphoserine|||Phosphothreonine; by PLK1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000301852 http://togogenome.org/gene/10090:Syt1 ^@ http://purl.uniprot.org/uniprot/H6RXZ1|||http://purl.uniprot.org/uniprot/P46096 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C2|||C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||No effect on calcium-dependent neurotransmitter release.|||Phospholipid binding|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Reduces affinity for calcium and results in decreased calcium-dependent neurotransmitter release.|||S-palmitoyl cysteine|||Synaptotagmin-1|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000183938 http://togogenome.org/gene/10090:Khdrbs2 ^@ http://purl.uniprot.org/uniprot/Q9WU01 ^@ 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.|||KH|||KH domain-containing, RNA-binding, signal transduction-associated protein 2|||Omega-N-methylarginine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000308954|||http://purl.uniprot.org/annotation/VSP_029065|||http://purl.uniprot.org/annotation/VSP_029066 http://togogenome.org/gene/10090:Btbd35f22 ^@ http://purl.uniprot.org/uniprot/J3QN64 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Vmn1r247 ^@ http://purl.uniprot.org/uniprot/D3YTW8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnksr2 ^@ http://purl.uniprot.org/uniprot/Q80YA9 ^@ 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|||Basic and acidic residues|||Basic residues|||CRIC|||Connector enhancer of kinase suppressor of ras 2|||DUF1170|||Disordered|||In isoform 2.|||PDZ|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000089971|||http://purl.uniprot.org/annotation/VSP_010890 http://togogenome.org/gene/10090:Sfrp1 ^@ http://purl.uniprot.org/uniprot/Q8C4U3 ^@ 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 ^@ FZ|||N-linked (GlcNAc...) asparagine|||NTR|||Secreted frizzled-related protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000032539 http://togogenome.org/gene/10090:Akr1c13 ^@ http://purl.uniprot.org/uniprot/Q571M4|||http://purl.uniprot.org/uniprot/Q8VC28 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Sequence Conflict|||Site|||Strand|||Turn ^@ Aldo-keto reductase family 1 member C13|||Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000124644 http://togogenome.org/gene/10090:Aasdhppt ^@ http://purl.uniprot.org/uniprot/Q9CQF6 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase ^@ http://purl.uniprot.org/annotation/PRO_0000175737|||http://purl.uniprot.org/annotation/VSP_016096 http://togogenome.org/gene/10090:Parp3 ^@ http://purl.uniprot.org/uniprot/Q3ULW8 ^@ 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 ^@ ADP-ribosyl aspartic acid|||ADP-ribosyl glutamic acid|||Basic and acidic residues|||Disordered|||In isoform 2.|||N6-(ADP-ribosyl)lysine|||Nuclear localization signal|||PARP alpha-helical|||PARP catalytic|||Protein mono-ADP-ribosyltransferase PARP3|||WGR ^@ http://purl.uniprot.org/annotation/PRO_0000446170|||http://purl.uniprot.org/annotation/VSP_060032 http://togogenome.org/gene/10090:Ap1b1 ^@ http://purl.uniprot.org/uniprot/O35643|||http://purl.uniprot.org/uniprot/Q8CC13 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 3'-nitrotyrosine|||AP-1 complex subunit beta-1|||Beta-adaptin appendage C-terminal subdomain|||Clathrin adaptor alpha/beta/gamma-adaptin appendage Ig-like subdomain|||Disordered|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000193739 http://togogenome.org/gene/10090:Fam114a1 ^@ http://purl.uniprot.org/uniprot/Q9D281 ^@ 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|||Phosphothreonine|||Polar residues|||Protein Noxp20 ^@ http://purl.uniprot.org/annotation/PRO_0000274562 http://togogenome.org/gene/10090:Polr1has ^@ http://purl.uniprot.org/uniprot/A0A0R4J0L3|||http://purl.uniprot.org/uniprot/Q8R0E5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Putative uncharacterized protein ZNRD1-AS1 ^@ http://purl.uniprot.org/annotation/PRO_0000324092 http://togogenome.org/gene/10090:Obox5 ^@ http://purl.uniprot.org/uniprot/G3X9P6 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Togaram1 ^@ http://purl.uniprot.org/uniprot/Q6A070 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Turn ^@ Abolishes association with microtubules and the ability to promote microtubule polymerization.|||Abolishes association with microtubules.|||Basic and acidic residues|||Disordered|||Expected to disrupt microtubule binding. Abolishes the ability to promote microtubule polymerization.|||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 isoform 2.|||Polar residues|||Resulty in increased tubulin polymerization in vitro.|||TOG 1|||TOG 2|||TOG 3|||TOG 4|||TOG array regulator of axonemal microtubules protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000251953|||http://purl.uniprot.org/annotation/VSP_047942 http://togogenome.org/gene/10090:Sharpin ^@ http://purl.uniprot.org/uniprot/Q91WA6 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ In isoform 2.|||Interaction with SHANK1|||Phosphoserine|||RanBP2-type|||Self-association|||Sharpin|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000280635|||http://purl.uniprot.org/annotation/VSP_023839 http://togogenome.org/gene/10090:Zfp644 ^@ http://purl.uniprot.org/uniprot/E9Q624|||http://purl.uniprot.org/uniprot/E9QA23|||http://purl.uniprot.org/uniprot/Q80TH4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Dgkh ^@ http://purl.uniprot.org/uniprot/A0A2I3BQ43|||http://purl.uniprot.org/uniprot/A0JP53|||http://purl.uniprot.org/uniprot/D3YXJ0 ^@ 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 ^@ DAGKc|||Diacylglycerol kinase eta|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||PH|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Polar residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000450665|||http://purl.uniprot.org/annotation/VSP_060668|||http://purl.uniprot.org/annotation/VSP_060669|||http://purl.uniprot.org/annotation/VSP_060670 http://togogenome.org/gene/10090:Arhgef3 ^@ http://purl.uniprot.org/uniprot/A0A286YDE6|||http://purl.uniprot.org/uniprot/A0A2X0SFN9|||http://purl.uniprot.org/uniprot/Q91X46 ^@ Chain|||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|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ DH|||Disordered|||In isoform 2.|||In isoform 3.|||PH|||Phosphoserine|||Rho guanine nucleotide exchange factor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000080913|||http://purl.uniprot.org/annotation/VSP_011613|||http://purl.uniprot.org/annotation/VSP_011614 http://togogenome.org/gene/10090:Btbd8 ^@ http://purl.uniprot.org/uniprot/Q3TEG0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Mcoln2 ^@ http://purl.uniprot.org/uniprot/Q8K595 ^@ Chain|||Disulfide Bond|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Helix|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Extracellular/lumenal pore loop|||Helical|||In isoform 2.|||Mucolipin-2|||Pore-forming|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000215366|||http://purl.uniprot.org/annotation/VSP_010822 http://togogenome.org/gene/10090:Rxrg ^@ http://purl.uniprot.org/uniprot/E9Q9V9|||http://purl.uniprot.org/uniprot/P28705 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Hinge|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Polar residues|||Retinoic acid receptor RXR-gamma ^@ http://purl.uniprot.org/annotation/PRO_0000053577 http://togogenome.org/gene/10090:Fkbp4 ^@ http://purl.uniprot.org/uniprot/P30416 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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|||Removed; alternate|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000075319|||http://purl.uniprot.org/annotation/PRO_0000391469 http://togogenome.org/gene/10090:Usp20 ^@ http://purl.uniprot.org/uniprot/Q8C6M1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||DUSP 1|||DUSP 2|||Disordered|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 20 ^@ http://purl.uniprot.org/annotation/PRO_0000390418 http://togogenome.org/gene/10090:Slc16a13 ^@ http://purl.uniprot.org/uniprot/Q8CE94 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Monocarboxylate transporter 13 ^@ http://purl.uniprot.org/annotation/PRO_0000287188 http://togogenome.org/gene/10090:Csnka2ip ^@ http://purl.uniprot.org/uniprot/A0A2K6EDK9|||http://purl.uniprot.org/uniprot/Q8CH19 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Casein kinase II subunit alpha'-interacting protein|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000436772 http://togogenome.org/gene/10090:Vmn1r256 ^@ http://purl.uniprot.org/uniprot/K9J7H2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ndufa13 ^@ http://purl.uniprot.org/uniprot/Q9ERS2 ^@ Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ Helical|||N-acetylalanine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118805 http://togogenome.org/gene/10090:Slc39a11 ^@ http://purl.uniprot.org/uniprot/Q8BWY7 ^@ 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 2.|||Zinc transporter ZIP11 ^@ http://purl.uniprot.org/annotation/PRO_0000308411|||http://purl.uniprot.org/annotation/VSP_028977|||http://purl.uniprot.org/annotation/VSP_028978 http://togogenome.org/gene/10090:Terf2ip ^@ http://purl.uniprot.org/uniprot/Q91VL8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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|||Polar residues|||Removed|||Telomeric repeat-binding factor 2-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000197127 http://togogenome.org/gene/10090:Matn3 ^@ http://purl.uniprot.org/uniprot/O35701 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Increased protein levels of Creld2 and Manf in chondrocytes. Prevents Matn3 protein aggregation; in association with A-72 and A-258.|||Matrilin-3|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine; by FAM20C|||Prevents Matn3 protein aggregation; in association with A-72 and D-189.|||Prevents Matn3 protein aggregation; in association with D-189 and A-258.|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000007658 http://togogenome.org/gene/10090:Tnpo1 ^@ http://purl.uniprot.org/uniprot/Q8BFY9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ 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.|||Transportin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000120766|||http://purl.uniprot.org/annotation/VSP_038030 http://togogenome.org/gene/10090:1700071K01Rik ^@ http://purl.uniprot.org/uniprot/Q3V2K0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Band 7 ^@ http://togogenome.org/gene/10090:Gtf2h4 ^@ http://purl.uniprot.org/uniprot/O70422|||http://purl.uniprot.org/uniprot/Q542U3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ General transcription factor IIH subunit 4|||Transcription factor Tfb2 C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000119254 http://togogenome.org/gene/10090:Atg4d ^@ http://purl.uniprot.org/uniprot/Q8BGV9 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||Cleavage; by CASP3|||Cryptic mitochondrial signal peptide|||Cysteine protease ATG4D|||Cysteine protease ATG4D, mitochondrial|||Disordered|||Increased programmed cell death in spermatogenic cells; decreased expression of MAP1LC3B.|||Nucleophile|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000215854|||http://purl.uniprot.org/annotation/PRO_0000423409 http://togogenome.org/gene/10090:Dtwd2 ^@ http://purl.uniprot.org/uniprot/B2RTH8|||http://purl.uniprot.org/uniprot/B7ZP35|||http://purl.uniprot.org/uniprot/Q9D0U1 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region ^@ DTW|||DXTW|||Disordered|||N-acetylmethionine|||Phosphoserine|||tRNA-uridine aminocarboxypropyltransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000271130 http://togogenome.org/gene/10090:Pias3 ^@ http://purl.uniprot.org/uniprot/O54714 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger ^@ Abolishes interaction with STAT3.|||Disordered|||E3 SUMO-protein ligase PIAS3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Greatly reduced interaction with STAT3.|||In isoform 2.|||In isoform 3.|||Interaction with CCAR2|||LXXLL motif|||Loss of promotion of IRF1 sumoylation, as well as of autosumoylation; partial loss of suppression of IRF1 transcriptional activity.|||Nuclear and cytoplasmic location.|||PINIT|||SAP|||SP-RING-type|||SUMO1-binding ^@ http://purl.uniprot.org/annotation/PRO_0000218980|||http://purl.uniprot.org/annotation/VSP_012203|||http://purl.uniprot.org/annotation/VSP_012204 http://togogenome.org/gene/10090:Rnase11 ^@ http://purl.uniprot.org/uniprot/Q5GAM9|||http://purl.uniprot.org/uniprot/W0UVF9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Putative inactive ribonuclease 11 ^@ http://purl.uniprot.org/annotation/PRO_0000415815|||http://purl.uniprot.org/annotation/PRO_5012407131 http://togogenome.org/gene/10090:Or4a73 ^@ http://purl.uniprot.org/uniprot/Q7TQZ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or13c7c ^@ http://purl.uniprot.org/uniprot/Q9QZ20 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Chd6 ^@ http://purl.uniprot.org/uniprot/A3KFM7|||http://purl.uniprot.org/uniprot/Q8BJ75 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Chromo|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 6|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Myb-like|||Phosphoserine|||Polar residues|||Required for DNA-dependent ATPase activity ^@ http://purl.uniprot.org/annotation/PRO_0000429353|||http://purl.uniprot.org/annotation/VSP_054901 http://togogenome.org/gene/10090:Hars ^@ http://purl.uniprot.org/uniprot/Q61035 ^@ 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 ^@ Histidine--tRNA ligase, cytoplasmic|||N-acetylalanine|||Phosphoserine|||Removed|||WHEP-TRS ^@ http://purl.uniprot.org/annotation/PRO_0000136334 http://togogenome.org/gene/10090:Tenm4 ^@ http://purl.uniprot.org/uniprot/Q3UHK6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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|||EGF-like 8|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||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_0000259509|||http://purl.uniprot.org/annotation/VSP_021404|||http://purl.uniprot.org/annotation/VSP_021405|||http://purl.uniprot.org/annotation/VSP_021406|||http://purl.uniprot.org/annotation/VSP_021407|||http://purl.uniprot.org/annotation/VSP_021408 http://togogenome.org/gene/10090:H4c9 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:B4galt7 ^@ http://purl.uniprot.org/uniprot/Q3TAW1|||http://purl.uniprot.org/uniprot/Q8R087 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Beta-1,4-galactosyltransferase 7|||Cytoplasmic|||Disordered|||Galactosyltransferase C-terminal|||Galactosyltransferase N-terminal|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000080551|||http://purl.uniprot.org/annotation/VSP_014231 http://togogenome.org/gene/10090:Ptpn5 ^@ http://purl.uniprot.org/uniprot/P54830|||http://purl.uniprot.org/uniprot/Q80WU9 ^@ 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|||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|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Disordered|||Helical|||In isoform STEP20 and isoform STEP46.|||In isoform STEP38 and isoform STEP20.|||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_0000094756|||http://purl.uniprot.org/annotation/VSP_005126|||http://purl.uniprot.org/annotation/VSP_005127|||http://purl.uniprot.org/annotation/VSP_005128 http://togogenome.org/gene/10090:Tcte1 ^@ http://purl.uniprot.org/uniprot/A6H639 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||Dynein regulatory complex subunit 5|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000326527 http://togogenome.org/gene/10090:Ccl17 ^@ http://purl.uniprot.org/uniprot/F6R5P4|||http://purl.uniprot.org/uniprot/Q9WUZ6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ C-C motif chemokine|||C-C motif chemokine 17|||Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_5005129866|||http://purl.uniprot.org/annotation/PRO_5015020191 http://togogenome.org/gene/10090:Rbm42 ^@ http://purl.uniprot.org/uniprot/Q91V81 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||N-acetylalanine|||Necessary for interaction with HNRNPK|||Phosphoserine|||Pro residues|||RNA-binding protein 42|||RRM|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000307751 http://togogenome.org/gene/10090:Fdps ^@ http://purl.uniprot.org/uniprot/Q920E5 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue|||Site ^@ Farnesyl pyrophosphate synthase|||Important for determining product chain length|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-acetyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000123945 http://togogenome.org/gene/10090:Cd55 ^@ http://purl.uniprot.org/uniprot/Q61475 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Complement decay-accelerating factor, GPI-anchored|||Disordered|||GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4 ^@ http://purl.uniprot.org/annotation/PRO_0000006004|||http://purl.uniprot.org/annotation/PRO_0000006005 http://togogenome.org/gene/10090:Dscc1 ^@ http://purl.uniprot.org/uniprot/Q14AI0 ^@ Chain|||Molecule Processing ^@ Chain ^@ Sister chromatid cohesion protein DCC1 ^@ http://purl.uniprot.org/annotation/PRO_0000318065 http://togogenome.org/gene/10090:Or10d4c ^@ http://purl.uniprot.org/uniprot/Q9EQ84 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Armc7 ^@ http://purl.uniprot.org/uniprot/Q3UJZ3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ ARM 1|||ARM 2|||Armadillo repeat-containing protein 7|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000242667 http://togogenome.org/gene/10090:H3c7 ^@ http://purl.uniprot.org/uniprot/B9EI85|||http://purl.uniprot.org/uniprot/P84228 ^@ Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||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 H2A/H2B/H3|||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; 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_0000221250 http://togogenome.org/gene/10090:Tff3 ^@ http://purl.uniprot.org/uniprot/Q62395 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Interchain|||P-type|||Trefoil factor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000023466 http://togogenome.org/gene/10090:Washc3 ^@ http://purl.uniprot.org/uniprot/G3UWG7|||http://purl.uniprot.org/uniprot/Q9CR27|||http://purl.uniprot.org/uniprot/Q9CYF6|||http://purl.uniprot.org/uniprot/S4R287 ^@ 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|||N-acetylmethionine|||Polar residues|||WASH complex subunit 3 ^@ http://purl.uniprot.org/annotation/PRO_0000076202 http://togogenome.org/gene/10090:Ccl6 ^@ http://purl.uniprot.org/uniprot/P27784 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ C-C motif chemokine 6|||CCL6(22-95)|||CCL6(23-95) ^@ http://purl.uniprot.org/annotation/PRO_0000005182|||http://purl.uniprot.org/annotation/PRO_0000041844|||http://purl.uniprot.org/annotation/PRO_0000041845 http://togogenome.org/gene/10090:Snrpb ^@ http://purl.uniprot.org/uniprot/P27048 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Pro residues|||Repeat-rich region|||Sm|||Small nuclear ribonucleoprotein-associated protein B ^@ http://purl.uniprot.org/annotation/PRO_0000125519 http://togogenome.org/gene/10090:Adra1b ^@ http://purl.uniprot.org/uniprot/Q9DBL0 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Tssk6 ^@ http://purl.uniprot.org/uniprot/Q925K9 ^@ 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|||Testis-specific serine/threonine-protein kinase 6 ^@ http://purl.uniprot.org/annotation/PRO_0000227747 http://togogenome.org/gene/10090:Opn3 ^@ http://purl.uniprot.org/uniprot/Q9WUK7 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis 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|||N6-(retinylidene)lysine|||Opsin-3|||Reduced basal glucose uptake and glucose-dependent mitochondrial respiration.|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000197814 http://togogenome.org/gene/10090:Cd200r2 ^@ http://purl.uniprot.org/uniprot/Q6XJV6 ^@ 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 ^@ Cell surface glycoprotein CD200 receptor 2|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000346452 http://togogenome.org/gene/10090:Zbtb10 ^@ http://purl.uniprot.org/uniprot/E9Q8X5|||http://purl.uniprot.org/uniprot/Q8BNK5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||BTB|||C2H2-type|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Hmga1 ^@ http://purl.uniprot.org/uniprot/A0A338P6E8|||http://purl.uniprot.org/uniprot/A0A338P6F6|||http://purl.uniprot.org/uniprot/P17095|||http://purl.uniprot.org/uniprot/Q3TE85|||http://purl.uniprot.org/uniprot/Q3TVP0|||http://purl.uniprot.org/uniprot/Q566K0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||High mobility group protein HMG-I/HMG-Y|||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 HIPK2 and CDC2|||Phosphothreonine|||Phosphothreonine; by HIPK2 and CDC2|||Polar residues|||Removed|||Symmetric dimethylarginine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000206709|||http://purl.uniprot.org/annotation/VSP_012406 http://togogenome.org/gene/10090:Slc25a23 ^@ http://purl.uniprot.org/uniprot/Q6GQS1|||http://purl.uniprot.org/uniprot/Q9D908 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ 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|||Linker region|||Mitochondrial adenyl nucleotide antiporter SLC25A23|||Mitochondrial intermembrane|||Mitochondrial matrix|||Polar residues|||Regulatory N-terminal domain|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000317610 http://togogenome.org/gene/10090:Elof1 ^@ http://purl.uniprot.org/uniprot/P60003 ^@ Binding Site|||Chain|||Helix|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Strand|||Turn ^@ Transcription elongation factor 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000120942 http://togogenome.org/gene/10090:Or7g27 ^@ http://purl.uniprot.org/uniprot/Q7TRG2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dnmt3l ^@ http://purl.uniprot.org/uniprot/A3EWM2|||http://purl.uniprot.org/uniprot/Q9CWR8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Zinc Finger ^@ ADD|||DNA (cytosine-5)-methyltransferase 3-like|||Disordered|||GATA-type; atypical|||Loss of binding to DNMT3A.|||PHD-type|||PHD-type; atypical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000088048 http://togogenome.org/gene/10090:Zfp983 ^@ http://purl.uniprot.org/uniprot/E9PUT0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Map1s ^@ http://purl.uniprot.org/uniprot/Q8C052 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||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|||Necessary for the microtubule-organizing center localization|||Necessary for the mitochondrial aggregation and genome destruction|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000311382|||http://purl.uniprot.org/annotation/PRO_0000311383|||http://purl.uniprot.org/annotation/PRO_0000311384 http://togogenome.org/gene/10090:Jup ^@ http://purl.uniprot.org/uniprot/Q02257 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Repeat ^@ ARM 1|||ARM 10|||ARM 11|||ARM 12|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Interaction with DSC1|||Interaction with DSC1 and DSG1|||Junction plakoglobin|||N-acetylmethionine|||O-linked (GlcNAc) threonine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000064279 http://togogenome.org/gene/10090:Rbis ^@ http://purl.uniprot.org/uniprot/Q0VG62 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Ribosomal biogenesis factor ^@ http://purl.uniprot.org/annotation/PRO_0000324605|||http://purl.uniprot.org/annotation/VSP_060139 http://togogenome.org/gene/10090:Mplkip ^@ http://purl.uniprot.org/uniprot/B2RTG9|||http://purl.uniprot.org/uniprot/Q9D011 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Asymmetric dimethylarginine|||Disordered|||M-phase-specific PLK1-interacting protein|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000065675 http://togogenome.org/gene/10090:Vmn1r200 ^@ http://purl.uniprot.org/uniprot/Q8R281 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rbp7 ^@ http://purl.uniprot.org/uniprot/Q540P4|||http://purl.uniprot.org/uniprot/Q9EPC5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Cytosolic fatty-acid binding proteins|||Retinoid-binding protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000067404 http://togogenome.org/gene/10090:Gprc6a ^@ http://purl.uniprot.org/uniprot/Q8K4Z6 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||G-protein coupled receptor family C group 6 member A|||Helical|||In isoform 2.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000043197|||http://purl.uniprot.org/annotation/VSP_016456|||http://purl.uniprot.org/annotation/VSP_016457 http://togogenome.org/gene/10090:Gab1 ^@ http://purl.uniprot.org/uniprot/A0A1B0GS41|||http://purl.uniprot.org/uniprot/Q505A4|||http://purl.uniprot.org/uniprot/Q9QYY0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||GRB2-associated-binding protein 1|||N-acetylserine|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000050284 http://togogenome.org/gene/10090:Psmb2 ^@ http://purl.uniprot.org/uniprot/Q9R1P3 ^@ 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_0000148044 http://togogenome.org/gene/10090:Mthfr ^@ http://purl.uniprot.org/uniprot/A2A7F7|||http://purl.uniprot.org/uniprot/Q3UDB2|||http://purl.uniprot.org/uniprot/Q497H7|||http://purl.uniprot.org/uniprot/Q9WU20 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Disordered|||Methylenetetrahydrofolate reductase (NADPH)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000190247 http://togogenome.org/gene/10090:Bpifb2 ^@ http://purl.uniprot.org/uniprot/Q14AV3|||http://purl.uniprot.org/uniprot/Q8C1E1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ BPI fold-containing family B member 2|||Lipid-binding serum glycoprotein C-terminal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000017165|||http://purl.uniprot.org/annotation/PRO_5014306930 http://togogenome.org/gene/10090:Ptp4a1 ^@ http://purl.uniprot.org/uniprot/B9EKL6|||http://purl.uniprot.org/uniprot/Q63739 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Strand ^@ Abolishes activity.|||Cysteine methyl ester|||Interaction with ATF5|||Phosphocysteine intermediate|||Protein tyrosine phosphatase type IVA 1|||Proton donor|||Removed in mature form|||S-farnesyl cysteine|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094782|||http://purl.uniprot.org/annotation/PRO_0000396728 http://togogenome.org/gene/10090:Trim75 ^@ http://purl.uniprot.org/uniprot/B2RTB3|||http://purl.uniprot.org/uniprot/Q3UWZ0 ^@ 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 75 ^@ http://purl.uniprot.org/annotation/PRO_0000331193 http://togogenome.org/gene/10090:Ccl20 ^@ http://purl.uniprot.org/uniprot/O89093|||http://purl.uniprot.org/uniprot/Q54AI7|||http://purl.uniprot.org/uniprot/Q642U4 ^@ 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 ^@ C-C motif chemokine|||C-C motif chemokine 20|||Chemokine interleukin-8-like|||In isoform Short. ^@ http://purl.uniprot.org/annotation/PRO_0000005218|||http://purl.uniprot.org/annotation/PRO_5009998713|||http://purl.uniprot.org/annotation/PRO_5014205916|||http://purl.uniprot.org/annotation/VSP_001062 http://togogenome.org/gene/10090:Cdh17 ^@ http://purl.uniprot.org/uniprot/Q3U1Y7|||http://purl.uniprot.org/uniprot/Q9R100 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin domain-containing protein|||Cadherin-17|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000003813|||http://purl.uniprot.org/annotation/PRO_5004229744 http://togogenome.org/gene/10090:Mapkapk3 ^@ http://purl.uniprot.org/uniprot/Q09HN3|||http://purl.uniprot.org/uniprot/Q3UMW7 ^@ 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 ^@ Autoinhibitory helix|||Bipartite nuclear localization signal 1|||Bipartite nuclear localization signal 2|||Disordered|||In isoform 2.|||In isoform 3.|||MAP kinase-activated protein kinase 3|||N-acetylmethionine|||Nuclear export signal (NES)|||Phosphoserine; by MAPK14|||Phosphoserine; by autocatalysis|||Phosphothreonine; by MAPK14|||Polar residues|||Prevents degradation of isoform 3.|||Protein kinase|||Proton acceptor|||p38 MAPK-binding site ^@ http://purl.uniprot.org/annotation/PRO_0000086294|||http://purl.uniprot.org/annotation/VSP_016386|||http://purl.uniprot.org/annotation/VSP_016387|||http://purl.uniprot.org/annotation/VSP_042175|||http://purl.uniprot.org/annotation/VSP_042176 http://togogenome.org/gene/10090:Zfp36l1 ^@ http://purl.uniprot.org/uniprot/P23950|||http://purl.uniprot.org/uniprot/Q543H2 ^@ 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 ^@ C3H1-type|||C3H1-type 1|||C3H1-type 2|||Disordered|||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|||mRNA decay activator protein ZFP36L1 ^@ http://purl.uniprot.org/annotation/PRO_0000089168 http://togogenome.org/gene/10090:Vmn2r52 ^@ http://purl.uniprot.org/uniprot/L7N2B2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982459 http://togogenome.org/gene/10090:Ctsl ^@ http://purl.uniprot.org/uniprot/P06797|||http://purl.uniprot.org/uniprot/Q543M3 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Activation peptide|||Cathepsin L|||Cathepsin L heavy chain|||Cathepsin L light chain|||Cathepsin propeptide inhibitor|||Cleavage; by autolysis|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) (high mannose) asparagine|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000026248|||http://purl.uniprot.org/annotation/PRO_0000026249|||http://purl.uniprot.org/annotation/PRO_0000026250|||http://purl.uniprot.org/annotation/PRO_0000026251|||http://purl.uniprot.org/annotation/PRO_0000450792|||http://purl.uniprot.org/annotation/PRO_5014205866 http://togogenome.org/gene/10090:Nacad ^@ http://purl.uniprot.org/uniprot/Q5SWP3 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||NAC-A/B|||NAC-alpha domain-containing protein 1|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000280749 http://togogenome.org/gene/10090:Acap1 ^@ http://purl.uniprot.org/uniprot/Q8K2H4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ 3'-nitrotyrosine|||ANK 1|||ANK 2|||ANK 3|||Arf-GAP|||Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1|||BAR|||C4-type|||Disordered|||Loss of catalytic activity. No loss of accumulation of coat proteins on internal membranes upon overexpression of Acap1.|||PH|||Prevents interaction with ITGB1 when S-554 is not phosphorylated|||Pro residues|||Required for formation of endosomal tubules when overexpressed with PIP5K1C|||Required for interaction with GULP1 ^@ http://purl.uniprot.org/annotation/PRO_0000306384 http://togogenome.org/gene/10090:Smcr8 ^@ http://purl.uniprot.org/uniprot/Q3UMB5 ^@ 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|||Guanine nucleotide exchange protein SMCR8|||In isoform 2.|||Interacts with WDR41 within the C9orf72-SMCR8 complex|||Phosphoserine|||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_0000287470|||http://purl.uniprot.org/annotation/VSP_025488 http://togogenome.org/gene/10090:Hagh ^@ http://purl.uniprot.org/uniprot/A0A0R4J052|||http://purl.uniprot.org/uniprot/G5E8T9|||http://purl.uniprot.org/uniprot/Q99KB8 ^@ 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 ^@ Hydroxyacylglutathione hydrolase, mitochondrial|||In isoform 2.|||Metallo-beta-lactamase|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000192343|||http://purl.uniprot.org/annotation/VSP_037931 http://togogenome.org/gene/10090:Ubac2 ^@ http://purl.uniprot.org/uniprot/Q8R1K1|||http://purl.uniprot.org/uniprot/Q8R1R2 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||UBA|||Ubiquitin-associated domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000280756 http://togogenome.org/gene/10090:Ift80 ^@ http://purl.uniprot.org/uniprot/Q8K057 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Repeat|||Splice Variant ^@ In isoform 2.|||Intraflagellar transport protein 80 homolog|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051043|||http://purl.uniprot.org/annotation/VSP_027991|||http://purl.uniprot.org/annotation/VSP_027992 http://togogenome.org/gene/10090:Sybu ^@ http://purl.uniprot.org/uniprot/Q8BHS8 ^@ 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.|||In isoform 6.|||Phosphoserine|||Polar residues|||Sufficient for interaction with KIF5B|||Sufficient for interaction with STX1A|||Syntabulin ^@ http://purl.uniprot.org/annotation/PRO_0000245510|||http://purl.uniprot.org/annotation/VSP_019723|||http://purl.uniprot.org/annotation/VSP_019724|||http://purl.uniprot.org/annotation/VSP_019725|||http://purl.uniprot.org/annotation/VSP_019726|||http://purl.uniprot.org/annotation/VSP_019727|||http://purl.uniprot.org/annotation/VSP_019728 http://togogenome.org/gene/10090:Thsd7b ^@ http://purl.uniprot.org/uniprot/Q6P4U0 ^@ 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|||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_0000260252 http://togogenome.org/gene/10090:Hdac8 ^@ http://purl.uniprot.org/uniprot/Q8VH37 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Histone deacetylase|||Histone deacetylase 8|||In isoform 2.|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000114709|||http://purl.uniprot.org/annotation/VSP_007178|||http://purl.uniprot.org/annotation/VSP_007179 http://togogenome.org/gene/10090:Egf ^@ http://purl.uniprot.org/uniprot/A0A0G2JDT8|||http://purl.uniprot.org/uniprot/A0A0G2JF92|||http://purl.uniprot.org/uniprot/P01132|||http://purl.uniprot.org/uniprot/Q3UWD7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1; incomplete|||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|||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|||LDL-receptor class B 7|||LDL-receptor class B 8|||N-linked (GlcNAc...) asparagine|||Not required for full biological activity|||Pro-epidermal growth factor ^@ http://purl.uniprot.org/annotation/PRO_0000007542|||http://purl.uniprot.org/annotation/PRO_0000007543 http://togogenome.org/gene/10090:Tbc1d21 ^@ http://purl.uniprot.org/uniprot/Q9D9D3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Rab-GAP TBC|||TBC1 domain family member 21 ^@ http://purl.uniprot.org/annotation/PRO_0000436614 http://togogenome.org/gene/10090:Fbxw11 ^@ http://purl.uniprot.org/uniprot/Q5SRY7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ F-box|||F-box/WD repeat-containing protein 11|||Homodimerization domain D|||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_0000396126|||http://purl.uniprot.org/annotation/VSP_039579|||http://purl.uniprot.org/annotation/VSP_039580|||http://purl.uniprot.org/annotation/VSP_039581 http://togogenome.org/gene/10090:Tas2r123 ^@ http://purl.uniprot.org/uniprot/P59528 ^@ 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 123 ^@ http://purl.uniprot.org/annotation/PRO_0000082194 http://togogenome.org/gene/10090:Nop58 ^@ http://purl.uniprot.org/uniprot/Q6DFW4 ^@ 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 ^@ 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|||Nop|||Nucleolar protein 58|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000287350 http://togogenome.org/gene/10090:Klrb1f ^@ http://purl.uniprot.org/uniprot/I3QI43|||http://purl.uniprot.org/uniprot/Q8VD98 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Killer cell lectin-like receptor subfamily B member 1F|||LCK-binding motif|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000271480 http://togogenome.org/gene/10090:Kctd16 ^@ http://purl.uniprot.org/uniprot/Q5DTY9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ BTB|||BTB/POZ domain-containing protein KCTD16|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000248594 http://togogenome.org/gene/10090:Fmo9 ^@ http://purl.uniprot.org/uniprot/Q14DT3|||http://purl.uniprot.org/uniprot/Q8C116 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Prxl2a ^@ http://purl.uniprot.org/uniprot/Q3U125|||http://purl.uniprot.org/uniprot/Q9CYH2 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Region|||Transmembrane ^@ Helical|||Peroxiredoxin-like 2A|||Redox-active|||Thioredoxin-like fold ^@ http://purl.uniprot.org/annotation/PRO_0000019551 http://togogenome.org/gene/10090:Rhox4a2 ^@ http://purl.uniprot.org/uniprot/Q9D3I8 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Rtbdn ^@ http://purl.uniprot.org/uniprot/Q8QZY4 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ Retbindin ^@ http://purl.uniprot.org/annotation/PRO_0000043175 http://togogenome.org/gene/10090:Parm1 ^@ http://purl.uniprot.org/uniprot/Q923D3 ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Prostate androgen-regulated mucin-like protein 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000045499 http://togogenome.org/gene/10090:Ypel3 ^@ http://purl.uniprot.org/uniprot/P61237 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Protein yippee-like 3|||Yippee ^@ http://purl.uniprot.org/annotation/PRO_0000212390 http://togogenome.org/gene/10090:Chordc1 ^@ http://purl.uniprot.org/uniprot/Q9D1P4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Basic and acidic residues|||CHORD 1|||CHORD 2|||CS|||Cysteine and histidine-rich domain-containing protein 1|||Disordered|||Interaction with HSP90AA1 and HSP90AB1|||Interaction with PPP5C|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000317771 http://togogenome.org/gene/10090:Polr1b ^@ http://purl.uniprot.org/uniprot/P70700 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ C4-type|||DNA-directed RNA polymerase I subunit RPA2|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000048073 http://togogenome.org/gene/10090:Serpina5 ^@ http://purl.uniprot.org/uniprot/P70458|||http://purl.uniprot.org/uniprot/Q8BVN1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ N-linked (GlcNAc...) asparagine|||Plasma serine protease inhibitor|||Reactive bond|||Removed in mature form|||Serpin|||Serpin domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000032428|||http://purl.uniprot.org/annotation/PRO_0000414092|||http://purl.uniprot.org/annotation/PRO_5004306003 http://togogenome.org/gene/10090:Cenpf ^@ http://purl.uniprot.org/uniprot/E9Q3P4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Centromere protein Cenp-F N-terminal|||Centromere protein Cenp-F leucine-rich repeat-containing|||Disordered|||Kinetochore protein Cenp-F/LEK1 Rb protein-binding|||Polar residues ^@ http://togogenome.org/gene/10090:Sar1b ^@ http://purl.uniprot.org/uniprot/Q9CQC9 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ GTP-binding protein SAR1b|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000206262 http://togogenome.org/gene/10090:Nol12 ^@ http://purl.uniprot.org/uniprot/Q8BG17 ^@ 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|||Basic residues|||Disordered|||Nucleolar protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000271208 http://togogenome.org/gene/10090:Cryba4 ^@ http://purl.uniprot.org/uniprot/E9QAS6|||http://purl.uniprot.org/uniprot/Q3V1A0|||http://purl.uniprot.org/uniprot/Q9JJV0 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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|||N-acetylthreonine|||N-terminal arm|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000057546 http://togogenome.org/gene/10090:Cse1l ^@ http://purl.uniprot.org/uniprot/Q9ERK4 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Exportin-2|||Importin N-terminal|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000117288 http://togogenome.org/gene/10090:Idh1 ^@ http://purl.uniprot.org/uniprot/O88844 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Strand|||Turn ^@ Critical for catalysis|||Decreased inhibition by cadmium ions.|||Isocitrate dehydrogenase [NADP] cytoplasmic|||N-acetylserine|||N6-acetyllysine|||N6-succinyllysine|||No effect on inhibition by cadmium ions.|||Phosphoserine|||Phosphotyrosine|||Removed|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000083578 http://togogenome.org/gene/10090:Got1 ^@ http://purl.uniprot.org/uniprot/P05201 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Aspartate aminotransferase, cytoplasmic|||N6-(pyridoxal phosphate)lysine|||N6-succinyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000123880 http://togogenome.org/gene/10090:Trp53i13 ^@ http://purl.uniprot.org/uniprot/B2RVS3|||http://purl.uniprot.org/uniprot/Q5F267 ^@ 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_0000333825|||http://purl.uniprot.org/annotation/PRO_5015087159 http://togogenome.org/gene/10090:Mical1 ^@ http://purl.uniprot.org/uniprot/Q8VDP3 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Acidic residues|||Calponin-homology (CH)|||Disordered|||Important for interaction with ARHGAP26 AND ARHGAP10|||In isoform 2.|||In isoform 3.|||LIM zinc-binding|||Monooxygenase domain|||Phosphoserine|||Phosphothreonine|||Polar residues|||[F-actin]-monooxygenase MICAL1|||bMERB ^@ http://purl.uniprot.org/annotation/PRO_0000075843|||http://purl.uniprot.org/annotation/VSP_042591|||http://purl.uniprot.org/annotation/VSP_042592 http://togogenome.org/gene/10090:Cyb5r1 ^@ http://purl.uniprot.org/uniprot/Q9DB73 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant|||Transmembrane ^@ FAD-binding FR-type|||Helical|||In isoform 2.|||NADH-cytochrome b5 reductase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000287546|||http://purl.uniprot.org/annotation/VSP_025557|||http://purl.uniprot.org/annotation/VSP_025558 http://togogenome.org/gene/10090:Ntpcr ^@ http://purl.uniprot.org/uniprot/Q9CQA9 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Cancer-related nucleoside-triphosphatase homolog|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000146712 http://togogenome.org/gene/10090:Lacc1 ^@ http://purl.uniprot.org/uniprot/Q8BZT9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Site ^@ Binding Site|||Chain|||Modified Residue|||Mutagenesis Site ^@ Complete loss of function.|||N6-acetyllysine|||Purine nucleoside phosphorylase LACC1|||Reduced function. ^@ http://purl.uniprot.org/annotation/PRO_0000163188 http://togogenome.org/gene/10090:Tlcd3b ^@ http://purl.uniprot.org/uniprot/Q7TNV1 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Splice Variant|||Transmembrane ^@ Ceramide synthase|||Helical|||In isoform 2.|||In isoform 3.|||TLC ^@ http://purl.uniprot.org/annotation/PRO_0000185543|||http://purl.uniprot.org/annotation/VSP_021636|||http://purl.uniprot.org/annotation/VSP_021637 http://togogenome.org/gene/10090:Plin3 ^@ http://purl.uniprot.org/uniprot/Q9DBG5 ^@ Chain|||Coiled-Coil|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||N-acetylserine|||N6-acetyllysine|||Perilipin-3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000099891 http://togogenome.org/gene/10090:Vmn2r84 ^@ http://purl.uniprot.org/uniprot/D3YWE3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015088508 http://togogenome.org/gene/10090:Cyp3a13 ^@ http://purl.uniprot.org/uniprot/Q3UW87|||http://purl.uniprot.org/uniprot/Q64464 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Cytochrome P450 3A13|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051796 http://togogenome.org/gene/10090:Cntn3 ^@ http://purl.uniprot.org/uniprot/Q07409 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ 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_0000014707|||http://purl.uniprot.org/annotation/PRO_0000014708 http://togogenome.org/gene/10090:Cd109 ^@ http://purl.uniprot.org/uniprot/A6MDD3|||http://purl.uniprot.org/uniprot/Q8R422 ^@ Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide ^@ Alpha-2-macroglobulin|||Alpha-2-macroglobulin bait region|||Alpha-macroglobulin receptor-binding|||Bait region (approximate)|||CD109 antigen|||GPI-anchor amidated alanine|||Isoglutamyl cysteine thioester (Cys-Gln)|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000255947|||http://purl.uniprot.org/annotation/PRO_0000255948|||http://purl.uniprot.org/annotation/PRO_5014297007 http://togogenome.org/gene/10090:Adam34l ^@ http://purl.uniprot.org/uniprot/Q7M766 ^@ Active Site|||Binding Site|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Disintegrin|||Disordered|||EGF-like|||Helical|||Peptidase M12B ^@ http://togogenome.org/gene/10090:Awat1 ^@ http://purl.uniprot.org/uniprot/A2ADU9 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Acyl-CoA wax alcohol acyltransferase 1|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000320296 http://togogenome.org/gene/10090:Lbhd1 ^@ http://purl.uniprot.org/uniprot/A0A087WPA0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||LBH|||Polar residues ^@ http://togogenome.org/gene/10090:Gimap9 ^@ http://purl.uniprot.org/uniprot/G3X987|||http://purl.uniprot.org/uniprot/Q8BYB6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict ^@ AIG1-type G|||G1|||G2|||G3|||G4|||G5|||GTPase IMAP family member 9 ^@ http://purl.uniprot.org/annotation/PRO_0000447245 http://togogenome.org/gene/10090:Ube2dnl1 ^@ http://purl.uniprot.org/uniprot/A2AFH1 ^@ Active Site|||Domain Extent|||Region|||Site ^@ Active Site|||Domain Extent ^@ Glycyl thioester intermediate|||UBC core ^@ http://togogenome.org/gene/10090:Hyou1 ^@ http://purl.uniprot.org/uniprot/Q9JKR6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Hypoxia up-regulated protein 1|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_5000057827 http://togogenome.org/gene/10090:Spaca4 ^@ http://purl.uniprot.org/uniprot/Q80ZQ0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ GPI-anchor amidated asparagine|||Removed in mature form|||Sperm acrosome membrane-associated protein 4|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000252452|||http://purl.uniprot.org/annotation/PRO_0000252453 http://togogenome.org/gene/10090:Or51i1 ^@ http://purl.uniprot.org/uniprot/E9Q7P5 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Mideas ^@ http://purl.uniprot.org/uniprot/E9Q2I4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||ELM2|||Polar residues|||SANT ^@ http://togogenome.org/gene/10090:Tmem229a ^@ http://purl.uniprot.org/uniprot/B9EJI9 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 229A ^@ http://purl.uniprot.org/annotation/PRO_0000391849 http://togogenome.org/gene/10090:Btnl2 ^@ http://purl.uniprot.org/uniprot/O70355 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Butyrophilin-like protein 2|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Ig-like V-type 1|||Ig-like V-type 2|||Ig-like V-type 3|||Ig-like V-type 4|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014538|||http://purl.uniprot.org/annotation/VSP_022147 http://togogenome.org/gene/10090:Eif2b5 ^@ http://purl.uniprot.org/uniprot/Q8CHW4 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphothreonine|||Translation initiation factor eIF-2B subunit epsilon|||W2 ^@ http://purl.uniprot.org/annotation/PRO_0000239429 http://togogenome.org/gene/10090:Tbxa2r ^@ http://purl.uniprot.org/uniprot/P30987|||http://purl.uniprot.org/uniprot/Q5FW61 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||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|||Phosphoserine|||Thromboxane A2 receptor ^@ http://purl.uniprot.org/annotation/PRO_0000070139 http://togogenome.org/gene/10090:Rad52 ^@ http://purl.uniprot.org/uniprot/G5E879|||http://purl.uniprot.org/uniprot/P43352 ^@ 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 ^@ Basic and acidic residues|||DNA repair protein RAD52 homolog|||Disordered|||Mediates interaction with RPA2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by ABL1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000173882 http://togogenome.org/gene/10090:Vat1l ^@ http://purl.uniprot.org/uniprot/Q80TB8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Phosphothreonine|||Synaptic vesicle membrane protein VAT-1 homolog-like ^@ http://purl.uniprot.org/annotation/PRO_0000160923 http://togogenome.org/gene/10090:Tmem30a ^@ http://purl.uniprot.org/uniprot/Q8VEK0 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cell cycle control protein 50A|||Cytoplasmic|||Disordered|||Exoplasmic loop|||Helical|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000244470 http://togogenome.org/gene/10090:Zfp51 ^@ http://purl.uniprot.org/uniprot/Q3U4L8|||http://purl.uniprot.org/uniprot/Q3UZS6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Defb41 ^@ http://purl.uniprot.org/uniprot/Q30KP6 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Signal Peptide|||Splice Variant ^@ Beta-defensin 41|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000352701|||http://purl.uniprot.org/annotation/VSP_057922 http://togogenome.org/gene/10090:Eif5a2 ^@ http://purl.uniprot.org/uniprot/Q8BGY2 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Eukaryotic translation initiation factor 5A-2|||Hypusine|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000229765 http://togogenome.org/gene/10090:Foxp2 ^@ http://purl.uniprot.org/uniprot/P58463 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Acidic residues|||C2H2-type|||CTBP1-binding|||Disordered|||Fork-head|||Forkhead box protein P2|||In isoform 2.|||Leucine-zipper|||Loss of dimerization. Almost complete loss of DNA-binding. Reduced transcriptional repression activity.|||No change in synaptic density.|||No significant effect on transcriptional repression activity.|||Polar residues|||Severely reduced transcriptional repression activity. ^@ http://purl.uniprot.org/annotation/PRO_0000091882|||http://purl.uniprot.org/annotation/VSP_011540 http://togogenome.org/gene/10090:Letm1 ^@ http://purl.uniprot.org/uniprot/Q9Z2I0 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Disordered|||Does not affect mitochondrial localization and ability to mediate calcium efflux from mitochondrion.|||Does not affect mitochondrial localization but abolishes ability to mediate calcium efflux from mitochondrion.|||EF-hand|||Helical|||Letm1 RBD|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrial proton/calcium exchanger protein|||Mitochondrion|||N6-acetyllysine|||Phosphothreonine; by PINK1 ^@ http://purl.uniprot.org/annotation/PRO_0000017695 http://togogenome.org/gene/10090:Obox7 ^@ http://purl.uniprot.org/uniprot/Q4KL20 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:F11r ^@ http://purl.uniprot.org/uniprot/O88792 ^@ 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|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||Junctional adhesion molecule A|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000015067 http://togogenome.org/gene/10090:Irf1 ^@ http://purl.uniprot.org/uniprot/P15314|||http://purl.uniprot.org/uniprot/Q3U5M1|||http://purl.uniprot.org/uniprot/Q5SX13 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||IRF tryptophan pentad repeat|||Interferon regulatory factor 1|||N6-acetyllysine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000154546 http://togogenome.org/gene/10090:Esp15 ^@ http://purl.uniprot.org/uniprot/A8R0U8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Prf1 ^@ http://purl.uniprot.org/uniprot/A2RSY7|||http://purl.uniprot.org/uniprot/P10820 ^@ 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|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn ^@ Abolished binding of the weakest calcium-binding site, leading to impaired interaction with lipid membranes.|||Abolished lipid-binding and pore formation; when associated with 427-A--A-430.|||Abolished lipid-binding and pore formation; when associated with 486-A--A-488.|||Beta stranded; Name=CH1|||Beta stranded; Name=CH2|||C2|||Decreased calcium-binding.|||Does not affect interaction with lipid membranes.|||EGF-like|||Important for oligomerization|||Loss of cytotoxicity.|||MACPF|||N-linked (GlcNAc...) asparagine|||Perforin-1|||Strongly decreased cytotoxicity. ^@ http://purl.uniprot.org/annotation/PRO_0000023610|||http://purl.uniprot.org/annotation/PRO_5014296814 http://togogenome.org/gene/10090:Bloc1s4 ^@ http://purl.uniprot.org/uniprot/Q8VED2 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Region ^@ Biogenesis of lysosome-related organelles complex 1 subunit 4|||Disordered|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000089976 http://togogenome.org/gene/10090:Schip1 ^@ http://purl.uniprot.org/uniprot/A0A097PIJ2|||http://purl.uniprot.org/uniprot/P0DPB4 ^@ 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|||Disordered|||In isoform Schip1-2.|||In isoform Schip1-3.|||In isoform Schip1-4.|||Polar residues|||Schwannomin interacting protein 1 C-terminal|||Schwannomin-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000288928|||http://purl.uniprot.org/annotation/VSP_025831|||http://purl.uniprot.org/annotation/VSP_025834|||http://purl.uniprot.org/annotation/VSP_046119|||http://purl.uniprot.org/annotation/VSP_046121 http://togogenome.org/gene/10090:Or2t44 ^@ http://purl.uniprot.org/uniprot/Q7TRZ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Phf11c ^@ http://purl.uniprot.org/uniprot/B4XVP9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||PHD-type ^@ http://togogenome.org/gene/10090:Nsl1 ^@ http://purl.uniprot.org/uniprot/E9Q3W6|||http://purl.uniprot.org/uniprot/E9QME3 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Tmppe ^@ http://purl.uniprot.org/uniprot/D3Z286 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Calcineurin-like phosphoesterase|||Helical ^@ http://togogenome.org/gene/10090:Gabre ^@ http://purl.uniprot.org/uniprot/A2AMW3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5022256029 http://togogenome.org/gene/10090:Edaradd ^@ http://purl.uniprot.org/uniprot/Q5D0F1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Death|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ltbr ^@ http://purl.uniprot.org/uniprot/B2RRV3|||http://purl.uniprot.org/uniprot/P50284 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||TNFR-Cys|||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_0000034553|||http://purl.uniprot.org/annotation/PRO_5015087152 http://togogenome.org/gene/10090:Utrn ^@ http://purl.uniprot.org/uniprot/A0A1W2P7C0|||http://purl.uniprot.org/uniprot/E9Q6R7|||http://purl.uniprot.org/uniprot/Q3UYS4|||http://purl.uniprot.org/uniprot/Q61636|||http://purl.uniprot.org/uniprot/Q6P6L2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Polar residues|||WW|||ZZ-type ^@ http://togogenome.org/gene/10090:Cyp2d11 ^@ http://purl.uniprot.org/uniprot/P24457 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Cytochrome P450 2D11|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051737 http://togogenome.org/gene/10090:Or2v2 ^@ http://purl.uniprot.org/uniprot/Q7TQS8|||http://purl.uniprot.org/uniprot/Q8VEY7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Alox12 ^@ http://purl.uniprot.org/uniprot/A2CF85|||http://purl.uniprot.org/uniprot/P39655 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Essential for stabilizing binding to COTL1|||Lipoxygenase|||Little activity (8-15%).|||Loss of activity.|||Nearly full activity.|||PLAT|||Phosphoserine|||Polyunsaturated fatty acid lipoxygenase ALOX12 ^@ http://purl.uniprot.org/annotation/PRO_0000220683 http://togogenome.org/gene/10090:Lrrc56 ^@ http://purl.uniprot.org/uniprot/Q8BMW2|||http://purl.uniprot.org/uniprot/Q8K375 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Leucine-rich repeat-containing protein 56|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000229924 http://togogenome.org/gene/10090:Gm14496 ^@ http://purl.uniprot.org/uniprot/K7N5U4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908701 http://togogenome.org/gene/10090:Rhox4a ^@ http://purl.uniprot.org/uniprot/Q9D3I8 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Cpd ^@ http://purl.uniprot.org/uniprot/O89001 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Carboxypeptidase D|||Carboxypeptidase-like 1|||Carboxypeptidase-like 2|||Carboxypeptidase-like 3|||Cell attachment site|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Important for catalytic activity|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton donor/acceptor|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000004402 http://togogenome.org/gene/10090:Zdhhc9 ^@ http://purl.uniprot.org/uniprot/P59268 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Disordered|||Helical|||Lumenal|||Palmitoyltransferase ZDHHC9|||Polar residues|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212881 http://togogenome.org/gene/10090:Ubqln3 ^@ http://purl.uniprot.org/uniprot/Q497R3|||http://purl.uniprot.org/uniprot/Q8C5U9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||STI1|||UBA|||Ubiquilin-3|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000211014 http://togogenome.org/gene/10090:Msl2 ^@ http://purl.uniprot.org/uniprot/Q69ZF8 ^@ 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|||Disordered|||E3 ubiquitin-protein ligase MSL2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||RING-type|||Sufficient for interaction with MSL1 ^@ http://purl.uniprot.org/annotation/PRO_0000299537 http://togogenome.org/gene/10090:Sh2d5 ^@ http://purl.uniprot.org/uniprot/A2AM67|||http://purl.uniprot.org/uniprot/Q8JZW5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ PID|||SH2|||SH2 domain-containing protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000231582 http://togogenome.org/gene/10090:Slc52a2 ^@ http://purl.uniprot.org/uniprot/Q9D8F3 ^@ 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|||Solute carrier family 52, riboflavin transporter, member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000042633|||http://purl.uniprot.org/annotation/VSP_015940|||http://purl.uniprot.org/annotation/VSP_015941 http://togogenome.org/gene/10090:Ifna9 ^@ http://purl.uniprot.org/uniprot/A0A7R8C3E4|||http://purl.uniprot.org/uniprot/P09235 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Interferon alpha-9|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000016382|||http://purl.uniprot.org/annotation/PRO_5031459621 http://togogenome.org/gene/10090:Bltp2 ^@ http://purl.uniprot.org/uniprot/Q5SYL3 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Bridge-like lipid transfer protein family member 2|||Disordered|||Phosphoserine|||Transmembrane domain ^@ http://purl.uniprot.org/annotation/PRO_0000248588 http://togogenome.org/gene/10090:Xk ^@ http://purl.uniprot.org/uniprot/Q059K7|||http://purl.uniprot.org/uniprot/Q9QXY7 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endoplasmic reticulum membrane adapter protein XK|||Extracellular|||Helical|||Interchain (with C-53 in Kell)|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000190768 http://togogenome.org/gene/10090:Rpl19 ^@ http://purl.uniprot.org/uniprot/A2A547|||http://purl.uniprot.org/uniprot/P84099|||http://purl.uniprot.org/uniprot/Q5I0T8 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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_0000131171 http://togogenome.org/gene/10090:Nsg1 ^@ http://purl.uniprot.org/uniprot/Q62092 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Neuronal vesicle trafficking-associated protein 1|||Required for GRIP1 interaction ^@ http://purl.uniprot.org/annotation/PRO_0000164364 http://togogenome.org/gene/10090:Defb39 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Y8|||http://purl.uniprot.org/uniprot/Q70KL3 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ Beta-defensin 39 ^@ http://purl.uniprot.org/annotation/PRO_0000006951|||http://purl.uniprot.org/annotation/PRO_5006451997 http://togogenome.org/gene/10090:Spx ^@ http://purl.uniprot.org/uniprot/A0A1C7CYU9 ^@ 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_5008753772 http://togogenome.org/gene/10090:Pqbp1 ^@ http://purl.uniprot.org/uniprot/A2AER7|||http://purl.uniprot.org/uniprot/Q91VJ5 ^@ 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; approximate|||1-2|||1-3; approximate|||1-4; approximate|||1-5; approximate|||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|||5 X 7 AA approximate tandem repeats of D-R-[NS]-H-E-K-S|||6 X 2 AA tandem repeats of [DE]-R|||Basic and acidic residues|||Disordered|||Important for interaction with TXNL4A|||Phosphoserine|||Polyglutamine-binding protein 1|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000076090 http://togogenome.org/gene/10090:Saa3 ^@ http://purl.uniprot.org/uniprot/P04918 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide ^@ Chain|||Helix|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Serum amyloid A-3 protein ^@ http://purl.uniprot.org/annotation/PRO_0000031591 http://togogenome.org/gene/10090:Or6c76 ^@ http://purl.uniprot.org/uniprot/Q8VEX8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Npm3 ^@ http://purl.uniprot.org/uniprot/Q9CPP0 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||Nucleoplasmin-3|||Omega-N-methylarginine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000219490 http://togogenome.org/gene/10090:4930447C04Rik ^@ http://purl.uniprot.org/uniprot/F8WHJ9|||http://purl.uniprot.org/uniprot/Q9CTN5 ^@ 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|||Polar residues|||Protein SIX6OS1 ^@ http://purl.uniprot.org/annotation/PRO_0000089889|||http://purl.uniprot.org/annotation/VSP_007121|||http://purl.uniprot.org/annotation/VSP_007122 http://togogenome.org/gene/10090:Trim16 ^@ http://purl.uniprot.org/uniprot/Q5SVT2|||http://purl.uniprot.org/uniprot/Q99PP9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ B box-type 1|||B box-type 2|||B30.2/SPRY|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Tripartite motif-containing protein 16 ^@ http://purl.uniprot.org/annotation/PRO_0000056223|||http://purl.uniprot.org/annotation/VSP_009099|||http://purl.uniprot.org/annotation/VSP_009100|||http://purl.uniprot.org/annotation/VSP_009101 http://togogenome.org/gene/10090:Nog ^@ http://purl.uniprot.org/uniprot/A2RTJ4|||http://purl.uniprot.org/uniprot/P97466 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Noggin ^@ http://purl.uniprot.org/annotation/PRO_0000019814|||http://purl.uniprot.org/annotation/PRO_5014296836 http://togogenome.org/gene/10090:Camta1 ^@ http://purl.uniprot.org/uniprot/A2A891 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||Basic and acidic residues|||CG-1|||Calmodulin-binding transcription activator 1|||Disordered|||IPT/TIG|||IQ 1|||IQ 2|||IQ 3|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4 and isoform 5.|||In isoform 5.|||Nuclear localization signal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000355043|||http://purl.uniprot.org/annotation/VSP_052987|||http://purl.uniprot.org/annotation/VSP_052988|||http://purl.uniprot.org/annotation/VSP_052989|||http://purl.uniprot.org/annotation/VSP_052990|||http://purl.uniprot.org/annotation/VSP_052991 http://togogenome.org/gene/10090:Pdzd9 ^@ http://purl.uniprot.org/uniprot/B9EJT5|||http://purl.uniprot.org/uniprot/Q9CQQ5|||http://purl.uniprot.org/uniprot/Q9D9M4 ^@ 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|||Disordered|||PDZ|||PDZ domain-containing protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000271217 http://togogenome.org/gene/10090:Lingo4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Q7|||http://purl.uniprot.org/uniprot/Q149C3 ^@ 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|||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_0000324185 http://togogenome.org/gene/10090:Tgfbr3l ^@ http://purl.uniprot.org/uniprot/D3YZZ2 ^@ 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 ^@ Disordered|||Helical|||Pro residues|||Transforming growth factor-beta receptor type 3-like protein|||ZP ^@ http://purl.uniprot.org/annotation/PRO_5003053003 http://togogenome.org/gene/10090:Or1j16 ^@ http://purl.uniprot.org/uniprot/Q8VGK4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Atg9b ^@ http://purl.uniprot.org/uniprot/Q6EBV9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Autophagy-related protein 9B|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Polar residues|||Tyrosine-based sorting signal ^@ http://purl.uniprot.org/annotation/PRO_0000314868 http://togogenome.org/gene/10090:Scn7a ^@ http://purl.uniprot.org/uniprot/B1AYL1|||http://purl.uniprot.org/uniprot/Q62467 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Ion transport|||Polar residues|||Sodium ion transport-associated ^@ http://togogenome.org/gene/10090:Ttn ^@ http://purl.uniprot.org/uniprot/E9Q8N1|||http://purl.uniprot.org/uniprot/Q3TZL3|||http://purl.uniprot.org/uniprot/Q3UT48|||http://purl.uniprot.org/uniprot/Q8BUC9|||http://purl.uniprot.org/uniprot/Q8BUJ0|||http://purl.uniprot.org/uniprot/Q8BUJ6|||http://purl.uniprot.org/uniprot/Q8BUX4|||http://purl.uniprot.org/uniprot/Q8C139 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Fibronectin type-III|||Ig-like|||Polar residues|||Pro residues|||Protein kinase ^@ http://togogenome.org/gene/10090:Clk4 ^@ http://purl.uniprot.org/uniprot/O35493|||http://purl.uniprot.org/uniprot/Q4FJV9 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||Disordered|||Dual specificity protein kinase CLK4|||In isoform 2.|||Loss of function.|||Phosphoserine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085874|||http://purl.uniprot.org/annotation/VSP_008205 http://togogenome.org/gene/10090:Actl7a ^@ http://purl.uniprot.org/uniprot/Q9QY84 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Actin-like protein 7A|||Disordered|||Homozygous knockin male mice are infertile. The spermatogenesis process is normal. However spermatozoa dysplay acrosomal ultrastructural defects. Complete absence of the ACTL7A protein in both testes and sperms. Abnormal distribution of PLCZ1 in sperms.|||Required for interaction with TES ^@ http://purl.uniprot.org/annotation/PRO_0000089138 http://togogenome.org/gene/10090:A830018L16Rik ^@ http://purl.uniprot.org/uniprot/B2RQF6|||http://purl.uniprot.org/uniprot/Q8BZJ8 ^@ 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.|||In isoform 4.|||Polar residues|||Uncharacterized protein C8orf34 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000330040|||http://purl.uniprot.org/annotation/VSP_033016|||http://purl.uniprot.org/annotation/VSP_033017|||http://purl.uniprot.org/annotation/VSP_033018|||http://purl.uniprot.org/annotation/VSP_033019|||http://purl.uniprot.org/annotation/VSP_033020|||http://purl.uniprot.org/annotation/VSP_033021 http://togogenome.org/gene/10090:Tacstd2 ^@ http://purl.uniprot.org/uniprot/Q8BGV3 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Thyroglobulin type-1|||Tumor-associated calcium signal transducer 2 ^@ http://purl.uniprot.org/annotation/PRO_0000380187 http://togogenome.org/gene/10090:Lpl ^@ http://purl.uniprot.org/uniprot/P11152 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 3'-nitrotyrosine|||Charge relay system|||Essential for determining substrate specificity|||Important for heparin binding|||Important for interaction with lipoprotein particles|||Interaction with GPIHBP1|||Lipoprotein lipase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PLAT ^@ http://purl.uniprot.org/annotation/PRO_0000017776 http://togogenome.org/gene/10090:Zkscan14 ^@ http://purl.uniprot.org/uniprot/Q9Z1D9 ^@ 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 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||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 394 ^@ http://purl.uniprot.org/annotation/PRO_0000047558 http://togogenome.org/gene/10090:Golt1b ^@ http://purl.uniprot.org/uniprot/Q9CR60 ^@ 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=4|||Lumenal|||N-acetylmethionine|||Vesicle transport protein GOT1B ^@ http://purl.uniprot.org/annotation/PRO_0000218583 http://togogenome.org/gene/10090:Serpina7 ^@ http://purl.uniprot.org/uniprot/Q3UEL9|||http://purl.uniprot.org/uniprot/Q8BII9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Serpin ^@ http://purl.uniprot.org/annotation/PRO_5015097476 http://togogenome.org/gene/10090:Plagl1 ^@ http://purl.uniprot.org/uniprot/Q9JLQ4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||C2H2-type|||Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Papolg ^@ http://purl.uniprot.org/uniprot/Q6PCL9|||http://purl.uniprot.org/uniprot/Q8R1V7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||Disordered|||Interaction with RNA|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Poly(A) polymerase gamma ^@ http://purl.uniprot.org/annotation/PRO_0000253025 http://togogenome.org/gene/10090:Dcx ^@ http://purl.uniprot.org/uniprot/O88809|||http://purl.uniprot.org/uniprot/Q6PGI2|||http://purl.uniprot.org/uniprot/Q9CXL6 ^@ 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 ^@ Disordered|||Doublecortin|||Doublecortin 1|||Doublecortin 2|||Neuronal migration protein doublecortin|||No effect on overall phosphorylation.|||No effect on overall phosphorylation. Reduces overall phosphorylation by 36%; when associated with A-332.|||No effect on overall phosphorylation. Reduces overall phosphorylation by 36%; when associated with A-339.|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphoserine; by CK2|||Phosphoserine; by CK2, MARK1 and PKA|||Phosphoserine; by MAPK|||Phosphoserine; by MARK1 and PKA|||Phosphoserine; by PKC|||Phosphothreonine; by CDK5|||Phosphothreonine; by MAPK|||Phosphothreonine; by PKC and MAPK|||Phosphotyrosine; by ABL|||Polar residues|||Reduces overall phosphorylation by 25%. ^@ http://purl.uniprot.org/annotation/PRO_0000079834 http://togogenome.org/gene/10090:Whamm ^@ http://purl.uniprot.org/uniprot/Q571B6 ^@ 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.|||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_0000295101|||http://purl.uniprot.org/annotation/VSP_026722|||http://purl.uniprot.org/annotation/VSP_026729 http://togogenome.org/gene/10090:F3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J088|||http://purl.uniprot.org/uniprot/P20352 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Motif|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Fibronectin type-III|||Helical|||Interferon/interleukin receptor|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Tissue factor|||WKS motif ^@ http://purl.uniprot.org/annotation/PRO_0000033639|||http://purl.uniprot.org/annotation/PRO_5015044287 http://togogenome.org/gene/10090:Krt20 ^@ http://purl.uniprot.org/uniprot/Q9D312 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Cleavage; by caspases|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type I cytoskeletal 20|||Linker 1|||Linker 12|||Phosphoserine|||Phosphoserine; by MAPKAPK2, MAPKAPK3 and PKC|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000308358 http://togogenome.org/gene/10090:Acads ^@ http://purl.uniprot.org/uniprot/Q07417 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ 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_0000000499 http://togogenome.org/gene/10090:Piga ^@ http://purl.uniprot.org/uniprot/A2AIH5|||http://purl.uniprot.org/uniprot/Q64323 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Glycosyl transferase family 1|||Helical|||Lumenal|||PIGA GPI anchor biosynthesis|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit A|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080327 http://togogenome.org/gene/10090:Dnai3 ^@ http://purl.uniprot.org/uniprot/B2RY71 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Region|||Repeat ^@ Disordered|||Dynein axonemal intermediate chain 3|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000450864 http://togogenome.org/gene/10090:Hps3 ^@ http://purl.uniprot.org/uniprot/E9PZY1|||http://purl.uniprot.org/uniprot/Q8BZ55|||http://purl.uniprot.org/uniprot/Q91VB4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ 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|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000084051 http://togogenome.org/gene/10090:Eomes ^@ http://purl.uniprot.org/uniprot/O54839 ^@ 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|||Eomesodermin homolog|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for transcription activation|||T-box ^@ http://purl.uniprot.org/annotation/PRO_0000184460|||http://purl.uniprot.org/annotation/VSP_038806 http://togogenome.org/gene/10090:Rai14 ^@ http://purl.uniprot.org/uniprot/A0A2I3BPY7|||http://purl.uniprot.org/uniprot/Q9EP71 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankycorbin|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000239631 http://togogenome.org/gene/10090:Myo16 ^@ http://purl.uniprot.org/uniprot/Q5DU14 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||Basic and acidic residues|||Disordered|||IQ|||In isoform 2.|||In isoform 3.|||Involved in CYFIP1- and NCKAP1-binding|||Myosin motor|||Polar residues|||Pro residues|||Slight reduction of phosphorylation in HEK293T cells. Abolishes phosphorylation in HEK293T cells and in neurons; when associated with F-1416.|||Slight reduction of phosphorylation in HEK293T cells. Abolishes phosphorylation in HEK293T cells and neurons; when associated with F-1441.|||Unconventional myosin-XVI ^@ http://purl.uniprot.org/annotation/PRO_0000289137|||http://purl.uniprot.org/annotation/VSP_042365|||http://purl.uniprot.org/annotation/VSP_042366|||http://purl.uniprot.org/annotation/VSP_052446 http://togogenome.org/gene/10090:Aadac ^@ http://purl.uniprot.org/uniprot/Q99PG0 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Arylacetamide deacetylase|||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_0000071543 http://togogenome.org/gene/10090:Pcdhb15 ^@ http://purl.uniprot.org/uniprot/Q91Y04 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099506 http://togogenome.org/gene/10090:Tnrc6b ^@ http://purl.uniprot.org/uniprot/Q3TRK2|||http://purl.uniprot.org/uniprot/Q8BKI2|||http://purl.uniprot.org/uniprot/Q8BWL0|||http://purl.uniprot.org/uniprot/Q8BX83|||http://purl.uniprot.org/uniprot/Q8VD67 ^@ 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 ^@ Argonaute hook|||Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with argonaute proteins|||PABPC1-interacting motif-2 (PAM2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RRM|||Silencing domain; interaction with CNOT1 and PAN3|||TNRC6 PABC binding|||Trinucleotide repeat-containing gene 6B protein ^@ http://purl.uniprot.org/annotation/PRO_0000373981|||http://purl.uniprot.org/annotation/VSP_037294|||http://purl.uniprot.org/annotation/VSP_037295|||http://purl.uniprot.org/annotation/VSP_037296|||http://purl.uniprot.org/annotation/VSP_037297 http://togogenome.org/gene/10090:C2cd5 ^@ http://purl.uniprot.org/uniprot/A0A0N4SW93|||http://purl.uniprot.org/uniprot/E9Q026|||http://purl.uniprot.org/uniprot/Q3TSE2|||http://purl.uniprot.org/uniprot/Q7TPS5 ^@ 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|||C2|||C2 domain-containing protein 5|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by PKB/AKT2|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247451|||http://purl.uniprot.org/annotation/VSP_019991|||http://purl.uniprot.org/annotation/VSP_019992|||http://purl.uniprot.org/annotation/VSP_019993 http://togogenome.org/gene/10090:Tmem234 ^@ http://purl.uniprot.org/uniprot/Q8R1E7 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 234 ^@ http://purl.uniprot.org/annotation/PRO_0000326485 http://togogenome.org/gene/10090:Mtg1 ^@ http://purl.uniprot.org/uniprot/Q8R2R6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide ^@ CP-type G|||Mitochondrial ribosome-associated GTPase 1|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000280263 http://togogenome.org/gene/10090:Cenpw ^@ http://purl.uniprot.org/uniprot/Q3URR0 ^@ Chain|||Molecule Processing ^@ Chain ^@ Centromere protein W ^@ http://purl.uniprot.org/annotation/PRO_0000311184 http://togogenome.org/gene/10090:Arfip2 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSM3|||http://purl.uniprot.org/uniprot/Q8K221 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ AH|||Arfaptin-2|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000064668 http://togogenome.org/gene/10090:Cstdc2 ^@ http://purl.uniprot.org/uniprot/Q9D264 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Cystatin ^@ http://purl.uniprot.org/annotation/PRO_5015020148 http://togogenome.org/gene/10090:Lmo2 ^@ http://purl.uniprot.org/uniprot/A2BHP3|||http://purl.uniprot.org/uniprot/A2BHP5|||http://purl.uniprot.org/uniprot/P25801|||http://purl.uniprot.org/uniprot/Q544Z2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||Pro residues|||Rhombotin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000075897 http://togogenome.org/gene/10090:Gas7 ^@ http://purl.uniprot.org/uniprot/B1ATI9|||http://purl.uniprot.org/uniprot/Q0VBR8|||http://purl.uniprot.org/uniprot/Q3U432|||http://purl.uniprot.org/uniprot/Q3U8N2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||F-BAR|||Polar residues|||Pro residues|||WW ^@ http://togogenome.org/gene/10090:Stt3a ^@ http://purl.uniprot.org/uniprot/P46978|||http://purl.uniprot.org/uniprot/Q3U573 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DK motif|||DXD motif 1|||DXD motif 2|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A|||Helical|||Important for catalytic activity|||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_0000072291 http://togogenome.org/gene/10090:Usp17le ^@ http://purl.uniprot.org/uniprot/A0A1B0GS33 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||USP ^@ http://togogenome.org/gene/10090:Chrnb1 ^@ http://purl.uniprot.org/uniprot/P09690 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Acetylcholine receptor subunit beta|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by Tyr-kinases ^@ http://purl.uniprot.org/annotation/PRO_0000000316 http://togogenome.org/gene/10090:Or5o1 ^@ http://purl.uniprot.org/uniprot/Q7TQW4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:C1qc ^@ http://purl.uniprot.org/uniprot/Q02105 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 4-hydroxyproline|||5-hydroxylysine|||C1q|||Collagen-like|||Complement C1q subcomponent subunit C|||Disordered|||Interchain ^@ http://purl.uniprot.org/annotation/PRO_0000003525 http://togogenome.org/gene/10090:Kcnh6 ^@ http://purl.uniprot.org/uniprot/M0QW64|||http://purl.uniprot.org/uniprot/Q32ME0 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Cyclic nucleotide-binding|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Mrgpra2b ^@ http://purl.uniprot.org/uniprot/E9QNZ7|||http://purl.uniprot.org/uniprot/Q91WW4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||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|||Mas-related G-protein coupled receptor member A2 ^@ http://purl.uniprot.org/annotation/PRO_0000069748 http://togogenome.org/gene/10090:Usp9x ^@ http://purl.uniprot.org/uniprot/P70398|||http://purl.uniprot.org/uniprot/Q4FE56|||http://purl.uniprot.org/uniprot/Q8BS89|||http://purl.uniprot.org/uniprot/Q8C7T5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Abolished deubiquitinase activity.|||Disordered|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Probable ubiquitin carboxyl-terminal hydrolase FAF-X|||Proton acceptor|||USP ^@ http://purl.uniprot.org/annotation/PRO_0000080691 http://togogenome.org/gene/10090:4921539E11Rik ^@ http://purl.uniprot.org/uniprot/Q9D5Q8 ^@ 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.|||Polar residues|||Uncharacterized protein C1orf141 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000294457|||http://purl.uniprot.org/annotation/VSP_026645|||http://purl.uniprot.org/annotation/VSP_026646|||http://purl.uniprot.org/annotation/VSP_026647 http://togogenome.org/gene/10090:Slc12a9 ^@ http://purl.uniprot.org/uniprot/Q99MR3 ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier family 12 member 9 ^@ http://purl.uniprot.org/annotation/PRO_0000331416 http://togogenome.org/gene/10090:Amelx ^@ http://purl.uniprot.org/uniprot/P63277|||http://purl.uniprot.org/uniprot/Q6PCW7|||http://purl.uniprot.org/uniprot/R9W2T8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Amelogenin, X isoform|||Disordered|||In isoform 1, isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000001201|||http://purl.uniprot.org/annotation/PRO_5004481827|||http://purl.uniprot.org/annotation/PRO_5015098430|||http://purl.uniprot.org/annotation/VSP_000230|||http://purl.uniprot.org/annotation/VSP_000231|||http://purl.uniprot.org/annotation/VSP_011688 http://togogenome.org/gene/10090:Spint3 ^@ http://purl.uniprot.org/uniprot/Q3UW09 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ BPTI/Kunitz inhibitor ^@ http://purl.uniprot.org/annotation/PRO_5015097504 http://togogenome.org/gene/10090:Rps15a ^@ http://purl.uniprot.org/uniprot/P62245 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ N6-succinyllysine|||Small ribosomal subunit protein uS8 ^@ http://purl.uniprot.org/annotation/PRO_0000126603 http://togogenome.org/gene/10090:Tmem247 ^@ http://purl.uniprot.org/uniprot/Q497K7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 247 ^@ http://purl.uniprot.org/annotation/PRO_0000328814 http://togogenome.org/gene/10090:Madcam1 ^@ http://purl.uniprot.org/uniprot/G5E838 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Adhesion molecule immunoglobulin-like|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015091895 http://togogenome.org/gene/10090:Gpr137 ^@ http://purl.uniprot.org/uniprot/E9Q9I0|||http://purl.uniprot.org/uniprot/Q3TD99|||http://purl.uniprot.org/uniprot/Q3UPL3|||http://purl.uniprot.org/uniprot/Q3UQ21|||http://purl.uniprot.org/uniprot/Q80ZU9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Non-terminal Residue|||Region|||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 GPR137|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000269997|||http://purl.uniprot.org/annotation/PRO_5015097492 http://togogenome.org/gene/10090:Dnah1 ^@ http://purl.uniprot.org/uniprot/E9Q8T7 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||CFDEFNR motif|||Disordered|||Dynein axonemal heavy chain 1|||GPAGTGKT motif|||In isoform 2.|||Stalk|||Stem ^@ http://purl.uniprot.org/annotation/PRO_0000442430|||http://purl.uniprot.org/annotation/VSP_059235|||http://purl.uniprot.org/annotation/VSP_059236 http://togogenome.org/gene/10090:Zfp217 ^@ http://purl.uniprot.org/uniprot/Q3U0X6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Grin2d ^@ http://purl.uniprot.org/uniprot/Q03391 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Basic residues|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Functional determinant of NMDA receptors|||Glutamate receptor ionotropic, NMDA 2D|||Helical|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||PDZ-binding|||Phosphoserine|||Pore-forming|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000011584 http://togogenome.org/gene/10090:Stard3nl ^@ http://purl.uniprot.org/uniprot/A0A0G2JE93|||http://purl.uniprot.org/uniprot/Q9DCI3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||FFAT|||Helical|||MENTAL|||N-acetylmethionine|||Phosphoserine|||STARD3 N-terminal-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000096420 http://togogenome.org/gene/10090:Ap2a1 ^@ http://purl.uniprot.org/uniprot/P17426 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||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_0000193731|||http://purl.uniprot.org/annotation/VSP_000162 http://togogenome.org/gene/10090:Med30 ^@ http://purl.uniprot.org/uniprot/Q9CQI9 ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Mediator of RNA polymerase II transcription subunit 30|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000239407 http://togogenome.org/gene/10090:Elmo1 ^@ http://purl.uniprot.org/uniprot/Q8BPU7 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant ^@ ELMO|||Engulfment and cell motility protein 1|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||PH|||Phosphoserine|||Phosphotyrosine; by HCK|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000153713|||http://purl.uniprot.org/annotation/VSP_007481|||http://purl.uniprot.org/annotation/VSP_007482|||http://purl.uniprot.org/annotation/VSP_007483|||http://purl.uniprot.org/annotation/VSP_007484|||http://purl.uniprot.org/annotation/VSP_007485 http://togogenome.org/gene/10090:Gimap6 ^@ http://purl.uniprot.org/uniprot/Q8K349 ^@ 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 ^@ AIG1-type G|||Basic and acidic residues|||Disordered|||G1|||G2|||G3|||G4|||G5|||GTPase IMAP family member 6|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000333012 http://togogenome.org/gene/10090:Inafm1 ^@ http://purl.uniprot.org/uniprot/E9PV59 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Fam177a2 ^@ http://purl.uniprot.org/uniprot/Q8BR63 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM177A1 ^@ http://purl.uniprot.org/annotation/PRO_0000089886 http://togogenome.org/gene/10090:Ppa2 ^@ http://purl.uniprot.org/uniprot/Q91VM9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Inorganic pyrophosphatase 2, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000025412|||http://purl.uniprot.org/annotation/VSP_011653|||http://purl.uniprot.org/annotation/VSP_011654 http://togogenome.org/gene/10090:Rhbdd2 ^@ http://purl.uniprot.org/uniprot/Q8VEK2 ^@ 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 ^@ Disordered|||Helical|||In isoform 2.|||Loss of cis-Golgi localization.|||No effect on cis-Golgi localization.|||Polar residues|||Rhomboid domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000254597|||http://purl.uniprot.org/annotation/VSP_021249 http://togogenome.org/gene/10090:Or5p56 ^@ http://purl.uniprot.org/uniprot/Q8VGI6 ^@ 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 5P56 ^@ http://purl.uniprot.org/annotation/PRO_0000150836 http://togogenome.org/gene/10090:Vmn2r36 ^@ http://purl.uniprot.org/uniprot/K7N741 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908743 http://togogenome.org/gene/10090:Vps13b ^@ http://purl.uniprot.org/uniprot/Q80TY5 ^@ 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 ^@ Chorein N-terminal|||Disordered|||Intermembrane lipid transfer protein VPS13B|||Localizes the protein to the Golgi apparatus|||Phosphoserine|||Polar residues|||Results in hypoactivity, impaired motor coordination and spatial learning.|||SHR-BD ^@ http://purl.uniprot.org/annotation/PRO_0000065881 http://togogenome.org/gene/10090:4931429L15Rik ^@ http://purl.uniprot.org/uniprot/E9PVU2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Atxn10 ^@ http://purl.uniprot.org/uniprot/P28658 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Ataxin-10|||Omega-N-methylarginine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000064749 http://togogenome.org/gene/10090:Fam241b ^@ http://purl.uniprot.org/uniprot/Q9D882 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Protein FAM241B ^@ http://purl.uniprot.org/annotation/PRO_0000089791 http://togogenome.org/gene/10090:Ovch2 ^@ http://purl.uniprot.org/uniprot/Q7M761 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Activation peptide|||CUB 1|||CUB 2|||Charge relay system|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Ovochymase-2|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000261183|||http://purl.uniprot.org/annotation/PRO_0000261184|||http://purl.uniprot.org/annotation/VSP_021668 http://togogenome.org/gene/10090:Ccdc179 ^@ http://purl.uniprot.org/uniprot/J3QM76 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 179|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000421699 http://togogenome.org/gene/10090:Mybl2 ^@ http://purl.uniprot.org/uniprot/P48972 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand ^@ 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|||Myb-related protein B|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphothreonine|||Phosphothreonine; by CDK2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000197059 http://togogenome.org/gene/10090:Clec10a ^@ http://purl.uniprot.org/uniprot/F8WHB7|||http://purl.uniprot.org/uniprot/P49300 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 10 member A|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046657 http://togogenome.org/gene/10090:Naa11 ^@ http://purl.uniprot.org/uniprot/A8W660|||http://purl.uniprot.org/uniprot/Q3UX61 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Interaction with NAA15|||N-acetyltransferase|||N-alpha-acetyltransferase 11|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000305010 http://togogenome.org/gene/10090:Dnah7c ^@ http://purl.uniprot.org/uniprot/A0A087WR13 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disordered|||EF-hand ^@ http://togogenome.org/gene/10090:Zfp933 ^@ http://purl.uniprot.org/uniprot/Q6PEE4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Efcab2 ^@ http://purl.uniprot.org/uniprot/Q9CQ46 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Dynein regulatory complex protein 8|||EF-hand 1|||EF-hand 2 ^@ http://purl.uniprot.org/annotation/PRO_0000253545 http://togogenome.org/gene/10090:Slc2a1 ^@ http://purl.uniprot.org/uniprot/P17809 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||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|||Lethality immediately after birth in knockin mice; caused by creation of a dileucine internalization motif that promotes mislocalization of the protein.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Solute carrier family 2, facilitated glucose transporter member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000050339 http://togogenome.org/gene/10090:Nek7 ^@ http://purl.uniprot.org/uniprot/Q3TN15|||http://purl.uniprot.org/uniprot/Q9ES74 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Site ^@ Autoinhibitory|||N-acetylmethionine|||NTE motif|||No effect on interaction with NLRP3.|||Phosphoserine|||Phosphoserine; by NEK9|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek7 ^@ http://purl.uniprot.org/annotation/PRO_0000086431 http://togogenome.org/gene/10090:Col18a1 ^@ http://purl.uniprot.org/uniprot/E9QPX1|||http://purl.uniprot.org/uniprot/P39061 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Abolishes zinc binding.|||Basic and acidic residues|||Cell attachment site|||Collagen alpha-1(XVIII) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Disordered|||Endostatin|||FZ|||In isoform 2.|||In isoform 3.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||No effect on zinc binding.|||No effect on zinc binding. Abolishes zinc binding; when associated with A-1593.|||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 (Xyl...) (chondroitin sulfate) serine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduces zinc binding by 60%. Abolishes zinc binding; when associated with A-1595.|||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/PRO_0000005795|||http://purl.uniprot.org/annotation/PRO_0000005796|||http://purl.uniprot.org/annotation/PRO_0000441862|||http://purl.uniprot.org/annotation/PRO_5003244834|||http://purl.uniprot.org/annotation/VSP_001157|||http://purl.uniprot.org/annotation/VSP_001158|||http://purl.uniprot.org/annotation/VSP_008303 http://togogenome.org/gene/10090:Or4a76 ^@ http://purl.uniprot.org/uniprot/L7MU51 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp967 ^@ http://purl.uniprot.org/uniprot/A2ART2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Glt28d2 ^@ http://purl.uniprot.org/uniprot/Q8BML3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Glycosyl transferase family 28 C-terminal ^@ http://togogenome.org/gene/10090:Tasl ^@ http://purl.uniprot.org/uniprot/Q9D3J9 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Modified Residue|||Motif ^@ Phosphoserine|||TLR adapter interacting with SLC15A4 on the lysosome|||pLxIS motif ^@ http://purl.uniprot.org/annotation/PRO_0000251253 http://togogenome.org/gene/10090:Eif3j1 ^@ http://purl.uniprot.org/uniprot/Q3UGC7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 3 subunit J-A|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Promotes stable association with the 40S ribosome|||Sufficient for interaction with EIF3B ^@ http://purl.uniprot.org/annotation/PRO_0000419334 http://togogenome.org/gene/10090:Snrpd1 ^@ http://purl.uniprot.org/uniprot/P62315 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region ^@ Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Required for interaction with SMN1|||Sm|||Small nuclear ribonucleoprotein Sm D1|||Sufficient for interaction with CLNS1A ^@ http://purl.uniprot.org/annotation/PRO_0000122202 http://togogenome.org/gene/10090:4921509C19Rik ^@ http://purl.uniprot.org/uniprot/Q8C0X8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Protein kinase|||Proton acceptor|||Sperm motility kinase X|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000307875 http://togogenome.org/gene/10090:Atp4b ^@ http://purl.uniprot.org/uniprot/P50992|||http://purl.uniprot.org/uniprot/Q0VBB6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||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_0000219092 http://togogenome.org/gene/10090:Enpep ^@ http://purl.uniprot.org/uniprot/P16406|||http://purl.uniprot.org/uniprot/Q52JJ6|||http://purl.uniprot.org/uniprot/Q6P3C1|||http://purl.uniprot.org/uniprot/Q8CD51 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Aminopeptidase N-like N-terminal|||Binds calcium which modulates its enzyme activity|||Cytoplasmic|||Disordered|||ERAP1-like C-terminal|||Extracellular|||Glutamyl aminopeptidase|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Peptidase M1 membrane alanine aminopeptidase|||Proton acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000095096 http://togogenome.org/gene/10090:Kcnq1 ^@ http://purl.uniprot.org/uniprot/P97414 ^@ Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-terminal assembly domain|||Cytoplasmic|||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 II.|||Interaction with AKAP9|||Interaction with CALM|||Interaction with CALM; calcium-dependent|||Interaction with KCNE1 C-terminus|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKA|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily KQT member 1|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054024|||http://purl.uniprot.org/annotation/VSP_000983|||http://purl.uniprot.org/annotation/VSP_011748 http://togogenome.org/gene/10090:Arfip1 ^@ http://purl.uniprot.org/uniprot/E9QAY5|||http://purl.uniprot.org/uniprot/G5E8V9 ^@ 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 ^@ AH|||Arfaptin-1|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000453921|||http://purl.uniprot.org/annotation/VSP_061208|||http://purl.uniprot.org/annotation/VSP_061209 http://togogenome.org/gene/10090:Flrt3 ^@ http://purl.uniprot.org/uniprot/Q8BGT1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes homooligomerization and FLRT3-mediated cell-cell adhesion; when associated with N-181.|||Abolishes homooligomerization and FLRT3-mediated cell-cell adhesion; when associated with T-183.|||Abolishes interaction with ADGRL3.|||Abolishes interaction with UNC5B.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000434517 http://togogenome.org/gene/10090:Ccdc27 ^@ http://purl.uniprot.org/uniprot/B1AX94|||http://purl.uniprot.org/uniprot/Q3V036 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Coiled-coil domain-containing protein 27|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000234021 http://togogenome.org/gene/10090:Trerf1 ^@ http://purl.uniprot.org/uniprot/Q8BXJ2 ^@ 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 ^@ Acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||ELM2|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SANT|||Transcriptional-regulating factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000197135|||http://purl.uniprot.org/annotation/VSP_015647|||http://purl.uniprot.org/annotation/VSP_015648|||http://purl.uniprot.org/annotation/VSP_015649|||http://purl.uniprot.org/annotation/VSP_015650|||http://purl.uniprot.org/annotation/VSP_015651 http://togogenome.org/gene/10090:Rps4x ^@ http://purl.uniprot.org/uniprot/P62702|||http://purl.uniprot.org/uniprot/Q545F8|||http://purl.uniprot.org/uniprot/Q545X8 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000130809 http://togogenome.org/gene/10090:Fzd4 ^@ http://purl.uniprot.org/uniprot/Q3V1B2|||http://purl.uniprot.org/uniprot/Q61088|||http://purl.uniprot.org/uniprot/Q8BKU9|||http://purl.uniprot.org/uniprot/Q8BLL2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||FZ|||Frizzled-4|||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_0000012986|||http://purl.uniprot.org/annotation/PRO_5004303749|||http://purl.uniprot.org/annotation/PRO_5009970846 http://togogenome.org/gene/10090:Klhl42 ^@ http://purl.uniprot.org/uniprot/B2KFS7|||http://purl.uniprot.org/uniprot/Q8BFQ9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 42 ^@ http://purl.uniprot.org/annotation/PRO_0000119129 http://togogenome.org/gene/10090:Asb5 ^@ http://purl.uniprot.org/uniprot/Q2VPQ8|||http://purl.uniprot.org/uniprot/Q9D1A4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Domain Extent|||Repeat|||Transmembrane ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 5|||Helical|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066931 http://togogenome.org/gene/10090:Scd4 ^@ http://purl.uniprot.org/uniprot/Q6T707 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Lumenal|||Polar residues|||Stearoyl-CoA desaturase 4 ^@ http://purl.uniprot.org/annotation/PRO_0000433872 http://togogenome.org/gene/10090:Man1b1 ^@ http://purl.uniprot.org/uniprot/A2AJ15 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000396622 http://togogenome.org/gene/10090:Tspyl1 ^@ http://purl.uniprot.org/uniprot/O88852 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Testis-specific Y-encoded-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000185671 http://togogenome.org/gene/10090:Cwh43 ^@ http://purl.uniprot.org/uniprot/Q91YL7 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PGAP2-interacting protein|||Required for function in lipid remodeling ^@ http://purl.uniprot.org/annotation/PRO_0000320616|||http://purl.uniprot.org/annotation/VSP_031684 http://togogenome.org/gene/10090:Pcbd2 ^@ http://purl.uniprot.org/uniprot/Q9CZL5 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Strand|||Turn ^@ N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Pterin-4-alpha-carbinolamine dehydratase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000063058 http://togogenome.org/gene/10090:Or8k16 ^@ http://purl.uniprot.org/uniprot/Q8VGC7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bsx ^@ http://purl.uniprot.org/uniprot/Q810B3 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||DNA Binding|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes the nuclear localization; when associated with G-101.|||Abolishes the nuclear localization; when associated with G-109.|||Brain-specific homeobox protein homolog|||Disordered|||Homeobox|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000048844|||http://purl.uniprot.org/annotation/VSP_027570|||http://purl.uniprot.org/annotation/VSP_027571 http://togogenome.org/gene/10090:H2bc24 ^@ http://purl.uniprot.org/uniprot/P10853|||http://purl.uniprot.org/uniprot/Q8CBB6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||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 H2A/H2B/H3|||Histone H2B type 1-F/J/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-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_0000071839 http://togogenome.org/gene/10090:Ece1 ^@ http://purl.uniprot.org/uniprot/A0A183ZRM3|||http://purl.uniprot.org/uniprot/Q4PZA2 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endothelin-converting enzyme 1|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform A.|||In isoform C.|||In isoform D.|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Peptidase M13 C-terminal|||Peptidase M13 N-terminal|||Phosphothreonine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000240629|||http://purl.uniprot.org/annotation/VSP_019399|||http://purl.uniprot.org/annotation/VSP_019400|||http://purl.uniprot.org/annotation/VSP_019401 http://togogenome.org/gene/10090:Pacsin3 ^@ http://purl.uniprot.org/uniprot/Q543N7|||http://purl.uniprot.org/uniprot/Q99JB8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||F-BAR|||Loss of DNM1-, SYNJ1- and WASL-binding. Loss of effect on transferrin endocytosis.|||Phosphoserine|||Phosphothreonine|||Protein kinase C and casein kinase II substrate protein 3|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000161801 http://togogenome.org/gene/10090:Zfp667 ^@ http://purl.uniprot.org/uniprot/Q2TL60 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||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|||KRAB|||Polar residues|||Zinc finger protein 667 ^@ http://purl.uniprot.org/annotation/PRO_0000251898 http://togogenome.org/gene/10090:Hsd11b2 ^@ http://purl.uniprot.org/uniprot/P51661 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ 11-beta-hydroxysteroid dehydrogenase type 2|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054628 http://togogenome.org/gene/10090:Irf2bp1 ^@ http://purl.uniprot.org/uniprot/Q8R3Y8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Cys-rich|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interferon regulatory factor 2-binding protein 1|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000328730|||http://purl.uniprot.org/annotation/VSP_032768 http://togogenome.org/gene/10090:Dnaaf11 ^@ http://purl.uniprot.org/uniprot/O88978 ^@ 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 ^@ Basic and acidic residues|||CS|||Disordered|||Dynein axonemal assembly factor 11|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084498 http://togogenome.org/gene/10090:Trh ^@ http://purl.uniprot.org/uniprot/Q62361 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Pro-thyrotropin-releasing hormone|||Proline amide|||Thyrotropin-releasing hormone ^@ http://purl.uniprot.org/annotation/PRO_0000022516|||http://purl.uniprot.org/annotation/PRO_0000022517|||http://purl.uniprot.org/annotation/PRO_0000022518|||http://purl.uniprot.org/annotation/PRO_0000022519|||http://purl.uniprot.org/annotation/PRO_0000022520|||http://purl.uniprot.org/annotation/PRO_0000022521 http://togogenome.org/gene/10090:Mthfd1 ^@ http://purl.uniprot.org/uniprot/Q3TW74|||http://purl.uniprot.org/uniprot/Q8BXX7|||http://purl.uniprot.org/uniprot/Q922D8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ C-1-tetrahydrofolate synthase, cytoplasmic|||C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processed|||Formyltetrahydrofolate synthetase domain|||Methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase (D/C) domain|||N-acetylmethionine|||Phosphoserine|||Removed; alternate|||Tetrahydrofolate dehydrogenase/cyclohydrolase NAD(P)-binding|||Tetrahydrofolate dehydrogenase/cyclohydrolase catalytic ^@ http://purl.uniprot.org/annotation/PRO_0000199322|||http://purl.uniprot.org/annotation/PRO_0000423281 http://togogenome.org/gene/10090:Or10ad1c ^@ http://purl.uniprot.org/uniprot/E9Q1P2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Jade1 ^@ http://purl.uniprot.org/uniprot/Q6ZPI0 ^@ 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|||C2HC pre-PHD-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with KAT7/HBO1 and histones|||Interaction with histones|||N6-acetyllysine|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein Jade-1 ^@ http://purl.uniprot.org/annotation/PRO_0000253530|||http://purl.uniprot.org/annotation/VSP_021048|||http://purl.uniprot.org/annotation/VSP_021049 http://togogenome.org/gene/10090:Phlda3 ^@ http://purl.uniprot.org/uniprot/Q9WV95 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Domain Extent|||Mutagenesis Site ^@ Impairs the ability to resucue growth in cdc25ts mutant yeasts.|||PH|||Pleckstrin homology-like domain family A member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000053903 http://togogenome.org/gene/10090:Cdkal1 ^@ http://purl.uniprot.org/uniprot/Q91WE6 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||MTTase N-terminal|||Phosphoserine|||Phosphothreonine|||Radical SAM core|||TRAM|||Threonylcarbamoyladenosine tRNA methylthiotransferase ^@ http://purl.uniprot.org/annotation/PRO_0000298671|||http://purl.uniprot.org/annotation/VSP_027454|||http://purl.uniprot.org/annotation/VSP_027455|||http://purl.uniprot.org/annotation/VSP_027456|||http://purl.uniprot.org/annotation/VSP_027457|||http://purl.uniprot.org/annotation/VSP_027458|||http://purl.uniprot.org/annotation/VSP_027459|||http://purl.uniprot.org/annotation/VSP_027460 http://togogenome.org/gene/10090:Khdc4 ^@ http://purl.uniprot.org/uniprot/Q3TCX3 ^@ 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.|||In isoform 3.|||In isoform 4.|||KH 1|||KH 2|||KH homology domain-containing protein 4|||Phosphoserine|||Polar residues|||Required for nuclear retention ^@ http://purl.uniprot.org/annotation/PRO_0000296670|||http://purl.uniprot.org/annotation/VSP_027244|||http://purl.uniprot.org/annotation/VSP_027245|||http://purl.uniprot.org/annotation/VSP_027246|||http://purl.uniprot.org/annotation/VSP_027247|||http://purl.uniprot.org/annotation/VSP_027248|||http://purl.uniprot.org/annotation/VSP_027249 http://togogenome.org/gene/10090:Bcl2a1c ^@ http://purl.uniprot.org/uniprot/Q0P538 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Bcl-2 Bcl-2 homology region 1-3 ^@ http://togogenome.org/gene/10090:Pxdn ^@ http://purl.uniprot.org/uniprot/Q3UQ28 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage; by FURIN|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Interchain (with C-1312); in homotrimer|||Interchain (with C-733); in homotrimer|||Kinky tail mutant mice show kinky tail and white spot at the belly; additionally, homozygous mutants show microphthalmia and anterior segment dysgenesis including corneal opacity, severe iris bombe (forward-bowing iris) and very shallow or absent anterior chamber.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||PXDN active fragment|||Peroxidasin homolog|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Required in homotrimerization|||Transition state stabilizer|||VWFC|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000319620|||http://purl.uniprot.org/annotation/PRO_0000455176 http://togogenome.org/gene/10090:Trim5 ^@ http://purl.uniprot.org/uniprot/E9PV98 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ B box-type|||B30.2/SPRY|||RING-type ^@ http://togogenome.org/gene/10090:Mettl25 ^@ http://purl.uniprot.org/uniprot/Q6NXH8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Probable methyltransferase-like protein 25 ^@ http://purl.uniprot.org/annotation/PRO_0000252149 http://togogenome.org/gene/10090:Scaf11 ^@ http://purl.uniprot.org/uniprot/E9PZM7|||http://purl.uniprot.org/uniprot/Q6ZPE9 ^@ 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|||Pro residues|||RING-type ^@ http://togogenome.org/gene/10090:Ribc1 ^@ http://purl.uniprot.org/uniprot/Q9D0B8 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ RIB43A-like with coiled-coils protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000254095 http://togogenome.org/gene/10090:Gclm ^@ http://purl.uniprot.org/uniprot/O09172 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Glutamate--cysteine ligase regulatory subunit|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000192574 http://togogenome.org/gene/10090:Tagln3 ^@ http://purl.uniprot.org/uniprot/Q9R1Q8 ^@ 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_0000204789 http://togogenome.org/gene/10090:Btg1c ^@ http://purl.uniprot.org/uniprot/Q3V0X0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Anti-proliferative protein ^@ http://togogenome.org/gene/10090:Gm1993 ^@ http://purl.uniprot.org/uniprot/A6X8I0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Amotl2 ^@ http://purl.uniprot.org/uniprot/Q8K371 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Angiomotin-like protein 2|||Basic and acidic residues|||Disordered|||PDZ-binding|||Phosphoserine|||Phosphotyrosine; by FGFR1|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000190673 http://togogenome.org/gene/10090:Cetn1 ^@ http://purl.uniprot.org/uniprot/P41209 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn ^@ Centrin-1|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000073560 http://togogenome.org/gene/10090:Tmem163 ^@ http://purl.uniprot.org/uniprot/Q8C996 ^@ 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|||Pro residues|||Required for interaction with MCOLN1|||Transmembrane protein 163 ^@ http://purl.uniprot.org/annotation/PRO_0000278540 http://togogenome.org/gene/10090:Rdh8 ^@ http://purl.uniprot.org/uniprot/D3Z6W3 ^@ Active Site|||Binding Site|||Site ^@ Active Site|||Binding Site ^@ Proton acceptor ^@ http://togogenome.org/gene/10090:Or2b7 ^@ http://purl.uniprot.org/uniprot/Q7TQU0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gm15128 ^@ http://purl.uniprot.org/uniprot/A2ADW8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Aqp11 ^@ http://purl.uniprot.org/uniprot/Q8BHH1 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Motif|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Aquaporin-11|||Cytoplasmic|||Does not affect endoplasmic reticulum localization. Does not affect plama membrane localization. Reduces oligomerization. Impairs water permeability.|||Does not affect oligomerization formation.|||Extracellular|||Helical|||Homozygous sudden juvenile death syndrome (sjds) mice die before 20 day of age and exhibit severe proximal tubule injury and formation of giant vacuoles in the renal cortex. Interfers with maintenance of AQP11 oligomeric structure. Aqp11 mutant mice developed proximal tubule (PT)-specific mitochondrial injury. Heterozygous sudden juvenile death syndrome (sjds) mice exhibit higher AQP11 levels but are not further increased in response to glucose. Upon glucose treatment, heterozygous Aqp11 mice show increased blood urea nitrogen levels that are prevented by the antioxidant sulforaphane or by phlorizin.|||NPA|||NPC|||Reduces oligomerization. ^@ http://purl.uniprot.org/annotation/PRO_0000063969 http://togogenome.org/gene/10090:Vmn1r78 ^@ http://purl.uniprot.org/uniprot/K7N608 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gsdme ^@ http://purl.uniprot.org/uniprot/Q9Z2D3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Modified Residue|||Region|||Site ^@ Cleavage; by CASP3 or granzyme B|||Gasdermin-E|||Gasdermin-E, C-terminal|||Gasdermin-E, N-terminal|||Membrane targeting domain|||S-(2-succinyl)cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000148179|||http://purl.uniprot.org/annotation/PRO_0000442749|||http://purl.uniprot.org/annotation/PRO_0000442750 http://togogenome.org/gene/10090:Prmt2 ^@ http://purl.uniprot.org/uniprot/Q3UID4|||http://purl.uniprot.org/uniprot/Q3UKX1 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ SH3 ^@ http://togogenome.org/gene/10090:Mettl3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J041|||http://purl.uniprot.org/uniprot/Q8C3P7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Gate loop 1|||Gate loop 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||Interaction with METTL14|||Interphase loop|||Loss of activity.|||N-acetylserine; alternate|||N6-adenosine-methyltransferase subunit METTL3|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; alternate|||Polar residues|||Positively charged region required for RNA-binding|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207631|||http://purl.uniprot.org/annotation/VSP_007867|||http://purl.uniprot.org/annotation/VSP_007868 http://togogenome.org/gene/10090:Senp8 ^@ http://purl.uniprot.org/uniprot/A0A1L1SRH8|||http://purl.uniprot.org/uniprot/Q3UWN3|||http://purl.uniprot.org/uniprot/Q9D2Z4 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ N-acetylmethionine|||Nucleophile|||Protease|||Sentrin-specific protease 8|||Ubiquitin-like protease family profile ^@ http://purl.uniprot.org/annotation/PRO_0000101728 http://togogenome.org/gene/10090:Dtx4 ^@ http://purl.uniprot.org/uniprot/Q6PDK8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase DTX4|||RING-type; atypical|||WWE 1|||WWE 2 ^@ http://purl.uniprot.org/annotation/PRO_0000280556 http://togogenome.org/gene/10090:Zscan26 ^@ http://purl.uniprot.org/uniprot/F8WJ31|||http://purl.uniprot.org/uniprot/Q5RJ54 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||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|||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 26 ^@ http://purl.uniprot.org/annotation/PRO_0000307314|||http://purl.uniprot.org/annotation/VSP_028703 http://togogenome.org/gene/10090:H2bc14 ^@ http://purl.uniprot.org/uniprot/B2RTK3|||http://purl.uniprot.org/uniprot/P10854 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||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 H2A/H2B/H3|||Histone H2B type 1-M|||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-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_0000071840 http://togogenome.org/gene/10090:Muc5b ^@ http://purl.uniprot.org/uniprot/E9Q5I3|||http://purl.uniprot.org/uniprot/Q8BYW0|||http://purl.uniprot.org/uniprot/Q9CV93 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide ^@ CTCK|||Disordered|||Polar residues|||VWFC|||VWFD|||VWFD domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5003245750|||http://purl.uniprot.org/annotation/PRO_5004307263 http://togogenome.org/gene/10090:Mdga2 ^@ http://purl.uniprot.org/uniprot/B2RQF5|||http://purl.uniprot.org/uniprot/P60755|||http://purl.uniprot.org/uniprot/Q3UV20 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide|||Transmembrane ^@ Fibronectin type-III|||GPI-anchor amidated aspartate|||Helical|||Ig-like|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||Ig-like 6|||MAM|||MAM domain-containing glycosylphosphatidylinositol anchor protein 2|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000014860|||http://purl.uniprot.org/annotation/PRO_0000292044|||http://purl.uniprot.org/annotation/PRO_5015087146 http://togogenome.org/gene/10090:Prorp ^@ http://purl.uniprot.org/uniprot/Q8JZY4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide ^@ Mitochondrial ribonuclease P catalytic subunit|||Mitochondrion|||PRORP ^@ http://purl.uniprot.org/annotation/PRO_0000360397 http://togogenome.org/gene/10090:Os9 ^@ http://purl.uniprot.org/uniprot/Q8K2C7 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||MRH|||N-linked (GlcNAc...) asparagine|||Protein OS-9 ^@ http://purl.uniprot.org/annotation/PRO_0000386449|||http://purl.uniprot.org/annotation/VSP_038220 http://togogenome.org/gene/10090:Car13 ^@ http://purl.uniprot.org/uniprot/Q9D6N1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase 13|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000077441 http://togogenome.org/gene/10090:Syt3 ^@ http://purl.uniprot.org/uniprot/G3X9Y1|||http://purl.uniprot.org/uniprot/O35681 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Abolishes disulfide-dependent homodimerization. Abolishes disulfide-dependent homodimerization; when associated with A-21.|||Abolishes disulfide-dependent homodimerization; when associated with A-10. Does not affect disulfide-dependent homodimerization; when associated with A-33.|||C2|||C2 1|||C2 2|||Cysteine motif|||Cytoplasmic|||Disordered|||Does not affect disulfide-dependent homodimerization; when associated with A-21.|||Helical|||Omega-N-methylarginine|||Polar residues|||Synaptotagmin-3|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000183946 http://togogenome.org/gene/10090:Klf10 ^@ http://purl.uniprot.org/uniprot/O89091|||http://purl.uniprot.org/uniprot/Q8C900 ^@ 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 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 10|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000047178 http://togogenome.org/gene/10090:Fbxw21 ^@ http://purl.uniprot.org/uniprot/Q8BI38 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Kptn ^@ http://purl.uniprot.org/uniprot/G3X8R1 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:C10H2orf16 ^@ http://purl.uniprot.org/uniprot/A0A1W2P6U8 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Ccdc3 ^@ http://purl.uniprot.org/uniprot/Q9D6Y1 ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Signal Peptide ^@ Coiled-coil domain-containing protein 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000020863 http://togogenome.org/gene/10090:Polr2m ^@ http://purl.uniprot.org/uniprot/Q6P6I6 ^@ 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|||DNA-directed RNA polymerase II subunit GRINL1A|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000326230|||http://purl.uniprot.org/annotation/VSP_032623 http://togogenome.org/gene/10090:Pltp ^@ http://purl.uniprot.org/uniprot/P55065|||http://purl.uniprot.org/uniprot/Q3UE59|||http://purl.uniprot.org/uniprot/Q3UFS5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide ^@ Lipid-binding serum glycoprotein C-terminal|||Lipid-binding serum glycoprotein N-terminal|||N-linked (GlcNAc...) asparagine|||Phospholipid transfer protein ^@ http://purl.uniprot.org/annotation/PRO_0000017163|||http://purl.uniprot.org/annotation/PRO_5004230055|||http://purl.uniprot.org/annotation/PRO_5014309196 http://togogenome.org/gene/10090:Tomm34 ^@ http://purl.uniprot.org/uniprot/Q9CYG7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Mitochondrial import receptor subunit TOM34|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6 ^@ http://purl.uniprot.org/annotation/PRO_0000106335|||http://purl.uniprot.org/annotation/VSP_035044 http://togogenome.org/gene/10090:Col6a3 ^@ http://purl.uniprot.org/uniprot/J3QQ16|||http://purl.uniprot.org/uniprot/Q9Z0I9 ^@ 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 ^@ BPTI/Kunitz inhibitor|||Basic and acidic residues|||Disordered|||Fibronectin type-III|||Pro residues|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5003777325|||http://purl.uniprot.org/annotation/PRO_5004338806 http://togogenome.org/gene/10090:Or5h17 ^@ http://purl.uniprot.org/uniprot/E9QKE8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Acbd5 ^@ http://purl.uniprot.org/uniprot/E9QNH7|||http://purl.uniprot.org/uniprot/Q5CZX6|||http://purl.uniprot.org/uniprot/Q5XG73 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Transmembrane ^@ ACB|||Acyl-CoA-binding domain-containing protein 5|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000287378|||http://purl.uniprot.org/annotation/PRO_5012203865|||http://purl.uniprot.org/annotation/VSP_025450|||http://purl.uniprot.org/annotation/VSP_025451 http://togogenome.org/gene/10090:Hnf1b ^@ http://purl.uniprot.org/uniprot/P27889 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Dimerization|||Disordered|||HNF-p1|||Hepatocyte nuclear factor 1-beta|||Homeobox; HNF1-type|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In strain: NSY.|||POU-specific atypical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000049122|||http://purl.uniprot.org/annotation/VSP_007099|||http://purl.uniprot.org/annotation/VSP_007100 http://togogenome.org/gene/10090:Trem3 ^@ http://purl.uniprot.org/uniprot/Q9JKE1 ^@ 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|||Helical|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Triggering receptor expressed on myeloid cells 3 ^@ http://purl.uniprot.org/annotation/PRO_5015099788 http://togogenome.org/gene/10090:Fibin ^@ http://purl.uniprot.org/uniprot/Q9CQS3 ^@ 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_0000349212 http://togogenome.org/gene/10090:Mctp2 ^@ http://purl.uniprot.org/uniprot/Q5RJH2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||C2 1|||C2 2|||C2 3|||Disordered|||Helical|||Multiple C2 and transmembrane domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000294473 http://togogenome.org/gene/10090:S100a14 ^@ http://purl.uniprot.org/uniprot/Q9D2Q8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ EF-hand|||Protein S100-A14 ^@ http://purl.uniprot.org/annotation/PRO_0000144022 http://togogenome.org/gene/10090:Slc16a4 ^@ http://purl.uniprot.org/uniprot/Q8R0M8 ^@ 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.|||In isoform 3.|||Monocarboxylate transporter 5 ^@ http://purl.uniprot.org/annotation/PRO_0000416125|||http://purl.uniprot.org/annotation/VSP_042510|||http://purl.uniprot.org/annotation/VSP_042511 http://togogenome.org/gene/10090:Usp50 ^@ http://purl.uniprot.org/uniprot/Q6P8X6 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Nucleophile|||Proton acceptor|||Putative ubiquitin carboxyl-terminal hydrolase 50|||USP ^@ http://purl.uniprot.org/annotation/PRO_0000249529|||http://purl.uniprot.org/annotation/VSP_020486|||http://purl.uniprot.org/annotation/VSP_020487 http://togogenome.org/gene/10090:Me3 ^@ http://purl.uniprot.org/uniprot/Q8BMF3 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Disordered|||Important for activity|||Mitochondrion|||NADP-dependent malic enzyme, mitochondrial|||Phosphoserine|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000018540 http://togogenome.org/gene/10090:Ndufaf2 ^@ http://purl.uniprot.org/uniprot/Q59J78 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transit Peptide ^@ Disordered|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000020055 http://togogenome.org/gene/10090:Vmn1r3 ^@ http://purl.uniprot.org/uniprot/A2AMT7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cldn3 ^@ http://purl.uniprot.org/uniprot/Q545A5|||http://purl.uniprot.org/uniprot/Q9Z0G9 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Claudin-3|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Interactions with TJP1, TJP2 and TJP3|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000144739|||http://purl.uniprot.org/annotation/VSP_001101 http://togogenome.org/gene/10090:Slc39a3 ^@ http://purl.uniprot.org/uniprot/A0A452J893|||http://purl.uniprot.org/uniprot/Q99K24 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Phosphoserine|||Zinc transporter ZIP3 ^@ http://purl.uniprot.org/annotation/PRO_0000312869 http://togogenome.org/gene/10090:Gabrg1 ^@ http://purl.uniprot.org/uniprot/Q9R0Y8 ^@ 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|||Gamma-aminobutyric acid receptor subunit gamma-1|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000000474 http://togogenome.org/gene/10090:Slu7 ^@ http://purl.uniprot.org/uniprot/Q8BHJ9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Bipartite nuclear localization signal|||CCHC-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylserine|||Phosphoserine|||Pre-mRNA-splicing factor SLU7|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000289196 http://togogenome.org/gene/10090:Necap1 ^@ http://purl.uniprot.org/uniprot/Q0VB06|||http://purl.uniprot.org/uniprot/Q9CR95 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Adaptin ear-binding coat-associated protein 1|||Disordered|||Loss of binding to AP-2 and can bind to AP-1; when associated with D-270.|||Loss of binding to AP-2 and can bind to AP-1; when associated with G-273.|||Loss of binding to AP-2.|||NECAP PHear|||No effect on binding to AP-2.|||Phosphothreonine|||Polar residues|||WXXF motif 1|||WXXF motif 2 ^@ http://purl.uniprot.org/annotation/PRO_0000213068 http://togogenome.org/gene/10090:Atp1a2 ^@ http://purl.uniprot.org/uniprot/Q3UHK5|||http://purl.uniprot.org/uniprot/Q6PIE5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Propeptide|||Region|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with phosphoinositide-3 kinase|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Sodium/potassium-transporting ATPase subunit alpha-2 ^@ http://purl.uniprot.org/annotation/PRO_0000002505|||http://purl.uniprot.org/annotation/PRO_0000002506 http://togogenome.org/gene/10090:Gtf3c3 ^@ http://purl.uniprot.org/uniprot/Q3TMP1 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||TPR ^@ http://togogenome.org/gene/10090:1810055G02Rik ^@ http://purl.uniprot.org/uniprot/Q9D8N1 ^@ 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|||Uncharacterized protein C11orf24 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000251888 http://togogenome.org/gene/10090:Slc13a1 ^@ http://purl.uniprot.org/uniprot/Q9JHI4 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 13 member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000172486|||http://purl.uniprot.org/annotation/VSP_006121|||http://purl.uniprot.org/annotation/VSP_006122 http://togogenome.org/gene/10090:Pierce2 ^@ http://purl.uniprot.org/uniprot/V9GXK1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Piercer of microtubule wall 2 protein ^@ http://purl.uniprot.org/annotation/PRO_0000455517 http://togogenome.org/gene/10090:Elp3 ^@ http://purl.uniprot.org/uniprot/Q9CZX0 ^@ 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 ^@ Elongator complex protein 3|||In isoform 2.|||N-acetyltransferase|||N6-methyllysine|||Phosphoserine|||Phosphotyrosine|||Radical SAM core ^@ http://purl.uniprot.org/annotation/PRO_0000283987|||http://purl.uniprot.org/annotation/VSP_024408 http://togogenome.org/gene/10090:Prps2 ^@ http://purl.uniprot.org/uniprot/Q9CS42 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Region ^@ Binding of phosphoribosylpyrophosphate|||Ribose-phosphate pyrophosphokinase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000141076 http://togogenome.org/gene/10090:Or4a81 ^@ http://purl.uniprot.org/uniprot/Q8VFB1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Morc2b ^@ http://purl.uniprot.org/uniprot/Q8C5W4 ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ATPase MORC2B|||CW-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000248244|||http://purl.uniprot.org/annotation/VSP_052135 http://togogenome.org/gene/10090:Or4c3d ^@ http://purl.uniprot.org/uniprot/Q60878 ^@ 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 4C3D ^@ http://purl.uniprot.org/annotation/PRO_0000150817 http://togogenome.org/gene/10090:Or8k32 ^@ http://purl.uniprot.org/uniprot/Q8VF52 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hapln4 ^@ http://purl.uniprot.org/uniprot/Q80WM4 ^@ 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 ^@ Hyaluronan and proteoglycan link protein 4|||Ig-like C2-type|||Link 1|||Link 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000013193 http://togogenome.org/gene/10090:BC024139 ^@ http://purl.uniprot.org/uniprot/Q8BVJ3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||GAR|||Polar residues ^@ http://togogenome.org/gene/10090:Ptprd ^@ http://purl.uniprot.org/uniprot/B9EJA3|||http://purl.uniprot.org/uniprot/Q64487 ^@ 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|||Signal Peptide|||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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes interaction with SLITRK2.|||Cleavage|||Cytoplasmic|||Decreases affinity for IL1RAP.|||Decreases affinity for interaction with IL1RAPL1.|||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 isoform A and isoform B.|||In isoform A and isoform L.|||In isoform B and isoform C.|||In isoform C, isoform E, isoform G, isoform I and isoform K.|||In isoform C, isoform H and isoform I.|||In isoform F and isoform G.|||In isoform J and isoform K.|||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 effect on interaction with SLITRK2. Decreases the affinity for IL1RAPL1. Abolishes interaction with IL1RAP.|||Phosphocysteine intermediate|||Receptor-type tyrosine-protein phosphatase delta|||Reduces affinity with IL1RAPL1. Reduces the synaptogenic activity to ~7%.|||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_0000025438|||http://purl.uniprot.org/annotation/PRO_5015087498|||http://purl.uniprot.org/annotation/VSP_043545|||http://purl.uniprot.org/annotation/VSP_043546|||http://purl.uniprot.org/annotation/VSP_043547|||http://purl.uniprot.org/annotation/VSP_043548|||http://purl.uniprot.org/annotation/VSP_043549|||http://purl.uniprot.org/annotation/VSP_043550|||http://purl.uniprot.org/annotation/VSP_043551|||http://purl.uniprot.org/annotation/VSP_043552|||http://purl.uniprot.org/annotation/VSP_043553 http://togogenome.org/gene/10090:Rnf32 ^@ http://purl.uniprot.org/uniprot/Q9JIT1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||IQ|||RING finger protein 32|||RING-type 1; atypical|||RING-type 2; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000245534 http://togogenome.org/gene/10090:Rfxap ^@ http://purl.uniprot.org/uniprot/Q8VCG9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Motif|||Region ^@ Acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nuclear localization signal|||Polar residues|||Regulatory factor X-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000300252 http://togogenome.org/gene/10090:Wdr19 ^@ http://purl.uniprot.org/uniprot/Q3UGF1 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||Reduced interaction with BBS1.|||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_0000233157|||http://purl.uniprot.org/annotation/VSP_018075|||http://purl.uniprot.org/annotation/VSP_018076|||http://purl.uniprot.org/annotation/VSP_018077 http://togogenome.org/gene/10090:Nr1h4 ^@ http://purl.uniprot.org/uniprot/Q3V1T8|||http://purl.uniprot.org/uniprot/Q60641 ^@ Binding Site|||Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Bile acid receptor|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Increases affinity to CDCA and transcriptional activity in response to CDCA; when associated with I-388.|||Increases affinity to CDCA and transcriptional activity in response to CDCA; when associated with N-370.|||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_0000053539|||http://purl.uniprot.org/annotation/VSP_003666|||http://purl.uniprot.org/annotation/VSP_058157 http://togogenome.org/gene/10090:Col5a1 ^@ http://purl.uniprot.org/uniprot/B1AWB9|||http://purl.uniprot.org/uniprot/O88207 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ 3-hydroxyproline|||4-hydroxyproline|||5-hydroxylysine|||Basic and acidic residues|||Collagen alpha-1(V) chain|||Disordered|||Fibrillar collagen NC1|||In isoform 2.|||Interrupted collagenous region|||Laminin G-like|||Nonhelical region|||Polar residues|||Pro residues|||Sulfotyrosine|||Triple-helical region ^@ http://purl.uniprot.org/annotation/PRO_0000041761|||http://purl.uniprot.org/annotation/PRO_5015087029|||http://purl.uniprot.org/annotation/VSP_059656 http://togogenome.org/gene/10090:Creg2 ^@ http://purl.uniprot.org/uniprot/Q8BGC9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Abolishes N-glycosylation.|||Disordered|||N-glycosylated.|||N-linked (GlcNAc...) asparagine|||Protein CREG2 ^@ http://purl.uniprot.org/annotation/PRO_0000006207 http://togogenome.org/gene/10090:Fer ^@ http://purl.uniprot.org/uniprot/P70451|||http://purl.uniprot.org/uniprot/Q3TME9|||http://purl.uniprot.org/uniprot/Q3TZJ5 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes autophosphorylation.|||Abolishes homooligomerization.|||Abolishes interaction with PPP1CA.|||Abolishes kinase activity.|||Disordered|||F-BAR|||Important for interaction with membranes containing phosphoinositides|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SH2|||Tyrosine-protein kinase Fer ^@ http://purl.uniprot.org/annotation/PRO_0000260825|||http://purl.uniprot.org/annotation/VSP_021634|||http://purl.uniprot.org/annotation/VSP_041766|||http://purl.uniprot.org/annotation/VSP_041767|||http://purl.uniprot.org/annotation/VSP_041768|||http://purl.uniprot.org/annotation/VSP_041769|||http://purl.uniprot.org/annotation/VSP_041770 http://togogenome.org/gene/10090:Psmb7 ^@ http://purl.uniprot.org/uniprot/P70195 ^@ Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Propeptide|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Helix|||Propeptide|||Sequence Conflict|||Strand|||Turn ^@ Nucleophile|||Proteasome subunit beta type-7|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000026647|||http://purl.uniprot.org/annotation/PRO_0000026648 http://togogenome.org/gene/10090:Tsks ^@ http://purl.uniprot.org/uniprot/O54887|||http://purl.uniprot.org/uniprot/Q147V4 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Phosphoserine; by TSSK1 and TSSK2|||Testis-specific serine kinase substrate ^@ http://purl.uniprot.org/annotation/PRO_0000065666 http://togogenome.org/gene/10090:Cd63 ^@ http://purl.uniprot.org/uniprot/P41731|||http://purl.uniprot.org/uniprot/Q549D0 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Abolishes localization to lysosomes.|||CD63 antigen|||Cytoplasmic|||Extracellular|||Helical|||Lysosomal targeting motif|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219217 http://togogenome.org/gene/10090:Nrn1 ^@ http://purl.uniprot.org/uniprot/Q8CFV4 ^@ Chain|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide ^@ Chain|||Lipid Binding|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated glycine|||Neuritin|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000262514|||http://purl.uniprot.org/annotation/PRO_0000262515 http://togogenome.org/gene/10090:Il13ra2 ^@ http://purl.uniprot.org/uniprot/O88786 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||In isoform 2.|||Interleukin-13 receptor subunit alpha-2|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000378452|||http://purl.uniprot.org/annotation/VSP_037588|||http://purl.uniprot.org/annotation/VSP_037589 http://togogenome.org/gene/10090:Acp4 ^@ http://purl.uniprot.org/uniprot/D3YTS9 ^@ Active Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Nucleophile|||Proton donor|||Testicular acid phosphatase ^@ http://purl.uniprot.org/annotation/PRO_5006722351 http://togogenome.org/gene/10090:Slco1c1 ^@ http://purl.uniprot.org/uniprot/Q9ERB5 ^@ 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|||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|||N-linked (GlcNAc...) asparagine|||Solute carrier organic anion transporter family member 1C1 ^@ http://purl.uniprot.org/annotation/PRO_0000191056 http://togogenome.org/gene/10090:Ferd3l ^@ http://purl.uniprot.org/uniprot/Q923Z4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Fer3-like protein|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000328683 http://togogenome.org/gene/10090:Pde1c ^@ http://purl.uniprot.org/uniprot/A0A0N4SWG4|||http://purl.uniprot.org/uniprot/A0A5F8MPG4|||http://purl.uniprot.org/uniprot/E9Q7V6|||http://purl.uniprot.org/uniprot/Q3USZ6|||http://purl.uniprot.org/uniprot/Q5D0E7|||http://purl.uniprot.org/uniprot/Q64338|||http://purl.uniprot.org/uniprot/Q8CDV2|||http://purl.uniprot.org/uniprot/Q9D5W0 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Calmodulin-binding|||Disordered|||Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C|||In isoform 1.|||In isoform 2.|||N-acetylmethionine|||PDEase|||Polar residues|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000198793|||http://purl.uniprot.org/annotation/VSP_004554|||http://purl.uniprot.org/annotation/VSP_012380|||http://purl.uniprot.org/annotation/VSP_012381|||http://purl.uniprot.org/annotation/VSP_012382 http://togogenome.org/gene/10090:Or5an1c ^@ http://purl.uniprot.org/uniprot/Q8VFV8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tet2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JF55|||http://purl.uniprot.org/uniprot/Q4JK59 ^@ 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 ^@ Binding Site|||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 ubiquitin)|||Impairs enzyme activity.|||In isoform 2.|||In isoform 3.|||Interaction with DNA|||Loss of 5-methylcytosine demethylase activity in vivo. No effect on interaction with DCAF1, nor on monoubiquitination.|||Loss of enzyme activity, no effect on interaction with DCAF1; when associated with A-1297.|||Loss of enzyme activity, no effect on interaction with DCAF1; when associated with Y-1295.|||Loss of enzyme activity.|||Loss of interaction with DCAF1, monoubiquitination and of 5-methylcytosine demethylase activity in vivo.|||Loss of monoubiquitination and of 5-methylcytosine demethylase activity in vivo. No effect on interaction with DCAF1.|||Methylcytosine dioxygenase TET1-3 oxygenase|||Methylcytosine dioxygenase TET2|||No effect on interaction with DCAF1, monoubiquitination, nor on 5-methylcytosine demethylase activity in vivo.|||Phosphoserine|||Polar residues|||Pro residues|||Strongly reduces ubiquitination, loss of DNA-binding, loss of 5-methylcytosine demethylase activity in vivo. Does not affect nuclear localization, nor interaction with DCAF1.|||Strongly reduces ubiquitination. ^@ http://purl.uniprot.org/annotation/PRO_0000324589|||http://purl.uniprot.org/annotation/VSP_032286|||http://purl.uniprot.org/annotation/VSP_032287 http://togogenome.org/gene/10090:Letmd1 ^@ http://purl.uniprot.org/uniprot/Q924L1 ^@ 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|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||LETM1 domain-containing protein 1|||Letm1 RBD|||Mitochondrial intermembrane|||Phosphoserine|||Required and sufficient for mitochondrial import ^@ http://purl.uniprot.org/annotation/PRO_0000310420|||http://purl.uniprot.org/annotation/VSP_029280|||http://purl.uniprot.org/annotation/VSP_029281 http://togogenome.org/gene/10090:Tgfbr3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J097|||http://purl.uniprot.org/uniprot/O88393 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with TGF-beta ligand|||Loss of glycosaminoglycan chains; when associated with A-533.|||Loss of glycosaminoglycan chains; when associated with A-544.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Transforming growth factor beta receptor type 3|||ZP ^@ http://purl.uniprot.org/annotation/PRO_0000041664|||http://purl.uniprot.org/annotation/PRO_5015044284 http://togogenome.org/gene/10090:Wbp2 ^@ http://purl.uniprot.org/uniprot/P97765|||http://purl.uniprot.org/uniprot/Q544A1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes interaction with NEDD4.|||Disordered|||GRAM|||In isoform 2.|||No effect on interaction with NEDD4.|||PPxY motif 1|||PPxY motif 2|||Phosphotyrosine|||Pro residues|||WW domain-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000065951|||http://purl.uniprot.org/annotation/VSP_059234 http://togogenome.org/gene/10090:Csrnp3 ^@ http://purl.uniprot.org/uniprot/P59055|||http://purl.uniprot.org/uniprot/Q7TNU4 ^@ 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 ^@ Acidic residues|||Cysteine/serine-rich nuclear protein 3|||Cysteine/serine-rich nuclear protein N-terminal|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000114789|||http://purl.uniprot.org/annotation/VSP_034260 http://togogenome.org/gene/10090:Or13f5 ^@ http://purl.uniprot.org/uniprot/Q7TS18 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccn3 ^@ http://purl.uniprot.org/uniprot/Q64299 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Abolishes extracellular secretion. Inhibits axonal growth of callosal projections when overexpressed.|||CCN family member 3|||CTCK|||IGFBP N-terminal|||N-linked (GlcNAc...) asparagine|||No effect on extracellular secretion.|||Reduces extracellular secretion. No significant effect on axonal growth of callosal projections when overexpressed.|||S-palmitoyl cysteine|||TSP type-1|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000014416 http://togogenome.org/gene/10090:Sntg1 ^@ http://purl.uniprot.org/uniprot/Q8BNW6|||http://purl.uniprot.org/uniprot/Q8C415|||http://purl.uniprot.org/uniprot/Q8CAI8|||http://purl.uniprot.org/uniprot/Q925E1 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ Gamma-1-syntrophin|||In isoform 2.|||PDZ|||PH ^@ http://purl.uniprot.org/annotation/PRO_0000184014|||http://purl.uniprot.org/annotation/VSP_006361|||http://purl.uniprot.org/annotation/VSP_006362 http://togogenome.org/gene/10090:Afap1 ^@ http://purl.uniprot.org/uniprot/Q80YS6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Actin filament-associated protein 1|||Disordered|||Interaction with F-actin|||N-acetylmethionine|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH2-binding 1|||SH2-binding 2|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000317659 http://togogenome.org/gene/10090:Ash2l ^@ http://purl.uniprot.org/uniprot/E9PU93|||http://purl.uniprot.org/uniprot/Q3UJ62|||http://purl.uniprot.org/uniprot/Q3UKZ9|||http://purl.uniprot.org/uniprot/Q91X20 ^@ 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 ^@ Asymmetric dimethylarginine; by PRMT1 and PRMT5|||B30.2/SPRY|||Basic and acidic residues|||C4-type|||DNA-binding|||Disordered|||Interaction with RBBP5|||PHD-type; atypical|||Phosphoserine|||Polar residues|||Set1/Ash2 histone methyltransferase complex subunit ASH2 ^@ http://purl.uniprot.org/annotation/PRO_0000064698 http://togogenome.org/gene/10090:Gm10471 ^@ http://purl.uniprot.org/uniprot/E9Q1C7 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Churc1 ^@ http://purl.uniprot.org/uniprot/Q6DG52 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Binding Site|||Chain|||Splice Variant ^@ In isoform 2.|||Protein Churchill ^@ http://purl.uniprot.org/annotation/PRO_0000089666|||http://purl.uniprot.org/annotation/VSP_013378|||http://purl.uniprot.org/annotation/VSP_013379 http://togogenome.org/gene/10090:Hmgb3 ^@ http://purl.uniprot.org/uniprot/O54879|||http://purl.uniprot.org/uniprot/Q544R9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Cysteine sulfonic acid (-SO3H)|||Cysteine sulfonic acid (-SO3H); alternate|||Disordered|||HMG box|||HMG box 1|||HMG box 2|||High mobility group protein B3|||In disulfide HMGB3; alternate|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000048540 http://togogenome.org/gene/10090:Stoml1 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1F1|||http://purl.uniprot.org/uniprot/Q8CI66 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Band 7|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type III membrane protein|||Phosphoserine|||SCP2|||Stomatin-like protein 1|||Tyrosine-type lysosomal sorting signal ^@ http://purl.uniprot.org/annotation/PRO_0000094030 http://togogenome.org/gene/10090:Rab23 ^@ http://purl.uniprot.org/uniprot/Q9D4I9 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Spem2 ^@ http://purl.uniprot.org/uniprot/Q8C5U4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Uncharacterized protein SPEM2 ^@ http://purl.uniprot.org/annotation/PRO_0000387570 http://togogenome.org/gene/10090:Uros ^@ http://purl.uniprot.org/uniprot/P51163|||http://purl.uniprot.org/uniprot/Q3TPL3|||http://purl.uniprot.org/uniprot/Q3UG55|||http://purl.uniprot.org/uniprot/Q3UKR3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Tetrapyrrole biosynthesis uroporphyrinogen III synthase|||Uroporphyrinogen-III synthase ^@ http://purl.uniprot.org/annotation/PRO_0000135252 http://togogenome.org/gene/10090:Gmeb2 ^@ http://purl.uniprot.org/uniprot/P58929 ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue ^@ 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_0000074093 http://togogenome.org/gene/10090:Sema4d ^@ http://purl.uniprot.org/uniprot/O09126 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Polar residues|||Sema|||Semaphorin-4D ^@ http://purl.uniprot.org/annotation/PRO_0000032328 http://togogenome.org/gene/10090:Socs7 ^@ http://purl.uniprot.org/uniprot/Q8VHQ2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Mediates interaction with SORBS3|||Pro residues|||SH2|||SOCS box|||Suppressor of cytokine signaling 7 ^@ http://purl.uniprot.org/annotation/PRO_0000181254 http://togogenome.org/gene/10090:Hba-x ^@ http://purl.uniprot.org/uniprot/P06467|||http://purl.uniprot.org/uniprot/Q78PA4 ^@ 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 ^@ Globin family profile|||Hemoglobin subunit zeta|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||distal binding residue|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000052852 http://togogenome.org/gene/10090:Mars2 ^@ http://purl.uniprot.org/uniprot/A2RT28|||http://purl.uniprot.org/uniprot/Q499X9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict|||Transit Peptide ^@ 'HIGH' region|||'KMSKS' region|||Methionine--tRNA ligase, mitochondrial|||Methionyl-tRNA synthetase anticodon-binding|||Methionyl/Leucyl tRNA synthetase|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000045494 http://togogenome.org/gene/10090:Vmn1r206 ^@ http://purl.uniprot.org/uniprot/Q8R277 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zdhhc24 ^@ http://purl.uniprot.org/uniprot/Q3TA22|||http://purl.uniprot.org/uniprot/Q6IR37 ^@ 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|||Extracellular|||Helical|||Probable palmitoyltransferase ZDHHC24|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000233711 http://togogenome.org/gene/10090:Dbp ^@ http://purl.uniprot.org/uniprot/Q3USN7|||http://purl.uniprot.org/uniprot/Q60925 ^@ 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 ^@ BZIP|||Basic motif|||D site-binding protein|||Disordered|||Leucine-zipper|||Phosphoserine|||Polar residues|||Pro residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076508 http://togogenome.org/gene/10090:Rdh14 ^@ http://purl.uniprot.org/uniprot/Q9ERI6 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Proton acceptor|||Retinol dehydrogenase 14 ^@ http://purl.uniprot.org/annotation/PRO_0000054771 http://togogenome.org/gene/10090:Gabpb1 ^@ http://purl.uniprot.org/uniprot/Q00420|||http://purl.uniprot.org/uniprot/Q3US22|||http://purl.uniprot.org/uniprot/Q3UT69 ^@ Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Turn ^@ Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Splice Variant|||Turn ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Decreased acetylation; when associated with R-340 and Lys-369.|||Decreased acetylation; when associated with R-69 and Lys-340.|||Decreased acetylation; when associated with R-69 and Lys-369.|||GA-binding protein subunit beta-1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylserine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000066994|||http://purl.uniprot.org/annotation/VSP_009333|||http://purl.uniprot.org/annotation/VSP_009334|||http://purl.uniprot.org/annotation/VSP_009335|||http://purl.uniprot.org/annotation/VSP_009336 http://togogenome.org/gene/10090:Cfd ^@ http://purl.uniprot.org/uniprot/B7ZNS9|||http://purl.uniprot.org/uniprot/P03953|||http://purl.uniprot.org/uniprot/Q3UP47 ^@ 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|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Activation peptide|||Charge relay system|||Complement factor D|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027562|||http://purl.uniprot.org/annotation/PRO_0000027563|||http://purl.uniprot.org/annotation/PRO_5014300200|||http://purl.uniprot.org/annotation/PRO_5014309214|||http://purl.uniprot.org/annotation/VSP_005382 http://togogenome.org/gene/10090:Brs3 ^@ http://purl.uniprot.org/uniprot/O54798 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||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_0000069198 http://togogenome.org/gene/10090:Dars2 ^@ http://purl.uniprot.org/uniprot/Q8BIP0 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Aspartate|||Aspartate--tRNA ligase, mitochondrial|||Mitochondrion|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000250737 http://togogenome.org/gene/10090:Ptpn20 ^@ http://purl.uniprot.org/uniprot/O55082 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 20 ^@ http://purl.uniprot.org/annotation/PRO_0000295756|||http://purl.uniprot.org/annotation/VSP_027074|||http://purl.uniprot.org/annotation/VSP_027075 http://togogenome.org/gene/10090:Crb1 ^@ http://purl.uniprot.org/uniprot/A0A7D6VMF7|||http://purl.uniprot.org/uniprot/A0A7D6VRP0|||http://purl.uniprot.org/uniprot/Q8VHS2 ^@ 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|||EGF-like|||EGF-like 10|||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 1; atypical|||EGF-like 2|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7|||EGF-like 8|||EGF-like 9|||Extracellular|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||N-linked (GlcNAc...) asparagine|||Protein crumbs homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000007501|||http://purl.uniprot.org/annotation/PRO_5027618876|||http://purl.uniprot.org/annotation/PRO_5027856461|||http://purl.uniprot.org/annotation/VSP_014730|||http://purl.uniprot.org/annotation/VSP_014731|||http://purl.uniprot.org/annotation/VSP_014732|||http://purl.uniprot.org/annotation/VSP_014733|||http://purl.uniprot.org/annotation/VSP_014734|||http://purl.uniprot.org/annotation/VSP_014735|||http://purl.uniprot.org/annotation/VSP_014736 http://togogenome.org/gene/10090:Vmn1r196 ^@ http://purl.uniprot.org/uniprot/Q5SVD5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Akap8 ^@ http://purl.uniprot.org/uniprot/Q059U9|||http://purl.uniprot.org/uniprot/Q9DBR0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ A-kinase anchor protein 8|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Bipartite nuclear localization signal|||C2H2 AKAP95-type|||C2H2 AKAP95-type 1|||C2H2 AKAP95-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with DDX5|||Interaction with DPY30|||Interaction with MCM2|||Involved in chromatin-binding|||Involved in condensin complex recruitment|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||RII-binding|||Required for interaction with MYCBP ^@ http://purl.uniprot.org/annotation/PRO_0000075382 http://togogenome.org/gene/10090:Kcns1 ^@ http://purl.uniprot.org/uniprot/O35173|||http://purl.uniprot.org/uniprot/Q3TY49 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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|||Ion transport|||Potassium channel tetramerisation-type BTB|||Potassium voltage-gated channel subfamily S member 1|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054082 http://togogenome.org/gene/10090:Tmem161a ^@ http://purl.uniprot.org/uniprot/Q8VCA6 ^@ 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.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 161A ^@ http://purl.uniprot.org/annotation/PRO_0000288085|||http://purl.uniprot.org/annotation/VSP_025643|||http://purl.uniprot.org/annotation/VSP_025644|||http://purl.uniprot.org/annotation/VSP_025645 http://togogenome.org/gene/10090:Btbd35f27 ^@ http://purl.uniprot.org/uniprot/Q5FWA1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Zfp60 ^@ http://purl.uniprot.org/uniprot/Q8K0D9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Cxcl1 ^@ http://purl.uniprot.org/uniprot/A2RTH0|||http://purl.uniprot.org/uniprot/P12850 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ C-X-C motif chemokine|||Chemokine interleukin-8-like|||Growth-regulated alpha protein|||KC(5-72) ^@ http://purl.uniprot.org/annotation/PRO_0000005053|||http://purl.uniprot.org/annotation/PRO_0000005054|||http://purl.uniprot.org/annotation/PRO_5014205106 http://togogenome.org/gene/10090:Sfn ^@ http://purl.uniprot.org/uniprot/O70456 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Chain|||Modified Residue|||Sequence Conflict|||Site ^@ 14-3-3 protein sigma|||Interaction with phosphoserine on interacting protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000058644 http://togogenome.org/gene/10090:Limd2 ^@ http://purl.uniprot.org/uniprot/Q8BGB5 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||LIM domain-containing protein 2|||LIM zinc-binding|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000251208 http://togogenome.org/gene/10090:Cyp4b1 ^@ http://purl.uniprot.org/uniprot/Q3TNA0|||http://purl.uniprot.org/uniprot/Q64462 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Cytochrome P450 4B1|||Helical|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000051820 http://togogenome.org/gene/10090:Arid3c ^@ http://purl.uniprot.org/uniprot/A6PWV5|||http://purl.uniprot.org/uniprot/B7ZP08 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ ARID|||AT-rich interactive domain-containing protein 3C|||Acidic residues|||Disordered|||Polar residues|||Pro residues|||REKLES ^@ http://purl.uniprot.org/annotation/PRO_0000333002 http://togogenome.org/gene/10090:Sycp2l ^@ http://purl.uniprot.org/uniprot/A0A0M3U1B0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Synaptonemal complex protein 2-like ^@ http://purl.uniprot.org/annotation/PRO_0000441742 http://togogenome.org/gene/10090:Tigd5 ^@ http://purl.uniprot.org/uniprot/Q499M4 ^@ 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 ^@ DDE-1|||Disordered|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||In isoform 2.|||Pro residues|||Tigger transposable element derived 5 ^@ http://purl.uniprot.org/annotation/PRO_0000416768|||http://purl.uniprot.org/annotation/VSP_042797 http://togogenome.org/gene/10090:Tut1 ^@ http://purl.uniprot.org/uniprot/Q8R3F9 ^@ 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.|||KA1; binds the bulging loops of U6 snRNA but is dispensable for terminal uridylyltransferase activity|||Matrin-type|||PAP-associated|||Phosphoserine|||Polar residues|||RRM|||Speckle targeted PIP5K1A-regulated poly(A) polymerase ^@ http://purl.uniprot.org/annotation/PRO_0000254187|||http://purl.uniprot.org/annotation/VSP_021201|||http://purl.uniprot.org/annotation/VSP_021202 http://togogenome.org/gene/10090:Kcna3 ^@ http://purl.uniprot.org/uniprot/P16390 ^@ Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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|||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_0000053978 http://togogenome.org/gene/10090:Vmn1r56 ^@ http://purl.uniprot.org/uniprot/Q9EPS9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Isl2 ^@ http://purl.uniprot.org/uniprot/Q0VAX2|||http://purl.uniprot.org/uniprot/Q9CXV0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||Disordered|||Homeobox|||Insulin gene enhancer protein ISL-2|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM-binding domain (LID)|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000075753 http://togogenome.org/gene/10090:Gnrh1 ^@ http://purl.uniprot.org/uniprot/P13562|||http://purl.uniprot.org/uniprot/Q3UTE9 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Signal Peptide|||Site ^@ Chain|||Modified Residue|||Peptide|||Signal Peptide|||Site ^@ Appears to be essential for biological activity|||Cleavage; by ACE|||Glycine amide|||Gonadoliberin-1|||Progonadoliberin|||Progonadoliberin-1|||Prolactin release-inhibiting factor 1|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000012404|||http://purl.uniprot.org/annotation/PRO_0000012405|||http://purl.uniprot.org/annotation/PRO_0000012406|||http://purl.uniprot.org/annotation/PRO_5010843499 http://togogenome.org/gene/10090:Dis3 ^@ http://purl.uniprot.org/uniprot/Q9CSH3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Exosome complex exonuclease RRP44|||N-acetylmethionine|||N6-acetyllysine|||PINc|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000314757 http://togogenome.org/gene/10090:Rtl5 ^@ http://purl.uniprot.org/uniprot/Q5DTT4|||http://purl.uniprot.org/uniprot/Q8C065 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||DUF4939|||Disordered|||Retrotransposon Gag-like protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000259630 http://togogenome.org/gene/10090:Ythdf3 ^@ http://purl.uniprot.org/uniprot/Q8BYK6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Removed|||YTH|||YTH domain-containing family protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000230992|||http://purl.uniprot.org/annotation/VSP_017833|||http://purl.uniprot.org/annotation/VSP_017834 http://togogenome.org/gene/10090:Fpr3 ^@ http://purl.uniprot.org/uniprot/O08790 ^@ 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|||Formyl peptide receptor-related sequence 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 ^@ http://purl.uniprot.org/annotation/PRO_0000069453 http://togogenome.org/gene/10090:Chrnb3 ^@ http://purl.uniprot.org/uniprot/Q3UZS0|||http://purl.uniprot.org/uniprot/Q8BMN3 ^@ 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|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit beta-3|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000384|||http://purl.uniprot.org/annotation/PRO_5015097518|||http://purl.uniprot.org/annotation/VSP_013775 http://togogenome.org/gene/10090:Crygc ^@ http://purl.uniprot.org/uniprot/A3RLD4|||http://purl.uniprot.org/uniprot/A3RLD5|||http://purl.uniprot.org/uniprot/Q61597 ^@ 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 ^@ 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 strain: CD-1.|||S-methylcysteine ^@ http://purl.uniprot.org/annotation/PRO_0000057597 http://togogenome.org/gene/10090:Nolc1 ^@ http://purl.uniprot.org/uniprot/A0A286YDA2|||http://purl.uniprot.org/uniprot/A0A286YDT3|||http://purl.uniprot.org/uniprot/E9Q5C9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 11 X 12 AA approximate repeats of an acidic serine cluster|||Abolished pyrophosphorylation.|||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|||Does not affect pyrophosphorylation.|||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 RPA194|||LisH|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nuclear localization signal|||Nucleolar and coiled-body phosphoprotein 1|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Polar residues|||Strongly reduced pyrophosphorylation. ^@ http://purl.uniprot.org/annotation/PRO_0000439641|||http://purl.uniprot.org/annotation/VSP_058892|||http://purl.uniprot.org/annotation/VSP_058893 http://togogenome.org/gene/10090:Acyp2 ^@ http://purl.uniprot.org/uniprot/P56375 ^@ 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 ^@ Acylphosphatase-2|||Acylphosphatase-like|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000158543 http://togogenome.org/gene/10090:Gpat4 ^@ http://purl.uniprot.org/uniprot/Q8K2C8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Glycerol-3-phosphate acyltransferase 4|||HXXXXD motif|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000024704 http://togogenome.org/gene/10090:Mmel1 ^@ http://purl.uniprot.org/uniprot/E9PVK7|||http://purl.uniprot.org/uniprot/Q9JLI3 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes formation the soluble form.|||Cleavage|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||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_0000248417|||http://purl.uniprot.org/annotation/PRO_0000248418|||http://purl.uniprot.org/annotation/VSP_020290|||http://purl.uniprot.org/annotation/VSP_020291 http://togogenome.org/gene/10090:Mtarc1 ^@ http://purl.uniprot.org/uniprot/Q9CW42 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||MOSC|||MOSC N-terminal region|||Mitochondrial amidoxime-reducing component 1|||Mitochondrial matrix|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000273336 http://togogenome.org/gene/10090:Pate3 ^@ http://purl.uniprot.org/uniprot/B3GLJ3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Prostate and testis expressed protein 3|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000354973 http://togogenome.org/gene/10090:Ldhal6b ^@ http://purl.uniprot.org/uniprot/Q8BVP2 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent ^@ Lactate/malate dehydrogenase C-terminal|||Lactate/malate dehydrogenase N-terminal|||Proton acceptor ^@ http://togogenome.org/gene/10090:Tle2 ^@ http://purl.uniprot.org/uniprot/Q3UN01|||http://purl.uniprot.org/uniprot/Q5DTI7|||http://purl.uniprot.org/uniprot/Q9WVB2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat ^@ Basic and acidic residues|||CcN domain|||Disordered|||GP domain|||Groucho/TLE N-terminal Q-rich|||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_0000051279 http://togogenome.org/gene/10090:Mt4 ^@ http://purl.uniprot.org/uniprot/P47945|||http://purl.uniprot.org/uniprot/Q3V2E2 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Metallothionein-4 ^@ http://purl.uniprot.org/annotation/PRO_0000197256 http://togogenome.org/gene/10090:Plvap ^@ http://purl.uniprot.org/uniprot/G3X924|||http://purl.uniprot.org/uniprot/Q91VC4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Plasmalemma vesicle-associated protein|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000058463 http://togogenome.org/gene/10090:Tspan9 ^@ http://purl.uniprot.org/uniprot/Q8BJU2 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-9 ^@ http://purl.uniprot.org/annotation/PRO_0000219254 http://togogenome.org/gene/10090:Sec22c ^@ http://purl.uniprot.org/uniprot/Q8BXT9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Longin|||Lumenal|||Vesicle-trafficking protein SEC22c ^@ http://purl.uniprot.org/annotation/PRO_0000324162 http://togogenome.org/gene/10090:Ciao1 ^@ http://purl.uniprot.org/uniprot/Q99KN2 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Motif|||Repeat|||Sequence Conflict ^@ 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_0000281106 http://togogenome.org/gene/10090:Lce1m ^@ http://purl.uniprot.org/uniprot/Q9CR91 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Axl ^@ http://purl.uniprot.org/uniprot/Q00993|||http://purl.uniprot.org/uniprot/Q6PE80|||http://purl.uniprot.org/uniprot/Q8CCF8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Interaction with GAS6|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase receptor UFO|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000024482|||http://purl.uniprot.org/annotation/PRO_5004304411|||http://purl.uniprot.org/annotation/PRO_5015098433 http://togogenome.org/gene/10090:Gipr ^@ http://purl.uniprot.org/uniprot/Q0P543 ^@ 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 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Gastric inhibitory polypeptide receptor|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000306251|||http://purl.uniprot.org/annotation/VSP_028433|||http://purl.uniprot.org/annotation/VSP_028434 http://togogenome.org/gene/10090:Slc1a5 ^@ http://purl.uniprot.org/uniprot/Q3UFR4|||http://purl.uniprot.org/uniprot/Q9ESU7 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Ube2h ^@ http://purl.uniprot.org/uniprot/E9Q3U1|||http://purl.uniprot.org/uniprot/P62257|||http://purl.uniprot.org/uniprot/Q3TTE3|||http://purl.uniprot.org/uniprot/Q3V2N4 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Glycyl thioester intermediate|||N6-acetyllysine|||UBC core|||Ubiquitin-conjugating enzyme E2 H ^@ http://purl.uniprot.org/annotation/PRO_0000082487 http://togogenome.org/gene/10090:Anxa5 ^@ http://purl.uniprot.org/uniprot/P48036 ^@ Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Repeat|||Sequence Conflict ^@ 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_0000067488 http://togogenome.org/gene/10090:Spag5 ^@ http://purl.uniprot.org/uniprot/Q7TME2 ^@ 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|||Interaction with KNSTRN|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Polar residues|||Sperm-associated antigen 5 ^@ http://purl.uniprot.org/annotation/PRO_0000072094 http://togogenome.org/gene/10090:Tmem60 ^@ http://purl.uniprot.org/uniprot/Q8K174 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 60 ^@ http://purl.uniprot.org/annotation/PRO_0000072582 http://togogenome.org/gene/10090:Mier2 ^@ http://purl.uniprot.org/uniprot/Q3U3N0 ^@ 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|||ELM2|||In isoform 2 and isoform 3.|||In isoform 3.|||Mesoderm induction early response protein 2|||Phosphoserine|||Polar residues|||SANT ^@ http://purl.uniprot.org/annotation/PRO_0000313679|||http://purl.uniprot.org/annotation/VSP_030096|||http://purl.uniprot.org/annotation/VSP_030097|||http://purl.uniprot.org/annotation/VSP_030098 http://togogenome.org/gene/10090:Snx2 ^@ http://purl.uniprot.org/uniprot/Q9CWK8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ BAR|||Disordered|||Interaction with RhoG|||Membrane-binding amphipathic helix|||N6-acetyllysine|||PX|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sorting nexin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000213839 http://togogenome.org/gene/10090:Pmp22 ^@ http://purl.uniprot.org/uniprot/P16646|||http://purl.uniprot.org/uniprot/Q5SXS3 ^@ 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 tr-J.|||In tr.|||N-linked (GlcNAc...) asparagine|||Peripheral myelin protein 22 ^@ http://purl.uniprot.org/annotation/PRO_0000164651 http://togogenome.org/gene/10090:Kcne4 ^@ http://purl.uniprot.org/uniprot/Q9WTW3 ^@ 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|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Potassium voltage-gated channel subfamily E member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000144293 http://togogenome.org/gene/10090:Or52z12 ^@ http://purl.uniprot.org/uniprot/Q8VGA1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp518b ^@ http://purl.uniprot.org/uniprot/J3QPN0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Defb47 ^@ http://purl.uniprot.org/uniprot/Q30KN1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015097370 http://togogenome.org/gene/10090:Rem2 ^@ http://purl.uniprot.org/uniprot/E9Q4D5|||http://purl.uniprot.org/uniprot/Q8VEL9 ^@ 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 ^@ Disordered|||GTP-binding protein REM 2|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000122484|||http://purl.uniprot.org/annotation/VSP_038749 http://togogenome.org/gene/10090:Enkd1 ^@ http://purl.uniprot.org/uniprot/Q7TSV9 ^@ 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|||Enkurin|||Enkurin domain-containing protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000265932 http://togogenome.org/gene/10090:Emcn ^@ http://purl.uniprot.org/uniprot/Q9R0H2 ^@ Chain|||Compositionally Biased Region|||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|||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.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000019291|||http://purl.uniprot.org/annotation/VSP_010827|||http://purl.uniprot.org/annotation/VSP_010828|||http://purl.uniprot.org/annotation/VSP_010829 http://togogenome.org/gene/10090:Brpf1 ^@ http://purl.uniprot.org/uniprot/A0A0N4SUS4|||http://purl.uniprot.org/uniprot/A0A0N4SUT9|||http://purl.uniprot.org/uniprot/A0A0N4SVG7|||http://purl.uniprot.org/uniprot/B2RRD7|||http://purl.uniprot.org/uniprot/E9PXP1|||http://purl.uniprot.org/uniprot/Q3U109|||http://purl.uniprot.org/uniprot/Q80XK2|||http://purl.uniprot.org/uniprot/Q8C905|||http://purl.uniprot.org/uniprot/Q9CTY1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||Bromo|||C2H2-type|||C2HC pre-PHD-type|||Disordered|||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_0000439813 http://togogenome.org/gene/10090:Tead2 ^@ http://purl.uniprot.org/uniprot/P48301|||http://purl.uniprot.org/uniprot/Q3UPV9|||http://purl.uniprot.org/uniprot/Q80UL2 ^@ 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 ^@ Disordered|||Pro residues|||TEA|||Transcriptional activation|||Transcriptional enhancer factor TEF-4 ^@ http://purl.uniprot.org/annotation/PRO_0000205933 http://togogenome.org/gene/10090:Lime1 ^@ http://purl.uniprot.org/uniprot/Q9EQR5 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Abolishes LCK, PIK3R1 and LYN binding; when associated with F-261.|||Abolishes palmitoylation and lipid raft localization; when associated with S-28.|||Abolishes palmitoylation and lipid raft localization; when associated with S-31.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||Interaction with CSK|||Interaction with GRB2|||Interaction with LCK and PIK3R1|||Interaction with LCK, PLCG2 and PIK3R1|||Lck-interacting transmembrane adapter 1|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by LYN or LCK|||Reduces GRB2 binding.|||S-palmitoyl cysteine|||Strongly reduces PLCG2 binding. Abolishes LCK, PIK3R1 and LYN binding; when associated with F-242. ^@ http://purl.uniprot.org/annotation/PRO_0000083333 http://togogenome.org/gene/10090:Ostc ^@ http://purl.uniprot.org/uniprot/Q78XF5 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Oligosaccharyltransferase complex subunit OSTC ^@ http://purl.uniprot.org/annotation/PRO_0000320603 http://togogenome.org/gene/10090:Oc90 ^@ http://purl.uniprot.org/uniprot/Q80ZM2|||http://purl.uniprot.org/uniprot/Q9Z0L3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Otoconin-90|||Phospholipase A2|||Phospholipase A2-like 1|||Phospholipase A2-like 2|||Phospholipase A2-like 3 ^@ http://purl.uniprot.org/annotation/PRO_0000022994|||http://purl.uniprot.org/annotation/PRO_5015020110|||http://purl.uniprot.org/annotation/VSP_004510|||http://purl.uniprot.org/annotation/VSP_004511|||http://purl.uniprot.org/annotation/VSP_004512|||http://purl.uniprot.org/annotation/VSP_004513|||http://purl.uniprot.org/annotation/VSP_004514|||http://purl.uniprot.org/annotation/VSP_004515 http://togogenome.org/gene/10090:Faf2 ^@ http://purl.uniprot.org/uniprot/Q3TDN2 ^@ 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 ^@ Basic and acidic residues|||Disordered|||FAS-associated factor 2|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Removed|||UBA|||UBX ^@ http://purl.uniprot.org/annotation/PRO_0000244065|||http://purl.uniprot.org/annotation/VSP_019504 http://togogenome.org/gene/10090:Ids ^@ http://purl.uniprot.org/uniprot/Q08890 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ 3-oxoalanine (Cys)|||Iduronate 2-sulfatase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000033431|||http://purl.uniprot.org/annotation/PRO_0000033432 http://togogenome.org/gene/10090:Esp3 ^@ http://purl.uniprot.org/uniprot/J3QN49 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Brk1 ^@ http://purl.uniprot.org/uniprot/Q91VR8 ^@ 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|||Protein BRICK1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000283647 http://togogenome.org/gene/10090:Ptprr ^@ http://purl.uniprot.org/uniprot/Q5U1U6|||http://purl.uniprot.org/uniprot/Q62132|||http://purl.uniprot.org/uniprot/Q8CEI8 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform Beta.|||In isoform Gamma.|||Loss of phosphatase activity.|||Loss of phosphorylation by PKA, constitutive MAPK binding.|||Mimics phosphorylation by PKA, prevents MAPK binding.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphoserine; by PKA|||Polar residues|||Receptor-type tyrosine-protein phosphatase R|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||protein-tyrosine-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000025460|||http://purl.uniprot.org/annotation/PRO_5004304029|||http://purl.uniprot.org/annotation/PRO_5014310138|||http://purl.uniprot.org/annotation/VSP_005159|||http://purl.uniprot.org/annotation/VSP_005160|||http://purl.uniprot.org/annotation/VSP_005161 http://togogenome.org/gene/10090:Naxd ^@ http://purl.uniprot.org/uniprot/J3QMM7|||http://purl.uniprot.org/uniprot/J3QN06|||http://purl.uniprot.org/uniprot/K3W4M4|||http://purl.uniprot.org/uniprot/Q9CZ42 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide|||Transmembrane ^@ ATP-dependent (S)-NAD(P)H-hydrate dehydratase|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||YjeF C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000337022|||http://purl.uniprot.org/annotation/VSP_033831|||http://purl.uniprot.org/annotation/VSP_033832 http://togogenome.org/gene/10090:Vmn1r160 ^@ http://purl.uniprot.org/uniprot/E9Q346 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Akr7a5 ^@ http://purl.uniprot.org/uniprot/Q8CG76 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Aflatoxin B1 aldehyde reductase member 2|||Disordered|||Lowers pKa of active site Tyr|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000070376 http://togogenome.org/gene/10090:Phf21b ^@ http://purl.uniprot.org/uniprot/Q8C966 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Zinc Finger ^@ Disordered|||PHD finger protein 21B|||PHD-type|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000226770 http://togogenome.org/gene/10090:Nutm1 ^@ http://purl.uniprot.org/uniprot/Q8BHP2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||N5-methylglutamine|||NUT family member 1|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000311395 http://togogenome.org/gene/10090:Ly6f ^@ http://purl.uniprot.org/uniprot/P35460 ^@ 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 glycine|||Lymphocyte antigen 6F|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036144|||http://purl.uniprot.org/annotation/PRO_0000036145 http://togogenome.org/gene/10090:Or2y14 ^@ http://purl.uniprot.org/uniprot/Q8VFA8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cgnl1 ^@ http://purl.uniprot.org/uniprot/Q6AW69 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Cingulin-like protein 1|||Disordered|||Head|||In isoform 3.|||In isoform 5.|||Phosphoserine|||Polar residues|||Tail|||ZIM ^@ http://purl.uniprot.org/annotation/PRO_0000312876|||http://purl.uniprot.org/annotation/VSP_061743|||http://purl.uniprot.org/annotation/VSP_061744 http://togogenome.org/gene/10090:Avpr1a ^@ http://purl.uniprot.org/uniprot/Q3U1H9|||http://purl.uniprot.org/uniprot/Q62463 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified 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_0000070200 http://togogenome.org/gene/10090:Grm4 ^@ http://purl.uniprot.org/uniprot/A0A140T8R6|||http://purl.uniprot.org/uniprot/G3XA00|||http://purl.uniprot.org/uniprot/Q68EF4 ^@ Binding Site|||Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||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.|||Metabotropic glutamate receptor 4|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000306852|||http://purl.uniprot.org/annotation/PRO_5007305333|||http://purl.uniprot.org/annotation/PRO_5015091858|||http://purl.uniprot.org/annotation/VSP_028517|||http://purl.uniprot.org/annotation/VSP_028518 http://togogenome.org/gene/10090:Zfp551 ^@ http://purl.uniprot.org/uniprot/B2RUI1 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Region|||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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 551 ^@ http://purl.uniprot.org/annotation/PRO_0000358931 http://togogenome.org/gene/10090:Ddx21 ^@ http://purl.uniprot.org/uniprot/Q6PCP0|||http://purl.uniprot.org/uniprot/Q9JIK5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict ^@ 1-1|||1-2|||1-3|||2-1|||2-2|||2-3|||3 X 37 AA tandem repeats|||3 X 5 AA repeats|||Basic and acidic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||N6-acetyllysine|||Nucleolar RNA helicase 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000055028 http://togogenome.org/gene/10090:Rps7 ^@ http://purl.uniprot.org/uniprot/P62082 ^@ 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|||N-acetylmethionine|||N6-acetyllysine; alternate|||Small ribosomal subunit protein eS7 ^@ http://purl.uniprot.org/annotation/PRO_0000174191 http://togogenome.org/gene/10090:D6Wsu163e ^@ http://purl.uniprot.org/uniprot/Q91YN0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Phosphoserine|||Protein C12orf4 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089843 http://togogenome.org/gene/10090:Odaph ^@ http://purl.uniprot.org/uniprot/J3QNT8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003777161 http://togogenome.org/gene/10090:H2ac20 ^@ http://purl.uniprot.org/uniprot/Q149V4|||http://purl.uniprot.org/uniprot/Q64523 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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 2-C|||Histone H2A/H2B/H3|||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|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000227512 http://togogenome.org/gene/10090:Islr ^@ http://purl.uniprot.org/uniprot/A0A146E664|||http://purl.uniprot.org/uniprot/Q6GU68 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide ^@ Ig-like|||Immunoglobulin superfamily containing leucine-rich repeat protein|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000312209|||http://purl.uniprot.org/annotation/PRO_5014247673 http://togogenome.org/gene/10090:Cacng7 ^@ http://purl.uniprot.org/uniprot/B9EJ14|||http://purl.uniprot.org/uniprot/P62956 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Transmembrane ^@ Helical|||Phosphoserine|||Voltage-dependent calcium channel gamma-7 subunit ^@ http://purl.uniprot.org/annotation/PRO_0000164688 http://togogenome.org/gene/10090:Ubr5 ^@ http://purl.uniprot.org/uniprot/A0A2I3BQS6|||http://purl.uniprot.org/uniprot/E9Q2H1|||http://purl.uniprot.org/uniprot/Q3TSI5|||http://purl.uniprot.org/uniprot/Q80TP3 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase UBR5|||E3 ubiquitin-protein ligase UBR5 ubiquitin-associated|||Glycyl thioester intermediate|||HECT|||N-acetylthreonine|||PABC|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Removed|||UBR-type ^@ http://purl.uniprot.org/annotation/PRO_0000086932 http://togogenome.org/gene/10090:Msr1 ^@ http://purl.uniprot.org/uniprot/P30204|||http://purl.uniprot.org/uniprot/Q8CED7 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Collagen-like|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform II.|||Macrophage scavenger receptor types I and II|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||SRCR|||Spacer ^@ http://purl.uniprot.org/annotation/PRO_0000181628|||http://purl.uniprot.org/annotation/VSP_006231|||http://purl.uniprot.org/annotation/VSP_006232 http://togogenome.org/gene/10090:Sh3bp5l ^@ http://purl.uniprot.org/uniprot/Q3TK15|||http://purl.uniprot.org/uniprot/Q99LH9 ^@ 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|||Phosphothreonine|||SH3 domain-binding protein 5-like ^@ http://purl.uniprot.org/annotation/PRO_0000317509 http://togogenome.org/gene/10090:Agap1 ^@ http://purl.uniprot.org/uniprot/A0A087WRF2|||http://purl.uniprot.org/uniprot/Q8BXK8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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|||N-acetylmethionine|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Small GTPase-like ^@ http://purl.uniprot.org/annotation/PRO_0000074219 http://togogenome.org/gene/10090:Fbxo43 ^@ http://purl.uniprot.org/uniprot/G3X9B2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||ZBR-type ^@ http://togogenome.org/gene/10090:Ppp1r37 ^@ http://purl.uniprot.org/uniprot/Q8BKR5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Acidic residues|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Phosphoserine|||Polar residues|||Pro residues|||Protein phosphatase 1 regulatory subunit 37 ^@ http://purl.uniprot.org/annotation/PRO_0000320940 http://togogenome.org/gene/10090:Rbm14 ^@ http://purl.uniprot.org/uniprot/Q8C2Q3 ^@ 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)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||RNA-binding protein 14|||RRM 1|||RRM 2|||TRBP-interacting domain; interaction with STIL ^@ http://purl.uniprot.org/annotation/PRO_0000081775|||http://purl.uniprot.org/annotation/VSP_015080 http://togogenome.org/gene/10090:Polg ^@ http://purl.uniprot.org/uniprot/Q3UG70|||http://purl.uniprot.org/uniprot/Q3UZX3|||http://purl.uniprot.org/uniprot/Q75WC0 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ DNA-directed DNA polymerase family A palm|||Disordered ^@ http://togogenome.org/gene/10090:Prss44 ^@ http://purl.uniprot.org/uniprot/Q402U7 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Charge relay system|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 44 ^@ http://purl.uniprot.org/annotation/PRO_0000413699|||http://purl.uniprot.org/annotation/VSP_041974|||http://purl.uniprot.org/annotation/VSP_041975 http://togogenome.org/gene/10090:Lrrcc1 ^@ http://purl.uniprot.org/uniprot/A0A9L6HJP5|||http://purl.uniprot.org/uniprot/E9QNC6|||http://purl.uniprot.org/uniprot/G5E8Y2|||http://purl.uniprot.org/uniprot/Q69ZB0 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||Leucine-rich repeat and coiled-coil domain-containing protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000337082|||http://purl.uniprot.org/annotation/VSP_033869|||http://purl.uniprot.org/annotation/VSP_033870|||http://purl.uniprot.org/annotation/VSP_033871 http://togogenome.org/gene/10090:Gm15056 ^@ http://purl.uniprot.org/uniprot/E9Q8Z3|||http://purl.uniprot.org/uniprot/F6ZR08 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5008953732|||http://purl.uniprot.org/annotation/PRO_5008956239 http://togogenome.org/gene/10090:Or5d16 ^@ http://purl.uniprot.org/uniprot/Q8VFR3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Irf8 ^@ http://purl.uniprot.org/uniprot/P23611|||http://purl.uniprot.org/uniprot/Q3UCV9|||http://purl.uniprot.org/uniprot/Q544J7 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent ^@ IRF tryptophan pentad repeat|||Interferon regulatory factor 8 ^@ http://purl.uniprot.org/annotation/PRO_0000154565 http://togogenome.org/gene/10090:Src ^@ http://purl.uniprot.org/uniprot/P05480 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||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|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Disordered|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||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_0000088142|||http://purl.uniprot.org/annotation/VSP_060883 http://togogenome.org/gene/10090:Rbm27 ^@ http://purl.uniprot.org/uniprot/Q5SFM8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||C3H1-type|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RNA-binding protein 27|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000273045|||http://purl.uniprot.org/annotation/VSP_022462|||http://purl.uniprot.org/annotation/VSP_022463 http://togogenome.org/gene/10090:Sycp1 ^@ http://purl.uniprot.org/uniprot/Q62209 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ DNA-binding|||Disordered|||Mediates head to head self-assembly of N-terminal ends|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Required for pH-induced assembly of C-terminal ends into antiparallel tetramers|||Synaptonemal complex protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072364 http://togogenome.org/gene/10090:Vps37d ^@ http://purl.uniprot.org/uniprot/Q810I0 ^@ 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.|||Pro residues|||VPS37 C-terminal|||Vacuolar protein sorting-associated protein 37D ^@ http://purl.uniprot.org/annotation/PRO_0000328928|||http://purl.uniprot.org/annotation/VSP_052739 http://togogenome.org/gene/10090:Zfp352 ^@ http://purl.uniprot.org/uniprot/A2AML7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Npy ^@ http://purl.uniprot.org/uniprot/P57774 ^@ Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ C-flanking peptide of NPY|||Cleavage; by FAP|||Disordered|||Neuropeptide Y|||Phosphothreonine|||Tyrosine amide ^@ http://purl.uniprot.org/annotation/PRO_0000025325|||http://purl.uniprot.org/annotation/PRO_0000025326 http://togogenome.org/gene/10090:Or6f1 ^@ http://purl.uniprot.org/uniprot/Q8VFP2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Afap1l1 ^@ http://purl.uniprot.org/uniprot/B2RSM5|||http://purl.uniprot.org/uniprot/Q8BZI0 ^@ 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 ^@ Actin filament-associated protein 1-like 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295240|||http://purl.uniprot.org/annotation/VSP_026860|||http://purl.uniprot.org/annotation/VSP_026861 http://togogenome.org/gene/10090:Ugt2b37 ^@ http://purl.uniprot.org/uniprot/Q8VCN3 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||UDP-glucuronosyltransferase ^@ http://purl.uniprot.org/annotation/PRO_5015020132 http://togogenome.org/gene/10090:Vmn1r216 ^@ http://purl.uniprot.org/uniprot/Q8R257 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Eva1c ^@ http://purl.uniprot.org/uniprot/A0A338P750|||http://purl.uniprot.org/uniprot/P58659|||http://purl.uniprot.org/uniprot/Q8CAX0 ^@ 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|||EVA1|||EVA1 domain-containing protein|||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_0000017672|||http://purl.uniprot.org/annotation/PRO_5004307379|||http://purl.uniprot.org/annotation/VSP_026600|||http://purl.uniprot.org/annotation/VSP_026601 http://togogenome.org/gene/10090:Gnaq ^@ http://purl.uniprot.org/uniprot/P21279 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ 5-glutamyl histamine|||Abolishes palmitoylation.|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(q) subunit alpha|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000203761 http://togogenome.org/gene/10090:Notch3 ^@ http://purl.uniprot.org/uniprot/Q61982 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ 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|||LNR 1|||LNR 2|||LNR 3|||N-linked (GlcNAc...) asparagine|||Neurogenic locus notch homolog protein 3|||No effect on NICD processing.|||Notch 3 extracellular truncation|||Notch 3 intracellular domain|||Omega-N-methylarginine|||PEST-like|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000007695|||http://purl.uniprot.org/annotation/PRO_0000007696|||http://purl.uniprot.org/annotation/PRO_0000007697 http://togogenome.org/gene/10090:Capg ^@ http://purl.uniprot.org/uniprot/Q3TNN6|||http://purl.uniprot.org/uniprot/Q99LB4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Gelsolin-like ^@ http://togogenome.org/gene/10090:Ndfip1 ^@ http://purl.uniprot.org/uniprot/Q8R0W6 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Abolishes interaction with NEDD4.|||Alters interaction with NEDD4.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with ITCH|||Interaction with UBE2L3|||N-acetylalanine|||NEDD4 family-interacting protein 1|||PPxY motif 1|||PPxY motif 2|||PPxY motif 3|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000076270 http://togogenome.org/gene/10090:Hes6 ^@ http://purl.uniprot.org/uniprot/Q9JHE6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Basic and acidic residues|||Disordered|||Orange|||Transcription cofactor HES-6|||WRPW motif|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127215 http://togogenome.org/gene/10090:Zic4 ^@ http://purl.uniprot.org/uniprot/G3UYE7|||http://purl.uniprot.org/uniprot/Q61467|||http://purl.uniprot.org/uniprot/Q8C8J4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ C2H2-type|||C2H2-type 1; atypical|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Polar residues|||Zinc finger protein ZIC 4 ^@ http://purl.uniprot.org/annotation/PRO_0000047254 http://togogenome.org/gene/10090:1700029F12Rik ^@ http://purl.uniprot.org/uniprot/Q810S0|||http://purl.uniprot.org/uniprot/Q9CRB4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Or5w14 ^@ http://purl.uniprot.org/uniprot/Q7TR40 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ctdp1 ^@ http://purl.uniprot.org/uniprot/Q7TSG2 ^@ 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 ^@ Acidic residues|||BRCT|||Basic and acidic residues|||Disordered|||FCP1 homology|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||RNA polymerase II subunit A C-terminal domain phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000212565|||http://purl.uniprot.org/annotation/VSP_009866|||http://purl.uniprot.org/annotation/VSP_009867 http://togogenome.org/gene/10090:Sv2b ^@ http://purl.uniprot.org/uniprot/Q8BG39 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Synaptic vesicle glycoprotein 2B ^@ http://purl.uniprot.org/annotation/PRO_0000239769 http://togogenome.org/gene/10090:Khk ^@ http://purl.uniprot.org/uniprot/A0A0J9YU79|||http://purl.uniprot.org/uniprot/A0A0J9YUK6|||http://purl.uniprot.org/uniprot/E9Q1Q9|||http://purl.uniprot.org/uniprot/P97328 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Sequence Conflict|||Strand|||Turn ^@ Carbohydrate kinase PfkB|||Ketohexokinase ^@ http://purl.uniprot.org/annotation/PRO_0000080089 http://togogenome.org/gene/10090:Hexim1 ^@ http://purl.uniprot.org/uniprot/Q8R409 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ 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|||Mediates interaction with CCNT1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein HEXIM1|||Required for inhibition of ESR1-dependent transcription ^@ http://purl.uniprot.org/annotation/PRO_0000305264 http://togogenome.org/gene/10090:Clock ^@ http://purl.uniprot.org/uniprot/A0A0J9YU61|||http://purl.uniprot.org/uniprot/O08785|||http://purl.uniprot.org/uniprot/Q6ZQD6|||http://purl.uniprot.org/uniprot/Q8C9W6 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Strand|||Turn ^@ BHLH|||Circadian locomoter output cycles protein kaput|||Decrease in sumoylation and its transcriptional activity. Abolishes sumoylation and interaction with ESR1 and decrease in its transcriptional activity; when associated with R-67.|||Decrease in sumoylation and its transcriptional activity. Abolishes sumoylation and interaction with ESR1 and decrease in its transcriptional activity; when associated with R-851.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Implicated in the circadian rhythmicity|||Important for interaction with BMAL1|||In isoform Short.|||Interaction with E-box DNA|||Interaction with NR3C1|||Interaction with SIRT1|||Nuclear localization signal|||PAC|||PAS|||PAS 1|||PAS 2|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphothreonine; by CDK5|||Polar residues|||Reduced BMAL1 binding. Abolishes transcriptional activation by the CLOCK-BMAL1 heterodimer.|||Reduced BMAL1 binding. Abolishes transcriptional activation by the CLOCK-BMAL1 heterodimer. Abolishes regulation of circadian clock.|||Reduced BMAL1 binding. Slightly reduced transcriptional activation by the CLOCK-BMAL1 heterodimer.|||Reduces histone acetyltransferase activity; when associated with A-656 and A-658.|||Reduces histone acetyltransferase activity; when associated with A-656 and A-659.|||Reduces histone acetyltransferase activity; when associated with A-658 and A-659.|||Reduces histone acetyltransferase activity; when associated with A-669 and A-670.|||Reduces histone acetyltransferase activity; when associated with A-669 and A-672.|||Reduces histone acetyltransferase activity; when associated with A-670 and A-672.|||Significant decrease in transcriptional activation by the CLOCK-BMAL1 heterodimer. Significant decrease in transcriptional activation by the CLOCK-BMAL1 heterodimer, reduced nuclear localization and DNA-binding; when associated with D-38.|||Significant decrease in transcriptional activation by the CLOCK-BMAL1 heterodimer. Significant decrease in transcriptional activation by the CLOCK-BMAL1 heterodimer, reduced nuclear localization and DNA-binding; when associated with D-42.|||Significant loss of phosphorylation.|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127164|||http://purl.uniprot.org/annotation/VSP_002103 http://togogenome.org/gene/10090:Sdc2 ^@ http://purl.uniprot.org/uniprot/P43407 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cleavage of ectodomain|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||O-linked (Xyl...) (glycosaminoglycan) serine|||Phosphoserine|||Polar residues|||Syndecan-2 ^@ http://purl.uniprot.org/annotation/PRO_0000033504 http://togogenome.org/gene/10090:Adam12 ^@ http://purl.uniprot.org/uniprot/Q61824 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 12|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphotyrosine; by SRC|||SH3-binding; class I|||SH3-binding; class II|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029080|||http://purl.uniprot.org/annotation/PRO_0000029081 http://togogenome.org/gene/10090:Ankrd6 ^@ http://purl.uniprot.org/uniprot/Q69ZU8 ^@ 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|||ANK 6|||ANK 7|||ANK 8|||Ankyrin repeat domain-containing protein 6|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000320066|||http://purl.uniprot.org/annotation/VSP_031592 http://togogenome.org/gene/10090:Zp1 ^@ http://purl.uniprot.org/uniprot/Q059L1|||http://purl.uniprot.org/uniprot/Q62005 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||P-type|||Processed zona pellucida sperm-binding protein 1|||Pyrrolidone carboxylic acid|||Removed in mature form|||ZP|||Zona pellucida sperm-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000041679|||http://purl.uniprot.org/annotation/PRO_0000041680|||http://purl.uniprot.org/annotation/PRO_0000304554|||http://purl.uniprot.org/annotation/PRO_5014306679 http://togogenome.org/gene/10090:Smim22 ^@ http://purl.uniprot.org/uniprot/J3QP37|||http://purl.uniprot.org/uniprot/V9GXA9 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Paxx ^@ http://purl.uniprot.org/uniprot/Q8K0Y7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Disordered|||Mediates interaction with XRCC5/Ku80 and XRCC6/Ku70 and association with the non-homologous end joining core complex|||PISA|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein PAXX|||XLM ^@ http://purl.uniprot.org/annotation/PRO_0000286105 http://togogenome.org/gene/10090:Matk ^@ http://purl.uniprot.org/uniprot/A0A0R4J1N6|||http://purl.uniprot.org/uniprot/A0A0R4J1P8|||http://purl.uniprot.org/uniprot/D3Z4T5|||http://purl.uniprot.org/uniprot/P41242 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||Megakaryocyte-associated tyrosine-protein kinase|||Polar residues|||Protein kinase|||Proton acceptor|||SH2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000088074|||http://purl.uniprot.org/annotation/VSP_004966|||http://purl.uniprot.org/annotation/VSP_011565 http://togogenome.org/gene/10090:Rsph14 ^@ http://purl.uniprot.org/uniprot/E9PWZ8|||http://purl.uniprot.org/uniprot/Q9D3W1 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ ARM|||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_0000432959 http://togogenome.org/gene/10090:Fabp3 ^@ http://purl.uniprot.org/uniprot/P11404|||http://purl.uniprot.org/uniprot/Q5EBJ0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand ^@ Cytosolic fatty-acid binding proteins|||Fatty acid-binding protein, heart|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by Tyr-kinases|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067322 http://togogenome.org/gene/10090:Spatc1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0X4|||http://purl.uniprot.org/uniprot/Q148B6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes CDC20 binding.|||Abolishes CDC20 binding; when associated with Q-314.|||Abolishes CDC20 binding; when associated with R-302.|||Disordered|||In isoform 2.|||Necessary for targeting to centrosomes|||Polar residues|||Speriolin|||Speriolin C-terminal|||Speriolin N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000312301|||http://purl.uniprot.org/annotation/VSP_029818 http://togogenome.org/gene/10090:Eid3 ^@ http://purl.uniprot.org/uniprot/Q3V124 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||EP300-interacting inhibitor of differentiation 3 ^@ http://purl.uniprot.org/annotation/PRO_0000315907 http://togogenome.org/gene/10090:Vtn ^@ http://purl.uniprot.org/uniprot/P29788 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Basic residues|||Cell attachment site|||Disordered|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Heparin-binding|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||SMB|||Sulfotyrosine|||Vitronectin ^@ http://purl.uniprot.org/annotation/PRO_0000036398 http://togogenome.org/gene/10090:Crtac1 ^@ http://purl.uniprot.org/uniprot/Q8R555 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Cartilage acidic protein 1|||EGF-like|||FG-GAP 1; atypical|||FG-GAP 2; atypical|||FG-GAP 3; atypical|||FG-GAP 4; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000007498 http://togogenome.org/gene/10090:Pik3ap1 ^@ http://purl.uniprot.org/uniprot/Q9EQ32 ^@ 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 ^@ DBB|||Disordered|||Fails to bind PIK3R1 in a BCR-signaling dependent manner; when associated with Y-264; Y-420 and Y-445. Loss of regulatory function in Toll-like receptor signaling probably due to loss of interaction with PIK3R1; when associated with Y-264; Y-420 and Y-445. Impairs mature B-cell generation; when associated with Y-264; Y-420 and Y-445.|||Fails to bind PIK3R1 in a BCR-signaling dependent manner; when associated with Y-264; Y-420 and Y-460. Loss of regulatory function in Toll-like receptor signaling probably due to loss of interaction with PIK3R1; when associated with Y-264; Y-420 and Y-460. Impairs mature B-cell generation; when associated with Y-264; Y-420 and Y-460.|||Fails to bind PIK3R1 in a BCR-signaling dependent manner; when associated with Y-264; Y-445 and Y-460. Loss of regulatory function in Toll-like receptor signaling probably due to loss of interaction with PIK3R1; when associated with Y-264; Y-445 and Y-460. Impairs mature B-cell generation; when associated with Y-264; Y-445 and Y-460.|||Fails to bind PIK3R1 in a BCR-signaling dependent manner; when associated with Y-420; Y-445 and Y-460. Loss of regulatory function in Toll-like receptor signaling probably due to loss of interaction with PIK3R1; when associated with Y-420; Y-445 and Y-460. Impairs mature B-cell generation; when associated with Y-420; Y-445 and Y-460.|||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_0000341274|||http://purl.uniprot.org/annotation/VSP_034241|||http://purl.uniprot.org/annotation/VSP_034242|||http://purl.uniprot.org/annotation/VSP_034243 http://togogenome.org/gene/10090:Tas1r2 ^@ http://purl.uniprot.org/uniprot/Q925I4 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||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|||In strain: DBA/2J.|||N-linked (GlcNAc...) asparagine|||Taste receptor type 1 member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000012958 http://togogenome.org/gene/10090:Ralgapb ^@ http://purl.uniprot.org/uniprot/A2ACC6|||http://purl.uniprot.org/uniprot/E9Q0J2|||http://purl.uniprot.org/uniprot/F8WHN4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Rap-GAP ^@ http://togogenome.org/gene/10090:Myo1c ^@ http://purl.uniprot.org/uniprot/Q9WTI7 ^@ 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 ^@ Actin-binding|||IQ 1|||IQ 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inhibits binding to PIP2 and disrupts membrane binding.|||Myosin motor|||N-acetylmethionine|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||TH1|||Unconventional myosin-Ic ^@ http://purl.uniprot.org/annotation/PRO_0000123446|||http://purl.uniprot.org/annotation/VSP_003350|||http://purl.uniprot.org/annotation/VSP_036863|||http://purl.uniprot.org/annotation/VSP_036864 http://togogenome.org/gene/10090:Ankrd52 ^@ http://purl.uniprot.org/uniprot/Q8BTI7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ 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|||Phosphoserine|||Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C ^@ http://purl.uniprot.org/annotation/PRO_0000244588 http://togogenome.org/gene/10090:4933409G03Rik ^@ http://purl.uniprot.org/uniprot/Q8C5U0 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tor4a ^@ http://purl.uniprot.org/uniprot/Q8BH02 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Torsin-4A ^@ http://purl.uniprot.org/annotation/PRO_0000287490 http://togogenome.org/gene/10090:Lmf1 ^@ http://purl.uniprot.org/uniprot/Q3U3R4 ^@ 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.|||In isoform 3.|||In isoform 4.|||Lipase maturation factor 1|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000276740|||http://purl.uniprot.org/annotation/VSP_022973|||http://purl.uniprot.org/annotation/VSP_022974|||http://purl.uniprot.org/annotation/VSP_022975|||http://purl.uniprot.org/annotation/VSP_022976 http://togogenome.org/gene/10090:Or2q1 ^@ http://purl.uniprot.org/uniprot/Q8VF81 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cep131 ^@ http://purl.uniprot.org/uniprot/B1AXI9|||http://purl.uniprot.org/uniprot/Q62036 ^@ 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|||Centrosomal protein of 131 kDa|||Disordered|||IQ|||Interaction with PLK4|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Phosphoserine; by MAPKAPK2 and PLK4|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064782 http://togogenome.org/gene/10090:Zfp275 ^@ http://purl.uniprot.org/uniprot/A2AIE7|||http://purl.uniprot.org/uniprot/G3X904|||http://purl.uniprot.org/uniprot/Q3UQ14 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Efhd2 ^@ http://purl.uniprot.org/uniprot/Q8C845 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disordered|||EF-hand ^@ http://togogenome.org/gene/10090:Atxn7l3b ^@ http://purl.uniprot.org/uniprot/Q3UD01 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Ataxin-7-like protein 3B|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000392530 http://togogenome.org/gene/10090:Guca1a ^@ http://purl.uniprot.org/uniprot/P43081 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict ^@ Deamidated asparagine|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Guanylyl cyclase-activating protein 1|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073804 http://togogenome.org/gene/10090:Supt4b ^@ http://purl.uniprot.org/uniprot/Q9Z199 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Region|||Zinc Finger ^@ C4-type|||Interaction with SUPT5H|||Transcription elongation factor SPT4-B ^@ http://purl.uniprot.org/annotation/PRO_0000210328 http://togogenome.org/gene/10090:Or6c206 ^@ http://purl.uniprot.org/uniprot/Q7TRI3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:C4b ^@ http://purl.uniprot.org/uniprot/P01029|||http://purl.uniprot.org/uniprot/Q3TYN1 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Alpha-2-macroglobulin bait region|||Alpha-2-macroglobulin bait region domain-containing protein|||Anaphylatoxin-like|||C4a anaphylatoxin|||Complement C4 alpha chain|||Complement C4 beta chain|||Complement C4 gamma chain|||Isoglutamyl cysteine thioester (Cys-Gln)|||N-linked (GlcNAc...) asparagine|||NTR|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000005973|||http://purl.uniprot.org/annotation/PRO_0000005974|||http://purl.uniprot.org/annotation/PRO_0000005975|||http://purl.uniprot.org/annotation/PRO_0000005976|||http://purl.uniprot.org/annotation/PRO_0000005977|||http://purl.uniprot.org/annotation/PRO_0000005978|||http://purl.uniprot.org/annotation/PRO_5004229687 http://togogenome.org/gene/10090:Or4c15 ^@ http://purl.uniprot.org/uniprot/Q7TR09 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kcnip4 ^@ http://purl.uniprot.org/uniprot/Q3UFC0|||http://purl.uniprot.org/uniprot/Q3YAA5|||http://purl.uniprot.org/uniprot/Q3YAA6|||http://purl.uniprot.org/uniprot/Q3YAA7|||http://purl.uniprot.org/uniprot/Q3YAA8|||http://purl.uniprot.org/uniprot/Q6PHZ8 ^@ 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 ^@ Disordered|||EF-hand|||EF-hand 1; degenerate|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with KCND2|||KIS|||Kv channel-interacting protein 4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000073827|||http://purl.uniprot.org/annotation/VSP_015069|||http://purl.uniprot.org/annotation/VSP_015070|||http://purl.uniprot.org/annotation/VSP_015071 http://togogenome.org/gene/10090:Ell2 ^@ http://purl.uniprot.org/uniprot/Q3UKU1 ^@ 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|||OCEL|||Phosphoserine|||Polar residues|||RNA polymerase II elongation factor ELL2 ^@ http://purl.uniprot.org/annotation/PRO_0000322974 http://togogenome.org/gene/10090:Tlr1 ^@ http://purl.uniprot.org/uniprot/B9EJ46|||http://purl.uniprot.org/uniprot/Q9EPQ1 ^@ 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|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||TIR|||Toll-like receptor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000034706 http://togogenome.org/gene/10090:Amigo2 ^@ http://purl.uniprot.org/uniprot/Q4VBE6|||http://purl.uniprot.org/uniprot/Q80ZD9 ^@ 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|||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_0000014510|||http://purl.uniprot.org/annotation/PRO_5014309442 http://togogenome.org/gene/10090:Spo11 ^@ http://purl.uniprot.org/uniprot/Q9WTK8 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Splice Variant ^@ In isoform 2 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||Meiotic recombination protein SPO11|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000145475|||http://purl.uniprot.org/annotation/VSP_007197|||http://purl.uniprot.org/annotation/VSP_007198|||http://purl.uniprot.org/annotation/VSP_007199|||http://purl.uniprot.org/annotation/VSP_007200 http://togogenome.org/gene/10090:Plcb4 ^@ http://purl.uniprot.org/uniprot/Q91UZ1 ^@ Active Site|||Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||C2|||Disordered|||PI-PLC Y-box|||Polar residues ^@ http://togogenome.org/gene/10090:Rrnad1 ^@ http://purl.uniprot.org/uniprot/E9PUL0|||http://purl.uniprot.org/uniprot/Q8BZG5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Methyltransferase|||Methyltransferase-like protein 25B|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000289053|||http://purl.uniprot.org/annotation/VSP_025878|||http://purl.uniprot.org/annotation/VSP_025879|||http://purl.uniprot.org/annotation/VSP_025880 http://togogenome.org/gene/10090:Tmem253 ^@ http://purl.uniprot.org/uniprot/Q3UNB8 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 253 ^@ http://purl.uniprot.org/annotation/PRO_0000343723 http://togogenome.org/gene/10090:Mag ^@ http://purl.uniprot.org/uniprot/P20917|||http://purl.uniprot.org/uniprot/Q3ZB60 ^@ Binding Site|||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|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes C-linked mannosylation.|||Abolishes ganglioside binding.|||Abolishes homodimerization.|||Abolishes protection against axon degeneration.|||C-linked (Man) tryptophan|||Cytoplasmic|||Decreases ganglioside binding.|||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 isoform S-MAG.|||Increases homodimerization.|||Interaction with RTN4R and RTN4RL2|||Myelin-associated glycoprotein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Required for normal axon myelination in the central nervous system|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000014857|||http://purl.uniprot.org/annotation/PRO_5015097549|||http://purl.uniprot.org/annotation/VSP_002527|||http://purl.uniprot.org/annotation/VSP_002528 http://togogenome.org/gene/10090:Rragc ^@ http://purl.uniprot.org/uniprot/Q99K70 ^@ 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 ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Disordered|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Ras-related GTP-binding protein C|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000239952|||http://purl.uniprot.org/annotation/VSP_052076|||http://purl.uniprot.org/annotation/VSP_052077 http://togogenome.org/gene/10090:Gsta1 ^@ http://purl.uniprot.org/uniprot/P13745 ^@ 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 ^@ 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|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000185788|||http://purl.uniprot.org/annotation/PRO_0000423204 http://togogenome.org/gene/10090:Thoc3 ^@ http://purl.uniprot.org/uniprot/Q8VE80 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ 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_0000051274 http://togogenome.org/gene/10090:Ggct ^@ http://purl.uniprot.org/uniprot/Q9D7X8 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Gamma-glutamylcyclotransferase|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000089581 http://togogenome.org/gene/10090:Bicc1 ^@ http://purl.uniprot.org/uniprot/G3X8S6|||http://purl.uniprot.org/uniprot/Q99MQ1 ^@ 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.|||KH 1|||KH 2|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Protein bicaudal C homolog 1|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000267715|||http://purl.uniprot.org/annotation/VSP_021950|||http://purl.uniprot.org/annotation/VSP_021951 http://togogenome.org/gene/10090:Grb10 ^@ http://purl.uniprot.org/uniprot/Q60760 ^@ 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 ^@ Disordered|||Growth factor receptor-bound protein 10|||In isoform 2.|||In isoform 3.|||PH|||Phosphoserine|||Phosphoserine; by MTOR and PKB/AKT1|||Polar residues|||Pro residues|||Ras-associating|||SH2 ^@ http://purl.uniprot.org/annotation/PRO_0000150347|||http://purl.uniprot.org/annotation/VSP_001844|||http://purl.uniprot.org/annotation/VSP_012379 http://togogenome.org/gene/10090:Sh3pxd2a ^@ http://purl.uniprot.org/uniprot/O89032 ^@ 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 and isoform 3.|||In isoform 3.|||PX|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||SH3 5|||SH3 and PX domain-containing protein 2A ^@ http://purl.uniprot.org/annotation/PRO_0000278489|||http://purl.uniprot.org/annotation/VSP_023314|||http://purl.uniprot.org/annotation/VSP_023315 http://togogenome.org/gene/10090:Trim17 ^@ http://purl.uniprot.org/uniprot/Q7TPM3 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Zinc Finger ^@ B box-type|||B30.2/SPRY|||Complete loss of auto-ubiquitination.|||E3 ubiquitin-protein ligase TRIM17|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056225 http://togogenome.org/gene/10090:Pald1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J007|||http://purl.uniprot.org/uniprot/P70261 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-myristoyl glycine|||Paladin|||Phosphoserine|||Protein-tyrosine phosphatase catalytic|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000286131 http://togogenome.org/gene/10090:Katnal1 ^@ http://purl.uniprot.org/uniprot/Q8K0T4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region ^@ Basic and acidic residues|||Disordered|||Katanin p60 ATPase-containing subunit A-like 1|||Males are infertile and show a significant reduction in the number of spermatids in testis, due to premature exfoliation of spermatids from the seminiferous epithelium. Sertoli cells contain reduced numbers of stable microtubules. The protein localizes exclusively to the basal compartment of Sertoli cells.|||N-acetylmethionine|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000084602 http://togogenome.org/gene/10090:Rhno1 ^@ http://purl.uniprot.org/uniprot/E9Q1D4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ncaph ^@ http://purl.uniprot.org/uniprot/Q8C156 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Condensin complex subunit 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000095039 http://togogenome.org/gene/10090:Vmn2r41 ^@ http://purl.uniprot.org/uniprot/E9Q5C7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245742 http://togogenome.org/gene/10090:Vps37b ^@ http://purl.uniprot.org/uniprot/Q8R0J7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Interaction with IST1|||Pro residues|||VPS37 C-terminal|||Vacuolar protein sorting-associated protein 37B ^@ http://purl.uniprot.org/annotation/PRO_0000287201 http://togogenome.org/gene/10090:C1rl ^@ http://purl.uniprot.org/uniprot/Q3UZ09 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ CUB|||Charge relay system|||Complement C1r subcomponent-like protein|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_0000318679 http://togogenome.org/gene/10090:Slc17a2 ^@ http://purl.uniprot.org/uniprot/Q5SZA1 ^@ 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|||Sodium-dependent phosphate transport protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000250387|||http://purl.uniprot.org/annotation/VSP_020639 http://togogenome.org/gene/10090:Dennd1c ^@ http://purl.uniprot.org/uniprot/Q8CFK6 ^@ 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|||Clathrin box|||DENN domain-containing protein 1C|||Disordered|||FXDXF motif|||In isoform 2.|||Phosphoserine|||Polar residues|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000304677|||http://purl.uniprot.org/annotation/VSP_028091|||http://purl.uniprot.org/annotation/VSP_028092 http://togogenome.org/gene/10090:Mrpl51 ^@ http://purl.uniprot.org/uniprot/Q9CPY1 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein mL51|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000273083 http://togogenome.org/gene/10090:Clec1b ^@ http://purl.uniprot.org/uniprot/Q9JL99 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-type lectin|||C-type lectin domain family 1 member B|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000280044|||http://purl.uniprot.org/annotation/VSP_023516 http://togogenome.org/gene/10090:Dnaja4 ^@ http://purl.uniprot.org/uniprot/Q9JMC3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Repeat|||Zinc Finger ^@ Basic and acidic residues|||CR-type|||CXXCXGXG motif|||Cysteine methyl ester|||Disordered|||DnaJ homolog subfamily A member 4|||J|||Phosphoserine|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000071015|||http://purl.uniprot.org/annotation/PRO_0000396761 http://togogenome.org/gene/10090:Zfp938 ^@ http://purl.uniprot.org/uniprot/E9Q9G3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Il5ra ^@ http://purl.uniprot.org/uniprot/P21183|||http://purl.uniprot.org/uniprot/Q05A81 ^@ 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|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Interleukin-5 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010894|||http://purl.uniprot.org/annotation/PRO_5014306680 http://togogenome.org/gene/10090:Mff ^@ http://purl.uniprot.org/uniprot/Q6PCP5 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Mitochondrial fission factor|||Mitochondrial intermembrane|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000289185|||http://purl.uniprot.org/annotation/VSP_025959|||http://purl.uniprot.org/annotation/VSP_025960|||http://purl.uniprot.org/annotation/VSP_025961 http://togogenome.org/gene/10090:Or6z3 ^@ http://purl.uniprot.org/uniprot/Q8VGH5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp973 ^@ http://purl.uniprot.org/uniprot/A2BE20 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Paics ^@ http://purl.uniprot.org/uniprot/Q9DCL9 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ AIR carboxylase domain|||Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase|||Linker|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||SAICAR synthetase domain ^@ http://purl.uniprot.org/annotation/PRO_0000075031 http://togogenome.org/gene/10090:Rab3b ^@ http://purl.uniprot.org/uniprot/Q9CZT8 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif ^@ Cysteine methyl ester|||Effector region|||N-acetylalanine|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-3B|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121082 http://togogenome.org/gene/10090:Gm4884 ^@ http://purl.uniprot.org/uniprot/E9PVP9|||http://purl.uniprot.org/uniprot/Q8CDP2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF4629|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tatdn2 ^@ http://purl.uniprot.org/uniprot/B7ZNL9|||http://purl.uniprot.org/uniprot/F8VQE6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Myocd ^@ http://purl.uniprot.org/uniprot/Q8VIM5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Activation of ANF promoter abolished, no effect on SM22 promoter.|||Basic and acidic residues|||Disordered|||HDAC5-binding|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4 and isoform 5.|||MEF2C-binding|||Myocardin|||No effect on SRF activation. Impairs SRF activation, reduces interaction with EP300 and SM-promoter activation; when associated with D-812; D-859 and D-866.|||No effect on SRF activation. Impairs SRF activation, reduces interaction with EP300 and SM-promoter activation; when associated with D-812; D-859 and D-893.|||No effect on SRF activation. Impairs SRF activation, reduces interaction with EP300 and SM-promoter activation; when associated with D-812; D-866 and D-893.|||No effect on SRF activation. Impairs SRF activation, reduces interaction with EP300 and SM-promoter activation; when associated with D-859; D-866 and D-893.|||No effect on SRF activation. No effect on SRF activation, on interaction with EP300 and on SM-promoter activation; when associated with A-859; A-866 and A-893.|||No effect on SRF activation; No effect on SRF activation, on interaction with EP300 and on SM-promoter activation; when associated with A-812; A-859 and A-893.|||No effect on SRF activation; No effect on SRF activation, on interaction with EP300 and on SM-specific genes transcription; when associated with A-812; A-859 and A-866.|||No effect on SRF activation; No effect on SRF activation. No effect on SRF activation, on interaction with EP300 and on SM-promoter activation; when associated with A-812, A-866 and A-893.|||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_0000126632|||http://purl.uniprot.org/annotation/VSP_007662|||http://purl.uniprot.org/annotation/VSP_007663|||http://purl.uniprot.org/annotation/VSP_041684 http://togogenome.org/gene/10090:Tmtc3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J173|||http://purl.uniprot.org/uniprot/G5E8C4|||http://purl.uniprot.org/uniprot/Q8BRH0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||DUF1736|||Disordered|||Helical|||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_0000280294|||http://purl.uniprot.org/annotation/VSP_023620|||http://purl.uniprot.org/annotation/VSP_023621 http://togogenome.org/gene/10090:Capn8 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0K6|||http://purl.uniprot.org/uniprot/Q91VA3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Calpain catalytic|||Calpain-8|||Domain III|||Domain IV|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||Linker|||Loss of activity. ^@ http://purl.uniprot.org/annotation/PRO_0000349281|||http://purl.uniprot.org/annotation/VSP_035306|||http://purl.uniprot.org/annotation/VSP_035307 http://togogenome.org/gene/10090:Rhox1 ^@ http://purl.uniprot.org/uniprot/B1APN4|||http://purl.uniprot.org/uniprot/Q4TU92 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent ^@ Homeobox ^@ http://togogenome.org/gene/10090:Ngf ^@ http://purl.uniprot.org/uniprot/P01139|||http://purl.uniprot.org/uniprot/Q6LDU8 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Abolishes production of the mature chain and promotes apoptosis of superior cervical ganglion neurons; when associated with 49-A-A-50 and 120-A-A-121.|||Abolishes production of the mature chain and promotes apoptosis of superior cervical ganglion neurons; when associated with 49-A-A-50 and 79-A-A-80.|||Abolishes production of the mature chain and promotes apoptosis of superior cervical ganglion neurons; when associated with 79-A-A-80 and 120-A-A-121.|||Beta-nerve growth factor|||N-linked (GlcNAc...) asparagine|||Near loss of the ability to trigger histamine release from mast cells. No effect on interaction with NTRK1.|||Nerve growth factor-related|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000019601|||http://purl.uniprot.org/annotation/PRO_0000019602 http://togogenome.org/gene/10090:Epcam ^@ http://purl.uniprot.org/uniprot/Q99JW5 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Epithelial cell adhesion molecule|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000380183 http://togogenome.org/gene/10090:Kcns2 ^@ http://purl.uniprot.org/uniprot/O35174|||http://purl.uniprot.org/uniprot/Q69ZQ8 ^@ Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||INTRAMEM|||Motif|||Non-terminal Residue|||Region|||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|||Potassium voltage-gated channel subfamily S member 2|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054085 http://togogenome.org/gene/10090:Babam1 ^@ http://purl.uniprot.org/uniprot/Q3UI43 ^@ 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|||BRISC and BRCA1-A complex member 1|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||Phosphoserine|||VWFA-like ^@ http://purl.uniprot.org/annotation/PRO_0000288459 http://togogenome.org/gene/10090:Arhgap15 ^@ http://purl.uniprot.org/uniprot/B1AW40|||http://purl.uniprot.org/uniprot/B2X2D4|||http://purl.uniprot.org/uniprot/Q811M1 ^@ 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 ^@ In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Rho GTPase-activating protein 15|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000317575|||http://purl.uniprot.org/annotation/VSP_031048|||http://purl.uniprot.org/annotation/VSP_031049|||http://purl.uniprot.org/annotation/VSP_031050|||http://purl.uniprot.org/annotation/VSP_031051|||http://purl.uniprot.org/annotation/VSP_031052 http://togogenome.org/gene/10090:Zfp830 ^@ http://purl.uniprot.org/uniprot/Q8R1N0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type|||Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Zinc finger protein 830 ^@ http://purl.uniprot.org/annotation/PRO_0000076194 http://togogenome.org/gene/10090:Flywch2 ^@ http://purl.uniprot.org/uniprot/Q9CQE9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||FLYWCH family member 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000316525 http://togogenome.org/gene/10090:Prss40 ^@ http://purl.uniprot.org/uniprot/A6H6T1 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Disordered|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 40 ^@ http://purl.uniprot.org/annotation/PRO_0000344982 http://togogenome.org/gene/10090:Trim13 ^@ http://purl.uniprot.org/uniprot/Q3TSD2|||http://purl.uniprot.org/uniprot/Q9CYB0 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ B box-type|||E3 ubiquitin-protein ligase TRIM13|||Helical|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056029 http://togogenome.org/gene/10090:Ccdc38 ^@ http://purl.uniprot.org/uniprot/Q8CDN8 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Splice Variant ^@ Coiled-coil domain-containing protein 38|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000234492|||http://purl.uniprot.org/annotation/VSP_018331|||http://purl.uniprot.org/annotation/VSP_018332 http://togogenome.org/gene/10090:Vmn1r116 ^@ http://purl.uniprot.org/uniprot/L7N2A6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sdk1 ^@ http://purl.uniprot.org/uniprot/Q3UH53 ^@ 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|||Turn ^@ 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|||Turn ^@ Abolishes homophilic interactions.|||Basic and acidic residues|||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.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Protein sidekick-1 ^@ http://purl.uniprot.org/annotation/PRO_0000226976|||http://purl.uniprot.org/annotation/VSP_017520|||http://purl.uniprot.org/annotation/VSP_017521 http://togogenome.org/gene/10090:Map1lc3b ^@ http://purl.uniprot.org/uniprot/Q9CQV6 ^@ Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Chain|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Site|||Strand|||Turn ^@ Cleavage; by ATG4B|||Microtubule-associated proteins 1A/1B light chain 3B|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000017200|||http://purl.uniprot.org/annotation/PRO_0000017201 http://togogenome.org/gene/10090:AI429214 ^@ http://purl.uniprot.org/uniprot/Q3TTJ4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Uncharacterized protein C8orf48 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000285632 http://togogenome.org/gene/10090:Slc2a7 ^@ http://purl.uniprot.org/uniprot/B1ARZ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:Pfas ^@ http://purl.uniprot.org/uniprot/Q5SUR0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Glutamine amidotransferase type-1|||Nucleophile|||Phosphoribosylformylglycinamidine synthase|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000370848 http://togogenome.org/gene/10090:Nanos1 ^@ http://purl.uniprot.org/uniprot/Q80WY3 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ C2HC 1|||C2HC 2|||Disordered|||Essential for its translational repressor activity|||Nanos homolog 1|||Nanos-type ^@ http://purl.uniprot.org/annotation/PRO_0000207686 http://togogenome.org/gene/10090:Ttf1 ^@ http://purl.uniprot.org/uniprot/Q3TQG6|||http://purl.uniprot.org/uniprot/Q62187 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||May be involved in interaction with ARF|||May be involved in localization to the nucleolus and interaction with ARF|||Myb-like 1|||Myb-like 2|||N-terminal region (NRD)|||Phosphoserine|||Polar residues|||Transcription termination factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000250473 http://togogenome.org/gene/10090:Or2ag13 ^@ http://purl.uniprot.org/uniprot/Q8VFM3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:B2m ^@ http://purl.uniprot.org/uniprot/P01887 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide|||Strand|||Turn ^@ Beta-2-microglobulin|||Ig-like C1-type|||In allele A.|||In allele W2, W4 and W5.|||In allele W2.|||In allele W3.|||In allele W4. ^@ http://purl.uniprot.org/annotation/PRO_0000018784 http://togogenome.org/gene/10090:Slf2 ^@ http://purl.uniprot.org/uniprot/E9Q839 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Coiled-coil SMC6 And NSE5 INteracting (CANIN)|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Dpp3 ^@ http://purl.uniprot.org/uniprot/Q3UDF3|||http://purl.uniprot.org/uniprot/Q99KK7 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Dipeptidyl peptidase 3|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000078239 http://togogenome.org/gene/10090:Arhgap29 ^@ http://purl.uniprot.org/uniprot/Q8CGF1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||F-BAR|||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_0000317583|||http://purl.uniprot.org/annotation/VSP_031060 http://togogenome.org/gene/10090:Sult2a3 ^@ http://purl.uniprot.org/uniprot/D3Z1W5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Tagap1 ^@ http://purl.uniprot.org/uniprot/P0CAX8 ^@ 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|||T-cell activation GTPase-activating protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000379567 http://togogenome.org/gene/10090:Mccc2 ^@ http://purl.uniprot.org/uniprot/B2RUK5|||http://purl.uniprot.org/uniprot/Q3ULD5|||http://purl.uniprot.org/uniprot/Q6PD20 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Acyl-CoA binding|||Carboxyltransferase|||CoA carboxyltransferase C-terminal|||CoA carboxyltransferase N-terminal|||Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000284068 http://togogenome.org/gene/10090:H3f4 ^@ http://purl.uniprot.org/uniprot/A0A8I4SYN6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Histone H2A/H2B/H3 ^@ http://togogenome.org/gene/10090:Eci3 ^@ http://purl.uniprot.org/uniprot/Q78JN3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Site ^@ ACB|||Disordered|||Enoyl-CoA delta isomerase 3, peroxisomal|||Important for catalytic activity|||Microbody targeting signal ^@ http://purl.uniprot.org/annotation/PRO_0000435335 http://togogenome.org/gene/10090:Fbln2 ^@ http://purl.uniprot.org/uniprot/P37889|||http://purl.uniprot.org/uniprot/Q3TGL4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Anaphylatoxin-like|||Anaphylatoxin-like 1|||Anaphylatoxin-like 2|||Anaphylatoxin-like 3|||Cell attachment site|||Disordered|||Domain III|||EGF-like|||EGF-like 10; calcium-binding|||EGF-like 11; 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|||Polar residues|||Subdomain NA (Cys-rich)|||Subdomain NB (Cys-free) ^@ http://purl.uniprot.org/annotation/PRO_0000007569|||http://purl.uniprot.org/annotation/PRO_5015097447|||http://purl.uniprot.org/annotation/VSP_001391 http://togogenome.org/gene/10090:Psmg3 ^@ http://purl.uniprot.org/uniprot/Q9CZH3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ N-acetylmethionine|||Proteasome assembly chaperone 3 ^@ http://purl.uniprot.org/annotation/PRO_0000271359 http://togogenome.org/gene/10090:Mrps10 ^@ http://purl.uniprot.org/uniprot/E9QJS0|||http://purl.uniprot.org/uniprot/G5E8U5|||http://purl.uniprot.org/uniprot/G5E8U8|||http://purl.uniprot.org/uniprot/Q501J4 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Polar residues|||Small ribosomal subunit protein uS10 ^@ http://togogenome.org/gene/10090:Ubap2 ^@ http://purl.uniprot.org/uniprot/Q91VX2 ^@ 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|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||UBA|||Ubiquitin-associated protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000270982 http://togogenome.org/gene/10090:Ppif ^@ http://purl.uniprot.org/uniprot/Q99KR7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ 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_0000025490 http://togogenome.org/gene/10090:Itih5 ^@ http://purl.uniprot.org/uniprot/Q8BJD1 ^@ 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 ^@ Disordered|||Inter-alpha-trypsin inhibitor heavy chain H5|||N-linked (GlcNAc...) asparagine|||VIT|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000331409 http://togogenome.org/gene/10090:Hsd17b7 ^@ http://purl.uniprot.org/uniprot/O88736 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000054587 http://togogenome.org/gene/10090:Npr1 ^@ http://purl.uniprot.org/uniprot/P18293|||http://purl.uniprot.org/uniprot/Q2TAY4|||http://purl.uniprot.org/uniprot/Q3UY30 ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Atrial natriuretic peptide receptor 1|||Cytoplasmic|||Extracellular|||Guanylate cyclase|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000012361|||http://purl.uniprot.org/annotation/PRO_5014308780 http://togogenome.org/gene/10090:Ccsap ^@ http://purl.uniprot.org/uniprot/Q8QZT2 ^@ 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|||Centriole, cilia and spindle-associated protein|||Disordered|||N-acetylmethionine|||Phosphoserine|||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_0000284644 http://togogenome.org/gene/10090:Gm6592 ^@ http://purl.uniprot.org/uniprot/A2AHC7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB-related ^@ http://togogenome.org/gene/10090:Rps27rt ^@ http://purl.uniprot.org/uniprot/Q6ZWU9 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Modified Residue|||Region|||Zinc Finger ^@ C4-type|||Disordered|||Phosphoserine|||Small ribosomal subunit protein eS27 ^@ http://purl.uniprot.org/annotation/PRO_0000149052 http://togogenome.org/gene/10090:Xkr7 ^@ http://purl.uniprot.org/uniprot/Q5GH64 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||XK-related protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000190789 http://togogenome.org/gene/10090:Cers5 ^@ http://purl.uniprot.org/uniprot/Q9D6K9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolished ceramide synthase activity.|||Basic and acidic residues|||Ceramide synthase 5|||Cytoplasmic|||Disordered|||Does not affect ceramide synthase activity.|||Helical|||Homeobox-like|||In isoform 2.|||Last loop motif|||Lumenal|||N-linked (GlcNAc...) asparagine|||TLC ^@ http://purl.uniprot.org/annotation/PRO_0000185515|||http://purl.uniprot.org/annotation/VSP_011192|||http://purl.uniprot.org/annotation/VSP_011193 http://togogenome.org/gene/10090:Pigr ^@ http://purl.uniprot.org/uniprot/O70570 ^@ 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 ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polymeric immunoglobulin receptor|||Secretory component ^@ http://purl.uniprot.org/annotation/PRO_0000014902|||http://purl.uniprot.org/annotation/PRO_0000014903 http://togogenome.org/gene/10090:Cdkn1a ^@ http://purl.uniprot.org/uniprot/P39689|||http://purl.uniprot.org/uniprot/Q564P6 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ C4-type|||Cyclin-dependent kinase inhibitor|||Cyclin-dependent kinase inhibitor 1|||Disordered|||Glycyl serine ester (Ser-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with TRIM39|||N-acetylserine|||PIP-box K+4 motif|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphoserine; by NUAK1|||Phosphothreonine; by PKA, PKB/AKT1, PIM1 and PIM2|||Removed|||Required for binding CDKs|||Required for binding cyclins ^@ http://purl.uniprot.org/annotation/PRO_0000190080 http://togogenome.org/gene/10090:Cracr2b ^@ http://purl.uniprot.org/uniprot/Q80ZJ8 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||EF-hand 1|||EF-hand 2|||EF-hand calcium-binding domain-containing protein 4A|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000283045 http://togogenome.org/gene/10090:Nlgn2 ^@ http://purl.uniprot.org/uniprot/Q69ZK9|||http://purl.uniprot.org/uniprot/Q6PHN2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||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|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Carboxylesterase type B|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neuroligin-2|||Phosphoserine|||Pro residues|||Reduced presynaptic differentiation.|||Required for interaction with LHFPL4 ^@ http://purl.uniprot.org/annotation/PRO_0000041879 http://togogenome.org/gene/10090:Hsf4 ^@ http://purl.uniprot.org/uniprot/B2RQY2|||http://purl.uniprot.org/uniprot/Q3UG93|||http://purl.uniprot.org/uniprot/Q9R0L1 ^@ 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 SUMO)|||HSF-type DNA-binding|||Heat shock factor protein 4|||Hydrophobic repeat HR-A/B|||Hydrophobic repeat HR-C|||In isoform HSF4A.|||Interactions with DUSP26, MAPK1 and MAPK2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000124572|||http://purl.uniprot.org/annotation/VSP_002419 http://togogenome.org/gene/10090:Mettl8 ^@ http://purl.uniprot.org/uniprot/A2AUU0 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Crosslink|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Mitochondrion|||tRNA N(3)-methylcytidine methyltransferase METTL8, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000311292|||http://purl.uniprot.org/annotation/VSP_029515|||http://purl.uniprot.org/annotation/VSP_029516|||http://purl.uniprot.org/annotation/VSP_029517|||http://purl.uniprot.org/annotation/VSP_029518|||http://purl.uniprot.org/annotation/VSP_037111 http://togogenome.org/gene/10090:Calr ^@ http://purl.uniprot.org/uniprot/B2MWM9|||http://purl.uniprot.org/uniprot/P14211 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||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|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||P-domain|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000004174|||http://purl.uniprot.org/annotation/PRO_5014205209 http://togogenome.org/gene/10090:Pcdhgb5 ^@ http://purl.uniprot.org/uniprot/Q91XX5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099514 http://togogenome.org/gene/10090:Ero1b ^@ http://purl.uniprot.org/uniprot/Q8R2E9 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Signal Peptide ^@ Alternate|||Complete loss of disulfide oxidase activity in vitro.|||ERO1-like protein beta|||N-linked (GlcNAc...) asparagine|||Redox-active|||Redox-active; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000008419 http://togogenome.org/gene/10090:Thsd1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0U4|||http://purl.uniprot.org/uniprot/A0A1B0GT60|||http://purl.uniprot.org/uniprot/G3XA27|||http://purl.uniprot.org/uniprot/Q9JM61 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TSP type-1|||Thrombospondin type-1 domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000249585|||http://purl.uniprot.org/annotation/PRO_5015044294|||http://purl.uniprot.org/annotation/PRO_5015091870 http://togogenome.org/gene/10090:Cfl1 ^@ http://purl.uniprot.org/uniprot/P18760|||http://purl.uniprot.org/uniprot/Q544Y7 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site ^@ ADF-H|||Cofilin-1|||Decreases abundance and increases disorganization of zygotic subcortical F-actin, disrupts centralization of the mitotic spindle and leads to asymmetric two-cell embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||N6-acetyllysine|||No effect on zygotic subcortical F-actin abundance and centralization of the mitotic spindle.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000214900 http://togogenome.org/gene/10090:Atp5pb ^@ http://purl.uniprot.org/uniprot/Q9CQQ7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ ATP synthase F(0) complex subunit B1, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000002514 http://togogenome.org/gene/10090:Ktn1 ^@ http://purl.uniprot.org/uniprot/A0A087WNW3|||http://purl.uniprot.org/uniprot/A0A087WP14|||http://purl.uniprot.org/uniprot/A0A087WP48|||http://purl.uniprot.org/uniprot/A0A087WP85|||http://purl.uniprot.org/uniprot/A0A087WPW5|||http://purl.uniprot.org/uniprot/A0A087WPX0|||http://purl.uniprot.org/uniprot/A0A087WQ25|||http://purl.uniprot.org/uniprot/A0A087WQD0|||http://purl.uniprot.org/uniprot/A0A087WQF8|||http://purl.uniprot.org/uniprot/A0A087WQG4|||http://purl.uniprot.org/uniprot/A0A087WQI3|||http://purl.uniprot.org/uniprot/A0A087WQQ5|||http://purl.uniprot.org/uniprot/A0A087WRS1|||http://purl.uniprot.org/uniprot/A0A087WS04|||http://purl.uniprot.org/uniprot/A0A087WS23|||http://purl.uniprot.org/uniprot/A0A087WS29|||http://purl.uniprot.org/uniprot/F8VQC7|||http://purl.uniprot.org/uniprot/Q61595 ^@ Chain|||Coiled-Coil|||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|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 10, isoform 12 and isoform 16.|||In isoform 2, isoform 3, isoform 4, isoform 7, isoform 8, isoform 10, isoform 11, isoform 12, isoform 13, isoform 14 and isoform 16.|||In isoform 2, isoform 3, isoform 5, isoform 6, isoform 9, isoform 13, isoform 14 and isoform 16.|||In isoform 2, isoform 3, isoform 7, isoform 8, isoform 9, isoform 12, isoform 14 and isoform 15.|||In isoform 2, isoform 4, isoform 6, isoform 8, isoform 9, isoform 12, isoform 13, isoform 14, isoform 15 and isoform 16.|||Kinectin|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Ribosome receptor lysine/proline rich ^@ http://purl.uniprot.org/annotation/PRO_0000238620|||http://purl.uniprot.org/annotation/VSP_052042|||http://purl.uniprot.org/annotation/VSP_052043|||http://purl.uniprot.org/annotation/VSP_052044|||http://purl.uniprot.org/annotation/VSP_052045|||http://purl.uniprot.org/annotation/VSP_052046 http://togogenome.org/gene/10090:Gdpd5 ^@ http://purl.uniprot.org/uniprot/A0A1L1STK0|||http://purl.uniprot.org/uniprot/Q640M6 ^@ 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|||GP-PDE|||Glycerophosphodiester phosphodiesterase domain-containing protein 5|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000251942 http://togogenome.org/gene/10090:Or2y10 ^@ http://purl.uniprot.org/uniprot/Q7TQT5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Stfa2 ^@ http://purl.uniprot.org/uniprot/P35174 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Motif|||Sequence Conflict|||Site|||Splice Variant ^@ In isoform 2.|||Reactive site|||Secondary area of contact|||Stefin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000207147|||http://purl.uniprot.org/annotation/VSP_044325 http://togogenome.org/gene/10090:Prnp ^@ http://purl.uniprot.org/uniprot/P04925|||http://purl.uniprot.org/uniprot/Q3UG89|||http://purl.uniprot.org/uniprot/Q4FJQ7 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||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|||Modified Residue|||Mutagenesis Site|||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|||Disordered|||GPI-anchor amidated serine|||Helical|||Hydroxyproline|||Interaction with ADGRG6|||Interaction with GRB2, ERI3 and SYN1|||Linked to long incubation time.|||Linked to long incubation time; requires 2 nucleotide substitutions.|||Major prion protein|||N-linked (GlcNAc...) asparagine|||No effect on interaction with GRB2.|||Prion/Doppel protein beta-ribbon|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000025697|||http://purl.uniprot.org/annotation/PRO_0000025698|||http://purl.uniprot.org/annotation/PRO_5004230118|||http://purl.uniprot.org/annotation/PRO_5014309351 http://togogenome.org/gene/10090:Tespa1 ^@ http://purl.uniprot.org/uniprot/Q3U132 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Protein TESPA1 ^@ http://purl.uniprot.org/annotation/PRO_0000315220|||http://purl.uniprot.org/annotation/VSP_030490|||http://purl.uniprot.org/annotation/VSP_030491|||http://purl.uniprot.org/annotation/VSP_030492 http://togogenome.org/gene/10090:Mfn1 ^@ http://purl.uniprot.org/uniprot/Q811U4 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Helical; Name=1|||Helical; Name=2|||Mitochondrial intermembrane|||Mitofusin-1|||Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regions ^@ http://purl.uniprot.org/annotation/PRO_0000127673 http://togogenome.org/gene/10090:Rpl7a ^@ http://purl.uniprot.org/uniprot/P12970|||http://purl.uniprot.org/uniprot/Q58ET1 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||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|||Ribosomal protein eL8/eL30/eS12/Gadd45 ^@ http://purl.uniprot.org/annotation/PRO_0000136748 http://togogenome.org/gene/10090:Fam205c ^@ http://purl.uniprot.org/uniprot/Q80YD3 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein SPATA31F3 ^@ http://purl.uniprot.org/annotation/PRO_0000319053|||http://purl.uniprot.org/annotation/VSP_031342 http://togogenome.org/gene/10090:Ccdc153 ^@ http://purl.uniprot.org/uniprot/P0C7Q1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic residues|||Coiled-coil domain-containing protein 153|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000342651 http://togogenome.org/gene/10090:Mdm4 ^@ http://purl.uniprot.org/uniprot/O35618|||http://purl.uniprot.org/uniprot/Q3UTC9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ DM2|||Disordered|||In isoform Short.|||Necessary for interaction with USP2|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CHEK1 and CHEK2|||Phosphoserine; by CHEK2|||Protein Mdm4|||RING-type|||RanBP2-type|||Region II|||SWIB/MDM2 ^@ http://purl.uniprot.org/annotation/PRO_0000157337|||http://purl.uniprot.org/annotation/VSP_003216|||http://purl.uniprot.org/annotation/VSP_003217 http://togogenome.org/gene/10090:Prr15 ^@ http://purl.uniprot.org/uniprot/A2RT92|||http://purl.uniprot.org/uniprot/Q9D1T5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Proline-rich protein 15 ^@ http://purl.uniprot.org/annotation/PRO_0000271110 http://togogenome.org/gene/10090:Ddx50 ^@ http://purl.uniprot.org/uniprot/Q99MJ9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region ^@ 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_0000055055 http://togogenome.org/gene/10090:Castor2 ^@ http://purl.uniprot.org/uniprot/Q8CAB8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ ACT 1|||ACT 2|||Cytosolic arginine sensor for mTORC1 subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000325893 http://togogenome.org/gene/10090:Numa1 ^@ http://purl.uniprot.org/uniprot/E9Q7G0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 4.1-binding domain|||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)|||Membrane-binding domain 1|||Membrane-binding domain 2|||N6-acetyllysine|||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|||Phosphotyrosine|||Polar residues|||Tail (Globular)|||Tankyrase-binding domain|||Tubulin-binding domain ^@ http://purl.uniprot.org/annotation/PRO_0000440879 http://togogenome.org/gene/10090:Wdr33 ^@ http://purl.uniprot.org/uniprot/A0A3Q4EGD8|||http://purl.uniprot.org/uniprot/Q8K1G7|||http://purl.uniprot.org/uniprot/Q8K4P0|||http://purl.uniprot.org/uniprot/Q9D1P6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Transmembrane ^@ Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Collagen-like|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||Pro residues|||Removed|||WD|||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_0000415291 http://togogenome.org/gene/10090:E430018J23Rik ^@ http://purl.uniprot.org/uniprot/E9PZQ8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ints2 ^@ http://purl.uniprot.org/uniprot/Q3TPV8|||http://purl.uniprot.org/uniprot/Q80UK8 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Integrator complex subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000236100|||http://purl.uniprot.org/annotation/VSP_018574|||http://purl.uniprot.org/annotation/VSP_018575 http://togogenome.org/gene/10090:Ccdc54 ^@ http://purl.uniprot.org/uniprot/Q9DAL3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Coiled-coil domain-containing protein 54|||Disordered|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000286670 http://togogenome.org/gene/10090:Eloa ^@ http://purl.uniprot.org/uniprot/Q8CB77 ^@ 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 ^@ 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_0000086961 http://togogenome.org/gene/10090:Pnmt ^@ http://purl.uniprot.org/uniprot/P40935|||http://purl.uniprot.org/uniprot/Q0VB50 ^@ Binding Site|||Chain|||Initiator Methionine|||Molecule Processing|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Region|||Repeat ^@ 1|||2|||2 X 7 AA repeats of G-S-D-[LP]-K-H-A|||Disordered|||Phenylethanolamine N-methyltransferase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000159710 http://togogenome.org/gene/10090:Aif1l ^@ http://purl.uniprot.org/uniprot/Q9EQX4 ^@ 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|||Region|||Sequence Conflict ^@ Allograft inflammatory factor 1-like|||Disordered|||EF-hand 1|||EF-hand 2; degenerate|||N-acetylserine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073871 http://togogenome.org/gene/10090:Colec11 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0M6|||http://purl.uniprot.org/uniprot/A0A1Y7VKG6|||http://purl.uniprot.org/uniprot/Q3SXB8 ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ C-type lectin|||Collagen-like|||Collectin-11|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000315045|||http://purl.uniprot.org/annotation/PRO_5011004920|||http://purl.uniprot.org/annotation/PRO_5039970673|||http://purl.uniprot.org/annotation/VSP_030472 http://togogenome.org/gene/10090:Ace ^@ http://purl.uniprot.org/uniprot/P09470|||http://purl.uniprot.org/uniprot/Q3TU20 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolished dipeptidyl carboxypeptidase activity. Knockin mice expressed in a knockout background display defects in male fertility. They however show normal blood pressure and kidney morphology.|||Abolishes peptidase activity but no effect on GPIase activity.|||Abolishes peptidase activity but no effect on GPIase activity; when associated with K-993.|||Abolishes peptidase activity but no effect on GPIase activity; when associated with K-997.|||Angiotensin-converting enzyme|||Angiotensin-converting enzyme, soluble form|||Cytoplasmic|||Extracellular|||Helical|||In ACE(7/7) mutant; knockin mice have normal blood pressure, renal function, and hematocrit. Knockin mice show normal plasma levels of angiotensin II but an elevation of plasma and urine peptide N-acetyl-SDKP (AcSDKP).|||In isoform Testis-specific.|||Juxtamembrane stalk|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Peptidase M2 1|||Peptidase M2 2|||Phosphoserine|||Proton acceptor 1|||Proton acceptor 2|||Proton donor 1|||Proton donor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000028539|||http://purl.uniprot.org/annotation/PRO_0000028540|||http://purl.uniprot.org/annotation/PRO_5014309162|||http://purl.uniprot.org/annotation/VSP_037638|||http://purl.uniprot.org/annotation/VSP_037639 http://togogenome.org/gene/10090:Hnrnpa2b1 ^@ http://purl.uniprot.org/uniprot/O88569 ^@ 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 ^@ Asymmetric dimethylarginine; alternate|||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 ribonucleoproteins A2/B1|||In isoform 2 and isoform 3.|||In isoform 3.|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000081837|||http://purl.uniprot.org/annotation/VSP_022595|||http://purl.uniprot.org/annotation/VSP_025012 http://togogenome.org/gene/10090:Zyg11a ^@ http://purl.uniprot.org/uniprot/A0A1Y7VNL1|||http://purl.uniprot.org/uniprot/A0A217FL76 ^@ Region|||Repeat ^@ Repeat ^@ ARM ^@ http://togogenome.org/gene/10090:Laptm5 ^@ http://purl.uniprot.org/uniprot/Q544S4|||http://purl.uniprot.org/uniprot/Q61168 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Lysosomal-associated transmembrane protein 5|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000084358 http://togogenome.org/gene/10090:Fmod ^@ http://purl.uniprot.org/uniprot/P50608|||http://purl.uniprot.org/uniprot/Q543D2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Repeat|||Signal Peptide ^@ Fibromodulin|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||LRRNT domain-containing protein|||N-linked (GlcNAc...) (keratan sulfate) asparagine|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000032740|||http://purl.uniprot.org/annotation/PRO_5014309545 http://togogenome.org/gene/10090:Srd5a2 ^@ http://purl.uniprot.org/uniprot/Q99N99 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ 3-oxo-5-alpha-steroid 4-dehydrogenase 2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000213678 http://togogenome.org/gene/10090:Mettl2 ^@ http://purl.uniprot.org/uniprot/Q8BMK1 ^@ 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.|||tRNA N(3)-methylcytidine methyltransferase METTL2 ^@ http://purl.uniprot.org/annotation/PRO_0000204453|||http://purl.uniprot.org/annotation/VSP_008479 http://togogenome.org/gene/10090:Klhl13 ^@ http://purl.uniprot.org/uniprot/Q80TF4 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Splice Variant ^@ BACK|||BTB|||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_0000119116|||http://purl.uniprot.org/annotation/VSP_037534|||http://purl.uniprot.org/annotation/VSP_037535|||http://purl.uniprot.org/annotation/VSP_037536|||http://purl.uniprot.org/annotation/VSP_037537 http://togogenome.org/gene/10090:Clic4 ^@ http://purl.uniprot.org/uniprot/Q543N5|||http://purl.uniprot.org/uniprot/Q9QYB1 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ 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_0000144211 http://togogenome.org/gene/10090:Satb1 ^@ http://purl.uniprot.org/uniprot/E9PVB7|||http://purl.uniprot.org/uniprot/Q60611 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ CUT|||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|||N6-acetyllysine|||Nuclear localization signal|||Nuclear matrix targeting sequence (NMTS)|||Phosphoserine|||Polar residues|||Pro residues|||Protein interaction|||ULD ^@ http://purl.uniprot.org/annotation/PRO_0000202399 http://togogenome.org/gene/10090:Rsl1d1 ^@ http://purl.uniprot.org/uniprot/Q8BVY0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ribosomal L1 domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000430629 http://togogenome.org/gene/10090:Cotl1 ^@ http://purl.uniprot.org/uniprot/Q544F6|||http://purl.uniprot.org/uniprot/Q9CQI6 ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn ^@ ADF-H|||Coactosin-like protein|||Flexible and important for F-actin binding|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000214955 http://togogenome.org/gene/10090:Gadl1 ^@ http://purl.uniprot.org/uniprot/A0A8Q0QWL6|||http://purl.uniprot.org/uniprot/Q80WP8 ^@ 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 ^@ Acidic amino acid decarboxylase GADL1|||In isoform 2.|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_0000312225|||http://purl.uniprot.org/annotation/VSP_029752 http://togogenome.org/gene/10090:Nemf ^@ http://purl.uniprot.org/uniprot/Q8CCP0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Induces an age-dependent neurodegenerative phenotype.|||Phosphoserine|||Phosphothreonine|||Ribosome quality control complex subunit NEMF ^@ http://purl.uniprot.org/annotation/PRO_0000097643|||http://purl.uniprot.org/annotation/VSP_008397|||http://purl.uniprot.org/annotation/VSP_008398|||http://purl.uniprot.org/annotation/VSP_010463|||http://purl.uniprot.org/annotation/VSP_010464|||http://purl.uniprot.org/annotation/VSP_010465|||http://purl.uniprot.org/annotation/VSP_010466 http://togogenome.org/gene/10090:Slc16a9 ^@ http://purl.uniprot.org/uniprot/Q7TM99 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Monocarboxylate transporter 9 ^@ http://purl.uniprot.org/annotation/PRO_0000289333 http://togogenome.org/gene/10090:Trit1 ^@ http://purl.uniprot.org/uniprot/Q80UN9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide|||Zinc Finger ^@ Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide|||Zinc Finger ^@ Core aggregation region|||Disordered|||In isoform 2.|||Interaction with isopentenylpyrophosphate transferase|||Interaction with substrate tRNA|||Matrin-type|||Mitochondrion|||Phosphoserine|||Reduced tRNA dimethylallyltransferase activity.|||tRNA dimethylallyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000019024|||http://purl.uniprot.org/annotation/VSP_010722 http://togogenome.org/gene/10090:Prr16 ^@ http://purl.uniprot.org/uniprot/A3KMN5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Polar residues|||Pro residues|||Protein Largen ^@ http://purl.uniprot.org/annotation/PRO_0000308160|||http://purl.uniprot.org/annotation/VSP_028882 http://togogenome.org/gene/10090:Hjv ^@ http://purl.uniprot.org/uniprot/Q7TQ32 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Cleavage; by autolysis|||Disordered|||GPI-anchor amidated aspartate|||Hemojuvelin|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Pro residues|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000030400|||http://purl.uniprot.org/annotation/PRO_0000030401|||http://purl.uniprot.org/annotation/VSP_011321 http://togogenome.org/gene/10090:Morf4l2 ^@ http://purl.uniprot.org/uniprot/Q9R0Q4 ^@ 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|||MRG|||Mortality factor 4-like protein 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000088769 http://togogenome.org/gene/10090:Spire2 ^@ http://purl.uniprot.org/uniprot/Q8K1S6 ^@ 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.|||KIND|||Phosphoserine|||Polar residues|||Protein spire homolog 2|||Spir-box|||WH2 1|||WH2 2|||WH2 3 ^@ http://purl.uniprot.org/annotation/PRO_0000320024|||http://purl.uniprot.org/annotation/VSP_031573 http://togogenome.org/gene/10090:Gm44504 ^@ http://purl.uniprot.org/uniprot/P21126|||http://purl.uniprot.org/uniprot/Q3UK94 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Required and sufficient for interaction with BAG6|||Ubiquitin-like|||Ubiquitin-like protein 4A ^@ http://purl.uniprot.org/annotation/PRO_0000114865 http://togogenome.org/gene/10090:Or8k41 ^@ http://purl.uniprot.org/uniprot/A0A1L1SR98 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cadm4 ^@ http://purl.uniprot.org/uniprot/Q8R464 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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_0000291981 http://togogenome.org/gene/10090:Htra2 ^@ http://purl.uniprot.org/uniprot/Q9JIY5 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site|||Transit Peptide|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Transit Peptide|||Transmembrane ^@ Charge relay system|||Helical|||IAP-binding motif|||Loss of interaction with XIAP.|||Loss of protease activity.|||Mitochondrion|||PDZ|||Serine protease|||Serine protease HTRA2, mitochondrial|||Stronger interaction with XIAP third BIR domain. ^@ http://purl.uniprot.org/annotation/PRO_0000026947|||http://purl.uniprot.org/annotation/PRO_0000026948 http://togogenome.org/gene/10090:Rnf40 ^@ http://purl.uniprot.org/uniprot/Q3U319 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase BRE1B|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055841 http://togogenome.org/gene/10090:Nr2f1 ^@ http://purl.uniprot.org/uniprot/B8JJI9|||http://purl.uniprot.org/uniprot/F7CII1|||http://purl.uniprot.org/uniprot/Q32NY6|||http://purl.uniprot.org/uniprot/Q60632 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ COUP transcription factor 1|||Disordered|||Important for dimerization|||NR C4-type|||NR LBD|||Nuclear receptor ^@ http://purl.uniprot.org/annotation/PRO_0000053603 http://togogenome.org/gene/10090:Zeb1 ^@ http://purl.uniprot.org/uniprot/Q64318 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; 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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger E-box-binding homeobox 1 ^@ http://purl.uniprot.org/annotation/PRO_0000047233 http://togogenome.org/gene/10090:Csnk1g1 ^@ http://purl.uniprot.org/uniprot/A0A0U1RNW0|||http://purl.uniprot.org/uniprot/A0A0U1RPD7|||http://purl.uniprot.org/uniprot/Q6P2B2|||http://purl.uniprot.org/uniprot/Q8BTH8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Casein kinase I isoform gamma-1|||Disordered|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000192840 http://togogenome.org/gene/10090:Eda2r ^@ http://purl.uniprot.org/uniprot/Q3KP88|||http://purl.uniprot.org/uniprot/Q8BX35 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||N-linked (GlcNAc...) asparagine|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 27 ^@ http://purl.uniprot.org/annotation/PRO_0000058939 http://togogenome.org/gene/10090:Bckdha ^@ http://purl.uniprot.org/uniprot/Q3U3J1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Dehydrogenase E1 component|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Nhej1 ^@ http://purl.uniprot.org/uniprot/Q3KNJ2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Basic residues|||Disordered|||Globular head|||In isoform 2.|||Leu-lock|||Non-homologous end-joining factor 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||XLM ^@ http://purl.uniprot.org/annotation/PRO_0000228655|||http://purl.uniprot.org/annotation/VSP_017690 http://togogenome.org/gene/10090:Nrros ^@ http://purl.uniprot.org/uniprot/Q8BMT4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes formation of disulfide bonds and ability to interact with TGFB1; when associated with A-219.|||Abolishes formation of disulfide bonds and ability to interact with TGFB1; when associated with A-363.|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||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_0000042661|||http://purl.uniprot.org/annotation/VSP_016019|||http://purl.uniprot.org/annotation/VSP_016020 http://togogenome.org/gene/10090:1700109H08Rik ^@ http://purl.uniprot.org/uniprot/Q9D9C0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ EF-hand ^@ http://togogenome.org/gene/10090:Il17re ^@ http://purl.uniprot.org/uniprot/Q8BH06 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interleukin-17 receptor E|||N-linked (GlcNAc...) asparagine|||Polar residues|||SEFIR ^@ http://purl.uniprot.org/annotation/PRO_0000309468|||http://purl.uniprot.org/annotation/VSP_029197|||http://purl.uniprot.org/annotation/VSP_029198|||http://purl.uniprot.org/annotation/VSP_029199|||http://purl.uniprot.org/annotation/VSP_029200 http://togogenome.org/gene/10090:Ndufs6 ^@ http://purl.uniprot.org/uniprot/P52503 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide ^@ Mitochondrion|||N6-acetyllysine|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000043171 http://togogenome.org/gene/10090:Krt36 ^@ http://purl.uniprot.org/uniprot/B1AQ75 ^@ 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 Ha6|||Linker 1|||Linker 12|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000363989 http://togogenome.org/gene/10090:Uggt1 ^@ http://purl.uniprot.org/uniprot/Q6P5E4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Glucosyltransferase|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Prevents secretion from ER|||UDP-glucose:glycoprotein glucosyltransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000012272 http://togogenome.org/gene/10090:Acsbg2 ^@ http://purl.uniprot.org/uniprot/Q2XU92 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Long-chain-fatty-acid--CoA ligase ACSBG2 ^@ http://purl.uniprot.org/annotation/PRO_0000315813 http://togogenome.org/gene/10090:Pde4d ^@ http://purl.uniprot.org/uniprot/A2RSH1|||http://purl.uniprot.org/uniprot/Q01063 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||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|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 3.|||In isoform 9.|||PDEase|||Phosphoserine|||Polar residues|||Proton donor|||cAMP-specific 3',5'-cyclic phosphodiesterase 4D ^@ http://purl.uniprot.org/annotation/PRO_0000198815|||http://purl.uniprot.org/annotation/VSP_012394|||http://purl.uniprot.org/annotation/VSP_012395|||http://purl.uniprot.org/annotation/VSP_012396|||http://purl.uniprot.org/annotation/VSP_012397 http://togogenome.org/gene/10090:Or5b104 ^@ http://purl.uniprot.org/uniprot/Q8VFK3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tex14 ^@ http://purl.uniprot.org/uniprot/Q7M6U3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||Abolishes interaction with CEP55.|||Basic and acidic residues|||D-box|||Disordered|||Does not affect interaction with CEP55.|||GPPX3Y|||In isoform 2.|||Inactive serine/threonine-protein kinase TEX14|||Mimicks phosphorylation state; inducing early depletion from kinetochores and subsequent degradation by the APC/C complex.|||Phosphoserine|||Phosphoserine; by PLK1|||Polar residues|||Prevents degradation during metaphase.|||Protein kinase|||Reduced phosphorylation by PLK1 and abolishes depletion from kinetochores and subsequent degradation by the APC/C complex. ^@ http://purl.uniprot.org/annotation/PRO_0000246996|||http://purl.uniprot.org/annotation/VSP_019870 http://togogenome.org/gene/10090:Lgals8 ^@ http://purl.uniprot.org/uniprot/A8DIL0|||http://purl.uniprot.org/uniprot/Q542M5|||http://purl.uniprot.org/uniprot/Q8C6H0|||http://purl.uniprot.org/uniprot/Q9JL15 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Site ^@ Critical for binding to sialylated and sulfated oligosaccharides|||Galectin|||Galectin 1|||Galectin 2|||Galectin-8 ^@ http://purl.uniprot.org/annotation/PRO_0000076944 http://togogenome.org/gene/10090:Or13p4 ^@ http://purl.uniprot.org/uniprot/Q8VFY3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Txndc5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Y7|||http://purl.uniprot.org/uniprot/E9PXX7|||http://purl.uniprot.org/uniprot/Q3TEE8|||http://purl.uniprot.org/uniprot/Q3UWX1|||http://purl.uniprot.org/uniprot/Q91W90 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Mass|||Modification|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Mass|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Prevents secretion from ER|||Redox-active|||Thioredoxin|||Thioredoxin 1|||Thioredoxin 2|||Thioredoxin 3|||Thioredoxin domain-containing protein 5|||protein disulfide-isomerase ^@ http://purl.uniprot.org/annotation/PRO_0000034184|||http://purl.uniprot.org/annotation/PRO_5014309159 http://togogenome.org/gene/10090:Smpd3 ^@ http://purl.uniprot.org/uniprot/Q9JJY3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||INTRAMEM|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Topological Domain ^@ Abolishes binding with phosphatidic acid. No effect on cell membrane location. Strongly decreases sphingomyelin phosphodiesterase activity. Abolishes sphingomyelin phosphodiesterase activity and locates at endoplasmic reticulum; when associated with A-33 and 45-DEL-48.|||Cytoplasmic|||Disordered|||Helical|||Important for substrate recognition|||No effect on binding with phosphatidic acid.|||Phosphoserine|||Polar residues|||Proton acceptor|||S-palmitoyl cysteine|||Sphingomyelin phosphodiesterase 3|||Strongly decreases binding with phosphatidic acid and phosphatidylserine. Abolishes binding with phosphatidic acid and phosphatidylserine; when associated with 45-DEL-48. Strongly decreases sphingomyelin phosphodiesterase activity; when associated with 45-DEL-48. Abolishes sphingomyelin phosphodiesterase activity and locates at endoplasmic reticulum; when associated with 45-DEL-48 and 92-A-A-93.|||Strongly decreases binding with phosphatidic acid and phosphatidylserine. Abolishes binding with phosphatidic acid and phosphatidylserine; when associated with A-33. Strongly decreases sphingomyelin phosphodiesterase activity; when associated with A-33. Abolishes sphingomyelin phosphodiesterase activity and locates at endoplasmic reticulum; when associated with A-33 and 92-A-A-93.|||Strongly decreases binding with phosphatidic acid. ^@ http://purl.uniprot.org/annotation/PRO_0000075693 http://togogenome.org/gene/10090:Asns ^@ http://purl.uniprot.org/uniprot/Q61024 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site ^@ Asparagine synthetase|||Asparagine synthetase [glutamine-hydrolyzing]|||For GATase activity|||Glutamine amidotransferase type-2|||Important for beta-aspartyl-AMP intermediate formation|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056912 http://togogenome.org/gene/10090:Dstn ^@ http://purl.uniprot.org/uniprot/Q4FK36|||http://purl.uniprot.org/uniprot/Q9R0P5 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif ^@ ADF-H|||Destrin|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000214919 http://togogenome.org/gene/10090:Scfd1 ^@ http://purl.uniprot.org/uniprot/Q8BRF7 ^@ 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|||Sec1 family domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000206288|||http://purl.uniprot.org/annotation/VSP_011310|||http://purl.uniprot.org/annotation/VSP_011311|||http://purl.uniprot.org/annotation/VSP_011312|||http://purl.uniprot.org/annotation/VSP_011313 http://togogenome.org/gene/10090:Stub1 ^@ http://purl.uniprot.org/uniprot/Q9WUD1 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||E3 ubiquitin-protein ligase CHIP|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired interaction with ATXN3; when associated with R-2 and R-4.|||Impaired interaction with ATXN3; when associated with R-2 and R-7.|||Impaired interaction with ATXN3; when associated with R-4 and R-7.|||Loss of E3 ubiquitin protein ligase activity.|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||U-box ^@ http://purl.uniprot.org/annotation/PRO_0000106330 http://togogenome.org/gene/10090:Or14c43 ^@ http://purl.uniprot.org/uniprot/Q7TS05 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ftdc2 ^@ http://purl.uniprot.org/uniprot/Q8BU47 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Ferritin-like diiron ^@ http://togogenome.org/gene/10090:Il1rapl1 ^@ http://purl.uniprot.org/uniprot/B1ASU0|||http://purl.uniprot.org/uniprot/Q0VDP7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like|||Interleukin-1 receptor accessory protein-like 1|||TIR ^@ http://purl.uniprot.org/annotation/PRO_5015087033|||http://purl.uniprot.org/annotation/PRO_5015097003 http://togogenome.org/gene/10090:Zdhhc25 ^@ http://purl.uniprot.org/uniprot/Q810M4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Palmitoyltransferase DHHC ^@ http://togogenome.org/gene/10090:Rab34 ^@ http://purl.uniprot.org/uniprot/Q64008 ^@ 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 ^@ Abolishes interaction with RILP and localization to the peri-Golgi region.|||Does not abolish interaction with RILP and localization to the peri-Golgi region.|||Effector region|||N-acetylmethionine|||Phosphoserine|||Ras-related protein Rab-34|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121244 http://togogenome.org/gene/10090:Ubald2 ^@ http://purl.uniprot.org/uniprot/Q8BQH4 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||N-acetylserine|||Removed|||UBA-like domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000239029 http://togogenome.org/gene/10090:Daglb ^@ http://purl.uniprot.org/uniprot/Q91WC9 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Charge relay system|||Cytoplasmic|||Diacylglycerol lipase-beta|||Extracellular|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000248351 http://togogenome.org/gene/10090:Gmppb ^@ http://purl.uniprot.org/uniprot/Q8BTZ7 ^@ Chain|||Molecule Processing ^@ Chain ^@ Mannose-1-phosphate guanyltransferase beta ^@ http://purl.uniprot.org/annotation/PRO_0000307163 http://togogenome.org/gene/10090:Sema6c ^@ http://purl.uniprot.org/uniprot/E9Q613|||http://purl.uniprot.org/uniprot/Q9WTM3 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sema|||Semaphorin-6C ^@ http://purl.uniprot.org/annotation/PRO_0000032345|||http://purl.uniprot.org/annotation/PRO_5015090364 http://togogenome.org/gene/10090:Spg11 ^@ http://purl.uniprot.org/uniprot/Q3UHA3 ^@ 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|||Spatacsin ^@ http://purl.uniprot.org/annotation/PRO_0000287468|||http://purl.uniprot.org/annotation/VSP_025485|||http://purl.uniprot.org/annotation/VSP_025486 http://togogenome.org/gene/10090:Slitrk5 ^@ http://purl.uniprot.org/uniprot/Q69ZV6|||http://purl.uniprot.org/uniprot/Q810B7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||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|||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_0000032682|||http://purl.uniprot.org/annotation/VSP_050708|||http://purl.uniprot.org/annotation/VSP_050709|||http://purl.uniprot.org/annotation/VSP_050710 http://togogenome.org/gene/10090:Pitrm1 ^@ http://purl.uniprot.org/uniprot/Q8K411 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide ^@ Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In strain: LG/J and SM/J.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Presequence protease, mitochondrial|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000249932|||http://purl.uniprot.org/annotation/VSP_020598|||http://purl.uniprot.org/annotation/VSP_020599 http://togogenome.org/gene/10090:Or5b120 ^@ http://purl.uniprot.org/uniprot/Q7TQQ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or4f61 ^@ http://purl.uniprot.org/uniprot/A2AVL6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dcaf11 ^@ http://purl.uniprot.org/uniprot/Q3TYA0|||http://purl.uniprot.org/uniprot/Q3UD98|||http://purl.uniprot.org/uniprot/Q91VU6 ^@ 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 ^@ DDB1- and CUL4-associated factor 11|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051372|||http://purl.uniprot.org/annotation/VSP_008425|||http://purl.uniprot.org/annotation/VSP_008426 http://togogenome.org/gene/10090:Epyc ^@ http://purl.uniprot.org/uniprot/P70186 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||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 (Xyl...) (dermatan sulfate) serine ^@ http://purl.uniprot.org/annotation/PRO_0000032769 http://togogenome.org/gene/10090:Pla2g4e ^@ http://purl.uniprot.org/uniprot/Q50L42 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ C2|||Cytosolic phospholipase A2 epsilon|||Disordered|||Impairs calcium-dependent biosynthesis of NAPEs and NAEs. Reduces tubule growth and cargo transport from clathrin-independent endosomes.|||In isoform 2.|||Nucleophile|||PLA2c|||Phosphoserine|||Polar residues|||Proton acceptor|||Required for localization at membrane structures ^@ http://purl.uniprot.org/annotation/PRO_0000247026|||http://purl.uniprot.org/annotation/VSP_019884|||http://purl.uniprot.org/annotation/VSP_019885|||http://purl.uniprot.org/annotation/VSP_019886 http://togogenome.org/gene/10090:Macf1 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQA6 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||EF-hand|||GAR|||Polar residues|||SH3 ^@ http://togogenome.org/gene/10090:Or4x13 ^@ http://purl.uniprot.org/uniprot/A0A1L1SQ02 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pebp1 ^@ http://purl.uniprot.org/uniprot/P70296 ^@ Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Strand ^@ Hippocampal cholinergic neurostimulating peptide|||Interaction with RAF1|||N-acetylalanine; in peptide hippocampal cholinergic neurostimulating|||Phosphatidylethanolamine-binding protein 1|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000023275|||http://purl.uniprot.org/annotation/PRO_0000023276 http://togogenome.org/gene/10090:Ddx27 ^@ http://purl.uniprot.org/uniprot/Q921N6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||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_0000055032|||http://purl.uniprot.org/annotation/VSP_007073|||http://purl.uniprot.org/annotation/VSP_007074 http://togogenome.org/gene/10090:Bend7 ^@ http://purl.uniprot.org/uniprot/Q0VE44|||http://purl.uniprot.org/uniprot/Q8BSV3 ^@ 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 ^@ BEN|||BEN domain-containing protein 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000244081|||http://purl.uniprot.org/annotation/VSP_019509|||http://purl.uniprot.org/annotation/VSP_019510 http://togogenome.org/gene/10090:Cspg4 ^@ http://purl.uniprot.org/uniprot/Q3URZ9|||http://purl.uniprot.org/uniprot/Q8VHY0 ^@ 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|||Signal Peptide|||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|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ CSPG|||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|||In isoform 2.|||In isoform 3.|||Interaction with COL5A1|||Interaction with COL6A2|||Laminin G-like 1|||Laminin G-like 2|||Loss of interaction with GRIP1 and GRIP2.|||N-linked (GlcNAc...) asparagine|||Neurite growth inhibition|||No effect on interaction with GRIP1 and GRIP2.|||O-linked (Xyl...) (chondroitin sulfate) serine|||PDZ-binding|||Phosphothreonine; by PKC/PRKCA|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000041963|||http://purl.uniprot.org/annotation/VSP_015656|||http://purl.uniprot.org/annotation/VSP_015657|||http://purl.uniprot.org/annotation/VSP_015658 http://togogenome.org/gene/10090:Rab3ip ^@ http://purl.uniprot.org/uniprot/A0A1W2P7K6|||http://purl.uniprot.org/uniprot/Q68EF0|||http://purl.uniprot.org/uniprot/Q8BR32 ^@ 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 ^@ GDP/GTP exchange factor Sec2 N-terminal|||Phosphoserine|||Rab-3A-interacting protein ^@ http://purl.uniprot.org/annotation/PRO_0000097145 http://togogenome.org/gene/10090:Mxi1 ^@ http://purl.uniprot.org/uniprot/P50540|||http://purl.uniprot.org/uniprot/Q3U3X2|||http://purl.uniprot.org/uniprot/Q3USD3|||http://purl.uniprot.org/uniprot/Q6P2L3 ^@ 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 ^@ BHLH|||Basic and acidic residues|||Disordered|||In isoform Short.|||Max-interacting protein 1|||Polar residues|||Pro residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127286|||http://purl.uniprot.org/annotation/VSP_002141 http://togogenome.org/gene/10090:H4c14 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Stac2 ^@ http://purl.uniprot.org/uniprot/Q8R1B0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Phorbol-ester/DAG-type|||Phosphoserine|||Pro residues|||SH3 1|||SH3 2|||SH3 and cysteine-rich domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000274414 http://togogenome.org/gene/10090:Kif13a ^@ http://purl.uniprot.org/uniprot/F8VQ75 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Kinesin motor|||Polar residues ^@ http://togogenome.org/gene/10090:Tmem171 ^@ http://purl.uniprot.org/uniprot/Q4KL18 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Transmembrane protein 171 ^@ http://purl.uniprot.org/annotation/PRO_0000249571 http://togogenome.org/gene/10090:Rfx2 ^@ http://purl.uniprot.org/uniprot/P48379 ^@ 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 ^@ Basic and acidic residues|||DNA-binding protein RFX2|||Disordered|||In isoform 2.|||Phosphoserine|||RFX-type winged-helix ^@ http://purl.uniprot.org/annotation/PRO_0000215289|||http://purl.uniprot.org/annotation/VSP_037812 http://togogenome.org/gene/10090:Cdr2 ^@ http://purl.uniprot.org/uniprot/P97817 ^@ 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_0000089457 http://togogenome.org/gene/10090:H13 ^@ http://purl.uniprot.org/uniprot/Q6PGJ8|||http://purl.uniprot.org/uniprot/Q9D8V0 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||Minor histocompatibility antigen H13|||N-linked (GlcNAc...) asparagine|||PAL|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000073908|||http://purl.uniprot.org/annotation/VSP_005199|||http://purl.uniprot.org/annotation/VSP_005200|||http://purl.uniprot.org/annotation/VSP_005201|||http://purl.uniprot.org/annotation/VSP_005202|||http://purl.uniprot.org/annotation/VSP_039805 http://togogenome.org/gene/10090:Sft2d3 ^@ http://purl.uniprot.org/uniprot/Q9CSV6 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||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_0000238614 http://togogenome.org/gene/10090:Lin28b ^@ http://purl.uniprot.org/uniprot/Q45KJ6 ^@ 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|||CCHC-type 1|||CCHC-type 2|||CSD|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Protein lin-28 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000253794|||http://purl.uniprot.org/annotation/VSP_021115|||http://purl.uniprot.org/annotation/VSP_021116|||http://purl.uniprot.org/annotation/VSP_021117|||http://purl.uniprot.org/annotation/VSP_021118|||http://purl.uniprot.org/annotation/VSP_021119|||http://purl.uniprot.org/annotation/VSP_021120|||http://purl.uniprot.org/annotation/VSP_021121 http://togogenome.org/gene/10090:Setdb2 ^@ http://purl.uniprot.org/uniprot/B2RXP3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||MBD|||Polar residues|||Pre-SET|||SET ^@ http://togogenome.org/gene/10090:Otud7b ^@ http://purl.uniprot.org/uniprot/B2RUR8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ A20-type|||Basic and acidic residues|||Catalytic|||Disordered|||Loss of deubiquitinating activity; when associated with R-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|||Regulatory loop|||Stabilizes the conformation of the regulatory loop|||TRAF-binding ^@ http://purl.uniprot.org/annotation/PRO_0000421819 http://togogenome.org/gene/10090:Iars ^@ http://purl.uniprot.org/uniprot/Q8BU30 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict ^@ 'HIGH' region|||'KMSKS' region|||Isoleucine--tRNA ligase, cytoplasmic|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000098598 http://togogenome.org/gene/10090:Kars ^@ http://purl.uniprot.org/uniprot/Q3TIV6|||http://purl.uniprot.org/uniprot/Q8R2P8|||http://purl.uniprot.org/uniprot/Q99MN1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Aminoacyl-transfer RNA synthetases class-II family profile|||Basic and acidic residues|||Disordered|||Lysine--tRNA ligase|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000152766 http://togogenome.org/gene/10090:Lrrc8c ^@ http://purl.uniprot.org/uniprot/Q8R502 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||Cytoplasmic|||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|||No effect on channel activity of the complex with LRRC8A.|||Phosphoserine|||Volume-regulated anion channel subunit LRRC8C ^@ http://purl.uniprot.org/annotation/PRO_0000076248 http://togogenome.org/gene/10090:Alas1 ^@ http://purl.uniprot.org/uniprot/Q3V0B2|||http://purl.uniprot.org/uniprot/Q8VC19 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ 5-aminolevulinate synthase presequence|||5-aminolevulinate synthase, non-specific, mitochondrial|||Aminotransferase class I/classII|||Disordered|||Hydroxyproline|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||Polar residues|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000001231 http://togogenome.org/gene/10090:Spc25 ^@ http://purl.uniprot.org/uniprot/Q3UA16 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||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_0000249566|||http://purl.uniprot.org/annotation/VSP_020518|||http://purl.uniprot.org/annotation/VSP_020519 http://togogenome.org/gene/10090:Vmn2r26 ^@ http://purl.uniprot.org/uniprot/Q6TAC4 ^@ 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|||Vomeronasal type-2 receptor 26 ^@ http://purl.uniprot.org/annotation/PRO_0000246125 http://togogenome.org/gene/10090:Itgb1bp2 ^@ http://purl.uniprot.org/uniprot/Q9R000 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Acidic residues|||CHORD 1|||CHORD 2|||CS|||Disordered|||Integrin beta-1-binding protein 2|||Polar residues|||SH2-binding|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000084268 http://togogenome.org/gene/10090:Rcor1 ^@ http://purl.uniprot.org/uniprot/A0A140T8R7|||http://purl.uniprot.org/uniprot/Q8CFE3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||SANT 1|||SANT 2 ^@ http://purl.uniprot.org/annotation/PRO_0000226774 http://togogenome.org/gene/10090:Golga3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1H6|||http://purl.uniprot.org/uniprot/E9QP99|||http://purl.uniprot.org/uniprot/P55937 ^@ 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|||Golgi-targeting domain|||Golgin subfamily A member 3|||In isoform 1.|||Interaction with GOPC|||N-acetylmethionine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000190058|||http://purl.uniprot.org/annotation/VSP_016071 http://togogenome.org/gene/10090:Or5w20 ^@ http://purl.uniprot.org/uniprot/A2AVC0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fshr ^@ http://purl.uniprot.org/uniprot/B2RQM3|||http://purl.uniprot.org/uniprot/P35378 ^@ 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|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) asparagine|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000012773|||http://purl.uniprot.org/annotation/PRO_5014205211 http://togogenome.org/gene/10090:Cacna2d2 ^@ http://purl.uniprot.org/uniprot/A0A411ACW5|||http://purl.uniprot.org/uniprot/A0A411ACX9|||http://purl.uniprot.org/uniprot/A0A411ACZ2|||http://purl.uniprot.org/uniprot/Q6PHS9 ^@ 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 ^@ Abolishes metal-binding and ability to regulate calcium current.|||Cache|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In du; variant allele entla.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2, isoform 5 and isoform 6.|||In isoform 3, isoform 5 and isoform 6.|||Induces a strong decrease in gabapentin-binding.|||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_0000304640|||http://purl.uniprot.org/annotation/PRO_0000304641|||http://purl.uniprot.org/annotation/PRO_0000304642|||http://purl.uniprot.org/annotation/VSP_028061|||http://purl.uniprot.org/annotation/VSP_028062|||http://purl.uniprot.org/annotation/VSP_028063 http://togogenome.org/gene/10090:Rexo2 ^@ http://purl.uniprot.org/uniprot/Q9D8S4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Site|||Transit Peptide ^@ Exonuclease|||Important for dinucleotide binding|||Mitochondrion|||N6-acetyllysine|||Oligoribonuclease, mitochondrial|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000041951 http://togogenome.org/gene/10090:Myl12b ^@ http://purl.uniprot.org/uniprot/Q3THE2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000284383 http://togogenome.org/gene/10090:Vmn2r110 ^@ http://purl.uniprot.org/uniprot/E9PWD5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003244267 http://togogenome.org/gene/10090:Adamtsl2 ^@ http://purl.uniprot.org/uniprot/A1A5B7|||http://purl.uniprot.org/uniprot/Q7TSK7 ^@ 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 ^@ ADAMTS-like protein 2|||Disordered|||N-linked (GlcNAc...) asparagine|||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|||TSP type-1 7 ^@ http://purl.uniprot.org/annotation/PRO_0000249683|||http://purl.uniprot.org/annotation/PRO_5014296717 http://togogenome.org/gene/10090:Zfp503 ^@ http://purl.uniprot.org/uniprot/Q7TMA2 ^@ 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 ^@ C2H2-type|||Disordered|||In isoform 2.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Zinc finger protein 503 ^@ http://purl.uniprot.org/annotation/PRO_0000292205|||http://purl.uniprot.org/annotation/VSP_026396|||http://purl.uniprot.org/annotation/VSP_026397|||http://purl.uniprot.org/annotation/VSP_026398 http://togogenome.org/gene/10090:Mmp2 ^@ http://purl.uniprot.org/uniprot/P33434|||http://purl.uniprot.org/uniprot/Q3UG07 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ 72 kDa type IV collagenase|||Activation peptide|||Collagen-binding|||Collagenase-like 1|||Collagenase-like 2|||Cysteine switch|||Disordered|||Fibronectin type-II|||Fibronectin type-II 1|||Fibronectin type-II 2|||Fibronectin type-II 3|||Fibronectin type-II domain-containing protein|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PEX|||Phosphotyrosine; by PKDCC|||Required for inhibitor TIMP2 binding|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028716|||http://purl.uniprot.org/annotation/PRO_0000028717|||http://purl.uniprot.org/annotation/PRO_0000391627|||http://purl.uniprot.org/annotation/PRO_5014309155|||http://purl.uniprot.org/annotation/VSP_044632 http://togogenome.org/gene/10090:Ckap2 ^@ http://purl.uniprot.org/uniprot/Q3V1H1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Association with alpha- and beta-tubulin|||Cytoskeleton-associated protein 2|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000245775 http://togogenome.org/gene/10090:Mtcl1 ^@ http://purl.uniprot.org/uniprot/Q3UHU5 ^@ 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.|||In isoform 3.|||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_0000280114|||http://purl.uniprot.org/annotation/VSP_023555|||http://purl.uniprot.org/annotation/VSP_023556 http://togogenome.org/gene/10090:Mylk3 ^@ http://purl.uniprot.org/uniprot/D3Z630|||http://purl.uniprot.org/uniprot/Q3UIZ8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Myosin light chain kinase 3|||Phosphoserine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000272201|||http://purl.uniprot.org/annotation/VSP_022369|||http://purl.uniprot.org/annotation/VSP_022370 http://togogenome.org/gene/10090:Cdc14a ^@ http://purl.uniprot.org/uniprot/Q6GQT0 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ A|||B|||Disordered|||Dual specificity protein phosphatase CDC14A|||In isoform 2.|||Linker|||Mutant mice are deaf, show fusion of stereocilia and degeneration of hair cells, and have low sperm counts.|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094877|||http://purl.uniprot.org/annotation/VSP_012324 http://togogenome.org/gene/10090:Tsr3 ^@ http://purl.uniprot.org/uniprot/Q5HZH2 ^@ 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 ^@ 18S rRNA aminocarboxypropyltransferase|||Acidic residues|||Basic and acidic residues|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000278670 http://togogenome.org/gene/10090:Sec24b ^@ http://purl.uniprot.org/uniprot/Q80ZX0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Gelsolin-like|||Polar residues|||Pro residues|||Sec23/Sec24 beta-sandwich|||Sec23/Sec24 helical|||Sec23/Sec24 trunk|||Zinc finger Sec23/Sec24-type ^@ http://togogenome.org/gene/10090:Cinp ^@ http://purl.uniprot.org/uniprot/Q9D0V8 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Splice Variant ^@ Cyclin-dependent kinase 2-interacting protein|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000326056|||http://purl.uniprot.org/annotation/VSP_032525|||http://purl.uniprot.org/annotation/VSP_032526|||http://purl.uniprot.org/annotation/VSP_032527|||http://purl.uniprot.org/annotation/VSP_032528 http://togogenome.org/gene/10090:Slc23a1 ^@ http://purl.uniprot.org/uniprot/Q9Z2J0 ^@ Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Solute carrier family 23 member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000165976 http://togogenome.org/gene/10090:Ap3b1 ^@ http://purl.uniprot.org/uniprot/Q3TQ07|||http://purl.uniprot.org/uniprot/Q3UPG0|||http://purl.uniprot.org/uniprot/Q9Z1T1 ^@ 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 ^@ AP-3 complex subunit beta 1 serine-rich|||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|||Clathrin/coatomer adaptor adaptin-like N-terminal|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000193747 http://togogenome.org/gene/10090:Ppm1d ^@ http://purl.uniprot.org/uniprot/Q3TZJ9|||http://purl.uniprot.org/uniprot/Q80WV2|||http://purl.uniprot.org/uniprot/Q9QZ67 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic residues|||Disordered|||Interaction with CHEK1|||PPM-type phosphatase|||Phosphoserine|||Polar residues|||Protein phosphatase 1D ^@ http://purl.uniprot.org/annotation/PRO_0000057753 http://togogenome.org/gene/10090:E2f5 ^@ http://purl.uniprot.org/uniprot/Q61502 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict ^@ DEF box|||Dimerization|||Disordered|||Leucine-zipper|||Polar residues|||RBL2 association|||Transactivation|||Transcription factor E2F5 ^@ http://purl.uniprot.org/annotation/PRO_0000219470 http://togogenome.org/gene/10090:Kcne1 ^@ http://purl.uniprot.org/uniprot/P23299|||http://purl.uniprot.org/uniprot/Q545H6 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphoserine; by PKC|||Potassium voltage-gated channel subfamily E member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000144279 http://togogenome.org/gene/10090:Apoc1 ^@ http://purl.uniprot.org/uniprot/P34928 ^@ Chain|||Experimental Information|||Mass|||Molecule Processing|||Signal Peptide ^@ Chain|||Mass|||Signal Peptide ^@ Apolipoprotein C-I|||Strain C57BL/6. Without methionine sulfoxide.|||Truncated apolipoprotein C-I ^@ http://purl.uniprot.org/annotation/PRO_0000002015|||http://purl.uniprot.org/annotation/PRO_0000391844 http://togogenome.org/gene/10090:Fhit ^@ http://purl.uniprot.org/uniprot/E9PZ91|||http://purl.uniprot.org/uniprot/O89106 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Site ^@ Bis(5'-adenosyl)-triphosphatase|||HIT|||Histidine triad motif|||Important for induction of apoptosis|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Tele-AMP-histidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000109790 http://togogenome.org/gene/10090:Agbl3 ^@ http://purl.uniprot.org/uniprot/Q8CDP0 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes deglutamylase activity.|||Cytosolic carboxypeptidase 3|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000283752|||http://purl.uniprot.org/annotation/VSP_024374|||http://purl.uniprot.org/annotation/VSP_024375|||http://purl.uniprot.org/annotation/VSP_024376|||http://purl.uniprot.org/annotation/VSP_024377|||http://purl.uniprot.org/annotation/VSP_024378|||http://purl.uniprot.org/annotation/VSP_024379 http://togogenome.org/gene/10090:Snx27 ^@ http://purl.uniprot.org/uniprot/Q3UHD6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||FERM-like region F1|||FERM-like region F2|||FERM-like region F3|||In isoform 2.|||PDZ|||PX|||Phosphoserine|||Ras-associating|||Sorting nexin-27 ^@ http://purl.uniprot.org/annotation/PRO_0000315357|||http://purl.uniprot.org/annotation/VSP_030540 http://togogenome.org/gene/10090:Pnisr ^@ http://purl.uniprot.org/uniprot/A2AJT5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Pfn1 ^@ http://purl.uniprot.org/uniprot/P62962 ^@ 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); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by ROCK1|||Phosphotyrosine|||Profilin-1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000199572 http://togogenome.org/gene/10090:Olfml2a ^@ http://purl.uniprot.org/uniprot/B2RQD8|||http://purl.uniprot.org/uniprot/Q8BHP7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Site ^@ Basic and acidic residues|||Cleavage|||Disordered|||Olfactomedin-like|||Olfactomedin-like protein 2A|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000311429|||http://purl.uniprot.org/annotation/PRO_5015087141 http://togogenome.org/gene/10090:Kcnmb2 ^@ http://purl.uniprot.org/uniprot/Q9CZM9 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Ball and chain|||Calcium-activated potassium channel subunit beta-2|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000187052 http://togogenome.org/gene/10090:Slc2a10 ^@ http://purl.uniprot.org/uniprot/A2A4V1|||http://purl.uniprot.org/uniprot/Q8VHD6 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||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|||Major facilitator superfamily (MFS) profile|||Solute carrier family 2, facilitated glucose transporter member 10 ^@ http://purl.uniprot.org/annotation/PRO_0000270192 http://togogenome.org/gene/10090:Or56a5 ^@ http://purl.uniprot.org/uniprot/Q8VGV1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Emid1 ^@ http://purl.uniprot.org/uniprot/Q5SUT2|||http://purl.uniprot.org/uniprot/Q91VF5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ Collagen-like|||Disordered|||EMI|||EMI domain-containing protein 1|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000007824|||http://purl.uniprot.org/annotation/PRO_5014309959|||http://purl.uniprot.org/annotation/VSP_008446 http://togogenome.org/gene/10090:Fam217a ^@ http://purl.uniprot.org/uniprot/A0A286YD65|||http://purl.uniprot.org/uniprot/F8WGE0|||http://purl.uniprot.org/uniprot/Q3UT29|||http://purl.uniprot.org/uniprot/Q9D9W6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Protein FAM217A ^@ http://purl.uniprot.org/annotation/PRO_0000089541 http://togogenome.org/gene/10090:Tecpr2 ^@ http://purl.uniprot.org/uniprot/Q3UH45|||http://purl.uniprot.org/uniprot/Q8CDN4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tnfrsf17 ^@ http://purl.uniprot.org/uniprot/O88472 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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_0000058936|||http://purl.uniprot.org/annotation/VSP_006507 http://togogenome.org/gene/10090:Ovca2 ^@ http://purl.uniprot.org/uniprot/Q9D7E3 ^@ Active Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Chain ^@ Charge relay system|||Esterase OVCA2 ^@ http://purl.uniprot.org/annotation/PRO_0000300877 http://togogenome.org/gene/10090:Or7a38 ^@ http://purl.uniprot.org/uniprot/E9Q5G9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fyb ^@ http://purl.uniprot.org/uniprot/B2RUR0|||http://purl.uniprot.org/uniprot/O35601 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Disordered|||FYN-binding protein 1|||In isoform FYB-120.|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH2-binding; to FYN|||SH2-binding; to LCP2|||SH3|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000087397|||http://purl.uniprot.org/annotation/VSP_004261 http://togogenome.org/gene/10090:Ptrh2 ^@ http://purl.uniprot.org/uniprot/Q8R2Y8 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Crosslink|||Sequence Conflict|||Transmembrane ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Peptidyl-tRNA hydrolase 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000029863 http://togogenome.org/gene/10090:Lypd2 ^@ http://purl.uniprot.org/uniprot/Q9DD23 ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated serine|||Ly6/PLAUR domain-containing protein 2|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000226749|||http://purl.uniprot.org/annotation/PRO_0000226750 http://togogenome.org/gene/10090:Vmn1r168 ^@ http://purl.uniprot.org/uniprot/K7N6B6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ncam1 ^@ http://purl.uniprot.org/uniprot/A0A0A6YY47|||http://purl.uniprot.org/uniprot/E9Q589|||http://purl.uniprot.org/uniprot/E9QB01|||http://purl.uniprot.org/uniprot/P13595 ^@ Binding Site|||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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||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|||GPI-anchor amidated serine|||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.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||Neural cell adhesion molecule 1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000015012|||http://purl.uniprot.org/annotation/PRO_5002024379|||http://purl.uniprot.org/annotation/PRO_5003245739|||http://purl.uniprot.org/annotation/PRO_5003245910|||http://purl.uniprot.org/annotation/VSP_002588|||http://purl.uniprot.org/annotation/VSP_034826|||http://purl.uniprot.org/annotation/VSP_034827|||http://purl.uniprot.org/annotation/VSP_034828|||http://purl.uniprot.org/annotation/VSP_034829 http://togogenome.org/gene/10090:Aldh3b3 ^@ http://purl.uniprot.org/uniprot/J3QMK6 ^@ Active Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Site ^@ Active Site|||Chain|||Lipid Binding|||Mutagenesis Site|||Propeptide ^@ Aldehyde dehydrogenase family 3 member B3|||Reduces membrane localization.|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000436530|||http://purl.uniprot.org/annotation/PRO_0000436531 http://togogenome.org/gene/10090:Ceacam9 ^@ http://purl.uniprot.org/uniprot/Q78T27 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015098642 http://togogenome.org/gene/10090:Rpp25 ^@ http://purl.uniprot.org/uniprot/Q91WE3 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Ribonuclease P protein subunit p25 ^@ http://purl.uniprot.org/annotation/PRO_0000237583 http://togogenome.org/gene/10090:Zfat ^@ http://purl.uniprot.org/uniprot/Q7TS63 ^@ Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Helix|||Region|||Splice Variant|||Strand|||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; 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.|||Polar residues|||Zinc finger protein ZFAT ^@ http://purl.uniprot.org/annotation/PRO_0000047567|||http://purl.uniprot.org/annotation/VSP_034940|||http://purl.uniprot.org/annotation/VSP_034941 http://togogenome.org/gene/10090:Ano1 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQF2|||http://purl.uniprot.org/uniprot/G8JL82|||http://purl.uniprot.org/uniprot/Q8BHY3 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||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 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Anoctamin dimerisation|||Anoctamin-1|||Cytoplasmic|||Decreased Ca(2+) sensitivity.|||Decreased permeability to chloride ions.|||Decreased threshold for activation by calcium.|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Increased Ca(2+) sensitivity.|||Increased permeability to chloride ions.|||Increased threshold for activation by calcium.|||Increased threshold for activation by calcium. Increased permeability to chloride ions.|||Low constitutive channel activity. Decreased threshold for activation by calcium.|||Moderately increased threshold for activation by calcium.|||N-linked (GlcNAc...) asparagine|||No effect of cysteine-modifying agent MTSET on ion permeability in contrast to wild-type where MTSET blocks current.|||No effect on threshold for activation by calcium.|||Phosphoserine|||Reduced anion permeability and increased cation permeability.|||Strongly increased threshold for activation by calcium.|||Unlikely to bind calcium but may play an important structural role ^@ http://purl.uniprot.org/annotation/PRO_0000288436|||http://purl.uniprot.org/annotation/VSP_025672 http://togogenome.org/gene/10090:Ssxa1 ^@ http://purl.uniprot.org/uniprot/B1AUS7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||KRAB-related|||Protein SSXA1 ^@ http://purl.uniprot.org/annotation/PRO_0000440991 http://togogenome.org/gene/10090:Chaf1b ^@ http://purl.uniprot.org/uniprot/Q9D0N7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ 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_0000050897 http://togogenome.org/gene/10090:1110004F10Rik ^@ http://purl.uniprot.org/uniprot/Q9R0P4 ^@ 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_0000263657 http://togogenome.org/gene/10090:Grtp1 ^@ http://purl.uniprot.org/uniprot/Q9D3N8 ^@ 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, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Rab-GAP TBC ^@ http://purl.uniprot.org/annotation/PRO_0000288709|||http://purl.uniprot.org/annotation/VSP_025756|||http://purl.uniprot.org/annotation/VSP_025757|||http://purl.uniprot.org/annotation/VSP_025758 http://togogenome.org/gene/10090:Zfp57 ^@ http://purl.uniprot.org/uniprot/Q8C6P8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||Crucial for 5-methylcytosine recognition|||Disordered|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 57 ^@ http://purl.uniprot.org/annotation/PRO_0000291965|||http://purl.uniprot.org/annotation/VSP_026331 http://togogenome.org/gene/10090:Ddx51 ^@ http://purl.uniprot.org/uniprot/Q6P9R1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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_0000228097 http://togogenome.org/gene/10090:Hmgn1 ^@ http://purl.uniprot.org/uniprot/P18608|||http://purl.uniprot.org/uniprot/Q8CEW1 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ ADP-ribosylserine; alternate|||Basic and acidic residues|||Disordered|||N6-acetyllysine|||Non-histone chromosomal protein HMG-14|||Phosphoserine|||Phosphoserine; alternate; by RPS6KA5|||Phosphoserine; by RPS6KA5|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000206692 http://togogenome.org/gene/10090:Daam2 ^@ http://purl.uniprot.org/uniprot/Q80U19 ^@ 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 ^@ DAD|||Disheveled-associated activator of morphogenesis 2|||Disordered|||FH1|||FH2|||GBD/FH3|||In isoform 2.|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000194910|||http://purl.uniprot.org/annotation/VSP_008005|||http://purl.uniprot.org/annotation/VSP_008006 http://togogenome.org/gene/10090:Odf3l1 ^@ http://purl.uniprot.org/uniprot/Q810P2 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ Protein CIMAP1C|||STPGR 1|||STPGR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000304786 http://togogenome.org/gene/10090:H2ac4 ^@ http://purl.uniprot.org/uniprot/B2RVF0|||http://purl.uniprot.org/uniprot/C0HKE1|||http://purl.uniprot.org/uniprot/C0HKE2|||http://purl.uniprot.org/uniprot/C0HKE3|||http://purl.uniprot.org/uniprot/C0HKE4|||http://purl.uniprot.org/uniprot/C0HKE5|||http://purl.uniprot.org/uniprot/C0HKE6|||http://purl.uniprot.org/uniprot/C0HKE7|||http://purl.uniprot.org/uniprot/C0HKE8|||http://purl.uniprot.org/uniprot/C0HKE9 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Histone H2A type 1-C|||Histone H2A type 1-D|||Histone H2A type 1-E|||Histone H2A type 1-G|||Histone H2A type 1-I|||Histone H2A type 1-N|||Histone H2A type 1-O|||Histone H2A type 1-P|||Histone H2A/H2B/H3|||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_0000439715|||http://purl.uniprot.org/annotation/PRO_0000439716|||http://purl.uniprot.org/annotation/PRO_0000439717|||http://purl.uniprot.org/annotation/PRO_0000439718|||http://purl.uniprot.org/annotation/PRO_0000439719|||http://purl.uniprot.org/annotation/PRO_0000439720|||http://purl.uniprot.org/annotation/PRO_0000439721|||http://purl.uniprot.org/annotation/PRO_0000439722|||http://purl.uniprot.org/annotation/PRO_0000439723 http://togogenome.org/gene/10090:Car9 ^@ http://purl.uniprot.org/uniprot/Q3UUZ9|||http://purl.uniprot.org/uniprot/Q8VHB5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||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|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Alpha-carbonic anhydrase|||Carbonic anhydrase|||Carbonic anhydrase 9|||Catalytic|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine|||O-linked (GlcNAc...) threonine|||Phosphotyrosine|||Proteoglycan-like (PG)|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004244|||http://purl.uniprot.org/annotation/PRO_5014309229|||http://purl.uniprot.org/annotation/VSP_007409|||http://purl.uniprot.org/annotation/VSP_007410 http://togogenome.org/gene/10090:Tmem184b ^@ http://purl.uniprot.org/uniprot/A0A2I3BQI5|||http://purl.uniprot.org/uniprot/Q8BG09 ^@ 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|||Transmembrane protein 184B ^@ http://purl.uniprot.org/annotation/PRO_0000211556 http://togogenome.org/gene/10090:Rnf123 ^@ http://purl.uniprot.org/uniprot/Q5XPI3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Asymmetric dimethylarginine|||B30.2/SPRY|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF123|||In isoform 2.|||Interaction with NFKB1|||N-acetylalanine|||Phosphoserine|||RING-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000250448|||http://purl.uniprot.org/annotation/VSP_020651 http://togogenome.org/gene/10090:Prg3 ^@ http://purl.uniprot.org/uniprot/Q9JL95 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||C-type lectin|||Disordered|||In isoform 2.|||Proteoglycan 3 ^@ http://purl.uniprot.org/annotation/PRO_0000248860|||http://purl.uniprot.org/annotation/VSP_034564 http://togogenome.org/gene/10090:Cyp2a4 ^@ http://purl.uniprot.org/uniprot/P15392 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Cytochrome P450 2A4|||N6-acetyllysine|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051666 http://togogenome.org/gene/10090:Ankrd66 ^@ http://purl.uniprot.org/uniprot/J3QNN4 ^@ Region|||Repeat ^@ Repeat ^@ ANK ^@ http://togogenome.org/gene/10090:Fbxo7 ^@ http://purl.uniprot.org/uniprot/Q3U7U3|||http://purl.uniprot.org/uniprot/Q3UD93|||http://purl.uniprot.org/uniprot/Q3UGI9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Disordered|||F-box|||F-box only protein 7|||Important for dimerization and interaction with PSMF1|||Important for interaction with CDK6|||Important for interaction with PINK1|||Omega-N-methylarginine|||Polar residues|||RFDP motif|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000307722 http://togogenome.org/gene/10090:Ppwd1 ^@ http://purl.uniprot.org/uniprot/Q8C908|||http://purl.uniprot.org/uniprot/Q8CEC6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||N-acetylalanine|||PPIase cyclophilin-type|||Peptidylprolyl isomerase domain and WD repeat-containing protein 1|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000240307 http://togogenome.org/gene/10090:Rbm38 ^@ http://purl.uniprot.org/uniprot/Q62176 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||RNA-binding protein 38|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081813 http://togogenome.org/gene/10090:Upk3bl ^@ http://purl.uniprot.org/uniprot/F8WJ60|||http://purl.uniprot.org/uniprot/Q9D701 ^@ 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|||Uroplakin-3b-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000375088|||http://purl.uniprot.org/annotation/PRO_5003379518 http://togogenome.org/gene/10090:Sik2 ^@ http://purl.uniprot.org/uniprot/F8VPT7|||http://purl.uniprot.org/uniprot/Q8CFH6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||Loss of kinase activity.|||Low levels of constitutive activity.|||N6-acetyllysine; by EP300|||Phosphoserine|||Phosphothreonine|||Pro residues|||Protein kinase|||Proton acceptor|||RK-rich region; required for cAMP responsiveness|||Reduced 14-3-3 interaction. Reduced inactivation following cAMP signaling.|||Reduced inhibitory activity towards TORCs in presence and absence of cAMP signaling.|||Reduced interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity.|||Reduced 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-358 and A-484.|||Reduced 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-358 and A-587.|||Reduced 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-484 and A-587.|||Serine/threonine-protein kinase SIK2|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000086663 http://togogenome.org/gene/10090:Sult1c1 ^@ http://purl.uniprot.org/uniprot/Q80VR3 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Proton acceptor|||Sulfotransferase 1C1 ^@ http://purl.uniprot.org/annotation/PRO_0000231634 http://togogenome.org/gene/10090:Poln ^@ http://purl.uniprot.org/uniprot/A0A0J9YTQ3|||http://purl.uniprot.org/uniprot/A0A0J9YVA9|||http://purl.uniprot.org/uniprot/A0A0R4J0E3|||http://purl.uniprot.org/uniprot/Q7TQ07 ^@ 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|||DNA polymerase nu|||DNA-directed DNA polymerase family A palm|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000227939|||http://purl.uniprot.org/annotation/VSP_017616 http://togogenome.org/gene/10090:Prune1 ^@ http://purl.uniprot.org/uniprot/Q8BIW1 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ DHH motif|||Disordered|||Essential for homodimerization|||Exopolyphosphatase PRUNE1|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000337988 http://togogenome.org/gene/10090:Lrrn3 ^@ http://purl.uniprot.org/uniprot/Q8CBC6 ^@ 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|||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_0000045824 http://togogenome.org/gene/10090:Brwd3 ^@ http://purl.uniprot.org/uniprot/A2AHJ4 ^@ 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|||Basic residues|||Bromo 1|||Bromo 2|||Bromodomain and WD repeat-containing protein 3|||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 8 ^@ http://purl.uniprot.org/annotation/PRO_0000283090|||http://purl.uniprot.org/annotation/VSP_024308|||http://purl.uniprot.org/annotation/VSP_024309|||http://purl.uniprot.org/annotation/VSP_024310|||http://purl.uniprot.org/annotation/VSP_024311 http://togogenome.org/gene/10090:Gm15097 ^@ http://purl.uniprot.org/uniprot/L7MU67 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or5d39 ^@ http://purl.uniprot.org/uniprot/Q7TR26 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pcdh9 ^@ http://purl.uniprot.org/uniprot/A0A0A6YWY8|||http://purl.uniprot.org/uniprot/A0A0A6YY09|||http://purl.uniprot.org/uniprot/A0A0A6YY37|||http://purl.uniprot.org/uniprot/F8VPK8 ^@ 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|||Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5002024612|||http://purl.uniprot.org/annotation/PRO_5002034124|||http://purl.uniprot.org/annotation/PRO_5015091371 http://togogenome.org/gene/10090:Fcho1 ^@ http://purl.uniprot.org/uniprot/Q8K285 ^@ 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 ^@ Disordered|||F-BAR|||F-BAR domain only protein 1|||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_0000271760 http://togogenome.org/gene/10090:Rbm41 ^@ http://purl.uniprot.org/uniprot/A2AG09|||http://purl.uniprot.org/uniprot/Q8JZV4 ^@ 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.|||In isoform 3.|||In isoform 4.|||RNA-binding protein 41|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000256268|||http://purl.uniprot.org/annotation/VSP_021350|||http://purl.uniprot.org/annotation/VSP_021351|||http://purl.uniprot.org/annotation/VSP_021352|||http://purl.uniprot.org/annotation/VSP_021353|||http://purl.uniprot.org/annotation/VSP_021354 http://togogenome.org/gene/10090:Lypd9 ^@ http://purl.uniprot.org/uniprot/Q8C5Z9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_5015099092 http://togogenome.org/gene/10090:Crxos ^@ http://purl.uniprot.org/uniprot/B6ZND8|||http://purl.uniprot.org/uniprot/B6ZND9|||http://purl.uniprot.org/uniprot/Q3UEY5|||http://purl.uniprot.org/uniprot/Q3UL53 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Sypl2 ^@ http://purl.uniprot.org/uniprot/O89104 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||MARVEL|||N-linked (GlcNAc...) asparagine|||Polar residues|||Synaptophysin-like protein 2|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000179167 http://togogenome.org/gene/10090:Zfp462 ^@ http://purl.uniprot.org/uniprot/B1AWL2|||http://purl.uniprot.org/uniprot/Q69ZA0|||http://purl.uniprot.org/uniprot/Q8CD61 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||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 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|||Interaction with PBX1|||N6-methyllysine|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger protein 462 ^@ http://purl.uniprot.org/annotation/PRO_0000445627 http://togogenome.org/gene/10090:Or10n1 ^@ http://purl.uniprot.org/uniprot/Q05AA1|||http://purl.uniprot.org/uniprot/Q60887 ^@ 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 10N1 ^@ http://purl.uniprot.org/annotation/PRO_0000150825 http://togogenome.org/gene/10090:Agps ^@ http://purl.uniprot.org/uniprot/A2AL50|||http://purl.uniprot.org/uniprot/Q8C0I1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Site|||Transit Peptide ^@ Alkyldihydroxyacetonephosphate synthase, peroxisomal|||Disordered|||FAD-binding PCMH-type|||Important for enzyme activity|||N6-acetyllysine|||Peroxisome|||Phosphoserine|||Phosphothreonine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000231676 http://togogenome.org/gene/10090:Vmn1r220 ^@ http://purl.uniprot.org/uniprot/Q8R272 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp78 ^@ http://purl.uniprot.org/uniprot/Q5U406|||http://purl.uniprot.org/uniprot/Q69ZK4|||http://purl.uniprot.org/uniprot/Q8BJ21 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dlg5 ^@ http://purl.uniprot.org/uniprot/E9Q9I2|||http://purl.uniprot.org/uniprot/E9Q9R9|||http://purl.uniprot.org/uniprot/Q3UH41|||http://purl.uniprot.org/uniprot/Q6NXJ3 ^@ 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 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant ^@ Basic and acidic residues|||CARD|||Disks large homolog 5|||Disordered|||Guanylate kinase-like|||In allele LP; loss of neuronal function and disruption of interactions between the SH3 and guanylate kinase-like domains.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000440556 http://togogenome.org/gene/10090:Ffar4 ^@ http://purl.uniprot.org/uniprot/Q3V2S5|||http://purl.uniprot.org/uniprot/Q7TMA4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Free fatty acid receptor 4|||G-protein coupled receptors family 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 LCFA-mediated phosphorylation and interaction with ARRB2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000069611 http://togogenome.org/gene/10090:Arpc2 ^@ http://purl.uniprot.org/uniprot/Q9CVB6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Actin-related protein 2/3 complex subunit 2|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000124034 http://togogenome.org/gene/10090:Prkaa2 ^@ http://purl.uniprot.org/uniprot/Q8BRK8 ^@ 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|||Region|||Sequence Conflict ^@ 5'-AMP-activated protein kinase catalytic subunit alpha-2|||AIS|||Loss of kinase activity.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LKB1 and CaMKK2|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000262957 http://togogenome.org/gene/10090:Mansc1 ^@ http://purl.uniprot.org/uniprot/Q9CR33 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||MANSC|||MANSC domain-containing protein 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000021638 http://togogenome.org/gene/10090:Ndrg4 ^@ http://purl.uniprot.org/uniprot/Q8BTG7 ^@ 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 NDRG4 ^@ http://purl.uniprot.org/annotation/PRO_0000159580|||http://purl.uniprot.org/annotation/VSP_022958|||http://purl.uniprot.org/annotation/VSP_022959 http://togogenome.org/gene/10090:Or8b35 ^@ http://purl.uniprot.org/uniprot/Q8VF63 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zkscan4 ^@ http://purl.uniprot.org/uniprot/Q5SZT6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||SCAN box ^@ http://togogenome.org/gene/10090:Dpp9 ^@ http://purl.uniprot.org/uniprot/Q8BVG4 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict|||Splice Variant ^@ Charge relay system|||Decreased levels of global dipeptidyl peptidase activity. Homozygous pups are born at the expected Mendelian rate and display no obvious morphological defects, but none survive to weaning. Homozygous pups display suckling defects and survive only when fed manually. The suckling defects are probably due to increased apoptosis of migratory tongue muscle progenitor cells, leading to defects in the development of intrinsic muscles in the distal tongue and decreased tongue size.|||Dipeptidyl peptidase 9|||In isoform 2.|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000122416|||http://purl.uniprot.org/annotation/VSP_013870|||http://purl.uniprot.org/annotation/VSP_013871|||http://purl.uniprot.org/annotation/VSP_013872 http://togogenome.org/gene/10090:Fam110d ^@ http://purl.uniprot.org/uniprot/Q80X91 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM110D ^@ http://purl.uniprot.org/annotation/PRO_0000318717 http://togogenome.org/gene/10090:Slc9a7 ^@ http://purl.uniprot.org/uniprot/Q8BLV3 ^@ 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|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Required for trans-Golgi network localization|||Sodium/hydrogen exchanger 7 ^@ http://purl.uniprot.org/annotation/PRO_0000052364|||http://purl.uniprot.org/annotation/VSP_009498|||http://purl.uniprot.org/annotation/VSP_009499 http://togogenome.org/gene/10090:Mbd4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0A8|||http://purl.uniprot.org/uniprot/Q9Z2D7 ^@ 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 ^@ Disordered|||MBD|||Methyl-CpG-binding domain protein 4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096265 http://togogenome.org/gene/10090:Catspere2 ^@ http://purl.uniprot.org/uniprot/A0A0A6YXX9 ^@ 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 ^@ Cation channel sperm-associated protein subunit epsilon-like protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_5002024633|||http://purl.uniprot.org/annotation/VSP_058976|||http://purl.uniprot.org/annotation/VSP_058977 http://togogenome.org/gene/10090:Or6c5b ^@ http://purl.uniprot.org/uniprot/A0A0N4SVC3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gypa ^@ http://purl.uniprot.org/uniprot/P14220|||http://purl.uniprot.org/uniprot/Q3TRN7|||http://purl.uniprot.org/uniprot/Q3TZH8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Glycophorin-A|||Helical|||Helical; Signal-anchor for type III membrane protein|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000149048 http://togogenome.org/gene/10090:Svop ^@ http://purl.uniprot.org/uniprot/Q8BFT9 ^@ 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|||Helical|||Phosphoserine|||Synaptic vesicle 2-related protein|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000279453 http://togogenome.org/gene/10090:Kif14 ^@ http://purl.uniprot.org/uniprot/L0N7N1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||FHA|||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_0000431706 http://togogenome.org/gene/10090:Ccdc121rt3 ^@ http://purl.uniprot.org/uniprot/E9Q8Z1|||http://purl.uniprot.org/uniprot/Q8CDD5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ DUF4515|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tpra1 ^@ http://purl.uniprot.org/uniprot/Q99MU1 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Transmembrane protein adipocyte-associated 1 ^@ http://purl.uniprot.org/annotation/PRO_0000076100 http://togogenome.org/gene/10090:Hkdc1 ^@ http://purl.uniprot.org/uniprot/Q91W97 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Hexokinase 1|||Hexokinase 2|||Hexokinase HKDC1|||Hexokinase large subdomain 1|||Hexokinase large subdomain 2|||Hexokinase small subdomain 1|||Hexokinase small subdomain 2|||Mitochondrial-binding peptide (MBP) ^@ http://purl.uniprot.org/annotation/PRO_0000299036 http://togogenome.org/gene/10090:Calr3 ^@ http://purl.uniprot.org/uniprot/Q9D9Q6 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||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-3|||N-domain|||N-linked (GlcNAc...) asparagine|||P-domain|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000004179 http://togogenome.org/gene/10090:Nr0b2 ^@ http://purl.uniprot.org/uniprot/Q62227 ^@ 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 ^@ NR LBD|||Nuclear receptor subfamily 0 group B member 2|||Symmetric dimethylarginine; by PRMT5 ^@ http://purl.uniprot.org/annotation/PRO_0000053753 http://togogenome.org/gene/10090:Rnf214 ^@ http://purl.uniprot.org/uniprot/Q8BFU3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Polar residues|||RING finger protein 214|||RING-type; atypical|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000280547|||http://purl.uniprot.org/annotation/VSP_023773|||http://purl.uniprot.org/annotation/VSP_023774|||http://purl.uniprot.org/annotation/VSP_023775|||http://purl.uniprot.org/annotation/VSP_023776 http://togogenome.org/gene/10090:Cnpy1 ^@ http://purl.uniprot.org/uniprot/Q4VAB4|||http://purl.uniprot.org/uniprot/Q8CBI6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Non-terminal Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Protein canopy homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000314016|||http://purl.uniprot.org/annotation/VSP_030193 http://togogenome.org/gene/10090:Abcc4 ^@ http://purl.uniprot.org/uniprot/E9Q236|||http://purl.uniprot.org/uniprot/E9Q467 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ 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|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||PDZ-binding|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000452319|||http://purl.uniprot.org/annotation/VSP_060951|||http://purl.uniprot.org/annotation/VSP_060952 http://togogenome.org/gene/10090:Hid1 ^@ http://purl.uniprot.org/uniprot/Q3UU20|||http://purl.uniprot.org/uniprot/Q8R1F6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Protein HID1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000079297|||http://purl.uniprot.org/annotation/VSP_014474 http://togogenome.org/gene/10090:Cphx1 ^@ http://purl.uniprot.org/uniprot/Q8BX39 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Tmem86a ^@ http://purl.uniprot.org/uniprot/Q9D8N3 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Lysoplasmalogenase TMEM86A|||Reduced lysoplasmalogenase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000201839 http://togogenome.org/gene/10090:Mavs ^@ http://purl.uniprot.org/uniprot/Q3U5B1|||http://purl.uniprot.org/uniprot/Q8VCF0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Asymmetric dimethylarginine|||CARD|||Cleavage; by CASP3|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Interaction with DHX33|||Interaction with TRAF2|||Interaction with TRAF6 1|||Interaction with TRAF6 2|||Mitochondrial antiviral-signaling protein|||Mitochondrial intermembrane|||Phosphoserine|||Phosphoserine; by TBK1|||Polar residues|||Required for interaction with NLRX1|||pLxIS motif ^@ http://purl.uniprot.org/annotation/PRO_0000144097 http://togogenome.org/gene/10090:Rspo4 ^@ http://purl.uniprot.org/uniprot/Q0P5Y9|||http://purl.uniprot.org/uniprot/Q8BJ73 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ Basic residues|||Disordered|||FU|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||R-spondin Fu-CRD|||R-spondin-4|||TSP type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000234447|||http://purl.uniprot.org/annotation/PRO_5004175354|||http://purl.uniprot.org/annotation/VSP_018326|||http://purl.uniprot.org/annotation/VSP_018327 http://togogenome.org/gene/10090:Apob ^@ http://purl.uniprot.org/uniprot/E9Q414 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Apolipoprotein B-100|||Apolipoprotein B-48|||Basic (possible receptor binding region)|||Heparin-binding|||LDL receptor binding|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine|||Vitellogenin ^@ http://purl.uniprot.org/annotation/PRO_0000420969|||http://purl.uniprot.org/annotation/PRO_0000420970 http://togogenome.org/gene/10090:Skint11 ^@ http://purl.uniprot.org/uniprot/A2A9I2|||http://purl.uniprot.org/uniprot/A7XV14|||http://purl.uniprot.org/uniprot/Q8C9B4 ^@ 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|||Selection and upkeep of intraepithelial T-cells protein 11 ^@ http://purl.uniprot.org/annotation/PRO_5000271645 http://togogenome.org/gene/10090:Speer4a ^@ http://purl.uniprot.org/uniprot/F8VPX6|||http://purl.uniprot.org/uniprot/Q9D9V5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Eif2s2 ^@ http://purl.uniprot.org/uniprot/Q3ULL5|||http://purl.uniprot.org/uniprot/Q99L45 ^@ 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 ^@ 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_0000137407 http://togogenome.org/gene/10090:Lrrc66 ^@ http://purl.uniprot.org/uniprot/Q8K0B3 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Transmembrane ^@ Disordered|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Leucine-rich repeat-containing protein 66|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000329434 http://togogenome.org/gene/10090:Wfs1 ^@ http://purl.uniprot.org/uniprot/P56695|||http://purl.uniprot.org/uniprot/Q3TDI2|||http://purl.uniprot.org/uniprot/Q3UN10 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Interaction with ATP6V1A|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Wolframin|||Wolframin EF-hand|||Wolframin OB-fold|||Wolframin cysteine-rich ^@ http://purl.uniprot.org/annotation/PRO_0000065964 http://togogenome.org/gene/10090:Dync2i2 ^@ http://purl.uniprot.org/uniprot/Q5U4F6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Region|||Repeat ^@ Cytoplasmic dynein 2 intermediate chain 2|||DYNLL2 binding|||DYNLRB1 binding|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000223621 http://togogenome.org/gene/10090:Pdcd2l ^@ http://purl.uniprot.org/uniprot/Q8C5N5 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylalanine|||Programmed cell death protein 2-like|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000272646 http://togogenome.org/gene/10090:Lef1 ^@ http://purl.uniprot.org/uniprot/P27782|||http://purl.uniprot.org/uniprot/Q3TYB0|||http://purl.uniprot.org/uniprot/Q8BGZ9|||http://purl.uniprot.org/uniprot/Q8C402 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||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|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||CTNNB1-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||HMG box|||In isoform 2.|||Lymphoid enhancer-binding factor 1|||Phosphoserine|||Phosphoserine; by NLK|||Phosphothreonine; by NLK|||Prevents nuclear translocation of CTNNB1.|||Strongly diminishes CTNNB1 binding and transactivation. Prevents nuclear translocation of CTNNB1. ^@ http://purl.uniprot.org/annotation/PRO_0000048596|||http://purl.uniprot.org/annotation/VSP_006983 http://togogenome.org/gene/10090:Fundc1 ^@ http://purl.uniprot.org/uniprot/Q9DB70 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Motif|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||FUN14 domain-containing protein 1|||Helical|||Mitochondrial intermembrane|||Phosphoserine|||Phosphotyrosine; by SRC|||YXXL ^@ http://purl.uniprot.org/annotation/PRO_0000271346 http://togogenome.org/gene/10090:Or13a21 ^@ http://purl.uniprot.org/uniprot/Q8VGT4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nap1l5 ^@ http://purl.uniprot.org/uniprot/Q9JJF0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Nucleosome assembly protein 1-like 5 ^@ http://purl.uniprot.org/annotation/PRO_0000317143 http://togogenome.org/gene/10090:Prl7c1 ^@ http://purl.uniprot.org/uniprot/A0A0M6L0E8|||http://purl.uniprot.org/uniprot/Q9CRB5 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prolactin-7C1 ^@ http://purl.uniprot.org/annotation/PRO_0000045151|||http://purl.uniprot.org/annotation/PRO_5015043315 http://togogenome.org/gene/10090:Lpcat2b ^@ http://purl.uniprot.org/uniprot/B2RT16|||http://purl.uniprot.org/uniprot/Q9D5U0 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Transmembrane ^@ EF-hand|||EF-hand 1|||EF-hand 2|||HXXXXD motif|||Helical|||Lysophosphatidylcholine acyltransferase 2B|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000247061 http://togogenome.org/gene/10090:Mllt10 ^@ http://purl.uniprot.org/uniprot/A2AS70|||http://purl.uniprot.org/uniprot/O54826 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ C2HC pre-PHD-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Leucine-zipper|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues|||Protein AF-10|||Required for interaction with histone H3 ^@ http://purl.uniprot.org/annotation/PRO_0000215936 http://togogenome.org/gene/10090:Or8d2b ^@ http://purl.uniprot.org/uniprot/Q9EQ98 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Inhbc ^@ http://purl.uniprot.org/uniprot/P55104|||http://purl.uniprot.org/uniprot/Q3V2A6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Inhibin beta C chain|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033732|||http://purl.uniprot.org/annotation/PRO_0000033733 http://togogenome.org/gene/10090:Pax1 ^@ http://purl.uniprot.org/uniprot/P09084 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant ^@ Chain|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant ^@ Disordered|||In un.|||PAI subdomain|||Paired|||Paired box protein Pax-1|||RED subdomain ^@ http://purl.uniprot.org/annotation/PRO_0000050173 http://togogenome.org/gene/10090:Cdc6 ^@ http://purl.uniprot.org/uniprot/A0A0R4J145|||http://purl.uniprot.org/uniprot/O89033 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ AAA+ ATPase|||Basic and acidic residues|||Cdc6 C-terminal|||Cell division control protein 6 homolog|||Cy|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000150980 http://togogenome.org/gene/10090:Wnt8a ^@ http://purl.uniprot.org/uniprot/Q0VBT1|||http://purl.uniprot.org/uniprot/Q64527 ^@ 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|||Protein Wnt|||Protein Wnt-8a ^@ http://purl.uniprot.org/annotation/PRO_0000041449|||http://purl.uniprot.org/annotation/PRO_5014306866 http://togogenome.org/gene/10090:Plagl2 ^@ http://purl.uniprot.org/uniprot/Q925T4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type ^@ http://togogenome.org/gene/10090:Atp6ap2 ^@ http://purl.uniprot.org/uniprot/Q1XID4|||http://purl.uniprot.org/uniprot/Q9CYN9 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Motif|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cleavage; by furin-like protease|||Cytoplasmic|||Extracellular|||Helical|||Mediates retrograde transport to the ER|||Renin receptor|||Renin receptor cytoplasmic fragment|||Renin receptor extracellular fragment ^@ http://purl.uniprot.org/annotation/PRO_0000022204|||http://purl.uniprot.org/annotation/PRO_0000447866|||http://purl.uniprot.org/annotation/PRO_0000447867|||http://purl.uniprot.org/annotation/PRO_5009970243 http://togogenome.org/gene/10090:Prkar2a ^@ http://purl.uniprot.org/uniprot/Q8K1M3 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Cyclic nucleotide-binding|||Disordered ^@ http://togogenome.org/gene/10090:Tm2d3 ^@ http://purl.uniprot.org/uniprot/Q8BJ83 ^@ 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.|||N-linked (GlcNAc...) asparagine|||TM2 domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000298990|||http://purl.uniprot.org/annotation/VSP_027497 http://togogenome.org/gene/10090:Lrrc32 ^@ http://purl.uniprot.org/uniprot/G3XA59 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||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 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 LRRC32 ^@ http://purl.uniprot.org/annotation/PRO_0000445577 http://togogenome.org/gene/10090:Tlr13 ^@ http://purl.uniprot.org/uniprot/Q6R5N8 ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||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 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 22|||LRR 23|||LRR 24|||LRR 25|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||N-linked (GlcNAc...) asparagine|||TIR|||Toll-like receptor 13 ^@ http://purl.uniprot.org/annotation/PRO_0000042795 http://togogenome.org/gene/10090:Nps ^@ http://purl.uniprot.org/uniprot/P0C0P8 ^@ Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Peptide|||Propeptide|||Signal Peptide ^@ Neuropeptide S ^@ http://purl.uniprot.org/annotation/PRO_0000042941|||http://purl.uniprot.org/annotation/PRO_0000042942 http://togogenome.org/gene/10090:Ift74 ^@ http://purl.uniprot.org/uniprot/B1AWG1|||http://purl.uniprot.org/uniprot/Q8BKE9 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Region ^@ Basic region|||Disordered|||Intraflagellar transport protein 74 homolog|||Omega-N-methylarginine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000084170 http://togogenome.org/gene/10090:Mrps34 ^@ http://purl.uniprot.org/uniprot/Q9JIK9 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict ^@ Chain|||Mutagenesis Site|||Sequence Conflict ^@ Decreases protein expression. Decreases mitochondrial ribosomal subunits and translationally competent mitoribosomes. Mutant mice show heart hypertrophy and liver steatosis.|||Small ribosomal subunit protein mS34 ^@ http://purl.uniprot.org/annotation/PRO_0000087731 http://togogenome.org/gene/10090:Abr ^@ http://purl.uniprot.org/uniprot/A0A2X0U2A7|||http://purl.uniprot.org/uniprot/E9PUE7|||http://purl.uniprot.org/uniprot/Q5SSL4 ^@ 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 ^@ Active breakpoint cluster region-related protein|||C2|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Polar residues|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000355539|||http://purl.uniprot.org/annotation/VSP_035903|||http://purl.uniprot.org/annotation/VSP_035904|||http://purl.uniprot.org/annotation/VSP_035905|||http://purl.uniprot.org/annotation/VSP_035906 http://togogenome.org/gene/10090:Slc5a6 ^@ http://purl.uniprot.org/uniprot/Q3TY45|||http://purl.uniprot.org/uniprot/Q5U4D8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Sodium-dependent multivitamin transporter ^@ http://purl.uniprot.org/annotation/PRO_0000105387 http://togogenome.org/gene/10090:Cd46 ^@ http://purl.uniprot.org/uniprot/O88174 ^@ 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|||In isoform 2.|||Membrane cofactor protein|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4 ^@ http://purl.uniprot.org/annotation/PRO_0000238971|||http://purl.uniprot.org/annotation/VSP_019038|||http://purl.uniprot.org/annotation/VSP_019039 http://togogenome.org/gene/10090:Timm23 ^@ http://purl.uniprot.org/uniprot/Q9CXU4 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Or10v1 ^@ http://purl.uniprot.org/uniprot/Q8VF55 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gipc1 ^@ http://purl.uniprot.org/uniprot/Q9Z0G0 ^@ 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|||PDZ|||PDZ domain-containing protein GIPC1|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000087493 http://togogenome.org/gene/10090:Dok4 ^@ http://purl.uniprot.org/uniprot/Q99KE3 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Motif ^@ DKFBH motif|||Docking protein 4|||IRS-type PTB|||PH ^@ http://purl.uniprot.org/annotation/PRO_0000187275 http://togogenome.org/gene/10090:Shank2 ^@ http://purl.uniprot.org/uniprot/D3Z5K8|||http://purl.uniprot.org/uniprot/Q80Z38 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||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_0000247760|||http://purl.uniprot.org/annotation/VSP_020040|||http://purl.uniprot.org/annotation/VSP_041614|||http://purl.uniprot.org/annotation/VSP_041615 http://togogenome.org/gene/10090:Grhl1 ^@ http://purl.uniprot.org/uniprot/E9QMF0|||http://purl.uniprot.org/uniprot/Q921D9 ^@ 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|||Grainyhead-like protein 1 homolog|||Grh/CP2 DB|||In isoform 2.|||Interaction with DNA|||Phosphothreonine|||Transcription activation ^@ http://purl.uniprot.org/annotation/PRO_0000227991|||http://purl.uniprot.org/annotation/VSP_017640|||http://purl.uniprot.org/annotation/VSP_017641 http://togogenome.org/gene/10090:Pan2 ^@ http://purl.uniprot.org/uniprot/Q8BGF7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Exonuclease|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Linker|||PAN2-PAN3 deadenylation complex catalytic subunit Pan2|||Phosphoserine|||USP|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000280522|||http://purl.uniprot.org/annotation/VSP_023750|||http://purl.uniprot.org/annotation/VSP_023751|||http://purl.uniprot.org/annotation/VSP_023752 http://togogenome.org/gene/10090:Kcnq3 ^@ http://purl.uniprot.org/uniprot/Q8K3F6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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|||Mediates interaction with calmodulin|||Phosphothreonine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily KQT member 3|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054035 http://togogenome.org/gene/10090:Glrb ^@ http://purl.uniprot.org/uniprot/A1KR23|||http://purl.uniprot.org/uniprot/P48168 ^@ 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|||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|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Glycine receptor subunit beta|||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 spastic 1.|||In spastic 2.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000000424|||http://purl.uniprot.org/annotation/PRO_5015085912 http://togogenome.org/gene/10090:Neil3 ^@ http://purl.uniprot.org/uniprot/Q8K203 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Disordered|||Endonuclease 8-like 3|||FPG-type|||GRF-type 1|||GRF-type 2|||Important for monofunctional glycosylase activity|||In isoform 2.|||In strain: Czech II.|||Phosphoserine|||Polar residues|||RanBP2-type|||Removed|||Required for glycosylase activity|||Schiff-base intermediate with DNA; via amino nitrogen ^@ http://purl.uniprot.org/annotation/PRO_0000170911|||http://purl.uniprot.org/annotation/VSP_012210 http://togogenome.org/gene/10090:Cfap45 ^@ http://purl.uniprot.org/uniprot/Q9D9U9 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Cilia- and flagella-associated protein 45|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000454202 http://togogenome.org/gene/10090:Ppp3cc ^@ http://purl.uniprot.org/uniprot/A0A2I3BPC5|||http://purl.uniprot.org/uniprot/P48455|||http://purl.uniprot.org/uniprot/Q80XK0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Motif|||Non-terminal Residue|||Region ^@ Autoinhibitory domain|||Autoinhibitory segment|||Calcineurin B binding|||Calmodulin-binding|||Catalytic|||Disordered|||Proton donor|||SAPNY motif|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform ^@ http://purl.uniprot.org/annotation/PRO_0000058829 http://togogenome.org/gene/10090:Mrps15 ^@ http://purl.uniprot.org/uniprot/Q9DC71 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||Small ribosomal subunit protein uS15m ^@ http://purl.uniprot.org/annotation/PRO_0000030615 http://togogenome.org/gene/10090:Serpinb9d ^@ http://purl.uniprot.org/uniprot/O08801|||http://purl.uniprot.org/uniprot/Q8BMT0 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ Serpin ^@ http://togogenome.org/gene/10090:Rxfp4 ^@ http://purl.uniprot.org/uniprot/Q5Y985|||http://purl.uniprot.org/uniprot/Q7TQP4 ^@ 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|||Relaxin-3 receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000070107 http://togogenome.org/gene/10090:Sectm1a ^@ http://purl.uniprot.org/uniprot/A2ABP9 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015086013 http://togogenome.org/gene/10090:Fbxl15 ^@ http://purl.uniprot.org/uniprot/Q91W61 ^@ 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_0000119932 http://togogenome.org/gene/10090:Mfrp ^@ http://purl.uniprot.org/uniprot/Q8K480 ^@ 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 ^@ CUB 1|||CUB 2|||Cytoplasmic|||Disordered|||Extracellular|||FZ|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||LDL-receptor class A 1|||LDL-receptor class A 2|||Membrane frizzled-related protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000228133|||http://purl.uniprot.org/annotation/VSP_017664 http://togogenome.org/gene/10090:Or7a36 ^@ http://purl.uniprot.org/uniprot/Q8VGX5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rab9 ^@ http://purl.uniprot.org/uniprot/Q9R0M6 ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Strand|||Turn ^@ Effector region|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Ras-related protein Rab-9A|||Removed|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121140 http://togogenome.org/gene/10090:Tnf ^@ http://purl.uniprot.org/uniprot/A0A0R4J210|||http://purl.uniprot.org/uniprot/P06804|||http://purl.uniprot.org/uniprot/Q3U593 ^@ Chain|||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|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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|||In strain: BALB/c and C57BL/6.|||Intracellular domain 1|||Intracellular domain 2|||N-linked (GlcNAc...) asparagine|||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_0000034435|||http://purl.uniprot.org/annotation/PRO_0000034436|||http://purl.uniprot.org/annotation/PRO_0000417255|||http://purl.uniprot.org/annotation/PRO_0000417256|||http://purl.uniprot.org/annotation/PRO_0000417257|||http://purl.uniprot.org/annotation/PRO_0000417258 http://togogenome.org/gene/10090:Rhox2b ^@ http://purl.uniprot.org/uniprot/A2A447 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Nhs ^@ http://purl.uniprot.org/uniprot/B1AV60|||http://purl.uniprot.org/uniprot/B9EJX2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Bap1 ^@ http://purl.uniprot.org/uniprot/Q99PU7 ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Abolishes ability to suppress tumorigenicity when expressed in NCI-H226 cells.|||Basic and acidic residues|||Basic residues|||Disordered|||HBM-like motif|||Important for enzyme activity|||Interaction with BRCA1|||Nuclear localization signal|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton donor|||Ubiquitin carboxyl-terminal hydrolase BAP1 ^@ http://purl.uniprot.org/annotation/PRO_0000211070 http://togogenome.org/gene/10090:Tcerg1 ^@ http://purl.uniprot.org/uniprot/Q3TH57|||http://purl.uniprot.org/uniprot/Q8CGF7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||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|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn ^@ Asymmetric dimethylarginine|||Basic and acidic 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.|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Transcription elongation regulator 1|||WW|||WW 1|||WW 2|||WW 3 ^@ http://purl.uniprot.org/annotation/PRO_0000076064|||http://purl.uniprot.org/annotation/VSP_011655|||http://purl.uniprot.org/annotation/VSP_011656|||http://purl.uniprot.org/annotation/VSP_011657 http://togogenome.org/gene/10090:Nupr1 ^@ http://purl.uniprot.org/uniprot/Q9WTK0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Nuclear localization signal|||Nuclear protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000058008 http://togogenome.org/gene/10090:Vmn1r120 ^@ http://purl.uniprot.org/uniprot/K7N6J6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clec7a ^@ http://purl.uniprot.org/uniprot/V9GXI5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:A1bg ^@ http://purl.uniprot.org/uniprot/Q19LI2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Alpha-1B-glycoprotein|||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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000355542 http://togogenome.org/gene/10090:Hspa4l ^@ http://purl.uniprot.org/uniprot/P48722 ^@ 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 4L|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000078281|||http://purl.uniprot.org/annotation/VSP_007500 http://togogenome.org/gene/10090:Kif20b ^@ http://purl.uniprot.org/uniprot/Q80WE4 ^@ 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 ^@ Binding Site|||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 and isoform 3.|||In isoform 2.|||In isoform 4.|||Interaction with PIN1|||Kinesin motor|||Kinesin-like protein KIF20B|||Necessary and sufficient for interaction with SHTN1|||Phosphoserine|||Phosphothreonine; by CDK1|||Polar residues|||Reduces interaction with SHTN1; when associated with A-1048.|||Reduces interaction with SHTN1; when associated with F-1047. ^@ http://purl.uniprot.org/annotation/PRO_0000274054|||http://purl.uniprot.org/annotation/VSP_022623|||http://purl.uniprot.org/annotation/VSP_022624|||http://purl.uniprot.org/annotation/VSP_022625|||http://purl.uniprot.org/annotation/VSP_022626 http://togogenome.org/gene/10090:Frmd4b ^@ http://purl.uniprot.org/uniprot/Q6ZQ04|||http://purl.uniprot.org/uniprot/Q8C0E8|||http://purl.uniprot.org/uniprot/Q920B0 ^@ 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 ^@ Basic and acidic residues|||Cytohesin Ubiquitin Protein Inducing|||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_0000219447|||http://purl.uniprot.org/annotation/VSP_040896 http://togogenome.org/gene/10090:Ptchd4 ^@ http://purl.uniprot.org/uniprot/B9EKX1|||http://purl.uniprot.org/uniprot/E9QMK6 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Patched domain-containing protein 4|||SSD ^@ http://purl.uniprot.org/annotation/PRO_0000389444 http://togogenome.org/gene/10090:AU015228 ^@ http://purl.uniprot.org/uniprot/Q3TQQ1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||HTH TFE/IIEalpha-type ^@ http://togogenome.org/gene/10090:Slc30a3 ^@ http://purl.uniprot.org/uniprot/P97441|||http://purl.uniprot.org/uniprot/Q3TMQ7|||http://purl.uniprot.org/uniprot/Q6NZC3|||http://purl.uniprot.org/uniprot/S4R169 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Phosphoserine|||Polar residues|||Probable proton-coupled zinc antiporter SLC30A3 ^@ http://purl.uniprot.org/annotation/PRO_0000206097 http://togogenome.org/gene/10090:Prr15l ^@ http://purl.uniprot.org/uniprot/Q8JZM2 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Proline-rich protein 15-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000294353 http://togogenome.org/gene/10090:Pfkfb2 ^@ http://purl.uniprot.org/uniprot/B2Z892|||http://purl.uniprot.org/uniprot/B2Z893|||http://purl.uniprot.org/uniprot/P70265|||http://purl.uniprot.org/uniprot/Q6GTL7|||http://purl.uniprot.org/uniprot/Q8CDS6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ 6-phosphofructo-2-kinase|||6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2|||Disordered|||Fructose-2,6-bisphosphatase|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by PKC|||Polar residues|||Proton donor/acceptor|||Removed|||Tele-phosphohistidine intermediate|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000179965 http://togogenome.org/gene/10090:Scgb1b2 ^@ http://purl.uniprot.org/uniprot/O35176 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015096772 http://togogenome.org/gene/10090:Nav1 ^@ http://purl.uniprot.org/uniprot/Q8CH77 ^@ 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 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Neuron navigator 1|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000286975|||http://purl.uniprot.org/annotation/VSP_025260|||http://purl.uniprot.org/annotation/VSP_025261|||http://purl.uniprot.org/annotation/VSP_025262|||http://purl.uniprot.org/annotation/VSP_025263|||http://purl.uniprot.org/annotation/VSP_025264|||http://purl.uniprot.org/annotation/VSP_025265|||http://purl.uniprot.org/annotation/VSP_025266|||http://purl.uniprot.org/annotation/VSP_025267 http://togogenome.org/gene/10090:Krt83 ^@ http://purl.uniprot.org/uniprot/E9Q1Y9 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ IF rod ^@ http://togogenome.org/gene/10090:Or2ag1b ^@ http://purl.uniprot.org/uniprot/K7N641 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc25a29 ^@ http://purl.uniprot.org/uniprot/Q8BL03 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Transmembrane ^@ Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial basic amino acids transporter|||Polar residues|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090633 http://togogenome.org/gene/10090:Serpinb1a ^@ http://purl.uniprot.org/uniprot/Q9D154 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ CARD-binding motif (CBM)|||Leukocyte elastase inhibitor A|||Phosphoserine|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000289120 http://togogenome.org/gene/10090:Cyp26a1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J061|||http://purl.uniprot.org/uniprot/O55127 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Cytochrome P450 26A1|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051981 http://togogenome.org/gene/10090:Sult2a8 ^@ http://purl.uniprot.org/uniprot/Q8BGL3 ^@ 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 ^@ Decreases sulfotransferase activity (at pH 6.27).|||Decreases sulfotransferase activity (at pH 6.27). Does not affect sulfotransferase activity (at pH 7.5).|||Decreases sulfotransferase activity (at pH 7.5).|||Has little effect on sulfotransferase activity (at pH 7.5).|||Impairs sulfotransferase activity.|||In isoform 2.|||Increases sulfotransferase activity (at pH 7.5).|||Increases sulfotransferase activity.|||Loss of sulfotransferase activity (at pH 7.5).|||Markedly decreases enzyme stability, both apo and ligand-bound forms. Markedly decreases sulfotransferase activity (at pH 7.5).|||Proton acceptor|||Sulfotransferase 2A8 ^@ http://purl.uniprot.org/annotation/PRO_0000453530|||http://purl.uniprot.org/annotation/VSP_061163 http://togogenome.org/gene/10090:Arhgap39 ^@ http://purl.uniprot.org/uniprot/G3X932|||http://purl.uniprot.org/uniprot/H7BX46|||http://purl.uniprot.org/uniprot/P59281 ^@ 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 ^@ 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_0000076093|||http://purl.uniprot.org/annotation/VSP_013707 http://togogenome.org/gene/10090:Tarsl2 ^@ http://purl.uniprot.org/uniprot/Q8BLY2 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes nuclear localization.|||Disordered|||Impairs aminoacylation activity.|||Impairs post-transfer editing activity but no effect on aminoacylation activity; when associated with A-222.|||Impairs post-transfer editing activity but no effect on aminoacylation activity; when associated with A-226.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Removed|||TGS|||Threonine--tRNA ligase 2, cytoplasmic ^@ http://purl.uniprot.org/annotation/PRO_0000333829 http://togogenome.org/gene/10090:Cyp3a59 ^@ http://purl.uniprot.org/uniprot/D3Z2W7 ^@ Binding Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Transmembrane ^@ Helical|||axial binding residue ^@ http://togogenome.org/gene/10090:Nup98 ^@ http://purl.uniprot.org/uniprot/A0A140T8J8|||http://purl.uniprot.org/uniprot/A0A1B0GRA7|||http://purl.uniprot.org/uniprot/A0A1B0GRB5|||http://purl.uniprot.org/uniprot/A0A1B0GSX7|||http://purl.uniprot.org/uniprot/B2RQL0|||http://purl.uniprot.org/uniprot/Q3TPG3|||http://purl.uniprot.org/uniprot/Q3UJE5|||http://purl.uniprot.org/uniprot/Q4FZE7|||http://purl.uniprot.org/uniprot/Q6PFD9 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Site|||Strand|||Turn ^@ Basic and acidic residues|||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|||N6-acetyllysine; alternate|||Nuclear pore complex protein Nup96|||Nuclear pore complex protein Nup98|||Nucleophile|||Peptidase S59|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces interaction with NUP88. ^@ http://purl.uniprot.org/annotation/PRO_0000421837|||http://purl.uniprot.org/annotation/PRO_0000421838 http://togogenome.org/gene/10090:Ubqln2 ^@ http://purl.uniprot.org/uniprot/Q9QZM0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||10|||11|||11 X 3 AA tandem repeats P-X-X|||2|||3|||4|||5|||6|||7|||8|||9|||Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||STI1 1|||STI1 2|||STI1 3|||STI1 4|||UBA|||Ubiquilin-2|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000211012 http://togogenome.org/gene/10090:Pstpip1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0P5|||http://purl.uniprot.org/uniprot/P97814 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ Complete loss of protein phosphorylation.|||F-BAR|||No effect on phosphorylation.|||Phosphoserine|||Phosphotyrosine; by ABL1|||Proline-serine-threonine phosphatase-interacting protein 1|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000058540 http://togogenome.org/gene/10090:Apcdd1 ^@ http://purl.uniprot.org/uniprot/Q3U128 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protein APCDD1 ^@ http://purl.uniprot.org/annotation/PRO_0000227521 http://togogenome.org/gene/10090:Ube2b ^@ http://purl.uniprot.org/uniprot/A2RSE4|||http://purl.uniprot.org/uniprot/P63147 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Glycyl thioester intermediate|||UBC core|||Ubiquitin-conjugating enzyme E2 B ^@ http://purl.uniprot.org/annotation/PRO_0000082448 http://togogenome.org/gene/10090:Mrps18b ^@ http://purl.uniprot.org/uniprot/Q542W5|||http://purl.uniprot.org/uniprot/Q99N84 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Transit Peptide ^@ Disordered|||In isoform 2.|||Mitochondrion|||Phosphoserine|||Polar residues|||Small ribosomal subunit protein mS40 ^@ http://purl.uniprot.org/annotation/PRO_0000030628|||http://purl.uniprot.org/annotation/VSP_005723 http://togogenome.org/gene/10090:Il22 ^@ http://purl.uniprot.org/uniprot/Q9JJY9 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Signal Peptide|||Strand|||Turn ^@ Interleukin-22|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015384 http://togogenome.org/gene/10090:Praf2 ^@ http://purl.uniprot.org/uniprot/Q9JIG8 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||PRA1 family protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000220882 http://togogenome.org/gene/10090:Vsig10 ^@ http://purl.uniprot.org/uniprot/D3YX43 ^@ 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 ^@ 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|||N-linked (GlcNAc...) asparagine|||V-set and immunoglobulin domain-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000395114 http://togogenome.org/gene/10090:Adgre5 ^@ http://purl.uniprot.org/uniprot/A0A0D9SEG8|||http://purl.uniprot.org/uniprot/E9QJS7|||http://purl.uniprot.org/uniprot/E9QMJ5|||http://purl.uniprot.org/uniprot/Q9DC42|||http://purl.uniprot.org/uniprot/Q9Z0M6 ^@ Chain|||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 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||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|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; 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|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000012869|||http://purl.uniprot.org/annotation/PRO_0000435126|||http://purl.uniprot.org/annotation/PRO_0000435127|||http://purl.uniprot.org/annotation/PRO_5002346888|||http://purl.uniprot.org/annotation/PRO_5003244809|||http://purl.uniprot.org/annotation/PRO_5003246388|||http://purl.uniprot.org/annotation/PRO_5015099681|||http://purl.uniprot.org/annotation/VSP_009413|||http://purl.uniprot.org/annotation/VSP_009414 http://togogenome.org/gene/10090:Slc35a4 ^@ http://purl.uniprot.org/uniprot/Q9D321 ^@ 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_0000337749 http://togogenome.org/gene/10090:Clec4a1 ^@ http://purl.uniprot.org/uniprot/Q80UI7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Pgap3 ^@ http://purl.uniprot.org/uniprot/A2A559 ^@ 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|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Post-GPI attachment to proteins factor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000339357|||http://purl.uniprot.org/annotation/VSP_034159 http://togogenome.org/gene/10090:Cct6b ^@ http://purl.uniprot.org/uniprot/Q61390 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ T-complex protein 1 subunit zeta-2 ^@ http://purl.uniprot.org/annotation/PRO_0000128364 http://togogenome.org/gene/10090:Rps6ka5 ^@ http://purl.uniprot.org/uniprot/Q3TUH8|||http://purl.uniprot.org/uniprot/Q8C050 ^@ 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|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ AGC-kinase C-terminal|||Disordered|||In isoform 1.|||Phosphoserine|||Phosphoserine; by MAPK1, MAPK3 and MAPK14|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by MAPK1, MAPK3 and MAPK14|||Polar residues|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Ribosomal protein S6 kinase alpha-5 ^@ http://purl.uniprot.org/annotation/PRO_0000086208|||http://purl.uniprot.org/annotation/VSP_050613 http://togogenome.org/gene/10090:Xlr3b ^@ http://purl.uniprot.org/uniprot/Q6P205 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||X-linked lymphocyte-regulated protein 3B ^@ http://purl.uniprot.org/annotation/PRO_0000361653 http://togogenome.org/gene/10090:Fgf9 ^@ http://purl.uniprot.org/uniprot/P54130 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict ^@ Chain|||Glycosylation Site|||Propeptide|||Sequence Conflict ^@ Fibroblast growth factor 9|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000008975|||http://purl.uniprot.org/annotation/PRO_0000008976 http://togogenome.org/gene/10090:Cfap157 ^@ http://purl.uniprot.org/uniprot/Q0VFX2 ^@ 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|||Cilia- and flagella-associated protein 157|||Disordered|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000307225 http://togogenome.org/gene/10090:Gm20908 ^@ http://purl.uniprot.org/uniprot/A0A087WRK1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Zmym1 ^@ http://purl.uniprot.org/uniprot/Q3TJB1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ TRASH ^@ http://togogenome.org/gene/10090:Atp8a1 ^@ http://purl.uniprot.org/uniprot/A0A0M3HEP7|||http://purl.uniprot.org/uniprot/P70704|||http://purl.uniprot.org/uniprot/Q3U9N5|||http://purl.uniprot.org/uniprot/Q52KQ7|||http://purl.uniprot.org/uniprot/Q8CA15 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cleavage; by calpain|||Cytoplasmic|||Decreases plasma membrane aminophospholipid translocation in neuronal cells.|||Exoplasmic loop|||Helical|||In isoform 2 and isoform 3.|||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|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Phospholipid-transporting ATPase IA|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000046361|||http://purl.uniprot.org/annotation/VSP_055306|||http://purl.uniprot.org/annotation/VSP_055307 http://togogenome.org/gene/10090:Lrp3 ^@ http://purl.uniprot.org/uniprot/E9Q1T6|||http://purl.uniprot.org/uniprot/E9Q711|||http://purl.uniprot.org/uniprot/Q3UEV4|||http://purl.uniprot.org/uniprot/Q52KH0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||CUB|||CUB domain-containing protein|||Disordered|||Helical|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5003243099|||http://purl.uniprot.org/annotation/PRO_5003245795|||http://purl.uniprot.org/annotation/PRO_5004230072 http://togogenome.org/gene/10090:Or52e18 ^@ http://purl.uniprot.org/uniprot/Q7TRP3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nlrp14 ^@ http://purl.uniprot.org/uniprot/Q6B966 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ 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 14 ^@ http://purl.uniprot.org/annotation/PRO_0000286339 http://togogenome.org/gene/10090:Creb1 ^@ http://purl.uniprot.org/uniprot/Q01147|||http://purl.uniprot.org/uniprot/Q543W0|||http://purl.uniprot.org/uniprot/Q547S9|||http://purl.uniprot.org/uniprot/Q62347 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Splice Variant ^@ Abolishes CREBBP binding.|||Attenuates light-induced phase shifts of locomotion and expression of c-Fos and mPer1 in the SCN.|||BZIP|||Basic motif|||Cyclic AMP-responsive element-binding protein 1|||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.|||KID|||Leucine-zipper|||Loss of phosphorylation by RPS6KA4 and RPS6KA5.|||Phosphoserine; by CaMK1, CaMK2, CaMK4, PKB/AKT1 or PKB/AKT2, RPS6KA3, RPS6KA4, RPS6KA5 and SGK1|||Phosphoserine; by CaMK2|||Phosphoserine; by HIPK2|||Required for binding TORCs|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076598|||http://purl.uniprot.org/annotation/VSP_060704 http://togogenome.org/gene/10090:Abcb6 ^@ http://purl.uniprot.org/uniprot/Q9DC29 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||ATP-binding cassette sub-family B member 6|||Cytoplasmic|||Helical|||Lumenal|||Required for ATPase activity|||Required for the lysosomal targeting|||Results in retention of the protein in the Golgi apparatus. ^@ http://purl.uniprot.org/annotation/PRO_0000268678 http://togogenome.org/gene/10090:Tdrd1 ^@ http://purl.uniprot.org/uniprot/Q99MV1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Abolishes localization to meiotic nuage; when associated with K-1023.|||Abolishes localization to meiotic nuage; when associated with N-1019.|||Disordered|||MYND-type|||Polar residues|||Significantly reduced binding to symmetric dimethylarginines.|||Strongly enhanced binding to symmetric dimethylarginines.|||Strongly reduced binding to symmetric dimethylarginines.|||Tudor 1|||Tudor 2|||Tudor 3|||Tudor 4|||Tudor domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000183162 http://togogenome.org/gene/10090:Rasal1 ^@ http://purl.uniprot.org/uniprot/Q9Z268 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger ^@ Btk-type|||C2 1|||C2 2|||PH|||Phosphothreonine|||Ras-GAP|||RasGAP-activating-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000056646 http://togogenome.org/gene/10090:Xxylt1 ^@ http://purl.uniprot.org/uniprot/Q3U4G3 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes enzyme activity.|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Increases enzyme activity.|||Interaction with target proteins|||Lumenal|||No effect on enzyme activity.|||No significant effect on enzyme activity.|||Reduces enzyme activity.|||Slightly reduces enzyme activity.|||Strongly reduces enzyme activity.|||Xyloside xylosyltransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000234428 http://togogenome.org/gene/10090:Mrtfa ^@ http://purl.uniprot.org/uniprot/Q8K4J6 ^@ 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|||Splice Variant|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand ^@ Disordered|||Does not induce a nuclear accumulation in unstimulated cells.|||Impaired interaction with G-actin, leading to cytoplasmic accumulation.|||Impaired interaction with G-actin, leading to nuclear accumulation in unstimulated cells.|||In 123-1A: Reduced interaction with G-actin, leading to a constitutively active SRF-MRTFA complex; when associated with A-24 and A-112.|||In 123-1A: Reduced interaction with G-actin, leading to a constitutively active SRF-MRTFA complex; when associated with A-24 and A-68.|||In 123-1A: Reduced interaction with G-actin, leading to a constitutively active SRF-MRTFA complex; when associated with A-68 and A-112.|||In isoform 2.|||Induces a nuclear accumulation in unstimulated cells.|||Induces a nuclear decrease in unstimulated cells.|||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 1|||RPEL 2|||RPEL 3|||SAP ^@ http://purl.uniprot.org/annotation/PRO_0000126626|||http://purl.uniprot.org/annotation/VSP_007652 http://togogenome.org/gene/10090:Capn2 ^@ http://purl.uniprot.org/uniprot/O08529 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Propeptide|||Region|||Sequence Conflict ^@ Anchors to the small subunit|||Calpain catalytic|||Calpain-2 catalytic subunit|||Domain III|||Domain IV|||EF-hand 1|||EF-hand 2|||Linker|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000026491|||http://purl.uniprot.org/annotation/PRO_0000026492 http://togogenome.org/gene/10090:Pcdhgc5 ^@ http://purl.uniprot.org/uniprot/Q91XW9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (Man...) threonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099535 http://togogenome.org/gene/10090:Adcyap1r1 ^@ http://purl.uniprot.org/uniprot/E9Q3E8|||http://purl.uniprot.org/uniprot/E9Q968|||http://purl.uniprot.org/uniprot/P70205|||http://purl.uniprot.org/uniprot/Q6NXJ9 ^@ 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 ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pituitary adenylate cyclase-activating polypeptide type I receptor ^@ http://purl.uniprot.org/annotation/PRO_0000012842|||http://purl.uniprot.org/annotation/PRO_5003243079|||http://purl.uniprot.org/annotation/PRO_5003243126|||http://purl.uniprot.org/annotation/PRO_5015098390 http://togogenome.org/gene/10090:Ugt1a6a ^@ http://purl.uniprot.org/uniprot/Q64435 ^@ 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|||UDP-glucuronosyltransferase 1-6 ^@ http://purl.uniprot.org/annotation/PRO_0000036017 http://togogenome.org/gene/10090:Tia1 ^@ http://purl.uniprot.org/uniprot/G5E8L2|||http://purl.uniprot.org/uniprot/P52912|||http://purl.uniprot.org/uniprot/Q564E7|||http://purl.uniprot.org/uniprot/Q80ZW7|||http://purl.uniprot.org/uniprot/Q8CII5 ^@ 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 ^@ Cytotoxic granule associated RNA binding protein TIA1|||Disordered|||N-acetylmethionine|||Polar residues|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000081977 http://togogenome.org/gene/10090:Cd200 ^@ http://purl.uniprot.org/uniprot/Q80VX2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015098923 http://togogenome.org/gene/10090:Trpc6 ^@ http://purl.uniprot.org/uniprot/Q3UZG1|||http://purl.uniprot.org/uniprot/Q61143|||http://purl.uniprot.org/uniprot/Q6NV56 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Short transient receptor potential channel 6|||Transient receptor ion channel ^@ http://purl.uniprot.org/annotation/PRO_0000215323 http://togogenome.org/gene/10090:Scn3b ^@ http://purl.uniprot.org/uniprot/H3BJR6|||http://purl.uniprot.org/uniprot/Q0P666|||http://purl.uniprot.org/uniprot/Q8BHK2 ^@ 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|||Helical|||Ig-like|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||Sodium channel subunit beta-3 ^@ http://purl.uniprot.org/annotation/PRO_0000014935|||http://purl.uniprot.org/annotation/PRO_5014306818 http://togogenome.org/gene/10090:Rpp14 ^@ http://purl.uniprot.org/uniprot/Q9CQH8 ^@ Chain|||Molecule Processing ^@ Chain ^@ Ribonuclease P protein subunit p14 ^@ http://purl.uniprot.org/annotation/PRO_0000140011 http://togogenome.org/gene/10090:Gpr3 ^@ http://purl.uniprot.org/uniprot/P35413 ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||G-protein coupled receptor 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|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069511 http://togogenome.org/gene/10090:L1td1 ^@ http://purl.uniprot.org/uniprot/Q587J6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||LINE-1 type transposase domain-containing protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000307218 http://togogenome.org/gene/10090:Atp6v0c ^@ http://purl.uniprot.org/uniprot/A3KML5|||http://purl.uniprot.org/uniprot/P63082 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Essential for proton translocation|||Helical|||Lumenal|||V-ATPase proteolipid subunit C-like|||V-type proton ATPase 16 kDa proteolipid subunit c ^@ http://purl.uniprot.org/annotation/PRO_0000071744 http://togogenome.org/gene/10090:Get4 ^@ http://purl.uniprot.org/uniprot/Q9D1H7 ^@ 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|||Disordered|||Golgi to ER traffic protein 4 homolog|||In isoform 2.|||Interacts with BAG6|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000228105|||http://purl.uniprot.org/annotation/VSP_017653 http://togogenome.org/gene/10090:Sdr42e1 ^@ http://purl.uniprot.org/uniprot/Q9D665 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Transmembrane ^@ Helical|||Proton acceptor|||Short-chain dehydrogenase/reductase family 42E member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000331756 http://togogenome.org/gene/10090:Or52e8b ^@ http://purl.uniprot.org/uniprot/Q7TRP1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tgm4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J071|||http://purl.uniprot.org/uniprot/Q8BZH1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict ^@ N-linked (GlcNAc...) asparagine|||Protein-glutamine gamma-glutamyltransferase 4|||Transglutaminase-like ^@ http://purl.uniprot.org/annotation/PRO_0000385448 http://togogenome.org/gene/10090:Fgl1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0E1|||http://purl.uniprot.org/uniprot/Q71KU9 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ Fibrinogen C-terminal|||Fibrinogen-like protein 1|||Interchain ^@ http://purl.uniprot.org/annotation/PRO_0000322979|||http://purl.uniprot.org/annotation/PRO_5015044283 http://togogenome.org/gene/10090:Rps16 ^@ http://purl.uniprot.org/uniprot/P14131 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ N6-acetyllysine|||Phosphoserine|||Small ribosomal subunit protein uS9 ^@ http://purl.uniprot.org/annotation/PRO_0000111480 http://togogenome.org/gene/10090:D130043K22Rik ^@ http://purl.uniprot.org/uniprot/Q3UFC3|||http://purl.uniprot.org/uniprot/Q5SZV5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Dyslexia-associated protein KIAA0319 homolog|||Endocytosis signal|||Extracellular|||Helical|||MANSC|||N-linked (GlcNAc...) asparagine|||PKD|||PKD 1|||PKD 2|||PKD 3|||PKD 4|||PKD 5|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000042947 http://togogenome.org/gene/10090:Zbtb44 ^@ http://purl.uniprot.org/uniprot/A0A1L1SSL7|||http://purl.uniprot.org/uniprot/Q8R0A2 ^@ 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 ^@ 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)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger and BTB domain-containing protein 44 ^@ http://purl.uniprot.org/annotation/PRO_0000274609|||http://purl.uniprot.org/annotation/VSP_022838 http://togogenome.org/gene/10090:Ankar ^@ http://purl.uniprot.org/uniprot/A2RT91|||http://purl.uniprot.org/uniprot/B7ZNI2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Repeat|||Sequence Conflict|||Transmembrane ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ARM|||ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||Ankyrin and armadillo repeat-containing protein|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000286807 http://togogenome.org/gene/10090:Smpd5 ^@ http://purl.uniprot.org/uniprot/D6MZJ6 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Region|||Site|||Transmembrane ^@ Disordered|||Helical|||Important for substrate recognition|||Proton acceptor|||Sphingomyelin phosphodiesterase 5 ^@ http://purl.uniprot.org/annotation/PRO_0000451401 http://togogenome.org/gene/10090:Plekhm3 ^@ http://purl.uniprot.org/uniprot/Q8BM47 ^@ 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 ^@ In isoform 2.|||PH 1|||PH 2|||Phorbol-ester/DAG-type|||Phosphoserine|||Pleckstrin homology domain-containing family M member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000326035|||http://purl.uniprot.org/annotation/VSP_032514|||http://purl.uniprot.org/annotation/VSP_032515 http://togogenome.org/gene/10090:Irf6 ^@ http://purl.uniprot.org/uniprot/P97431 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disordered|||IRF tryptophan pentad repeat|||Interferon regulatory factor 6|||Mice show an atypical limb development, are covered by an abnormal smooth skin and die shortly after birth. The esophageal lumen is obliterated by adhesion of the stratified, squamous epithelium lining this structure. The hindlimbs, tail and body are fused together by a thickened epidermis. Epidermis is hyperproliferative but does not undergo a normal differentiation program. ^@ http://purl.uniprot.org/annotation/PRO_0000154561 http://togogenome.org/gene/10090:Hmgn5 ^@ http://purl.uniprot.org/uniprot/Q9JL35 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ 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|||May abolish association with nucleosomes; when associated with E-18.|||May abolish association with nucleosomes; when associated with E-22.|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000206718 http://togogenome.org/gene/10090:Gjc3 ^@ http://purl.uniprot.org/uniprot/Q921C1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Gap junction gamma-3 protein|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000354706 http://togogenome.org/gene/10090:Deaf1 ^@ http://purl.uniprot.org/uniprot/Q3TYJ5|||http://purl.uniprot.org/uniprot/Q80V49|||http://purl.uniprot.org/uniprot/Q9Z1T5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger ^@ Abolishes nuclear localization.|||Acidic residues|||Deformed epidermal autoregulatory factor 1 homolog|||Disordered|||In isoform 2.|||Interaction with LMO4|||MYND-type|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||SAND ^@ http://purl.uniprot.org/annotation/PRO_0000074085|||http://purl.uniprot.org/annotation/VSP_038703|||http://purl.uniprot.org/annotation/VSP_038704|||http://purl.uniprot.org/annotation/VSP_038705 http://togogenome.org/gene/10090:Or52ab4 ^@ http://purl.uniprot.org/uniprot/Q8VG01 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Eif4g1 ^@ http://purl.uniprot.org/uniprot/E9Q9E1|||http://purl.uniprot.org/uniprot/Q6NZJ6 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||EIF4A-binding|||EIF4E-binding|||Eukaryotic translation initiation factor 4 gamma 1|||In isoform 2.|||MI|||MIF4G|||N6-acetyllysine|||Necessary but not sufficient for MKNK1-binding|||Omega-N-methylarginine|||PABPC1-binding|||Phosphoserine|||Phosphoserine; by PKC/PRKCA|||Phosphothreonine|||Polar residues|||Pro residues|||W2|||eIF3/EIF4A-binding ^@ http://purl.uniprot.org/annotation/PRO_0000213322|||http://purl.uniprot.org/annotation/VSP_013974|||http://purl.uniprot.org/annotation/VSP_013975 http://togogenome.org/gene/10090:Bnip2 ^@ http://purl.uniprot.org/uniprot/O54940|||http://purl.uniprot.org/uniprot/Q91VL0 ^@ 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 ^@ Acidic residues|||BCL2/adenovirus E1B 19 kDa protein-interacting protein 2|||CRAL-TRIO|||Disordered|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000064962 http://togogenome.org/gene/10090:Mapk1ip1 ^@ http://purl.uniprot.org/uniprot/Q9D7G9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic residues|||Disordered|||MAPK-interacting and spindle-stabilizing protein|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000209888 http://togogenome.org/gene/10090:Emx2 ^@ http://purl.uniprot.org/uniprot/Q04744 ^@ 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 EMX2 ^@ http://purl.uniprot.org/annotation/PRO_0000048869 http://togogenome.org/gene/10090:Ip6k1 ^@ http://purl.uniprot.org/uniprot/Q6PD10 ^@ 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|||Inositol hexakisphosphate kinase 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000066875 http://togogenome.org/gene/10090:Alg1 ^@ http://purl.uniprot.org/uniprot/Q921Q3 ^@ 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 ^@ Chitobiosyldiphosphodolichol beta-mannosyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000080250|||http://purl.uniprot.org/annotation/VSP_032516 http://togogenome.org/gene/10090:Brd9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J175|||http://purl.uniprot.org/uniprot/Q3UQU0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ 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|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000239220 http://togogenome.org/gene/10090:Naa60 ^@ http://purl.uniprot.org/uniprot/H3BIY0|||http://purl.uniprot.org/uniprot/H3BJZ6|||http://purl.uniprot.org/uniprot/Q9DBU2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Modified Residue|||Region|||Topological Domain ^@ Cytoplasmic|||Helical|||N-acetyltransferase|||N-alpha-acetyltransferase 60|||N6-acetyllysine; by autocatalysis|||Required for homodimerization ^@ http://purl.uniprot.org/annotation/PRO_0000321567 http://togogenome.org/gene/10090:Vmn1r101 ^@ http://purl.uniprot.org/uniprot/E9Q365 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Actl6b ^@ http://purl.uniprot.org/uniprot/Q99MR0 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Actin-like protein 6B|||Essential for mediating its function in dendritic development; may contribute to neuronal-specific targeting ^@ http://purl.uniprot.org/annotation/PRO_0000089136 http://togogenome.org/gene/10090:Lbx2 ^@ http://purl.uniprot.org/uniprot/Q9WUN8 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Region|||Sequence Conflict ^@ Disordered|||Homeobox|||Transcription factor LBX2 ^@ http://purl.uniprot.org/annotation/PRO_0000311329 http://togogenome.org/gene/10090:Ces2f ^@ http://purl.uniprot.org/uniprot/Q08ED5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Carboxylesterase type B|||Carboxylic ester hydrolase ^@ http://purl.uniprot.org/annotation/PRO_5015019984 http://togogenome.org/gene/10090:Gpx4 ^@ http://purl.uniprot.org/uniprot/O70325|||http://purl.uniprot.org/uniprot/Q76LV0 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non standard residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Non standard residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Basic residues|||Disordered|||Early embryonic lethality in homozygous mice. Male subfertility in heterozygous mice due to impaired spermatogenesis.|||In isoform Cytoplasmic.|||In isoform Nuclear.|||Mice develop normally and were born at the expected Mendelian ratio. Homozygous mice however lose body weight by P14-P16 and are susceptible to fatal epileptic seizures. Cells are extremely sensitive to peroxide-induced cell death because the enzyme is inactivated: The enzyme undergoes overoxidation and irreversible inactivation in the presence of exceeding concentrations of its substrates. Unlike the wild-type enzyme, which can form a selenylamide in the absence of reducing equivalents, thereby preventing its irreversible overoxidation, the mutant fails to form such an intermediate during its catalytic cycle.|||Mitochondrion|||Phospholipid hydroperoxide glutathione peroxidase|||Phosphoserine|||Selenocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000013069|||http://purl.uniprot.org/annotation/VSP_018743|||http://purl.uniprot.org/annotation/VSP_059349 http://togogenome.org/gene/10090:Trim34b ^@ http://purl.uniprot.org/uniprot/K7N6K2 ^@ 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|||E3 ubiquitin-protein ligase TRIM34B|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000457054 http://togogenome.org/gene/10090:Sbf1 ^@ http://purl.uniprot.org/uniprot/Q6ZPE2 ^@ 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|||GRAM|||In isoform 2.|||Myotubularin phosphatase|||Myotubularin-related protein 5|||N6-methyllysine|||PH|||Phosphoserine|||Phosphothreonine|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000293476|||http://purl.uniprot.org/annotation/VSP_047523 http://togogenome.org/gene/10090:Rtca ^@ http://purl.uniprot.org/uniprot/Q9D7H3 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ RNA 3'-terminal phosphate cyclase|||Tele-AMP-histidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000156411 http://togogenome.org/gene/10090:Gpr20 ^@ http://purl.uniprot.org/uniprot/Q8BYC4 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||G-protein coupled receptor 20|||Helical; 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_0000303233 http://togogenome.org/gene/10090:Pfpl ^@ http://purl.uniprot.org/uniprot/Q5RKV8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||MACPF|||Macrophage-expressed gene 1 protein ^@ http://purl.uniprot.org/annotation/PRO_5015098011 http://togogenome.org/gene/10090:Cul3 ^@ http://purl.uniprot.org/uniprot/Q9CTE0|||http://purl.uniprot.org/uniprot/Q9JLV5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Cullin protein neddylation|||Cullin-3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||Interaction with KLHL18|||N-acetylserine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000119794 http://togogenome.org/gene/10090:Crisp3 ^@ http://purl.uniprot.org/uniprot/Q03402 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Cysteine-rich secretory protein 3|||N-linked (GlcNAc...) asparagine|||SCP|||ShKT ^@ http://purl.uniprot.org/annotation/PRO_0000006269 http://togogenome.org/gene/10090:Trmu ^@ http://purl.uniprot.org/uniprot/Q9DAT5 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Region|||Site ^@ Cysteine persulfide intermediate|||Disordered|||Interaction with tRNA|||Interaction with target base in tRNA|||Mitochondrial tRNA-specific 2-thiouridylase 1|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000121709 http://togogenome.org/gene/10090:Fat3 ^@ http://purl.uniprot.org/uniprot/E9QK16 ^@ 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 ^@ Cadherin|||Disordered|||EGF-like|||Helical|||Laminin G|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015090379 http://togogenome.org/gene/10090:Catsper2 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ85 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Ion transport ^@ http://togogenome.org/gene/10090:Pja2 ^@ http://purl.uniprot.org/uniprot/Q80U04 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||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; by PKA|||Polar residues|||RING-type; atypical|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000278231|||http://purl.uniprot.org/annotation/VSP_023199 http://togogenome.org/gene/10090:Plxnb2 ^@ http://purl.uniprot.org/uniprot/B2RXS4 ^@ 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 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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_0000415710 http://togogenome.org/gene/10090:Hyls1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1K7|||http://purl.uniprot.org/uniprot/Q9CXX0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Centriolar and ciliogenesis-associated protein HYLS1|||Centriolar and ciliogenesis-associated protein HYLS1 C-terminal|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000284927 http://togogenome.org/gene/10090:Pou6f2 ^@ http://purl.uniprot.org/uniprot/Q8BJI4 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||POU domain, class 6, transcription factor 2|||POU-specific|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000100763 http://togogenome.org/gene/10090:Or52p2 ^@ http://purl.uniprot.org/uniprot/Q8VG23 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pofut1 ^@ http://purl.uniprot.org/uniprot/Q91ZW2 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ GDP-fucose protein O-fucosyltransferase 1|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000012149 http://togogenome.org/gene/10090:Or4k15 ^@ http://purl.uniprot.org/uniprot/A2RTN7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Edil3 ^@ http://purl.uniprot.org/uniprot/O35474|||http://purl.uniprot.org/uniprot/Q8C4U8|||http://purl.uniprot.org/uniprot/Q8C8K0 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Cell attachment site|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like repeat and discoidin I-like domain-containing protein 3|||F5/8 type C|||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_0000007523|||http://purl.uniprot.org/annotation/PRO_5015099024|||http://purl.uniprot.org/annotation/PRO_5015099057|||http://purl.uniprot.org/annotation/VSP_050400|||http://purl.uniprot.org/annotation/VSP_050401 http://togogenome.org/gene/10090:Mapk3 ^@ http://purl.uniprot.org/uniprot/Q63844 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict ^@ 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_0000186252 http://togogenome.org/gene/10090:Bcl2l11 ^@ http://purl.uniprot.org/uniprot/O54918|||http://purl.uniprot.org/uniprot/Q3TR86|||http://purl.uniprot.org/uniprot/Q3U7X3|||http://purl.uniprot.org/uniprot/Q542N5|||http://purl.uniprot.org/uniprot/Q6PEB3 ^@ 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|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant ^@ Apoptosis Bim N-terminal|||Apoptosis Bim N-terminal domain-containing protein|||BH3|||Basic and acidic residues|||Bcl-2-like protein 11|||Bcl-x interacting BH3|||Disordered|||In isoform BimL.|||In isoform BimS.|||Loss of MCL1-binding, strong decrease in BCL2L1-binding, no effect on USP27X-binding; when associated with I-153 del.|||Loss of MCL1-binding, strong decrease in BCL2L1-binding, no effect on USP27X-binding; when associated with L-150 del.|||Loss of TRIM2-binding; when associated with A-55 and A-65.|||Loss of TRIM2-binding; when associated with A-55 and A-73.|||Loss of TRIM2-binding; when associated with A-65 and A-73.|||Phosphoserine|||Phosphoserine; by MAPK|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000143110|||http://purl.uniprot.org/annotation/PRO_5004229618|||http://purl.uniprot.org/annotation/VSP_000536|||http://purl.uniprot.org/annotation/VSP_000537 http://togogenome.org/gene/10090:R3hdm1 ^@ http://purl.uniprot.org/uniprot/B9EHE8|||http://purl.uniprot.org/uniprot/E9Q9Q2|||http://purl.uniprot.org/uniprot/Q80ZH9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||R3H|||SUZ ^@ http://togogenome.org/gene/10090:Nipbl ^@ http://purl.uniprot.org/uniprot/Q6KCD5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Nipped-B-like protein|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||PxVxL motif ^@ http://purl.uniprot.org/annotation/PRO_0000218597|||http://purl.uniprot.org/annotation/VSP_011094|||http://purl.uniprot.org/annotation/VSP_011095|||http://purl.uniprot.org/annotation/VSP_011096|||http://purl.uniprot.org/annotation/VSP_011097|||http://purl.uniprot.org/annotation/VSP_011098|||http://purl.uniprot.org/annotation/VSP_011099 http://togogenome.org/gene/10090:Sqle ^@ http://purl.uniprot.org/uniprot/P52019|||http://purl.uniprot.org/uniprot/Q3TQK8 ^@ Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Region|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Hydrophobic; mediates interaction with membranes|||Important for enzyme activity|||Interaction with MARCHF6|||Required for degradation in response to high membrane cholesterol levels|||Squalene epoxidase|||Squalene monooxygenase|||Sufficient for enzyme activity ^@ http://purl.uniprot.org/annotation/PRO_0000209839 http://togogenome.org/gene/10090:1810009A15Rik ^@ http://purl.uniprot.org/uniprot/Q9D937 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic residues|||Disordered|||Polar residues|||Uncharacterized protein C11orf98 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000432397 http://togogenome.org/gene/10090:Nefl ^@ http://purl.uniprot.org/uniprot/P08551 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||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_0000063788 http://togogenome.org/gene/10090:Ugt1a7c ^@ http://purl.uniprot.org/uniprot/Q6ZQM8 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Signal Peptide|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase 1A7 ^@ http://purl.uniprot.org/annotation/PRO_0000269994 http://togogenome.org/gene/10090:Mphosph8 ^@ http://purl.uniprot.org/uniprot/Q3TYA6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Site ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Basic and acidic residues|||Chromo|||Disordered|||Histone H3K9me3 binding|||Interaction with histone H3K9me3|||M-phase phosphoprotein 8|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Phosphothreonine; by CDK1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000415976 http://togogenome.org/gene/10090:3830403N18Rik ^@ http://purl.uniprot.org/uniprot/Q9D6C3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Xpo1 ^@ http://purl.uniprot.org/uniprot/Q6P5F9|||http://purl.uniprot.org/uniprot/Q8BYY5 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Strand|||Turn ^@ 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|||N6-acetyllysine|||Necessary for interaction with RANBP3|||Necessary for interaction with Ran and nuclear export complex formation|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000204706 http://togogenome.org/gene/10090:Spef1l ^@ http://purl.uniprot.org/uniprot/A0A1B0GR09|||http://purl.uniprot.org/uniprot/A0A1B0GT96|||http://purl.uniprot.org/uniprot/Q3V2J1 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Calponin-homology (CH)|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Txnrd1 ^@ http://purl.uniprot.org/uniprot/Q9JMH6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Modified Residue|||Non standard residue|||Region|||Sequence Conflict|||Splice Variant ^@ Cysteinyl-selenocysteine (Cys-Sec)|||Disordered|||In isoform 2.|||N6-succinyllysine|||Phosphotyrosine|||Polar residues|||Proton acceptor|||Redox-active|||Selenocysteine|||Thioredoxin reductase 1, cytoplasmic ^@ http://purl.uniprot.org/annotation/PRO_0000067982|||http://purl.uniprot.org/annotation/VSP_031566 http://togogenome.org/gene/10090:Agr2 ^@ http://purl.uniprot.org/uniprot/O88312 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Signal Peptide ^@ Anterior gradient protein 2 homolog|||Basic and acidic residues|||Disordered|||Homodimer stabilization; interchain|||Required to promote cell adhesion ^@ http://purl.uniprot.org/annotation/PRO_0000001038 http://togogenome.org/gene/10090:Smyd2 ^@ http://purl.uniprot.org/uniprot/Q8R5A0|||http://purl.uniprot.org/uniprot/Q9D177 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Strand|||Turn|||Zinc Finger ^@ Abolishes methyltransferase activity.|||MYND-type|||N-lysine methyltransferase SMYD2|||Phosphoserine|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000218310 http://togogenome.org/gene/10090:Cox8a ^@ http://purl.uniprot.org/uniprot/Q64445 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Cytochrome c oxidase subunit 8A, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000006189 http://togogenome.org/gene/10090:Ergic2 ^@ http://purl.uniprot.org/uniprot/Q9CR89 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endoplasmic reticulum-Golgi intermediate compartment protein 2|||Helical|||In isoform 2.|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000239384|||http://purl.uniprot.org/annotation/VSP_019211|||http://purl.uniprot.org/annotation/VSP_019212 http://togogenome.org/gene/10090:Ptf1a ^@ http://purl.uniprot.org/uniprot/A2ATA7|||http://purl.uniprot.org/uniprot/Q9QX98 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ BHLH|||Disordered|||Pancreas transcription factor 1 subunit alpha|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000233144 http://togogenome.org/gene/10090:Ak5 ^@ http://purl.uniprot.org/uniprot/Q920P5 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Region|||Sequence Conflict|||Splice Variant ^@ Adenylate kinase 1|||Adenylate kinase 2|||Adenylate kinase isoenzyme 5|||In isoform 2.|||LID 1|||LID 2|||NMP 1|||NMP 2 ^@ http://purl.uniprot.org/annotation/PRO_0000158931|||http://purl.uniprot.org/annotation/VSP_037880 http://togogenome.org/gene/10090:Il20rb ^@ http://purl.uniprot.org/uniprot/E9Q9A6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Fibronectin type-III|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245856 http://togogenome.org/gene/10090:Gal3st2 ^@ http://purl.uniprot.org/uniprot/A2RTS9|||http://purl.uniprot.org/uniprot/Q3UN22 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Zfp113 ^@ http://purl.uniprot.org/uniprot/Q5DTG4|||http://purl.uniprot.org/uniprot/Q8C689 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Nek11 ^@ http://purl.uniprot.org/uniprot/Q8C0Q4 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine; by CHEK1|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek11 ^@ http://purl.uniprot.org/annotation/PRO_0000086440 http://togogenome.org/gene/10090:Rfx7 ^@ http://purl.uniprot.org/uniprot/F8VPJ6|||http://purl.uniprot.org/uniprot/Q8C1T6 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||RFX-type winged-helix ^@ http://togogenome.org/gene/10090:Asz1 ^@ http://purl.uniprot.org/uniprot/Q8VD46 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1|||Disordered|||Phosphoserine|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000066970 http://togogenome.org/gene/10090:Slurp2 ^@ http://purl.uniprot.org/uniprot/P0DP59 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Secreted Ly-6/uPAR domain-containing protein 2|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000440647 http://togogenome.org/gene/10090:Or5b21 ^@ http://purl.uniprot.org/uniprot/Q0VEZ4|||http://purl.uniprot.org/uniprot/Q8VFX2 ^@ 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 5B21 ^@ http://purl.uniprot.org/annotation/PRO_0000150869 http://togogenome.org/gene/10090:Gfra2 ^@ http://purl.uniprot.org/uniprot/O08842|||http://purl.uniprot.org/uniprot/Q3UET6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||GDNF family receptor alpha-2|||GDNF/GAS1|||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_0000010787|||http://purl.uniprot.org/annotation/PRO_0000010788|||http://purl.uniprot.org/annotation/VSP_001662|||http://purl.uniprot.org/annotation/VSP_057520 http://togogenome.org/gene/10090:Clcn5 ^@ http://purl.uniprot.org/uniprot/Q3UL16|||http://purl.uniprot.org/uniprot/Q8C6W8|||http://purl.uniprot.org/uniprot/Q9WVD4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Motif|||Non-terminal Residue|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ CBS|||CBS 1|||CBS 2|||Cytoplasmic|||H(+)/Cl(-) exchange transporter 5|||Helical|||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|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3 ^@ http://purl.uniprot.org/annotation/PRO_0000094447|||http://purl.uniprot.org/annotation/VSP_060655 http://togogenome.org/gene/10090:Snrpa1 ^@ http://purl.uniprot.org/uniprot/P57784 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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|||Phosphoserine|||U2 small nuclear ribonucleoprotein A' ^@ http://purl.uniprot.org/annotation/PRO_0000074175 http://togogenome.org/gene/10090:Plaat3 ^@ http://purl.uniprot.org/uniprot/Q8R3U1 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes enzyme activity.|||Acyl-thioester intermediate|||Cytoplasmic|||Helical|||In isoform 2.|||LRAT|||Loss of phospholipase activity and loss of organelle membrane rupture.|||Lumenal|||Phospholipase A and acyltransferase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000152485|||http://purl.uniprot.org/annotation/VSP_013542 http://togogenome.org/gene/10090:Ercc1 ^@ http://purl.uniprot.org/uniprot/E9PUM0|||http://purl.uniprot.org/uniprot/P07903 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ DNA excision repair protein ERCC-1|||Disordered|||ERCC1-like central|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HhH2, dimerization with ERRC4/XPF|||N-acetylmethionine|||Nuclear localization signal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087007 http://togogenome.org/gene/10090:Dynll1 ^@ http://purl.uniprot.org/uniprot/P63168 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Modified Residue|||Region ^@ 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_0000195127 http://togogenome.org/gene/10090:Macroh2a1 ^@ http://purl.uniprot.org/uniprot/Q8CA90|||http://purl.uniprot.org/uniprot/Q9CTH9|||http://purl.uniprot.org/uniprot/Q9QZQ8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant ^@ Abolished ability to bind poly-ADP-ribose and inhibit PARP1.|||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.|||Macro|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000227904|||http://purl.uniprot.org/annotation/VSP_061611 http://togogenome.org/gene/10090:Urod ^@ http://purl.uniprot.org/uniprot/P70697 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site ^@ N-acetylmethionine|||Transition state stabilizer|||Uroporphyrinogen decarboxylase ^@ http://purl.uniprot.org/annotation/PRO_0000187570 http://togogenome.org/gene/10090:Perp ^@ http://purl.uniprot.org/uniprot/Q9JK95 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||p53 apoptosis effector related to PMP-22 ^@ http://purl.uniprot.org/annotation/PRO_0000226995 http://togogenome.org/gene/10090:Or51a39 ^@ http://purl.uniprot.org/uniprot/Q8VGX7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bex6 ^@ http://purl.uniprot.org/uniprot/Q3TZW7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Protein BEX6 ^@ http://purl.uniprot.org/annotation/PRO_0000229789 http://togogenome.org/gene/10090:Rab5c ^@ http://purl.uniprot.org/uniprot/P35278|||http://purl.uniprot.org/uniprot/Q3TJ39|||http://purl.uniprot.org/uniprot/Q8C266 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Region|||Strand|||Turn ^@ Disordered|||Effector region|||Phosphoserine|||Polar residues|||Ras-related protein Rab-5C|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121111 http://togogenome.org/gene/10090:Mybl1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J132|||http://purl.uniprot.org/uniprot/E9QLX9|||http://purl.uniprot.org/uniprot/P51960 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||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 Repro9; male sterility due to defects in spermatogenesis. Impaired piRNA biogenesis.|||In isoform Short.|||Myb-like|||Myb-related protein A|||N6-acetyllysine|||Negative regulatory domain|||Transcriptional activation domain ^@ http://purl.uniprot.org/annotation/PRO_0000197055|||http://purl.uniprot.org/annotation/VSP_003300 http://togogenome.org/gene/10090:Sumo2 ^@ http://purl.uniprot.org/uniprot/P61957 ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Propeptide|||Strand|||Turn ^@ 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|||N6-acetyllysine; alternate|||Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)|||Small ubiquitin-related modifier 2|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000035951|||http://purl.uniprot.org/annotation/PRO_0000035952 http://togogenome.org/gene/10090:Zfp410 ^@ http://purl.uniprot.org/uniprot/Q8BKX7 ^@ 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 ^@ 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 410 ^@ http://purl.uniprot.org/annotation/PRO_0000047572|||http://purl.uniprot.org/annotation/VSP_008490|||http://purl.uniprot.org/annotation/VSP_008491|||http://purl.uniprot.org/annotation/VSP_008492|||http://purl.uniprot.org/annotation/VSP_008493 http://togogenome.org/gene/10090:Stra8 ^@ http://purl.uniprot.org/uniprot/P70278 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Nuclear export signal (NES)|||Nuclear localization signal (NLS)|||Stimulated by retinoic acid gene 8 protein ^@ http://purl.uniprot.org/annotation/PRO_0000318115 http://togogenome.org/gene/10090:Rhd ^@ http://purl.uniprot.org/uniprot/A0A0R4J0A2|||http://purl.uniprot.org/uniprot/Q8CF94 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Transmembrane ^@ Ammonium transporter AmtB-like|||Blood group Rh(D) polypeptide|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000383326 http://togogenome.org/gene/10090:Mynn ^@ http://purl.uniprot.org/uniprot/Q99MD8 ^@ 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 ^@ BTB|||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|||C2H2-type 8|||Disordered|||In isoform 2.|||In isoform 3.|||Myoneurin|||Nuclear localization signal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000248218|||http://purl.uniprot.org/annotation/VSP_020218|||http://purl.uniprot.org/annotation/VSP_020219|||http://purl.uniprot.org/annotation/VSP_020220 http://togogenome.org/gene/10090:Cdv3 ^@ http://purl.uniprot.org/uniprot/A0A087WNP6|||http://purl.uniprot.org/uniprot/F8WGL9|||http://purl.uniprot.org/uniprot/Q4VAA2 ^@ 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.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ABL|||Polar residues|||Protein CDV3|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000299561|||http://purl.uniprot.org/annotation/VSP_027762|||http://purl.uniprot.org/annotation/VSP_027763 http://togogenome.org/gene/10090:Lat2 ^@ http://purl.uniprot.org/uniprot/Q9JHL0 ^@ 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|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||Linker for activation of T-cells family member 2|||Phosphoserine|||Phosphotyrosine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000083335|||http://purl.uniprot.org/annotation/VSP_016646 http://togogenome.org/gene/10090:H2-M10.1 ^@ http://purl.uniprot.org/uniprot/O19443|||http://purl.uniprot.org/uniprot/Q860W7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5004303677|||http://purl.uniprot.org/annotation/PRO_5015096739 http://togogenome.org/gene/10090:Dusp11 ^@ http://purl.uniprot.org/uniprot/Q6NXK5|||http://purl.uniprot.org/uniprot/Q9D851 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Phosphocysteine intermediate|||Polar residues|||Proton donor/acceptor|||RNA/RNP complex-1-interacting phosphatase|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094817 http://togogenome.org/gene/10090:Ipo5 ^@ http://purl.uniprot.org/uniprot/Q8BKC5 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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.|||N-acetylalanine|||Phosphoserine|||Ran-GTP binding|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000120772|||http://purl.uniprot.org/annotation/VSP_009658 http://togogenome.org/gene/10090:Fam83b ^@ http://purl.uniprot.org/uniprot/Q0VBM2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM83B|||Required for interaction with RAF1 and for the function ^@ http://purl.uniprot.org/annotation/PRO_0000297563 http://togogenome.org/gene/10090:Cab39l ^@ http://purl.uniprot.org/uniprot/Q9DB16 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ Calcium-binding protein 39-like|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000209827|||http://purl.uniprot.org/annotation/VSP_007417|||http://purl.uniprot.org/annotation/VSP_007418 http://togogenome.org/gene/10090:Sf1 ^@ http://purl.uniprot.org/uniprot/E9Q4Q2|||http://purl.uniprot.org/uniprot/Q3TZI3|||http://purl.uniprot.org/uniprot/Q3UI45 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ CCHC-type|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Or1af1 ^@ http://purl.uniprot.org/uniprot/Q7TRY4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kat6a ^@ http://purl.uniprot.org/uniprot/G3X940 ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||H15|||MYST-type HAT|||PHD-type|||Polar residues|||Pro residues|||Proton donor/acceptor ^@ http://togogenome.org/gene/10090:Ddx41 ^@ http://purl.uniprot.org/uniprot/Q3UAC4|||http://purl.uniprot.org/uniprot/Q91VN6|||http://purl.uniprot.org/uniprot/Q9CUY2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||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|||Phosphoserine|||Phosphotyrosine|||Probable ATP-dependent RNA helicase DDX41|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000054971 http://togogenome.org/gene/10090:Timd2 ^@ http://purl.uniprot.org/uniprot/A8C1R4|||http://purl.uniprot.org/uniprot/Q8R183 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Polar residues|||T-cell immunoglobulin and mucin domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000042099|||http://purl.uniprot.org/annotation/PRO_5015086602 http://togogenome.org/gene/10090:Lox ^@ http://purl.uniprot.org/uniprot/P28301|||http://purl.uniprot.org/uniprot/Q3TP83|||http://purl.uniprot.org/uniprot/Q3TXH3 ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ 2',4',5'-topaquinone|||Cleavage; by ADAMTS2 and ADAMTS14|||Disordered|||Homozygous mice display tortuous vessels aneurysm, loss of oxidase activity and die perinatally of aortic aneurysm and dissection. Heterozygous mice display thicker arterial wall with discontinuous elastic lamellae.|||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_0000018522|||http://purl.uniprot.org/annotation/PRO_0000018523|||http://purl.uniprot.org/annotation/PRO_0000447886|||http://purl.uniprot.org/annotation/PRO_5004229539|||http://purl.uniprot.org/annotation/PRO_5014309123 http://togogenome.org/gene/10090:Pik3r5 ^@ http://purl.uniprot.org/uniprot/A1A4T4|||http://purl.uniprot.org/uniprot/Q5SW28 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Heterodimerization|||Interaction with beta-gamma G protein dimers|||N-acetylmethionine|||Phosphoinositide 3-kinase regulatory subunit 5|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000058422 http://togogenome.org/gene/10090:Rpgr ^@ http://purl.uniprot.org/uniprot/A0A067XG46|||http://purl.uniprot.org/uniprot/A2ADP2|||http://purl.uniprot.org/uniprot/Q3UTY5|||http://purl.uniprot.org/uniprot/Q8CAJ5|||http://purl.uniprot.org/uniprot/Q8CDM3|||http://purl.uniprot.org/uniprot/Q9R0X5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Cysteine methyl ester|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||RCC1|||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_0000206639|||http://purl.uniprot.org/annotation/PRO_0000370845|||http://purl.uniprot.org/annotation/VSP_005551|||http://purl.uniprot.org/annotation/VSP_005552|||http://purl.uniprot.org/annotation/VSP_005553|||http://purl.uniprot.org/annotation/VSP_005554|||http://purl.uniprot.org/annotation/VSP_005555|||http://purl.uniprot.org/annotation/VSP_045292 http://togogenome.org/gene/10090:Rab1b ^@ http://purl.uniprot.org/uniprot/Q0PD66|||http://purl.uniprot.org/uniprot/Q9D1G1 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Cysteine methyl ester|||Disordered|||Effector region|||Increases the interaction with MTMR6.|||N-acetylmethionine|||No effect on the interaction with MTMR6.|||Ras-related protein Rab-1B|||S-geranylgeranyl cysteine|||Switch 2 region; required for interaction with REP1/CHM ^@ http://purl.uniprot.org/annotation/PRO_0000121062 http://togogenome.org/gene/10090:Aldh1l1 ^@ http://purl.uniprot.org/uniprot/Q8R0Y6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Site ^@ Aldehyde dehydrogenase domain|||Carrier|||Cytosolic 10-formyltetrahydrofolate dehydrogenase|||Essential for catalytic activity|||Hydrolase domain|||N6-acetyllysine|||N6-succinyllysine|||O-(pantetheine 4'-phosphoryl)serine|||Phosphoserine|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000199420 http://togogenome.org/gene/10090:Spdye4b ^@ http://purl.uniprot.org/uniprot/Q8CDE8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cdc20 ^@ http://purl.uniprot.org/uniprot/Q9JJ66 ^@ 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 ^@ Cell division cycle protein 20 homolog|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||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_0000050901 http://togogenome.org/gene/10090:Rell2 ^@ http://purl.uniprot.org/uniprot/Q8BRJ3 ^@ 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|||Polar residues|||RELT-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000249846 http://togogenome.org/gene/10090:Gm136 ^@ http://purl.uniprot.org/uniprot/A2AT48|||http://purl.uniprot.org/uniprot/Q3V037 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Uncharacterized protein C6orf163 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000271363 http://togogenome.org/gene/10090:Sox13 ^@ http://purl.uniprot.org/uniprot/Q04891 ^@ 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 ^@ Basic and acidic residues|||Disordered|||HMG box|||Phosphoserine|||Polar residues|||Required for homodimerization|||Transcription factor SOX-13 ^@ http://purl.uniprot.org/annotation/PRO_0000048757 http://togogenome.org/gene/10090:Nfkbiz ^@ http://purl.uniprot.org/uniprot/Q9EST8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Abolishes nuclear localization.|||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_0000323578|||http://purl.uniprot.org/annotation/VSP_032024|||http://purl.uniprot.org/annotation/VSP_032025 http://togogenome.org/gene/10090:Cox17 ^@ http://purl.uniprot.org/uniprot/P56394|||http://purl.uniprot.org/uniprot/Q54AC6 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Motif|||Mutagenesis Site|||Region ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||Cytochrome c oxidase copper chaperone|||Disordered|||Significant reduction of copper binding; when associated with G-23 and G-24.|||Significant reduction of copper binding; when associated with G-23 and G-26.|||Significant reduction of copper binding; when associated with G-24 and G-26. ^@ http://purl.uniprot.org/annotation/PRO_0000213539 http://togogenome.org/gene/10090:Tectb ^@ http://purl.uniprot.org/uniprot/O08524|||http://purl.uniprot.org/uniprot/Q1HL20 ^@ 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 alanine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||ZP ^@ http://purl.uniprot.org/annotation/PRO_0000041743|||http://purl.uniprot.org/annotation/PRO_0000041744|||http://purl.uniprot.org/annotation/PRO_5014308329 http://togogenome.org/gene/10090:Fzd2 ^@ http://purl.uniprot.org/uniprot/Q9JIP6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||FZ|||Frizzled-2|||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_0000012979 http://togogenome.org/gene/10090:Abhd17b ^@ http://purl.uniprot.org/uniprot/Q7M759 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Site ^@ Active Site|||Chain|||Modified Residue|||Mutagenesis Site ^@ Alpha/beta hydrolase domain-containing protein 17B|||Charge relay system|||Loss of catalytic activity.|||Loss of catalytic activity. No effect on its localization. Trapping-mutant that stabilizes interaction with LG4/PSD95.|||Loss of palmitoylation activity towards LG4/PSD95 and appears more diffused at the plasma membrane.|||Loss of palmitoylation and plasma membrane localization. Loss of LG4/PSD95 depalmitoylation.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000281112 http://togogenome.org/gene/10090:Sfxn3 ^@ http://purl.uniprot.org/uniprot/Q3U4F0|||http://purl.uniprot.org/uniprot/Q91V61 ^@ 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.|||N-acetylmethionine|||Sideroflexin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000177038|||http://purl.uniprot.org/annotation/VSP_007388 http://togogenome.org/gene/10090:Gpr173 ^@ http://purl.uniprot.org/uniprot/Q6PI62 ^@ 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_0000069651 http://togogenome.org/gene/10090:P2rx6 ^@ http://purl.uniprot.org/uniprot/E9PY29|||http://purl.uniprot.org/uniprot/O54803|||http://purl.uniprot.org/uniprot/Q149L9 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 6 ^@ http://purl.uniprot.org/annotation/PRO_0000161558 http://togogenome.org/gene/10090:Igf2bp2 ^@ http://purl.uniprot.org/uniprot/Q5SF07 ^@ 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.|||Insulin-like growth factor 2 mRNA-binding protein 2|||KH 1|||KH 2|||KH 3|||KH 4|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000244497|||http://purl.uniprot.org/annotation/VSP_019576 http://togogenome.org/gene/10090:Dgat2 ^@ http://purl.uniprot.org/uniprot/Q9DCV3 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Diacylglycerol O-acyltransferase 2|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000249046 http://togogenome.org/gene/10090:Rfesd ^@ http://purl.uniprot.org/uniprot/Q8K2P6 ^@ 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|||Phosphoserine|||Rieske 1|||Rieske 2|||Rieske domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000313814|||http://purl.uniprot.org/annotation/VSP_030156|||http://purl.uniprot.org/annotation/VSP_030157 http://togogenome.org/gene/10090:Mcmbp ^@ http://purl.uniprot.org/uniprot/Q8R3C0 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Mini-chromosome maintenance complex-binding protein|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000089828 http://togogenome.org/gene/10090:Vmn2r115 ^@ http://purl.uniprot.org/uniprot/E9Q0E7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003244348 http://togogenome.org/gene/10090:Atrnl1 ^@ http://purl.uniprot.org/uniprot/Q6A051 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||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.|||In isoform 3.|||Interaction with MC4R|||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_0000334651|||http://purl.uniprot.org/annotation/VSP_033720|||http://purl.uniprot.org/annotation/VSP_033721|||http://purl.uniprot.org/annotation/VSP_033722|||http://purl.uniprot.org/annotation/VSP_033723 http://togogenome.org/gene/10090:Zfp709 ^@ http://purl.uniprot.org/uniprot/Q8C0I0|||http://purl.uniprot.org/uniprot/Q8VC29 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Defa27 ^@ http://purl.uniprot.org/uniprot/F2Z403 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Mammalian defensins ^@ http://purl.uniprot.org/annotation/PRO_5003294225 http://togogenome.org/gene/10090:Ggh ^@ http://purl.uniprot.org/uniprot/Q9Z0L8 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Gamma-glutamyl hydrolase|||In isoform II.|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000026540|||http://purl.uniprot.org/annotation/VSP_005447 http://togogenome.org/gene/10090:Krcc1 ^@ http://purl.uniprot.org/uniprot/Q99JT5 ^@ 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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000306397 http://togogenome.org/gene/10090:Atg2a ^@ http://purl.uniprot.org/uniprot/Q6P4T0 ^@ 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 ^@ Autophagy-related protein 2 homolog A|||Basic and acidic residues|||Chorein N-terminal|||Disordered|||Phosphoserine|||Polar residues|||WIPI-interacting ^@ http://purl.uniprot.org/annotation/PRO_0000315235 http://togogenome.org/gene/10090:Mogs ^@ http://purl.uniprot.org/uniprot/Q80UM7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Endoplasmic reticulum targeting|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Mannosyl-oligosaccharide glucosidase|||N-linked (GlcNAc...) asparagine|||Required for endoplasmic reticulum targeting ^@ http://purl.uniprot.org/annotation/PRO_0000057711 http://togogenome.org/gene/10090:Clasp1 ^@ http://purl.uniprot.org/uniprot/A0A087WQ31|||http://purl.uniprot.org/uniprot/A0A087WQF1|||http://purl.uniprot.org/uniprot/A0A087WS18|||http://purl.uniprot.org/uniprot/A5D6Q8|||http://purl.uniprot.org/uniprot/E9Q6L0|||http://purl.uniprot.org/uniprot/E9QKH0|||http://purl.uniprot.org/uniprot/Q80TV8 ^@ 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 ^@ CLIP-associating protein 1|||Disordered|||HEAT|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||In isoform 2.|||Interaction with CLIP2 and RSN|||Interaction with PHLDB2|||Interaction with microtubules, MAPRE1 and MAPRE3|||Localization to kinetochores|||Phosphoserine|||Phosphothreonine|||Polar residues|||TOG ^@ http://purl.uniprot.org/annotation/PRO_0000272274|||http://purl.uniprot.org/annotation/VSP_022390|||http://purl.uniprot.org/annotation/VSP_022391|||http://purl.uniprot.org/annotation/VSP_022392 http://togogenome.org/gene/10090:Suds3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J243|||http://purl.uniprot.org/uniprot/Q8BR65 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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_0000097653 http://togogenome.org/gene/10090:Ppp1r3f ^@ http://purl.uniprot.org/uniprot/B9EHL3|||http://purl.uniprot.org/uniprot/Q9JIG4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abrogates PP1-binding.|||Acidic residues|||CBM21|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||PP1-binding motif|||Phosphoserine|||Protein phosphatase 1 regulatory subunit 3F ^@ http://purl.uniprot.org/annotation/PRO_0000257497|||http://purl.uniprot.org/annotation/VSP_021363 http://togogenome.org/gene/10090:Syt15 ^@ http://purl.uniprot.org/uniprot/Q8C6N3 ^@ 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 ^@ C2 1|||C2 2|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||Synaptotagmin-15 ^@ http://purl.uniprot.org/annotation/PRO_0000183981|||http://purl.uniprot.org/annotation/VSP_008649|||http://purl.uniprot.org/annotation/VSP_008650 http://togogenome.org/gene/10090:Megf10 ^@ http://purl.uniprot.org/uniprot/Q6DIB5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||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 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|||Extracellular|||Helical|||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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000309733 http://togogenome.org/gene/10090:Or6c207 ^@ http://purl.uniprot.org/uniprot/Q8VFH3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Calb2 ^@ http://purl.uniprot.org/uniprot/Q08331 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Calretinin|||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_0000073480 http://togogenome.org/gene/10090:Tmem52b ^@ http://purl.uniprot.org/uniprot/Q0VBF2 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 52B ^@ http://purl.uniprot.org/annotation/PRO_0000294449 http://togogenome.org/gene/10090:Tmem141 ^@ http://purl.uniprot.org/uniprot/A2AJB2 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 141 ^@ http://purl.uniprot.org/annotation/PRO_0000293709 http://togogenome.org/gene/10090:Lypd8l ^@ http://purl.uniprot.org/uniprot/Q6YI28 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_5015098603 http://togogenome.org/gene/10090:Ppp1r11 ^@ http://purl.uniprot.org/uniprot/A5A4Y9|||http://purl.uniprot.org/uniprot/Q8K1L5 ^@ 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 ^@ Atypical RING finger domain 1|||Atypical RING finger domain 2|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase PPP1R11|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000239621 http://togogenome.org/gene/10090:Edn1 ^@ http://purl.uniprot.org/uniprot/P22387|||http://purl.uniprot.org/uniprot/Q544E0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Big endothelin-1|||Cleavage; by KEL|||Endothelin-1|||Endothelin-like|||Endothelin-like toxin ^@ http://purl.uniprot.org/annotation/PRO_0000008062|||http://purl.uniprot.org/annotation/PRO_0000008063|||http://purl.uniprot.org/annotation/PRO_0000008064|||http://purl.uniprot.org/annotation/PRO_0000436397|||http://purl.uniprot.org/annotation/PRO_5014309627 http://togogenome.org/gene/10090:Apoe ^@ http://purl.uniprot.org/uniprot/P08226|||http://purl.uniprot.org/uniprot/Q3TXU4 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Turn ^@ 1|||2|||3|||4|||5|||6|||7|||8|||8 X 22 AA approximate tandem repeats|||Apolipoprotein E|||Homooligomerization|||LDL and other lipoprotein receptors binding|||Lipid-binding and lipoprotein association|||Methionine sulfoxide|||Phosphoserine|||Specificity for association with VLDL ^@ http://purl.uniprot.org/annotation/PRO_0000001990|||http://purl.uniprot.org/annotation/PRO_5014309124 http://togogenome.org/gene/10090:Rbmy ^@ http://purl.uniprot.org/uniprot/O35698 ^@ 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|||RNA-binding motif protein, Y chromosome, family 1 member A1|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000341540 http://togogenome.org/gene/10090:Steap1 ^@ http://purl.uniprot.org/uniprot/Q3UNB9|||http://purl.uniprot.org/uniprot/Q9CWR7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Ferric oxidoreductase|||Helical|||Phosphoserine|||STEAP1 protein|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000191695 http://togogenome.org/gene/10090:Phf2 ^@ http://purl.uniprot.org/uniprot/Q9WTU0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000059291 http://togogenome.org/gene/10090:Tspyl3 ^@ http://purl.uniprot.org/uniprot/Q3UYP3|||http://purl.uniprot.org/uniprot/Q6PE20 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Aadat ^@ http://purl.uniprot.org/uniprot/Q9WVM8 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Transit Peptide ^@ Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial|||Mitochondrion|||N6-(pyridoxal phosphate)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000020603 http://togogenome.org/gene/10090:Slc25a13 ^@ http://purl.uniprot.org/uniprot/Q8C140|||http://purl.uniprot.org/uniprot/Q9QXX4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-terminal domain|||Carrier domain|||EF-hand|||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|||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|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090602 http://togogenome.org/gene/10090:6720489N17Rik ^@ http://purl.uniprot.org/uniprot/Q8BGU1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB ^@ http://togogenome.org/gene/10090:Sult5a1 ^@ http://purl.uniprot.org/uniprot/Q91X36 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Pdss1 ^@ http://purl.uniprot.org/uniprot/Q33DR2 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ All trans-polyprenyl-diphosphate synthase PDSS1 ^@ http://purl.uniprot.org/annotation/PRO_0000123976 http://togogenome.org/gene/10090:Fam241a ^@ http://purl.uniprot.org/uniprot/Q9CZL2 ^@ 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|||Uncharacterized protein FAM241A ^@ http://purl.uniprot.org/annotation/PRO_0000286630 http://togogenome.org/gene/10090:Mrgprb2 ^@ http://purl.uniprot.org/uniprot/Q3KNA1|||http://purl.uniprot.org/uniprot/W8W3G3 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||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|||Mas-related G-protein coupled receptor member B2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000304878 http://togogenome.org/gene/10090:Or1e35 ^@ http://purl.uniprot.org/uniprot/Q8VGR3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tnfrsf8 ^@ http://purl.uniprot.org/uniprot/Q60846 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||TNFR-Cys 1|||TNFR-Cys 2|||Tumor necrosis factor receptor superfamily member 8 ^@ http://purl.uniprot.org/annotation/PRO_0000034575 http://togogenome.org/gene/10090:Dhx35 ^@ http://purl.uniprot.org/uniprot/Q8K1G9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Helicase ATP-binding|||Helicase C-terminal ^@ http://togogenome.org/gene/10090:Or7g19 ^@ http://purl.uniprot.org/uniprot/Q7TRG9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dnlz ^@ http://purl.uniprot.org/uniprot/Q9D113 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transit Peptide|||Zinc Finger ^@ Binding Site|||Chain|||Region|||Transit Peptide|||Zinc Finger ^@ DNL-type|||DNL-type zinc finger protein|||Disordered|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000317167 http://togogenome.org/gene/10090:Il13ra1 ^@ http://purl.uniprot.org/uniprot/O09030|||http://purl.uniprot.org/uniprot/Q8BNM4 ^@ 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|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III domain-containing protein|||Helical|||Interleukin-13 receptor subunit alpha-1|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010940|||http://purl.uniprot.org/annotation/PRO_5004303774 http://togogenome.org/gene/10090:Lyz3 ^@ http://purl.uniprot.org/uniprot/Q8BM26|||http://purl.uniprot.org/uniprot/Q8BM27 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Non-terminal Residue|||Signal Peptide ^@ Glycosyl hydrolases family 22 (GH22)|||Glycosyl hydrolases family 22 (GH22) domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5004304175|||http://purl.uniprot.org/annotation/PRO_5015099042 http://togogenome.org/gene/10090:Zfp101 ^@ http://purl.uniprot.org/uniprot/Q8BP18|||http://purl.uniprot.org/uniprot/Q8C687 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Gng5 ^@ http://purl.uniprot.org/uniprot/Q3UKC8|||http://purl.uniprot.org/uniprot/Q80SZ7 ^@ Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide ^@ Cysteine methyl ester|||G protein gamma|||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_0000012629|||http://purl.uniprot.org/annotation/PRO_0000012630 http://togogenome.org/gene/10090:Fhip2a ^@ http://purl.uniprot.org/uniprot/Q8CDM8 ^@ 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|||FHF complex subunit HOOK interacting protein 2A|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284649|||http://purl.uniprot.org/annotation/VSP_024592 http://togogenome.org/gene/10090:Ano5 ^@ http://purl.uniprot.org/uniprot/Q75UR0 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Anoctamin-5|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000191756|||http://purl.uniprot.org/annotation/VSP_015628|||http://purl.uniprot.org/annotation/VSP_015629|||http://purl.uniprot.org/annotation/VSP_015630|||http://purl.uniprot.org/annotation/VSP_015631|||http://purl.uniprot.org/annotation/VSP_035571|||http://purl.uniprot.org/annotation/VSP_035572 http://togogenome.org/gene/10090:Prss48 ^@ http://purl.uniprot.org/uniprot/Q14B25 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 48 ^@ http://purl.uniprot.org/annotation/PRO_0000331637 http://togogenome.org/gene/10090:Mpzl1 ^@ http://purl.uniprot.org/uniprot/A0A0A6YXW1|||http://purl.uniprot.org/uniprot/A0A0R4J0V2|||http://purl.uniprot.org/uniprot/Q3TEW6 ^@ 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|||ITIM motif 1|||ITIM motif 2|||Ig-like|||Ig-like V-type|||In isoform 2.|||Myelin protein zero-like protein 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000240336|||http://purl.uniprot.org/annotation/PRO_5015044295|||http://purl.uniprot.org/annotation/PRO_5036453745|||http://purl.uniprot.org/annotation/VSP_019345 http://togogenome.org/gene/10090:Osbpl2 ^@ http://purl.uniprot.org/uniprot/Q8BX94 ^@ 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|||Oxysterol-binding protein-related protein 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000100370 http://togogenome.org/gene/10090:Arl6ip5 ^@ http://purl.uniprot.org/uniprot/Q8R5J9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||N-acetylmethionine|||PRA1 family protein 3|||Required for homodimer formation and heterodimer formation with ARL6IP1|||Significant decrease in interaction with ARL6IP1 and no influence on SLC1A1/EAAC1-mediated glutamate transport; when associated with A-110.|||Significant decrease in interaction with ARL6IP1 and no influence on SLC1A1/EAAC1-mediated glutamate transport; when associated with A-112.|||Targeting to endoplasmic reticulum membrane ^@ http://purl.uniprot.org/annotation/PRO_0000220884 http://togogenome.org/gene/10090:Hoxa11 ^@ http://purl.uniprot.org/uniprot/P31311 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000200096 http://togogenome.org/gene/10090:Tmx4 ^@ http://purl.uniprot.org/uniprot/Q0P5W2|||http://purl.uniprot.org/uniprot/Q8C0L0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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_0000034192|||http://purl.uniprot.org/annotation/PRO_5014306812 http://togogenome.org/gene/10090:Neurog3 ^@ http://purl.uniprot.org/uniprot/P70661|||http://purl.uniprot.org/uniprot/Q548G3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Disordered|||Neurogenin-3|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127403 http://togogenome.org/gene/10090:Ccdc93 ^@ http://purl.uniprot.org/uniprot/E9QAD4|||http://purl.uniprot.org/uniprot/Q7TQK5|||http://purl.uniprot.org/uniprot/Q8BUE0 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ CCDC93 coiled-coil|||Coiled-coil domain-containing protein 93|||Disordered|||Phosphoserine|||Sufficient for interaction with CCDC22|||Sufficient for interaction with WASHC2C ^@ http://purl.uniprot.org/annotation/PRO_0000234605 http://togogenome.org/gene/10090:Tmem192 ^@ http://purl.uniprot.org/uniprot/Q9CXT7 ^@ 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|||Phosphotyrosine|||Transmembrane protein 192 ^@ http://purl.uniprot.org/annotation/PRO_0000311268|||http://purl.uniprot.org/annotation/VSP_029503 http://togogenome.org/gene/10090:Rnf138 ^@ http://purl.uniprot.org/uniprot/Q9CQE0|||http://purl.uniprot.org/uniprot/Q9CSA3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 2|||C2HC RNF-type|||Disordered|||E3 ubiquitin-protein ligase RNF138|||In isoform 2.|||Phosphothreonine|||RING-type|||UIM ^@ http://purl.uniprot.org/annotation/PRO_0000261608|||http://purl.uniprot.org/annotation/VSP_021733 http://togogenome.org/gene/10090:Npc1l1 ^@ http://purl.uniprot.org/uniprot/A3KMG9|||http://purl.uniprot.org/uniprot/Z4YJC9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Non-terminal Residue|||Signal Peptide|||Transmembrane ^@ Helical|||SSD ^@ http://purl.uniprot.org/annotation/PRO_5002654761|||http://purl.uniprot.org/annotation/PRO_5015103021 http://togogenome.org/gene/10090:Hirip3 ^@ http://purl.uniprot.org/uniprot/Q8BLH7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||HIRA-interacting protein 3|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000367046 http://togogenome.org/gene/10090:Ncstn ^@ http://purl.uniprot.org/uniprot/P57716 ^@ 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|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nicastrin ^@ http://purl.uniprot.org/annotation/PRO_0000019682 http://togogenome.org/gene/10090:Uqcc2 ^@ http://purl.uniprot.org/uniprot/Q9CQY6 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||Ubiquinol-cytochrome c reductase complex assembly factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000089527 http://togogenome.org/gene/10090:Blk ^@ http://purl.uniprot.org/uniprot/P16277 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||Impairs the interaction with CD79A and CD79B.|||Leads to constitutive activation of BLK.|||N-myristoyl glycine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||SH2|||SH3|||Tyrosine-protein kinase Blk ^@ http://purl.uniprot.org/annotation/PRO_0000088062 http://togogenome.org/gene/10090:Sipa1 ^@ http://purl.uniprot.org/uniprot/E9Q0Y4|||http://purl.uniprot.org/uniprot/Q3UE96|||http://purl.uniprot.org/uniprot/Q3V403 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PDZ|||Polar residues|||Rap-GAP ^@ http://togogenome.org/gene/10090:Olig3 ^@ http://purl.uniprot.org/uniprot/Q6PFG8 ^@ 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_0000127418 http://togogenome.org/gene/10090:Tmem98 ^@ http://purl.uniprot.org/uniprot/Q91X86 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Required for interaction with MYRF|||Transmembrane protein 98 ^@ http://purl.uniprot.org/annotation/PRO_0000251712 http://togogenome.org/gene/10090:Fgf11 ^@ http://purl.uniprot.org/uniprot/A0A7U3L4H2|||http://purl.uniprot.org/uniprot/P70378|||http://purl.uniprot.org/uniprot/Q6NXW2 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Fibroblast growth factor 11 ^@ http://purl.uniprot.org/annotation/PRO_0000147603 http://togogenome.org/gene/10090:Gng14 ^@ http://purl.uniprot.org/uniprot/B2RVA4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ G protein gamma ^@ http://togogenome.org/gene/10090:Skint6 ^@ http://purl.uniprot.org/uniprot/A7XUZ6 ^@ 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 C1-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Selection and upkeep of intraepithelial T-cells protein 6 ^@ http://purl.uniprot.org/annotation/PRO_5000271640|||http://purl.uniprot.org/annotation/VSP_034886|||http://purl.uniprot.org/annotation/VSP_034887 http://togogenome.org/gene/10090:Rmdn1 ^@ http://purl.uniprot.org/uniprot/Q9DCV4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ N6-succinyllysine|||Regulator of microtubule dynamics protein 1|||TPR 1|||TPR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000187183 http://togogenome.org/gene/10090:Pcgf1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J141|||http://purl.uniprot.org/uniprot/Q8R023 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Zinc Finger ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Necessary for repressor activity|||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 the interaction with the KDM2B-SKP1 heterodimeric complex ^@ http://purl.uniprot.org/annotation/PRO_0000277856 http://togogenome.org/gene/10090:Fgf20 ^@ http://purl.uniprot.org/uniprot/Q9ESL9 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Fibroblast growth factor 20 ^@ http://purl.uniprot.org/annotation/PRO_0000147617 http://togogenome.org/gene/10090:Pphln1 ^@ http://purl.uniprot.org/uniprot/G3UWD4|||http://purl.uniprot.org/uniprot/G3X959|||http://purl.uniprot.org/uniprot/Q3TYM7|||http://purl.uniprot.org/uniprot/Q3UBL8|||http://purl.uniprot.org/uniprot/Q8K2H1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ 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)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N6-acetyllysine; alternate|||Nuclear localization signal|||Periphilin-1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000058538|||http://purl.uniprot.org/annotation/VSP_009908 http://togogenome.org/gene/10090:Rhoq ^@ http://purl.uniprot.org/uniprot/Q8R527 ^@ 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|||Removed in mature form|||Rho-related GTP-binding protein RhoQ|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000198872|||http://purl.uniprot.org/annotation/PRO_0000281223 http://togogenome.org/gene/10090:Or10u3 ^@ http://purl.uniprot.org/uniprot/Q7TS26 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mrgprb3 ^@ http://purl.uniprot.org/uniprot/Q91ZC1 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||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|||Mas-related G-protein coupled receptor member B3 ^@ http://purl.uniprot.org/annotation/PRO_0000305298 http://togogenome.org/gene/10090:Dlk1 ^@ http://purl.uniprot.org/uniprot/B4YB46|||http://purl.uniprot.org/uniprot/B4YB48|||http://purl.uniprot.org/uniprot/G3UWU8|||http://purl.uniprot.org/uniprot/Q09163|||http://purl.uniprot.org/uniprot/Q925U3|||http://purl.uniprot.org/uniprot/Q9DAU5 ^@ 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 B.|||In isoform C.|||In isoform C2.|||In isoform D.|||In isoform D2.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||N-linked (GlcNAc...) asparagine; atypical; partial|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; partial|||Protein delta homolog 1 ^@ http://purl.uniprot.org/annotation/CAR_000160|||http://purl.uniprot.org/annotation/CAR_000161|||http://purl.uniprot.org/annotation/CAR_000162|||http://purl.uniprot.org/annotation/CAR_000183|||http://purl.uniprot.org/annotation/PRO_0000007520|||http://purl.uniprot.org/annotation/PRO_0000007521|||http://purl.uniprot.org/annotation/PRO_5003456661|||http://purl.uniprot.org/annotation/PRO_5015087313|||http://purl.uniprot.org/annotation/PRO_5015087314|||http://purl.uniprot.org/annotation/PRO_5015099550|||http://purl.uniprot.org/annotation/PRO_5015099688|||http://purl.uniprot.org/annotation/VSP_001378|||http://purl.uniprot.org/annotation/VSP_001379|||http://purl.uniprot.org/annotation/VSP_001380|||http://purl.uniprot.org/annotation/VSP_001381|||http://purl.uniprot.org/annotation/VSP_001382 http://togogenome.org/gene/10090:Zfp788 ^@ http://purl.uniprot.org/uniprot/Q3TQT9|||http://purl.uniprot.org/uniprot/Q8BUQ3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Arrb2 ^@ http://purl.uniprot.org/uniprot/A0A158SIT9|||http://purl.uniprot.org/uniprot/J3JS97|||http://purl.uniprot.org/uniprot/Q91YI4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Arrestin C-terminal-like|||Beta-arrestin-2|||Hydroxyproline; by PHD2|||In isoform 2.|||Interaction with AP2B1|||Interaction with TRAF6|||Nuclear localization. Causes nuclear relocalization of MAPK10.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif ^@ http://purl.uniprot.org/annotation/PRO_0000205200|||http://purl.uniprot.org/annotation/VSP_020652 http://togogenome.org/gene/10090:St18 ^@ http://purl.uniprot.org/uniprot/Q148A0|||http://purl.uniprot.org/uniprot/Q80TY4 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||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|||Myelin transcription factor 1|||Polar residues|||Suppression of tumorigenicity 18 protein ^@ http://purl.uniprot.org/annotation/PRO_0000234031 http://togogenome.org/gene/10090:Prkag2 ^@ http://purl.uniprot.org/uniprot/Q3TMN8|||http://purl.uniprot.org/uniprot/Q8BIQ9|||http://purl.uniprot.org/uniprot/Q91WG5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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 isoform B.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204382|||http://purl.uniprot.org/annotation/VSP_015586 http://togogenome.org/gene/10090:Reg3b ^@ http://purl.uniprot.org/uniprot/P35230 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Motif|||Propeptide|||Signal Peptide ^@ C-type lectin|||EPN|||Regenerating islet-derived protein 3-beta 15 kDa form|||Regenerating islet-derived protein 3-beta 16.5 kDa form ^@ http://purl.uniprot.org/annotation/PRO_0000017432|||http://purl.uniprot.org/annotation/PRO_0000422747|||http://purl.uniprot.org/annotation/PRO_0000422748 http://togogenome.org/gene/10090:Mapk6 ^@ http://purl.uniprot.org/uniprot/Q61532 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes binding to MAPKAPK5.|||Disordered|||FRIEDE motif|||Kinase defective mutant, abolishes activity.|||Mimicks phosphorylation state and induces constitutive protein kinase activity.|||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|||Unable to activate MAPKAPK5 promote MAPKAPK5 localization to the cytoplasm. ^@ http://purl.uniprot.org/annotation/PRO_0000186258 http://togogenome.org/gene/10090:Or8b40 ^@ http://purl.uniprot.org/uniprot/Q9EQA4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wfdc1 ^@ http://purl.uniprot.org/uniprot/Q3UQ76|||http://purl.uniprot.org/uniprot/Q9ESH5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||WAP|||WAP four-disulfide core domain protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000041366|||http://purl.uniprot.org/annotation/PRO_5014309176 http://togogenome.org/gene/10090:Fam118b ^@ http://purl.uniprot.org/uniprot/Q8C569 ^@ 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.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Protein FAM118B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000295105|||http://purl.uniprot.org/annotation/VSP_026730 http://togogenome.org/gene/10090:Cavin1 ^@ http://purl.uniprot.org/uniprot/O54724 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region ^@ 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|||Leucine-zipper 1|||Leucine-zipper 2|||Leucine-zipper 3|||Loss of phosphorylation.|||N-acetylmethionine|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Required for homotrimerization and for interaction with CAVIN2 and CAVIN3|||Significant loss of phosphorylation and loss of regulation of ribosomal transcriptional activity. ^@ http://purl.uniprot.org/annotation/PRO_0000097095 http://togogenome.org/gene/10090:Mbnl2 ^@ http://purl.uniprot.org/uniprot/Q8C181 ^@ 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.|||In isoform 4.|||Muscleblind-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000274873|||http://purl.uniprot.org/annotation/VSP_022889|||http://purl.uniprot.org/annotation/VSP_022890|||http://purl.uniprot.org/annotation/VSP_022891 http://togogenome.org/gene/10090:Neu3 ^@ http://purl.uniprot.org/uniprot/Q543I9|||http://purl.uniprot.org/uniprot/Q9JMH7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Repeat ^@ BNR 1|||BNR 2|||BNR 3|||FRIP motif|||Nucleophile|||Phosphoserine|||Proton acceptor|||Sialidase|||Sialidase-3 ^@ http://purl.uniprot.org/annotation/PRO_0000208904 http://togogenome.org/gene/10090:Slc6a8 ^@ http://purl.uniprot.org/uniprot/A2ALM6|||http://purl.uniprot.org/uniprot/Q8VBW1 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 1.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Sodium- and chloride-dependent creatine transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000214775|||http://purl.uniprot.org/annotation/VSP_061625|||http://purl.uniprot.org/annotation/VSP_061626 http://togogenome.org/gene/10090:Mrc1 ^@ http://purl.uniprot.org/uniprot/Q2HZ94|||http://purl.uniprot.org/uniprot/Q61830 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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|||Extracellular|||Fibronectin type-II|||Helical|||Macrophage mannose receptor 1|||N-linked (GlcNAc...) asparagine|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000017549|||http://purl.uniprot.org/annotation/PRO_5015097281 http://togogenome.org/gene/10090:Tpx2 ^@ http://purl.uniprot.org/uniprot/A2APB8|||http://purl.uniprot.org/uniprot/Q8BTJ3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes interaction with AURKA.|||Aurora-A binding|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||TPX2 C-terminal|||TPX2 central|||Targeting protein for Xklp2 ^@ http://purl.uniprot.org/annotation/PRO_0000393112 http://togogenome.org/gene/10090:Ccdc134 ^@ http://purl.uniprot.org/uniprot/Q8C7V8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 134|||Disordered|||In isoform 2.|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000254110|||http://purl.uniprot.org/annotation/VSP_021181 http://togogenome.org/gene/10090:Vstm2a ^@ http://purl.uniprot.org/uniprot/Q8R0A6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide ^@ Abolishes glycosylation and impairs secretion.|||Disordered|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Polar residues|||V-set and transmembrane domain-containing protein 2A ^@ http://purl.uniprot.org/annotation/PRO_0000014776 http://togogenome.org/gene/10090:Dsg1a ^@ http://purl.uniprot.org/uniprot/Q61495 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||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-alpha|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000003839|||http://purl.uniprot.org/annotation/PRO_0000003840 http://togogenome.org/gene/10090:H2-Q9 ^@ http://purl.uniprot.org/uniprot/Q52PG7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015097740 http://togogenome.org/gene/10090:Cap2 ^@ http://purl.uniprot.org/uniprot/Q9CYT6 ^@ 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 ^@ Adenylyl cyclase-associated protein 2|||C-CAP/cofactor C-like|||Disordered|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000205701 http://togogenome.org/gene/10090:Zfp811 ^@ http://purl.uniprot.org/uniprot/A0A0J9YU71|||http://purl.uniprot.org/uniprot/A0A3Q4EGT7|||http://purl.uniprot.org/uniprot/Q80WT1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Taar5 ^@ http://purl.uniprot.org/uniprot/B2RTA0|||http://purl.uniprot.org/uniprot/Q5QD14 ^@ 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|||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|||Trace amine-associated receptor 5 ^@ http://purl.uniprot.org/annotation/PRO_0000070155 http://togogenome.org/gene/10090:Pate5 ^@ http://purl.uniprot.org/uniprot/Q9D262 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099708 http://togogenome.org/gene/10090:Cntfr ^@ http://purl.uniprot.org/uniprot/O88507 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ 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_0000010993|||http://purl.uniprot.org/annotation/PRO_0000010994 http://togogenome.org/gene/10090:Cpne9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0J1|||http://purl.uniprot.org/uniprot/Q1RLL3|||http://purl.uniprot.org/uniprot/Q8BRJ6 ^@ 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 ^@ C2|||C2 1|||C2 2|||Copine-9|||Disordered|||Pro residues|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000277584 http://togogenome.org/gene/10090:Higd1c ^@ http://purl.uniprot.org/uniprot/Q1XG80|||http://purl.uniprot.org/uniprot/Q76I25 ^@ 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_0000215776 http://togogenome.org/gene/10090:Abcf2 ^@ http://purl.uniprot.org/uniprot/Q99LE6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family F member 2|||Basic and acidic residues|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000093324 http://togogenome.org/gene/10090:Pygo2 ^@ http://purl.uniprot.org/uniprot/Q3V113|||http://purl.uniprot.org/uniprot/Q80V76 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PHD-type|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:1700020L24Rik ^@ http://purl.uniprot.org/uniprot/Q8C1R3 ^@ 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 C17orf50 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000251203 http://togogenome.org/gene/10090:Aqp1 ^@ http://purl.uniprot.org/uniprot/Q02013 ^@ Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2|||Phosphoserine|||Phosphotyrosine|||Substrate discrimination ^@ http://purl.uniprot.org/annotation/PRO_0000063921 http://togogenome.org/gene/10090:Slc25a3 ^@ http://purl.uniprot.org/uniprot/G5E902|||http://purl.uniprot.org/uniprot/Q8VEM8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Modified Residue|||Repeat|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||N6-methyllysine|||Phosphotyrosine|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000019257 http://togogenome.org/gene/10090:Lrrtm2 ^@ http://purl.uniprot.org/uniprot/Q8BGA3|||http://purl.uniprot.org/uniprot/Q8C8L1 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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_0000018354|||http://purl.uniprot.org/annotation/PRO_5004303954 http://togogenome.org/gene/10090:Firrm ^@ http://purl.uniprot.org/uniprot/Q3TQQ9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ FIGNL1-interacting regulator of recombination and mitosis|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000279462|||http://purl.uniprot.org/annotation/VSP_023446|||http://purl.uniprot.org/annotation/VSP_023447 http://togogenome.org/gene/10090:Cdh26 ^@ http://purl.uniprot.org/uniprot/P59862|||http://purl.uniprot.org/uniprot/Q3V1P3 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin-like protein 26|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000003830|||http://purl.uniprot.org/annotation/PRO_5015097523 http://togogenome.org/gene/10090:Traf6 ^@ http://purl.uniprot.org/uniprot/P70196 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Abolished ubiquitination by the SCF(FBXL2) complex.|||Decreased interaction with FBXL2.|||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|||In isoform 2.|||Interaction with TANK|||Interaction with TAX1BP1|||MATH|||RING-type|||TNF receptor-associated factor 6|||TRAF-type 1|||TRAF-type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000056408|||http://purl.uniprot.org/annotation/VSP_007404|||http://purl.uniprot.org/annotation/VSP_007405 http://togogenome.org/gene/10090:Saal1 ^@ http://purl.uniprot.org/uniprot/G1UCX4|||http://purl.uniprot.org/uniprot/Q9D2C2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Protein SAAL1 ^@ http://purl.uniprot.org/annotation/PRO_0000279541|||http://purl.uniprot.org/annotation/VSP_023483 http://togogenome.org/gene/10090:Rpl23 ^@ http://purl.uniprot.org/uniprot/P62830 ^@ 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_0000128613 http://togogenome.org/gene/10090:Dynlt1f ^@ http://purl.uniprot.org/uniprot/P51807 ^@ 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 ^@ Dynein light chain Tctex-type 1|||Interaction with GNB1|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000195153 http://togogenome.org/gene/10090:Cmpk2 ^@ http://purl.uniprot.org/uniprot/Q3U5Q7 ^@ Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Coiled-Coil|||Mutagenesis Site|||Sequence Conflict|||Transit Peptide ^@ Catalytically inactive with subsequent loss of NLRP3 inflammasome activation.|||Mitochondrion|||UMP-CMP kinase 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000331525 http://togogenome.org/gene/10090:Fut10 ^@ http://purl.uniprot.org/uniprot/Q5F2L2 ^@ 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 ^@ Alpha-(1,3)-fucosyltransferase 10|||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_0000299003|||http://purl.uniprot.org/annotation/VSP_027507|||http://purl.uniprot.org/annotation/VSP_027508|||http://purl.uniprot.org/annotation/VSP_027509 http://togogenome.org/gene/10090:Or13a28 ^@ http://purl.uniprot.org/uniprot/Q8VGM2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cstpp1 ^@ http://purl.uniprot.org/uniprot/Q8BHR8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Splice Variant ^@ Centriolar satellite-associated tubulin polyglutamylase complex regulator 1|||Disordered|||In isoform 2.|||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_0000281427|||http://purl.uniprot.org/annotation/VSP_024002|||http://purl.uniprot.org/annotation/VSP_024003 http://togogenome.org/gene/10090:Prl8a9 ^@ http://purl.uniprot.org/uniprot/A0A0M6L0N6|||http://purl.uniprot.org/uniprot/Q9CQ58 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prolactin-8A9 ^@ http://purl.uniprot.org/annotation/PRO_0000045327|||http://purl.uniprot.org/annotation/PRO_5015043308 http://togogenome.org/gene/10090:Slfn5 ^@ http://purl.uniprot.org/uniprot/Q8CBA2 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Schlafen family member 5 ^@ http://purl.uniprot.org/annotation/PRO_0000282983 http://togogenome.org/gene/10090:Mlxipl ^@ http://purl.uniprot.org/uniprot/Q99MZ3 ^@ 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 ^@ Carbohydrate-responsive element-binding protein|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Leucine-zipper|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine|||Polar residues|||Pro residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127505|||http://purl.uniprot.org/annotation/VSP_002174|||http://purl.uniprot.org/annotation/VSP_002175|||http://purl.uniprot.org/annotation/VSP_002176|||http://purl.uniprot.org/annotation/VSP_002177|||http://purl.uniprot.org/annotation/VSP_002178|||http://purl.uniprot.org/annotation/VSP_002179|||http://purl.uniprot.org/annotation/VSP_002180 http://togogenome.org/gene/10090:Tnni2 ^@ http://purl.uniprot.org/uniprot/P13412 ^@ 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|||Disordered|||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_0000186144 http://togogenome.org/gene/10090:Wfdc16 ^@ http://purl.uniprot.org/uniprot/A2A5H4|||http://purl.uniprot.org/uniprot/Q5DQQ4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ WAP ^@ http://purl.uniprot.org/annotation/PRO_5014309747 http://togogenome.org/gene/10090:Ctsj ^@ http://purl.uniprot.org/uniprot/A0A0R4J0V8|||http://purl.uniprot.org/uniprot/Q9R014 ^@ 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|||Cathepsin J|||Cathepsin propeptide inhibitor|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000026230|||http://purl.uniprot.org/annotation/PRO_0000026231|||http://purl.uniprot.org/annotation/PRO_5015018183 http://togogenome.org/gene/10090:Or8g2 ^@ http://purl.uniprot.org/uniprot/Q8VFN5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:BC051665 ^@ http://purl.uniprot.org/uniprot/E9Q623|||http://purl.uniprot.org/uniprot/Q3ULD9|||http://purl.uniprot.org/uniprot/Q80X23 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Cathepsin L1-like|||Cathepsin propeptide inhibitor|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_5018656013|||http://purl.uniprot.org/annotation/PRO_5018669853|||http://purl.uniprot.org/annotation/PRO_5018759054 http://togogenome.org/gene/10090:Spaar ^@ http://purl.uniprot.org/uniprot/A0A1B0GSZ0|||http://purl.uniprot.org/uniprot/Q9D3L1 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Small regulatory polypeptide of amino acid response ^@ http://purl.uniprot.org/annotation/PRO_0000439039 http://togogenome.org/gene/10090:Aifm2 ^@ http://purl.uniprot.org/uniprot/Q8BUE4 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Site|||Splice Variant|||Transmembrane ^@ 4-hydroxy-2-nonenal adduction|||Decreases the NADH oxidoreductase activity. Has not effect on mitochondria to nucleus translocation.|||Ferroptosis suppressor protein 1|||Helical|||Impairs the NADH oxidoreductase activity. Impairs mitochondria to nucleus translocation. Confers protection to doxorubicin-induced cytotoxicity.|||In isoform 2.|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000238923|||http://purl.uniprot.org/annotation/VSP_052049 http://togogenome.org/gene/10090:Cdh2 ^@ http://purl.uniprot.org/uniprot/P15116|||http://purl.uniprot.org/uniprot/Q3UIC2|||http://purl.uniprot.org/uniprot/Q8BSI9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes dimerization.|||CRISPR/Cas9-mutated knockin mice manifest motor-associated features of hyperactivity such as greater traveling distance, increased velocity and prolonged mobility time compared with control mice. Synaptic release is attenuated in neuron from mutant mice and synaptic vesicle clusters size is reduced in presynaptic terminals.|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin domain-containing protein|||Cadherin-2|||Cytoplasmic|||Decreased calcium-dependent cell-cell adhesion.|||Disordered|||Extracellular|||Helical|||Loss of calcium-dependent cell-cell adhesion.|||Loss of dimerization; when associated with A-161.|||Loss of dimerization; when associated with E-173.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Severely impaired the binding of calcium to all three sites. ^@ http://purl.uniprot.org/annotation/PRO_0000003733|||http://purl.uniprot.org/annotation/PRO_0000003734|||http://purl.uniprot.org/annotation/PRO_5004229985|||http://purl.uniprot.org/annotation/PRO_5004304240 http://togogenome.org/gene/10090:Herpud2 ^@ http://purl.uniprot.org/uniprot/Q9JJC9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 2 protein|||Polar residues|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000280628 http://togogenome.org/gene/10090:Pcbp1 ^@ http://purl.uniprot.org/uniprot/P60335 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KH 1|||KH 2|||KH 3|||N-acetylmethionine|||Phosphoserine|||Poly(rC)-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000050088 http://togogenome.org/gene/10090:Xntrpc ^@ http://purl.uniprot.org/uniprot/F8VQM8 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Transient receptor ion channel ^@ http://togogenome.org/gene/10090:Zbtb7a ^@ http://purl.uniprot.org/uniprot/O88939 ^@ 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 ^@ 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 SUMO2)|||In isoform 2.|||Mediates interaction with KHDRBS1|||Mediates interaction with RELA|||Mediates interaction with SMAD4|||Phosphoserine|||Zinc finger and BTB domain-containing protein 7A ^@ http://purl.uniprot.org/annotation/PRO_0000047716|||http://purl.uniprot.org/annotation/VSP_035026 http://togogenome.org/gene/10090:Hoxd8 ^@ http://purl.uniprot.org/uniprot/A2ASN1|||http://purl.uniprot.org/uniprot/F6W963|||http://purl.uniprot.org/uniprot/P23463|||http://purl.uniprot.org/uniprot/Q9CUH8|||http://purl.uniprot.org/uniprot/Q9CUQ8 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Non-terminal Residue|||Region ^@ Antp-type hexapeptide|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Hox-D8|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000200217 http://togogenome.org/gene/10090:Dysf ^@ http://purl.uniprot.org/uniprot/A0A0N4SUN3|||http://purl.uniprot.org/uniprot/A0A0N4SV63|||http://purl.uniprot.org/uniprot/A0A0N4SVX9|||http://purl.uniprot.org/uniprot/A0A0N4SWH3|||http://purl.uniprot.org/uniprot/E9Q423|||http://purl.uniprot.org/uniprot/Q9ESD7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||C2|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||C2 6|||C2 7|||Cytoplasmic|||Disordered|||Dysferlin|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000057880|||http://purl.uniprot.org/annotation/VSP_035930|||http://purl.uniprot.org/annotation/VSP_035931|||http://purl.uniprot.org/annotation/VSP_035932|||http://purl.uniprot.org/annotation/VSP_035933 http://togogenome.org/gene/10090:Vmn1r177 ^@ http://purl.uniprot.org/uniprot/E9PXM3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Npy5r ^@ http://purl.uniprot.org/uniprot/O70342|||http://purl.uniprot.org/uniprot/Q543U8 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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-linked (GlcNAc...) asparagine|||Neuropeptide Y receptor type 5|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069940 http://togogenome.org/gene/10090:Igdcc4 ^@ http://purl.uniprot.org/uniprot/Q9EQS9 ^@ 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 ^@ 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|||Immunoglobulin superfamily DCC subclass member 4|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000304623|||http://purl.uniprot.org/annotation/VSP_028047|||http://purl.uniprot.org/annotation/VSP_028048 http://togogenome.org/gene/10090:Hoxb4 ^@ http://purl.uniprot.org/uniprot/P10284 ^@ 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-B4|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000200123 http://togogenome.org/gene/10090:Tfpi ^@ http://purl.uniprot.org/uniprot/O54819|||http://purl.uniprot.org/uniprot/Q8BSB7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ BPTI/Kunitz inhibitor|||BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||BPTI/Kunitz inhibitor 3|||In isoform Beta.|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Tissue factor pathway inhibitor ^@ http://purl.uniprot.org/annotation/PRO_0000016873|||http://purl.uniprot.org/annotation/PRO_5015024081|||http://purl.uniprot.org/annotation/VSP_003032|||http://purl.uniprot.org/annotation/VSP_003033 http://togogenome.org/gene/10090:Klra4 ^@ http://purl.uniprot.org/uniprot/Q542S4|||http://purl.uniprot.org/uniprot/Q60651 ^@ 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|||Helical; Signal-anchor for type II membrane protein|||In isoform D2.|||In strain: NOD and NOR.|||Killer cell lectin-like receptor 4|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046682|||http://purl.uniprot.org/annotation/VSP_003068 http://togogenome.org/gene/10090:Rcor3 ^@ http://purl.uniprot.org/uniprot/A0A0A6YWP7|||http://purl.uniprot.org/uniprot/A0A0A6YWY4|||http://purl.uniprot.org/uniprot/A0A0A6YXM5|||http://purl.uniprot.org/uniprot/B2RSN6|||http://purl.uniprot.org/uniprot/Q6PGA0 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||ELM2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||REST corepressor 3|||SANT ^@ http://purl.uniprot.org/annotation/PRO_0000226782|||http://purl.uniprot.org/annotation/VSP_017463|||http://purl.uniprot.org/annotation/VSP_017464 http://togogenome.org/gene/10090:Trim52 ^@ http://purl.uniprot.org/uniprot/Q8CDV4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Pro residues|||RING-type ^@ http://togogenome.org/gene/10090:Ms4a1 ^@ http://purl.uniprot.org/uniprot/P19437|||http://purl.uniprot.org/uniprot/Q542S5 ^@ Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Lipid Binding|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ B-lymphocyte antigen CD20|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Phosphothreonine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000158628 http://togogenome.org/gene/10090:Cd70 ^@ http://purl.uniprot.org/uniprot/O55237|||http://purl.uniprot.org/uniprot/Q05A52 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ CD70 antigen|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||TNF family profile ^@ http://purl.uniprot.org/annotation/PRO_0000185498 http://togogenome.org/gene/10090:Acaa1b ^@ http://purl.uniprot.org/uniprot/Q3UKM0|||http://purl.uniprot.org/uniprot/Q8VCH0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Site|||Transit Peptide ^@ 3-ketoacyl-CoA thiolase B, peroxisomal|||Acyl-thioester intermediate|||Increases nucleophilicity of active site Cys|||N6-acetyllysine|||PTS2-type peroxisomal targeting signal|||Peroxisome|||Proton acceptor|||Proton donor/acceptor|||Thiolase C-terminal|||Thiolase N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000034069 http://togogenome.org/gene/10090:Vmn1r67 ^@ http://purl.uniprot.org/uniprot/A6H640|||http://purl.uniprot.org/uniprot/G5E8C1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Garin4 ^@ http://purl.uniprot.org/uniprot/B7XG49 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Golgi associated RAB2 interactor protein-like Rab2B-binding ^@ http://togogenome.org/gene/10090:Chrdl1 ^@ http://purl.uniprot.org/uniprot/Q3TP73|||http://purl.uniprot.org/uniprot/Q920C1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Cell attachment site|||Chordin-like protein 1|||Disordered|||In isoform Beta.|||N-linked (GlcNAc...) asparagine|||VWFC|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000005369|||http://purl.uniprot.org/annotation/PRO_5010843311|||http://purl.uniprot.org/annotation/VSP_001076|||http://purl.uniprot.org/annotation/VSP_001077 http://togogenome.org/gene/10090:Ttll10 ^@ http://purl.uniprot.org/uniprot/A4Q9F3|||http://purl.uniprot.org/uniprot/B1ASM0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Essential for specifying elongation versus initiation step of the polyglycylase activity|||In isoform 2.|||Loss of NAP1 polyglycylase activity.|||Polar residues|||Pro residues|||Protein polyglycylase TTLL10|||TTL ^@ http://purl.uniprot.org/annotation/PRO_0000324522|||http://purl.uniprot.org/annotation/VSP_032265 http://togogenome.org/gene/10090:Mup3 ^@ http://purl.uniprot.org/uniprot/P04939|||http://purl.uniprot.org/uniprot/Q3KQQ2 ^@ 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 ^@ Lipocalin/cytosolic fatty-acid binding|||Major urinary protein 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017929|||http://purl.uniprot.org/annotation/PRO_5015097412 http://togogenome.org/gene/10090:Elac1 ^@ http://purl.uniprot.org/uniprot/Q8VEB6 ^@ 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.|||Proton acceptor|||Zinc phosphodiesterase ELAC protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000155826|||http://purl.uniprot.org/annotation/VSP_009167 http://togogenome.org/gene/10090:Slc39a4 ^@ http://purl.uniprot.org/uniprot/Q78IQ7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Essential for SLC39A4 endocytosis|||Essential role in Zn(2+) sensing|||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|||In isoform 2.|||Loss of zinc uptake activity. Abolishes plasma membrane localization.|||M1 metal binding site|||M2 metal binding site|||N-linked (GlcNAc...) asparagine|||Reduces zinc uptake activity. Accumulated to high levels in the plasma membrane. Does not affect KM. No longer zinc responsive.|||Reduces zinc uptake activity. Does not affect KM. Accumulated to high levels in the plasma membrane. No longer zinc responsive.|||Reduces zinc uptake activity. Reduces plasma membrane localization.|||Zinc transporter ZIP4 ^@ http://purl.uniprot.org/annotation/PRO_0000042621|||http://purl.uniprot.org/annotation/VSP_015913|||http://purl.uniprot.org/annotation/VSP_015914 http://togogenome.org/gene/10090:Oprl1 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPZ9|||http://purl.uniprot.org/uniprot/B0R0C0|||http://purl.uniprot.org/uniprot/P35377|||http://purl.uniprot.org/uniprot/Q542U1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Site|||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|||Important for G protein-mediated signaling|||In isoform KOR3A.|||In isoform KOR3B.|||In isoform KOR3C.|||In isoform KOR3D.|||In isoform KOR3E.|||N-linked (GlcNAc...) asparagine|||Nociceptin receptor|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069981|||http://purl.uniprot.org/annotation/VSP_001898|||http://purl.uniprot.org/annotation/VSP_001899|||http://purl.uniprot.org/annotation/VSP_001900|||http://purl.uniprot.org/annotation/VSP_001901|||http://purl.uniprot.org/annotation/VSP_001902|||http://purl.uniprot.org/annotation/VSP_001903|||http://purl.uniprot.org/annotation/VSP_001904|||http://purl.uniprot.org/annotation/VSP_001905|||http://purl.uniprot.org/annotation/VSP_001906 http://togogenome.org/gene/10090:Cfap95 ^@ http://purl.uniprot.org/uniprot/Q9CQC3 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cilia- and flagella-associated protein 95|||Cytoplasmic|||Disordered|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000271064 http://togogenome.org/gene/10090:Fbxw8 ^@ http://purl.uniprot.org/uniprot/Q8BIA4 ^@ 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|||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_0000050998|||http://purl.uniprot.org/annotation/VSP_008502 http://togogenome.org/gene/10090:Serpinf1 ^@ http://purl.uniprot.org/uniprot/P97298 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pigment epithelium-derived factor|||Polar residues|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000032509 http://togogenome.org/gene/10090:Ces4a ^@ http://purl.uniprot.org/uniprot/Q8R0W5 ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Acyl-ester intermediate|||Carboxylesterase 4A|||Charge relay system|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000325924 http://togogenome.org/gene/10090:Vopp1 ^@ http://purl.uniprot.org/uniprot/Q8R1C3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Pro residues|||WW domain binding protein VOPP1 ^@ http://purl.uniprot.org/annotation/PRO_0000325918|||http://purl.uniprot.org/annotation/VSP_032478|||http://purl.uniprot.org/annotation/VSP_032479 http://togogenome.org/gene/10090:Defa5 ^@ http://purl.uniprot.org/uniprot/L7N230 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Mammalian defensins ^@ http://purl.uniprot.org/annotation/PRO_5003982199 http://togogenome.org/gene/10090:Tm4sf5 ^@ http://purl.uniprot.org/uniprot/Q91XF2|||http://purl.uniprot.org/uniprot/Q9D8G1 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Glod5 ^@ http://purl.uniprot.org/uniprot/Q9D8I3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Glyoxalase domain-containing protein 5|||VOC ^@ http://purl.uniprot.org/annotation/PRO_0000305327 http://togogenome.org/gene/10090:Ncmap ^@ http://purl.uniprot.org/uniprot/A2A992|||http://purl.uniprot.org/uniprot/Q99JS0 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Noncompact myelin-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000265079 http://togogenome.org/gene/10090:Alkbh6 ^@ http://purl.uniprot.org/uniprot/Q8K2U2 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Alpha-ketoglutarate-dependent dioxygenase alkB homolog 6|||Fe2OG dioxygenase ^@ http://purl.uniprot.org/annotation/PRO_0000323717 http://togogenome.org/gene/10090:Entpd1 ^@ http://purl.uniprot.org/uniprot/P55772|||http://purl.uniprot.org/uniprot/Q544U5|||http://purl.uniprot.org/uniprot/Q8CDV7 ^@ 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|||Ectonucleoside triphosphate diphosphohydrolase 1|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000209903 http://togogenome.org/gene/10090:Ly6c1 ^@ http://purl.uniprot.org/uniprot/A0A087WNZ5|||http://purl.uniprot.org/uniprot/A0A087WRG9|||http://purl.uniprot.org/uniprot/P0CW02 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ GPI-anchor amidated glycine|||Lymphocyte antigen 6C1|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000408033|||http://purl.uniprot.org/annotation/PRO_0000408034|||http://purl.uniprot.org/annotation/PRO_5001831786|||http://purl.uniprot.org/annotation/PRO_5001831844 http://togogenome.org/gene/10090:Or4f15 ^@ http://purl.uniprot.org/uniprot/Q8VF83 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zmym6 ^@ http://purl.uniprot.org/uniprot/A2A7U2|||http://purl.uniprot.org/uniprot/Q8BS54 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||TRASH ^@ http://togogenome.org/gene/10090:Klrd1 ^@ http://purl.uniprot.org/uniprot/O54707 ^@ 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-type lectin|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Interchain (with C-116 in KLRC1/NGK2A)|||N-linked (GlcNAc...) asparagine|||Natural killer cells antigen CD94 ^@ http://purl.uniprot.org/annotation/PRO_0000378458 http://togogenome.org/gene/10090:Tcf25 ^@ http://purl.uniprot.org/uniprot/B2ZAC8|||http://purl.uniprot.org/uniprot/Q8R3L2 ^@ 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 4.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Ribosome quality control complex subunit TCF25 ^@ http://purl.uniprot.org/annotation/PRO_0000087266|||http://purl.uniprot.org/annotation/VSP_020023|||http://purl.uniprot.org/annotation/VSP_020024|||http://purl.uniprot.org/annotation/VSP_020025|||http://purl.uniprot.org/annotation/VSP_020026|||http://purl.uniprot.org/annotation/VSP_020027|||http://purl.uniprot.org/annotation/VSP_020028 http://togogenome.org/gene/10090:Bcap29 ^@ http://purl.uniprot.org/uniprot/Q542A1|||http://purl.uniprot.org/uniprot/Q61334 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Motif|||Topological Domain|||Transmembrane ^@ B-cell receptor-associated protein 29|||BAP29/BAP31 transmembrane|||Bap31/Bap29 cytoplasmic coiled-coil|||Cytoplasmic|||Di-lysine motif|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000142889 http://togogenome.org/gene/10090:Atp9b ^@ http://purl.uniprot.org/uniprot/A0A286YCV0|||http://purl.uniprot.org/uniprot/D3YV00|||http://purl.uniprot.org/uniprot/P98195 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Polar residues|||Probable phospholipid-transporting ATPase IIB ^@ http://purl.uniprot.org/annotation/PRO_0000046378|||http://purl.uniprot.org/annotation/VSP_035908 http://togogenome.org/gene/10090:Oaz3 ^@ http://purl.uniprot.org/uniprot/Q9R109 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Ornithine decarboxylase antizyme 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000220860 http://togogenome.org/gene/10090:Zhx3 ^@ http://purl.uniprot.org/uniprot/Q3UPQ8|||http://purl.uniprot.org/uniprot/Q8C0Q2 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||Homeobox|||Homeobox 1|||Homeobox 2|||Homeobox 3|||Homeobox 4|||Homeobox 5|||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_0000049396 http://togogenome.org/gene/10090:Kif26a ^@ http://purl.uniprot.org/uniprot/Q52KG5 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Kinesin motor|||Kinesin-like protein KIF26A|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000307300 http://togogenome.org/gene/10090:Frmpd3 ^@ http://purl.uniprot.org/uniprot/A0A140LIW3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||FERM|||PDZ|||Polar residues|||Pro residues|||Ras-associating ^@ http://togogenome.org/gene/10090:Ptges3l ^@ http://purl.uniprot.org/uniprot/Q9D9A7 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ CS|||In isoform 2.|||Putative protein PTGES3L ^@ http://purl.uniprot.org/annotation/PRO_0000418441|||http://purl.uniprot.org/annotation/VSP_044056 http://togogenome.org/gene/10090:Rac2 ^@ http://purl.uniprot.org/uniprot/Q05144 ^@ 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|||N6-acetyllysine|||Ras-related C3 botulinum toxin substrate 2|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000042048|||http://purl.uniprot.org/annotation/PRO_0000042049 http://togogenome.org/gene/10090:Ptcd1 ^@ http://purl.uniprot.org/uniprot/Q8C2E4 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||PPR 1|||PPR 2|||PPR 3|||PPR 4|||PPR 5|||PPR 6|||PPR 7|||PPR 8|||PPR 9|||Pentatricopeptide repeat-containing protein 1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000097090 http://togogenome.org/gene/10090:Sdf2l1 ^@ http://purl.uniprot.org/uniprot/Q9ESP1 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||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_0000031958 http://togogenome.org/gene/10090:Slc26a11 ^@ http://purl.uniprot.org/uniprot/Q80ZD3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||STAS|||Sodium-independent sulfate anion transporter ^@ http://purl.uniprot.org/annotation/PRO_0000320687|||http://purl.uniprot.org/annotation/VSP_052687|||http://purl.uniprot.org/annotation/VSP_052688 http://togogenome.org/gene/10090:Tnfsf13b ^@ http://purl.uniprot.org/uniprot/A0A0U5J6R6|||http://purl.uniprot.org/uniprot/Q3KP92|||http://purl.uniprot.org/uniprot/Q8BVA3|||http://purl.uniprot.org/uniprot/Q9WU72 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In strain: NZB.|||N-linked (GlcNAc...) asparagine|||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_0000034530|||http://purl.uniprot.org/annotation/PRO_0000034531|||http://purl.uniprot.org/annotation/VSP_041184 http://togogenome.org/gene/10090:Rrn3 ^@ http://purl.uniprot.org/uniprot/B2RS91 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||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_0000384905 http://togogenome.org/gene/10090:Sf3a1 ^@ http://purl.uniprot.org/uniprot/Q3TVM1|||http://purl.uniprot.org/uniprot/Q8K4Z5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Strand|||Turn ^@ Acidic residues|||Basic and acidic residues|||Critical for binding to SF3A3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Pro residues|||Required and sufficient for nuclear import|||SURP motif|||SURP motif 1|||SURP motif 2|||Splicing factor 3A subunit 1|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000114918 http://togogenome.org/gene/10090:Cyp2c65 ^@ http://purl.uniprot.org/uniprot/Q148B1|||http://purl.uniprot.org/uniprot/Q9CVC8 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Signal Peptide ^@ Chain|||Non-terminal Residue|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015097031 http://togogenome.org/gene/10090:Gulp1 ^@ http://purl.uniprot.org/uniprot/E0CXC5|||http://purl.uniprot.org/uniprot/Q8K2A1 ^@ 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.|||PID|||PTB domain-containing engulfment adapter protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000296680|||http://purl.uniprot.org/annotation/VSP_027252 http://togogenome.org/gene/10090:Ogfod3 ^@ http://purl.uniprot.org/uniprot/Q9D136 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||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|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000325886 http://togogenome.org/gene/10090:Nutm2 ^@ http://purl.uniprot.org/uniprot/Q3V0C3 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||NUT family member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000337996 http://togogenome.org/gene/10090:Cyp4f13 ^@ http://purl.uniprot.org/uniprot/Q99N19 ^@ Binding Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Uchl3 ^@ http://purl.uniprot.org/uniprot/Q8BWQ9|||http://purl.uniprot.org/uniprot/Q9JKB1 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Important for enzyme activity|||Interaction with ubiquitin|||Interaction with ubiquitin. Crossover loop which restricts access of large ubiquitin adducts to the active site|||No increase in phosphorylation of AKT1, FOXO1 and INSR. No increased expression of SLC2A1, FABP4 nor ADIPOQ. Impaired formation of large lipid droplets.|||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_0000211062 http://togogenome.org/gene/10090:Il36b ^@ http://purl.uniprot.org/uniprot/Q9D6Z6 ^@ Chain|||Molecule Processing|||Propeptide ^@ Chain|||Propeptide ^@ Interleukin-36 beta ^@ http://purl.uniprot.org/annotation/PRO_0000153647|||http://purl.uniprot.org/annotation/PRO_0000430548 http://togogenome.org/gene/10090:Appl1 ^@ http://purl.uniprot.org/uniprot/Q8K3H0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ BAR|||Basic and acidic residues|||DCC-interacting protein 13-alpha|||Disordered|||F&H|||PH|||PID|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Required for RAB5A binding ^@ http://purl.uniprot.org/annotation/PRO_0000079986 http://togogenome.org/gene/10090:Lyrm4 ^@ http://purl.uniprot.org/uniprot/Q8K215 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ LYR motif-containing protein 4|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000174309 http://togogenome.org/gene/10090:Cmbl ^@ http://purl.uniprot.org/uniprot/Q8R1G2 ^@ Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Carboxymethylenebutenolidase homolog|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000308189 http://togogenome.org/gene/10090:Slc35c2 ^@ http://purl.uniprot.org/uniprot/Q5GMH2|||http://purl.uniprot.org/uniprot/Q8VCX2 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier family 35 member C2|||Sugar phosphate transporter ^@ http://purl.uniprot.org/annotation/PRO_0000213400 http://togogenome.org/gene/10090:Henmt1 ^@ http://purl.uniprot.org/uniprot/Q8CAE2 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict|||Splice Variant ^@ Abolishes methyltransferase activity.|||In isoform 2.|||Small RNA 2'-O-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000304141|||http://purl.uniprot.org/annotation/VSP_028012 http://togogenome.org/gene/10090:Pggt1b ^@ http://purl.uniprot.org/uniprot/Q8BUY9 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Repeat ^@ Geranylgeranyl transferase type-1 subunit beta|||PFTB 1|||PFTB 2|||PFTB 3|||PFTB 4 ^@ http://purl.uniprot.org/annotation/PRO_0000119770 http://togogenome.org/gene/10090:Cfap46 ^@ http://purl.uniprot.org/uniprot/E9Q2C0|||http://purl.uniprot.org/uniprot/Q8BZQ3 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ucn ^@ http://purl.uniprot.org/uniprot/P81615 ^@ Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Modified Residue|||Peptide|||Propeptide|||Signal Peptide ^@ Urocortin|||Valine amide ^@ http://purl.uniprot.org/annotation/PRO_0000006235|||http://purl.uniprot.org/annotation/PRO_0000006236 http://togogenome.org/gene/10090:Or2d4 ^@ http://purl.uniprot.org/uniprot/Q9EP55 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Srxn1 ^@ http://purl.uniprot.org/uniprot/A2AQU8|||http://purl.uniprot.org/uniprot/Q9D975 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Interchain|||Omega-N-methylarginine|||ParB/Sulfiredoxin|||Phosphoserine|||Sulfiredoxin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000211432 http://togogenome.org/gene/10090:Drc1 ^@ http://purl.uniprot.org/uniprot/Q3USS3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Dynein regulatory complex protein 1|||Loss of DRC1 in spermatozoa of homozygous mice. Sperm flagella have a disorganized axoneme and lack N-DRC, radial spokes and dynein arms. ^@ http://purl.uniprot.org/annotation/PRO_0000277883 http://togogenome.org/gene/10090:Cyp51 ^@ http://purl.uniprot.org/uniprot/Q8K0C4 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Lanosterol 14-alpha demethylase|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000376796 http://togogenome.org/gene/10090:Lrrc10b ^@ http://purl.uniprot.org/uniprot/G3XA50 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Boll ^@ http://purl.uniprot.org/uniprot/E9PWH1|||http://purl.uniprot.org/uniprot/Q924M5 ^@ 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 ^@ DAZ|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein boule-like|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081496|||http://purl.uniprot.org/annotation/VSP_061272|||http://purl.uniprot.org/annotation/VSP_061273 http://togogenome.org/gene/10090:Mmp12 ^@ http://purl.uniprot.org/uniprot/P34960|||http://purl.uniprot.org/uniprot/Q3TCW6 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cysteine switch|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Macrophage metalloelastase|||N-linked (GlcNAc...) asparagine|||Peptidase metallopeptidase|||Phosphotyrosine; by PKDCC|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028778|||http://purl.uniprot.org/annotation/PRO_0000028779 http://togogenome.org/gene/10090:Abcc6 ^@ http://purl.uniprot.org/uniprot/Q9R1S7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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 6|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000093367 http://togogenome.org/gene/10090:Gm867 ^@ http://purl.uniprot.org/uniprot/A0A1W2P7T4 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Tdrd7 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQD1|||http://purl.uniprot.org/uniprot/Q8K1H1 ^@ 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 ^@ Disordered|||HTH OST-type|||HTH OST-type 1|||HTH OST-type 2|||HTH OST-type 3|||Interaction with CABLES1|||Interaction with CDK17|||Phosphoserine|||Polar residues|||Tudor|||Tudor 1|||Tudor 2|||Tudor domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000183170 http://togogenome.org/gene/10090:Rasgef1c ^@ http://purl.uniprot.org/uniprot/Q9D300 ^@ 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.|||N-terminal Ras-GEF|||Polar residues|||Ras-GEF|||Ras-GEF domain-containing family member 1C ^@ http://purl.uniprot.org/annotation/PRO_0000297645|||http://purl.uniprot.org/annotation/VSP_027317 http://togogenome.org/gene/10090:Yrdc ^@ http://purl.uniprot.org/uniprot/Q3U5F4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||Phosphoserine|||Threonylcarbamoyl-AMP synthase|||YrdC-like ^@ http://purl.uniprot.org/annotation/PRO_0000341403 http://togogenome.org/gene/10090:Ms4a13 ^@ http://purl.uniprot.org/uniprot/Q5FWC3 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Membrane-spanning 4-domains subfamily A member 13 ^@ http://purl.uniprot.org/annotation/PRO_0000315056|||http://purl.uniprot.org/annotation/VSP_030478 http://togogenome.org/gene/10090:C1ql2 ^@ http://purl.uniprot.org/uniprot/A0A3B0J351|||http://purl.uniprot.org/uniprot/Q8CFR0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Turn ^@ C1q|||Collagen-like|||Complement C1q-like protein 2|||Disordered|||No effect on homotrimer formation, but loss of higher-order oligomeric complexes; when associated with A-29. Does not affect heterooligomerization with C1QL4; when associated with A-29.|||No effect on homotrimer formation, but loss of higher-order oligomeric complexes; when associated with A-33. Does not affect heterooligomerization with C1QL4; when associated with A-33.|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000274336|||http://purl.uniprot.org/annotation/PRO_5017341241 http://togogenome.org/gene/10090:Utp6 ^@ http://purl.uniprot.org/uniprot/Q8VCY6 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ HAT 1|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||U3 small nucleolar RNA-associated protein 6 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000239466 http://togogenome.org/gene/10090:Fam185a ^@ http://purl.uniprot.org/uniprot/Q7TPD2 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Protein FAM185A ^@ http://purl.uniprot.org/annotation/PRO_0000321831|||http://purl.uniprot.org/annotation/VSP_031805|||http://purl.uniprot.org/annotation/VSP_031806 http://togogenome.org/gene/10090:Lurap1l ^@ http://purl.uniprot.org/uniprot/Q8K2P1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Leucine rich adaptor protein 1-like|||N-acetylmethionine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089741 http://togogenome.org/gene/10090:Trpm7 ^@ http://purl.uniprot.org/uniprot/A2AI57|||http://purl.uniprot.org/uniprot/Q923J1 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Alpha-type protein kinase|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Loss of kinase activity; when associated with A-1813.|||Loss of kinase activity; when associated with A-1820.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pore-forming|||Proton acceptor|||Severe reduction of kinase activity.|||Transient receptor potential cation channel subfamily M member 7 ^@ http://purl.uniprot.org/annotation/PRO_0000215332 http://togogenome.org/gene/10090:Cd226 ^@ http://purl.uniprot.org/uniprot/Q5DW69|||http://purl.uniprot.org/uniprot/Q8K4E2|||http://purl.uniprot.org/uniprot/Q8K4E3|||http://purl.uniprot.org/uniprot/Q8K4F0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ CD226 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000014667|||http://purl.uniprot.org/annotation/PRO_5014309751 http://togogenome.org/gene/10090:Scn9a ^@ http://purl.uniprot.org/uniprot/B1AYL0|||http://purl.uniprot.org/uniprot/E9PW82|||http://purl.uniprot.org/uniprot/Q62205 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Modified Residue|||Region|||Repeat|||Site|||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|||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|||Is directly targeted by the spider protoxin-II|||Phosphoserine; by PKC|||Polar residues|||Pore-forming|||Sodium channel protein type 9 subunit alpha|||Sodium ion transport-associated|||Voltage-gated Na+ ion channel cytoplasmic ^@ http://purl.uniprot.org/annotation/PRO_0000048503 http://togogenome.org/gene/10090:Igll1 ^@ http://purl.uniprot.org/uniprot/P20764 ^@ 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 ^@ C region|||Ig-like C1-type|||Immunoglobulin lambda-like polypeptide 1|||Interchain (with a heavy chain)|||J region ^@ http://purl.uniprot.org/annotation/PRO_0000153611 http://togogenome.org/gene/10090:Exoc4 ^@ http://purl.uniprot.org/uniprot/O35382|||http://purl.uniprot.org/uniprot/Q9CXE1 ^@ 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 ^@ Disordered|||Exocyst complex component 4|||Exocyst complex component Sec8 N-terminal|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118935 http://togogenome.org/gene/10090:Sec14l3 ^@ http://purl.uniprot.org/uniprot/Q3UWW2|||http://purl.uniprot.org/uniprot/Q5SQ27 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ CRAL-TRIO|||GOLD ^@ http://togogenome.org/gene/10090:Pnpla8 ^@ http://purl.uniprot.org/uniprot/Q8K1N1 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Calcium-independent phospholipase A2-gamma|||DGA/G|||Disordered|||GXGXXG|||GXSXG|||Helical|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Nucleophile|||PNPLA|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000303215 http://togogenome.org/gene/10090:Or55b3 ^@ http://purl.uniprot.org/uniprot/E9PWI5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pigs ^@ http://purl.uniprot.org/uniprot/Q3V307|||http://purl.uniprot.org/uniprot/Q6PD26 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||GPI transamidase component PIG-S|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000218605 http://togogenome.org/gene/10090:Or1o3 ^@ http://purl.uniprot.org/uniprot/Q8VFD9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lcp1 ^@ http://purl.uniprot.org/uniprot/Q61233 ^@ 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|||Region|||Sequence Conflict ^@ 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|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Plastin-2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073744 http://togogenome.org/gene/10090:Galnt10 ^@ http://purl.uniprot.org/uniprot/Q5SQF9|||http://purl.uniprot.org/uniprot/Q6P9S7 ^@ 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|||Flexible loop|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 10|||Ricin B lectin|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059123 http://togogenome.org/gene/10090:Gk ^@ http://purl.uniprot.org/uniprot/B1ASZ3|||http://purl.uniprot.org/uniprot/Q3TEN9|||http://purl.uniprot.org/uniprot/Q3TET2|||http://purl.uniprot.org/uniprot/Q64516 ^@ 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 ^@ Carbohydrate kinase FGGY C-terminal|||Carbohydrate kinase FGGY N-terminal|||Glycerol kinase|||In isoform 1 and isoform 2.|||In isoform 1. ^@ http://purl.uniprot.org/annotation/PRO_0000059538|||http://purl.uniprot.org/annotation/VSP_034650|||http://purl.uniprot.org/annotation/VSP_034651 http://togogenome.org/gene/10090:Rassf2 ^@ http://purl.uniprot.org/uniprot/Q8BMS9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Ras association domain-containing protein 2|||Ras-associating|||SARAH ^@ http://purl.uniprot.org/annotation/PRO_0000233038 http://togogenome.org/gene/10090:Or4c109 ^@ http://purl.uniprot.org/uniprot/A2ATG3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:D430041D05Rik ^@ http://purl.uniprot.org/uniprot/D3YZ21|||http://purl.uniprot.org/uniprot/F6ZGR6 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Adgrg1 ^@ http://purl.uniprot.org/uniprot/Q8K209 ^@ Binding Site|||Chain|||Domain Extent|||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|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ ADGRG1 C-terminal fragment|||ADGRG1 N-terminal fragment|||Abolishes proteolytic cleavage and cell surface localization.|||Adhesion G-protein coupled receptor G1|||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|||N-linked (GlcNAc...) asparagine|||Reduced cell surface localization. ^@ http://purl.uniprot.org/annotation/PRO_0000012882|||http://purl.uniprot.org/annotation/PRO_0000436505|||http://purl.uniprot.org/annotation/PRO_0000436506 http://togogenome.org/gene/10090:Smtn ^@ http://purl.uniprot.org/uniprot/Q921U8 ^@ 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 ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||In isoform L2 and isoform S2.|||In isoform S1 and isoform S2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Smoothelin ^@ http://purl.uniprot.org/annotation/PRO_0000318593|||http://purl.uniprot.org/annotation/VSP_031243|||http://purl.uniprot.org/annotation/VSP_031244 http://togogenome.org/gene/10090:Bola1 ^@ http://purl.uniprot.org/uniprot/Q9D8S9 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ BolA-like protein 1|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000201234 http://togogenome.org/gene/10090:S1pr5 ^@ http://purl.uniprot.org/uniprot/Q91X56 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Modified Residue|||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|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine|||Sphingosine 1-phosphate receptor 5 ^@ http://purl.uniprot.org/annotation/PRO_0000069437 http://togogenome.org/gene/10090:Vmn1r18 ^@ http://purl.uniprot.org/uniprot/Q8R2C8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Plin2 ^@ http://purl.uniprot.org/uniprot/P43883 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ N-acetylalanine|||Perilipin-2|||Phosphoserine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000099889 http://togogenome.org/gene/10090:Isca1 ^@ http://purl.uniprot.org/uniprot/Q9D924 ^@ Binding Site|||Chain|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Transit Peptide ^@ Iron-sulfur cluster assembly 1 homolog, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000042736 http://togogenome.org/gene/10090:Hnmt ^@ http://purl.uniprot.org/uniprot/A2AQK4|||http://purl.uniprot.org/uniprot/Q91VF2 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Histamine N-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000084022 http://togogenome.org/gene/10090:Cluap1 ^@ http://purl.uniprot.org/uniprot/Q8R3P7 ^@ 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|||Clusterin-associated protein 1|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000239453 http://togogenome.org/gene/10090:Or52b2 ^@ http://purl.uniprot.org/uniprot/Q8VGW5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tmtc2 ^@ http://purl.uniprot.org/uniprot/Q56A06 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Repeat|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein O-mannosyl-transferase TMTC2|||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_0000280304|||http://purl.uniprot.org/annotation/VSP_023628|||http://purl.uniprot.org/annotation/VSP_023629 http://togogenome.org/gene/10090:Eipr1 ^@ http://purl.uniprot.org/uniprot/Q8K0G5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ EARP and GARP complex-interacting protein 1|||N-acetylmethionine|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000051300 http://togogenome.org/gene/10090:Ero1a ^@ http://purl.uniprot.org/uniprot/Q4FK57|||http://purl.uniprot.org/uniprot/Q8R180 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Alternate|||ERO1-like protein alpha|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphoserine|||Redox-active|||Redox-active; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000008416|||http://purl.uniprot.org/annotation/PRO_5014309355 http://togogenome.org/gene/10090:Mtrr ^@ http://purl.uniprot.org/uniprot/A0A0R4J0G9|||http://purl.uniprot.org/uniprot/Q8C1A3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ FAD-binding FR-type|||Flavodoxin-like|||Hinge|||Methionine synthase reductase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000409308 http://togogenome.org/gene/10090:Unc79 ^@ http://purl.uniprot.org/uniprot/Q0KK59 ^@ 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|||Polar residues|||Protein unc-79 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000315619 http://togogenome.org/gene/10090:Sidt1 ^@ http://purl.uniprot.org/uniprot/E9Q247|||http://purl.uniprot.org/uniprot/Q6AXF6|||http://purl.uniprot.org/uniprot/Q6Q3F6|||http://purl.uniprot.org/uniprot/Q8BZK2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreased affinity for 700-bp RNA.|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||SID1 transmembrane family member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000032576|||http://purl.uniprot.org/annotation/PRO_5003243057|||http://purl.uniprot.org/annotation/VSP_013522 http://togogenome.org/gene/10090:Dennd3 ^@ http://purl.uniprot.org/uniprot/A2RT67 ^@ 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 ^@ Abolishes interaction with 14-3-3 proteins.|||Abrogates the intramolecular linker-DENN domain interaction and enhances GEF activity towards Rab12.|||Basic and acidic residues|||DENN domain-containing protein 3|||Disordered|||Greatly reduces interaction with 14-3-3 proteins.|||Linker|||Phosphoserine; by ULK1|||Phosphotyrosine|||Retains the intramolecular linker-DENN domain interaction and impairs GEF activity towards Rab12.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000304673 http://togogenome.org/gene/10090:Or5ak4 ^@ http://purl.uniprot.org/uniprot/Q7TRA2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Irx2 ^@ http://purl.uniprot.org/uniprot/P81066 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Homeobox; TALE-type|||Iroquois-class homeodomain protein IRX-2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000049154 http://togogenome.org/gene/10090:Brme1 ^@ http://purl.uniprot.org/uniprot/Q6DIA7 ^@ 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|||Break repair meiotic recombinase recruitment factor 1|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Required for interaction with HSF2BP|||Required for nuclear location ^@ http://purl.uniprot.org/annotation/PRO_0000295738|||http://purl.uniprot.org/annotation/VSP_027045 http://togogenome.org/gene/10090:Ggact ^@ http://purl.uniprot.org/uniprot/Q923B0 ^@ 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 ^@ Gamma-glutamylaminecyclotransferase|||In isoform 2.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000320204|||http://purl.uniprot.org/annotation/VSP_031641|||http://purl.uniprot.org/annotation/VSP_031642 http://togogenome.org/gene/10090:Vmn1r112 ^@ http://purl.uniprot.org/uniprot/G3UY48 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nab2 ^@ http://purl.uniprot.org/uniprot/Q3TYF1|||http://purl.uniprot.org/uniprot/Q61127 ^@ 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 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.|||NAB co-repressor|||NCD1|||NCD2|||NGFI-A-binding protein 2|||Nab N-terminal|||Necessary for nuclear localization|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000077043|||http://purl.uniprot.org/annotation/VSP_003388|||http://purl.uniprot.org/annotation/VSP_003389 http://togogenome.org/gene/10090:Zc3h18 ^@ http://purl.uniprot.org/uniprot/G3X8T2|||http://purl.uniprot.org/uniprot/H3BIW0|||http://purl.uniprot.org/uniprot/Q0P678 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||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 SUMO2)|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger CCCH domain-containing protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000311243|||http://purl.uniprot.org/annotation/VSP_029456|||http://purl.uniprot.org/annotation/VSP_029457 http://togogenome.org/gene/10090:Fcgr1 ^@ http://purl.uniprot.org/uniprot/P26151 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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|||Interaction with EPB41L2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000015140 http://togogenome.org/gene/10090:Srpk2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J124|||http://purl.uniprot.org/uniprot/O54781|||http://purl.uniprot.org/uniprot/Q8CBI1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Acidic residues|||Cleavage; by caspase-3|||Disordered|||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_0000086678|||http://purl.uniprot.org/annotation/PRO_0000414753|||http://purl.uniprot.org/annotation/PRO_0000414754 http://togogenome.org/gene/10090:Ankrd13b ^@ http://purl.uniprot.org/uniprot/Q5F259 ^@ 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 ^@ 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_0000240644|||http://purl.uniprot.org/annotation/VSP_019405 http://togogenome.org/gene/10090:Zfp511 ^@ http://purl.uniprot.org/uniprot/Q6P0X2 ^@ 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 2.|||Omega-N-methylarginine|||Zinc finger protein 511 ^@ http://purl.uniprot.org/annotation/PRO_0000353091|||http://purl.uniprot.org/annotation/VSP_035623 http://togogenome.org/gene/10090:Procr ^@ http://purl.uniprot.org/uniprot/Q64695|||http://purl.uniprot.org/uniprot/Q8K357 ^@ 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|||Endothelial protein C receptor|||Extracellular|||Helical|||MHC class I-like antigen recognition-like|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000021192|||http://purl.uniprot.org/annotation/PRO_5014312167 http://togogenome.org/gene/10090:Cfap119 ^@ http://purl.uniprot.org/uniprot/Q6NZQ0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Cilia- and flagella-associated protein 119|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000321843 http://togogenome.org/gene/10090:Gramd2a ^@ http://purl.uniprot.org/uniprot/Q3V3G7 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||GRAM|||GRAM domain-containing protein 2A|||Helical|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000287455|||http://purl.uniprot.org/annotation/VSP_025478 http://togogenome.org/gene/10090:Itprip ^@ http://purl.uniprot.org/uniprot/Q3TNL8 ^@ Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Inositol 1,4,5-trisphosphate receptor-interacting protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000293729|||http://purl.uniprot.org/annotation/VSP_026571 http://togogenome.org/gene/10090:Ssr4 ^@ http://purl.uniprot.org/uniprot/Q3TVJ8|||http://purl.uniprot.org/uniprot/Q62186|||http://purl.uniprot.org/uniprot/Q9D8L3 ^@ Chain|||Crosslink|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Disulfide Bond|||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_0000033293|||http://purl.uniprot.org/annotation/PRO_5010843329|||http://purl.uniprot.org/annotation/PRO_5015099683 http://togogenome.org/gene/10090:Prepl ^@ http://purl.uniprot.org/uniprot/Q8BKS6|||http://purl.uniprot.org/uniprot/Q8C167 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant ^@ Charge relay system|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of catalytic activity. No effect on the redistribution of AP-1 from the membrane to the cytoplasm.|||Peptidase S9 prolyl oligopeptidase catalytic|||Peptidase S9A N-terminal|||Phosphoserine|||Prolyl endopeptidase-like ^@ http://purl.uniprot.org/annotation/PRO_0000314862|||http://purl.uniprot.org/annotation/VSP_030404|||http://purl.uniprot.org/annotation/VSP_030405|||http://purl.uniprot.org/annotation/VSP_030406|||http://purl.uniprot.org/annotation/VSP_030407 http://togogenome.org/gene/10090:Or8b1 ^@ http://purl.uniprot.org/uniprot/K7N5P3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gpr6 ^@ http://purl.uniprot.org/uniprot/Q6YNI2 ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 6|||Helical; 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_0000069515 http://togogenome.org/gene/10090:Faf1 ^@ http://purl.uniprot.org/uniprot/P54731 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||FAS-associated factor 1|||Phosphoserine|||Phosphothreonine|||UBA|||UBX ^@ http://purl.uniprot.org/annotation/PRO_0000211039 http://togogenome.org/gene/10090:Tmem11 ^@ http://purl.uniprot.org/uniprot/Q8BK08 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Transmembrane protein 11, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000072563 http://togogenome.org/gene/10090:Rims4 ^@ http://purl.uniprot.org/uniprot/P60191 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ C2|||Phosphoserine|||Regulating synaptic membrane exocytosis protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000190208 http://togogenome.org/gene/10090:Pou3f4 ^@ http://purl.uniprot.org/uniprot/A6H6L6|||http://purl.uniprot.org/uniprot/P62515 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||POU domain, class 3, transcription factor 4|||POU-specific|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000100734 http://togogenome.org/gene/10090:Pgc ^@ http://purl.uniprot.org/uniprot/Q9D7R7 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Signal Peptide ^@ Activation peptide|||Gastricsin|||Peptidase A1 ^@ http://purl.uniprot.org/annotation/PRO_0000026063|||http://purl.uniprot.org/annotation/PRO_0000026064 http://togogenome.org/gene/10090:Cryga ^@ http://purl.uniprot.org/uniprot/P04345 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ 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 A ^@ http://purl.uniprot.org/annotation/PRO_0000057595 http://togogenome.org/gene/10090:Ankk1 ^@ http://purl.uniprot.org/uniprot/Q8BZ25 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Repeat ^@ 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 protein kinase domain-containing protein 1|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085621 http://togogenome.org/gene/10090:Fbl ^@ http://purl.uniprot.org/uniprot/P35550 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||rRNA 2'-O-methyltransferase fibrillarin ^@ http://purl.uniprot.org/annotation/PRO_0000148508 http://togogenome.org/gene/10090:Gm10037 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VMN9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB ^@ http://togogenome.org/gene/10090:Noc2l ^@ http://purl.uniprot.org/uniprot/J3QK52|||http://purl.uniprot.org/uniprot/Q3UZI6 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Psg28 ^@ http://purl.uniprot.org/uniprot/Q4KL66 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Or52s19 ^@ http://purl.uniprot.org/uniprot/A2RS33 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnot1 ^@ http://purl.uniprot.org/uniprot/A0A1D5RMJ8|||http://purl.uniprot.org/uniprot/B7ZWL1|||http://purl.uniprot.org/uniprot/Q6ZQ08 ^@ 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 ^@ CCR4-NOT transcription complex subunit 1|||CCR4-NOT transcription complex subunit 1 CAF1-binding|||CCR4-NOT transcription complex subunit 1 HEAT repeat|||CCR4-NOT transcription complex subunit 1 TTP binding|||CCR4-Not complex component Not1 C-terminal|||Disordered|||Homozygous mutant embryos show a small pancreas, exencephaly, eye defects and edema.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Interaction with CNOT6, CNOT6L, CNOT7 and CNOT8|||Interaction with ZFP36|||LXXLL|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315542|||http://purl.uniprot.org/annotation/VSP_030564|||http://purl.uniprot.org/annotation/VSP_030565|||http://purl.uniprot.org/annotation/VSP_030566 http://togogenome.org/gene/10090:Sgcb ^@ http://purl.uniprot.org/uniprot/P82349 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Beta-sarcoglycan|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000175244 http://togogenome.org/gene/10090:Abca2 ^@ http://purl.uniprot.org/uniprot/A2AJ26 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ ABC transporter|||Disordered|||Helical|||Pro residues ^@ http://togogenome.org/gene/10090:Pars2 ^@ http://purl.uniprot.org/uniprot/A8Y5T6|||http://purl.uniprot.org/uniprot/Q8CFI5 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide ^@ Aminoacyl-transfer RNA synthetases class-II family profile|||Mitochondrion|||Probable proline--tRNA ligase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000035819 http://togogenome.org/gene/10090:Marcksl1 ^@ http://purl.uniprot.org/uniprot/P28667 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Complete loss of MAPK-mediated phosphorylation; when associated with A-120 and A-148. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-120 and A-148.|||Complete loss of MAPK-mediated phosphorylation; when associated with A-120 and A-183. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-120 and A-183.|||Complete loss of MAPK-mediated phosphorylation; when associated with A-148 and A-183. In neurons, induces the generation of large, flat lamellipodial protrusions; when associated with A-148 and A-183.|||Disordered|||Effector domain involved in lipid-binding and calmodulin-binding|||Induction of F-actin-bundling; when associated with D-120 and D-148. In neurons, induces the generation of long and prominent filopodia; when associated with D-120 and D-148.|||Induction of F-actin-bundling; when associated with D-120 and D-183. In neurons, induces the generation of long and prominent filopodia; when associated with D-120 and D-183.|||Induction of F-actin-bundling; when associated with D-148 and D-183. In neurons, induces the generation of long and prominent filopodia; when associated with D-148 and D-183.|||MARCKS-related protein|||N-myristoyl glycine|||Phosphoserine|||Phosphoserine; by MAPK8|||Phosphoserine; by PKC|||Phosphothreonine|||Phosphothreonine; by MAPK8|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000157153 http://togogenome.org/gene/10090:Olfr1141 ^@ http://purl.uniprot.org/uniprot/Q8VFQ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Srprb ^@ http://purl.uniprot.org/uniprot/P47758 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transmembrane|||Turn ^@ Helical|||Phosphoserine|||Phosphothreonine|||Signal recognition particle receptor subunit beta ^@ http://purl.uniprot.org/annotation/PRO_0000101228 http://togogenome.org/gene/10090:Dguok ^@ http://purl.uniprot.org/uniprot/Q504N4|||http://purl.uniprot.org/uniprot/Q9QX60 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Deoxyguanosine kinase, mitochondrial|||Deoxynucleoside kinase|||In isoform 2.|||Mitochondrion|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000016841|||http://purl.uniprot.org/annotation/VSP_003027 http://togogenome.org/gene/10090:Zfp651 ^@ http://purl.uniprot.org/uniprot/E9PZ11 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||BTB|||Basic and acidic residues|||C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Arhgef40 ^@ http://purl.uniprot.org/uniprot/Q3UPH7 ^@ 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|||Basic residues|||DH|||Disordered|||In isoform 2, isoform 3 and isoform 6.|||In isoform 2.|||In isoform 6.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho guanine nucleotide exchange factor 40 ^@ http://purl.uniprot.org/annotation/PRO_0000314823|||http://purl.uniprot.org/annotation/VSP_030387|||http://purl.uniprot.org/annotation/VSP_030388|||http://purl.uniprot.org/annotation/VSP_030389 http://togogenome.org/gene/10090:Nudt15 ^@ http://purl.uniprot.org/uniprot/Q8BG93 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Region ^@ Interaction with PCNA|||Nucleotide triphosphate diphosphatase NUDT15|||Nudix box|||Nudix hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000057116 http://togogenome.org/gene/10090:Xrcc1 ^@ http://purl.uniprot.org/uniprot/Q3TGI0|||http://purl.uniprot.org/uniprot/Q60596 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Phosphoserine|||Phosphothreonine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000066045 http://togogenome.org/gene/10090:Fmo3 ^@ http://purl.uniprot.org/uniprot/P97501|||http://purl.uniprot.org/uniprot/Q3UEN4 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Transmembrane ^@ Flavin-containing monooxygenase 3|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000147656 http://togogenome.org/gene/10090:Spg21 ^@ http://purl.uniprot.org/uniprot/A2RT57|||http://purl.uniprot.org/uniprot/Q9CQC8 ^@ 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 ^@ AB hydrolase-1|||In isoform 2.|||Maspardin|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000227982|||http://purl.uniprot.org/annotation/VSP_017634 http://togogenome.org/gene/10090:Slc18a2 ^@ http://purl.uniprot.org/uniprot/Q8BRU6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal, vesicle|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by CK2|||Synaptic vesicular amine transporter ^@ http://purl.uniprot.org/annotation/PRO_0000127515 http://togogenome.org/gene/10090:Akr1b3 ^@ http://purl.uniprot.org/uniprot/P45376|||http://purl.uniprot.org/uniprot/Q3UDY1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site ^@ Aldo-keto reductase family 1 member B1|||Lowers pKa of active site Tyr|||N-acetylalanine|||N6-acetyllysine|||NADP-dependent oxidoreductase|||Phosphoserine|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000124624 http://togogenome.org/gene/10090:Got2 ^@ http://purl.uniprot.org/uniprot/P05202 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ 3'-nitrotyrosine; alternate|||Aspartate aminotransferase, mitochondrial|||Asymmetric dimethylarginine|||Heterozygous mice are viable and healthy. Results in early lethality at homozygosity.|||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_0000001216 http://togogenome.org/gene/10090:Htr4 ^@ http://purl.uniprot.org/uniprot/A0A494BA82|||http://purl.uniprot.org/uniprot/P97288 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 isoform 5-HT4(A).|||In isoform 5-HT4(E).|||In isoform 5-HT4(F).|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000068966|||http://purl.uniprot.org/annotation/VSP_001851|||http://purl.uniprot.org/annotation/VSP_001852|||http://purl.uniprot.org/annotation/VSP_001853 http://togogenome.org/gene/10090:Mcl1 ^@ http://purl.uniprot.org/uniprot/P97287 ^@ Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Chain|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ BH1|||BH2|||BH3|||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 homolog|||PEST-like|||Phosphoserine|||Phosphoserine; by GSK3-alpha and GSK3-beta|||Phosphothreonine; by MAPK ^@ http://purl.uniprot.org/annotation/PRO_0000143081|||http://purl.uniprot.org/annotation/VSP_046443 http://togogenome.org/gene/10090:Tns1 ^@ http://purl.uniprot.org/uniprot/A0A087WQS0|||http://purl.uniprot.org/uniprot/E9Q0S6|||http://purl.uniprot.org/uniprot/Q7TSV1|||http://purl.uniprot.org/uniprot/Q8C6V6|||http://purl.uniprot.org/uniprot/Q9DBT6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||C2 tensin-type|||Disordered|||O-linked (GalNAc...) serine|||PTB|||Phorbol-ester/DAG-type|||Phosphatase tensin-type|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH2|||Tensin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000457045 http://togogenome.org/gene/10090:Casq2 ^@ http://purl.uniprot.org/uniprot/O09161 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||Calsequestrin-2|||Disordered|||Impairs calcium-dependent oligomerization and promotes ventricular tachycardia.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000004219 http://togogenome.org/gene/10090:Pth ^@ http://purl.uniprot.org/uniprot/Q9Z0L6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Parathyroid hormone ^@ http://purl.uniprot.org/annotation/PRO_5015024084 http://togogenome.org/gene/10090:Nim1k ^@ http://purl.uniprot.org/uniprot/Q8BHI9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase NIM1 ^@ http://purl.uniprot.org/annotation/PRO_0000247667 http://togogenome.org/gene/10090:Rgmb ^@ http://purl.uniprot.org/uniprot/Q7TQ33 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage; by autolysis|||GPI-anchor amidated cysteine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Repulsive guidance molecule B ^@ http://purl.uniprot.org/annotation/PRO_0000030396|||http://purl.uniprot.org/annotation/PRO_0000030397 http://togogenome.org/gene/10090:Rnaseh2a ^@ http://purl.uniprot.org/uniprot/Q9CWY8 ^@ 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 ^@ Disordered|||Loss of enzyme activity.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||RNase H type-2|||Ribonuclease H2 subunit A|||Strongly reduced in vitro enzyme activity. ^@ http://purl.uniprot.org/annotation/PRO_0000111711 http://togogenome.org/gene/10090:Atg12 ^@ http://purl.uniprot.org/uniprot/Q9CQY1 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor protein)|||Ubiquitin-like protein ATG12 ^@ http://purl.uniprot.org/annotation/PRO_0000212472 http://togogenome.org/gene/10090:Ggcx ^@ http://purl.uniprot.org/uniprot/B2RS80|||http://purl.uniprot.org/uniprot/Q9QYC7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||HTTM|||Helical|||Lumenal|||N-acetylalanine|||Removed|||Vitamin K-dependent gamma-carboxylase ^@ http://purl.uniprot.org/annotation/PRO_0000191824 http://togogenome.org/gene/10090:Tex9 ^@ http://purl.uniprot.org/uniprot/Q9D845 ^@ 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.|||Polar residues|||Testis-expressed protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000244482|||http://purl.uniprot.org/annotation/VSP_019570|||http://purl.uniprot.org/annotation/VSP_019571|||http://purl.uniprot.org/annotation/VSP_019572 http://togogenome.org/gene/10090:Vcan ^@ http://purl.uniprot.org/uniprot/E9PYH0|||http://purl.uniprot.org/uniprot/E9QMK2|||http://purl.uniprot.org/uniprot/E9QMK3|||http://purl.uniprot.org/uniprot/G3XA35|||http://purl.uniprot.org/uniprot/Q8BS97 ^@ 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 ^@ Basic and acidic residues|||C-type lectin|||Disordered|||EGF-like|||Ig-like|||Link|||Polar residues|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_5003244320|||http://purl.uniprot.org/annotation/PRO_5003246273|||http://purl.uniprot.org/annotation/PRO_5003246417|||http://purl.uniprot.org/annotation/PRO_5015091860|||http://purl.uniprot.org/annotation/PRO_5015099068 http://togogenome.org/gene/10090:Cldn14 ^@ http://purl.uniprot.org/uniprot/A2RSP0|||http://purl.uniprot.org/uniprot/Q9Z0S3 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Claudin-14|||Cytoplasmic|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000144770 http://togogenome.org/gene/10090:Alox12b ^@ http://purl.uniprot.org/uniprot/O70582|||http://purl.uniprot.org/uniprot/Q2KHL0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Site ^@ Arachidonate 12-lipoxygenase, 12R-type|||Essential for stabilizing binding to COTL1|||In strain: C57BL/6 XSJL.|||Increased enzymatic activity and changed stereoselectivity of the oxygenation reaction to produce (11R)-HPETE preferentially instead of (12R)-HPETE.|||Lipoxygenase|||Loss of enzymatic activity.|||PLAT|||Reduced enzymatic activity and altered stereoselectivity of the oxygenation reaction.|||Reduced enzymatic activity and changed stereoselectivity of the oxygenation reaction. ^@ http://purl.uniprot.org/annotation/PRO_0000220690 http://togogenome.org/gene/10090:Sertad1 ^@ http://purl.uniprot.org/uniprot/Q9JL10 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||SERTA|||SERTA domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000191612 http://togogenome.org/gene/10090:Snrpg ^@ http://purl.uniprot.org/uniprot/P62309 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Sm|||Small nuclear ribonucleoprotein G ^@ http://purl.uniprot.org/annotation/PRO_0000125546 http://togogenome.org/gene/10090:Ear14 ^@ http://purl.uniprot.org/uniprot/Q5GAN2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_5015020043 http://togogenome.org/gene/10090:Usp18 ^@ http://purl.uniprot.org/uniprot/Q3UAR6|||http://purl.uniprot.org/uniprot/Q9WTV6 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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_0000080645 http://togogenome.org/gene/10090:Map3k7cl ^@ http://purl.uniprot.org/uniprot/P58500|||http://purl.uniprot.org/uniprot/Q544C0 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ MAP3K7 C-terminal-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000072424 http://togogenome.org/gene/10090:Tmem88b ^@ http://purl.uniprot.org/uniprot/Q3TYP4 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 88B ^@ http://purl.uniprot.org/annotation/PRO_0000346447 http://togogenome.org/gene/10090:Defa34 ^@ http://purl.uniprot.org/uniprot/D3Z0J0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Mammalian defensins ^@ http://purl.uniprot.org/annotation/PRO_5003053161 http://togogenome.org/gene/10090:Zfp428 ^@ http://purl.uniprot.org/uniprot/H3BLD9|||http://purl.uniprot.org/uniprot/Q8C1M2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||C2H2-type|||Disordered|||Phosphothreonine|||Zinc finger protein 428 ^@ http://purl.uniprot.org/annotation/PRO_0000312347 http://togogenome.org/gene/10090:Dsg1b ^@ http://purl.uniprot.org/uniprot/B2RQH0|||http://purl.uniprot.org/uniprot/Q7TSF1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin|||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-beta|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000003841|||http://purl.uniprot.org/annotation/PRO_0000003842|||http://purl.uniprot.org/annotation/PRO_5014298301 http://togogenome.org/gene/10090:Strn ^@ http://purl.uniprot.org/uniprot/O55106 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Calmodulin-binding|||Caveolin-binding|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Striatin|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000051233 http://togogenome.org/gene/10090:Aptx ^@ http://purl.uniprot.org/uniprot/Q7TQC5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Aprataxin|||Basic and acidic residues|||C2H2-type|||Disordered|||FHA-like|||HIT|||Histidine triad motif|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Interaction with DNA substrate|||Interactions with ADPRT/PARP1 and NCL|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Tele-AMP-histidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000109840|||http://purl.uniprot.org/annotation/VSP_010542|||http://purl.uniprot.org/annotation/VSP_010543|||http://purl.uniprot.org/annotation/VSP_010544 http://togogenome.org/gene/10090:Hand1 ^@ http://purl.uniprot.org/uniprot/Q5SQG1|||http://purl.uniprot.org/uniprot/Q64279 ^@ 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 ^@ Adopts a nucleus-wide distribution; when associated with D-107.|||Adopts a nucleus-wide distribution; when associated with D-109.|||BHLH|||Basic and acidic residues|||Disordered|||Heart- and neural crest derivatives-expressed protein 1|||Phosphoserine; by PLK4|||Phosphothreonine; by PLK4|||Remains exclusively in the nucleolus; when associated with A-107.|||Remains exclusively in the nucleolus; when associated with A-109.|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127185 http://togogenome.org/gene/10090:Lce1a1 ^@ http://purl.uniprot.org/uniprot/Q9CQH5 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Acad8 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0P1|||http://purl.uniprot.org/uniprot/Q9D7B6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA dehydrogenase/oxidase N-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||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_0000000523 http://togogenome.org/gene/10090:Ippk ^@ http://purl.uniprot.org/uniprot/Q6P1C1 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Motif|||Sequence Conflict|||Strand|||Turn ^@ EXKPK motif|||Inositol-pentakisphosphate 2-kinase ^@ http://purl.uniprot.org/annotation/PRO_0000110530 http://togogenome.org/gene/10090:Ttc39b ^@ http://purl.uniprot.org/uniprot/Q8BYY4 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Repeat|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 39B ^@ http://purl.uniprot.org/annotation/PRO_0000292002|||http://purl.uniprot.org/annotation/VSP_026359|||http://purl.uniprot.org/annotation/VSP_026360|||http://purl.uniprot.org/annotation/VSP_026361|||http://purl.uniprot.org/annotation/VSP_026362 http://togogenome.org/gene/10090:Erich1 ^@ http://purl.uniprot.org/uniprot/E9PY43|||http://purl.uniprot.org/uniprot/Q3UGP3 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or1x2 ^@ http://purl.uniprot.org/uniprot/Q8VFE6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cabp5 ^@ http://purl.uniprot.org/uniprot/Q543X4|||http://purl.uniprot.org/uniprot/Q9JLK3 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Calcium-binding protein 5|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4 ^@ http://purl.uniprot.org/annotation/PRO_0000073525 http://togogenome.org/gene/10090:Zbtb8b ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Q8|||http://purl.uniprot.org/uniprot/I7HLR7|||http://purl.uniprot.org/uniprot/Q8CII0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger ^@ BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||Disordered|||Zinc finger and BTB domain-containing protein 8B ^@ http://purl.uniprot.org/annotation/PRO_0000047722 http://togogenome.org/gene/10090:Hars2 ^@ http://purl.uniprot.org/uniprot/G5E823|||http://purl.uniprot.org/uniprot/Q99KK9 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Signal Peptide|||Transit Peptide ^@ Anticodon-binding|||Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core|||Histidine--tRNA ligase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||histidine--tRNA ligase ^@ http://purl.uniprot.org/annotation/PRO_0000254584|||http://purl.uniprot.org/annotation/PRO_5015091893 http://togogenome.org/gene/10090:Slc25a35 ^@ http://purl.uniprot.org/uniprot/Q5SWT3 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Repeat|||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 35 ^@ http://purl.uniprot.org/annotation/PRO_0000291795 http://togogenome.org/gene/10090:Pkn2 ^@ http://purl.uniprot.org/uniprot/Q8BWW9 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ AGC-kinase C-terminal|||C2|||Cleavage; by caspase-3|||Disordered|||In isoform 2.|||In isoform 3.|||Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-155.|||Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-60.|||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 apical junction formation.|||Protein kinase|||Proton acceptor|||REM-1 1|||REM-1 2|||REM-1 3|||Serine/threonine-protein kinase N2 ^@ http://purl.uniprot.org/annotation/PRO_0000055723|||http://purl.uniprot.org/annotation/VSP_012042|||http://purl.uniprot.org/annotation/VSP_042185|||http://purl.uniprot.org/annotation/VSP_042186 http://togogenome.org/gene/10090:Timm22 ^@ http://purl.uniprot.org/uniprot/B0QZS8|||http://purl.uniprot.org/uniprot/Q9CQ85 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Helical|||Mitochondrial import inner membrane translocase subunit TIM22|||Mitochondrial import inner membrane translocase subunit Tim22 ^@ http://purl.uniprot.org/annotation/PRO_0000210299|||http://purl.uniprot.org/annotation/PRO_5002754267 http://togogenome.org/gene/10090:Lpcat1 ^@ http://purl.uniprot.org/uniprot/Q3TFD2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes activity.|||Cytoplasmic|||Di-lysine motif|||Disordered|||EF-hand 1|||EF-hand 2|||Greatly reduced activity.|||HXXXXD motif|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Loss of activity.|||Loss of lyso-PAFAT activity. LPCAT activity is partially reduced.|||Lumenal|||Lysophosphatidylcholine acyltransferase 1|||No activity for acetyl-CoA. Activity for palmitoyl-CoA decreased.|||No effect on activity for acetyl-CoA. Reduced activity for palmitoyl-CoA.|||Reduced activity.|||Slightly increased activity.|||Slightly reduced activity. ^@ http://purl.uniprot.org/annotation/PRO_0000247065|||http://purl.uniprot.org/annotation/VSP_019913|||http://purl.uniprot.org/annotation/VSP_019914 http://togogenome.org/gene/10090:Rpl10l ^@ http://purl.uniprot.org/uniprot/P86048 ^@ Chain|||Molecule Processing ^@ Chain ^@ Large ribosomal subunit protein uL16-like ^@ http://purl.uniprot.org/annotation/PRO_0000354975 http://togogenome.org/gene/10090:Or8g35 ^@ http://purl.uniprot.org/uniprot/Q9EQ97 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dock10 ^@ http://purl.uniprot.org/uniprot/Q8BZN6 ^@ 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 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 10|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000190003|||http://purl.uniprot.org/annotation/VSP_007718|||http://purl.uniprot.org/annotation/VSP_058821|||http://purl.uniprot.org/annotation/VSP_061616|||http://purl.uniprot.org/annotation/VSP_061617|||http://purl.uniprot.org/annotation/VSP_061618 http://togogenome.org/gene/10090:Zfp990 ^@ http://purl.uniprot.org/uniprot/B1AVN5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Gm14137 ^@ http://purl.uniprot.org/uniprot/Q8CE97 ^@ Chain|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Region|||Transit Peptide ^@ Disordered|||Mitochondrion|||Uncharacterized protein C15orf62 homolog, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000332137 http://togogenome.org/gene/10090:Mrfap1 ^@ http://purl.uniprot.org/uniprot/Q9CQL7 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Disordered|||MORF4 family-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000306177 http://togogenome.org/gene/10090:Nfya ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Y8|||http://purl.uniprot.org/uniprot/P23708|||http://purl.uniprot.org/uniprot/Q3UP82|||http://purl.uniprot.org/uniprot/Q9DBV7 ^@ 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 ^@ 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_0000198769|||http://purl.uniprot.org/annotation/VSP_000850 http://togogenome.org/gene/10090:Cox7a2l ^@ http://purl.uniprot.org/uniprot/E9PZS8|||http://purl.uniprot.org/uniprot/Q3UDK5|||http://purl.uniprot.org/uniprot/Q61387 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide|||Transmembrane ^@ Chain|||Modified Residue|||Transit Peptide|||Transmembrane ^@ Cytochrome c oxidase subunit 7A-related protein, mitochondrial|||Helical|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000006155 http://togogenome.org/gene/10090:Ccl25 ^@ http://purl.uniprot.org/uniprot/D3YWJ1|||http://purl.uniprot.org/uniprot/O35903|||http://purl.uniprot.org/uniprot/Q3V2F3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||C-C motif chemokine 25|||Chemokine interleukin-8-like|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000005236|||http://purl.uniprot.org/annotation/PRO_5015097527 http://togogenome.org/gene/10090:Ten1 ^@ http://purl.uniprot.org/uniprot/Q9D7K2 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ CST complex subunit TEN1|||Disordered|||OB|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000392993 http://togogenome.org/gene/10090:Grik4 ^@ http://purl.uniprot.org/uniprot/Q8BMF5 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Glutamate receptor ionotropic, kainate 4|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000042577 http://togogenome.org/gene/10090:Gabarap ^@ http://purl.uniprot.org/uniprot/Q9DCD6 ^@ Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Chain|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Site|||Strand ^@ Cleavage; by ATG4B|||Gamma-aminobutyric acid receptor-associated protein|||Interaction with GABRG2|||Interaction with GPHN|||Interaction with beta-tubulin|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000212364|||http://purl.uniprot.org/annotation/PRO_0000423066 http://togogenome.org/gene/10090:Acaa2 ^@ http://purl.uniprot.org/uniprot/Q8BWT1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ 3-ketoacyl-CoA thiolase, mitochondrial|||Acyl-thioester intermediate|||Increases nucleophilicity of active site Cys|||Mitochondrion; not cleaved|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000223300 http://togogenome.org/gene/10090:Sgk2 ^@ http://purl.uniprot.org/uniprot/Q3UW73|||http://purl.uniprot.org/uniprot/Q9QZS5 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ AGC-kinase C-terminal|||Disordered|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine; by PDPK1|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Sgk2 ^@ http://purl.uniprot.org/annotation/PRO_0000086647|||http://purl.uniprot.org/annotation/VSP_004933 http://togogenome.org/gene/10090:Gpr31b ^@ http://purl.uniprot.org/uniprot/F8VQN3 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||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_0000415340 http://togogenome.org/gene/10090:P2ry12 ^@ http://purl.uniprot.org/uniprot/Q546L4|||http://purl.uniprot.org/uniprot/Q9CPV9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||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|||N-linked (GlcNAc...) asparagine|||P2Y purinoceptor 12|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000070038 http://togogenome.org/gene/10090:Il20ra ^@ http://purl.uniprot.org/uniprot/Q6PHB0 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Interleukin-20 receptor subunit alpha|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000011037 http://togogenome.org/gene/10090:Plekhh1 ^@ http://purl.uniprot.org/uniprot/Q80TI1 ^@ 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|||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_0000310949|||http://purl.uniprot.org/annotation/VSP_029350|||http://purl.uniprot.org/annotation/VSP_029351 http://togogenome.org/gene/10090:Triobp ^@ http://purl.uniprot.org/uniprot/A0A2U3TZ82|||http://purl.uniprot.org/uniprot/Q99KW3 ^@ 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.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PLK1|||Polar residues|||TRIO and F-actin-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000072434|||http://purl.uniprot.org/annotation/VSP_016762|||http://purl.uniprot.org/annotation/VSP_017718|||http://purl.uniprot.org/annotation/VSP_017719|||http://purl.uniprot.org/annotation/VSP_017720|||http://purl.uniprot.org/annotation/VSP_017721 http://togogenome.org/gene/10090:Metrn ^@ http://purl.uniprot.org/uniprot/A2RSN4|||http://purl.uniprot.org/uniprot/Q8C1Q4 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Meteorin ^@ http://purl.uniprot.org/annotation/PRO_0000021681|||http://purl.uniprot.org/annotation/PRO_5014296813|||http://purl.uniprot.org/annotation/VSP_010844|||http://purl.uniprot.org/annotation/VSP_010845 http://togogenome.org/gene/10090:Ccl27a ^@ http://purl.uniprot.org/uniprot/A0A0R4J0X6|||http://purl.uniprot.org/uniprot/A2AMS6|||http://purl.uniprot.org/uniprot/A2AMS7|||http://purl.uniprot.org/uniprot/Q9Z1X0 ^@ 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 ^@ C-C motif chemokine 27|||Chemokine interleukin-8-like|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000005240|||http://purl.uniprot.org/annotation/PRO_5006451976|||http://purl.uniprot.org/annotation/VSP_001065 http://togogenome.org/gene/10090:Dnmbp ^@ http://purl.uniprot.org/uniprot/A0A0R4J055|||http://purl.uniprot.org/uniprot/A0A1D5RLL6|||http://purl.uniprot.org/uniprot/Q6TXD4|||http://purl.uniprot.org/uniprot/Q9CWU8 ^@ 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 ^@ BAR|||Basic and acidic residues|||DH|||Disordered|||Dynamin-binding protein|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||SH3 5|||SH3 6 ^@ http://purl.uniprot.org/annotation/PRO_0000079960|||http://purl.uniprot.org/annotation/VSP_012081|||http://purl.uniprot.org/annotation/VSP_012082|||http://purl.uniprot.org/annotation/VSP_012083 http://togogenome.org/gene/10090:Gja4 ^@ http://purl.uniprot.org/uniprot/P28235|||http://purl.uniprot.org/uniprot/Q3UPZ2 ^@ 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 alpha-4 protein|||Gap junction protein cysteine-rich|||Helical|||Requires 2 nucleotide substitutions. ^@ http://purl.uniprot.org/annotation/PRO_0000057815 http://togogenome.org/gene/10090:Krt19 ^@ http://purl.uniprot.org/uniprot/B1AQ78|||http://purl.uniprot.org/uniprot/P19001 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Site ^@ 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|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Rod-like helical tail|||Stutter ^@ http://purl.uniprot.org/annotation/PRO_0000063672 http://togogenome.org/gene/10090:Cdo1 ^@ http://purl.uniprot.org/uniprot/P60334 ^@ Binding Site|||Chain|||Crosslink|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Crosslink|||Helix|||Strand|||Turn ^@ 3'-(S-cysteinyl)-tyrosine (Cys-Tyr)|||Cysteine dioxygenase type 1 ^@ http://purl.uniprot.org/annotation/PRO_0000206607 http://togogenome.org/gene/10090:Atg4c ^@ http://purl.uniprot.org/uniprot/Q3UYA5|||http://purl.uniprot.org/uniprot/Q811C2 ^@ 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 ^@ Cysteine protease ATG4C|||N-acetylmethionine|||Nucleophile|||Peptidase C54 catalytic|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000215850 http://togogenome.org/gene/10090:Moxd1 ^@ http://purl.uniprot.org/uniprot/Q9CXI3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ DBH-like monooxygenase protein 1|||DOMON|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000305218 http://togogenome.org/gene/10090:Marchf1 ^@ http://purl.uniprot.org/uniprot/Q6NZQ8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Almost complete loss of down-regulation of CD86 cell surface expression; when associated with S-225.|||Disordered|||E3 ubiquitin-protein ligase MARCHF1|||Helical|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 5.|||Loss of ubiquitin ligase activity and loss of down-regulation of CD86 cell surface expression.|||Partial loss of down-regulation of CD86 cell surface expression. Almost complete loss of down-regulation of CD86 cell surface expression; when associated with F-232.|||Polar residues|||RING-CH-type|||Responsible for down-regulation of CD86 and MHC class II cell surface expression|||Responsible for low stability ^@ http://purl.uniprot.org/annotation/PRO_0000274366|||http://purl.uniprot.org/annotation/VSP_022726|||http://purl.uniprot.org/annotation/VSP_022727|||http://purl.uniprot.org/annotation/VSP_022728 http://togogenome.org/gene/10090:Gm14322 ^@ http://purl.uniprot.org/uniprot/A2AW66 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Vmn2r58 ^@ http://purl.uniprot.org/uniprot/K7N6V2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908934 http://togogenome.org/gene/10090:Fam89a ^@ http://purl.uniprot.org/uniprot/Q14BJ1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Polar residues|||Protein FAM89A ^@ http://purl.uniprot.org/annotation/PRO_0000358921|||http://purl.uniprot.org/annotation/VSP_036132 http://togogenome.org/gene/10090:Ppp2r2b ^@ http://purl.uniprot.org/uniprot/Q6ZWR4 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||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_0000071423|||http://purl.uniprot.org/annotation/VSP_037982|||http://purl.uniprot.org/annotation/VSP_037983 http://togogenome.org/gene/10090:Mei4 ^@ http://purl.uniprot.org/uniprot/Q8BRM6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Meiosis-specific protein MEI4 ^@ http://purl.uniprot.org/annotation/PRO_0000343704|||http://purl.uniprot.org/annotation/VSP_034675 http://togogenome.org/gene/10090:Or6c212 ^@ http://purl.uniprot.org/uniprot/Q8VFI4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Naf1 ^@ http://purl.uniprot.org/uniprot/E9QJT2|||http://purl.uniprot.org/uniprot/Q3UMQ8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H/ACA ribonucleoprotein complex non-core subunit NAF1|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000315638 http://togogenome.org/gene/10090:Acsm5 ^@ http://purl.uniprot.org/uniprot/Q8BGA8 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||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_0000306102|||http://purl.uniprot.org/annotation/VSP_028399|||http://purl.uniprot.org/annotation/VSP_028400 http://togogenome.org/gene/10090:Smim1 ^@ http://purl.uniprot.org/uniprot/P0C8K7|||http://purl.uniprot.org/uniprot/Q3V499 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-acetylmethionine|||Phosphoserine|||Pro residues|||Small integral membrane protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000356183 http://togogenome.org/gene/10090:Nfyb ^@ http://purl.uniprot.org/uniprot/P63139|||http://purl.uniprot.org/uniprot/Q8C590 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Region ^@ 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_0000204610 http://togogenome.org/gene/10090:Tmem63a ^@ http://purl.uniprot.org/uniprot/Q91YT8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Transmembrane ^@ CSC1-like protein 1|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000280726 http://togogenome.org/gene/10090:Calhm1 ^@ http://purl.uniprot.org/uniprot/A0A1Y1C8H8|||http://purl.uniprot.org/uniprot/D3Z291 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Affects basolateral membrane sorting in vitro but not in vivo; when associated with 76-A-A-77 and A-222.|||Affects basolateral membrane sorting in vitro but not in vivo; when associated with 76-A-A-77 and A-225.|||Affects basolateral membrane sorting in vitro but not in vivo; when associated with A-222 and A-225.|||Calcium homeostasis modulator protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000422239 http://togogenome.org/gene/10090:Hdgfl2 ^@ http://purl.uniprot.org/uniprot/Q3UMU9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ 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 2.|||In isoform 3.|||In isoform 4.|||Interaction with DPF3/BAF45C isoform 2|||Loss of interaction with SMARCA4.|||PWWP|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317644|||http://purl.uniprot.org/annotation/VSP_031117|||http://purl.uniprot.org/annotation/VSP_031118|||http://purl.uniprot.org/annotation/VSP_031119|||http://purl.uniprot.org/annotation/VSP_047648 http://togogenome.org/gene/10090:Egln1 ^@ http://purl.uniprot.org/uniprot/Q91YE3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Beta(2)beta(3) 'finger-like' loop|||Disordered|||Egl nine homolog 1|||Fe2OG dioxygenase|||MYND-type; atypical|||N-acetylalanine|||Phosphoserine|||Removed|||Required for nuclear export|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000206662 http://togogenome.org/gene/10090:Tbc1d25 ^@ http://purl.uniprot.org/uniprot/A1A5B6|||http://purl.uniprot.org/uniprot/A2VCT6|||http://purl.uniprot.org/uniprot/E9PWX7 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rab-GAP TBC|||TBC1 domain family member 25 ^@ http://purl.uniprot.org/annotation/PRO_0000288509 http://togogenome.org/gene/10090:Tas2r131 ^@ http://purl.uniprot.org/uniprot/Q7M708 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sox4 ^@ http://purl.uniprot.org/uniprot/Q06831 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand ^@ 9aaTAD|||Disordered|||HMG box|||N6-acetyllysine|||Polar residues|||Transcription factor SOX-4 ^@ http://purl.uniprot.org/annotation/PRO_0000048725 http://togogenome.org/gene/10090:Npff ^@ http://purl.uniprot.org/uniprot/Q9WVA8 ^@ Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Modified Residue|||Peptide|||Propeptide|||Signal Peptide ^@ Neuropeptide AF-like|||Neuropeptide FF|||Neuropeptide SF|||Phenylalanine amide ^@ http://purl.uniprot.org/annotation/PRO_0000009903|||http://purl.uniprot.org/annotation/PRO_0000009904|||http://purl.uniprot.org/annotation/PRO_0000009905|||http://purl.uniprot.org/annotation/PRO_0000009906|||http://purl.uniprot.org/annotation/PRO_0000009907 http://togogenome.org/gene/10090:Hpf1 ^@ http://purl.uniprot.org/uniprot/Q8CFE2 ^@ Active Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ ADP-ribosyltyrosine|||Histone PARylation factor 1|||Interaction with PARP1|||N-acetylmethionine|||N6-acetyllysine|||PolyADP-ribosyl aspartic acid|||PolyADP-ribosyl glutamic acid|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000294447 http://togogenome.org/gene/10090:Krt90 ^@ http://purl.uniprot.org/uniprot/E9Q1Z0|||http://purl.uniprot.org/uniprot/Q8BIS2 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disordered|||IF rod ^@ http://togogenome.org/gene/10090:Kctd21 ^@ http://purl.uniprot.org/uniprot/B2RTJ2|||http://purl.uniprot.org/uniprot/Q3URF8 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent ^@ BTB|||BTB/POZ domain-containing protein KCTD21 ^@ http://purl.uniprot.org/annotation/PRO_0000281152 http://togogenome.org/gene/10090:Fnbp1 ^@ http://purl.uniprot.org/uniprot/A2AQ41|||http://purl.uniprot.org/uniprot/A2AQ43|||http://purl.uniprot.org/uniprot/A2AQ44|||http://purl.uniprot.org/uniprot/Q80TY0 ^@ 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 ^@ Basic and acidic residues|||Disordered|||F-BAR|||Formin-binding protein 1|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||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|||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_0000261431|||http://purl.uniprot.org/annotation/VSP_021697|||http://purl.uniprot.org/annotation/VSP_021698|||http://purl.uniprot.org/annotation/VSP_021699|||http://purl.uniprot.org/annotation/VSP_021700|||http://purl.uniprot.org/annotation/VSP_021701|||http://purl.uniprot.org/annotation/VSP_021702|||http://purl.uniprot.org/annotation/VSP_021703 http://togogenome.org/gene/10090:Psd4 ^@ http://purl.uniprot.org/uniprot/Q8BLR5 ^@ 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|||PH|||PH and SEC7 domain-containing protein 4|||Phosphoserine|||Polar residues|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000251732 http://togogenome.org/gene/10090:Abcb1a ^@ http://purl.uniprot.org/uniprot/P21447 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-dependent translocase ABCB1|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000093336 http://togogenome.org/gene/10090:Slc25a19 ^@ http://purl.uniprot.org/uniprot/A2A9V5|||http://purl.uniprot.org/uniprot/Q80XJ6|||http://purl.uniprot.org/uniprot/Q9DAM5 ^@ Chain|||Molecule Processing|||Motif|||Region|||Repeat|||Transmembrane ^@ Chain|||Motif|||Repeat|||Transmembrane ^@ Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial thiamine pyrophosphate carrier|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3|||Substrate recognition ^@ http://purl.uniprot.org/annotation/PRO_0000090613 http://togogenome.org/gene/10090:9030624G23Rik ^@ http://purl.uniprot.org/uniprot/Q9D308 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Pcdha3 ^@ http://purl.uniprot.org/uniprot/Q91Y16 ^@ 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|||Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099533 http://togogenome.org/gene/10090:Pdzd2 ^@ http://purl.uniprot.org/uniprot/E9Q1M1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PDZ|||Polar residues ^@ http://togogenome.org/gene/10090:Mrpl48 ^@ http://purl.uniprot.org/uniprot/A0A140LHT6|||http://purl.uniprot.org/uniprot/E9QPQ8|||http://purl.uniprot.org/uniprot/Q8JZS9 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Large ribosomal subunit protein mL48|||Mitochondrion|||N6-succinyllysine|||Small ribosomal subunit protein uS10 ^@ http://purl.uniprot.org/annotation/PRO_0000261658 http://togogenome.org/gene/10090:Foxred1 ^@ http://purl.uniprot.org/uniprot/Q3TQB2 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ FAD-dependent oxidoreductase domain-containing protein 1|||Helical|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000274144|||http://purl.uniprot.org/annotation/VSP_022630 http://togogenome.org/gene/10090:Or1j12 ^@ http://purl.uniprot.org/uniprot/Q8VGL0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Por ^@ http://purl.uniprot.org/uniprot/P37040 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||FAD-binding FR-type|||Flavodoxin-like|||Helical|||Lumenal|||N-acetylglycine|||NADPH--cytochrome P450 reductase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000167597 http://togogenome.org/gene/10090:Serpinb3d ^@ http://purl.uniprot.org/uniprot/Q6UKZ0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Krtap3-2 ^@ http://purl.uniprot.org/uniprot/Q9D638 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||3 X 5 AA repeats of C-C-X(3)|||Keratin-associated protein 3-2|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000358595 http://togogenome.org/gene/10090:Saysd1 ^@ http://purl.uniprot.org/uniprot/Q8K190 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||SAYSvFN domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000089518 http://togogenome.org/gene/10090:Cst12 ^@ http://purl.uniprot.org/uniprot/E9Q1S9|||http://purl.uniprot.org/uniprot/Q9DAN8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Cystatin|||Cystatin-12|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000285791 http://togogenome.org/gene/10090:Micu2 ^@ http://purl.uniprot.org/uniprot/Q8CD10 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Abolishes interaction with MICU2.|||Calcium uptake protein 2, mitochondrial|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Interchain (with C-465 in MICU1)|||Mitochondrion|||Phosphoserine|||Strong reduction of mitochondrial Ca(2+) peaks. ^@ http://purl.uniprot.org/annotation/PRO_0000251218 http://togogenome.org/gene/10090:Trp63 ^@ http://purl.uniprot.org/uniprot/O88898|||http://purl.uniprot.org/uniprot/Q3UVI3|||http://purl.uniprot.org/uniprot/Q569E5|||http://purl.uniprot.org/uniprot/Q5CZX0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes interaction with WWP1.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Heterozygous mutant mice have reduced fertility, reduced ovary size and accelerated oocyte loss via apoptosis.|||In isoform 2, isoform 4 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 5 and isoform 6.|||Interaction with HIPK2|||Oligomerization|||Polar residues|||SAM|||Transactivation inhibition|||Transcription activation|||Tumor protein 63|||p53 DNA-binding|||p53 tetramerisation ^@ http://purl.uniprot.org/annotation/PRO_0000185730|||http://purl.uniprot.org/annotation/VSP_012471|||http://purl.uniprot.org/annotation/VSP_012472|||http://purl.uniprot.org/annotation/VSP_012473|||http://purl.uniprot.org/annotation/VSP_012474 http://togogenome.org/gene/10090:Cybc1 ^@ http://purl.uniprot.org/uniprot/Q3TYS2 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Cytochrome b-245 chaperone 1|||Disordered|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000281419 http://togogenome.org/gene/10090:Nuak2 ^@ http://purl.uniprot.org/uniprot/Q8BZN4 ^@ 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 ^@ Disordered|||In isoform 2.|||N-acetylmethionine|||NUAK family SNF1-like kinase 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000247757|||http://purl.uniprot.org/annotation/VSP_052095 http://togogenome.org/gene/10090:AI661453 ^@ http://purl.uniprot.org/uniprot/Q91Z58 ^@ 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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Uncharacterized protein C6orf132 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000320613|||http://purl.uniprot.org/annotation/VSP_034436|||http://purl.uniprot.org/annotation/VSP_034437 http://togogenome.org/gene/10090:Vat1 ^@ http://purl.uniprot.org/uniprot/Q499X4|||http://purl.uniprot.org/uniprot/Q62465 ^@ 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|||Enoyl reductase (ER)|||N-acetylserine|||Phosphoserine|||Pro residues|||Removed|||Synaptic vesicle membrane protein VAT-1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000160919 http://togogenome.org/gene/10090:Vmn2r10 ^@ http://purl.uniprot.org/uniprot/K7N621 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908801 http://togogenome.org/gene/10090:Oxnad1 ^@ http://purl.uniprot.org/uniprot/Q8VE38 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ FAD-binding FR-type|||In isoform 2.|||Oxidoreductase NAD-binding domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000299572|||http://purl.uniprot.org/annotation/VSP_027765 http://togogenome.org/gene/10090:Adam9 ^@ http://purl.uniprot.org/uniprot/A0A140LHU0|||http://purl.uniprot.org/uniprot/Q3U1W3|||http://purl.uniprot.org/uniprot/Q3UG15|||http://purl.uniprot.org/uniprot/Q61072 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Abolishes catalytic activity.|||Cleavage|||Cleavage; by furin-like protease|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 9|||Disordered|||Does not affect shedding activity; when associated with A-203.|||Does not affect shedding activity; when associated with A-205.|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Pro residues|||Reduces the shedding activity; when associated with A-56. Does not prevent pro-domain processing between the pro- and metalloprotease domain; when associated with A-56. ^@ http://purl.uniprot.org/annotation/PRO_0000029063|||http://purl.uniprot.org/annotation/PRO_5004229891|||http://purl.uniprot.org/annotation/PRO_5007303278|||http://purl.uniprot.org/annotation/PRO_5014309198 http://togogenome.org/gene/10090:Armt1 ^@ http://purl.uniprot.org/uniprot/A6H630 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Splice Variant ^@ Damage-control phosphatase ARMT1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed|||Subfamily III RTxK motif ^@ http://purl.uniprot.org/annotation/PRO_0000358925|||http://purl.uniprot.org/annotation/VSP_036133|||http://purl.uniprot.org/annotation/VSP_036134|||http://purl.uniprot.org/annotation/VSP_036135|||http://purl.uniprot.org/annotation/VSP_036136|||http://purl.uniprot.org/annotation/VSP_036137|||http://purl.uniprot.org/annotation/VSP_036138|||http://purl.uniprot.org/annotation/VSP_036139 http://togogenome.org/gene/10090:Col19a1 ^@ http://purl.uniprot.org/uniprot/Q0VF58 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Cell attachment site|||Collagen alpha-1(XIX) 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|||Collagen-like 9|||Disordered|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||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_0000284731 http://togogenome.org/gene/10090:Cdc42se2 ^@ http://purl.uniprot.org/uniprot/Q8BGH7 ^@ Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Sequence Conflict ^@ CDC42 small effector protein 2|||CRIB|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000334640 http://togogenome.org/gene/10090:Tnfsf14 ^@ http://purl.uniprot.org/uniprot/A0A0U5JAA8|||http://purl.uniprot.org/uniprot/Q9QYH9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Site|||Topological Domain|||Transmembrane ^@ Cleavage|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||TNF family profile|||Tumor necrosis factor ligand superfamily member 14, membrane form|||Tumor necrosis factor ligand superfamily member 14, soluble form ^@ http://purl.uniprot.org/annotation/PRO_0000034534|||http://purl.uniprot.org/annotation/PRO_0000034535 http://togogenome.org/gene/10090:Ccin ^@ http://purl.uniprot.org/uniprot/B2RX51|||http://purl.uniprot.org/uniprot/Q8CDE2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Modified Residue|||Repeat ^@ BACK|||BTB|||Calicin|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000284432 http://togogenome.org/gene/10090:Hspb7 ^@ http://purl.uniprot.org/uniprot/P35385 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Heat shock protein beta-7|||Polar residues|||Required for localization to SC35 splicing speckles|||sHSP ^@ http://purl.uniprot.org/annotation/PRO_0000125942 http://togogenome.org/gene/10090:Lmtk2 ^@ http://purl.uniprot.org/uniprot/Q3TYD6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase LMTK2 ^@ http://purl.uniprot.org/annotation/PRO_0000259459 http://togogenome.org/gene/10090:Cntnap4 ^@ http://purl.uniprot.org/uniprot/Q99P47 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Contactin-associated protein-like 4|||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_0000019511 http://togogenome.org/gene/10090:Or10a3n ^@ http://purl.uniprot.org/uniprot/Q7TRU3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hps6 ^@ http://purl.uniprot.org/uniprot/Q8BLY7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant ^@ BLOC-2 complex member HPS6|||Disordered|||In allele ru; HPS-like mutant.|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000084057 http://togogenome.org/gene/10090:Tcam1 ^@ http://purl.uniprot.org/uniprot/Q80X70|||http://purl.uniprot.org/uniprot/Q99NB3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5004295898|||http://purl.uniprot.org/annotation/PRO_5015099618 http://togogenome.org/gene/10090:Radx ^@ http://purl.uniprot.org/uniprot/Q8C779 ^@ 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|||In isoform 2.|||OB|||Polar residues|||RPA-related protein RADX ^@ http://purl.uniprot.org/annotation/PRO_0000254128|||http://purl.uniprot.org/annotation/VSP_021184 http://togogenome.org/gene/10090:Vmn2r57 ^@ http://purl.uniprot.org/uniprot/L7N269 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982392 http://togogenome.org/gene/10090:Ndufa1 ^@ http://purl.uniprot.org/uniprot/O35683|||http://purl.uniprot.org/uniprot/Q545K0 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane ^@ Chain|||Helix|||Strand|||Transmembrane ^@ Helical|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000118818 http://togogenome.org/gene/10090:Bmp7 ^@ http://purl.uniprot.org/uniprot/P23359 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Bone morphogenetic protein 7|||Disordered|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033878|||http://purl.uniprot.org/annotation/PRO_0000033879 http://togogenome.org/gene/10090:Pcdhb11 ^@ http://purl.uniprot.org/uniprot/Q8C5K2|||http://purl.uniprot.org/uniprot/Q91UZ8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Cadherin domain-containing protein|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5004304332|||http://purl.uniprot.org/annotation/PRO_5015099495 http://togogenome.org/gene/10090:Pvr ^@ http://purl.uniprot.org/uniprot/Q8K094 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015099251 http://togogenome.org/gene/10090:Tmie ^@ http://purl.uniprot.org/uniprot/B2RSF0|||http://purl.uniprot.org/uniprot/Q8K467 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Transmembrane inner ear expressed protein ^@ http://purl.uniprot.org/annotation/PRO_0000022556 http://togogenome.org/gene/10090:Kbtbd8 ^@ http://purl.uniprot.org/uniprot/Q3UQV5 ^@ 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 repeat and BTB domain-containing protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000278221|||http://purl.uniprot.org/annotation/VSP_023186 http://togogenome.org/gene/10090:Fgf5 ^@ http://purl.uniprot.org/uniprot/A0A7U3L698|||http://purl.uniprot.org/uniprot/P15656 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||Fibroblast growth factor|||Fibroblast growth factor 5|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000008959|||http://purl.uniprot.org/annotation/PRO_5031596561|||http://purl.uniprot.org/annotation/VSP_001520|||http://purl.uniprot.org/annotation/VSP_001521 http://togogenome.org/gene/10090:Rnaseh2c ^@ http://purl.uniprot.org/uniprot/Q9CQ18 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ N-acetylmethionine|||Ribonuclease H2 subunit C ^@ http://purl.uniprot.org/annotation/PRO_0000248386 http://togogenome.org/gene/10090:Ppil3 ^@ http://purl.uniprot.org/uniprot/Q9D6L8 ^@ 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.|||N-acetylserine|||Omega-N-methylarginine|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase-like 3|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000064167|||http://purl.uniprot.org/annotation/VSP_015469 http://togogenome.org/gene/10090:Rimkla ^@ http://purl.uniprot.org/uniprot/Q6PFX8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ ATP-grasp|||Disordered|||N-acetylaspartylglutamate synthase A|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000282569 http://togogenome.org/gene/10090:Or5t16 ^@ http://purl.uniprot.org/uniprot/Q7TR59 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cmtm5 ^@ http://purl.uniprot.org/uniprot/Q45TP8|||http://purl.uniprot.org/uniprot/Q9D6G9 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Splice Variant|||Transmembrane ^@ CKLF-like MARVEL transmembrane domain-containing protein 5|||Helical|||In isoform 2.|||MARVEL ^@ http://purl.uniprot.org/annotation/PRO_0000186106|||http://purl.uniprot.org/annotation/VSP_008266 http://togogenome.org/gene/10090:Rest ^@ http://purl.uniprot.org/uniprot/Q8VIG1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Abolished binding to neuron-restrictive silencer element.|||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|||C2H2-type 8|||C2H2-type 9|||Decreased binding to neuron-restrictive silencer element.|||Disordered|||In isoform 2.|||In isoform 3.|||Increased binding to neuron-restrictive silencer element.|||Interaction with RCOR1|||Interaction with SIN3A|||Interaction with SIN3B|||Interaction with ZFP90|||Phosphoserine|||Polar residues|||Pro residues|||RE1-silencing transcription factor|||Required for binding to the neuron-restrictive silencer element ^@ http://purl.uniprot.org/annotation/PRO_0000269548|||http://purl.uniprot.org/annotation/VSP_022069|||http://purl.uniprot.org/annotation/VSP_022070|||http://purl.uniprot.org/annotation/VSP_022071|||http://purl.uniprot.org/annotation/VSP_022072 http://togogenome.org/gene/10090:Galnt4 ^@ http://purl.uniprot.org/uniprot/O08832 ^@ 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|||Site|||Topological Domain|||Transmembrane ^@ Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Interaction with glycopeptide substrate|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 4|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059109 http://togogenome.org/gene/10090:Eif2b1 ^@ http://purl.uniprot.org/uniprot/Q99LC8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ N6-acetyllysine|||Translation initiation factor eIF-2B subunit alpha ^@ http://purl.uniprot.org/annotation/PRO_0000156056 http://togogenome.org/gene/10090:Cyp2j13 ^@ http://purl.uniprot.org/uniprot/B1AWM4|||http://purl.uniprot.org/uniprot/B1AWM5|||http://purl.uniprot.org/uniprot/Q3UNV4 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Als2 ^@ http://purl.uniprot.org/uniprot/Q920R0 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Alsin|||DH|||Disordered|||In isoform 2.|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN 8|||N6-acetyllysine|||PH|||Phosphoserine|||Phosphothreonine|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||VPS9 ^@ http://purl.uniprot.org/annotation/PRO_0000080904|||http://purl.uniprot.org/annotation/VSP_050525|||http://purl.uniprot.org/annotation/VSP_050526 http://togogenome.org/gene/10090:Wrnip1 ^@ http://purl.uniprot.org/uniprot/Q91XU0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||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.|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||UBZ4-type ^@ http://purl.uniprot.org/annotation/PRO_0000084786|||http://purl.uniprot.org/annotation/VSP_051784|||http://purl.uniprot.org/annotation/VSP_051785 http://togogenome.org/gene/10090:H1f5 ^@ http://purl.uniprot.org/uniprot/P43276 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.5|||N-acetylserine|||N6-(beta-hydroxybutyryl)lysine|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine|||N6-methyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000195918 http://togogenome.org/gene/10090:Neurl4 ^@ http://purl.uniprot.org/uniprot/H3BJZ3|||http://purl.uniprot.org/uniprot/H3BK72|||http://purl.uniprot.org/uniprot/Q5NCX5 ^@ 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.|||NHR|||NHR 1|||NHR 2|||NHR 3|||NHR 4|||NHR 5|||NHR 6|||Neuralized-like protein 4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000299106|||http://purl.uniprot.org/annotation/VSP_027564 http://togogenome.org/gene/10090:Cpt2 ^@ http://purl.uniprot.org/uniprot/P52825|||http://purl.uniprot.org/uniprot/Q3UN55 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transit Peptide ^@ Carnitine O-palmitoyltransferase 2, mitochondrial|||Choline/carnitine acyltransferase|||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_0000004426 http://togogenome.org/gene/10090:Slc7a3 ^@ http://purl.uniprot.org/uniprot/P70423 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cationic amino acid transporter 3|||Cytoplasmic|||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=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_0000054267 http://togogenome.org/gene/10090:Pcsk5 ^@ http://purl.uniprot.org/uniprot/Q04592|||http://purl.uniprot.org/uniprot/Q91VK0 ^@ 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 PC5A.|||N-linked (GlcNAc...) asparagine|||P/Homo B|||PLAC|||Peptidase S8|||Proprotein convertase subtilisin/kexin type 5 ^@ http://purl.uniprot.org/annotation/PRO_0000027104|||http://purl.uniprot.org/annotation/PRO_0000027105|||http://purl.uniprot.org/annotation/VSP_005438|||http://purl.uniprot.org/annotation/VSP_005439 http://togogenome.org/gene/10090:Ssxb9 ^@ http://purl.uniprot.org/uniprot/A2BI93 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB|||KRAB-related ^@ http://togogenome.org/gene/10090:4930550C14Rik ^@ http://purl.uniprot.org/uniprot/Q9D4W2 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Protein MFI ^@ http://purl.uniprot.org/annotation/PRO_0000263666 http://togogenome.org/gene/10090:Dusp8 ^@ http://purl.uniprot.org/uniprot/O09112|||http://purl.uniprot.org/uniprot/Q7TSZ9 ^@ 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|||Disordered|||Dual specificity protein phosphatase 8|||Phosphocysteine intermediate|||Polar residues|||Pro residues|||Rhodanese|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094811 http://togogenome.org/gene/10090:Slc6a14 ^@ http://purl.uniprot.org/uniprot/A1L359|||http://purl.uniprot.org/uniprot/Q9JMA9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||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_0000214796 http://togogenome.org/gene/10090:Zfp827 ^@ http://purl.uniprot.org/uniprot/G5E8U2|||http://purl.uniprot.org/uniprot/Q505G8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Motif|||Region|||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|||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 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_0000325891|||http://purl.uniprot.org/annotation/VSP_032466|||http://purl.uniprot.org/annotation/VSP_032467 http://togogenome.org/gene/10090:Ifngr1 ^@ http://purl.uniprot.org/uniprot/P15261 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Complete loss of STAT1 and STAT3 activation.|||Complete loss of interaction with SOCS1.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interferon gamma receptor 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000011010 http://togogenome.org/gene/10090:Taar7e ^@ http://purl.uniprot.org/uniprot/A6H6B4|||http://purl.uniprot.org/uniprot/Q5QD09 ^@ 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|||Trace amine-associated receptor 7e ^@ http://purl.uniprot.org/annotation/PRO_0000070169 http://togogenome.org/gene/10090:Asap1 ^@ http://purl.uniprot.org/uniprot/E9QMJ1|||http://purl.uniprot.org/uniprot/H3BKE6|||http://purl.uniprot.org/uniprot/H3BL41|||http://purl.uniprot.org/uniprot/Q3TXY1|||http://purl.uniprot.org/uniprot/Q3UJA5|||http://purl.uniprot.org/uniprot/Q9QWY8 ^@ 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|||Splice Variant|||Strand|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||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 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by FAK2|||Polar residues|||Pro residues|||SH3|||Significant reduction in binding to SRC and CRK and decrease in phosphorylation; when associated with A-910. Loss of binding and phosphorylation; when associated with A-811 and A-910.|||Significant reduction in binding to SRC and CRK and decrease in phosphorylation; when associated with A-913. Loss of binding and phosphorylation; when associated with A-811 and A-913.|||Significant reduction in binding to SRC and CRK and loss of phosphorylation. Loss of binding and phosphorylation; when associated with A-910 and A-913. ^@ http://purl.uniprot.org/annotation/PRO_0000074197|||http://purl.uniprot.org/annotation/VSP_008366|||http://purl.uniprot.org/annotation/VSP_008367|||http://purl.uniprot.org/annotation/VSP_008368 http://togogenome.org/gene/10090:Mesd ^@ http://purl.uniprot.org/uniprot/Q9ERE7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Basic and acidic residues|||Chaperone domain|||Disordered|||Escort domain|||LRP chaperone MESD|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000096444 http://togogenome.org/gene/10090:Ccnt2 ^@ http://purl.uniprot.org/uniprot/Q7TQK0 ^@ 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|||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_0000436037|||http://purl.uniprot.org/annotation/VSP_058225|||http://purl.uniprot.org/annotation/VSP_058226 http://togogenome.org/gene/10090:Tafa5 ^@ http://purl.uniprot.org/uniprot/Q91WE9 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ Chemokine-like protein TAFA-5|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000042733|||http://purl.uniprot.org/annotation/VSP_016069 http://togogenome.org/gene/10090:Klrb1b ^@ http://purl.uniprot.org/uniprot/A0A1U9W1A4|||http://purl.uniprot.org/uniprot/Q99JB4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||ITIM motif|||Killer cell lectin-like receptor subfamily B member 1B allele B|||LCK-binding motif ^@ http://purl.uniprot.org/annotation/PRO_0000271479 http://togogenome.org/gene/10090:Xrcc3 ^@ http://purl.uniprot.org/uniprot/Q80W51|||http://purl.uniprot.org/uniprot/Q9CXE6 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ DNA repair protein XRCC3|||N-acetylmethionine|||RecA family profile 1 ^@ http://purl.uniprot.org/annotation/PRO_0000122952 http://togogenome.org/gene/10090:Qpct ^@ http://purl.uniprot.org/uniprot/A0A0R4J0G6|||http://purl.uniprot.org/uniprot/A0A3B2W7G1|||http://purl.uniprot.org/uniprot/Q3UFN2|||http://purl.uniprot.org/uniprot/Q9CYK2 ^@ Active Site|||Binding Site|||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|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Glutaminyl-peptide cyclotransferase|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M28|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000022196|||http://purl.uniprot.org/annotation/VSP_013911 http://togogenome.org/gene/10090:Rpl30 ^@ http://purl.uniprot.org/uniprot/P62889|||http://purl.uniprot.org/uniprot/Q497D7|||http://purl.uniprot.org/uniprot/Q58DZ3|||http://purl.uniprot.org/uniprot/Q5PR15 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Large ribosomal subunit protein eL30|||N6-acetyllysine; alternate|||Phosphoserine|||Ribosomal protein eL8/eL30/eS12/Gadd45 ^@ http://purl.uniprot.org/annotation/PRO_0000146122 http://togogenome.org/gene/10090:Slc35c1 ^@ http://purl.uniprot.org/uniprot/Q78H73|||http://purl.uniprot.org/uniprot/Q8BLX4|||http://purl.uniprot.org/uniprot/Q8BZX8|||http://purl.uniprot.org/uniprot/Q8C0J3|||http://purl.uniprot.org/uniprot/Q8R2I1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Transmembrane ^@ GDP-fucose transporter 1|||Helical|||Sugar phosphate transporter ^@ http://purl.uniprot.org/annotation/PRO_0000343221 http://togogenome.org/gene/10090:Dera ^@ http://purl.uniprot.org/uniprot/Q91YP3 ^@ Active Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Chain ^@ Deoxyribose-phosphate aldolase|||Proton donor/acceptor|||Schiff-base intermediate with acetaldehyde ^@ http://purl.uniprot.org/annotation/PRO_0000057311 http://togogenome.org/gene/10090:Fkbp14 ^@ http://purl.uniprot.org/uniprot/P59024|||http://purl.uniprot.org/uniprot/Q542Q0 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Signal Peptide ^@ 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_0000025522|||http://purl.uniprot.org/annotation/PRO_5014309598 http://togogenome.org/gene/10090:Krt35 ^@ http://purl.uniprot.org/uniprot/Q497I4 ^@ 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 Ha5|||Linker 1|||Linker 12|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000361025 http://togogenome.org/gene/10090:Trank1 ^@ http://purl.uniprot.org/uniprot/Q8BV79 ^@ 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|||Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR and ankyrin repeat-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000348239|||http://purl.uniprot.org/annotation/VSP_035117 http://togogenome.org/gene/10090:Rpl36al ^@ http://purl.uniprot.org/uniprot/P83882|||http://purl.uniprot.org/uniprot/Q5M9P1 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Large ribosomal subunit protein eL42 ^@ http://purl.uniprot.org/annotation/PRO_0000149120 http://togogenome.org/gene/10090:Pclaf ^@ http://purl.uniprot.org/uniprot/Q9CQX4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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|||Initiation motif|||KEN box|||N6-acetyllysine; alternate|||PCNA-associated factor|||PIP-box|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096685 http://togogenome.org/gene/10090:Or10ab4 ^@ http://purl.uniprot.org/uniprot/Q7TRV1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ctbp2 ^@ http://purl.uniprot.org/uniprot/P56546|||http://purl.uniprot.org/uniprot/Q3UGL5|||http://purl.uniprot.org/uniprot/Q91YZ2 ^@ 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 ^@ Asymmetric dimethylarginine|||C-terminal-binding protein 2|||D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding|||D-isomer specific 2-hydroxyacid dehydrogenase catalytic|||Disordered|||In isoform 2.|||Phosphoserine; by HIPK2|||Polar residues|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000076045|||http://purl.uniprot.org/annotation/VSP_027616 http://togogenome.org/gene/10090:Pear1 ^@ http://purl.uniprot.org/uniprot/Q8VIK5|||http://purl.uniprot.org/uniprot/Q9CXP0 ^@ 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|||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|||EMI domain-containing protein|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Platelet endothelial aggregation receptor 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000309738|||http://purl.uniprot.org/annotation/PRO_5004325010|||http://purl.uniprot.org/annotation/VSP_029260|||http://purl.uniprot.org/annotation/VSP_029261|||http://purl.uniprot.org/annotation/VSP_029262|||http://purl.uniprot.org/annotation/VSP_029263 http://togogenome.org/gene/10090:Chmp1a ^@ http://purl.uniprot.org/uniprot/Q921W0 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Motif ^@ Charged multivesicular body protein 1a|||MIT-interacting motif|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000211449 http://togogenome.org/gene/10090:Tgm1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J293|||http://purl.uniprot.org/uniprot/Q9JLF6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Phosphothreonine|||Protein-glutamine gamma-glutamyltransferase K|||Transglutaminase-like ^@ http://purl.uniprot.org/annotation/PRO_0000213702 http://togogenome.org/gene/10090:Liph ^@ http://purl.uniprot.org/uniprot/Q8CIV3 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Charge relay system|||In isoform 2.|||In isoform 3.|||Lipase member H|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000273322|||http://purl.uniprot.org/annotation/VSP_022505|||http://purl.uniprot.org/annotation/VSP_022506 http://togogenome.org/gene/10090:Or1j21 ^@ http://purl.uniprot.org/uniprot/Q8VGK5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Olfactory receptor 1J21 ^@ http://purl.uniprot.org/annotation/PRO_0000422154 http://togogenome.org/gene/10090:Wfdc6b ^@ http://purl.uniprot.org/uniprot/F6ULY1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ BPTI/Kunitz inhibitor|||WAP|||WAP four-disulfide core domain protein 6B ^@ http://purl.uniprot.org/annotation/PRO_0000415852 http://togogenome.org/gene/10090:Ctxn2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J179|||http://purl.uniprot.org/uniprot/Q3URE8 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Cortexin-2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000284617 http://togogenome.org/gene/10090:Top2a ^@ http://purl.uniprot.org/uniprot/Q01320 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ 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|||Important for DNA bending; intercalates between base pairs of target DNA|||Interaction with DNA|||Interaction with PLSCR1|||N-acetylmethionine|||N6-acetyllysine; alternate|||O-(5'-phospho-DNA)-tyrosine intermediate|||Phosphoserine|||Phosphoserine; by CK1|||Phosphothreonine|||Polar residues|||Toprim|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000145364 http://togogenome.org/gene/10090:Cdk1 ^@ http://purl.uniprot.org/uniprot/P11440 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ 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|||N-acetylmethionine|||N6-acetyllysine; alternate|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CAK|||Phosphotyrosine|||Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCD|||Phosphotyrosine; by PKR|||Phosphotyrosine; by WEE1 and WEE2|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085725 http://togogenome.org/gene/10090:Spaca7 ^@ http://purl.uniprot.org/uniprot/Q9D2S4 ^@ 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|||Sperm acrosome-associated protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000350569 http://togogenome.org/gene/10090:Bcorl1 ^@ http://purl.uniprot.org/uniprot/A2AQH4 ^@ 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 ^@ ANK 1|||ANK 2|||ANK 3|||BCL-6 corepressor-like protein 1|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||PCGF Ub-like fold domain (PUFD); required for the interaction with the KDM2B-SKP1 heterodimeric complex|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000312269 http://togogenome.org/gene/10090:Aimp2 ^@ http://purl.uniprot.org/uniprot/Q8R010|||http://purl.uniprot.org/uniprot/Q8R3V2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ AIMP2 thioredoxin-like|||Aminoacyl tRNA synthase complex-interacting multifunctional protein 2|||GST C-terminal|||Glutathione S-transferase C-terminal|||Interaction with PRKN|||Interaction with TP53|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000316841 http://togogenome.org/gene/10090:Pigx ^@ http://purl.uniprot.org/uniprot/F6YX19|||http://purl.uniprot.org/uniprot/Q99LV7 ^@ 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|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphatidylinositol-glycan biosynthesis class X protein ^@ http://purl.uniprot.org/annotation/PRO_0000246296|||http://purl.uniprot.org/annotation/PRO_5030002998|||http://purl.uniprot.org/annotation/VSP_019843 http://togogenome.org/gene/10090:Atosb ^@ http://purl.uniprot.org/uniprot/Q8BR27 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Atos homolog protein B|||Disordered|||Phosphoserine|||Pro residues|||Required for macropage invasion|||Transactivation domain 1 (TAD1) ^@ http://purl.uniprot.org/annotation/PRO_0000313622 http://togogenome.org/gene/10090:Hhip ^@ http://purl.uniprot.org/uniprot/Q7TN16 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide ^@ EGF-like 1|||EGF-like 2|||Hedgehog-interacting protein|||Interaction with SHH zinc binding site|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000007624 http://togogenome.org/gene/10090:Prrc2c ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ79|||http://purl.uniprot.org/uniprot/Q3TLH4|||http://purl.uniprot.org/uniprot/S4R294|||http://purl.uniprot.org/uniprot/S4R2J9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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 5.|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein PRRC2C ^@ http://purl.uniprot.org/annotation/PRO_0000349240|||http://purl.uniprot.org/annotation/VSP_035255 http://togogenome.org/gene/10090:Or4c113 ^@ http://purl.uniprot.org/uniprot/L7MU54 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tuba4a ^@ http://purl.uniprot.org/uniprot/P68368 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict ^@ 3'-nitrotyrosine|||MREC motif|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Tubulin alpha-4A chain ^@ http://purl.uniprot.org/annotation/PRO_0000048123 http://togogenome.org/gene/10090:Taf1b ^@ http://purl.uniprot.org/uniprot/P97358 ^@ 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|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ B-linker|||B-reader|||C-terminal cyclin fold|||In isoform 2.|||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_0000304406|||http://purl.uniprot.org/annotation/VSP_028024|||http://purl.uniprot.org/annotation/VSP_028025 http://togogenome.org/gene/10090:Dzip3 ^@ http://purl.uniprot.org/uniprot/E9QNZ2|||http://purl.uniprot.org/uniprot/Q7TPV2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase DZIP3|||In isoform 2.|||In isoform 3.|||Polar residues|||RING-type|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000055899|||http://purl.uniprot.org/annotation/VSP_010973|||http://purl.uniprot.org/annotation/VSP_010974|||http://purl.uniprot.org/annotation/VSP_010975|||http://purl.uniprot.org/annotation/VSP_010976|||http://purl.uniprot.org/annotation/VSP_010977 http://togogenome.org/gene/10090:Lrrn2 ^@ http://purl.uniprot.org/uniprot/Q6PHP6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015098442 http://togogenome.org/gene/10090:Bag1 ^@ http://purl.uniprot.org/uniprot/Q60739|||http://purl.uniprot.org/uniprot/Q9CUY1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||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.|||Interaction with HSPA8|||Interaction with PPP1R15A|||Polar residues|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000002782|||http://purl.uniprot.org/annotation/VSP_018667 http://togogenome.org/gene/10090:Mroh1 ^@ http://purl.uniprot.org/uniprot/E0CZ22 ^@ Region|||Repeat ^@ Repeat ^@ HEAT ^@ http://togogenome.org/gene/10090:Gosr1 ^@ http://purl.uniprot.org/uniprot/O88630 ^@ Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Golgi SNAP receptor complex member 1|||Helical; Anchor for type IV membrane protein|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000212543 http://togogenome.org/gene/10090:Serpinb2 ^@ http://purl.uniprot.org/uniprot/P12388|||http://purl.uniprot.org/uniprot/Q542A3 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ N-linked (GlcNAc...) asparagine|||Not cleaved|||Plasminogen activator inhibitor 2, macrophage|||Reactive bond|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_0000223297 http://togogenome.org/gene/10090:Hoxb9 ^@ http://purl.uniprot.org/uniprot/P20615 ^@ Chain|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox|||Homeobox protein Hox-B9|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000200156 http://togogenome.org/gene/10090:Triml1 ^@ http://purl.uniprot.org/uniprot/Q8BVP1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Coiled-Coil|||Domain Extent|||Zinc Finger ^@ B30.2/SPRY|||Probable E3 ubiquitin-protein ligase TRIML1|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000274599 http://togogenome.org/gene/10090:Vmn1r73 ^@ http://purl.uniprot.org/uniprot/Q8R293 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wiz ^@ http://purl.uniprot.org/uniprot/G5E8J8|||http://purl.uniprot.org/uniprot/O88286 ^@ 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 ^@ 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|||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 EHMT1 and EHMT2.|||In isoform 2.|||In isoform 3.|||In isoform S.|||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_0000286055|||http://purl.uniprot.org/annotation/VSP_024953|||http://purl.uniprot.org/annotation/VSP_024954|||http://purl.uniprot.org/annotation/VSP_024955|||http://purl.uniprot.org/annotation/VSP_024956|||http://purl.uniprot.org/annotation/VSP_024957|||http://purl.uniprot.org/annotation/VSP_024958 http://togogenome.org/gene/10090:Nsmf ^@ http://purl.uniprot.org/uniprot/A2AJ92|||http://purl.uniprot.org/uniprot/A2AJ95|||http://purl.uniprot.org/uniprot/A2AJ96|||http://purl.uniprot.org/uniprot/Q3TNG2|||http://purl.uniprot.org/uniprot/Q3TY90|||http://purl.uniprot.org/uniprot/Q99NF2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||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|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000096779|||http://purl.uniprot.org/annotation/VSP_014764|||http://purl.uniprot.org/annotation/VSP_014765|||http://purl.uniprot.org/annotation/VSP_014766|||http://purl.uniprot.org/annotation/VSP_014767|||http://purl.uniprot.org/annotation/VSP_014768|||http://purl.uniprot.org/annotation/VSP_014769 http://togogenome.org/gene/10090:Ddb2 ^@ http://purl.uniprot.org/uniprot/Q99J79 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Modified Residue|||Motif|||Region|||Repeat ^@ DNA damage-binding protein 2|||DWD box|||Disordered|||N6-acetyllysine|||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_0000050954 http://togogenome.org/gene/10090:Sparc ^@ http://purl.uniprot.org/uniprot/P07214|||http://purl.uniprot.org/uniprot/Q5NCU4|||http://purl.uniprot.org/uniprot/Q5NCU5 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ EF-hand|||Follistatin-like|||Kazal-like|||N-linked (GlcNAc...) asparagine|||SPARC ^@ http://purl.uniprot.org/annotation/PRO_0000020305|||http://purl.uniprot.org/annotation/PRO_5004260298|||http://purl.uniprot.org/annotation/PRO_5014309913 http://togogenome.org/gene/10090:Gas2 ^@ http://purl.uniprot.org/uniprot/P11862|||http://purl.uniprot.org/uniprot/Q9D699 ^@ 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 proteolytic processing.|||Calponin-homology (CH)|||Cleavage; by a caspase during apoptosis|||Disordered|||GAR|||Growth arrest-specific protein 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000190441 http://togogenome.org/gene/10090:Chrna10 ^@ http://purl.uniprot.org/uniprot/B2RX82 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_5015087160 http://togogenome.org/gene/10090:Ttll5 ^@ http://purl.uniprot.org/uniprot/E9Q425|||http://purl.uniprot.org/uniprot/Q8CHB8 ^@ 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|||Site|||Splice Variant ^@ Acidic residues|||Disordered|||Essential for specifying initiation versus elongation step of the polyglutamylase activity|||In isoform 2.|||Polar residues|||TTL|||Tubulin polyglutamylase TTLL5|||c-MTBD region ^@ http://purl.uniprot.org/annotation/PRO_0000223342|||http://purl.uniprot.org/annotation/VSP_041931 http://togogenome.org/gene/10090:Actr1a ^@ http://purl.uniprot.org/uniprot/P61164 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Alpha-centractin|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000089059 http://togogenome.org/gene/10090:Hras ^@ http://purl.uniprot.org/uniprot/Q61411 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||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|||Crosslink|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Cysteine methyl ester|||Effector region|||Found in chemically induced liver tumors.|||GTPase HRas|||GTPase HRas, N-terminally processed|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hypervariable region|||In isoform 2.|||N-acetylmethionine|||N-acetylthreonine; in GTPase HRas, N-terminally processed|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000042998|||http://purl.uniprot.org/annotation/PRO_0000042999|||http://purl.uniprot.org/annotation/PRO_0000326478|||http://purl.uniprot.org/annotation/VSP_041598 http://togogenome.org/gene/10090:Dnajc27 ^@ http://purl.uniprot.org/uniprot/Q8CFP6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes GTP binding.|||Abolishes GTPase activity.|||DnaJ homolog subfamily C member 27|||Increases GTPase activity.|||J|||Required for interaction with MAPK1 ^@ http://purl.uniprot.org/annotation/PRO_0000332976 http://togogenome.org/gene/10090:Epb41l4b ^@ http://purl.uniprot.org/uniprot/A2ALK6|||http://purl.uniprot.org/uniprot/Q3TMR3|||http://purl.uniprot.org/uniprot/Q9JMC8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Abolishes in vitro phosphorylation.|||Band 4.1-like protein 4B|||Disordered|||FERM|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000219405 http://togogenome.org/gene/10090:Ppargc1b ^@ http://purl.uniprot.org/uniprot/Q8VHJ7 ^@ 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 ^@ Abolishes DNA transcriptional activity when missing|||Acidic residues|||Basic and acidic residues|||Disordered|||HCFC1-binding-motif (HBM)|||In isoform 2.|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||Peroxisome proliferator-activated receptor gamma coactivator 1-beta|||Phosphoserine|||Polar residues|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000240159|||http://purl.uniprot.org/annotation/VSP_019302 http://togogenome.org/gene/10090:Sash3 ^@ http://purl.uniprot.org/uniprot/Q8K352 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM|||SAM and SH3 domain-containing protein 3|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000071963 http://togogenome.org/gene/10090:Prl3a1 ^@ http://purl.uniprot.org/uniprot/Q78Y73 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015098645 http://togogenome.org/gene/10090:Or5p62 ^@ http://purl.uniprot.org/uniprot/Q8VFD0 ^@ 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 5P62 ^@ http://purl.uniprot.org/annotation/PRO_0000150843 http://togogenome.org/gene/10090:Pcdhb2 ^@ http://purl.uniprot.org/uniprot/Q91Y00 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Cadherin|||Helical ^@ http://togogenome.org/gene/10090:Fem1c ^@ http://purl.uniprot.org/uniprot/B2RRW5|||http://purl.uniprot.org/uniprot/Q8CEF1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||N-acetylmethionine|||Protein fem-1 homolog C|||TPR 1|||TPR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000324537 http://togogenome.org/gene/10090:Gm20937 ^@ http://purl.uniprot.org/uniprot/J3QNI1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:C87436 ^@ http://purl.uniprot.org/uniprot/Q8R3C1 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Uncharacterized protein C2orf42 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000300123|||http://purl.uniprot.org/annotation/VSP_027792|||http://purl.uniprot.org/annotation/VSP_027793|||http://purl.uniprot.org/annotation/VSP_027794|||http://purl.uniprot.org/annotation/VSP_027795 http://togogenome.org/gene/10090:Tmem240 ^@ http://purl.uniprot.org/uniprot/B2RWJ3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Phosphoserine|||Transmembrane protein 240 ^@ http://purl.uniprot.org/annotation/PRO_0000431907 http://togogenome.org/gene/10090:Krt31 ^@ http://purl.uniprot.org/uniprot/Q61765 ^@ 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 Ha1|||Linker 1|||Linker 12|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063685 http://togogenome.org/gene/10090:Mustn1 ^@ http://purl.uniprot.org/uniprot/Q99JI1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Disordered|||Musculoskeletal embryonic nuclear protein 1|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000299448 http://togogenome.org/gene/10090:Reep2 ^@ http://purl.uniprot.org/uniprot/C1IE02|||http://purl.uniprot.org/uniprot/Q8VCD6 ^@ 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|||Receptor expression-enhancing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000101824 http://togogenome.org/gene/10090:Arl1 ^@ http://purl.uniprot.org/uniprot/P61211 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding ^@ ADP-ribosylation factor-like protein 1|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207451 http://togogenome.org/gene/10090:Dffb ^@ http://purl.uniprot.org/uniprot/O54788|||http://purl.uniprot.org/uniprot/Q7TS81|||http://purl.uniprot.org/uniprot/Q8BP66 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Strand|||Turn ^@ CIDE-N|||DNA fragmentation factor subunit beta ^@ http://purl.uniprot.org/annotation/PRO_0000144714 http://togogenome.org/gene/10090:Vmn1r83 ^@ http://purl.uniprot.org/uniprot/Q8R287 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gata4 ^@ http://purl.uniprot.org/uniprot/E9PXW9|||http://purl.uniprot.org/uniprot/Q08369|||http://purl.uniprot.org/uniprot/Q3UYJ1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||GATA-type|||GATA-type 1|||GATA-type 2|||N6-methyllysine; by EZH2|||Polar residues|||Transcription factor GATA-4 ^@ http://purl.uniprot.org/annotation/PRO_0000083414 http://togogenome.org/gene/10090:Chst3 ^@ http://purl.uniprot.org/uniprot/O88199 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 3|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000085189 http://togogenome.org/gene/10090:Usp29 ^@ http://purl.uniprot.org/uniprot/Q8CAH4|||http://purl.uniprot.org/uniprot/Q9ES63 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Impaired ability to mediate deubiquitination of CGAS.|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 29|||Ubiquitin carboxyl-terminal hydrolase 37 pleckstrin homology-like ^@ http://purl.uniprot.org/annotation/PRO_0000080661 http://togogenome.org/gene/10090:Entr1 ^@ http://purl.uniprot.org/uniprot/A2AIW0|||http://purl.uniprot.org/uniprot/A2AIW3 ^@ 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|||Endosome-associated-trafficking regulator 1|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Polar residues|||Required for interaction with PTPN13 ^@ http://purl.uniprot.org/annotation/PRO_0000324286|||http://purl.uniprot.org/annotation/VSP_032178|||http://purl.uniprot.org/annotation/VSP_032179|||http://purl.uniprot.org/annotation/VSP_032180|||http://purl.uniprot.org/annotation/VSP_032181|||http://purl.uniprot.org/annotation/VSP_032182|||http://purl.uniprot.org/annotation/VSP_032183 http://togogenome.org/gene/10090:Pitpnb ^@ http://purl.uniprot.org/uniprot/P53811 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Modified Residue|||Mutagenesis Site ^@ Abolishes phosphorylation by PKC and impairs Golgi targeting; no effect on phospholipid transfer activity.|||N6-acetyllysine|||No effect on phosphorylation by PKC; abolishes phospholipid transfer activity.|||Phosphatidylinositol transfer protein beta isoform|||Phosphoserine; by PKC ^@ http://purl.uniprot.org/annotation/PRO_0000191644 http://togogenome.org/gene/10090:Ly6g5b ^@ http://purl.uniprot.org/uniprot/N0E6I7|||http://purl.uniprot.org/uniprot/Q8K1T4 ^@ 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 ^@ In isoform 2.|||Lymphocyte antigen 6 complex locus protein G5b|||N-linked (GlcNAc...) asparagine|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000318603|||http://purl.uniprot.org/annotation/PRO_5014306404|||http://purl.uniprot.org/annotation/VSP_031256 http://togogenome.org/gene/10090:Or4f56 ^@ http://purl.uniprot.org/uniprot/A2AVW3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Utp25 ^@ http://purl.uniprot.org/uniprot/A0A0R4J114|||http://purl.uniprot.org/uniprot/Q8BTT6 ^@ 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|||Basic and acidic residues|||Disordered|||Phosphoserine|||Promotes p53/TP53 degradation|||Represses p53/TP53 degradation|||U3 small nucleolar RNA-associated protein 25 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000254150 http://togogenome.org/gene/10090:4930426D05Rik ^@ http://purl.uniprot.org/uniprot/Q9D5L2 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Bcas2 ^@ http://purl.uniprot.org/uniprot/Q9D287 ^@ 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|||Phosphoserine|||Pre-mRNA-splicing factor SPF27|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000064862 http://togogenome.org/gene/10090:Kpnb1 ^@ http://purl.uniprot.org/uniprot/P70168|||http://purl.uniprot.org/uniprot/Q3UHW8 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Ran-GTP binding ^@ http://purl.uniprot.org/annotation/PRO_0000120746 http://togogenome.org/gene/10090:Gpr15 ^@ http://purl.uniprot.org/uniprot/Q0VDU3 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||G-protein coupled receptor 15|||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_0000303232 http://togogenome.org/gene/10090:Zfp239 ^@ http://purl.uniprot.org/uniprot/P24399 ^@ 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|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Zinc finger protein 239 ^@ http://purl.uniprot.org/annotation/PRO_0000047481 http://togogenome.org/gene/10090:Ap3s1 ^@ http://purl.uniprot.org/uniprot/A0A286YDU3|||http://purl.uniprot.org/uniprot/Q3U8S0|||http://purl.uniprot.org/uniprot/Q9DCR2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ AP complex mu/sigma subunit|||AP-3 complex subunit sigma-1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000193816 http://togogenome.org/gene/10090:Stat1 ^@ http://purl.uniprot.org/uniprot/A0A087WSP5|||http://purl.uniprot.org/uniprot/Q8C3V4|||http://purl.uniprot.org/uniprot/Q8C497|||http://purl.uniprot.org/uniprot/Q8C8M3|||http://purl.uniprot.org/uniprot/Q8CFQ1|||http://purl.uniprot.org/uniprot/Q99K94 ^@ Coiled-Coil|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||SH2 ^@ http://togogenome.org/gene/10090:Rag1 ^@ http://purl.uniprot.org/uniprot/P15919|||http://purl.uniprot.org/uniprot/Q3TR87 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Abolishes autoubiquitination.|||Allows robust hairpin activity.|||Basic and acidic residues|||Capable of both nicking and hairpinning.|||Capable of nicking and retains some hairpinning.|||Capable of nicking but defective for hairpinning.|||Defects in converting nicked products to hairpins.|||Deficient in both nicking and hairpin formation.|||Disordered|||Displays lower E3 ligase activity and affects the joining step of V(D)J recombination.|||Essential for DNA hairpin formation, participates in base-stacking interactions near the cleavage site|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired cleavage (both nicking and hairpin formation).|||Impaired cleavage (defective in hairpin formation).|||Impaired cleavage.|||Impairs DNA-binding and hairpin formation while maintaining some nicking activity.|||Impairs DNA-binding and reduces hairpin formation without affecting nicking activity.|||Impairs DNA-binding; when associated with A-443.|||Impairs DNA-binding; when associated with A-445.|||Loss of DNA-binding.|||Loss of E3 ligase activity and affects the joining step of V(D)J recombination.|||Loss of cleavage (both nicking and hairpin formation).|||Loss of cleavage and strand transfer activities without affecting allelic exclusion.|||Loss of cleavage and strand transfer activities.|||Moderately defective with 56% of activity.|||NBD|||RAG1 importin-binding|||RAG1-type|||RING-type|||Reduced hairpin activity.|||V(D)J recombination-activating protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000056005 http://togogenome.org/gene/10090:Inf2 ^@ http://purl.uniprot.org/uniprot/E9QLA5|||http://purl.uniprot.org/uniprot/Q0GNC1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||FH1|||FH2|||GBD/FH3|||In isoform 2.|||Inverted formin-2|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Strongly inhibits depolymerization; when associated with A-1009 and A-1010.|||Strongly inhibits depolymerization; when associated with A-1009 and A-1019.|||Strongly inhibits depolymerization; when associated with A-1010 and A-1019.|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000259890|||http://purl.uniprot.org/annotation/VSP_021560 http://togogenome.org/gene/10090:Sncb ^@ http://purl.uniprot.org/uniprot/Q91ZZ3 ^@ 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|||Phosphoserine; by BARK1, CK2 and GRK5 ^@ http://purl.uniprot.org/annotation/PRO_0000286176 http://togogenome.org/gene/10090:Fam186b ^@ http://purl.uniprot.org/uniprot/D3Z420 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Padi6 ^@ http://purl.uniprot.org/uniprot/Q8K3V4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Protein-arginine deiminase type-6 ^@ http://purl.uniprot.org/annotation/PRO_0000220037 http://togogenome.org/gene/10090:Myf6 ^@ http://purl.uniprot.org/uniprot/P15375|||http://purl.uniprot.org/uniprot/Q0VEJ7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Disordered|||Myogenic factor 6|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127352 http://togogenome.org/gene/10090:Rnf223 ^@ http://purl.uniprot.org/uniprot/A0A1B0GR81 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||RING-type ^@ http://togogenome.org/gene/10090:Omg ^@ http://purl.uniprot.org/uniprot/G3XA53|||http://purl.uniprot.org/uniprot/Q63912|||http://purl.uniprot.org/uniprot/Q8CAB4 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Non-terminal Residue|||Propeptide|||Repeat|||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_0000021890|||http://purl.uniprot.org/annotation/PRO_0000021891|||http://purl.uniprot.org/annotation/PRO_5015091877 http://togogenome.org/gene/10090:Slc25a39 ^@ http://purl.uniprot.org/uniprot/Q14BQ5|||http://purl.uniprot.org/uniprot/Q9D8K8 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Repeat|||Transmembrane ^@ Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Probable mitochondrial glutathione transporter SLC25A39|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090597 http://togogenome.org/gene/10090:Mageb18 ^@ http://purl.uniprot.org/uniprot/Q8BQR7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic residues|||Disordered|||MAGE|||Melanoma-associated antigen B18|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000436362 http://togogenome.org/gene/10090:Gm12169 ^@ http://purl.uniprot.org/uniprot/F2Z474 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5003290095 http://togogenome.org/gene/10090:Slc35a1 ^@ http://purl.uniprot.org/uniprot/Q61420 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane|||Turn ^@ CMP-sialic acid transporter|||Cytoplasmic|||Disordered|||Helical|||Loss of CMP-sialic acid transport activity but no effect on CDP-ribitol transport activity.|||Lumenal|||No effect on CDP-ribitol and CMP-sialic acid transport activity.|||No effect on CMP-sialic acid transport activity.|||Results in localization to the endoplasmic reticulum. ^@ http://purl.uniprot.org/annotation/PRO_0000213352 http://togogenome.org/gene/10090:Nell2 ^@ http://purl.uniprot.org/uniprot/Q61220 ^@ 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 ^@ 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|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Protein kinase C-binding protein NELL2|||VWFC 1|||VWFC 2 ^@ http://purl.uniprot.org/annotation/PRO_0000007667 http://togogenome.org/gene/10090:Col2a1 ^@ http://purl.uniprot.org/uniprot/P28481 ^@ Binding Site|||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|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant ^@ 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 isoform 2 and isoform 3.|||In isoform 3 and isoform 7.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||In sedc mice.|||Interchain (with C-1289)|||Interchain (with C-1306)|||N-terminal propeptide|||Nonhelical region (C-terminal)|||O-linked (Gal...) hydroxylysine|||Pro residues|||Triple-helical region|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000005732|||http://purl.uniprot.org/annotation/PRO_0000005733|||http://purl.uniprot.org/annotation/PRO_0000005734|||http://purl.uniprot.org/annotation/VSP_022780|||http://purl.uniprot.org/annotation/VSP_022781|||http://purl.uniprot.org/annotation/VSP_022782|||http://purl.uniprot.org/annotation/VSP_022783|||http://purl.uniprot.org/annotation/VSP_022784|||http://purl.uniprot.org/annotation/VSP_022785 http://togogenome.org/gene/10090:Cnpy2 ^@ http://purl.uniprot.org/uniprot/Q9QXT0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Signal Peptide ^@ Phosphoserine|||Prevents secretion from ER|||Protein canopy homolog 2|||Saposin B-type ^@ http://purl.uniprot.org/annotation/PRO_0000031667 http://togogenome.org/gene/10090:Socs3 ^@ http://purl.uniprot.org/uniprot/O35718 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand ^@ Abolishes binding to EPOR. No effect on binding to JAK2.|||Abolishes binding to JAK2. No effect on binding to EPOR.|||Disordered|||Extended SH2 subdomain (ESS)|||Kinase inhibitory region (KIR)|||Little effect on LIF-induced signal transduction suppression. Loss of EPO-induced signal transduction suppression. Abolishes binding to JAK2 and EPOR.|||Loss of LIF/EPO-induced signal transduction suppression. Abolishes binding to JAK2 and to EPOR.|||No effect on LIF-induced signal transduction suppression.|||SH2|||SOCS box|||Suppressor of cytokine signaling 3 ^@ http://purl.uniprot.org/annotation/PRO_0000181244 http://togogenome.org/gene/10090:Uggt2 ^@ http://purl.uniprot.org/uniprot/E9Q4X2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Glucosyltransferase 24 catalytic|||UDP-glucose:glycoprotein glucosyltransferase thioredoxin-like|||UGGT thioredoxin-like ^@ http://purl.uniprot.org/annotation/PRO_5003245890 http://togogenome.org/gene/10090:Cfap65 ^@ http://purl.uniprot.org/uniprot/Q3V0B4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cilia- and flagella-associated protein 65|||Disordered|||Helical|||MSP ^@ http://purl.uniprot.org/annotation/PRO_0000288806 http://togogenome.org/gene/10090:4930555G01Rik ^@ http://purl.uniprot.org/uniprot/Q8C5Y7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Atp6v0d1 ^@ http://purl.uniprot.org/uniprot/P51863 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Phosphotyrosine|||V-type proton ATPase subunit d 1 ^@ http://purl.uniprot.org/annotation/PRO_0000119351 http://togogenome.org/gene/10090:D1Pas1 ^@ http://purl.uniprot.org/uniprot/B9EIA2|||http://purl.uniprot.org/uniprot/P16381 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Basic and acidic 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-acetylserine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Putative ATP-dependent RNA helicase Pl10|||Q motif|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000055008 http://togogenome.org/gene/10090:Mmp25 ^@ http://purl.uniprot.org/uniprot/Q3U435 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Lipid Binding|||Motif|||Propeptide|||Region|||Repeat|||Transmembrane ^@ Cysteine switch|||Disordered|||GPI-anchor amidated alanine|||Helical|||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_0000288635|||http://purl.uniprot.org/annotation/PRO_0000288636|||http://purl.uniprot.org/annotation/PRO_0000288637 http://togogenome.org/gene/10090:Gm8882 ^@ http://purl.uniprot.org/uniprot/E9Q7E4 ^@ 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_5003244476 http://togogenome.org/gene/10090:Zbtb21 ^@ http://purl.uniprot.org/uniprot/E9Q3R9|||http://purl.uniprot.org/uniprot/E9Q444|||http://purl.uniprot.org/uniprot/G3X9A3|||http://purl.uniprot.org/uniprot/Q80XC5|||http://purl.uniprot.org/uniprot/Q8BSP5|||http://purl.uniprot.org/uniprot/Q8CC25 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB|||Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:G6pc ^@ http://purl.uniprot.org/uniprot/P35576 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Glucose-6-phosphatase catalytic subunit 1|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Prevents secretion from ER|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000087414 http://togogenome.org/gene/10090:Ascl5 ^@ http://purl.uniprot.org/uniprot/M0QWB7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Achaete-scute homolog 5|||Basic motif|||Disordered|||Helix-loop-helix motif|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000456969 http://togogenome.org/gene/10090:Cd200r4 ^@ http://purl.uniprot.org/uniprot/H3BJX3|||http://purl.uniprot.org/uniprot/Q6XJV4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Acquires binding to CD200; when associated with K-87 and F-138.|||Acquires binding to CD200; when associated with K-87 and T-90.|||Acquires binding to CD200; when associated with T-90 and F-138.|||Cell surface glycoprotein CD200 receptor 4|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000346454 http://togogenome.org/gene/10090:Srrm1 ^@ http://purl.uniprot.org/uniprot/A2A8V9|||http://purl.uniprot.org/uniprot/E9PUK6|||http://purl.uniprot.org/uniprot/Q52KI8 ^@ 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|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000076327|||http://purl.uniprot.org/annotation/VSP_016524|||http://purl.uniprot.org/annotation/VSP_016525 http://togogenome.org/gene/10090:Ly6k ^@ http://purl.uniprot.org/uniprot/Q9CWP4 ^@ Chain|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Lipid Binding|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated glycine|||Lymphocyte antigen 6K|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000318201|||http://purl.uniprot.org/annotation/PRO_0000337086 http://togogenome.org/gene/10090:Tex50 ^@ http://purl.uniprot.org/uniprot/Q9D5B7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Transmembrane ^@ Basic residues|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099668 http://togogenome.org/gene/10090:Zfp750 ^@ http://purl.uniprot.org/uniprot/Q8BH05 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type; degenerate|||Disordered|||Polar residues|||Zinc finger protein 750 ^@ http://purl.uniprot.org/annotation/PRO_0000247071 http://togogenome.org/gene/10090:Igsf5 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1E1|||http://purl.uniprot.org/uniprot/A0A0R4J105|||http://purl.uniprot.org/uniprot/D3YXH1|||http://purl.uniprot.org/uniprot/Q7TSN7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type 1|||Ig-like V-type 2|||Immunoglobulin subtype|||Immunoglobulin superfamily member 5|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000316296|||http://purl.uniprot.org/annotation/PRO_5002106978|||http://purl.uniprot.org/annotation/PRO_5003052734|||http://purl.uniprot.org/annotation/PRO_5015044296 http://togogenome.org/gene/10090:Exosc3 ^@ http://purl.uniprot.org/uniprot/Q7TQK4 ^@ Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Exosome complex component RRP40|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087132 http://togogenome.org/gene/10090:Tm6sf2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0J9|||http://purl.uniprot.org/uniprot/E9QM19|||http://purl.uniprot.org/uniprot/Q8R1J1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ EXPERA|||EXPERA 1|||EXPERA 2|||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.|||Transmembrane 6 superfamily member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000262719|||http://purl.uniprot.org/annotation/VSP_021806 http://togogenome.org/gene/10090:Poc5 ^@ http://purl.uniprot.org/uniprot/Q9DBS8 ^@ 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 ^@ Centrin-binding (CBR) 1|||Centrin-binding (CBR) 2|||Centrin-binding (CBR) 3|||Centrosomal protein POC5|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000281910|||http://purl.uniprot.org/annotation/VSP_024101|||http://purl.uniprot.org/annotation/VSP_024102 http://togogenome.org/gene/10090:Or2g1 ^@ http://purl.uniprot.org/uniprot/Q8VFQ1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ldb2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFS7|||http://purl.uniprot.org/uniprot/O55203 ^@ 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 3.|||In isoform 3.|||LIM domain-binding protein 2|||LIM interaction|||LIM interaction domain (LID)|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084388|||http://purl.uniprot.org/annotation/VSP_014369|||http://purl.uniprot.org/annotation/VSP_014370|||http://purl.uniprot.org/annotation/VSP_027829 http://togogenome.org/gene/10090:Glce ^@ http://purl.uniprot.org/uniprot/Q9EPS3 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Critical for catalysis|||Cytoplasmic|||D-glucuronyl C5-epimerase|||Helical; Signal-anchor for type II membrane protein|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000192646 http://togogenome.org/gene/10090:Rbbp5 ^@ http://purl.uniprot.org/uniprot/Q8BX09 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||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 ASH2L|||Interaction with WDR5|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine; by CDK1|||Polar residues|||Retinoblastoma-binding protein 5|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000390999|||http://purl.uniprot.org/annotation/VSP_038671|||http://purl.uniprot.org/annotation/VSP_038672 http://togogenome.org/gene/10090:Ppfia3 ^@ http://purl.uniprot.org/uniprot/P60469|||http://purl.uniprot.org/uniprot/Q9CWF5 ^@ Chain|||Coiled-Coil|||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|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn ^@ 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_0000191030|||http://purl.uniprot.org/annotation/VSP_057923 http://togogenome.org/gene/10090:Brf1 ^@ http://purl.uniprot.org/uniprot/G3X8S2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||TFIIB-type ^@ http://togogenome.org/gene/10090:Septin12 ^@ http://purl.uniprot.org/uniprot/Q9D451|||http://purl.uniprot.org/uniprot/Q9D9U8 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Septin-type G ^@ http://togogenome.org/gene/10090:Vmn1r191 ^@ http://purl.uniprot.org/uniprot/Q8K4D0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp69 ^@ http://purl.uniprot.org/uniprot/A2A761|||http://purl.uniprot.org/uniprot/Q6NZQ1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||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|||KRAB|||Polar residues|||Zinc finger protein 69 ^@ http://purl.uniprot.org/annotation/PRO_0000444716 http://togogenome.org/gene/10090:Dnajb7 ^@ http://purl.uniprot.org/uniprot/Q9QYI8 ^@ 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|||DnaJ homolog subfamily B member 7|||J ^@ http://purl.uniprot.org/annotation/PRO_0000071028 http://togogenome.org/gene/10090:Tnfsf15 ^@ http://purl.uniprot.org/uniprot/A0A0U5J7F3|||http://purl.uniprot.org/uniprot/B2RR33|||http://purl.uniprot.org/uniprot/Q5UBV8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Important for binding TNFRSF6B|||N-linked (GlcNAc...) asparagine|||TNF family profile|||Tumor necrosis factor ligand superfamily member 15 ^@ http://purl.uniprot.org/annotation/PRO_0000333232 http://togogenome.org/gene/10090:Cmah ^@ http://purl.uniprot.org/uniprot/Q61419 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Propeptide|||Sequence Conflict|||Splice Variant ^@ Cytidine monophosphate-N-acetylneuraminic acid hydroxylase|||In isoform 2.|||Rieske ^@ http://purl.uniprot.org/annotation/PRO_0000030699|||http://purl.uniprot.org/annotation/PRO_0000030700|||http://purl.uniprot.org/annotation/VSP_013769 http://togogenome.org/gene/10090:Ssr3 ^@ http://purl.uniprot.org/uniprot/Q4FK79|||http://purl.uniprot.org/uniprot/Q9DCF9 ^@ 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_0000191691|||http://purl.uniprot.org/annotation/VSP_013474|||http://purl.uniprot.org/annotation/VSP_013475 http://togogenome.org/gene/10090:Or10al3 ^@ http://purl.uniprot.org/uniprot/Q7TRJ5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dchs1 ^@ http://purl.uniprot.org/uniprot/E9PVD3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||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 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protocadherin-16 ^@ http://purl.uniprot.org/annotation/PRO_0000429045 http://togogenome.org/gene/10090:Espn ^@ http://purl.uniprot.org/uniprot/Q9DD12|||http://purl.uniprot.org/uniprot/Q9ET47 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Turn ^@ 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 isoform 2 and isoform 3.|||In isoform 2, isoform 4, isoform 3 and isoform 5.|||In isoform 2, isoform 5, isoform 6 and isoform 7.|||In isoform 4 and isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Phosphoserine|||Polar residues|||Pro residues|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000334667|||http://purl.uniprot.org/annotation/VSP_033730|||http://purl.uniprot.org/annotation/VSP_033731|||http://purl.uniprot.org/annotation/VSP_033732|||http://purl.uniprot.org/annotation/VSP_033733|||http://purl.uniprot.org/annotation/VSP_033734|||http://purl.uniprot.org/annotation/VSP_033735|||http://purl.uniprot.org/annotation/VSP_033736|||http://purl.uniprot.org/annotation/VSP_033737|||http://purl.uniprot.org/annotation/VSP_033738|||http://purl.uniprot.org/annotation/VSP_033739|||http://purl.uniprot.org/annotation/VSP_033740 http://togogenome.org/gene/10090:Jak2 ^@ http://purl.uniprot.org/uniprot/Q62120 ^@ 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|||Region|||Sequence Conflict ^@ About 60% loss of STAT1 phosphorylation by JAK2.|||Affects the phosphorylation pattern.|||Decreased the ability of JAK2 to autophosphorylate.|||FERM|||Interaction with cytokine/interferon/growth hormone receptors|||More stably associated with the erythropoietin receptor complex.|||Phosphorylation mimic mutant, leads to dissociation of JAK2 from the erythropoietin receptor complex.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Reduced activity in response to growth hormone.|||SH2; atypical|||Tyrosine-protein kinase JAK2 ^@ http://purl.uniprot.org/annotation/PRO_0000088113 http://togogenome.org/gene/10090:Clmp ^@ http://purl.uniprot.org/uniprot/Q8R373 ^@ 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 ^@ Basic and acidic residues|||CXADR-like membrane protein|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000293027 http://togogenome.org/gene/10090:Unk ^@ http://purl.uniprot.org/uniprot/Q3UYU7|||http://purl.uniprot.org/uniprot/Q8BL48 ^@ 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|||Turn|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Basic residues|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||C3H1-type 5|||Disordered|||In isoform 2.|||Phosphoserine|||RING finger protein unkempt homolog|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000213900|||http://purl.uniprot.org/annotation/VSP_010274 http://togogenome.org/gene/10090:Mtus1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0N9|||http://purl.uniprot.org/uniprot/A0A0R4J147|||http://purl.uniprot.org/uniprot/A0A0R4J1L9|||http://purl.uniprot.org/uniprot/Q5HZI1 ^@ 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 and isoform 3.|||In isoform 3.|||In isoform 4.|||Microtubule-associated tumor suppressor 1 homolog|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000305198|||http://purl.uniprot.org/annotation/VSP_028279|||http://purl.uniprot.org/annotation/VSP_028280|||http://purl.uniprot.org/annotation/VSP_028281|||http://purl.uniprot.org/annotation/VSP_028282|||http://purl.uniprot.org/annotation/VSP_028283 http://togogenome.org/gene/10090:Kif4 ^@ http://purl.uniprot.org/uniprot/P33174 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Chromosome-associated kinesin KIF4|||Disordered|||Globular|||Kinesin motor|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000125438 http://togogenome.org/gene/10090:Dennd6a ^@ http://purl.uniprot.org/uniprot/Q8BH65 ^@ 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 and isoform 4.|||In isoform 4.|||N6-methyllysine|||Phosphoserine|||Protein DENND6A|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000289117|||http://purl.uniprot.org/annotation/VSP_025918|||http://purl.uniprot.org/annotation/VSP_025919|||http://purl.uniprot.org/annotation/VSP_025920|||http://purl.uniprot.org/annotation/VSP_025921 http://togogenome.org/gene/10090:Or5b109 ^@ http://purl.uniprot.org/uniprot/Q7TQR3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gnl2 ^@ http://purl.uniprot.org/uniprot/Q3V3N5|||http://purl.uniprot.org/uniprot/Q99LH1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||CP-type G|||Disordered|||N-acetylmethionine|||Nucleolar GTP-binding protein 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000215807 http://togogenome.org/gene/10090:Tomt ^@ http://purl.uniprot.org/uniprot/A1Y9I9 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Site ^@ Binding Site|||Chain|||Mutagenesis Site ^@ Absence of auditory brain stem response (ABR) to click stimuli demonstrates that the mice are profoundly deaf. Distortion product otoacoustic emissions (DPOAEs) are absent at 4 weeks of age at all frequencies tested. Normal hair bundle morphology as at postnatal day (P) 5 the sensory epithelia are patterned into three rows of outer hair cells (OHCs) and one row of inner hair cells (IHCs). The bundles of OHCs appear similar in size to those of wild-type mice and form a normal staircase pattern.|||Enhanced interaction with TMC1.|||In add; reduces methyltransferase activity; causes hyperkinesis, circling, head-tossing, aggression, progressive degeneration of the organ of Corti, hair cell defects and profound deafness. Distortion product otoacoustic emissions (DPOAEs) are absent at 4 weeks of age at all frequencies tested. At postnatal day (P) 5 the sensory epithelia are patterned into three rows of outer hair cells (OHCs) and one row of inner hair cells (IHCs) with no obvious structural abnormalities. The bundles of OHCs appear similar in size to those of wild-type mice and form a normal staircase pattern. The hair bundles of OHCs have a slightly more rounded morphology, especially in basal regions of the cochlea. The morphology of IHCs is not significantly altered. Hair cells are maintained in the presence of gentamicin, an aminoglycoside antibiotic that enters hair cells through their transduction channels and normally causes hair cell death. Mechanotransduction currents are very small in P4 hair cells and completely absent in P7 hair cells. Membrane potential, outward-evoked currents and nonlinear capacitance are normal in OHCs. No difference in the expression or localization of tip link proteins CDH23 and PCDH15 or ATP2B2, MYO7A, ESPN and WHRN proteins at P5-P8 in hair bundles of hair cells. No difference in the number of tip links in IHCs and OHCs at P7-P8. No difference in the levels of catecholamines, including norepinephrine, homovanillic acid (HVA) and norepinephrine, or serotonin levels in the inner ear. Loss of reverse polarity currents.|||Is able to rescue the mechanotransduction defect of L-48.|||Transmembrane O-methyltransferase homolog ^@ http://purl.uniprot.org/annotation/PRO_0000354094 http://togogenome.org/gene/10090:Riok1 ^@ http://purl.uniprot.org/uniprot/Q922Q2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 4-aspartylphosphate intermediate|||Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase RIO1 ^@ http://purl.uniprot.org/annotation/PRO_0000314490 http://togogenome.org/gene/10090:Zc4h2 ^@ http://purl.uniprot.org/uniprot/Q05BE0|||http://purl.uniprot.org/uniprot/Q68FG0 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C4H2-type|||In isoform 2.|||Zinc finger C4H2 domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000083912|||http://purl.uniprot.org/annotation/VSP_013470 http://togogenome.org/gene/10090:Gdf3 ^@ http://purl.uniprot.org/uniprot/Q07104 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Growth/differentiation factor 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000033910|||http://purl.uniprot.org/annotation/PRO_0000033911 http://togogenome.org/gene/10090:Fem1b ^@ http://purl.uniprot.org/uniprot/Q9Z2G0 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||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 reduced FNIP1.|||Abolished association with BEX family proteins (BEX1, BEX2, BEX3 and/or BEX4), leading to constitutive ubiquitination of FNIP1.|||Cleavage; by a caspase-3-like protease|||Protein fem-1 homolog B|||TPR ^@ http://purl.uniprot.org/annotation/PRO_0000324531 http://togogenome.org/gene/10090:Fam221b ^@ http://purl.uniprot.org/uniprot/Q8C627 ^@ 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|||Protein FAM221B ^@ http://purl.uniprot.org/annotation/PRO_0000309265|||http://purl.uniprot.org/annotation/VSP_029102|||http://purl.uniprot.org/annotation/VSP_029103 http://togogenome.org/gene/10090:Ankrd24 ^@ http://purl.uniprot.org/uniprot/Q80VM7|||http://purl.uniprot.org/uniprot/Q8VD21 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 24|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000328837 http://togogenome.org/gene/10090:Btnl1 ^@ http://purl.uniprot.org/uniprot/Q7TST0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ B30.2/SPRY|||Basic and acidic residues|||Butyrophilin-like protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000014536 http://togogenome.org/gene/10090:Ly96 ^@ http://purl.uniprot.org/uniprot/A0A087WQZ9|||http://purl.uniprot.org/uniprot/Q14AM4|||http://purl.uniprot.org/uniprot/Q64HC9|||http://purl.uniprot.org/uniprot/Q9JHF9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Turn ^@ Abolishes dimerization of the TLR4 complex and stimulation of TNF production in response to bacterial lipopolysaccharide.|||Interaction with lipopolysaccharide|||Lymphocyte antigen 96|||MD-2-related lipid-recognition|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000018620|||http://purl.uniprot.org/annotation/PRO_5001831830|||http://purl.uniprot.org/annotation/PRO_5004268091|||http://purl.uniprot.org/annotation/PRO_5014306915 http://togogenome.org/gene/10090:Vmn1r209 ^@ http://purl.uniprot.org/uniprot/Q5NC97 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Angptl4 ^@ http://purl.uniprot.org/uniprot/Q9Z1P8 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ ANGPTL4 C-terminal chain|||ANGPTL4 N-terminal chain|||Angiopoietin-related protein 4|||Cleavage|||Disordered|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009125|||http://purl.uniprot.org/annotation/PRO_0000446861|||http://purl.uniprot.org/annotation/PRO_0000446862 http://togogenome.org/gene/10090:Sstr3 ^@ http://purl.uniprot.org/uniprot/P30935 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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_0000070125 http://togogenome.org/gene/10090:Ivd ^@ http://purl.uniprot.org/uniprot/Q9JHI5 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Isovaleryl-CoA dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000000532 http://togogenome.org/gene/10090:Tmem174 ^@ http://purl.uniprot.org/uniprot/Q9DCX7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 174 ^@ http://purl.uniprot.org/annotation/PRO_0000282578 http://togogenome.org/gene/10090:Prickle3 ^@ http://purl.uniprot.org/uniprot/Q80VL3|||http://purl.uniprot.org/uniprot/Q8BNH2 ^@ 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 residues|||Disordered|||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_0000075823 http://togogenome.org/gene/10090:Slc24a5 ^@ http://purl.uniprot.org/uniprot/A2ATP8|||http://purl.uniprot.org/uniprot/Q8C261 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||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|||Sodium/calcium exchanger membrane region|||Sodium/potassium/calcium exchanger 5 ^@ http://purl.uniprot.org/annotation/PRO_0000045754 http://togogenome.org/gene/10090:Or8b12i ^@ http://purl.uniprot.org/uniprot/Q8VGG4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Muc6 ^@ http://purl.uniprot.org/uniprot/Q0VAV1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Polar residues|||Pro residues|||VWFD ^@ http://purl.uniprot.org/annotation/PRO_5015096996 http://togogenome.org/gene/10090:Arhgap18 ^@ http://purl.uniprot.org/uniprot/Q8K0Q5 ^@ 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|||Phosphothreonine|||Polar residues|||Rho GTPase-activating protein 18|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000245790 http://togogenome.org/gene/10090:Gspt1 ^@ http://purl.uniprot.org/uniprot/Q8CCV1|||http://purl.uniprot.org/uniprot/Q8R050 ^@ 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.|||Polar residues|||Tr-type G|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000091481|||http://purl.uniprot.org/annotation/VSP_043829 http://togogenome.org/gene/10090:Fam107a ^@ http://purl.uniprot.org/uniprot/Q78TU8 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Motif|||Region ^@ Chain|||Coiled-Coil|||Motif|||Region ^@ Actin-associated protein FAM107A|||Disordered|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000444955 http://togogenome.org/gene/10090:Gstp1 ^@ http://purl.uniprot.org/uniprot/P19157 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Strand|||Turn ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase P 1|||N6-acetyllysine|||N6-succinyllysine|||Phosphothreonine|||Phosphotyrosine; by EGFR|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000185903 http://togogenome.org/gene/10090:Tmem129 ^@ http://purl.uniprot.org/uniprot/Q8K304 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Sequence Conflict|||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_0000291042|||http://purl.uniprot.org/annotation/VSP_026159 http://togogenome.org/gene/10090:Rint1 ^@ http://purl.uniprot.org/uniprot/Q8BZ36 ^@ 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 ^@ Disordered|||In isoform 2.|||Polar residues|||RAD50-interacting protein 1|||RINT1/TIP20 ^@ http://purl.uniprot.org/annotation/PRO_0000097350|||http://purl.uniprot.org/annotation/VSP_012658 http://togogenome.org/gene/10090:Dus1l ^@ http://purl.uniprot.org/uniprot/Q8C2P3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Proton donor|||tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like ^@ http://purl.uniprot.org/annotation/PRO_0000247227 http://togogenome.org/gene/10090:Zscan4d ^@ http://purl.uniprot.org/uniprot/A7KBS4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||SCAN box|||Zinc finger and SCAN domain containing protein 4D ^@ http://purl.uniprot.org/annotation/PRO_0000394245 http://togogenome.org/gene/10090:H2bc7 ^@ http://purl.uniprot.org/uniprot/P10853 ^@ 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-F/J/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-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_0000071839 http://togogenome.org/gene/10090:Mxra8 ^@ http://purl.uniprot.org/uniprot/Q9DBV4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||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|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||Matrix remodeling-associated protein 8|||N-linked (GlcNAc...) asparagine|||No significant effect on integrin ITGAV:ITGB3 binding.|||Phosphoserine|||Polar residues|||RGD 1|||RGD 2|||Reduced integrin ITGAV:ITGB3 binding. ^@ http://purl.uniprot.org/annotation/PRO_0000298666 http://togogenome.org/gene/10090:Osbpl5 ^@ http://purl.uniprot.org/uniprot/G5E833|||http://purl.uniprot.org/uniprot/Q9ER64 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Oxysterol-binding protein-related protein 5|||PH|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000100374 http://togogenome.org/gene/10090:Heatr5a ^@ http://purl.uniprot.org/uniprot/Q5PRF0 ^@ 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.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000311991|||http://purl.uniprot.org/annotation/VSP_029687 http://togogenome.org/gene/10090:Klhdc1 ^@ http://purl.uniprot.org/uniprot/Q80YG3 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000228992 http://togogenome.org/gene/10090:Fbxw28 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFZ2|||http://purl.uniprot.org/uniprot/E9Q8A4|||http://purl.uniprot.org/uniprot/Q3UPQ4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Shc3 ^@ http://purl.uniprot.org/uniprot/Q61120 ^@ 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|||Phosphoserine|||Polar residues|||SH2|||SHC-transforming protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000097735 http://togogenome.org/gene/10090:Cnot7 ^@ http://purl.uniprot.org/uniprot/Q60809 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Site ^@ Binding Site|||Chain|||Mutagenesis Site ^@ CCR4-NOT transcription complex subunit 7|||Severe decrease of interaction with BTG4. ^@ http://purl.uniprot.org/annotation/PRO_0000212845 http://togogenome.org/gene/10090:Siglecg ^@ http://purl.uniprot.org/uniprot/Q80ZE3|||http://purl.uniprot.org/uniprot/Q8BY18 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Decreases interaction with RIGI; when associated with F-590, F-635 and F-659.|||Decreases interaction with RIGI; when associated with F-590, F-659 and F-682.|||Decreases interaction with RIGI; when associated with F-590,F-635 and F-682.|||Decreases interaction with RIGI; when associated with F-635, F-659 and F-682.|||Decreases interaction with membrane IgM (with greater effect in B1a than in B2 cells).|||Disordered|||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|||Ig-like domain-containing protein|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Sialic acid-binding Ig-like lectin 10 ^@ http://purl.uniprot.org/annotation/PRO_5004306039|||http://purl.uniprot.org/annotation/PRO_5010508953 http://togogenome.org/gene/10090:Pate12 ^@ http://purl.uniprot.org/uniprot/D3YX25 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5003052351 http://togogenome.org/gene/10090:Polr3gl ^@ http://purl.uniprot.org/uniprot/D3YXS1|||http://purl.uniprot.org/uniprot/Q8R0C0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||DNA-directed RNA polymerase III subunit RPC7-like|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000311591 http://togogenome.org/gene/10090:Qrfprl ^@ http://purl.uniprot.org/uniprot/G3UWA8|||http://purl.uniprot.org/uniprot/Q8BHH0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tspan32 ^@ http://purl.uniprot.org/uniprot/G3X9S3|||http://purl.uniprot.org/uniprot/Q3U3L6|||http://purl.uniprot.org/uniprot/Q7TNQ7|||http://purl.uniprot.org/uniprot/Q9JHH2 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 1, isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||Tetraspanin-32 ^@ http://purl.uniprot.org/annotation/PRO_0000219279|||http://purl.uniprot.org/annotation/VSP_003939|||http://purl.uniprot.org/annotation/VSP_003940|||http://purl.uniprot.org/annotation/VSP_003941|||http://purl.uniprot.org/annotation/VSP_003942|||http://purl.uniprot.org/annotation/VSP_003943 http://togogenome.org/gene/10090:Or10a3 ^@ http://purl.uniprot.org/uniprot/Q8VEW1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or6e1 ^@ http://purl.uniprot.org/uniprot/Q9Z1V0 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6E1 ^@ http://purl.uniprot.org/annotation/PRO_0000422153 http://togogenome.org/gene/10090:Or5i1 ^@ http://purl.uniprot.org/uniprot/G3X9L8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dhrs4 ^@ http://purl.uniprot.org/uniprot/Q99LB2 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Site ^@ Dehydrogenase/reductase SDR family member 4|||Important for the maintenance of the quaternary structure, the catalytic activity and cold stability|||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 3alpha-hydroxysteroids and benzil into S-benzoin ^@ http://purl.uniprot.org/annotation/PRO_0000054648 http://togogenome.org/gene/10090:Arid1a ^@ http://purl.uniprot.org/uniprot/A2BH40 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ ARID|||AT-rich interactive domain-containing protein 1A|||Acidic residues|||Asymmetric dimethylarginine|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||LXXLL|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000391619|||http://purl.uniprot.org/annotation/VSP_038737|||http://purl.uniprot.org/annotation/VSP_038738|||http://purl.uniprot.org/annotation/VSP_038739|||http://purl.uniprot.org/annotation/VSP_038740 http://togogenome.org/gene/10090:Mdc1 ^@ http://purl.uniprot.org/uniprot/E9QK89|||http://purl.uniprot.org/uniprot/Q5PSV9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Interaction with CHEK2|||Interaction with the MRN complex|||Mediator of DNA damage checkpoint protein 1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000096318 http://togogenome.org/gene/10090:Gm4297 ^@ http://purl.uniprot.org/uniprot/D3YWB7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:S100a5 ^@ http://purl.uniprot.org/uniprot/P63084|||http://purl.uniprot.org/uniprot/Q149U2 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ EF-hand|||EF-hand 1|||EF-hand 2|||Protein S100-A5 ^@ http://purl.uniprot.org/annotation/PRO_0000143981 http://togogenome.org/gene/10090:Foxa1 ^@ http://purl.uniprot.org/uniprot/P35582 ^@ 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 ^@ Disordered|||Essential for DNA binding|||Fork-head|||Hepatocyte nuclear factor 3-alpha|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000091793 http://togogenome.org/gene/10090:Vapb ^@ http://purl.uniprot.org/uniprot/Q8BH80 ^@ Coiled-Coil|||Domain Extent|||Region|||Transmembrane ^@ Coiled-Coil|||Domain Extent|||Transmembrane ^@ Helical|||MSP ^@ http://togogenome.org/gene/10090:Ndufb2 ^@ http://purl.uniprot.org/uniprot/Q9CPU2 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Region|||Strand|||Transit Peptide|||Turn ^@ Disordered|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000020043 http://togogenome.org/gene/10090:Vmn1r57 ^@ http://purl.uniprot.org/uniprot/K7N731 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc41a3 ^@ http://purl.uniprot.org/uniprot/G3X937|||http://purl.uniprot.org/uniprot/Q921R8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||SLC41A/MgtE integral membrane|||Solute carrier family 41 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000295593|||http://purl.uniprot.org/annotation/VSP_026939 http://togogenome.org/gene/10090:Tex36 ^@ http://purl.uniprot.org/uniprot/Q9D5N9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Domain of unknown function with conserved HDNR motif ^@ http://togogenome.org/gene/10090:Catsper3 ^@ http://purl.uniprot.org/uniprot/E0Z0E0|||http://purl.uniprot.org/uniprot/E0Z0E1|||http://purl.uniprot.org/uniprot/Q80W99 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Helix|||INTRAMEM|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cation channel sperm-associated protein 3|||Cytoplasmic|||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.|||Ion transport ^@ http://purl.uniprot.org/annotation/PRO_0000295680|||http://purl.uniprot.org/annotation/VSP_026978 http://togogenome.org/gene/10090:Mcpt2 ^@ http://purl.uniprot.org/uniprot/P15119|||http://purl.uniprot.org/uniprot/Q541U2 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Mast cell protease 2|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027451|||http://purl.uniprot.org/annotation/PRO_0000027452|||http://purl.uniprot.org/annotation/PRO_5014309546 http://togogenome.org/gene/10090:Gtpbp2 ^@ http://purl.uniprot.org/uniprot/Q3UJK4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||GTP-binding protein 2|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000248501 http://togogenome.org/gene/10090:Emc2 ^@ http://purl.uniprot.org/uniprot/Q6A0D1|||http://purl.uniprot.org/uniprot/Q9CRD2 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat ^@ Chain|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Repeat ^@ ER membrane protein complex subunit 2|||N-acetylalanine|||N6-acetyllysine|||Removed|||TPR|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000106354 http://togogenome.org/gene/10090:Or4c1 ^@ http://purl.uniprot.org/uniprot/Q7TQZ8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:BC035044 ^@ http://purl.uniprot.org/uniprot/E0CXF8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Sytl2 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPX2|||http://purl.uniprot.org/uniprot/Q69ZF4|||http://purl.uniprot.org/uniprot/Q7TMU6|||http://purl.uniprot.org/uniprot/Q99N50 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||C2|||C2 1|||C2 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 11.|||In isoform 5, isoform 8 and isoform 11.|||In isoform 6 and isoform 8.|||In isoform 7.|||Loss of membrane localization; when associated with Q-698; Q-699; Q-700 and Q-705.|||Loss of membrane localization; when associated with Q-698; Q-699; Q-700 and Q-706.|||Loss of membrane localization; when associated with Q-698; Q-699; Q-705 and Q-706.|||Loss of membrane localization; when associated with Q-698; Q-700; Q-705 and Q-706.|||Loss of membrane localization; when associated with Q-699; Q-700; Q-705 and Q-706.|||Polar residues|||RabBD|||Synaptotagmin-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000190214|||http://purl.uniprot.org/annotation/VSP_007889|||http://purl.uniprot.org/annotation/VSP_007890|||http://purl.uniprot.org/annotation/VSP_007891|||http://purl.uniprot.org/annotation/VSP_007892|||http://purl.uniprot.org/annotation/VSP_007893|||http://purl.uniprot.org/annotation/VSP_007894 http://togogenome.org/gene/10090:Ptprm ^@ http://purl.uniprot.org/uniprot/P28828|||http://purl.uniprot.org/uniprot/Q68FM4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||MAM|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Receptor-type tyrosine-protein phosphatase mu|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2|||protein-tyrosine-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000025449|||http://purl.uniprot.org/annotation/PRO_5015098147 http://togogenome.org/gene/10090:Tg ^@ http://purl.uniprot.org/uniprot/O08710 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ Cholinesterase-like (ChEL)|||Diiodotyrosine|||Diiodotyrosine; alternate|||Disordered|||Impairs secretion.|||In cog; impairs secretion due to ER retention.|||Iodotyrosine|||Iodotyrosine; alternate|||N-linked (GlcNAc...) asparagine|||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_0000008637 http://togogenome.org/gene/10090:Alppl2 ^@ http://purl.uniprot.org/uniprot/P24823|||http://purl.uniprot.org/uniprot/Q7TPW4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Alkaline phosphatase|||Alkaline phosphatase, germ cell type|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Phosphoserine intermediate|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000024045|||http://purl.uniprot.org/annotation/PRO_0000024046|||http://purl.uniprot.org/annotation/PRO_5004291769 http://togogenome.org/gene/10090:Rhou ^@ http://purl.uniprot.org/uniprot/Q9EQT3 ^@ Binding Site|||Chain|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Region ^@ Disordered|||Rho-related GTP-binding protein RhoU|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000326436 http://togogenome.org/gene/10090:Fermt3 ^@ http://purl.uniprot.org/uniprot/Q3TEE6|||http://purl.uniprot.org/uniprot/Q8K1B8 ^@ 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|||Strand|||Turn ^@ FERM|||Fermitin family homolog 3|||Impairs ability to activate integrins.|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000219455 http://togogenome.org/gene/10090:Psmc4 ^@ http://purl.uniprot.org/uniprot/P54775 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand ^@ 26S proteasome regulatory subunit 6B|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000084687 http://togogenome.org/gene/10090:Cd79b ^@ http://purl.uniprot.org/uniprot/P15530 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ B-cell antigen receptor complex-associated protein beta chain|||Cytoplasmic|||Extracellular|||Helical|||ITAM|||Ig-like V-type|||Interchain (with C-113 in alpha chain)|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC-type Tyr-kinases ^@ http://purl.uniprot.org/annotation/PRO_0000014561 http://togogenome.org/gene/10090:Plppr2 ^@ http://purl.uniprot.org/uniprot/Q8VCY8 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phospholipid phosphatase-related protein type 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000317539|||http://purl.uniprot.org/annotation/VSP_031012 http://togogenome.org/gene/10090:Map4k3 ^@ http://purl.uniprot.org/uniprot/A0A3Q4EGQ9|||http://purl.uniprot.org/uniprot/Q8BV99|||http://purl.uniprot.org/uniprot/Q99JP0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||CNH|||Disordered|||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_0000086278 http://togogenome.org/gene/10090:Tmem95 ^@ http://purl.uniprot.org/uniprot/P0DJF3 ^@ 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|||Sperm-egg fusion protein TMEM95 ^@ http://purl.uniprot.org/annotation/PRO_0000416121 http://togogenome.org/gene/10090:Has1 ^@ http://purl.uniprot.org/uniprot/Q3UUP6|||http://purl.uniprot.org/uniprot/Q61647 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Topological Domain|||Transmembrane ^@ 75% decrease of both activities.|||85%-90% decrease of both activities.|||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|||Loss of HA activity.|||Loss of both activities.|||N-linked (GlcNAc...) asparagine|||No effect. ^@ http://purl.uniprot.org/annotation/PRO_0000197170 http://togogenome.org/gene/10090:Brap ^@ http://purl.uniprot.org/uniprot/Q99MP8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||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|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ BRCA1-associated protein|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||RING-type|||UBP-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000055826|||http://purl.uniprot.org/annotation/VSP_050761|||http://purl.uniprot.org/annotation/VSP_050762 http://togogenome.org/gene/10090:Th ^@ http://purl.uniprot.org/uniprot/P24529 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Site ^@ Disordered|||Important for substrate specificity|||Phosphoserine|||Phosphoserine; by CaMK2 and PKA|||Tyrosine 3-monooxygenase ^@ http://purl.uniprot.org/annotation/PRO_0000205562 http://togogenome.org/gene/10090:Wdpcp ^@ http://purl.uniprot.org/uniprot/B1ATJ7|||http://purl.uniprot.org/uniprot/Q8C456 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Acidic residues|||Disordered|||In isoform 2.|||WD 1|||WD 2|||WD repeat-containing and planar cell polarity effector protein fritz homolog ^@ http://purl.uniprot.org/annotation/PRO_0000325803|||http://purl.uniprot.org/annotation/VSP_032411 http://togogenome.org/gene/10090:Csta2 ^@ http://purl.uniprot.org/uniprot/Q9D8D6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Cystatin ^@ http://togogenome.org/gene/10090:Ccng1 ^@ http://purl.uniprot.org/uniprot/P51945|||http://purl.uniprot.org/uniprot/Q5D0F7|||http://purl.uniprot.org/uniprot/Q5NC86 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict ^@ Cyclin-G1|||Cyclin-like ^@ http://purl.uniprot.org/annotation/PRO_0000080466 http://togogenome.org/gene/10090:Acot10 ^@ http://purl.uniprot.org/uniprot/Q32MW3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide ^@ Acyl-coenzyme A thioesterase 10, mitochondrial|||HotDog ACOT-type 1|||HotDog ACOT-type 2|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000306248 http://togogenome.org/gene/10090:Afg1l ^@ http://purl.uniprot.org/uniprot/Q3V384 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ AFG1-like ATPase ^@ http://purl.uniprot.org/annotation/PRO_0000279522 http://togogenome.org/gene/10090:Tti1 ^@ http://purl.uniprot.org/uniprot/Q91V83 ^@ 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|||Phosphoserine; by CK2|||TELO2-interacting protein 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000050752 http://togogenome.org/gene/10090:Or4c58 ^@ http://purl.uniprot.org/uniprot/Q8VGN4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dedd2 ^@ http://purl.uniprot.org/uniprot/Q8QZV0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Bipartite nuclear localization signal|||DED|||DNA-binding death effector domain-containing protein 2|||Disordered|||Nuclear localization signal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000191278 http://togogenome.org/gene/10090:Havcr1 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ86|||http://purl.uniprot.org/uniprot/Q3V033|||http://purl.uniprot.org/uniprot/Q5QNS5 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hepatitis A virus cellular receptor 1 homolog|||Ig-like|||Ig-like V-type|||In isoform 2.|||In strain: HBA.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000014982|||http://purl.uniprot.org/annotation/PRO_5015032373|||http://purl.uniprot.org/annotation/PRO_5015097520|||http://purl.uniprot.org/annotation/VSP_015224 http://togogenome.org/gene/10090:Slc25a44 ^@ http://purl.uniprot.org/uniprot/Q3TMC4|||http://purl.uniprot.org/uniprot/Q3TNN4|||http://purl.uniprot.org/uniprot/Q8BGF9 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Region|||Repeat|||Transmembrane ^@ Disordered|||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_0000253065 http://togogenome.org/gene/10090:Hmgxb4 ^@ http://purl.uniprot.org/uniprot/Q80Y32|||http://purl.uniprot.org/uniprot/Q8BTT5 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||HMG box ^@ http://togogenome.org/gene/10090:Or8k37 ^@ http://purl.uniprot.org/uniprot/A0A1L1STZ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dok1 ^@ http://purl.uniprot.org/uniprot/P97465|||http://purl.uniprot.org/uniprot/Q3UWF9 ^@ 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 ^@ Disordered|||Docking protein 1|||IRS-type PTB|||N-acetylmethionine|||PH|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by INSR|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000187269 http://togogenome.org/gene/10090:Zfp458 ^@ http://purl.uniprot.org/uniprot/Q6P5C7 ^@ 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 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; degenerate|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 728 ^@ http://purl.uniprot.org/annotation/PRO_0000421024 http://togogenome.org/gene/10090:Hc ^@ http://purl.uniprot.org/uniprot/P06684 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Signal Peptide|||Strand ^@ Anaphylatoxin-like|||C5a anaphylatoxin|||Complement C5 alpha chain|||Complement C5 alpha' chain|||Complement C5 beta chain|||Involved in C5AR1 binding|||N-linked (GlcNAc...) asparagine|||NTR ^@ http://purl.uniprot.org/annotation/PRO_0000005991|||http://purl.uniprot.org/annotation/PRO_0000005992|||http://purl.uniprot.org/annotation/PRO_0000005993|||http://purl.uniprot.org/annotation/PRO_0000005994|||http://purl.uniprot.org/annotation/PRO_0000005995 http://togogenome.org/gene/10090:Stxbp1 ^@ http://purl.uniprot.org/uniprot/O08599 ^@ 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 ^@ Enhances binding to SNARE complex component STX1A promoting formation of the SNARE complex and thereby increasing release of neurotransmitters from neurons and thus synaptic transmission.|||In isoform 2.|||In strain: DBA/2J.|||Phosphoserine|||Syntaxin-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000206278|||http://purl.uniprot.org/annotation/VSP_010496 http://togogenome.org/gene/10090:Ccl7 ^@ http://purl.uniprot.org/uniprot/A9Z1Z1|||http://purl.uniprot.org/uniprot/Q03366 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ C-C motif chemokine|||C-C motif chemokine 7|||Chemokine interleukin-8-like|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000005184|||http://purl.uniprot.org/annotation/PRO_5014205202 http://togogenome.org/gene/10090:Relch ^@ http://purl.uniprot.org/uniprot/A0A087WSS1|||http://purl.uniprot.org/uniprot/E9QM90|||http://purl.uniprot.org/uniprot/G3X9J4|||http://purl.uniprot.org/uniprot/Q148V7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||HEAT|||HEAT 1|||HEAT 2|||HEAT 3|||In isoform 2.|||In isoform 3.|||Interaction with RAB11A and RAB11B|||LisH|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RAB11-binding protein RELCH|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000313094|||http://purl.uniprot.org/annotation/VSP_030018|||http://purl.uniprot.org/annotation/VSP_030019|||http://purl.uniprot.org/annotation/VSP_030020|||http://purl.uniprot.org/annotation/VSP_030021 http://togogenome.org/gene/10090:Gskip ^@ http://purl.uniprot.org/uniprot/Q3TBR1|||http://purl.uniprot.org/uniprot/Q8BGR8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ GSK3B-interacting protein|||GSKIP|||In isoform 2.|||Interaction with GSK3B and acts as GSK3B inhibitor|||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_0000220952|||http://purl.uniprot.org/annotation/VSP_008199 http://togogenome.org/gene/10090:Fancm ^@ http://purl.uniprot.org/uniprot/Q8BGE5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Basic and acidic residues|||DEAH box|||Disordered|||Fanconi anemia group M protein homolog|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with FAAP24|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000055177|||http://purl.uniprot.org/annotation/VSP_015991|||http://purl.uniprot.org/annotation/VSP_015992|||http://purl.uniprot.org/annotation/VSP_015993|||http://purl.uniprot.org/annotation/VSP_015994|||http://purl.uniprot.org/annotation/VSP_015995 http://togogenome.org/gene/10090:Nme1 ^@ http://purl.uniprot.org/uniprot/P15532|||http://purl.uniprot.org/uniprot/Q5NC81 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N6-acetyllysine|||Nucleoside diphosphate kinase A|||Nucleoside diphosphate kinase-like|||Phosphoserine|||Pros-phosphohistidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000137115 http://togogenome.org/gene/10090:Btnl4 ^@ http://purl.uniprot.org/uniprot/A2CG29 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ B30.2/SPRY|||Disordered|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015086059 http://togogenome.org/gene/10090:Purb ^@ http://purl.uniprot.org/uniprot/O35295 ^@ 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_0000225616 http://togogenome.org/gene/10090:Triqk ^@ http://purl.uniprot.org/uniprot/B2B9E1 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Triple QxxK/R motif-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000398147 http://togogenome.org/gene/10090:Ccna1 ^@ http://purl.uniprot.org/uniprot/Q61456 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Cyclin-A1|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000080334 http://togogenome.org/gene/10090:Plppr4 ^@ http://purl.uniprot.org/uniprot/Q7TME0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Loss of function in LPA import into cell.|||Loss of function in regulation of glutamatergic synaptic transmission.|||N-linked (GlcNAc...) asparagine|||No effect on localization. Decreased O-glycosylation. Loss of function in LPA internalization into cells. Loss of function in regulation of glutamatergic synaptic transmission.|||Phospholipid phosphatase-related protein type 4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317437 http://togogenome.org/gene/10090:Ceacam11 ^@ http://purl.uniprot.org/uniprot/Q4KL40|||http://purl.uniprot.org/uniprot/Q9D0Z8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Immunoglobulin V-set ^@ http://togogenome.org/gene/10090:Exosc9 ^@ http://purl.uniprot.org/uniprot/Q9JHI7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Acidic residues|||Disordered|||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); alternate|||N6-acetyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000139972 http://togogenome.org/gene/10090:Marchf4 ^@ http://purl.uniprot.org/uniprot/Q80TE3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||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_0000055931 http://togogenome.org/gene/10090:Zic2 ^@ http://purl.uniprot.org/uniprot/F8VPV3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Vmn2r62 ^@ http://purl.uniprot.org/uniprot/K7N712 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908823 http://togogenome.org/gene/10090:Cpne4 ^@ http://purl.uniprot.org/uniprot/Q8BLR2 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ C2 1|||C2 2|||Copine-4|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000144842 http://togogenome.org/gene/10090:Cxcr2 ^@ http://purl.uniprot.org/uniprot/P35343 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ C-X-C chemokine receptor type 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_0000069339 http://togogenome.org/gene/10090:Lactbl1 ^@ http://purl.uniprot.org/uniprot/S4R213 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Beta-lactamase-related|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Nalf2 ^@ http://purl.uniprot.org/uniprot/A2BDP1 ^@ 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|||NALCN channel auxiliary factor 2|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000339376 http://togogenome.org/gene/10090:Vmn2r93 ^@ http://purl.uniprot.org/uniprot/L7N1Z9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982281 http://togogenome.org/gene/10090:Adam1b ^@ http://purl.uniprot.org/uniprot/Q8R534 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Acidic residues|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 1b|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000029034|||http://purl.uniprot.org/annotation/PRO_0000029035 http://togogenome.org/gene/10090:Smim17 ^@ http://purl.uniprot.org/uniprot/A0A504 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Adamts17 ^@ http://purl.uniprot.org/uniprot/E9Q4D1|||http://purl.uniprot.org/uniprot/Q3V310 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ PLAC|||Peptidase M12B|||Peptidase M12B domain-containing protein|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_5003244414|||http://purl.uniprot.org/annotation/PRO_5004230532 http://togogenome.org/gene/10090:Btg1 ^@ http://purl.uniprot.org/uniprot/P62325|||http://purl.uniprot.org/uniprot/Q3UEG0 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Anti-proliferative protein|||Phosphoserine|||Protein BTG1 ^@ http://purl.uniprot.org/annotation/PRO_0000143801 http://togogenome.org/gene/10090:Ark2n ^@ http://purl.uniprot.org/uniprot/Q0VAW6|||http://purl.uniprot.org/uniprot/Q8BH50 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||Disordered|||E3 ubiquitin-protein ligase Arkadia N-terminal|||In isoform 2.|||Increased phosphorylation. Increases muscle specific force.|||Loss of phosphorylation by AMPK. Decreases muscle specific force.|||Phosphoserine|||Phosphoserine; by AMPK|||Polar residues|||Protein ARK2N|||Required for interaction with CSNK2B ^@ http://purl.uniprot.org/annotation/PRO_0000079313|||http://purl.uniprot.org/annotation/VSP_014754|||http://purl.uniprot.org/annotation/VSP_014755 http://togogenome.org/gene/10090:Syn2 ^@ http://purl.uniprot.org/uniprot/Q64332|||http://purl.uniprot.org/uniprot/Q8CE19 ^@ 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 ^@ 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_0000183022|||http://purl.uniprot.org/annotation/VSP_015203|||http://purl.uniprot.org/annotation/VSP_015204 http://togogenome.org/gene/10090:Tmc3 ^@ http://purl.uniprot.org/uniprot/E9Q6Y0|||http://purl.uniprot.org/uniprot/F8VQI4|||http://purl.uniprot.org/uniprot/Q7TQ69 ^@ 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|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||TMC|||Transmembrane channel-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000259603|||http://purl.uniprot.org/annotation/VSP_052203|||http://purl.uniprot.org/annotation/VSP_052204 http://togogenome.org/gene/10090:Trmt2b ^@ http://purl.uniprot.org/uniprot/Q8BQJ6 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||Nucleophile|||Proton acceptor|||tRNA (uracil-5-)-methyltransferase homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000311933 http://togogenome.org/gene/10090:Heatr5b ^@ http://purl.uniprot.org/uniprot/Q8C547 ^@ 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 1|||HEAT 2|||HEAT 3|||HEAT repeat-containing protein 5B|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000311995|||http://purl.uniprot.org/annotation/VSP_029693|||http://purl.uniprot.org/annotation/VSP_029694|||http://purl.uniprot.org/annotation/VSP_029695|||http://purl.uniprot.org/annotation/VSP_029696 http://togogenome.org/gene/10090:Ehbp1l1 ^@ http://purl.uniprot.org/uniprot/A0A494B9G7|||http://purl.uniprot.org/uniprot/A0A494BA91|||http://purl.uniprot.org/uniprot/E9QP49|||http://purl.uniprot.org/uniprot/G5E8Y6|||http://purl.uniprot.org/uniprot/Q99MS7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ BMERB|||Basic and acidic residues|||C2 NT-type|||CAAX motif|||Calponin-homology (CH)|||Disordered|||EH domain-binding protein 1-like protein 1|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4 and isoform 5.|||In isoform 5.|||Interaction with BIN1 and AMPH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||bMERB ^@ http://purl.uniprot.org/annotation/PRO_0000285205|||http://purl.uniprot.org/annotation/VSP_024837|||http://purl.uniprot.org/annotation/VSP_024838|||http://purl.uniprot.org/annotation/VSP_024839|||http://purl.uniprot.org/annotation/VSP_024840 http://togogenome.org/gene/10090:Kcnj2 ^@ http://purl.uniprot.org/uniprot/P35561|||http://purl.uniprot.org/uniprot/Q543W5 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Helix|||INTRAMEM|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Inward rectifier potassium channel 2|||Inward rectifier potassium channel C-terminal|||N-myristoyl glycine|||PDZ-binding|||Pore-forming|||Potassium channel inwardly rectifying Kir N-terminal|||Potassium channel inwardly rectifying transmembrane|||Removed|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||S-nitrosocysteine|||Selectivity filter|||The mutant protein is able to coassemble and traffic to the cell membrane. ^@ http://purl.uniprot.org/annotation/PRO_0000154925 http://togogenome.org/gene/10090:Tbc1d4 ^@ http://purl.uniprot.org/uniprot/E0CX53|||http://purl.uniprot.org/uniprot/E9Q6Q8|||http://purl.uniprot.org/uniprot/Q8BYJ6 ^@ 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 and isoform 4.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||PID|||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_0000208027|||http://purl.uniprot.org/annotation/VSP_013891|||http://purl.uniprot.org/annotation/VSP_036872|||http://purl.uniprot.org/annotation/VSP_036873|||http://purl.uniprot.org/annotation/VSP_036874|||http://purl.uniprot.org/annotation/VSP_036875|||http://purl.uniprot.org/annotation/VSP_036876|||http://purl.uniprot.org/annotation/VSP_036877|||http://purl.uniprot.org/annotation/VSP_036878 http://togogenome.org/gene/10090:Atp13a4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0M2|||http://purl.uniprot.org/uniprot/E9QPP7|||http://purl.uniprot.org/uniprot/Q5XF90|||http://purl.uniprot.org/uniprot/S4R234 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||Probable cation-transporting ATPase 13A4 ^@ http://purl.uniprot.org/annotation/PRO_0000318676|||http://purl.uniprot.org/annotation/VSP_031262|||http://purl.uniprot.org/annotation/VSP_031263|||http://purl.uniprot.org/annotation/VSP_031264|||http://purl.uniprot.org/annotation/VSP_031265 http://togogenome.org/gene/10090:Nprl2 ^@ http://purl.uniprot.org/uniprot/Q9WUE4 ^@ Binding Site|||Chain|||Crosslink|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Region|||Site ^@ Arginine finger|||GATOR1 complex protein NPRL2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with PDPK1 ^@ http://purl.uniprot.org/annotation/PRO_0000213320 http://togogenome.org/gene/10090:Lamp3 ^@ http://purl.uniprot.org/uniprot/Q7TST5|||http://purl.uniprot.org/uniprot/Q8BZW9 ^@ 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|||Helical|||Lumenal|||Lysosome-associated membrane glycoprotein 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000223697|||http://purl.uniprot.org/annotation/PRO_5004304283 http://togogenome.org/gene/10090:Kdm1a ^@ http://purl.uniprot.org/uniprot/A3KG93|||http://purl.uniprot.org/uniprot/Q6ZQ88 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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)|||Lysine-specific histone demethylase 1A|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||SWIRM ^@ http://purl.uniprot.org/annotation/PRO_0000099882 http://togogenome.org/gene/10090:Fndc3b ^@ http://purl.uniprot.org/uniprot/A0A0R4J0H8|||http://purl.uniprot.org/uniprot/Q6NWW9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Fibronectin type III domain-containing protein 3B|||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|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000284892 http://togogenome.org/gene/10090:Psg18 ^@ http://purl.uniprot.org/uniprot/B2RSG7|||http://purl.uniprot.org/uniprot/E9Q8L0|||http://purl.uniprot.org/uniprot/Q3TIY4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like|||Immunoglobulin subtype ^@ http://togogenome.org/gene/10090:Rtn3 ^@ http://purl.uniprot.org/uniprot/Q9ES97 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with BACE1|||Interaction with FADD|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Reticulon|||Reticulon-3 ^@ http://purl.uniprot.org/annotation/PRO_0000168164|||http://purl.uniprot.org/annotation/VSP_023762|||http://purl.uniprot.org/annotation/VSP_023763|||http://purl.uniprot.org/annotation/VSP_023764|||http://purl.uniprot.org/annotation/VSP_023765 http://togogenome.org/gene/10090:Pex16 ^@ http://purl.uniprot.org/uniprot/Q91XC9 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Interaction with PEX19|||Peroxisomal|||Peroxisomal membrane protein PEX16|||Required for peroxisomal location ^@ http://purl.uniprot.org/annotation/PRO_0000366961 http://togogenome.org/gene/10090:Zar1l ^@ http://purl.uniprot.org/uniprot/C3VD30 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Zinc Finger ^@ 3CxxC-type|||Basic and acidic residues|||Disordered|||Polar residues|||Protein ZAR1-like ^@ http://purl.uniprot.org/annotation/PRO_0000457518 http://togogenome.org/gene/10090:Cep128 ^@ http://purl.uniprot.org/uniprot/B7ZNX8|||http://purl.uniprot.org/uniprot/Q8BI22 ^@ 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|||Centrosomal protein of 128 kDa|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089947|||http://purl.uniprot.org/annotation/VSP_030197|||http://purl.uniprot.org/annotation/VSP_030198 http://togogenome.org/gene/10090:Chst14 ^@ http://purl.uniprot.org/uniprot/Q80V53 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 14|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000189673 http://togogenome.org/gene/10090:Frg2f1 ^@ http://purl.uniprot.org/uniprot/Q6P3A2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Setx ^@ http://purl.uniprot.org/uniprot/A2AKX3 ^@ 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|||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 isoform 2.|||Necessary for nuclear localization|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable helicase senataxin ^@ http://purl.uniprot.org/annotation/PRO_0000307777|||http://purl.uniprot.org/annotation/VSP_028827 http://togogenome.org/gene/10090:Cenpx ^@ http://purl.uniprot.org/uniprot/Q8C4X1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Centromere protein X|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000337181|||http://purl.uniprot.org/annotation/VSP_033950|||http://purl.uniprot.org/annotation/VSP_033951|||http://purl.uniprot.org/annotation/VSP_033952 http://togogenome.org/gene/10090:Pou3f3 ^@ http://purl.uniprot.org/uniprot/P31361 ^@ 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 3|||POU-specific|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000100728 http://togogenome.org/gene/10090:Scd2 ^@ http://purl.uniprot.org/uniprot/P13011 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Lumenal|||Polar residues|||Stearoyl-CoA desaturase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000185398 http://togogenome.org/gene/10090:Nosip ^@ http://purl.uniprot.org/uniprot/Q9D6T0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Nitric oxide synthase-interacting protein|||Nuclear localization signal|||Phosphoserine|||U-box-like ^@ http://purl.uniprot.org/annotation/PRO_0000280587|||http://purl.uniprot.org/annotation/VSP_023795 http://togogenome.org/gene/10090:Csde1 ^@ http://purl.uniprot.org/uniprot/A0A0G2JF72|||http://purl.uniprot.org/uniprot/Q3U1S6|||http://purl.uniprot.org/uniprot/Q8JZN2|||http://purl.uniprot.org/uniprot/Q91W50 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue ^@ CSD|||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)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||SUZ-C ^@ http://purl.uniprot.org/annotation/PRO_0000100349 http://togogenome.org/gene/10090:Eif1ad19 ^@ http://purl.uniprot.org/uniprot/F6YNI8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||S1-like ^@ http://togogenome.org/gene/10090:Gper1 ^@ http://purl.uniprot.org/uniprot/Q8BMP4 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||G-protein coupled estrogen receptor 1|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Loss of interaction with DLG4.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069311 http://togogenome.org/gene/10090:Midn ^@ http://purl.uniprot.org/uniprot/Q3TPJ7 ^@ 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 and isoform 3.|||In isoform 3.|||Midnolin|||Polar residues|||Required for nucleolar localization|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000287537|||http://purl.uniprot.org/annotation/VSP_025552|||http://purl.uniprot.org/annotation/VSP_025553 http://togogenome.org/gene/10090:Ucp1 ^@ http://purl.uniprot.org/uniprot/P12242 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Repeat|||Topological Domain|||Transmembrane ^@ Cysteine sulfenic acid (-SOH)|||Decreased UCP1 activity in thermogenic respiration.|||Decreased sensitivity to activation by noradrenaline in thermogenic respiration.|||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|||No effect on UCP1 activity in thermogenic respiration.|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090659 http://togogenome.org/gene/10090:Nucks1 ^@ http://purl.uniprot.org/uniprot/A0A087WRY3|||http://purl.uniprot.org/uniprot/Q80XU3 ^@ 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|||Basic and acidic residues|||Basic residues|||Disordered|||Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000057979 http://togogenome.org/gene/10090:Cyld ^@ http://purl.uniprot.org/uniprot/A0A1B0GSE5|||http://purl.uniprot.org/uniprot/Q80TQ2 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ B-box|||CAP-Gly|||CAP-Gly 1|||CAP-Gly 2|||CAP-Gly 3|||Decreased inhibition of NF-kappa-B.|||Disordered|||In isoform 1.|||In isoform 3.|||Increased inhibition of NF-kappa-B.|||Interaction with IKBKG/NEMO|||Interaction with TRAF2|||Interaction with TRIP|||Loss of deubiquitinating activity.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase CYLD ^@ http://purl.uniprot.org/annotation/PRO_0000080699|||http://purl.uniprot.org/annotation/VSP_011278|||http://purl.uniprot.org/annotation/VSP_011279|||http://purl.uniprot.org/annotation/VSP_011280 http://togogenome.org/gene/10090:Patz1 ^@ http://purl.uniprot.org/uniprot/Q5NBZ1|||http://purl.uniprot.org/uniprot/Q80XS2|||http://purl.uniprot.org/uniprot/Q9JMG9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BTB|||C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Lexm ^@ http://purl.uniprot.org/uniprot/A2AVQ5 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Ciliary microtubule-associated protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000297586 http://togogenome.org/gene/10090:Abhd17a ^@ http://purl.uniprot.org/uniprot/Q99JW1 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Modified Residue|||Region|||Splice Variant ^@ Alpha/beta hydrolase domain-containing protein 17A|||Charge relay system|||Disordered|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000297510|||http://purl.uniprot.org/annotation/VSP_027272 http://togogenome.org/gene/10090:Vcl ^@ http://purl.uniprot.org/uniprot/Q64727 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ 1|||2|||3|||3 X 112 AA tandem repeats|||C-terminal tail|||Disordered|||Facilitates phospholipid membrane insertion|||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_0000064253 http://togogenome.org/gene/10090:Or10ag53 ^@ http://purl.uniprot.org/uniprot/Q7TR53 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Col4a2 ^@ http://purl.uniprot.org/uniprot/B2RQQ8|||http://purl.uniprot.org/uniprot/P08122 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ 3'-bromotyrosine|||Basic and acidic residues|||Canstatin|||Collagen IV NC1|||Collagen alpha-2(IV) chain|||Disordered|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide (7S domain)|||Pro residues|||Triple-helical region ^@ http://purl.uniprot.org/annotation/PRO_0000005826|||http://purl.uniprot.org/annotation/PRO_0000005827|||http://purl.uniprot.org/annotation/PRO_0000390487|||http://purl.uniprot.org/annotation/PRO_5014298362 http://togogenome.org/gene/10090:Cdk10 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLN0|||http://purl.uniprot.org/uniprot/Q0VH02|||http://purl.uniprot.org/uniprot/Q3UMM4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Cyclin-dependent kinase 10|||Disordered|||Phosphothreonine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000261028 http://togogenome.org/gene/10090:Lce6a ^@ http://purl.uniprot.org/uniprot/D3YV94 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Gja5 ^@ http://purl.uniprot.org/uniprot/A0A654ICB8|||http://purl.uniprot.org/uniprot/Q01231 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction alpha-5 protein|||Gap junction protein cysteine-rich|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000057820 http://togogenome.org/gene/10090:Cep19 ^@ http://purl.uniprot.org/uniprot/Q9CQA8 ^@ Chain|||Molecule Processing ^@ Chain ^@ Centrosomal protein of 19 kDa ^@ http://purl.uniprot.org/annotation/PRO_0000251961 http://togogenome.org/gene/10090:Ube2l3 ^@ http://purl.uniprot.org/uniprot/P68037|||http://purl.uniprot.org/uniprot/Q561N4 ^@ 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 ^@ Glycyl thioester intermediate|||N6-acetyllysine|||UBC core|||Ubiquitin-conjugating enzyme E2 L3 ^@ http://purl.uniprot.org/annotation/PRO_0000082477 http://togogenome.org/gene/10090:Spata25 ^@ http://purl.uniprot.org/uniprot/Q9DA57 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Spermatogenesis-associated protein 25 ^@ http://purl.uniprot.org/annotation/PRO_0000079479 http://togogenome.org/gene/10090:Htr2b ^@ http://purl.uniprot.org/uniprot/Q02152 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Motif|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ 5-hydroxytryptamine receptor 2B|||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|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling|||PDZ-binding|||S-palmitoyl cysteine|||[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family members ^@ http://purl.uniprot.org/annotation/PRO_0000068954 http://togogenome.org/gene/10090:Lnx1 ^@ http://purl.uniprot.org/uniprot/A4QPD4|||http://purl.uniprot.org/uniprot/E9Q4N3|||http://purl.uniprot.org/uniprot/E9Q6Q0|||http://purl.uniprot.org/uniprot/O70263|||http://purl.uniprot.org/uniprot/Q3UUJ9 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Zinc Finger ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Zinc Finger ^@ Abolishes binding to NUMB protein.|||Disordered|||E3 ubiquitin-protein ligase LNX|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with MAGEB18|||Loss of function.|||NPXY motif|||No effect on binding to NUMB protein.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ domain-containing protein|||Phosphoserine|||RING-type|||Slightly affects binding to NUMB protein. ^@ http://purl.uniprot.org/annotation/PRO_0000055914|||http://purl.uniprot.org/annotation/PRO_5012249044|||http://purl.uniprot.org/annotation/PRO_5012655420|||http://purl.uniprot.org/annotation/PRO_5014296943|||http://purl.uniprot.org/annotation/VSP_005734|||http://purl.uniprot.org/annotation/VSP_012588|||http://purl.uniprot.org/annotation/VSP_012589 http://togogenome.org/gene/10090:Bglap3 ^@ http://purl.uniprot.org/uniprot/P54615 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ 4-carboxyglutamate|||Gla|||Osteocalcin-related protein ^@ http://purl.uniprot.org/annotation/PRO_0000011090|||http://purl.uniprot.org/annotation/PRO_0000011091 http://togogenome.org/gene/10090:Tmem69 ^@ http://purl.uniprot.org/uniprot/Q3KQJ0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 69 ^@ http://purl.uniprot.org/annotation/PRO_0000282851 http://togogenome.org/gene/10090:Milr1 ^@ http://purl.uniprot.org/uniprot/A0A140T8Q6|||http://purl.uniprot.org/uniprot/B7ZP19|||http://purl.uniprot.org/uniprot/Q3TB92 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes interaction with PTPN6 and PTPN11. Loss of function; when associated with F-216.|||Abolishes interaction with PTPN6 and PTPN11. Loss of function; when associated with F-241.|||Allergin-1|||Cytoplasmic|||Extracellular|||Helical|||ITIM motif|||Ig-like|||Ig-like C2-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000307365|||http://purl.uniprot.org/annotation/PRO_5007305376|||http://purl.uniprot.org/annotation/PRO_5015087446|||http://purl.uniprot.org/annotation/VSP_028742 http://togogenome.org/gene/10090:Gm7102 ^@ http://purl.uniprot.org/uniprot/J3QQ10|||http://purl.uniprot.org/uniprot/Q3TQY8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Tceal5 ^@ http://purl.uniprot.org/uniprot/Q14C38|||http://purl.uniprot.org/uniprot/Q8CCT4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Transcription elongation factor A protein-like 5 ^@ http://purl.uniprot.org/annotation/PRO_0000239212 http://togogenome.org/gene/10090:Rai2 ^@ http://purl.uniprot.org/uniprot/Q6P8M4|||http://purl.uniprot.org/uniprot/Q9QVY8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Retinoic acid-induced protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000097162 http://togogenome.org/gene/10090:Vps13c ^@ http://purl.uniprot.org/uniprot/A1ILG8|||http://purl.uniprot.org/uniprot/Q8BX70 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Atg2/VPS13 C-terminal|||Chorein N-terminal|||FFAT|||In isoform 2.|||In isoform 3.|||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|||VPS13 middle RBG modules|||Vacuolar protein sorting-associated protein 13 DH-like|||Vacuolar protein sorting-associated protein 13 VPS13 adaptor binding|||Vacuolar protein sorting-associated protein 13 extended chorein ^@ http://purl.uniprot.org/annotation/PRO_0000262950|||http://purl.uniprot.org/annotation/VSP_052246|||http://purl.uniprot.org/annotation/VSP_052247|||http://purl.uniprot.org/annotation/VSP_052248 http://togogenome.org/gene/10090:Tomm70a ^@ http://purl.uniprot.org/uniprot/Q9CZW5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000106337 http://togogenome.org/gene/10090:Dennd10 ^@ http://purl.uniprot.org/uniprot/Q3TH34|||http://purl.uniprot.org/uniprot/Q9D8N2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ DENN domain-containing protein 10|||UDENN|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000187036 http://togogenome.org/gene/10090:Pygm ^@ http://purl.uniprot.org/uniprot/Q9WUB3 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Site ^@ Glycogen phosphorylase, muscle form|||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_0000188531 http://togogenome.org/gene/10090:Eogt ^@ http://purl.uniprot.org/uniprot/Q8BYW9 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Glycosylation Site|||Motif|||Signal Peptide ^@ EGF domain-specific O-linked N-acetylglucosamine transferase|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Required for optimal activity ^@ http://purl.uniprot.org/annotation/PRO_0000301972 http://togogenome.org/gene/10090:Litaf ^@ http://purl.uniprot.org/uniprot/Q9JLJ0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region ^@ Abolishes interaction with NEDD4.|||LITAF|||Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog|||Membrane-binding amphipathic helix|||No effect on interaction with NEDD4.|||PPxY motif ^@ http://purl.uniprot.org/annotation/PRO_0000084441 http://togogenome.org/gene/10090:Fam13a ^@ http://purl.uniprot.org/uniprot/Q8BGI4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM13A ^@ http://purl.uniprot.org/annotation/PRO_0000058921 http://togogenome.org/gene/10090:Ifi207 ^@ http://purl.uniprot.org/uniprot/E9Q3L4|||http://purl.uniprot.org/uniprot/Q8BW36 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||HIN-200|||Polar residues|||Pyrin ^@ http://togogenome.org/gene/10090:Esp4 ^@ http://purl.uniprot.org/uniprot/A8R0T8 ^@ 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_5015086682 http://togogenome.org/gene/10090:C030006K11Rik ^@ http://purl.uniprot.org/uniprot/Q8VE95 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ UPF0598 protein C8orf82 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000340670 http://togogenome.org/gene/10090:Phf7 ^@ http://purl.uniprot.org/uniprot/A0A2I3BR08|||http://purl.uniprot.org/uniprot/A2RTI5|||http://purl.uniprot.org/uniprot/Q9DAG9 ^@ 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 ^@ C2HC pre-PHD-type|||Disordered|||In isoform 2.|||PHD finger protein 7|||PHD-type|||Polar residues|||RING-type|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000055997|||http://purl.uniprot.org/annotation/VSP_013491 http://togogenome.org/gene/10090:Lyst ^@ http://purl.uniprot.org/uniprot/G5E8Q0|||http://purl.uniprot.org/uniprot/P97412 ^@ 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 ^@ Acidic residues|||BEACH|||BEACH-type PH|||Basic and acidic residues|||Disordered|||In bg; macrophages and dendritic cells show impaired pro-inflammatory cytokine production in response to stimulation of TLR3 and TLR4 receptors; shows impaired inflammatory responses to lipopolysaccharides; following bacteria infections, shows defective phagosomal maturation.|||In isoform 2.|||Lysosomal-trafficking regulator|||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_0000051072|||http://purl.uniprot.org/annotation/VSP_006783|||http://purl.uniprot.org/annotation/VSP_006784 http://togogenome.org/gene/10090:Nyx ^@ http://purl.uniprot.org/uniprot/P83503 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide ^@ 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_0000032777 http://togogenome.org/gene/10090:Gas8 ^@ http://purl.uniprot.org/uniprot/Q49MD7|||http://purl.uniprot.org/uniprot/Q60779 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disordered|||Dynein regulatory complex subunit 4|||Growth arrest-specific protein 8|||Interaction with SMO|||Microtubule-binding|||Moderate decrease in cilia motility.|||Regulates microtubule-binding ^@ http://purl.uniprot.org/annotation/PRO_0000220378 http://togogenome.org/gene/10090:Eif3l ^@ http://purl.uniprot.org/uniprot/Q8QZY1 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Eukaryotic translation initiation factor 3 subunit L|||N-acetylserine|||N6-acetyllysine|||PCI|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000297498 http://togogenome.org/gene/10090:Capn15 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLS3|||http://purl.uniprot.org/uniprot/Q9JLG8 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Calpain catalytic|||Calpain-15|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||RanBP2-type|||RanBP2-type 1|||RanBP2-type 2|||RanBP2-type 3|||RanBP2-type 4|||RanBP2-type 5 ^@ http://purl.uniprot.org/annotation/PRO_0000278771|||http://purl.uniprot.org/annotation/VSP_023363|||http://purl.uniprot.org/annotation/VSP_023364|||http://purl.uniprot.org/annotation/VSP_023365 http://togogenome.org/gene/10090:Or2y1e ^@ http://purl.uniprot.org/uniprot/Q8VFA4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rrm2 ^@ http://purl.uniprot.org/uniprot/P11157 ^@ Active Site|||Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Strand|||Turn ^@ Cy|||Phosphoserine|||Phosphothreonine|||Ribonucleoside-diphosphate reductase subunit M2 ^@ http://purl.uniprot.org/annotation/PRO_0000190450 http://togogenome.org/gene/10090:Mknk2 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZX7|||http://purl.uniprot.org/uniprot/Q3TPM2|||http://purl.uniprot.org/uniprot/Q8CDB0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||Loss of activity.|||MAP kinase binding|||MAP kinase-interacting serine/threonine-protein kinase 2|||Normal MAPK3/ERK1 and MAPK1/ER2K-binding.|||Normal MAPK3/ERK1 and MAPK1/ERK2-binding.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Reduced MAPK3/ERK1 and MAPK1/ER2K-binding.|||Reduced MAPK3/ERK1 and MAPK1/ERK2-binding.|||Reduced phosphorylation. ^@ http://purl.uniprot.org/annotation/PRO_0000086337|||http://purl.uniprot.org/annotation/VSP_007355 http://togogenome.org/gene/10090:Clec3a ^@ http://purl.uniprot.org/uniprot/B2RVD1|||http://purl.uniprot.org/uniprot/Q9EPW4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ C-type lectin|||C-type lectin domain family 3 member A ^@ http://purl.uniprot.org/annotation/PRO_0000017375|||http://purl.uniprot.org/annotation/PRO_5014298313 http://togogenome.org/gene/10090:Creb3l1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J082|||http://purl.uniprot.org/uniprot/Q9Z125 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ BZIP|||Basic and acidic residues|||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|||Loss of proteolytic cleavage; when associated with L-392 and A-423.|||Loss of proteolytic cleavage; when associated with L-392 and V-426.|||Loss of proteolytic cleavage; when associated with V-423 and V-426.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Processed cyclic AMP-responsive element-binding protein 3-like protein 1|||Required for transcription activation|||S1P recognition|||S2P recognition|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000288065|||http://purl.uniprot.org/annotation/PRO_0000296207|||http://purl.uniprot.org/annotation/VSP_025633 http://togogenome.org/gene/10090:Stn1 ^@ http://purl.uniprot.org/uniprot/Q3UXU8|||http://purl.uniprot.org/uniprot/Q8K2X3 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand ^@ CST complex subunit STN1|||Impairs single-stranded DNA binding; when associated with A-151.|||Impairs single-stranded DNA binding; when associated with A-96.|||Interaction with CTC1|||OB|||Removed|||Stn1 C-terminal|||Winged helix-turn-helix (wHTH) 1|||Winged helix-turn-helix (wHTH) 2 ^@ http://purl.uniprot.org/annotation/PRO_0000058021 http://togogenome.org/gene/10090:Ubxn10 ^@ http://purl.uniprot.org/uniprot/Q8BG34 ^@ 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|||Phosphoserine|||Polar residues|||UBX|||UBX domain-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000211030 http://togogenome.org/gene/10090:Msx3 ^@ http://purl.uniprot.org/uniprot/B2RPS3|||http://purl.uniprot.org/uniprot/G3X9C7|||http://purl.uniprot.org/uniprot/P70354 ^@ 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 ^@ Disordered|||Homeobox|||Homeobox protein MSX-3|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000049104 http://togogenome.org/gene/10090:Adam25 ^@ http://purl.uniprot.org/uniprot/A0A0R4J160|||http://purl.uniprot.org/uniprot/Q9R159 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||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|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 25|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029124|||http://purl.uniprot.org/annotation/PRO_0000029125 http://togogenome.org/gene/10090:Sh3gl3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0B8|||http://purl.uniprot.org/uniprot/Q497N4|||http://purl.uniprot.org/uniprot/Q62421|||http://purl.uniprot.org/uniprot/Q9CZV7 ^@ 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 ^@ BAR|||Disordered|||Endophilin-A3|||Interaction with ARC|||Membrane-binding amphipathic helix|||Polar residues|||Required for dimerization upon membrane association|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000146751 http://togogenome.org/gene/10090:Slco6c1 ^@ http://purl.uniprot.org/uniprot/Q8C0X7 ^@ 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 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Solute carrier organic anion transporter family member 6C1 ^@ http://purl.uniprot.org/annotation/PRO_0000454937|||http://purl.uniprot.org/annotation/VSP_061423 http://togogenome.org/gene/10090:Igfbp1 ^@ http://purl.uniprot.org/uniprot/P47876 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide ^@ Cell attachment site|||IGFBP N-terminal|||Insulin-like growth factor-binding protein 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000014366 http://togogenome.org/gene/10090:Tulp1 ^@ http://purl.uniprot.org/uniprot/Q9Z273 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Tubby-related protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000186467 http://togogenome.org/gene/10090:Ccdc81 ^@ http://purl.uniprot.org/uniprot/Q9D5W4 ^@ 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 81|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288878 http://togogenome.org/gene/10090:Mettl13 ^@ http://purl.uniprot.org/uniprot/Q91YR5 ^@ 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.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||eEF1A lysine and N-terminal methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000050780|||http://purl.uniprot.org/annotation/VSP_013923|||http://purl.uniprot.org/annotation/VSP_013924|||http://purl.uniprot.org/annotation/VSP_013925|||http://purl.uniprot.org/annotation/VSP_013926 http://togogenome.org/gene/10090:Cd177 ^@ http://purl.uniprot.org/uniprot/Q8R2S8 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ CD177 antigen|||Extracellular|||Helical; Anchor for type IV membrane protein|||N-linked (GlcNAc...) asparagine|||UPAR/Ly6 1|||UPAR/Ly6 2|||UPAR/Ly6 3|||UPAR/Ly6 4 ^@ http://purl.uniprot.org/annotation/PRO_0000378449 http://togogenome.org/gene/10090:Ephb3 ^@ http://purl.uniprot.org/uniprot/P54754 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Eph LBD|||Ephrin type-B receptor 3|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000016832 http://togogenome.org/gene/10090:Yif1a ^@ http://purl.uniprot.org/uniprot/Q91XB7 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylalanine|||Phosphoserine|||Protein YIF1A|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000233276 http://togogenome.org/gene/10090:Rpl34-ps1 ^@ http://purl.uniprot.org/uniprot/Q9D1R9 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Crosslink|||Modified Residue ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL34|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000131832 http://togogenome.org/gene/10090:Dhrs9 ^@ http://purl.uniprot.org/uniprot/Q148Q4|||http://purl.uniprot.org/uniprot/Q58NB6 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Signal Peptide ^@ Dehydrogenase/reductase SDR family member 9|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000042618|||http://purl.uniprot.org/annotation/PRO_5014306919 http://togogenome.org/gene/10090:Irx3 ^@ http://purl.uniprot.org/uniprot/P81067 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox; TALE-type|||In isoform 2.|||Iroquois-class homeodomain protein IRX-3|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000049156|||http://purl.uniprot.org/annotation/VSP_038351 http://togogenome.org/gene/10090:Krt80 ^@ http://purl.uniprot.org/uniprot/Q0VBK2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type II cytoskeletal 80|||Linker 1|||Linker 12|||Phosphoserine|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000314897 http://togogenome.org/gene/10090:Or6n2 ^@ http://purl.uniprot.org/uniprot/E9Q5F1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nrgn ^@ http://purl.uniprot.org/uniprot/P60761 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Region|||Secondary Structure|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Site ^@ Abolishes calmodulin binding, unable to potentiate synaptic transmission.|||Citrulline; partial|||Collagen-like|||Crucial for interaction with calmodulin|||Disordered|||IQ|||N-acetylmethionine|||NEUG(55-78)|||Neurogranin|||Omega-N-methylarginine|||Or C-51 with C-4 or C-9|||Phosphoserine; by PHK and PKC ^@ http://purl.uniprot.org/annotation/PRO_0000159592|||http://purl.uniprot.org/annotation/PRO_0000377702 http://togogenome.org/gene/10090:Vmn1r13 ^@ http://purl.uniprot.org/uniprot/G5E8I3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:4930579G24Rik ^@ http://purl.uniprot.org/uniprot/Q3UUX7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Uncharacterized protein C4orf46 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000335690 http://togogenome.org/gene/10090:Epha3 ^@ http://purl.uniprot.org/uniprot/Q8BRB1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Eph LBD|||Fibronectin type-III|||Helical|||Protein kinase|||Proton acceptor|||SAM|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_5015099064 http://togogenome.org/gene/10090:Evl ^@ http://purl.uniprot.org/uniprot/E9PVP4|||http://purl.uniprot.org/uniprot/F8WJB9|||http://purl.uniprot.org/uniprot/P70429|||http://purl.uniprot.org/uniprot/Q6PB99 ^@ 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|||Disordered|||EVH2|||EVH2 block A|||EVH2 block B|||EVH2 block C|||Ena/VASP-like protein|||In isoform 1.|||KLKR|||Phosphoserine|||Polar residues|||Pro residues|||Required for interaction with ZDHHC17|||WH1 ^@ http://purl.uniprot.org/annotation/PRO_0000087105|||http://purl.uniprot.org/annotation/VSP_004045 http://togogenome.org/gene/10090:Mmgt2 ^@ http://purl.uniprot.org/uniprot/Q8R3L0 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Membrane magnesium transporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000365625 http://togogenome.org/gene/10090:Npdc1 ^@ http://purl.uniprot.org/uniprot/Q64322|||http://purl.uniprot.org/uniprot/Q8CFL4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Neural proliferation differentiation and control protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000021831 http://togogenome.org/gene/10090:Pdcd10 ^@ http://purl.uniprot.org/uniprot/Q8VE70 ^@ 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)|||N6-acetyllysine|||Programmed cell death protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000187563 http://togogenome.org/gene/10090:Peli3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J057|||http://purl.uniprot.org/uniprot/D3Z6V8|||http://purl.uniprot.org/uniprot/Q8BXR6 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolished E3 ubiquitin ligase activity and ability to regulate the NOD2 signaling.|||Abolished ability to regulate the NOD2 signaling; when associated with A-131.|||Abolished ability to regulate the NOD2 signaling; when associated with A-161.|||Disordered|||E3 ubiquitin-protein ligase pellino homolog 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000194177 http://togogenome.org/gene/10090:Lipo3 ^@ http://purl.uniprot.org/uniprot/Q3UT41 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Signal Peptide ^@ Charge relay system|||Lipase|||Nucleophile|||Partial AB-hydrolase lipase ^@ http://purl.uniprot.org/annotation/PRO_5015097496 http://togogenome.org/gene/10090:Thap12 ^@ http://purl.uniprot.org/uniprot/Q9CUX1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Zinc Finger ^@ 52 kDa repressor of the inhibitor of the protein kinase|||Disordered|||Phosphoserine|||Polar residues|||THAP-type ^@ http://purl.uniprot.org/annotation/PRO_0000068635 http://togogenome.org/gene/10090:Gamt ^@ http://purl.uniprot.org/uniprot/O35969 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant ^@ Guanidinoacetate N-methyltransferase|||In isoform 2.|||N-acetylserine|||Phosphoserine|||RMT2|||Removed|||S-adenosyl-L-methionine ^@ http://purl.uniprot.org/annotation/PRO_0000087431|||http://purl.uniprot.org/annotation/VSP_017727 http://togogenome.org/gene/10090:Or1n1 ^@ http://purl.uniprot.org/uniprot/Q8VGK1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cts3 ^@ http://purl.uniprot.org/uniprot/Q91ZD5|||http://purl.uniprot.org/uniprot/Q9DAZ8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Cathepsin M|||Cathepsin propeptide inhibitor|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_5012745694|||http://purl.uniprot.org/annotation/PRO_5015099523 http://togogenome.org/gene/10090:Prrt2 ^@ http://purl.uniprot.org/uniprot/E9PUL5 ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||INTRAMEM|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proline-rich transmembrane protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000415735 http://togogenome.org/gene/10090:Sele ^@ http://purl.uniprot.org/uniprot/Q00690|||http://purl.uniprot.org/uniprot/Q3U5F6 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||E-selectin|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6 ^@ http://purl.uniprot.org/annotation/PRO_0000017493|||http://purl.uniprot.org/annotation/PRO_5015097467 http://togogenome.org/gene/10090:Tubgcp4 ^@ http://purl.uniprot.org/uniprot/Q543T6|||http://purl.uniprot.org/uniprot/Q8BWR3|||http://purl.uniprot.org/uniprot/Q8BYN2|||http://purl.uniprot.org/uniprot/Q9D4F8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Gamma tubulin complex component C-terminal|||Gamma tubulin complex component protein N-terminal|||Gamma-tubulin complex component 4 ^@ http://purl.uniprot.org/annotation/PRO_0000078125 http://togogenome.org/gene/10090:Cacng2 ^@ http://purl.uniprot.org/uniprot/O88602|||http://purl.uniprot.org/uniprot/Q3ZB20 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Transmembrane ^@ Abolishes phosphorylation.|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||No interaction with DLG1 and DLG4.|||Phosphoserine|||Phosphothreonine; by PKA|||Phosphotyrosine|||Voltage-dependent calcium channel gamma-2 subunit ^@ http://purl.uniprot.org/annotation/PRO_0000164674 http://togogenome.org/gene/10090:Tamalin ^@ http://purl.uniprot.org/uniprot/Q9JJA9 ^@ 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|||General receptor for phosphoinositides 1-associated scaffold protein|||Interaction with PSCD3|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000087585 http://togogenome.org/gene/10090:Inpp5f ^@ http://purl.uniprot.org/uniprot/B2RQ14|||http://purl.uniprot.org/uniprot/Q8CDA1 ^@ 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|||HSac2|||Has a diffuse cytosolic localization.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of inositol 4-phosphatase activity. No effect on subcellular localization. No effect on interaction with OCRL, INPP5B and IPP4A.|||Phosphatidylinositide phosphatase SAC2|||Phosphoserine|||Polar residues|||SAC|||hSac2 ^@ http://purl.uniprot.org/annotation/PRO_0000331622|||http://purl.uniprot.org/annotation/VSP_033270|||http://purl.uniprot.org/annotation/VSP_033271|||http://purl.uniprot.org/annotation/VSP_033272|||http://purl.uniprot.org/annotation/VSP_033273|||http://purl.uniprot.org/annotation/VSP_033274 http://togogenome.org/gene/10090:Zxdc ^@ http://purl.uniprot.org/uniprot/Q8C8V1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Pro residues|||Zinc finger protein ZXDC ^@ http://purl.uniprot.org/annotation/PRO_0000292804|||http://purl.uniprot.org/annotation/VSP_026439|||http://purl.uniprot.org/annotation/VSP_026440|||http://purl.uniprot.org/annotation/VSP_026441|||http://purl.uniprot.org/annotation/VSP_026442|||http://purl.uniprot.org/annotation/VSP_026443|||http://purl.uniprot.org/annotation/VSP_026444 http://togogenome.org/gene/10090:Ifit3 ^@ http://purl.uniprot.org/uniprot/Q64345 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ Interferon-induced protein with tetratricopeptide repeats 3|||TPR 1|||TPR 2|||TPR 3|||TPR 4 ^@ http://purl.uniprot.org/annotation/PRO_0000106350 http://togogenome.org/gene/10090:Gpam ^@ http://purl.uniprot.org/uniprot/Q61586 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Modified Residue|||Motif|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Cytoplasmic|||Glycerol-3-phosphate acyltransferase 1, mitochondrial|||HXXXXD motif|||Helical|||Mitochondrial intermembrane|||Mitochondrion|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000024691 http://togogenome.org/gene/10090:Serpinb6e ^@ http://purl.uniprot.org/uniprot/I7HJI3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Pcmtd1 ^@ http://purl.uniprot.org/uniprot/P59913|||http://purl.uniprot.org/uniprot/Q3TGS5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Region ^@ AdoMet binding motif|||BC-box|||Basic and acidic residues|||CUL-box|||Disordered|||N-myristoyl glycine|||Protein-L-isoaspartate O-methyltransferase domain-containing protein 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000111926 http://togogenome.org/gene/10090:Nsun6 ^@ http://purl.uniprot.org/uniprot/A2ASK1|||http://purl.uniprot.org/uniprot/Q7TS68 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ N6-acetyllysine|||Nucleophile|||PUA|||SAM-dependent MTase RsmB/NOP-type|||tRNA (cytosine(72)-C(5))-methyltransferase NSUN6 ^@ http://purl.uniprot.org/annotation/PRO_0000263115 http://togogenome.org/gene/10090:Wnk3 ^@ http://purl.uniprot.org/uniprot/Q80XP9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with KLHL3|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase WNK3 ^@ http://purl.uniprot.org/annotation/PRO_0000278775|||http://purl.uniprot.org/annotation/VSP_041934 http://togogenome.org/gene/10090:Fap ^@ http://purl.uniprot.org/uniprot/P97321 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Antiplasmin-cleaving enzyme FAP, soluble form|||Charge relay system|||Cleavage|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Localized at the cell surface, inhibits gelatinase and dipeptidyl peptidase activities and stimulates tumor suppression activity.|||N-linked (GlcNAc...) asparagine|||Prolyl endopeptidase FAP ^@ http://purl.uniprot.org/annotation/PRO_0000122425|||http://purl.uniprot.org/annotation/PRO_0000430644|||http://purl.uniprot.org/annotation/VSP_005368|||http://purl.uniprot.org/annotation/VSP_005369 http://togogenome.org/gene/10090:Spata13 ^@ http://purl.uniprot.org/uniprot/E0CYU0|||http://purl.uniprot.org/uniprot/E9Q3I3|||http://purl.uniprot.org/uniprot/Q5DU57 ^@ 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 ^@ ABR (APC-binding region) domain|||Basic and acidic residues|||C-terminal tail|||DH|||Disordered|||In isoform 2.|||PH|||Phosphoserine|||Polar residues|||Pro residues|||SH3|||Spermatogenesis-associated protein 13 ^@ http://purl.uniprot.org/annotation/PRO_0000278449|||http://purl.uniprot.org/annotation/VSP_023287 http://togogenome.org/gene/10090:Pithd1 ^@ http://purl.uniprot.org/uniprot/Q8BWR2 ^@ 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.|||PITH|||PITH domain-containing protein 1|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000285033|||http://purl.uniprot.org/annotation/VSP_024808 http://togogenome.org/gene/10090:Dnttip2 ^@ http://purl.uniprot.org/uniprot/Q8R2M2 ^@ 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 ^@ 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_0000318506 http://togogenome.org/gene/10090:Hs3st2 ^@ http://purl.uniprot.org/uniprot/Q673U1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate glucosamine 3-O-sulfotransferase 2|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000085215|||http://purl.uniprot.org/annotation/VSP_013179|||http://purl.uniprot.org/annotation/VSP_013180|||http://purl.uniprot.org/annotation/VSP_013181|||http://purl.uniprot.org/annotation/VSP_013182 http://togogenome.org/gene/10090:Actr6 ^@ http://purl.uniprot.org/uniprot/Q9D864 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Actin-related protein 6|||N-acetylthreonine|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089106 http://togogenome.org/gene/10090:Tas2r140 ^@ http://purl.uniprot.org/uniprot/Q7TQA4 ^@ 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 140 ^@ http://purl.uniprot.org/annotation/PRO_0000082293 http://togogenome.org/gene/10090:Ppfia2 ^@ http://purl.uniprot.org/uniprot/B8QI34|||http://purl.uniprot.org/uniprot/F7CYX4|||http://purl.uniprot.org/uniprot/Q8BSS9 ^@ 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 ^@ Disordered|||Liprin-alpha-2|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM|||SAM 1|||SAM 2|||SAM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000191028 http://togogenome.org/gene/10090:Fam205a1 ^@ http://purl.uniprot.org/uniprot/D3YZF6 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||SPATA31|||SPATA31F3-like ^@ http://togogenome.org/gene/10090:Ralyl ^@ http://purl.uniprot.org/uniprot/A0A0A6YXQ8|||http://purl.uniprot.org/uniprot/Q8BTF8 ^@ 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.|||Polar residues|||RNA-binding Raly-like protein|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000299526|||http://purl.uniprot.org/annotation/VSP_027727|||http://purl.uniprot.org/annotation/VSP_027728 http://togogenome.org/gene/10090:Or5p69 ^@ http://purl.uniprot.org/uniprot/Q8VG07 ^@ 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 5P69 ^@ http://purl.uniprot.org/annotation/PRO_0000150849 http://togogenome.org/gene/10090:Myo9b ^@ http://purl.uniprot.org/uniprot/E9PWZ6|||http://purl.uniprot.org/uniprot/E9PZW8|||http://purl.uniprot.org/uniprot/Q3TRQ0 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Actin-binding|||Basic and acidic residues|||Disordered|||Myosin motor|||Phorbol-ester/DAG-type|||Polar residues|||Pro residues|||Ras-associating|||Rho-GAP ^@ http://togogenome.org/gene/10090:Prp2 ^@ http://purl.uniprot.org/uniprot/F8VPU9 ^@ 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_5015091375 http://togogenome.org/gene/10090:9930021J03Rik ^@ http://purl.uniprot.org/uniprot/H3BKP8 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||Bromo|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Pcdhb4 ^@ http://purl.uniprot.org/uniprot/Q8CBE8|||http://purl.uniprot.org/uniprot/Q8CE07|||http://purl.uniprot.org/uniprot/Q91XZ6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Cadherin domain-containing protein|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5004304006|||http://purl.uniprot.org/annotation/PRO_5004304427|||http://purl.uniprot.org/annotation/PRO_5015099501 http://togogenome.org/gene/10090:Trf ^@ http://purl.uniprot.org/uniprot/Q921I1 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Dimethylated arginine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Serotransferrin|||Transferrin-like 1|||Transferrin-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000035716 http://togogenome.org/gene/10090:Mylip ^@ http://purl.uniprot.org/uniprot/Q8BM54 ^@ 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|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Critical for homodimerization|||Disordered|||E3 ubiquitin-protein ligase MYLIP|||FERM|||In isoform 2.|||Loss of ubiquitin ligase activity.|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055973|||http://purl.uniprot.org/annotation/VSP_011830 http://togogenome.org/gene/10090:Tmem248 ^@ http://purl.uniprot.org/uniprot/Q3TBN1 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 248 ^@ http://purl.uniprot.org/annotation/PRO_0000295127 http://togogenome.org/gene/10090:C9orf72 ^@ http://purl.uniprot.org/uniprot/Q6DFW0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Guanine nucleotide exchange factor C9orf72 homolog|||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_0000089712|||http://purl.uniprot.org/annotation/VSP_059260 http://togogenome.org/gene/10090:Relb ^@ http://purl.uniprot.org/uniprot/Q04863|||http://purl.uniprot.org/uniprot/Q8K220 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||Leucine-zipper|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||RHD|||Strongly reduces transcriptional activity and interaction with NFKB1/p50 and NFKB2/p52.|||Transcription factor RelB ^@ http://purl.uniprot.org/annotation/PRO_0000205174 http://togogenome.org/gene/10090:Arl2bp ^@ http://purl.uniprot.org/uniprot/Q9D385 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ ADP-ribosylation factor-like protein 2-binding protein|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000287115|||http://purl.uniprot.org/annotation/VSP_025319|||http://purl.uniprot.org/annotation/VSP_025320 http://togogenome.org/gene/10090:Scgb2b12 ^@ http://purl.uniprot.org/uniprot/S4R2L0 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015101142 http://togogenome.org/gene/10090:Vmn1r9 ^@ http://purl.uniprot.org/uniprot/A2RST7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp287 ^@ http://purl.uniprot.org/uniprot/Q9EQB9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||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|||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_0000047512 http://togogenome.org/gene/10090:Or2b11 ^@ http://purl.uniprot.org/uniprot/Q7TS30 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ehd1 ^@ http://purl.uniprot.org/uniprot/Q80ZZ0|||http://purl.uniprot.org/uniprot/Q9WVK4 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolishes interaction with PACSIN2.|||Dynamin-type G|||EF-hand|||EH|||EH domain-containing protein 1|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000146110 http://togogenome.org/gene/10090:Gbp5 ^@ http://purl.uniprot.org/uniprot/Q8BMN7|||http://purl.uniprot.org/uniprot/Q8CFB4 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ Cysteine methyl ester|||Disordered|||GB1/RHD3-type G|||GTPase domain (Globular)|||Guanylate-binding protein 5|||In isoform 2.|||NLRP3-binding|||Removed in mature form|||Required for tetramerization, but not for dimerization|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000190970|||http://purl.uniprot.org/annotation/PRO_0000370786|||http://purl.uniprot.org/annotation/VSP_057889|||http://purl.uniprot.org/annotation/VSP_057890 http://togogenome.org/gene/10090:Gba ^@ http://purl.uniprot.org/uniprot/P17439 ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Lysosomal acid glucosylceramidase|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000012178 http://togogenome.org/gene/10090:Slc6a4 ^@ http://purl.uniprot.org/uniprot/Q60857 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Interaction with RAB4A|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Sodium-dependent serotonin transporter ^@ http://purl.uniprot.org/annotation/PRO_0000214759 http://togogenome.org/gene/10090:Usp33 ^@ http://purl.uniprot.org/uniprot/A0A0H2UKB8|||http://purl.uniprot.org/uniprot/Q8R5K2 ^@ 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|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ DUSP|||DUSP 1|||DUSP 2|||Disordered|||In isoform 2.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 33 ^@ http://purl.uniprot.org/annotation/PRO_0000390424|||http://purl.uniprot.org/annotation/VSP_038531 http://togogenome.org/gene/10090:Chtop ^@ http://purl.uniprot.org/uniprot/B7ZMS6|||http://purl.uniprot.org/uniprot/E9PW20|||http://purl.uniprot.org/uniprot/Q9CY57 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Chromatin target of PRMT1 protein|||Chromatin target of PRMT1 protein C-terminal|||Disordered|||GAR motif; involved in 5hmC binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||Interaction with PRMT1|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089264|||http://purl.uniprot.org/annotation/VSP_011743|||http://purl.uniprot.org/annotation/VSP_011744|||http://purl.uniprot.org/annotation/VSP_011745 http://togogenome.org/gene/10090:Sva ^@ http://purl.uniprot.org/uniprot/Q3SXH3 ^@ Disulfide Bond|||Modification|||Region|||Transmembrane ^@ Disulfide Bond|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Or4f14b ^@ http://purl.uniprot.org/uniprot/Q7TQX1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kcnj13 ^@ http://purl.uniprot.org/uniprot/P86046 ^@ Chain|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Modified Residue|||Motif|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Inward rectifier potassium channel 13|||Phosphoserine; by PKA|||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_0000355142 http://togogenome.org/gene/10090:Eml6 ^@ http://purl.uniprot.org/uniprot/Q5SQM0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||Echinoderm microtubule-associated protein-like 6|||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_0000284398 http://togogenome.org/gene/10090:4930505A04Rik ^@ http://purl.uniprot.org/uniprot/Q5SPV6 ^@ 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 C2orf73 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000332214|||http://purl.uniprot.org/annotation/VSP_033354 http://togogenome.org/gene/10090:Ampd1 ^@ http://purl.uniprot.org/uniprot/Q3V1D3 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ AMP deaminase 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000269718 http://togogenome.org/gene/10090:Spopl ^@ http://purl.uniprot.org/uniprot/Q2M2N2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ BTB|||In isoform 2.|||MATH|||Speckle-type POZ protein-like ^@ http://purl.uniprot.org/annotation/PRO_0000274589|||http://purl.uniprot.org/annotation/VSP_022824 http://togogenome.org/gene/10090:Plch2 ^@ http://purl.uniprot.org/uniprot/A2AP18|||http://purl.uniprot.org/uniprot/F7C3A0|||http://purl.uniprot.org/uniprot/Q6PAS6 ^@ 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|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2|||Acidic residues|||Basic and acidic residues|||C2|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Inhibition of activity.|||Necessary for plasma membrane localization|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000308959|||http://purl.uniprot.org/annotation/VSP_029075|||http://purl.uniprot.org/annotation/VSP_029076|||http://purl.uniprot.org/annotation/VSP_029077|||http://purl.uniprot.org/annotation/VSP_029078|||http://purl.uniprot.org/annotation/VSP_029079|||http://purl.uniprot.org/annotation/VSP_029081|||http://purl.uniprot.org/annotation/VSP_029082|||http://purl.uniprot.org/annotation/VSP_029083|||http://purl.uniprot.org/annotation/VSP_029084 http://togogenome.org/gene/10090:Rtl6 ^@ http://purl.uniprot.org/uniprot/Q505G4 ^@ 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_0000289098 http://togogenome.org/gene/10090:Tmem260 ^@ http://purl.uniprot.org/uniprot/Q8BMD6 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Protein O-mannosyl-transferase TMEM260 ^@ http://purl.uniprot.org/annotation/PRO_0000089906|||http://purl.uniprot.org/annotation/VSP_008622 http://togogenome.org/gene/10090:Mageb5b ^@ http://purl.uniprot.org/uniprot/A2A9Q9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||MAGE ^@ http://togogenome.org/gene/10090:Gpr160 ^@ http://purl.uniprot.org/uniprot/Q3U3F9 ^@ 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|||Probable G-protein coupled receptor 160 ^@ http://purl.uniprot.org/annotation/PRO_0000069644 http://togogenome.org/gene/10090:Or51d1 ^@ http://purl.uniprot.org/uniprot/E9Q550 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp266 ^@ http://purl.uniprot.org/uniprot/E9Q2S7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ddias ^@ http://purl.uniprot.org/uniprot/E9QLR9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Replication factor A C-terminal ^@ http://togogenome.org/gene/10090:Dnah8 ^@ http://purl.uniprot.org/uniprot/Q91XQ0 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Disordered|||Dynein axonemal heavy chain 8|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Stalk ^@ http://purl.uniprot.org/annotation/PRO_0000274045|||http://purl.uniprot.org/annotation/VSP_022616|||http://purl.uniprot.org/annotation/VSP_022617 http://togogenome.org/gene/10090:Stau2 ^@ http://purl.uniprot.org/uniprot/D3Z6D2|||http://purl.uniprot.org/uniprot/Q8CJ67 ^@ 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 ^@ Abrogates RNA-binding by DRBM 3 and interaction with XPO5 and nuclear export; when associated with A-235.|||Abrogates RNA-binding by DRBM 3 and interaction with XPO5 and nuclear export; when associated with A-237.|||DRBM|||DRBM 1|||DRBM 2|||DRBM 3|||DRBM 4|||Disordered|||Double-stranded RNA-binding protein Staufen homolog 2|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Nuclear localization signal 1|||Nuclear localization signal 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Prevents nuclear localization of mutants lacking DRBM 3 function; when associated with 257-AA-258.|||Prevents nuclear localization of mutants lacking DRBM 3 function; when associated with 289-AAA-291.|||Required for dendritic transport ^@ http://purl.uniprot.org/annotation/PRO_0000072247|||http://purl.uniprot.org/annotation/VSP_015378|||http://purl.uniprot.org/annotation/VSP_015379|||http://purl.uniprot.org/annotation/VSP_015380|||http://purl.uniprot.org/annotation/VSP_015381|||http://purl.uniprot.org/annotation/VSP_015382|||http://purl.uniprot.org/annotation/VSP_015383|||http://purl.uniprot.org/annotation/VSP_015384 http://togogenome.org/gene/10090:Ap5s1 ^@ http://purl.uniprot.org/uniprot/Q9D742 ^@ Chain|||Molecule Processing ^@ Chain ^@ AP-5 complex subunit sigma-1 ^@ http://purl.uniprot.org/annotation/PRO_0000079424 http://togogenome.org/gene/10090:Bicral ^@ http://purl.uniprot.org/uniprot/B2RX81|||http://purl.uniprot.org/uniprot/Q8CHH5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ BRD4-interacting chromatin-remodeling complex-associated protein-like|||Basic and acidic residues|||Disordered|||GLTSCR protein conserved|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000248603 http://togogenome.org/gene/10090:Inip ^@ http://purl.uniprot.org/uniprot/Q3TXT3 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Splice Variant ^@ In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||SOSS complex subunit C ^@ http://purl.uniprot.org/annotation/PRO_0000279420|||http://purl.uniprot.org/annotation/VSP_023425 http://togogenome.org/gene/10090:Trim54 ^@ http://purl.uniprot.org/uniprot/Q9ERP3 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Acidic residues|||B box-type|||Basic and acidic residues|||COS|||Disordered|||Mediates microtubule-binding and homooligomerization|||RING-type|||Tripartite motif-containing protein 54 ^@ http://purl.uniprot.org/annotation/PRO_0000056283 http://togogenome.org/gene/10090:Rhod ^@ http://purl.uniprot.org/uniprot/G3X9Y4|||http://purl.uniprot.org/uniprot/P97348 ^@ 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|||Disordered|||Effector region|||Removed in mature form|||Rho-related GTP-binding protein RhoD|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000198864|||http://purl.uniprot.org/annotation/PRO_0000223366 http://togogenome.org/gene/10090:Vwa1 ^@ http://purl.uniprot.org/uniprot/Q8R2Z5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No formation of homomultimers. No formation of homodimers; when associated with S-369.|||No formation of homomultimers. No formation of homodimers; when associated with S-393.|||Phosphoserine|||VWFA|||von Willebrand factor A domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000307157|||http://purl.uniprot.org/annotation/VSP_028618 http://togogenome.org/gene/10090:Vmn2r49 ^@ http://purl.uniprot.org/uniprot/D3Z6L3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003052650 http://togogenome.org/gene/10090:COX3 ^@ http://purl.uniprot.org/uniprot/P00416|||http://purl.uniprot.org/uniprot/Q7JCX7 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytochrome c oxidase subunit 3|||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|||Mitochondrial intermembrane|||Mitochondrial matrix ^@ http://purl.uniprot.org/annotation/PRO_0000183809 http://togogenome.org/gene/10090:Slc18b1 ^@ http://purl.uniprot.org/uniprot/E9PU92|||http://purl.uniprot.org/uniprot/Q8BTD6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:Krt84 ^@ http://purl.uniprot.org/uniprot/Q99M73 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type II cuticular Hb4|||Linker 1|||Linker 12|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063701 http://togogenome.org/gene/10090:Paqr9 ^@ http://purl.uniprot.org/uniprot/Q6TCG2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Membrane progesterone receptor epsilon ^@ http://purl.uniprot.org/annotation/PRO_0000218853 http://togogenome.org/gene/10090:Rnf34 ^@ http://purl.uniprot.org/uniprot/Q99KR6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site|||Zinc Finger ^@ Acidic residues|||Cleavage; by caspase-3|||Disordered|||E3 ubiquitin-protein ligase RNF34|||FYVE-type|||Phosphoserine|||RING-type|||SAP 1|||SAP 2 ^@ http://purl.uniprot.org/annotation/PRO_0000056073 http://togogenome.org/gene/10090:Slc29a2 ^@ http://purl.uniprot.org/uniprot/Q61672 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Equilibrative nucleoside transporter 2|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000209341 http://togogenome.org/gene/10090:Zfp942 ^@ http://purl.uniprot.org/uniprot/B8JJA7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dnajb2 ^@ http://purl.uniprot.org/uniprot/Q9QYI5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||CAAX motif|||Cysteine methyl ester|||Disordered|||DnaJ homolog subfamily B member 2|||In isoform 3 and isoform 2.|||In isoform 3.|||J|||N-acetylalanine|||Phosphoserine|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine|||UIM 1|||UIM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000438688|||http://purl.uniprot.org/annotation/PRO_0000438689|||http://purl.uniprot.org/annotation/VSP_058708|||http://purl.uniprot.org/annotation/VSP_058709|||http://purl.uniprot.org/annotation/VSP_058710 http://togogenome.org/gene/10090:Col6a5 ^@ http://purl.uniprot.org/uniprot/A0A140T8W1|||http://purl.uniprot.org/uniprot/A6H584 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Cell attachment site|||Collagen alpha-5(VI) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Disordered|||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_5000253010|||http://purl.uniprot.org/annotation/PRO_5007305481 http://togogenome.org/gene/10090:Net1 ^@ http://purl.uniprot.org/uniprot/Q3USZ7|||http://purl.uniprot.org/uniprot/Q9Z206 ^@ 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 ^@ Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||Inhibits transformation by N-terminal truncated form.|||Leads to cytoplasmic relocalization; when associated with 12-A--A-16.|||Leads to cytoplasmic relocalization; when associated with 67-A--A-70.|||N-acetylmethionine|||Necessary for nuclear localization|||Neuroepithelial cell-transforming gene 1 protein|||Nuclear localization signal|||PH|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000080925|||http://purl.uniprot.org/annotation/VSP_011622|||http://purl.uniprot.org/annotation/VSP_011623 http://togogenome.org/gene/10090:Pak5 ^@ http://purl.uniprot.org/uniprot/Q8C015 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||CRIB|||Disordered|||Linker|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PAK 5 ^@ http://purl.uniprot.org/annotation/PRO_0000086478 http://togogenome.org/gene/10090:Coa7 ^@ http://purl.uniprot.org/uniprot/Q921H9 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat ^@ Cytochrome c oxidase assembly factor 7|||N-acetylalanine|||Removed|||Sel1-like 1|||Sel1-like 2|||Sel1-like 3|||Sel1-like 4|||Sel1-like 5 ^@ http://purl.uniprot.org/annotation/PRO_0000282365 http://togogenome.org/gene/10090:Gm5134 ^@ http://purl.uniprot.org/uniprot/E9QAB5|||http://purl.uniprot.org/uniprot/Q3V0B7|||http://purl.uniprot.org/uniprot/Q8BIM1 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Sox1 ^@ http://purl.uniprot.org/uniprot/P53783 ^@ 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_0000048713 http://togogenome.org/gene/10090:Nae1 ^@ http://purl.uniprot.org/uniprot/E0CZE0|||http://purl.uniprot.org/uniprot/Q3UK27|||http://purl.uniprot.org/uniprot/Q8VBW6 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Interaction with UBA3|||N-acetylalanine|||N6-acetyllysine|||NEDD8-activating enzyme E1 regulatory subunit|||Removed|||THIF-type NAD/FAD binding fold ^@ http://purl.uniprot.org/annotation/PRO_0000194953 http://togogenome.org/gene/10090:Aurkb ^@ http://purl.uniprot.org/uniprot/O70126 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Aurora kinase B|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085657 http://togogenome.org/gene/10090:Arhgap25 ^@ http://purl.uniprot.org/uniprot/Q8BYW1 ^@ 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.|||In isoform 3.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho GTPase-activating protein 25|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000056717|||http://purl.uniprot.org/annotation/VSP_019233|||http://purl.uniprot.org/annotation/VSP_019234 http://togogenome.org/gene/10090:Kctd1 ^@ http://purl.uniprot.org/uniprot/E9Q6T9|||http://purl.uniprot.org/uniprot/Q5M956 ^@ 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 ^@ Acidic residues|||BTB|||BTB/POZ domain-containing protein KCTD1|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247145|||http://purl.uniprot.org/annotation/VSP_019931 http://togogenome.org/gene/10090:Ccdc60 ^@ http://purl.uniprot.org/uniprot/Q8C4J0 ^@ 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|||Coiled-coil domain-containing protein 60|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000239666|||http://purl.uniprot.org/annotation/VSP_019251|||http://purl.uniprot.org/annotation/VSP_019252 http://togogenome.org/gene/10090:Trim24 ^@ http://purl.uniprot.org/uniprot/E9Q1U8|||http://purl.uniprot.org/uniprot/Q3V0H4|||http://purl.uniprot.org/uniprot/Q64127 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Zinc Finger ^@ B box-type|||B box-type 1|||B box-type 2|||Breakpoint for translocation to form TRIM24-BRAF oncogene|||Bromo|||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 isoform Short.|||Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)|||Loss of sumoylation; when associated with R-724.|||Loss of sumoylation; when associated with R-742.|||Nuclear localization signal|||Nuclear receptor binding site (NRBS)|||Omega-N-methylarginine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RING-type|||Transcription intermediary factor 1-alpha ^@ http://purl.uniprot.org/annotation/PRO_0000056391|||http://purl.uniprot.org/annotation/VSP_005773 http://togogenome.org/gene/10090:Gabrr2 ^@ http://purl.uniprot.org/uniprot/P56476 ^@ 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|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000000489|||http://purl.uniprot.org/annotation/VSP_044374 http://togogenome.org/gene/10090:Lta4h ^@ http://purl.uniprot.org/uniprot/P24527 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Alters leukotriene hydrolase activity, strongly enhancing the formation of a metabolite that is normally produced in trace amounts.|||Complete loss of LTA4 hydrolase and peptidase enzyme activities.|||Covalently modified during suicide inhibition by leukotrienes|||Essential for epoxide hydrolase activity, but not for aminopeptidase activity|||Leukotriene A-4 hydrolase|||N6-acetyllysine|||Phosphoserine|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000095125 http://togogenome.org/gene/10090:Map2k5 ^@ http://purl.uniprot.org/uniprot/Q9WVS7 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand ^@ Disordered|||Dominant active form; when associated with D-311.|||Dominant active form; when associated with D-315.|||Dominant negative form; when associated with A-311.|||Dominant negative form; when associated with V-315.|||Dual specificity mitogen-activated protein kinase kinase 5|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with MAP3K2/MAP3K3|||Interaction with MAPK7|||Loss of MAP3K2/MAP3K3 binding; when associated with A-64.|||Loss of MAP3K2/MAP3K3 binding; when associated with A-65.|||Loss of MAP3K2/MAP3K3 binding; when associated with A-67.|||Loss of MAP3K2/MAP3K3 binding; when associated with A-68.|||Loss of MAPK7 binding; when associated with A-20.|||Loss of MAPK7 binding; when associated with A-21.|||PB1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086384|||http://purl.uniprot.org/annotation/VSP_015836|||http://purl.uniprot.org/annotation/VSP_015837|||http://purl.uniprot.org/annotation/VSP_015838|||http://purl.uniprot.org/annotation/VSP_015839|||http://purl.uniprot.org/annotation/VSP_015840 http://togogenome.org/gene/10090:Gem ^@ http://purl.uniprot.org/uniprot/P55041|||http://purl.uniprot.org/uniprot/Q3TH76 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Calmodulin-binding|||Disordered|||GTP-binding protein GEM|||No calmodulin binding. ^@ http://purl.uniprot.org/annotation/PRO_0000122476 http://togogenome.org/gene/10090:Tfap2a ^@ http://purl.uniprot.org/uniprot/A0A0R4J1E6|||http://purl.uniprot.org/uniprot/A0A286YCU0|||http://purl.uniprot.org/uniprot/A0A286YD43|||http://purl.uniprot.org/uniprot/P34056|||http://purl.uniprot.org/uniprot/Q3UL09|||http://purl.uniprot.org/uniprot/Q8BPN4 ^@ 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 ^@ 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 isoform 2.|||In isoform 3.|||In isoform 4.|||PPxY motif|||Phosphoserine; by PKA|||Polar residues|||Pro residues|||Transcription factor AP-2 C-terminal|||Transcription factor AP-2-alpha ^@ http://purl.uniprot.org/annotation/PRO_0000184797|||http://purl.uniprot.org/annotation/VSP_006402|||http://purl.uniprot.org/annotation/VSP_006403|||http://purl.uniprot.org/annotation/VSP_006404 http://togogenome.org/gene/10090:Zfp804a ^@ http://purl.uniprot.org/uniprot/A2AKY4|||http://purl.uniprot.org/uniprot/Q8BHP6|||http://purl.uniprot.org/uniprot/Q8CFV3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||C2H2-type|||Disordered|||Polar residues|||Zinc finger protein 804A ^@ http://purl.uniprot.org/annotation/PRO_0000289141 http://togogenome.org/gene/10090:1700001K19Rik ^@ http://purl.uniprot.org/uniprot/Q80ZT1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Slit2 ^@ http://purl.uniprot.org/uniprot/A0A140T8T2|||http://purl.uniprot.org/uniprot/G3UY21|||http://purl.uniprot.org/uniprot/G3UYX7|||http://purl.uniprot.org/uniprot/Q9R1B9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ CTCK|||Cleavage|||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|||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 2 protein|||Slit homolog 2 protein C-product|||Slit homolog 2 protein N-product ^@ http://purl.uniprot.org/annotation/PRO_0000007728|||http://purl.uniprot.org/annotation/PRO_0000007729|||http://purl.uniprot.org/annotation/PRO_0000007730|||http://purl.uniprot.org/annotation/PRO_5003457039|||http://purl.uniprot.org/annotation/PRO_5003457223|||http://purl.uniprot.org/annotation/PRO_5007305548 http://togogenome.org/gene/10090:Bak1 ^@ http://purl.uniprot.org/uniprot/O08734 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Transmembrane|||Turn ^@ BH1|||BH2|||BH3|||Bcl-2 homologous antagonist/killer|||Disordered|||Helical|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000143060 http://togogenome.org/gene/10090:Nab1 ^@ http://purl.uniprot.org/uniprot/A0A087WSU4|||http://purl.uniprot.org/uniprot/Q61122 ^@ 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 ^@ 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|||Loss of transcriptional repression.|||Loss of transcriptional repression; when associated with Q-64.|||Loss of transcriptional repression; when associated with R-33.|||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_0000077040 http://togogenome.org/gene/10090:Mdh1b ^@ http://purl.uniprot.org/uniprot/Q5F204 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Putative malate dehydrogenase 1B ^@ http://purl.uniprot.org/annotation/PRO_0000331436 http://togogenome.org/gene/10090:Habp2 ^@ http://purl.uniprot.org/uniprot/E9QM92|||http://purl.uniprot.org/uniprot/Q3UEI7|||http://purl.uniprot.org/uniprot/Q3V1J8|||http://purl.uniprot.org/uniprot/Q8K0D2 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Charge relay system|||Cleavage|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like domain-containing protein|||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 isoform 2.|||Interchain (between heavy and light chains)|||Kringle|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027903|||http://purl.uniprot.org/annotation/PRO_0000027904|||http://purl.uniprot.org/annotation/PRO_0000027905|||http://purl.uniprot.org/annotation/PRO_0000027906|||http://purl.uniprot.org/annotation/PRO_5003246411|||http://purl.uniprot.org/annotation/PRO_5004229928|||http://purl.uniprot.org/annotation/PRO_5015097522|||http://purl.uniprot.org/annotation/VSP_015395 http://togogenome.org/gene/10090:Ecsit ^@ http://purl.uniprot.org/uniprot/A0A0R4J174|||http://purl.uniprot.org/uniprot/Q9QZH6 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||ECSIT C-terminal|||Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000291987 http://togogenome.org/gene/10090:Septin7 ^@ http://purl.uniprot.org/uniprot/E9Q1G8|||http://purl.uniprot.org/uniprot/O55131 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||G1 motif|||G3 motif|||G4 motif|||Interaction with SEPTIN12|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Septin-7|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173529 http://togogenome.org/gene/10090:Zfp703 ^@ http://purl.uniprot.org/uniprot/E9PXD8|||http://purl.uniprot.org/uniprot/F6M3K1|||http://purl.uniprot.org/uniprot/P0CL69 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||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_0000407219 http://togogenome.org/gene/10090:Jph4 ^@ http://purl.uniprot.org/uniprot/Q80WT0 ^@ 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 ^@ Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||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_0000159853|||http://purl.uniprot.org/annotation/VSP_008197|||http://purl.uniprot.org/annotation/VSP_008198 http://togogenome.org/gene/10090:Dnajc21 ^@ http://purl.uniprot.org/uniprot/E9Q8D0 ^@ 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 1|||C2H2-type 2|||Disordered|||DnaJ homolog subfamily C member 21|||J|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000437995 http://togogenome.org/gene/10090:Hsp90aa1 ^@ http://purl.uniprot.org/uniprot/P07901|||http://purl.uniprot.org/uniprot/Q80Y52 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Interaction with FLCN and FNIP1|||Interaction with FNIP2 and TSC1|||Interaction with NR1D1|||Interaction with NR3C1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine; by PRKDC|||Phosphotyrosine|||Removed|||Required for homodimerization|||S-nitrosocysteine|||TPR repeat-binding ^@ http://purl.uniprot.org/annotation/PRO_0000062912 http://togogenome.org/gene/10090:Dclre1b ^@ http://purl.uniprot.org/uniprot/Q8C7W7 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ 5' exonuclease Apollo|||Abolishes exonuclease activity without affecting the telomere localization, leading to impaired 3'-overhang at the leading end telomeres.|||Abolishes exonuclease activity, leading to activate the ATM signaling pathway; when associated with 31-A--N-35.|||Abolishes exonuclease activity, leading to activate the ATM signaling pathway; when associated with A-230.|||Abolishes interaction with TERF2 and localization to telomeres, leading to activate the ATM signaling pathway.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||TBM ^@ http://purl.uniprot.org/annotation/PRO_0000209120|||http://purl.uniprot.org/annotation/VSP_015174|||http://purl.uniprot.org/annotation/VSP_015175|||http://purl.uniprot.org/annotation/VSP_015176 http://togogenome.org/gene/10090:Or10h5 ^@ http://purl.uniprot.org/uniprot/K7N6V7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cbln1 ^@ http://purl.uniprot.org/uniprot/Q7TNF5|||http://purl.uniprot.org/uniprot/Q9R171 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Abolishes homohexamer formation from homotrimers; when associated with A-34.|||Abolishes homohexamer formation from homotrimers; when associated with A-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|||No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with GRID2, NRXN1 and NRXN3. Loss of N-glycosylation; when associated with Q-23.|||No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with GRID2, NRXN1 and NRXN3. Loss of N-glycosylation; when associated with Q-79.|||Retention in the endoplasmic reticulum/cis-Golgi; when associated with E-110.|||Retention in the endoplasmic reticulum/cis-Golgi; when associated with H-112.|||[des-Ser1]-cerebellin ^@ http://purl.uniprot.org/annotation/PRO_0000003549|||http://purl.uniprot.org/annotation/PRO_0000274211|||http://purl.uniprot.org/annotation/PRO_0000274212|||http://purl.uniprot.org/annotation/PRO_5014311823 http://togogenome.org/gene/10090:Fmo1 ^@ http://purl.uniprot.org/uniprot/P50285|||http://purl.uniprot.org/uniprot/Q3UNX7 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Non-terminal Residue|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Flavin-containing monooxygenase 1|||Helical|||Important for substrate binding|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000147640 http://togogenome.org/gene/10090:Pip ^@ http://purl.uniprot.org/uniprot/P02816|||http://purl.uniprot.org/uniprot/Q3UU48 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Prolactin-inducible protein homolog|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000024290|||http://purl.uniprot.org/annotation/PRO_5014309227 http://togogenome.org/gene/10090:Cdkn2d ^@ http://purl.uniprot.org/uniprot/Q3US51|||http://purl.uniprot.org/uniprot/Q60773 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Turn ^@ Chain|||Helix|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Turn ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cyclin-dependent kinase 4 inhibitor D|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000144189 http://togogenome.org/gene/10090:Klf17 ^@ http://purl.uniprot.org/uniprot/Q8CFA7 ^@ 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|||C2H2-type 3|||Disordered|||Krueppel-like factor 17|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000047556 http://togogenome.org/gene/10090:Cnst ^@ http://purl.uniprot.org/uniprot/Q8CBC4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Consortin|||Cytoplasmic|||Disordered|||Does not affect binding to connexins but results in their intracellular accumulation.|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288907|||http://purl.uniprot.org/annotation/VSP_025821|||http://purl.uniprot.org/annotation/VSP_025822|||http://purl.uniprot.org/annotation/VSP_038657 http://togogenome.org/gene/10090:Or4d6 ^@ http://purl.uniprot.org/uniprot/Q0VDY1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Toporsl ^@ http://purl.uniprot.org/uniprot/Q9D2F8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Pold1 ^@ http://purl.uniprot.org/uniprot/P52431 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ CysA-type|||CysB motif|||DNA polymerase delta catalytic subunit|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nuclear localization signal|||Omega-N-methylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000046444 http://togogenome.org/gene/10090:Ripk4 ^@ http://purl.uniprot.org/uniprot/Q9ERK0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Site|||Strand|||Turn ^@ ANK 1|||ANK 10|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Basic and acidic residues|||Cleavage|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Protein kinase|||Proton acceptor|||Receptor-interacting serine/threonine-protein kinase 4 ^@ http://purl.uniprot.org/annotation/PRO_0000273726 http://togogenome.org/gene/10090:Usp44 ^@ http://purl.uniprot.org/uniprot/Q8C2S0 ^@ 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 deubiquitinase activity.|||Basic and acidic residues|||Disordered|||Nucleophile|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 44 ^@ http://purl.uniprot.org/annotation/PRO_0000395811 http://togogenome.org/gene/10090:Slc10a1 ^@ http://purl.uniprot.org/uniprot/A0A8V5KH54|||http://purl.uniprot.org/uniprot/O08705 ^@ 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 ^@ Disordered|||Helical|||Hepatic sodium/bile acid cotransporter|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000052336|||http://purl.uniprot.org/annotation/VSP_061644 http://togogenome.org/gene/10090:Bub3 ^@ http://purl.uniprot.org/uniprot/Q9WVA3 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Crosslink|||Modified Residue|||Repeat|||Sequence Conflict ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Mitotic checkpoint protein BUB3|||N6-acetyllysine|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000050892 http://togogenome.org/gene/10090:Lypd11 ^@ http://purl.uniprot.org/uniprot/Q8CFJ5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ UPAR/Ly6 ^@ http://togogenome.org/gene/10090:Gm20498 ^@ http://purl.uniprot.org/uniprot/E9PVN6|||http://purl.uniprot.org/uniprot/Q3UFD0|||http://purl.uniprot.org/uniprot/Q9D6K5 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Mitochondrial intermembrane|||PDZ|||Synaptojanin-2-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000375982|||http://purl.uniprot.org/annotation/VSP_053101|||http://purl.uniprot.org/annotation/VSP_053102|||http://purl.uniprot.org/annotation/VSP_053103|||http://purl.uniprot.org/annotation/VSP_053104 http://togogenome.org/gene/10090:Tuba3a ^@ http://purl.uniprot.org/uniprot/P05214|||http://purl.uniprot.org/uniprot/Q5FW91 ^@ 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|||Site ^@ 3'-nitrotyrosine|||Detyrosinated tubulin alpha-3 chain|||Involved in polymerization|||MREC motif|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Tubulin alpha-3 chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase ^@ http://purl.uniprot.org/annotation/PRO_0000048122|||http://purl.uniprot.org/annotation/PRO_0000437401 http://togogenome.org/gene/10090:Vmn1r240 ^@ http://purl.uniprot.org/uniprot/D3YZG3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Chat ^@ http://purl.uniprot.org/uniprot/Q8BQV2 ^@ Active Site|||Domain Extent|||Region|||Site ^@ Active Site|||Domain Extent|||Region ^@ Choline/carnitine acyltransferase|||Disordered|||Proton acceptor ^@ http://togogenome.org/gene/10090:Ankrd22 ^@ http://purl.uniprot.org/uniprot/Q9D3J5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 22 ^@ http://purl.uniprot.org/annotation/PRO_0000320069 http://togogenome.org/gene/10090:Tmem213 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0C3|||http://purl.uniprot.org/uniprot/Q08EA8 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Transmembrane protein 213 ^@ http://purl.uniprot.org/annotation/PRO_0000337055 http://togogenome.org/gene/10090:Or2z8 ^@ http://purl.uniprot.org/uniprot/Q7TRY2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mup12 ^@ http://purl.uniprot.org/uniprot/P11588|||http://purl.uniprot.org/uniprot/Q58ES8 ^@ 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 ^@ Lipocalin/cytosolic fatty-acid binding|||Major urinary protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000017927|||http://purl.uniprot.org/annotation/PRO_5014309708 http://togogenome.org/gene/10090:Arid2 ^@ http://purl.uniprot.org/uniprot/E9Q7E2|||http://purl.uniprot.org/uniprot/Q9D982 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Zinc Finger ^@ ARID|||AT-rich interactive domain-containing protein 2|||Basic and acidic residues|||C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||LXXLL|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RFX-type winged-helix|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000442429 http://togogenome.org/gene/10090:Gstm1 ^@ http://purl.uniprot.org/uniprot/P10649 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Mass|||Modified Residue ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 1|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000185826 http://togogenome.org/gene/10090:Stk10 ^@ http://purl.uniprot.org/uniprot/A1A553|||http://purl.uniprot.org/uniprot/O55098 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Activation segment|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 10 ^@ http://purl.uniprot.org/annotation/PRO_0000086698 http://togogenome.org/gene/10090:Prok1 ^@ http://purl.uniprot.org/uniprot/Q14A28 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Prokineticin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000377457|||http://purl.uniprot.org/annotation/VSP_053117 http://togogenome.org/gene/10090:Mfsd3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J004|||http://purl.uniprot.org/uniprot/Q5U419 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Helical|||Major facilitator superfamily domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000273393|||http://purl.uniprot.org/annotation/PRO_5015044278 http://togogenome.org/gene/10090:Gucy1a1 ^@ http://purl.uniprot.org/uniprot/Q9ERL9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ Guanylate cyclase|||Guanylate cyclase soluble subunit alpha-1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000074111 http://togogenome.org/gene/10090:Or8g51 ^@ http://purl.uniprot.org/uniprot/Q8VF78 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zup1 ^@ http://purl.uniprot.org/uniprot/Q3T9Z9 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 2; atypical|||C2H2-type 3; atypical|||C2H2-type 4|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole|||MIU|||N6-acetyllysine|||Nucleophile|||Proton acceptor|||Zinc finger-containing ubiquitin peptidase 1|||zUBD/ZHA ^@ http://purl.uniprot.org/annotation/PRO_0000244338|||http://purl.uniprot.org/annotation/VSP_019534|||http://purl.uniprot.org/annotation/VSP_019535|||http://purl.uniprot.org/annotation/VSP_019536|||http://purl.uniprot.org/annotation/VSP_019537 http://togogenome.org/gene/10090:Dusp13 ^@ http://purl.uniprot.org/uniprot/Q7TNW3|||http://purl.uniprot.org/uniprot/Q9DA25|||http://purl.uniprot.org/uniprot/Q9QYJ7 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ Dual specificity protein phosphatase 13B|||Phosphocysteine intermediate|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094821 http://togogenome.org/gene/10090:H3c13 ^@ http://purl.uniprot.org/uniprot/B9EI85|||http://purl.uniprot.org/uniprot/P84228 ^@ Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||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 H2A/H2B/H3|||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; 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_0000221250 http://togogenome.org/gene/10090:Fam219b ^@ http://purl.uniprot.org/uniprot/Q14DQ1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Phosphoserine|||Protein FAM219B ^@ http://purl.uniprot.org/annotation/PRO_0000358919|||http://purl.uniprot.org/annotation/VSP_036130|||http://purl.uniprot.org/annotation/VSP_036131 http://togogenome.org/gene/10090:Ccdc160 ^@ http://purl.uniprot.org/uniprot/Q3UYG1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Coiled-coil domain-containing protein 160|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000345952 http://togogenome.org/gene/10090:Myct1 ^@ http://purl.uniprot.org/uniprot/Q8R411 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Motif|||Sequence Conflict|||Transmembrane ^@ Bipartite nuclear localization signal|||Helical|||Myc target protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000310960 http://togogenome.org/gene/10090:Prrc1 ^@ http://purl.uniprot.org/uniprot/Q3UPH1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Polar residues|||Pro residues|||Protein PRRC1 ^@ http://purl.uniprot.org/annotation/PRO_0000307339 http://togogenome.org/gene/10090:Oscar ^@ http://purl.uniprot.org/uniprot/Q8VBT3 ^@ 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 1|||Ig-like 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Osteoclast-associated immunoglobulin-like receptor ^@ http://purl.uniprot.org/annotation/PRO_0000310952|||http://purl.uniprot.org/annotation/VSP_029356 http://togogenome.org/gene/10090:Helz2 ^@ http://purl.uniprot.org/uniprot/A2AS03|||http://purl.uniprot.org/uniprot/E9QAM5|||http://purl.uniprot.org/uniprot/Q3TZD5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ AAA+ ATPase|||C2H2-type|||C2H2-type; atypical|||DEAA box|||Disordered|||Helicase with zinc finger domain 2|||Interaction with THRAP3|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||LXXLL motif 5|||Omega-N-methylarginine|||Ribonuclease II/R ^@ http://purl.uniprot.org/annotation/PRO_0000424355 http://togogenome.org/gene/10090:Jarid2 ^@ http://purl.uniprot.org/uniprot/Q62315 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ ARID|||Acidic residues|||Basic and acidic residues|||Disordered|||GSGFP motif|||In isoform 2.|||JmjC|||JmjN|||Leads to cytoplasmic relocalization.|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein Jumonji|||Sufficient for interaction with the PRC2 complex ^@ http://purl.uniprot.org/annotation/PRO_0000200592|||http://purl.uniprot.org/annotation/VSP_038758 http://togogenome.org/gene/10090:Fcgbp ^@ http://purl.uniprot.org/uniprot/E9Q9C6|||http://purl.uniprot.org/uniprot/Q8C5Q6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide ^@ Disordered|||VWFD|||VWFD domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_5003244520|||http://purl.uniprot.org/annotation/PRO_5004307324 http://togogenome.org/gene/10090:Krtap6-5 ^@ http://purl.uniprot.org/uniprot/Q925H3 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ 25 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 6-5 ^@ http://purl.uniprot.org/annotation/PRO_0000356217 http://togogenome.org/gene/10090:Nr4a2 ^@ http://purl.uniprot.org/uniprot/Q06219|||http://purl.uniprot.org/uniprot/Q3TYI4 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||DNA Binding|||Domain Extent|||Motif|||Region|||Splice Variant|||Zinc Finger ^@ Bipartite nuclear localization signal (NLS1)|||Disordered|||In isoform NURR1A.|||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_0000053719|||http://purl.uniprot.org/annotation/VSP_003710|||http://purl.uniprot.org/annotation/VSP_003711 http://togogenome.org/gene/10090:Wdr44 ^@ http://purl.uniprot.org/uniprot/Q6NVE8 ^@ 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 ^@ Basic and acidic residues|||Binding activity|||Disordered|||Important for interaction with RAB11A|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD repeat-containing protein 44 ^@ http://purl.uniprot.org/annotation/PRO_0000262770|||http://purl.uniprot.org/annotation/VSP_021811 http://togogenome.org/gene/10090:Ccdc86 ^@ http://purl.uniprot.org/uniprot/Q9JJ89 ^@ 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|||Citrulline|||Coiled-coil domain-containing protein 86|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000286093 http://togogenome.org/gene/10090:Pomgnt1 ^@ http://purl.uniprot.org/uniprot/Q91X88 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Catalytic|||Cytoplasmic|||Disordered|||GG-type lectin|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Interaction with O-glycosylated substrate glycoprotein|||Lumenal|||Phosphoserine|||Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000191391|||http://purl.uniprot.org/annotation/VSP_014972|||http://purl.uniprot.org/annotation/VSP_014973|||http://purl.uniprot.org/annotation/VSP_014974 http://togogenome.org/gene/10090:Orm2 ^@ http://purl.uniprot.org/uniprot/P07361 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide ^@ Alpha-1-acid glycoprotein 2|||Disordered|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000017863 http://togogenome.org/gene/10090:Tspear ^@ http://purl.uniprot.org/uniprot/J3S6Y1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||EAR 7|||In isoform 2.|||In isoform 3.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Thrombospondin-type laminin G domain and EAR repeat-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000420603|||http://purl.uniprot.org/annotation/VSP_044542|||http://purl.uniprot.org/annotation/VSP_044543|||http://purl.uniprot.org/annotation/VSP_044544 http://togogenome.org/gene/10090:Rab35 ^@ http://purl.uniprot.org/uniprot/Q6PHN9 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site ^@ Effector region|||Loss of GTPase activity. Increased fast recycling.|||Loss of interaction with MICALL1.|||O-(2-cholinephosphoryl)serine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-35|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121246 http://togogenome.org/gene/10090:Commd6 ^@ http://purl.uniprot.org/uniprot/B7ZNP2|||http://purl.uniprot.org/uniprot/B7ZNP3|||http://purl.uniprot.org/uniprot/Q3V4B5 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ COMM|||COMM domain-containing protein 6|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000294141 http://togogenome.org/gene/10090:Or5k15 ^@ http://purl.uniprot.org/uniprot/E9Q9T3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ciao2b ^@ http://purl.uniprot.org/uniprot/Q9D187 ^@ Chain|||Molecule Processing ^@ Chain ^@ Cytosolic iron-sulfur assembly component 2B ^@ http://purl.uniprot.org/annotation/PRO_0000212692 http://togogenome.org/gene/10090:Hnrnpdl ^@ http://purl.uniprot.org/uniprot/D3YTQ3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||RRM ^@ http://togogenome.org/gene/10090:Ache ^@ http://purl.uniprot.org/uniprot/P21836|||http://purl.uniprot.org/uniprot/Q543Z1 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Signal Peptide|||Strand|||Turn ^@ Acetylcholinesterase|||Acetylcholinesterase tetramerisation|||Acyl-ester intermediate|||Carboxylesterase type B|||Carboxylic ester hydrolase|||Charge relay system|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000008588|||http://purl.uniprot.org/annotation/PRO_5014205864 http://togogenome.org/gene/10090:Foxb2 ^@ http://purl.uniprot.org/uniprot/B9EII5|||http://purl.uniprot.org/uniprot/Q64733 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic residues|||Disordered|||Fork-head|||Forkhead box protein B2|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000091805 http://togogenome.org/gene/10090:Mdh1 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPN8|||http://purl.uniprot.org/uniprot/P14152 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ 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_0000113410 http://togogenome.org/gene/10090:S100pbp ^@ http://purl.uniprot.org/uniprot/Q9D5K4 ^@ 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 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||Polar residues|||S100P-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000317052|||http://purl.uniprot.org/annotation/VSP_052662|||http://purl.uniprot.org/annotation/VSP_052663|||http://purl.uniprot.org/annotation/VSP_052664|||http://purl.uniprot.org/annotation/VSP_052665|||http://purl.uniprot.org/annotation/VSP_052666|||http://purl.uniprot.org/annotation/VSP_052667|||http://purl.uniprot.org/annotation/VSP_052668 http://togogenome.org/gene/10090:Otc ^@ http://purl.uniprot.org/uniprot/P11725|||http://purl.uniprot.org/uniprot/Q543H3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transit Peptide ^@ Aspartate/ornithine carbamoyltransferase Asp/Orn-binding|||Aspartate/ornithine carbamoyltransferase carbamoyl-P binding|||In spf.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Ornithine transcarbamylase, mitochondrial|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000020335 http://togogenome.org/gene/10090:Mfsd9 ^@ http://purl.uniprot.org/uniprot/Q8C0T7 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Major facilitator superfamily domain-containing protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000305026 http://togogenome.org/gene/10090:Klhl21 ^@ http://purl.uniprot.org/uniprot/Q3U410 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ BACK|||BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 21 ^@ http://purl.uniprot.org/annotation/PRO_0000326128 http://togogenome.org/gene/10090:Ndufs1 ^@ http://purl.uniprot.org/uniprot/Q91VD9 ^@ 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|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ 2Fe-2S ferredoxin-type|||4Fe-4S His(Cys)3-ligated-type|||4Fe-4S Mo/W bis-MGD-type|||Mitochondrion|||N6-acetyllysine|||NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000019969 http://togogenome.org/gene/10090:Vmn1r77 ^@ http://purl.uniprot.org/uniprot/E9PY60 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnga1 ^@ http://purl.uniprot.org/uniprot/P29974 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||P-helix|||Selectivity filter|||cGMP-gated cation channel alpha-1 ^@ http://purl.uniprot.org/annotation/PRO_0000219309 http://togogenome.org/gene/10090:Slc44a5 ^@ http://purl.uniprot.org/uniprot/Q5RJI2 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Choline transporter-like protein 5|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000191728 http://togogenome.org/gene/10090:Gal3st2c ^@ http://purl.uniprot.org/uniprot/Q3ULK5 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Nfil3 ^@ http://purl.uniprot.org/uniprot/O08750 ^@ 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 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|||Necessary for transcriptional repression and sufficient for interaction with PER2|||Nuclear factor interleukin-3-regulated protein|||Phosphoserine|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000292668 http://togogenome.org/gene/10090:Snapc5 ^@ http://purl.uniprot.org/uniprot/Q8R2K7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||snRNA-activating protein complex subunit 5 ^@ http://purl.uniprot.org/annotation/PRO_0000072029 http://togogenome.org/gene/10090:2410004P03Rik ^@ http://purl.uniprot.org/uniprot/A0A087WQY2|||http://purl.uniprot.org/uniprot/D3Z430 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Slc22a12 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1I9|||http://purl.uniprot.org/uniprot/Q8CFZ5 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Solute carrier family 22 member 12 ^@ http://purl.uniprot.org/annotation/PRO_0000307945 http://togogenome.org/gene/10090:Prr23a2 ^@ http://purl.uniprot.org/uniprot/D3YWX5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Pro residues ^@ http://togogenome.org/gene/10090:Spty2d1 ^@ http://purl.uniprot.org/uniprot/Q68FG3 ^@ 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 ^@ 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|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Protein SPT2 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000315737 http://togogenome.org/gene/10090:Mecom ^@ http://purl.uniprot.org/uniprot/G3UZ13|||http://purl.uniprot.org/uniprot/P14404 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Splice Variant|||Strand|||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 isoform 1.|||In isoform 4.|||Interaction with SUV39H1 and probably MAPK9 and SMAD3|||Nuclear localization signal|||Phosphoserine|||Polar residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000047274|||http://purl.uniprot.org/annotation/VSP_059487|||http://purl.uniprot.org/annotation/VSP_059488|||http://purl.uniprot.org/annotation/VSP_059489 http://togogenome.org/gene/10090:Gm4559 ^@ http://purl.uniprot.org/uniprot/A4IF42 ^@ Experimental Information|||Non-terminal Residue ^@ Non-terminal Residue ^@ ^@ http://togogenome.org/gene/10090:Or8u8 ^@ http://purl.uniprot.org/uniprot/Q8VFL0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Klhdc8b ^@ http://purl.uniprot.org/uniprot/Q9D2D9 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||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_0000119132 http://togogenome.org/gene/10090:T2 ^@ http://purl.uniprot.org/uniprot/A0A338P791 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Ptprs ^@ http://purl.uniprot.org/uniprot/B0V2N1|||http://purl.uniprot.org/uniprot/Q3TQ52 ^@ 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|||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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes binding to chondroitin sulfate proteoglycans. Abolishes receptor oligomerization via binding to large heparan sulfate proteoglycan structures.|||Cleavage|||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|||Ig-like domain-containing protein|||Important for binding to glycosaminoglycan chains|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Receptor-type tyrosine-protein phosphatase S|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000358321|||http://purl.uniprot.org/annotation/PRO_5004229675|||http://purl.uniprot.org/annotation/VSP_036057|||http://purl.uniprot.org/annotation/VSP_036058|||http://purl.uniprot.org/annotation/VSP_036059|||http://purl.uniprot.org/annotation/VSP_036060|||http://purl.uniprot.org/annotation/VSP_036061|||http://purl.uniprot.org/annotation/VSP_036062 http://togogenome.org/gene/10090:Rnf7 ^@ http://purl.uniprot.org/uniprot/D3Z392|||http://purl.uniprot.org/uniprot/Q9WTZ1 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Zinc Finger ^@ Anaphase-promoting complex subunit 11 RING-H2 finger|||Disordered|||N-acetylalanine|||RING-box protein 2|||RING-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056024 http://togogenome.org/gene/10090:Rogdi ^@ http://purl.uniprot.org/uniprot/Q3TDK6 ^@ 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 ^@ In isoform 2.|||In isoform 3.|||N-acetylalanine|||Protein rogdi homolog|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000315665|||http://purl.uniprot.org/annotation/VSP_030600|||http://purl.uniprot.org/annotation/VSP_030601 http://togogenome.org/gene/10090:Zfand2b ^@ http://purl.uniprot.org/uniprot/Q91X58 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Turn|||Zinc Finger ^@ AN1-type 1|||AN1-type 2|||AN1-type zinc finger protein 2B|||CAAX motif|||Cysteine methyl ester|||Decreased 'Lys-48'-linked polyubiquitin binding.|||Decreased 'Lys-48'-linked polyubiquitin binding. Loss of 'Lys-48'-linked polyubiquitin binding, loss of interaction with BAG6 and loss of association with the proteasome complex; when associated with Q-229 and Q-231.|||Decreased 'Lys-48'-linked polyubiquitin binding. Loss of interaction with BAG6. Decreased association with the proteasome complex.|||Decreased 'Lys-48'-linked polyubiquitin binding. Loss of interaction with ubiquitin polymers and ubiquitinated proteins, loss of interaction with BAG6 and no effect on association with the proteasome complex; when associated with Q-201 and Q-229. Loss of 'Lys-48'-linked polyubiquitin binding, loss of interaction with BAG6 and loss of association with the proteasome complex; when associated with Q-205 and Q-229.|||Decreased 'Lys-48'-linked polyubiquitin binding. Loss of interaction with ubiquitin polymers and ubiquitinated proteins, loss of interaction with BAG6 and no effect on association with the proteasome complex; when associated with Q-201 and Q-231. Loss of 'Lys-48'-linked polyubiquitin binding, loss of interaction with BAG6 and loss of association with the proteasome complex; when associated with Q-205 and Q-231.|||Decreased 'Lys-48'-linked polyubiquitin binding; when associated with A-230.|||Decreased 'Lys-48'-linked polyubiquitin binding; when associated with Q-227.|||Disordered|||Loss of interaction with ubiquitin polymers and ubiquitinated proteins, loss of interaction with BAG6 and no effect on association with the proteasome complex; when associated with Q-229 and Q-231.|||Loss of localization to the endoplasmic reticulum membrane. Loss of interaction with BAG6. No effect on association with the proteasome complex.|||No effect on 'Lys-48'-linked polyubiquitin binding.|||No effect on association with the proteasome complex; when associated with A-163 and A-173.|||No effect on association with the proteasome complex; when associated with A-163 and A-187.|||No effect on association with the proteasome complex; when associated with A-173 and A-187.|||No effect on association with the proteasome complex; when associated with D-163 and D-173.|||No effect on association with the proteasome complex; when associated with D-163 and D-187.|||No effect on association with the proteasome complex; when associated with D-173 and D-187.|||Phosphoserine; by MAPK14|||Removed in mature form|||S-geranylgeranyl cysteine|||UIM 1|||UIM 2|||VCP/p97-interacting motif (VIM) ^@ http://purl.uniprot.org/annotation/PRO_0000232877|||http://purl.uniprot.org/annotation/PRO_0000444336 http://togogenome.org/gene/10090:Polr3b ^@ http://purl.uniprot.org/uniprot/P59470 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Sequence Conflict|||Zinc Finger ^@ C4-type|||DNA-directed RNA polymerase III subunit RPC2 ^@ http://purl.uniprot.org/annotation/PRO_0000048093 http://togogenome.org/gene/10090:Ctso ^@ http://purl.uniprot.org/uniprot/Q4QQL3|||http://purl.uniprot.org/uniprot/Q8BM88 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cathepsin O|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000026323|||http://purl.uniprot.org/annotation/PRO_0000026324|||http://purl.uniprot.org/annotation/PRO_5018595357 http://togogenome.org/gene/10090:Bhmt ^@ http://purl.uniprot.org/uniprot/O35490 ^@ 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 ^@ Betaine--homocysteine S-methyltransferase 1|||Hcy-binding|||N6-succinyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000114622 http://togogenome.org/gene/10090:Ffar3 ^@ http://purl.uniprot.org/uniprot/Q08AU6|||http://purl.uniprot.org/uniprot/Q3UFD7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Free fatty acid 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|||Loss of SCFA-independent constitutive G protein-coupled receptor activity.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000227783 http://togogenome.org/gene/10090:Kdm5d ^@ http://purl.uniprot.org/uniprot/Q62240 ^@ Binding Site|||Chain|||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|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ARID|||Basic and acidic residues|||C5HC2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||JmjC|||JmjN|||Lysine-specific demethylase 5D|||PHD-type 1|||PHD-type 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000200589|||http://purl.uniprot.org/annotation/VSP_026412|||http://purl.uniprot.org/annotation/VSP_026413|||http://purl.uniprot.org/annotation/VSP_026414|||http://purl.uniprot.org/annotation/VSP_026415|||http://purl.uniprot.org/annotation/VSP_026416 http://togogenome.org/gene/10090:Cd8a ^@ http://purl.uniprot.org/uniprot/P01731|||http://purl.uniprot.org/uniprot/Q8CAX3 ^@ 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|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In strain: C.AKR.|||N-linked (GlcNAc...) asparagine|||Polar residues|||T-cell surface glycoprotein CD8 alpha chain ^@ http://purl.uniprot.org/annotation/PRO_0000014639|||http://purl.uniprot.org/annotation/PRO_5015099101 http://togogenome.org/gene/10090:Psme1 ^@ http://purl.uniprot.org/uniprot/P97371|||http://purl.uniprot.org/uniprot/Q5HZK3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||Disordered|||Proteasome activator PA28 C-terminal|||Proteasome activator PA28 N-terminal|||Proteasome activator complex subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000161781 http://togogenome.org/gene/10090:Nsd1 ^@ http://purl.uniprot.org/uniprot/E9QAE4|||http://purl.uniprot.org/uniprot/Q3UL03 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ AWS|||Basic and acidic residues|||Disordered|||PHD-type|||PWWP|||Polar residues|||Post-SET|||RING-type|||SET ^@ http://togogenome.org/gene/10090:Il1f10 ^@ http://purl.uniprot.org/uniprot/Q8R459 ^@ Chain|||Molecule Processing ^@ Chain ^@ Interleukin-1 family member 10 ^@ http://purl.uniprot.org/annotation/PRO_0000153651 http://togogenome.org/gene/10090:Odc1 ^@ http://purl.uniprot.org/uniprot/P00860 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Strand|||Turn ^@ Loss of activity.|||N6-(pyridoxal phosphate)lysine|||Ornithine decarboxylase|||Partial loss of activity.|||Phosphoserine; by CK2|||Proton donor; shared with dimeric partner|||S-nitrosocysteine|||Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000149892 http://togogenome.org/gene/10090:Acsm2 ^@ http://purl.uniprot.org/uniprot/Q8K0L3 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Acyl-coenzyme A synthetase ACSM2, mitochondrial|||In isoform 2.|||In isoform 3.|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000306095|||http://purl.uniprot.org/annotation/VSP_028393|||http://purl.uniprot.org/annotation/VSP_028394 http://togogenome.org/gene/10090:Pde7a ^@ http://purl.uniprot.org/uniprot/P70453|||http://purl.uniprot.org/uniprot/Q3U3Y7|||http://purl.uniprot.org/uniprot/Q6P5G2 ^@ 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 ^@ High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A|||In isoform 2.|||PDEase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000198834|||http://purl.uniprot.org/annotation/VSP_004594 http://togogenome.org/gene/10090:Cacng8 ^@ http://purl.uniprot.org/uniprot/S4R2F1 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Tex26 ^@ http://purl.uniprot.org/uniprot/Q0VB26 ^@ Chain|||Molecule Processing ^@ Chain ^@ Testis-expressed protein 26 ^@ http://purl.uniprot.org/annotation/PRO_0000263724 http://togogenome.org/gene/10090:Lgr6 ^@ http://purl.uniprot.org/uniprot/Q3UVD5 ^@ 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|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||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_0000303884 http://togogenome.org/gene/10090:Fabp1 ^@ http://purl.uniprot.org/uniprot/P12710|||http://purl.uniprot.org/uniprot/Q3V2F7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Cytosolic fatty-acid binding proteins|||Fatty acid-binding protein, liver|||N-acetylmethionine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000067335 http://togogenome.org/gene/10090:Or5b113 ^@ http://purl.uniprot.org/uniprot/Q8VFW1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Theg ^@ http://purl.uniprot.org/uniprot/Q9JMB1 ^@ 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 ^@ Disordered|||In isoform 2.|||Phosphoserine|||Sperm microtubule associated protein 2|||THEG 1|||THEG 2|||THEG 3|||THEG 4|||THEG 5|||THEG 6|||THEG 7 ^@ http://purl.uniprot.org/annotation/PRO_0000306268|||http://purl.uniprot.org/annotation/VSP_028447 http://togogenome.org/gene/10090:Cstf1 ^@ http://purl.uniprot.org/uniprot/Q99LC2 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ Cleavage stimulation factor subunit 1|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000050945 http://togogenome.org/gene/10090:Or14c39 ^@ http://purl.uniprot.org/uniprot/F8VQ84 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccr1l1 ^@ http://purl.uniprot.org/uniprot/P51676 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C-C chemokine receptor 1-like protein 1|||Cytoplasmic|||Extracellular|||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_0000069298 http://togogenome.org/gene/10090:Agap2 ^@ http://purl.uniprot.org/uniprot/Q3UHD9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||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 2|||Basic and acidic residues|||C4-type|||Disordered|||G domain|||In isoform 2.|||Interaction with EPB41L1|||Interaction with PLCG1|||Interactions with HOMER1 and NF2|||PH|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000235913|||http://purl.uniprot.org/annotation/VSP_018542 http://togogenome.org/gene/10090:Asphd1 ^@ http://purl.uniprot.org/uniprot/Q2TA57 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Splice Variant|||Topological Domain|||Transmembrane ^@ Aspartate beta-hydroxylase domain-containing protein 1|||Cytoplasmic|||Helical|||In isoform 2.|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000394142|||http://purl.uniprot.org/annotation/VSP_039171 http://togogenome.org/gene/10090:Lin9 ^@ http://purl.uniprot.org/uniprot/A0A0A6YVZ7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DIRP|||Disordered ^@ http://togogenome.org/gene/10090:Gm10662 ^@ http://purl.uniprot.org/uniprot/Q3UT86 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Fndc3a ^@ http://purl.uniprot.org/uniprot/Q8BX90 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ 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|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087322 http://togogenome.org/gene/10090:Sirt5 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VM56|||http://purl.uniprot.org/uniprot/Q8K2C6 ^@ 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 ^@ Deacetylase sirtuin-type|||Loss of enzyme activity.|||Mitochondrion|||NAD-dependent protein deacylase sirtuin-5, mitochondrial|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000110267 http://togogenome.org/gene/10090:Mospd1 ^@ http://purl.uniprot.org/uniprot/Q3UT40|||http://purl.uniprot.org/uniprot/Q8VEL0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Localizes to the nucleus instead of the cytoplasm.|||MSP|||Motile sperm domain-containing protein 1|||Nuclear export signal ^@ http://purl.uniprot.org/annotation/PRO_0000213460|||http://purl.uniprot.org/annotation/VSP_014045 http://togogenome.org/gene/10090:Gnas ^@ http://purl.uniprot.org/uniprot/A0A571BEI3|||http://purl.uniprot.org/uniprot/P63094|||http://purl.uniprot.org/uniprot/Q6R0H6|||http://purl.uniprot.org/uniprot/Q6R0H7|||http://purl.uniprot.org/uniprot/Q9Z0F1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant ^@ ADP-ribosylarginine; by cholera toxin|||Abolishes S-palmitoylation.|||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 isoform Gnas-2.|||In isoform Gnas-3.|||In isoform Nesp55-2.|||In isoform XLas-2.|||In isoform XLas-3.|||In isoform XLas-4.|||In unc mutant; uncouples receptors from adenylyl cyclases.|||LHAL tetrapeptide|||N-palmitoyl glycine|||Neuroendocrine secretory protein 55|||Phosphoserine|||Polar residues|||Pro residues|||Protein ALEX|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000203723|||http://purl.uniprot.org/annotation/PRO_0000253965|||http://purl.uniprot.org/annotation/PRO_0000253970|||http://purl.uniprot.org/annotation/PRO_0000253971|||http://purl.uniprot.org/annotation/PRO_0000253972|||http://purl.uniprot.org/annotation/PRO_0000253985|||http://purl.uniprot.org/annotation/VSP_011567|||http://purl.uniprot.org/annotation/VSP_021153|||http://purl.uniprot.org/annotation/VSP_052176|||http://purl.uniprot.org/annotation/VSP_052177|||http://purl.uniprot.org/annotation/VSP_052178|||http://purl.uniprot.org/annotation/VSP_052179|||http://purl.uniprot.org/annotation/VSP_052180|||http://purl.uniprot.org/annotation/VSP_052181 http://togogenome.org/gene/10090:Senp3 ^@ http://purl.uniprot.org/uniprot/Q9EP97 ^@ Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Acidic residues|||Disordered|||Nuclear localization signal|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Protease|||Sentrin-specific protease 3 ^@ http://purl.uniprot.org/annotation/PRO_0000101722 http://togogenome.org/gene/10090:Srp68 ^@ http://purl.uniprot.org/uniprot/Q8BMA6 ^@ 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|||N6-acetyllysine|||Phosphoserine|||RNA-binding|||Required for interaction with SRP72|||Signal recognition particle subunit SRP68 ^@ http://purl.uniprot.org/annotation/PRO_0000135228 http://togogenome.org/gene/10090:Hcst ^@ http://purl.uniprot.org/uniprot/Q9QUJ0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||GRB2 binding site|||Helical|||Hematopoietic cell signal transducer|||In isoform 2.|||PIK3R1 binding site|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000330290|||http://purl.uniprot.org/annotation/VSP_033023 http://togogenome.org/gene/10090:Retsat ^@ http://purl.uniprot.org/uniprot/Q64FW2 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Chain|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ All-trans-retinol 13,14-reductase|||Loss of catalytic activity, as measured by the saturation of retinol to 13,14-dihydroretinol. Loss of adipocyte differentiation in a 3T3-L1 cell culture model.|||Loss of localization to the endoplasmic reticulum. ^@ http://purl.uniprot.org/annotation/PRO_0000225667 http://togogenome.org/gene/10090:Dcaf4 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VNZ0|||http://purl.uniprot.org/uniprot/Q99LF7 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ Disordered|||Polar residues|||WD ^@ http://togogenome.org/gene/10090:Txndc11 ^@ http://purl.uniprot.org/uniprot/Q8K2W3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues|||Redox-active|||Thioredoxin 1|||Thioredoxin 2|||Thioredoxin domain-containing protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000120174|||http://purl.uniprot.org/annotation/VSP_014338|||http://purl.uniprot.org/annotation/VSP_014339 http://togogenome.org/gene/10090:Rmdn2 ^@ http://purl.uniprot.org/uniprot/Q8BSE0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Regulator of microtubule dynamics protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000287506 http://togogenome.org/gene/10090:Defb20 ^@ http://purl.uniprot.org/uniprot/Q30KP3 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 20 ^@ http://purl.uniprot.org/annotation/PRO_0000352705 http://togogenome.org/gene/10090:Cep78 ^@ http://purl.uniprot.org/uniprot/A0A494BA29|||http://purl.uniprot.org/uniprot/Q6IRU7 ^@ 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|||Centrosomal protein of 78 kDa|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000291953 http://togogenome.org/gene/10090:Polr2a ^@ http://purl.uniprot.org/uniprot/P08775 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ 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-[SRNTEVKGN]|||DNA-directed RNA polymerase II subunit RPB1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); by NEDD4|||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-1859; R-1866; R-1873; R-1887; R-1908; R-1922 and R-1936.|||Loss of methylation and dimethylation but no effect on phosphorylation; when associated with S-1838; S-1859; S-1866; S-1873; S-1887; S-1908 and S-1922. Highly decreases methylation and dimethylation; when associated with S-1859; S-1866; S-1873; S-1887; S-1908 and S-1922. Decreases methylation but no effect on dimethylation; when associated with S-1859; S-1866 and S-1887.|||Loss of methylation and dimethylation but no effect on phosphorylation; when associated with S-1838; S-1859; S-1866; S-1873; S-1887; S-1908 and S-1936. Highly decreases methylation and dimethylation; when associated with S-1859; S-1866; S-1873; S-1887; S-1908 and S-1936.|||Loss of methylation and dimethylation but no effect on phosphorylation; when associated with S-1838; S-1859; S-1866; S-1873; S-1887; S-1922 and S-1936. Highly decreases methylation and dimethylation; when associated with S-1859; S-1866; S-1873; S-1887; S-1922 and S-1936. Decreases methylation but no effect on dimethylation; when associated with S-1859; S-1866; S-1887 and S-1936.|||Loss of methylation and dimethylation but no effect on phosphorylation; when associated with S-1838; S-1859; S-1866; S-1873; S-1908; S-1922 and S-1936. Highly decreases methylation and dimethylation; when associated with S-1859; S-1866; S-1873; S-1908; S-1922 and S-1936. Decreases methylation but no effect on dimethylation; when associated with S-1859; S-1866; S-1908 and S-1936.|||Loss of methylation and dimethylation but no effect on phosphorylation; when associated with S-1838; S-1859; S-1866; S-1887; S-1908; S-1922 and S-1936. Highly decreases methylation and dimethylation; when associated with S-1859; S-1866; S-1887; S-1908 and S-1936.|||Loss of methylation and dimethylation but no effect on phosphorylation; when associated with S-1838; S-1859; S-1873; S-1887; S-1908; S-1922 and S-1936. Highly decreases methylation and dimethylation; when associated with S-1859; S-1873; S-1887; S-1908; S-1922 and S-1936. Decreases methylation but no effect on dimethylation; when associated with S-1859; S-1887; S-1908 and S-1936.|||Loss of methylation and dimethylation but no effect on phosphorylation; when associated with S-1838; S-1866; S-1873; S-1887; S-1908; S-1922 and S-1936. Highly decreases methylation and dimethylation; when associated with S-1866; S-1873; S-1887; S-1908; S-1922 and S-1936. Decreases methylation but no effect on dimethylation; when associated with S-1866; S-1887; S-1908 and S-1936.|||Loss of methylation and dimethylation but no effect on phosphorylation; when associated with S-1859; S-1866; S-1873; S-1887; S-1908; S-1922 and S-1936.|||Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1873; R-1887 and R-1908. 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 ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1873; R-1887 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-1922 and R-1936.|||Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; R-1873; 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-1908; R-1922 and R-1936.|||Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; R-1866; 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-1887; R-1908; R-1922 and R-1936.|||Loss of ubiquitination, no effect on interaction with WWP2; when associated with R-1859; 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-1859; R-1859; R-1873; R-1887; R-1908; R-1922 and R-1936.|||Loss of ubiquitination, no effect on interaction with WWP2; when associated with 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-1866; R-1873; R-1887; R-1908; R-1922 and R-1936.|||Mice appear phenotypically normal. Simultaneous knockout of Xpa leads to growth retardation, skeletal abnormalities, cataracts, progressive motor neuron degeneration and death at 5-6 months.|||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_0000073941 http://togogenome.org/gene/10090:Or5g25 ^@ http://purl.uniprot.org/uniprot/Q8VFK2 ^@ 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 5G25 ^@ http://purl.uniprot.org/annotation/PRO_0000150858 http://togogenome.org/gene/10090:Cnga3 ^@ http://purl.uniprot.org/uniprot/A0A0A6YXW9|||http://purl.uniprot.org/uniprot/A0A6H2E2T0|||http://purl.uniprot.org/uniprot/Q9JJZ8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Cyclic nucleotide-binding|||Cyclic nucleotide-gated cation channel alpha-3|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000219318 http://togogenome.org/gene/10090:Myoz1 ^@ http://purl.uniprot.org/uniprot/Q9JK37 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Myozenin-1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000111096 http://togogenome.org/gene/10090:Il24 ^@ http://purl.uniprot.org/uniprot/Q925S4 ^@ Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interleukin-24|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000042240 http://togogenome.org/gene/10090:Gpr143 ^@ http://purl.uniprot.org/uniprot/P70259|||http://purl.uniprot.org/uniprot/Q549B6 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||G-protein coupled receptor 143|||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|||Necessary for its G protein-activation ability and normal distribution of melanosomes|||lysosomal/melanosomal membrane localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000195087 http://togogenome.org/gene/10090:Btd ^@ http://purl.uniprot.org/uniprot/A0A0R4J131|||http://purl.uniprot.org/uniprot/Q8CIF4 ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Biotinidase|||CN hydrolase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000019708|||http://purl.uniprot.org/annotation/PRO_5015044298 http://togogenome.org/gene/10090:Kif5c ^@ http://purl.uniprot.org/uniprot/P28738 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||Globular|||Kinesin heavy chain isoform 5C|||Kinesin motor|||Microtubule-binding|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000125356 http://togogenome.org/gene/10090:Zp3 ^@ http://purl.uniprot.org/uniprot/P10761 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Causes a mild reduction of protein solubility.|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Processed zona pellucida sperm-binding protein 3|||Pyrrolidone carboxylic acid|||Reduces protein solubility and causes formation of an abnormal disulfide bond between C-111 and C-139 in approximately half of the molecules.|||Reduces protein solubility.|||Removed in mature form|||Strongly reduces protein solubility.|||ZP|||Zona pellucida sperm-binding protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000041715|||http://purl.uniprot.org/annotation/PRO_0000041716|||http://purl.uniprot.org/annotation/PRO_0000304572 http://togogenome.org/gene/10090:Cyp1a2 ^@ http://purl.uniprot.org/uniprot/P00186 ^@ Binding Site|||Chain|||Glycosylation Site|||Initiator Methionine|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site ^@ Binding Site|||Chain|||Glycosylation Site|||Initiator Methionine|||Sequence Variant ^@ Cytochrome P450 1A2|||In P2.|||O-linked (GlcNAc) serine|||Removed|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051654 http://togogenome.org/gene/10090:Pbdc1 ^@ http://purl.uniprot.org/uniprot/Q9D0B6 ^@ 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|||Protein PBDC1 ^@ http://purl.uniprot.org/annotation/PRO_0000254106|||http://purl.uniprot.org/annotation/VSP_021180 http://togogenome.org/gene/10090:Lamb3 ^@ http://purl.uniprot.org/uniprot/Q61087|||http://purl.uniprot.org/uniprot/Q8C5B3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Domain I|||Domain II|||Domain alpha|||Interchain|||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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000017072 http://togogenome.org/gene/10090:Or10ak16 ^@ http://purl.uniprot.org/uniprot/Q8VEY6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Arl4a ^@ http://purl.uniprot.org/uniprot/P61213 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding ^@ ADP-ribosylation factor-like protein 4A|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207460 http://togogenome.org/gene/10090:Syndig1l ^@ http://purl.uniprot.org/uniprot/B2RRM8|||http://purl.uniprot.org/uniprot/Q3USQ7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane ^@ Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Synapse differentiation-inducing gene protein 1-like ^@ http://purl.uniprot.org/annotation/PRO_0000332726 http://togogenome.org/gene/10090:Prdm15 ^@ http://purl.uniprot.org/uniprot/E9Q8T2 ^@ 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 ^@ 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; degenerate|||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.|||PR domain zinc finger protein 15|||Polar residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000444718|||http://purl.uniprot.org/annotation/VSP_059647 http://togogenome.org/gene/10090:Tmem121 ^@ http://purl.uniprot.org/uniprot/Q80XA0 ^@ 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_0000251246 http://togogenome.org/gene/10090:Trnp1 ^@ http://purl.uniprot.org/uniprot/Q80ZI1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Pro residues|||TMF-regulated nuclear protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000336089 http://togogenome.org/gene/10090:Mgmt ^@ http://purl.uniprot.org/uniprot/P26187|||http://purl.uniprot.org/uniprot/Q4VA39 ^@ 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|||Methylated-DNA--protein-cysteine methyltransferase|||Methylated-DNA-[protein]-cysteine S-methyltransferase DNA binding|||Methylguanine DNA methyltransferase ribonuclease-like|||Nucleophile; methyl group acceptor|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000139360 http://togogenome.org/gene/10090:Spcs1 ^@ http://purl.uniprot.org/uniprot/Q9D958 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Signal peptidase complex subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000215155 http://togogenome.org/gene/10090:Kcnu1 ^@ http://purl.uniprot.org/uniprot/G3X9P7|||http://purl.uniprot.org/uniprot/O54982 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Calcium-activated potassium channel BK alpha subunit|||Cytoplasmic|||Disordered|||Does not induce any change in single channel conductance or variance in open current levels.|||Extracellular|||Helical|||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|||Homozygous males are infertile. In mutant sperm, the protein is barely detectable by Western blot.|||Ion transport|||Polar residues|||Pore-forming; Name=P region|||Potassium channel subfamily U member 1|||RCK N-terminal|||Segment S1|||Segment S7|||Segment S8|||Segment S9|||Selectivity for potassium ^@ http://purl.uniprot.org/annotation/PRO_0000349188 http://togogenome.org/gene/10090:Vsig2 ^@ http://purl.uniprot.org/uniprot/Q9Z109 ^@ 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|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||V-set and immunoglobulin domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000015005|||http://purl.uniprot.org/annotation/VSP_014120 http://togogenome.org/gene/10090:Izumo1r ^@ http://purl.uniprot.org/uniprot/Q8BUM2|||http://purl.uniprot.org/uniprot/Q8BY83|||http://purl.uniprot.org/uniprot/Q9EQF4 ^@ Chain|||Disulfide Bond|||Domain Extent|||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|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Does not affect ability to promote sperm-egg interaction.|||Folate receptor-like|||Folate receptor-like domain-containing protein|||GPI-anchor amidated glycine|||Impaired ability to promote sperm-egg interaction due to reduced interaction with IZUMO1.|||Important for interaction with IZUMO1|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with IZUMO1.|||Reduced stability of the protein.|||Reduces apparent molecular weight of the protein, in agreement with the loss of one glycosylation site. Abolishes secretion of the extracellular domain; when associated with G-185.|||Reduces apparent molecular weight of the protein, in agreement with the loss of one glycosylation site. Abolishes secretion of the extracellular domain; when associated with Q-73.|||Sperm-egg fusion protein Juno ^@ http://purl.uniprot.org/annotation/PRO_0000332988|||http://purl.uniprot.org/annotation/PRO_0000429473|||http://purl.uniprot.org/annotation/PRO_5004305994|||http://purl.uniprot.org/annotation/PRO_5015099061|||http://purl.uniprot.org/annotation/VSP_033414 http://togogenome.org/gene/10090:Gm3409 ^@ http://purl.uniprot.org/uniprot/A0A0G2JE67|||http://purl.uniprot.org/uniprot/L7N464 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Slc4a1ap ^@ http://purl.uniprot.org/uniprot/E9PX68|||http://purl.uniprot.org/uniprot/E9Q585|||http://purl.uniprot.org/uniprot/Q3UUI2|||http://purl.uniprot.org/uniprot/Q5BKS1 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||FHA|||Polar residues ^@ http://togogenome.org/gene/10090:Phyhd1 ^@ http://purl.uniprot.org/uniprot/Q9DB26 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Phosphothreonine|||Phytanoyl-CoA dioxygenase domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000313634 http://togogenome.org/gene/10090:Opalin ^@ http://purl.uniprot.org/uniprot/Q3USW3|||http://purl.uniprot.org/uniprot/Q7M750 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Impairs cell surface expression.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Opalin|||Required for plasma membrane localization ^@ http://purl.uniprot.org/annotation/PRO_0000072592 http://togogenome.org/gene/10090:Rufy3 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFT8|||http://purl.uniprot.org/uniprot/Q9D394 ^@ 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|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||FYVE-type|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Protein RUFY3|||RUN ^@ http://purl.uniprot.org/annotation/PRO_0000245834|||http://purl.uniprot.org/annotation/VSP_019792|||http://purl.uniprot.org/annotation/VSP_019793|||http://purl.uniprot.org/annotation/VSP_019794 http://togogenome.org/gene/10090:Zbp1 ^@ http://purl.uniprot.org/uniprot/A2APF7|||http://purl.uniprot.org/uniprot/Q9QY24 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Abolished ability to activate pyroptosis, necroptosis and apoptosis (PANoptosis) in response to influenza A virus (IAV) infection in knockin mice.|||Basic and acidic residues|||Disordered|||Does not greatly affect phosphorylation status.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In ZBP1(Zalpha1); no effect. In ZBP1(Zalpha1-Zalpha2); knockin mice are viable and develop mild skin lesions in response to influenza A virus (IAV); mice are protected from the activation of RIPK3 and MLKL as well as the cell death; when associated with 122-D--A-126.|||In ZBP1(Zalpha2); abolished ability to sense influenza A virus (IAV) Z-RNAs. In ZBP1(Zalpha2); knockin mice are viable and develop mild skin lesions in response to influenza A virus (IAV). ZBP1(Zalpha2) knockin mice are protected from the activation of RIPK3 and MLKL as well as the cell death. In ZBP1(Zalpha1-Zalpha2); knockin mice are viable and develop mild skin lesions in response to influenza A virus (IAV); mice are protected from the activation of RIPK3 and MLKL as well as the cell death; when associated with 46-D--A-50.|||In isoform 2.|||In mRHIMA; abolished interaction with RIPK3 and subsequent necroptosis. In ZBP1(Mr1) knockin mice are viable and do not develop skin inflammation in response to lethal dose of influenza A virus (IAV).|||In mRHIMB; does not affect ability to induce necroptosis.|||Polar residues|||RIP homotypic interaction motif (RHIM) 1|||RIP homotypic interaction motif (RHIM) 2|||Z-DNA-binding protein 1|||Z-binding|||Z-binding 1|||Z-binding 2 ^@ http://purl.uniprot.org/annotation/PRO_0000066565|||http://purl.uniprot.org/annotation/VSP_004083|||http://purl.uniprot.org/annotation/VSP_004084 http://togogenome.org/gene/10090:Eras ^@ http://purl.uniprot.org/uniprot/Q0VEC9|||http://purl.uniprot.org/uniprot/Q7TN89 ^@ 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 ^@ Cysteine methyl ester|||Disordered|||Effector region|||GTPase ERas|||Polar residues|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000247540|||http://purl.uniprot.org/annotation/PRO_0000247541 http://togogenome.org/gene/10090:Smim35 ^@ http://purl.uniprot.org/uniprot/E9Q2Z6 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Small integral membrane protein 35 ^@ http://purl.uniprot.org/annotation/PRO_0000443402 http://togogenome.org/gene/10090:Fut9 ^@ http://purl.uniprot.org/uniprot/O88819|||http://purl.uniprot.org/uniprot/Q14AE3 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9|||Cytoplasmic|||Fucosyltransferase N-terminal|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000221119 http://togogenome.org/gene/10090:Oxct2a ^@ http://purl.uniprot.org/uniprot/Q9JJN4 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Chain|||Region|||Transit Peptide ^@ 5-glutamyl coenzyme A thioester intermediate|||Disordered|||Mitochondrion|||Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000366209 http://togogenome.org/gene/10090:Csf3r ^@ http://purl.uniprot.org/uniprot/P40223 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Signal Peptide|||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|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010875 http://togogenome.org/gene/10090:Aagab ^@ http://purl.uniprot.org/uniprot/Q8R2R3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Alpha- and gamma-adaptin-binding protein p34|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000058135 http://togogenome.org/gene/10090:Adrm1 ^@ http://purl.uniprot.org/uniprot/Q9JKV1 ^@ 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|||Polar residues|||Proteasomal ubiquitin receptor ADRM1|||Pru|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000020632 http://togogenome.org/gene/10090:Eif1ad7 ^@ http://purl.uniprot.org/uniprot/Q8BX20 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||S1-like ^@ http://togogenome.org/gene/10090:Mmp9 ^@ http://purl.uniprot.org/uniprot/P41245 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ Activation peptide|||Cysteine switch|||Disordered|||Fibronectin type-II 1|||Fibronectin type-II 2|||Fibronectin type-II 3|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Matrix metalloproteinase-9|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028758|||http://purl.uniprot.org/annotation/PRO_0000028759 http://togogenome.org/gene/10090:Ptx4 ^@ http://purl.uniprot.org/uniprot/A0A3B2WCG1|||http://purl.uniprot.org/uniprot/E9QNW3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5003246305|||http://purl.uniprot.org/annotation/PRO_5017210949 http://togogenome.org/gene/10090:Mterf2 ^@ http://purl.uniprot.org/uniprot/Q8BKY8 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||Transcription termination factor 2, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000255465 http://togogenome.org/gene/10090:Rtn4ip1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0S3|||http://purl.uniprot.org/uniprot/Q924D0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide ^@ Enoyl reductase (ER)|||Mitochondrion|||Reticulon-4-interacting protein 1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000042115 http://togogenome.org/gene/10090:Phkb ^@ http://purl.uniprot.org/uniprot/Q7TSH2 ^@ Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Lipid Binding|||Modified Residue|||Region ^@ Calmodulin-binding|||Phosphorylase b kinase regulatory subunit beta|||Phosphoserine|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000057737 http://togogenome.org/gene/10090:Sgpp1 ^@ http://purl.uniprot.org/uniprot/Q3UDY2|||http://purl.uniprot.org/uniprot/Q9JI99 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Nucleophile|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Phosphatidic acid phosphatase type 2/haloperoxidase|||Phosphoserine|||Phosphothreonine|||Proton donor|||Sphingosine-1-phosphate phosphatase 1|||Stabilizes the active site histidine for nucleophilic attack ^@ http://purl.uniprot.org/annotation/PRO_0000114478 http://togogenome.org/gene/10090:Lhfpl2 ^@ http://purl.uniprot.org/uniprot/Q8BGA2 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane ^@ Chain|||Sequence Variant|||Transmembrane ^@ Causes malformations in the distal reproductive tract development in both female and male.|||Helical|||LHFPL tetraspan subfamily member 2 protein ^@ http://purl.uniprot.org/annotation/PRO_0000244764 http://togogenome.org/gene/10090:Tlr3 ^@ http://purl.uniprot.org/uniprot/Q99MB1 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||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 21|||LRR 22|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||TIR|||Toll-like receptor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000034716 http://togogenome.org/gene/10090:Cdc25b ^@ http://purl.uniprot.org/uniprot/P30306|||http://purl.uniprot.org/uniprot/Q3U535|||http://purl.uniprot.org/uniprot/Q9DBN8 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||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_0000198645 http://togogenome.org/gene/10090:Tsx ^@ http://purl.uniprot.org/uniprot/P70675|||http://purl.uniprot.org/uniprot/Q78Z65 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Testis-specific protein TSX ^@ http://purl.uniprot.org/annotation/PRO_0000065672 http://togogenome.org/gene/10090:Or3a1 ^@ http://purl.uniprot.org/uniprot/Q8VFX7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:B3galt1 ^@ http://purl.uniprot.org/uniprot/O54904 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Beta-1,3-galactosyltransferase 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In strain: 129/SvJ.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219146 http://togogenome.org/gene/10090:Lcn5 ^@ http://purl.uniprot.org/uniprot/A2AJB7 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Signal Peptide|||Splice Variant ^@ Epididymal-specific lipocalin-5, major form|||Epididymal-specific lipocalin-5, minor form|||In isoform 2.|||In isoform 3.|||In isoform 4. ^@ http://purl.uniprot.org/annotation/PRO_0000339292|||http://purl.uniprot.org/annotation/PRO_0000339293|||http://purl.uniprot.org/annotation/VSP_052838|||http://purl.uniprot.org/annotation/VSP_052839|||http://purl.uniprot.org/annotation/VSP_052840 http://togogenome.org/gene/10090:H2-Q10 ^@ http://purl.uniprot.org/uniprot/P01898 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Extracellular|||H-2 class I histocompatibility antigen, Q10 alpha chain|||Helical|||Ig-like C1-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000018936 http://togogenome.org/gene/10090:Cks1b ^@ http://purl.uniprot.org/uniprot/P61025 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Cyclin-dependent kinases regulatory subunit 1|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000206236 http://togogenome.org/gene/10090:Gjc1 ^@ http://purl.uniprot.org/uniprot/A0A654IER4|||http://purl.uniprot.org/uniprot/P28229 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||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_0000057827 http://togogenome.org/gene/10090:Slc26a4 ^@ http://purl.uniprot.org/uniprot/Q9R155 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Helical|||Pendrin|||STAS ^@ http://purl.uniprot.org/annotation/PRO_0000080165 http://togogenome.org/gene/10090:Ube2t ^@ http://purl.uniprot.org/uniprot/Q9CQ37 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||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)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl thioester intermediate|||Phosphoserine|||UBC core|||Ubiquitin-conjugating enzyme E2 T ^@ http://purl.uniprot.org/annotation/PRO_0000082510 http://togogenome.org/gene/10090:Cep44 ^@ http://purl.uniprot.org/uniprot/Q5HZK1 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict ^@ Binds with microtubules and centrioles|||Centrosomal protein of 44 kDa ^@ http://purl.uniprot.org/annotation/PRO_0000293724 http://togogenome.org/gene/10090:Aplnr ^@ http://purl.uniprot.org/uniprot/Q9WV08 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Apelin 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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069175 http://togogenome.org/gene/10090:Wapl ^@ http://purl.uniprot.org/uniprot/B7ZP47|||http://purl.uniprot.org/uniprot/Q65Z40 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||FGF motif 1|||FGF motif 2|||FGF motif 3|||Mediates interaction with the cohesin complex|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WAPL|||Wings apart-like protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000245233 http://togogenome.org/gene/10090:Tmprss11e ^@ http://purl.uniprot.org/uniprot/Q5S248 ^@ 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 11E catalytic chain|||Transmembrane protease serine 11E non-catalytic chain ^@ http://purl.uniprot.org/annotation/PRO_0000027893|||http://purl.uniprot.org/annotation/PRO_0000027894 http://togogenome.org/gene/10090:Mink1 ^@ http://purl.uniprot.org/uniprot/G3X9G2|||http://purl.uniprot.org/uniprot/Q5SXG3|||http://purl.uniprot.org/uniprot/Q7TT13|||http://purl.uniprot.org/uniprot/Q9JM52 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||CNH|||Disordered|||In isoform 1.|||In isoform 3.|||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_0000086330|||http://purl.uniprot.org/annotation/VSP_007061|||http://purl.uniprot.org/annotation/VSP_007062 http://togogenome.org/gene/10090:Sh3rf2 ^@ http://purl.uniprot.org/uniprot/Q8BZT2 ^@ 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 ^@ Disordered|||E3 ubiquitin-protein ligase SH3RF2|||In isoform 2.|||Interaction with PAK4|||Interaction with PPP1CA|||Phosphoserine|||Polar residues|||RING-type|||SH3 1|||SH3 2|||SH3 3 ^@ http://purl.uniprot.org/annotation/PRO_0000269513|||http://purl.uniprot.org/annotation/VSP_022060 http://togogenome.org/gene/10090:Agfg2 ^@ http://purl.uniprot.org/uniprot/Q3U2K8|||http://purl.uniprot.org/uniprot/Q80WC7 ^@ 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 ^@ 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_0000204829|||http://purl.uniprot.org/annotation/VSP_010669|||http://purl.uniprot.org/annotation/VSP_010670 http://togogenome.org/gene/10090:Snx6 ^@ http://purl.uniprot.org/uniprot/Q6P8X1 ^@ 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|||Region|||Sequence Conflict ^@ BAR|||Interaction with PIM1|||Membrane-binding amphipathic helix|||N-acetylmethionine|||N-acetylmethionine; in Sorting nexin-6, N-terminally processed|||PX|||Phosphoserine|||Removed; alternate|||Sorting nexin-6|||Sorting nexin-6, N-terminally processed ^@ http://purl.uniprot.org/annotation/PRO_0000236198|||http://purl.uniprot.org/annotation/PRO_0000423278 http://togogenome.org/gene/10090:Pnma8a ^@ http://purl.uniprot.org/uniprot/Q80VM8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Paraneoplastic antigen-like protein 8A ^@ http://purl.uniprot.org/annotation/PRO_0000325838 http://togogenome.org/gene/10090:Pramel7 ^@ http://purl.uniprot.org/uniprot/Q810Y8 ^@ 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|||Preferentially expressed antigen in melanoma-like protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000440672 http://togogenome.org/gene/10090:Gm8267 ^@ http://purl.uniprot.org/uniprot/E9PW76 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Srgap3 ^@ http://purl.uniprot.org/uniprot/E9QN14|||http://purl.uniprot.org/uniprot/F8VPQ4|||http://purl.uniprot.org/uniprot/Q812A2|||http://purl.uniprot.org/uniprot/Q91Z68 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||F-BAR|||Phosphoserine|||Polar residues|||Rho-GAP|||SH3|||SLIT-ROBO Rho GTPase-activating protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000056770 http://togogenome.org/gene/10090:Dennd2a ^@ http://purl.uniprot.org/uniprot/Q8C4S8 ^@ 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|||DENN domain-containing protein 2A|||Disordered|||Phosphoserine|||Polar residues|||Pro residues|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000242683 http://togogenome.org/gene/10090:Or5ac20 ^@ http://purl.uniprot.org/uniprot/Q8VGQ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Spring1 ^@ http://purl.uniprot.org/uniprot/Q8BTG6 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||SREBP regulating gene protein ^@ http://purl.uniprot.org/annotation/PRO_0000294330 http://togogenome.org/gene/10090:Eml3 ^@ http://purl.uniprot.org/uniprot/Q8VC03 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Disordered|||Echinoderm microtubule-associated protein-like 3|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine; by CDK1|||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_0000284391 http://togogenome.org/gene/10090:B3gnt8 ^@ http://purl.uniprot.org/uniprot/Q8R3I9 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8 ^@ http://purl.uniprot.org/annotation/PRO_0000306382 http://togogenome.org/gene/10090:Tekt2 ^@ http://purl.uniprot.org/uniprot/Q922G7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Sequence Conflict ^@ Tektin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000184566 http://togogenome.org/gene/10090:Zc3h4 ^@ http://purl.uniprot.org/uniprot/E9Q8K8|||http://purl.uniprot.org/uniprot/Q6ISX3|||http://purl.uniprot.org/uniprot/Q6PAI8|||http://purl.uniprot.org/uniprot/Q6ZPZ3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Zinc finger CCCH domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000234069|||http://purl.uniprot.org/annotation/VSP_018209 http://togogenome.org/gene/10090:Tas2r113 ^@ http://purl.uniprot.org/uniprot/Q7M711 ^@ 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 113 ^@ http://purl.uniprot.org/annotation/PRO_0000248256 http://togogenome.org/gene/10090:Espnl ^@ http://purl.uniprot.org/uniprot/Q3UYR4 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Region|||Repeat ^@ ANK 1|||ANK 10|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Disordered|||Espin-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000312512 http://togogenome.org/gene/10090:Fzd5 ^@ http://purl.uniprot.org/uniprot/Q9EQD0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||PDZ-binding ^@ http://purl.uniprot.org/annotation/PRO_0000243936 http://togogenome.org/gene/10090:Rbm48 ^@ http://purl.uniprot.org/uniprot/H9H9R8|||http://purl.uniprot.org/uniprot/Q8K2X2 ^@ 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.|||RNA-binding protein 48|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000321515|||http://purl.uniprot.org/annotation/VSP_031785 http://togogenome.org/gene/10090:Ncbp1 ^@ http://purl.uniprot.org/uniprot/Q3UYV9 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000239779 http://togogenome.org/gene/10090:Vmn1r175 ^@ http://purl.uniprot.org/uniprot/K7N6T9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Alpk1 ^@ http://purl.uniprot.org/uniprot/E9QNX4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Alpha-type protein kinase|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Vmn1r228 ^@ http://purl.uniprot.org/uniprot/Q8R2A7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ofcc1 ^@ http://purl.uniprot.org/uniprot/C3S7Q5 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Mafb ^@ http://purl.uniprot.org/uniprot/P54841 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Turn ^@ Basic motif|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Leucine-zipper|||Loss of SUMO modification, increases transactivation activity, increases macrophage differentiation and inhibits myeloid progenitor growth; when associated with R-297.|||Loss of SUMO modification, increases transactivation activity, increases macrophage differentiation and inhibits myeloid progenitor growth; when associated with R-32.|||Loss of transcriptional activity.|||Polar residues|||Reduces ability to activate insulin and glucagon gene expression.|||Transcription factor MafB|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076495 http://togogenome.org/gene/10090:Chd1l ^@ http://purl.uniprot.org/uniprot/Q9CXF7 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Chromodomain-helicase-DNA-binding protein 1-like|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Macro|||Phosphoserine|||Regulatory linker segment (RLS)|||Required for ATPase activity ^@ http://purl.uniprot.org/annotation/PRO_0000332142|||http://purl.uniprot.org/annotation/VSP_033343 http://togogenome.org/gene/10090:1110065P20Rik ^@ http://purl.uniprot.org/uniprot/B1ARW8|||http://purl.uniprot.org/uniprot/E9Q9M4 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Disordered|||Uncharacterized protein C1orf122 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000385169 http://togogenome.org/gene/10090:Sec61g ^@ http://purl.uniprot.org/uniprot/G3UWH0|||http://purl.uniprot.org/uniprot/P60060|||http://purl.uniprot.org/uniprot/Q5SWJ8 ^@ 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_0000104196 http://togogenome.org/gene/10090:Gsdma3 ^@ http://purl.uniprot.org/uniprot/A0A679AUV5|||http://purl.uniprot.org/uniprot/Q5Y4Y6 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand|||Transmembrane|||Turn ^@ Abolished ability to form a pore.|||Beta stranded|||Gain-of-function mutation; causes an alopecia phenotype.|||Gasdermin PUB|||Gasdermin pore forming|||Gasdermin-A3|||Gasdermin-A3, C-terminal|||Gasdermin-A3, N-terminal|||Impaired ability to induce pyroptosis; when associated with A-132.|||Impaired pore-formation.|||In AE mutant; gain-of-function mutation; causes an alopecia phenotype; constitutively active in triggering cell death. Mice also display hypoplastic mammary glands, impairing lactation function.|||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.|||In Bsk mutant; gain-of-function mutation; causes an alopecia phenotype. Attenuates intramolecular interaction between the N- and C-terminal domains, hence may relieve autoinhibition; constitutively active in triggering pyroptosis.|||In Dfl mutant; gain-of-function mutation; causes an alopecia phenotype.|||In Fgn mutant; gain-of-function mutation; causes an alopecia phenotype. Attenuates intramolecular interaction between the N- and C-terminal domains, hence may relieve autoinhibition; constitutively active in triggering pyroptosis.|||In Rco2 mutant; gain-of-function mutation; causes an alopecia phenotype. Attenuates intramolecular interaction between the N- and C-terminal domains, hence may relieve autoinhibition; constitutively active in triggering pyroptosis.|||In Re-den mutant; gain-of-function mutation; causes an alopecia phenotype. Attenuates intramolecular interaction between the N- and C-terminal domains, hence may relieve autoinhibition; constitutively active in triggering pyroptosis.|||In Rim3 mutant; gain-of-function mutation; causes an alopecia phenotype. Attenuates intramolecular interaction between the N- and C-terminal domains, hence may relieve autoinhibition; constitutively active in triggering pyroptosis.|||Markedly decreased induction of pyroptosis and defects in liposome-binding. No spontaneous pyroptosis-inducing activity; when associated with K-14.|||No spontaneous pyroptosis-inducing activity; when associated with D-184.|||Spontaneous pyroptosis-inducing activity.|||Triggers pyroptosis|||Weak or no effect on ability to induce pyroptosis. Impaired ability to induce pyroptosis; when associated with A-145. ^@ http://purl.uniprot.org/annotation/PRO_0000347272|||http://purl.uniprot.org/annotation/PRO_0000451670|||http://purl.uniprot.org/annotation/PRO_0000451671 http://togogenome.org/gene/10090:Zfp595 ^@ http://purl.uniprot.org/uniprot/Q3UWJ2|||http://purl.uniprot.org/uniprot/Q8BIN6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Def6 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZX1|||http://purl.uniprot.org/uniprot/Q8C2K1 ^@ 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|||Differentially expressed in FDCP 6|||Disordered|||In isoform 2.|||N6-acetyllysine|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000294523|||http://purl.uniprot.org/annotation/VSP_026671 http://togogenome.org/gene/10090:S100a10 ^@ http://purl.uniprot.org/uniprot/P08207|||http://purl.uniprot.org/uniprot/Q3TC45 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Transmembrane ^@ Ancestral calcium site|||EF-hand|||Helical|||N6-acetyllysine|||Protein S100-A10 ^@ http://purl.uniprot.org/annotation/PRO_0000144004 http://togogenome.org/gene/10090:Clec4b2 ^@ http://purl.uniprot.org/uniprot/Q67DU8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Dach2 ^@ http://purl.uniprot.org/uniprot/B1AU60|||http://purl.uniprot.org/uniprot/B1AXA6|||http://purl.uniprot.org/uniprot/Q925Q8 ^@ 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 ^@ DACHbox-C|||DACHbox-N|||Dachshund homolog 2|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000095600|||http://purl.uniprot.org/annotation/VSP_009493|||http://purl.uniprot.org/annotation/VSP_009494|||http://purl.uniprot.org/annotation/VSP_009495|||http://purl.uniprot.org/annotation/VSP_009496|||http://purl.uniprot.org/annotation/VSP_009497 http://togogenome.org/gene/10090:Ogdhl ^@ http://purl.uniprot.org/uniprot/B2RXT3|||http://purl.uniprot.org/uniprot/E9Q7L0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Transketolase-like pyrimidine-binding ^@ http://togogenome.org/gene/10090:Itga1 ^@ http://purl.uniprot.org/uniprot/Q3V3R4|||http://purl.uniprot.org/uniprot/Q8BPT3 ^@ 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 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_0000273722 http://togogenome.org/gene/10090:Syce1 ^@ http://purl.uniprot.org/uniprot/Q9D495 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Synaptonemal complex central element protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000261428 http://togogenome.org/gene/10090:Cavin2 ^@ http://purl.uniprot.org/uniprot/Q63918 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Caveolae-associated protein 2|||Disordered|||Interaction with CAVIN1|||Leucine-zipper|||N-acetylglycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000238919 http://togogenome.org/gene/10090:Uck1 ^@ http://purl.uniprot.org/uniprot/A2AN37|||http://purl.uniprot.org/uniprot/P52623|||http://purl.uniprot.org/uniprot/Q3V218 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ Disordered|||Phosphoribulokinase/uridine kinase|||Phosphothreonine|||Uridine-cytidine kinase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000164454 http://togogenome.org/gene/10090:Mtarc2 ^@ http://purl.uniprot.org/uniprot/Q922Q1 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||MOSC|||Mitochondrial amidoxime reducing component 2|||Mitochondrion|||N6-acetyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000273342 http://togogenome.org/gene/10090:Adamts5 ^@ http://purl.uniprot.org/uniprot/Q8BGP4|||http://purl.uniprot.org/uniprot/Q9R001 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ A disintegrin and metalloproteinase with thrombospondin motifs 5|||C-linked (Man) tryptophan|||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_0000029172|||http://purl.uniprot.org/annotation/PRO_0000029173 http://togogenome.org/gene/10090:Cyp2b9 ^@ http://purl.uniprot.org/uniprot/P12790 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Cytochrome P450 2B9|||Phosphoserine; by PKA|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051684 http://togogenome.org/gene/10090:Anks6 ^@ http://purl.uniprot.org/uniprot/E9PUD3 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ ANK|||Disordered|||Polar residues|||SAM ^@ http://togogenome.org/gene/10090:Fbxw14 ^@ http://purl.uniprot.org/uniprot/Q4FZL9|||http://purl.uniprot.org/uniprot/Q8C2Y5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Tnfrsf11b ^@ http://purl.uniprot.org/uniprot/O08712|||http://purl.uniprot.org/uniprot/Q3UK97 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Strand ^@ Death|||Death 1|||Death 2|||In strain: 129/Ola and NIHSwiss.|||Involved in dimerization|||N-linked (GlcNAc...) asparagine|||TNFR-Cys|||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_0000034588|||http://purl.uniprot.org/annotation/PRO_5010843442 http://togogenome.org/gene/10090:Rbpms2 ^@ http://purl.uniprot.org/uniprot/Q8VC52 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Important for homodimerization|||N-acetylserine|||RNA-binding protein with multiple splicing 2|||RRM|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000274910 http://togogenome.org/gene/10090:Ercc5 ^@ http://purl.uniprot.org/uniprot/E9QM61|||http://purl.uniprot.org/uniprot/Q3UV64 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||XPG N-terminal|||XPG-I ^@ http://togogenome.org/gene/10090:Psmd11 ^@ http://purl.uniprot.org/uniprot/Q3UWW9|||http://purl.uniprot.org/uniprot/Q5BKQ9|||http://purl.uniprot.org/uniprot/Q8BG32 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ 26S proteasome non-ATPase regulatory subunit 11|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||PCI|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000173858 http://togogenome.org/gene/10090:Lrtm2 ^@ http://purl.uniprot.org/uniprot/Q8BGX3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||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_0000263687 http://togogenome.org/gene/10090:Bspry ^@ http://purl.uniprot.org/uniprot/B2RT02|||http://purl.uniprot.org/uniprot/Q80YW5 ^@ 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 ^@ B box and SPRY domain-containing protein|||B box-type|||B30.2/SPRY|||Basic and acidic residues|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000244258|||http://purl.uniprot.org/annotation/VSP_019529 http://togogenome.org/gene/10090:Rad21l ^@ http://purl.uniprot.org/uniprot/A2AU37 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Double-strand-break repair protein rad21-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000321922 http://togogenome.org/gene/10090:Zfp592 ^@ http://purl.uniprot.org/uniprot/Q52KI9|||http://purl.uniprot.org/uniprot/Q8BG03|||http://purl.uniprot.org/uniprot/Q8BHZ4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type|||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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||Phosphoserine|||Polar residues|||Zinc finger protein 592 ^@ http://purl.uniprot.org/annotation/PRO_0000047683 http://togogenome.org/gene/10090:Crybb1 ^@ http://purl.uniprot.org/uniprot/Q9WVJ5 ^@ 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 ^@ Beta-crystallin B1|||Beta-crystallin B1B|||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|||N-acetylserine|||N-terminal arm|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000006337|||http://purl.uniprot.org/annotation/PRO_0000006338 http://togogenome.org/gene/10090:Nsdhl ^@ http://purl.uniprot.org/uniprot/Q3US15|||http://purl.uniprot.org/uniprot/Q9R1J0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Variant|||Transmembrane ^@ 3-beta hydroxysteroid dehydrogenase/isomerase|||Helical|||In bpa.|||In bpa; does not rescue the yeast mutant lacking the ortholog erg26.|||In str; does not rescue the yeast mutant lacking the ortholog erg26.|||In str; rescues the yeast mutant lacking the ortholog erg26.|||N-acetylmethionine|||Prevents secretion from ER|||Proton acceptor|||Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating ^@ http://purl.uniprot.org/annotation/PRO_0000087800 http://togogenome.org/gene/10090:Tagln ^@ http://purl.uniprot.org/uniprot/P37804 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ Calponin-homology (CH)|||Calponin-like|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Removed|||Transgelin ^@ http://purl.uniprot.org/annotation/PRO_0000204782 http://togogenome.org/gene/10090:4933411K16Rik ^@ http://purl.uniprot.org/uniprot/Q80Y39 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Uncharacterized protein C10orf62 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000274242 http://togogenome.org/gene/10090:Vmn1r40 ^@ http://purl.uniprot.org/uniprot/Q9EQ46 ^@ 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|||Vomeronasal type-1 receptor 40 ^@ http://purl.uniprot.org/annotation/PRO_0000239979 http://togogenome.org/gene/10090:Akap9 ^@ http://purl.uniprot.org/uniprot/E9QQ10|||http://purl.uniprot.org/uniprot/Q70FJ1 ^@ 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 ^@ A-kinase anchor protein 9|||Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||PKA-RII subunit binding domain|||Pericentrin/AKAP-450 centrosomal targeting|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000395481|||http://purl.uniprot.org/annotation/VSP_039481|||http://purl.uniprot.org/annotation/VSP_039482 http://togogenome.org/gene/10090:Nptx1 ^@ http://purl.uniprot.org/uniprot/A2ACL9|||http://purl.uniprot.org/uniprot/Q3UST4|||http://purl.uniprot.org/uniprot/Q62443 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Neuronal pentraxin-1|||Pentraxin (PTX)|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000023548|||http://purl.uniprot.org/annotation/PRO_5014296786 http://togogenome.org/gene/10090:Mrpl4 ^@ http://purl.uniprot.org/uniprot/Q9DCU6 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Large ribosomal subunit protein uL4m|||Omega-N-methylarginine ^@ http://purl.uniprot.org/annotation/PRO_0000238950 http://togogenome.org/gene/10090:Samd7 ^@ http://purl.uniprot.org/uniprot/Q8C8Y5 ^@ 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.|||SAM|||Sterile alpha motif domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000263103|||http://purl.uniprot.org/annotation/VSP_059092|||http://purl.uniprot.org/annotation/VSP_059093 http://togogenome.org/gene/10090:Zmat4 ^@ http://purl.uniprot.org/uniprot/Q8BZ94 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Splice Variant|||Zinc Finger ^@ In isoform 2.|||In isoform 3.|||Matrin-type 1|||Matrin-type 2|||Matrin-type 3|||Matrin-type 4|||Zinc finger matrin-type protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000298917|||http://purl.uniprot.org/annotation/VSP_027477|||http://purl.uniprot.org/annotation/VSP_027478 http://togogenome.org/gene/10090:Dpy19l4 ^@ http://purl.uniprot.org/uniprot/A2AJQ3 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||N-acetylalanine|||Probable C-mannosyltransferase DPY19L4|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000311882|||http://purl.uniprot.org/annotation/VSP_029632 http://togogenome.org/gene/10090:Crnkl1 ^@ http://purl.uniprot.org/uniprot/P63154 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Modified Residue|||Motif|||Region|||Repeat ^@ Crooked neck-like protein 1|||Disordered|||HAT 1|||HAT 10|||HAT 11|||HAT 12|||HAT 13|||HAT 14|||HAT 15|||HAT 16|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||HAT 6|||HAT 7|||HAT 8|||HAT 9|||Mediates interaction with HSP90|||Nuclear localization signal|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000205720 http://togogenome.org/gene/10090:Or6c7 ^@ http://purl.uniprot.org/uniprot/A0A1L1SV77 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp330 ^@ http://purl.uniprot.org/uniprot/Q922H9 ^@ 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 ^@ Acidic residues|||C4-type 1|||C4-type 2|||C4-type 3|||C4-type 4|||Disordered|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Zinc finger protein 330 ^@ http://purl.uniprot.org/annotation/PRO_0000066591|||http://purl.uniprot.org/annotation/VSP_011428 http://togogenome.org/gene/10090:Gzme ^@ http://purl.uniprot.org/uniprot/P08884 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Granzyme E|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027407|||http://purl.uniprot.org/annotation/PRO_0000027408 http://togogenome.org/gene/10090:H2bc1 ^@ http://purl.uniprot.org/uniprot/P70696 ^@ Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand ^@ Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Strand ^@ Dimethylated arginine|||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_0000071843 http://togogenome.org/gene/10090:Ctsq ^@ http://purl.uniprot.org/uniprot/Q91ZF4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Cathepsin propeptide inhibitor|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_5015020135 http://togogenome.org/gene/10090:Hrnr ^@ http://purl.uniprot.org/uniprot/E9QNP3|||http://purl.uniprot.org/uniprot/F8WJ23|||http://purl.uniprot.org/uniprot/Q8BLX1 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||EF-hand|||Polar residues ^@ http://togogenome.org/gene/10090:Sem1 ^@ http://purl.uniprot.org/uniprot/P60897 ^@ Chain|||Molecule Processing ^@ Chain ^@ 26S proteasome complex subunit SEM1 ^@ http://purl.uniprot.org/annotation/PRO_0000122962 http://togogenome.org/gene/10090:Cyp2c38 ^@ http://purl.uniprot.org/uniprot/P56655 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Sequence Conflict|||Signal Peptide ^@ Cytochrome P450 2C38|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051721 http://togogenome.org/gene/10090:Alkal2 ^@ http://purl.uniprot.org/uniprot/Q80UG6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ ALK and LTK ligand 2 ^@ http://purl.uniprot.org/annotation/PRO_0000353120 http://togogenome.org/gene/10090:Insl5 ^@ http://purl.uniprot.org/uniprot/A2AIY3|||http://purl.uniprot.org/uniprot/Q9WUG6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Propeptide|||Signal Peptide ^@ Connecting peptide|||Insulin-like|||Insulin-like peptide INSL5 A chain|||Insulin-like peptide INSL5 B chain|||Interchain (between B and A chains) ^@ http://purl.uniprot.org/annotation/PRO_0000016166|||http://purl.uniprot.org/annotation/PRO_0000016167|||http://purl.uniprot.org/annotation/PRO_0000016168|||http://purl.uniprot.org/annotation/PRO_5015086022 http://togogenome.org/gene/10090:Nrsn1 ^@ http://purl.uniprot.org/uniprot/P97799 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Neurensin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000270584 http://togogenome.org/gene/10090:Ift20 ^@ http://purl.uniprot.org/uniprot/Q61025 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Region|||Splice Variant ^@ IFT57-binding|||In isoform 2.|||Intraflagellar transport protein 20 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000249304|||http://purl.uniprot.org/annotation/VSP_020392 http://togogenome.org/gene/10090:Pde6a ^@ http://purl.uniprot.org/uniprot/Q8K0A8 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PDEase|||Polar residues|||Proton donor ^@ http://togogenome.org/gene/10090:Mbd1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J159|||http://purl.uniprot.org/uniprot/Q9Z2E2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||CXXC-type|||CXXC-type 1|||CXXC-type 2|||CXXC-type 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|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3 and isoform 5.|||MBD|||Methyl-CpG-binding domain protein 1|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Transcriptional repression domain (TRD) ^@ http://purl.uniprot.org/annotation/PRO_0000096259|||http://purl.uniprot.org/annotation/VSP_011072|||http://purl.uniprot.org/annotation/VSP_011073|||http://purl.uniprot.org/annotation/VSP_011074|||http://purl.uniprot.org/annotation/VSP_011075 http://togogenome.org/gene/10090:Gm3604 ^@ http://purl.uniprot.org/uniprot/A0A087WPN2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Atp6v0a4 ^@ http://purl.uniprot.org/uniprot/Q3UP55|||http://purl.uniprot.org/uniprot/Q920R6 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||V-type proton ATPase 116 kDa subunit a 4|||Vacuolar ^@ http://purl.uniprot.org/annotation/PRO_0000119220 http://togogenome.org/gene/10090:Fbrs ^@ http://purl.uniprot.org/uniprot/Q8R089 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Pro residues|||Probable fibrosin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000087207 http://togogenome.org/gene/10090:Spem1 ^@ http://purl.uniprot.org/uniprot/Q5F289 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Spermatid maturation protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000307807 http://togogenome.org/gene/10090:Eif4e3 ^@ http://purl.uniprot.org/uniprot/Q9DBB5 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||Eukaryotic translation initiation factor 4E type 3 ^@ http://purl.uniprot.org/annotation/PRO_0000287698 http://togogenome.org/gene/10090:Wnt3 ^@ http://purl.uniprot.org/uniprot/A2A649|||http://purl.uniprot.org/uniprot/P17553 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt|||Proto-oncogene Wnt-3 ^@ http://purl.uniprot.org/annotation/PRO_0000041417|||http://purl.uniprot.org/annotation/PRO_5014296783 http://togogenome.org/gene/10090:Utp15 ^@ http://purl.uniprot.org/uniprot/Q8C7V3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000051322 http://togogenome.org/gene/10090:Pkp2 ^@ http://purl.uniprot.org/uniprot/Q9CQ73 ^@ 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 ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Plakophilin-2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000456831 http://togogenome.org/gene/10090:Tbk1 ^@ http://purl.uniprot.org/uniprot/A1L361|||http://purl.uniprot.org/uniprot/Q9WUN2 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with AZI2, TANK and TBKBP1|||Phosphoserine|||Phosphoserine; by autocatalysis and IKKB|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase TBK1|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000086744 http://togogenome.org/gene/10090:Ranbp9 ^@ http://purl.uniprot.org/uniprot/E9Q5D6|||http://purl.uniprot.org/uniprot/P69566 ^@ 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 ^@ B30.2/SPRY|||CTLH|||Disordered|||In isoform 2.|||Interaction with CALB1|||Interaction with FMR1|||LisH|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||Ran-binding protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000097170|||http://purl.uniprot.org/annotation/VSP_028266|||http://purl.uniprot.org/annotation/VSP_028267 http://togogenome.org/gene/10090:Washc5 ^@ http://purl.uniprot.org/uniprot/Q8C2E7 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||WASH complex subunit 5 ^@ http://purl.uniprot.org/annotation/PRO_0000050734|||http://purl.uniprot.org/annotation/VSP_010323|||http://purl.uniprot.org/annotation/VSP_010324 http://togogenome.org/gene/10090:Myom3 ^@ http://purl.uniprot.org/uniprot/A2ABU4 ^@ 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|||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|||Myomesin-3|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315395 http://togogenome.org/gene/10090:A430057M04Rik ^@ http://purl.uniprot.org/uniprot/Q8C520 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Gpihbp1 ^@ http://purl.uniprot.org/uniprot/A0A087WNV7|||http://purl.uniprot.org/uniprot/Q9D1N2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide ^@ 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|||Loss of interaction with LPL.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes LPL transport to the lumenal surface of endothelial cells.|||Polar residues|||Reduced number of monomers.|||Removed in mature form|||Sulfotyrosine|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000343798|||http://purl.uniprot.org/annotation/PRO_0000429859|||http://purl.uniprot.org/annotation/PRO_5015029545 http://togogenome.org/gene/10090:Trim31 ^@ http://purl.uniprot.org/uniprot/Q8R0K2 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Zinc Finger ^@ Abolished E3 ubiquitin-protein ligase activity and ability to ubiquitinate MAVS.|||B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM31|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000386639 http://togogenome.org/gene/10090:Lrmda ^@ http://purl.uniprot.org/uniprot/Q9D9B4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Region|||Repeat ^@ Disordered|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||Leucine-rich melanocyte differentiation-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000089782 http://togogenome.org/gene/10090:Scgb2b20 ^@ http://purl.uniprot.org/uniprot/J3QK77 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015095469 http://togogenome.org/gene/10090:Or2f1 ^@ http://purl.uniprot.org/uniprot/Q7TRV7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp948 ^@ http://purl.uniprot.org/uniprot/Q6DFU8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Gcn1 ^@ http://purl.uniprot.org/uniprot/E9PVA8|||http://purl.uniprot.org/uniprot/Q3UHQ5|||http://purl.uniprot.org/uniprot/Q8BIX2|||http://purl.uniprot.org/uniprot/Q8BTM7 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ 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 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|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In Gcn1(DeltaRWDBD) mice; mild growth retardation, leading to death soon after birth, most likely due to respiratory failure.|||N-acetylalanine|||Phosphoserine|||RWDBD region|||Removed|||Stalled ribosome sensor GCN1|||TOG ^@ http://purl.uniprot.org/annotation/PRO_0000435424 http://togogenome.org/gene/10090:Eif1ad ^@ http://purl.uniprot.org/uniprot/Q3THJ3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable RNA-binding protein EIF1AD|||S1-like ^@ http://purl.uniprot.org/annotation/PRO_0000314153 http://togogenome.org/gene/10090:Etfrf1 ^@ http://purl.uniprot.org/uniprot/Q91V16 ^@ Chain|||Molecule Processing|||Natural Variation|||Sequence Variant ^@ Chain|||Sequence Variant ^@ Electron transfer flavoprotein regulatory factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000251183 http://togogenome.org/gene/10090:Camkk1 ^@ http://purl.uniprot.org/uniprot/Q8VBY2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase kinase 1|||Calmodulin-binding|||Disordered|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||RP domain ^@ http://purl.uniprot.org/annotation/PRO_0000086142 http://togogenome.org/gene/10090:Dnttip1 ^@ http://purl.uniprot.org/uniprot/Q3THA4|||http://purl.uniprot.org/uniprot/Q99LB0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region ^@ A.T hook|||Basic and acidic residues|||DNTTIP1 dimerisation|||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_0000072474 http://togogenome.org/gene/10090:Plek ^@ http://purl.uniprot.org/uniprot/Q5F271|||http://purl.uniprot.org/uniprot/Q9JHK5 ^@ 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 ^@ DEP|||N6-acetyllysine|||PH|||PH 1|||PH 2|||Phosphoserine|||Pleckstrin ^@ http://purl.uniprot.org/annotation/PRO_0000053860 http://togogenome.org/gene/10090:Or4k41 ^@ http://purl.uniprot.org/uniprot/Q7TQY1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Atp6v1f ^@ http://purl.uniprot.org/uniprot/Q9D1K2 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ V-type proton ATPase subunit F ^@ http://purl.uniprot.org/annotation/PRO_0000144800 http://togogenome.org/gene/10090:Kcnj6 ^@ http://purl.uniprot.org/uniprot/A0A0R4J239|||http://purl.uniprot.org/uniprot/A0A338P6L0|||http://purl.uniprot.org/uniprot/P48542|||http://purl.uniprot.org/uniprot/Q0VB45|||http://purl.uniprot.org/uniprot/Q8C4T8|||http://purl.uniprot.org/uniprot/Q8C8Y6 ^@ 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 ^@ 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|||Cytoplasmic|||Disordered|||Extracellular|||G protein-activated inward rectifier potassium channel 2|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In isoform GIRK2-1.|||In isoform GIRK2B.|||In isoform GIRK2C.|||In wv.|||Inward rectifier potassium channel C-terminal|||PDZ-binding|||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_0000154944|||http://purl.uniprot.org/annotation/VSP_002803|||http://purl.uniprot.org/annotation/VSP_002804|||http://purl.uniprot.org/annotation/VSP_002805|||http://purl.uniprot.org/annotation/VSP_002806|||http://purl.uniprot.org/annotation/VSP_002807|||http://purl.uniprot.org/annotation/VSP_002808 http://togogenome.org/gene/10090:Prkg2 ^@ http://purl.uniprot.org/uniprot/Q8C4R2|||http://purl.uniprot.org/uniprot/Q8CAH8 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Region ^@ AGC-kinase C-terminal|||Cyclic nucleotide-binding|||Disordered|||Protein kinase|||Proton acceptor ^@ http://togogenome.org/gene/10090:Lrrc40 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0W6|||http://purl.uniprot.org/uniprot/Q9CRC8 ^@ 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 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|||Leucine-rich repeat-containing protein 40|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000226259 http://togogenome.org/gene/10090:Eps8l3 ^@ http://purl.uniprot.org/uniprot/Q91WL0 ^@ 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|||Epidermal growth factor receptor kinase substrate 8-like protein 3|||PTB|||Phosphoserine|||Polar residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000239088 http://togogenome.org/gene/10090:Amy1 ^@ http://purl.uniprot.org/uniprot/P00687 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site ^@ Alpha-amylase 1|||Nucleophile|||Proton donor|||Pyrrolidone carboxylic acid|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000001403 http://togogenome.org/gene/10090:Pld2 ^@ http://purl.uniprot.org/uniprot/P97813|||http://purl.uniprot.org/uniprot/Q3UNY4|||http://purl.uniprot.org/uniprot/Q5SXG5|||http://purl.uniprot.org/uniprot/Q6NV49|||http://purl.uniprot.org/uniprot/Q80ZW1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ 2-fold increase in basal phospholipase activity.|||Catalytic|||Disordered|||PH|||PLD phosphodiesterase|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2|||PX|||Phospholipase D2|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000218806 http://togogenome.org/gene/10090:Rufy1 ^@ http://purl.uniprot.org/uniprot/Q8BIJ7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||FYVE-type|||Interaction with RAB4|||Phosphoserine|||Phosphotyrosine|||RUN|||RUN and FYVE domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000245829 http://togogenome.org/gene/10090:Tmem267 ^@ http://purl.uniprot.org/uniprot/H3BJ86|||http://purl.uniprot.org/uniprot/Q8VDR5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Helical|||Transmembrane protein 267 ^@ http://purl.uniprot.org/annotation/PRO_0000281922|||http://purl.uniprot.org/annotation/PRO_5015093547 http://togogenome.org/gene/10090:Magi2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JE00|||http://purl.uniprot.org/uniprot/A0A0G2JEG6|||http://purl.uniprot.org/uniprot/Q9WVQ1 ^@ 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|||Disordered|||Does not affect interaction with USH1G.|||Guanylate kinase-like|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||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_0000094587|||http://purl.uniprot.org/annotation/VSP_008436|||http://purl.uniprot.org/annotation/VSP_008437|||http://purl.uniprot.org/annotation/VSP_018580|||http://purl.uniprot.org/annotation/VSP_018581 http://togogenome.org/gene/10090:Or51f23 ^@ http://purl.uniprot.org/uniprot/E9PWA8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r125 ^@ http://purl.uniprot.org/uniprot/L7N227 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:A4galt ^@ http://purl.uniprot.org/uniprot/Q0R0H6|||http://purl.uniprot.org/uniprot/Q3TRS1|||http://purl.uniprot.org/uniprot/Q3UF00|||http://purl.uniprot.org/uniprot/Q67BJ4 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Topological Domain|||Transmembrane ^@ Alpha 1,4-glycosyltransferase|||Cytoplasmic|||DXD motif|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lactosylceramide 4-alpha-galactosyltransferase|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000080579 http://togogenome.org/gene/10090:Tktl1 ^@ http://purl.uniprot.org/uniprot/Q99MX0 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Proton donor|||Transketolase-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000271265 http://togogenome.org/gene/10090:Birc5 ^@ http://purl.uniprot.org/uniprot/O70201|||http://purl.uniprot.org/uniprot/Q549P2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Site|||Splice Variant|||Strand|||Turn ^@ BIR|||Baculoviral IAP repeat-containing protein 5|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with FBXL7|||N6-acetyllysine|||Phosphothreonine|||Phosphothreonine; by AURKB|||Phosphothreonine; by CDK1 and CDK15 ^@ http://purl.uniprot.org/annotation/PRO_0000122357|||http://purl.uniprot.org/annotation/VSP_002455|||http://purl.uniprot.org/annotation/VSP_002456|||http://purl.uniprot.org/annotation/VSP_002457 http://togogenome.org/gene/10090:Gkn3 ^@ http://purl.uniprot.org/uniprot/Q9D0T7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Signal Peptide ^@ BRICHOS|||Gastrokine-3|||Impaired secretion.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000394474 http://togogenome.org/gene/10090:Gria3 ^@ http://purl.uniprot.org/uniprot/B0QZW1|||http://purl.uniprot.org/uniprot/Q0VGS8|||http://purl.uniprot.org/uniprot/Q3UY17|||http://purl.uniprot.org/uniprot/Q9Z2W9 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Extracellular|||Glutamate receptor|||Glutamate receptor 3|||Helical|||Helical; Name=M4|||Helical; Pore-forming|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Receptor ligand binding region|||Receptor ligand binding region domain-containing protein|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000042230|||http://purl.uniprot.org/annotation/PRO_5004230276|||http://purl.uniprot.org/annotation/PRO_5015086983|||http://purl.uniprot.org/annotation/PRO_5027141796 http://togogenome.org/gene/10090:Shd ^@ http://purl.uniprot.org/uniprot/O88834 ^@ 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.|||SH2|||SH2 domain-containing adapter protein D ^@ http://purl.uniprot.org/annotation/PRO_0000246774|||http://purl.uniprot.org/annotation/VSP_019860 http://togogenome.org/gene/10090:Trmt10c ^@ http://purl.uniprot.org/uniprot/Q3UFY8 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||Phosphoserine|||SAM-dependent MTase TRM10-type|||tRNA methyltransferase 10 homolog C ^@ http://purl.uniprot.org/annotation/PRO_0000311310 http://togogenome.org/gene/10090:Panx2 ^@ http://purl.uniprot.org/uniprot/Q6IMP4 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pannexin-2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000208489|||http://purl.uniprot.org/annotation/VSP_039093|||http://purl.uniprot.org/annotation/VSP_039094 http://togogenome.org/gene/10090:Kctd13 ^@ http://purl.uniprot.org/uniprot/Q8BGV7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ BTB|||BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000191298 http://togogenome.org/gene/10090:Rhox10 ^@ http://purl.uniprot.org/uniprot/Q4TU83 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Nkx6-1 ^@ http://purl.uniprot.org/uniprot/Q99MA9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region ^@ 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_0000048953 http://togogenome.org/gene/10090:Calhm5 ^@ http://purl.uniprot.org/uniprot/Q8R100 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Calcium homeostasis modulator protein 5|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000186727 http://togogenome.org/gene/10090:Slc22a14 ^@ http://purl.uniprot.org/uniprot/Q497L9 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 14|||Strongly reduced riboflavin transport; when associated with 391-A--A-394.|||Strongly reduced riboflavin transport; when associated with A-275. ^@ http://purl.uniprot.org/annotation/PRO_0000452752 http://togogenome.org/gene/10090:H2al1d ^@ http://purl.uniprot.org/uniprot/Q5M8Q2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Histone H2A-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000440627 http://togogenome.org/gene/10090:Spsb2 ^@ http://purl.uniprot.org/uniprot/O88838 ^@ 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|||In isoform 2.|||Loss of interaction with MET and PARW.|||Loss of interaction with MET and PARW. Loss of interaction with NOS2.|||Loss of interaction with NOS2.|||Loss of interaction with PARW. No effect on interaction with MET. Loss of interaction with NOS2.|||Loss of interaction with PAWR. Significant loss of interaction with NOS2.|||No loss of interaction with NOS2.|||No loss of interaction with PAWR.|||Polar residues|||SOCS box|||SPRY domain-containing SOCS box protein 2|||Significant loss of interaction with NOS2.|||Strongly reduced interaction with MET and PARW.|||Strongly reduced interaction with MET. Loss of interaction with PARW. ^@ http://purl.uniprot.org/annotation/PRO_0000238475|||http://purl.uniprot.org/annotation/VSP_018613 http://togogenome.org/gene/10090:Ppp4r3a ^@ http://purl.uniprot.org/uniprot/E9Q481|||http://purl.uniprot.org/uniprot/Q6P2K6 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Serine/threonine-protein phosphatase 4 regulatory subunit 3-like central|||Serine/threonine-protein phosphatase 4 regulatory subunit 3A|||WH1 ^@ http://purl.uniprot.org/annotation/PRO_0000254599|||http://purl.uniprot.org/annotation/VSP_021257 http://togogenome.org/gene/10090:Samd5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J186|||http://purl.uniprot.org/uniprot/Q3V1H9 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes binding to EPHA5 SAM domain.|||Disordered|||SAM|||Sterile alpha motif domain-containing protein 5|||Strongly reduced binding affinity for EPHA5 SAM domain. ^@ http://purl.uniprot.org/annotation/PRO_0000311362 http://togogenome.org/gene/10090:Mrps25 ^@ http://purl.uniprot.org/uniprot/Q9D125 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Small ribosomal subunit protein mS25 ^@ http://purl.uniprot.org/annotation/PRO_0000087709 http://togogenome.org/gene/10090:Dnajc12 ^@ http://purl.uniprot.org/uniprot/D3Z0D9|||http://purl.uniprot.org/uniprot/Q9CWA0|||http://purl.uniprot.org/uniprot/Q9R022 ^@ 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 ^@ Basic and acidic residues|||Disordered|||DnaJ homolog subfamily C member 12|||J|||N-acetylmethionine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000071067 http://togogenome.org/gene/10090:Fbxl3 ^@ http://purl.uniprot.org/uniprot/Q5PRF6|||http://purl.uniprot.org/uniprot/Q8C4V4 ^@ 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 ^@ Basic and acidic residues|||Disordered|||F-box|||F-box/LRR-repeat protein 3|||In after-hour (afh) mutant; lengthening in circadian periodicity.|||In isoform 2.|||In overtime (ovtm) mutant; loss of function, lengthening of the circadian periodiocity and Cry1 stabilization of protein levels.|||Induces relocalization to the cytosol.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||No effect. ^@ http://purl.uniprot.org/annotation/PRO_0000119843|||http://purl.uniprot.org/annotation/VSP_008414 http://togogenome.org/gene/10090:Mfsd14b ^@ http://purl.uniprot.org/uniprot/Q8CIA9 ^@ 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|||Hippocampus abundant transcript-like protein 1|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000239230 http://togogenome.org/gene/10090:Or7c70 ^@ http://purl.uniprot.org/uniprot/Q7TQU8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Raet1d ^@ http://purl.uniprot.org/uniprot/Q9JI58 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form|||Retinoic acid early-inducible protein 1-delta ^@ http://purl.uniprot.org/annotation/PRO_0000019733|||http://purl.uniprot.org/annotation/PRO_0000019734 http://togogenome.org/gene/10090:Gnl3 ^@ http://purl.uniprot.org/uniprot/Q8CI11 ^@ 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|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic|||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|||Mislocalized to the nucleoplasm. No effect on MDM2-binding.|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000122445|||http://purl.uniprot.org/annotation/VSP_013412 http://togogenome.org/gene/10090:Gm3182 ^@ http://purl.uniprot.org/uniprot/K7N6V6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Car12 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0W4|||http://purl.uniprot.org/uniprot/Q8CI85|||http://purl.uniprot.org/uniprot/Q8K2J1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase|||Carbonic anhydrase 12|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004249|||http://purl.uniprot.org/annotation/PRO_5015099249|||http://purl.uniprot.org/annotation/PRO_5025099256 http://togogenome.org/gene/10090:Rhox2g ^@ http://purl.uniprot.org/uniprot/L7MUB9 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Nin ^@ http://purl.uniprot.org/uniprot/Q3UR16|||http://purl.uniprot.org/uniprot/Q61043 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||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 isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Ninein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000096845|||http://purl.uniprot.org/annotation/VSP_059551|||http://purl.uniprot.org/annotation/VSP_059552|||http://purl.uniprot.org/annotation/VSP_059553|||http://purl.uniprot.org/annotation/VSP_059554|||http://purl.uniprot.org/annotation/VSP_059555|||http://purl.uniprot.org/annotation/VSP_059556 http://togogenome.org/gene/10090:Arhgap30 ^@ http://purl.uniprot.org/uniprot/E9QMX7|||http://purl.uniprot.org/uniprot/Q640N3 ^@ 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.|||Phosphoserine|||Polar residues|||Rho GTPase-activating protein 30|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000280479|||http://purl.uniprot.org/annotation/VSP_023736 http://togogenome.org/gene/10090:Bbs10 ^@ http://purl.uniprot.org/uniprot/Q9DBI2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Bardet-Biedl syndrome 10 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000235273 http://togogenome.org/gene/10090:Ncl ^@ http://purl.uniprot.org/uniprot/P09405 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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 1|||RRM 2|||RRM 3|||RRM 4|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000081693 http://togogenome.org/gene/10090:Trim30d ^@ http://purl.uniprot.org/uniprot/E9PWL0|||http://purl.uniprot.org/uniprot/Q3TNW3 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ B box-type|||B30.2/SPRY|||RING-type ^@ http://togogenome.org/gene/10090:Ccdc70 ^@ http://purl.uniprot.org/uniprot/Q9D9B0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Coiled-coil domain-containing protein 70|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000234434 http://togogenome.org/gene/10090:Clip1 ^@ http://purl.uniprot.org/uniprot/D3Z2Z1|||http://purl.uniprot.org/uniprot/D3Z3M7|||http://purl.uniprot.org/uniprot/F8WIA1|||http://purl.uniprot.org/uniprot/Q922J3 ^@ 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|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ CAP-Gly|||CAP-Gly 1|||CAP-Gly 2|||CAP-Gly domain-containing linker protein 1|||CCHC-type|||Disordered|||Important for tubulin binding|||In isoform 2.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000240672|||http://purl.uniprot.org/annotation/VSP_019425 http://togogenome.org/gene/10090:Stat3 ^@ http://purl.uniprot.org/uniprot/P42227|||http://purl.uniprot.org/uniprot/Q3ULI4|||http://purl.uniprot.org/uniprot/Q6GU23 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Allysine; alternate|||Decreased transcriptional activation.|||Essential for nuclear import|||In isoform Del-701.|||In isoform Stat3B.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on nuclear import; when associated with A-77 and A-78.|||No effect on nuclear import; when associated with A-77 and W-174.|||No effect on nuclear import; when associated with A-78 and W-174.|||Nuclear localization to the same extent as wild-type; when associated with A-609.|||Nuclear localization to the same extent as wild-type; when associated with F-705.|||Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCE|||Phosphothreonine|||Phosphotyrosine; by FER and PTK6|||Removed|||SH2|||Signal transducer and activator of transcription 3 ^@ http://purl.uniprot.org/annotation/PRO_0000182418|||http://purl.uniprot.org/annotation/VSP_006287|||http://purl.uniprot.org/annotation/VSP_010475 http://togogenome.org/gene/10090:Hspbp1 ^@ http://purl.uniprot.org/uniprot/Q99P31 ^@ 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 ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||Disordered|||Hsp70-binding protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084037 http://togogenome.org/gene/10090:Syt13 ^@ http://purl.uniprot.org/uniprot/Q9EQT6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C2 1|||C2 2|||Cytoplasmic|||Helical|||Synaptotagmin-13|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000183976 http://togogenome.org/gene/10090:Map3k12 ^@ http://purl.uniprot.org/uniprot/Q60700 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Disordered|||Leucine-zipper 1|||Leucine-zipper 2|||Loss of kinase activity.|||Mitogen-activated protein kinase kinase kinase 12|||No effect on kinase activity.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086262 http://togogenome.org/gene/10090:Adprh ^@ http://purl.uniprot.org/uniprot/P54923 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Region ^@ ADP-ribosylhydrolase ARH1|||Substrate ^@ http://purl.uniprot.org/annotation/PRO_0000157284 http://togogenome.org/gene/10090:Slc33a1 ^@ http://purl.uniprot.org/uniprot/Q99J27 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Acetyl-coenzyme A transporter 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Mice homozygous for the mutation display early developmental arrest. Heterozygous animals display a deregulated form of autophagy.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000076166 http://togogenome.org/gene/10090:AU041133 ^@ http://purl.uniprot.org/uniprot/A0A0J9YVH3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Pfn4 ^@ http://purl.uniprot.org/uniprot/Q9D6I3 ^@ Chain|||Molecule Processing ^@ Chain ^@ Profilin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000199582 http://togogenome.org/gene/10090:Ndnf ^@ http://purl.uniprot.org/uniprot/Q8C119 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Fibronectin type-III 1|||Fibronectin type-III 2|||N-linked (GlcNAc...) asparagine|||Protein NDNF ^@ http://purl.uniprot.org/annotation/PRO_0000301966 http://togogenome.org/gene/10090:Or2ak5 ^@ http://purl.uniprot.org/uniprot/Q5NCD7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r53 ^@ http://purl.uniprot.org/uniprot/L7N473 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://togogenome.org/gene/10090:Baz1b ^@ http://purl.uniprot.org/uniprot/Q9Z277 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||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.|||N6-acetyllysine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tyrosine-protein kinase BAZ1B|||WAC ^@ http://purl.uniprot.org/annotation/PRO_0000211171|||http://purl.uniprot.org/annotation/VSP_037470 http://togogenome.org/gene/10090:Actl10 ^@ http://purl.uniprot.org/uniprot/A2AKE7 ^@ Chain|||Molecule Processing ^@ Chain ^@ Actin-like protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000374670 http://togogenome.org/gene/10090:Arhgap45 ^@ http://purl.uniprot.org/uniprot/D3Z7R7|||http://purl.uniprot.org/uniprot/G3X9Q3|||http://purl.uniprot.org/uniprot/Q3TBD2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||F-BAR|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Rho GTPase-activating protein 45|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000330314|||http://purl.uniprot.org/annotation/VSP_033029|||http://purl.uniprot.org/annotation/VSP_033030|||http://purl.uniprot.org/annotation/VSP_033031|||http://purl.uniprot.org/annotation/VSP_033032 http://togogenome.org/gene/10090:Sult6b2 ^@ http://purl.uniprot.org/uniprot/B7ZWN4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Med12 ^@ http://purl.uniprot.org/uniprot/A2AGH6|||http://purl.uniprot.org/uniprot/Q2NLB9 ^@ 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 ^@ Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Interaction with CTNNB1 and GLI3|||Mediator complex subunit Med12 catenin-binding|||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_0000312957|||http://purl.uniprot.org/annotation/VSP_029977|||http://purl.uniprot.org/annotation/VSP_029978|||http://purl.uniprot.org/annotation/VSP_029979|||http://purl.uniprot.org/annotation/VSP_029980 http://togogenome.org/gene/10090:Gm2244 ^@ http://purl.uniprot.org/uniprot/L7N2A3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tas2r134 ^@ http://purl.uniprot.org/uniprot/Q7TQB0 ^@ 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 134 ^@ http://purl.uniprot.org/annotation/PRO_0000082269 http://togogenome.org/gene/10090:Haghl ^@ http://purl.uniprot.org/uniprot/D3YZU6|||http://purl.uniprot.org/uniprot/Q9DB32 ^@ 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.|||Metallo-beta-lactamase ^@ http://purl.uniprot.org/annotation/PRO_0000313602|||http://purl.uniprot.org/annotation/VSP_030057|||http://purl.uniprot.org/annotation/VSP_030058 http://togogenome.org/gene/10090:Edc3 ^@ http://purl.uniprot.org/uniprot/A0ELI5|||http://purl.uniprot.org/uniprot/Q8K2D3 ^@ 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 ^@ DFDF|||Disordered|||Enhancer of mRNA-decapping protein 3|||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_0000119056 http://togogenome.org/gene/10090:Ptcd3 ^@ http://purl.uniprot.org/uniprot/Q14C51 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ Disordered|||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_0000305029 http://togogenome.org/gene/10090:Mrps33 ^@ http://purl.uniprot.org/uniprot/Q58DZ5|||http://purl.uniprot.org/uniprot/Q9D2R8 ^@ 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|||N-acetylserine|||Removed|||Small ribosomal subunit protein mS33 ^@ http://purl.uniprot.org/annotation/PRO_0000087728 http://togogenome.org/gene/10090:Prokr2 ^@ http://purl.uniprot.org/uniprot/E0CY28|||http://purl.uniprot.org/uniprot/Q8K458 ^@ 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|||Prokineticin receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000070084 http://togogenome.org/gene/10090:Hspa1l ^@ http://purl.uniprot.org/uniprot/P16627 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Region|||Sequence Conflict ^@ Heat shock 70 kDa protein 1-like|||Nucleotide-binding domain (NBD)|||Substrate-binding domain (SBD) ^@ http://purl.uniprot.org/annotation/PRO_0000078256 http://togogenome.org/gene/10090:Cd163 ^@ http://purl.uniprot.org/uniprot/B7ZMW6|||http://purl.uniprot.org/uniprot/Q2VLH6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Internalization signal|||N-linked (GlcNAc...) asparagine|||SRCR|||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_0000238940|||http://purl.uniprot.org/annotation/PRO_0000238941|||http://purl.uniprot.org/annotation/PRO_5002867194|||http://purl.uniprot.org/annotation/VSP_019016 http://togogenome.org/gene/10090:Rptor ^@ http://purl.uniprot.org/uniprot/A2ACM0|||http://purl.uniprot.org/uniprot/A4FUW1 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Raptor N-terminal CASPase-like ^@ http://togogenome.org/gene/10090:Xndc1 ^@ http://purl.uniprot.org/uniprot/E9PVR2|||http://purl.uniprot.org/uniprot/Q8BRU2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DNA-repair protein Xrcc1 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cfap36 ^@ http://purl.uniprot.org/uniprot/Q8C6E0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||Cilia- and flagella-associated protein 36|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000278639 http://togogenome.org/gene/10090:Ccdc105 ^@ http://purl.uniprot.org/uniprot/Q9D4K7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Phosphotyrosine|||Tektin-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000279392 http://togogenome.org/gene/10090:Pkd2 ^@ http://purl.uniprot.org/uniprot/O35245 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes location at nodal cilia and cannot complement the laterality defect of null mutants.|||Abolishes location at nodal cilia and cannot complement the laterality defect of null mutants; when associated with G-6.|||Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||EF-hand|||Extracellular|||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 isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In lrm4; mice exhibit gross left-right abnormalities. Embryos do not show defects in kidney development. The nodes appear normal. Abolishes location at nodal cilia, but does not affect interaction with Pkd1l1.|||Linker|||N-linked (GlcNAc...) asparagine|||No effect on location at nodal cilia and can rescue the laterality defect of null mutants. Abolishes location at nodal cilia and cannot complement the laterality defect of null mutants; when associated with DEL 819-966.|||Omega-N-methylarginine|||Phosphoserine|||Polycystin-2|||Pore-forming|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000164357|||http://purl.uniprot.org/annotation/VSP_042485|||http://purl.uniprot.org/annotation/VSP_042486|||http://purl.uniprot.org/annotation/VSP_042487|||http://purl.uniprot.org/annotation/VSP_042488|||http://purl.uniprot.org/annotation/VSP_042489|||http://purl.uniprot.org/annotation/VSP_042490 http://togogenome.org/gene/10090:Crem ^@ http://purl.uniprot.org/uniprot/D3YXV5|||http://purl.uniprot.org/uniprot/D3Z011|||http://purl.uniprot.org/uniprot/D3Z326|||http://purl.uniprot.org/uniprot/D3Z6A5|||http://purl.uniprot.org/uniprot/D3Z7M6|||http://purl.uniprot.org/uniprot/E9PV35|||http://purl.uniprot.org/uniprot/E9PWV9|||http://purl.uniprot.org/uniprot/F6QWT6|||http://purl.uniprot.org/uniprot/F6VJ22|||http://purl.uniprot.org/uniprot/P27699|||http://purl.uniprot.org/uniprot/Q3TTH6|||http://purl.uniprot.org/uniprot/Q78Z98|||http://purl.uniprot.org/uniprot/Q9CQ87|||http://purl.uniprot.org/uniprot/Q9D599 ^@ 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 ^@ BZIP|||Basic motif|||Disordered|||In isoform 11.|||In isoform 2, isoform 3 and isoform 7.|||In isoform 2, isoform 3, isoform 4, isoform 6 and isoform 10.|||In isoform 2, isoform 5, isoform 6, isoform 7, isoform 8, isoform 10 and isoform 11.|||In isoform 4, isoform 8, isoform 9 and isoform 10.|||In isoform 5.|||KID|||Leucine-zipper|||Loss of in vitro phosphorylation by TSSK4.|||Phosphoserine|||bZIP|||cAMP-responsive element modulator ^@ http://purl.uniprot.org/annotation/PRO_0000076608|||http://purl.uniprot.org/annotation/VSP_000602|||http://purl.uniprot.org/annotation/VSP_000603|||http://purl.uniprot.org/annotation/VSP_000604|||http://purl.uniprot.org/annotation/VSP_000605|||http://purl.uniprot.org/annotation/VSP_000606|||http://purl.uniprot.org/annotation/VSP_000607|||http://purl.uniprot.org/annotation/VSP_038016|||http://purl.uniprot.org/annotation/VSP_055987 http://togogenome.org/gene/10090:Nlrp4b ^@ http://purl.uniprot.org/uniprot/Q8C6J9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||NACHT|||NACHT, LRR and PYD domains-containing protein 4B|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000286330 http://togogenome.org/gene/10090:Neil1 ^@ http://purl.uniprot.org/uniprot/Q8K4Q6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Endonuclease 8-like 1|||In isoform 2.|||Proton donor|||Proton donor; for beta-elimination activity|||Removed|||Schiff-base intermediate with DNA ^@ http://purl.uniprot.org/annotation/PRO_0000170906|||http://purl.uniprot.org/annotation/VSP_012207 http://togogenome.org/gene/10090:Polr1c ^@ http://purl.uniprot.org/uniprot/P52432 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ DNA-directed RNA polymerases I and III subunit RPAC1|||N-acetylalanine|||Removed|||Temperature-sensitive defect in the interaction with RPB14.|||Unable to interact with RPB14. ^@ http://purl.uniprot.org/annotation/PRO_0000132740 http://togogenome.org/gene/10090:Usp5 ^@ http://purl.uniprot.org/uniprot/P56399|||http://purl.uniprot.org/uniprot/Q3U4W8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||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_0000080624 http://togogenome.org/gene/10090:Car4 ^@ http://purl.uniprot.org/uniprot/Q64444 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Signal Peptide|||Strand ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase 4|||GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000004228|||http://purl.uniprot.org/annotation/PRO_0000004229 http://togogenome.org/gene/10090:Slc12a1 ^@ http://purl.uniprot.org/uniprot/P55014 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||In isoform A4.|||In isoform B.|||In isoform F.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine|||RFXV motif|||Solute carrier family 12 member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000178019|||http://purl.uniprot.org/annotation/VSP_006099|||http://purl.uniprot.org/annotation/VSP_006100|||http://purl.uniprot.org/annotation/VSP_006101|||http://purl.uniprot.org/annotation/VSP_006102 http://togogenome.org/gene/10090:Prss28 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZZ8|||http://purl.uniprot.org/uniprot/Q924N9 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 28 ^@ http://purl.uniprot.org/annotation/PRO_0000349225|||http://purl.uniprot.org/annotation/PRO_5039970674 http://togogenome.org/gene/10090:Draxin ^@ http://purl.uniprot.org/uniprot/Q6PAL1 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Draxin|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000273244 http://togogenome.org/gene/10090:Tifab ^@ http://purl.uniprot.org/uniprot/Q8JZM6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ FHA|||TRAF-interacting protein with FHA domain-containing protein B ^@ http://purl.uniprot.org/annotation/PRO_0000320693 http://togogenome.org/gene/10090:Tulp3 ^@ http://purl.uniprot.org/uniprot/O88413 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Tubby-related protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000186471 http://togogenome.org/gene/10090:Chkb ^@ http://purl.uniprot.org/uniprot/O55229|||http://purl.uniprot.org/uniprot/Q54AG5 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region ^@ Choline/ethanolamine kinase|||Disordered|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000206223 http://togogenome.org/gene/10090:Rps13 ^@ http://purl.uniprot.org/uniprot/P62301|||http://purl.uniprot.org/uniprot/Q5BLJ7 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue ^@ 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|||Small ribosomal subunit protein uS15|||Small ribosomal subunit protein uS15 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000115662 http://togogenome.org/gene/10090:Grb7 ^@ http://purl.uniprot.org/uniprot/Q03160 ^@ 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 ^@ Abolishes interaction with FHL2.|||Disordered|||Growth factor receptor-bound protein 7|||PH|||Phosphoserine|||Phosphotyrosine; by FAK1|||Polar residues|||Pro residues|||Ras-associating|||SH2|||Strongly reduced tyrosine phosphorylation. Abolishes interaction with FHL2. ^@ http://purl.uniprot.org/annotation/PRO_0000150345 http://togogenome.org/gene/10090:Atp6v1g2 ^@ http://purl.uniprot.org/uniprot/G5E923|||http://purl.uniprot.org/uniprot/Q54A87|||http://purl.uniprot.org/uniprot/Q9WTT4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||V-type proton ATPase subunit G 2 ^@ http://purl.uniprot.org/annotation/PRO_0000192902 http://togogenome.org/gene/10090:Gfm2 ^@ http://purl.uniprot.org/uniprot/E9Q7N5|||http://purl.uniprot.org/uniprot/Q3TSU6|||http://purl.uniprot.org/uniprot/Q8R2Q4 ^@ 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 ^@ In isoform 2.|||In isoform 3.|||Ribosome-releasing factor 2, mitochondrial|||Tr-type G|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000007451|||http://purl.uniprot.org/annotation/VSP_038195|||http://purl.uniprot.org/annotation/VSP_038196 http://togogenome.org/gene/10090:Or4k40 ^@ http://purl.uniprot.org/uniprot/Q7TQY2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Aplp2 ^@ http://purl.uniprot.org/uniprot/Q06335|||http://purl.uniprot.org/uniprot/Q60709|||http://purl.uniprot.org/uniprot/Q64348 ^@ 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|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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.|||Interaction with DAB2|||N-linked (GlcNAc...) asparagine|||NPXY motif|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Required for Cu(2+) reduction ^@ http://purl.uniprot.org/annotation/PRO_0000000208|||http://purl.uniprot.org/annotation/PRO_5014310246|||http://purl.uniprot.org/annotation/PRO_5015098090|||http://purl.uniprot.org/annotation/VSP_041386 http://togogenome.org/gene/10090:Stk31 ^@ http://purl.uniprot.org/uniprot/Q99MW1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Protein kinase|||Serine/threonine-protein kinase 31|||Tudor ^@ http://purl.uniprot.org/annotation/PRO_0000086716 http://togogenome.org/gene/10090:Proser2 ^@ http://purl.uniprot.org/uniprot/Q8C5R2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine; alternate|||Disordered|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proline and serine-rich protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000089793 http://togogenome.org/gene/10090:Rps29 ^@ http://purl.uniprot.org/uniprot/P62274 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Small ribosomal subunit protein uS14 ^@ http://purl.uniprot.org/annotation/PRO_0000131020 http://togogenome.org/gene/10090:Thtpa ^@ http://purl.uniprot.org/uniprot/Q8JZL3 ^@ 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 ^@ CYTH|||N-acetylalanine|||Removed|||Thiamine-triphosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000221492 http://togogenome.org/gene/10090:Mia ^@ http://purl.uniprot.org/uniprot/Q61865 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ Melanoma-derived growth regulatory protein|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000019029 http://togogenome.org/gene/10090:Or8h7 ^@ http://purl.uniprot.org/uniprot/A2AVA9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fam229a ^@ http://purl.uniprot.org/uniprot/B2KGE5 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Protein FAM229A ^@ http://purl.uniprot.org/annotation/PRO_0000421724 http://togogenome.org/gene/10090:Hprt ^@ http://purl.uniprot.org/uniprot/P00493 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Modified Residue|||Sequence Conflict ^@ 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|||N6-acetyllysine|||Phosphothreonine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000139588 http://togogenome.org/gene/10090:Tmem221 ^@ http://purl.uniprot.org/uniprot/Q8K071 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Transmembrane protein 221 ^@ http://purl.uniprot.org/annotation/PRO_0000332135 http://togogenome.org/gene/10090:Prss52 ^@ http://purl.uniprot.org/uniprot/Q9D9M0 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Charge relay system|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 52 ^@ http://purl.uniprot.org/annotation/PRO_0000328817 http://togogenome.org/gene/10090:Retn ^@ http://purl.uniprot.org/uniprot/Q5BMX4|||http://purl.uniprot.org/uniprot/Q99P87 ^@ Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Strand|||Turn ^@ Interchain|||Resistin ^@ http://purl.uniprot.org/annotation/PRO_0000030342|||http://purl.uniprot.org/annotation/PRO_5014309744 http://togogenome.org/gene/10090:Or56a4 ^@ http://purl.uniprot.org/uniprot/Q7TRN8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wdr53 ^@ http://purl.uniprot.org/uniprot/Q9DB94 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ Disordered|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat-containing protein 53 ^@ http://purl.uniprot.org/annotation/PRO_0000051414 http://togogenome.org/gene/10090:Nrap ^@ http://purl.uniprot.org/uniprot/Q80XB4 ^@ 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 ^@ In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In 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 5|||Nebulin 6|||Nebulin 7|||Nebulin 8|||Nebulin 9|||Nebulin-related-anchoring protein|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000248859|||http://purl.uniprot.org/annotation/VSP_052159|||http://purl.uniprot.org/annotation/VSP_052160|||http://purl.uniprot.org/annotation/VSP_052162 http://togogenome.org/gene/10090:Ndufb3 ^@ http://purl.uniprot.org/uniprot/Q9CQZ6 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Transmembrane ^@ Disordered|||Helical|||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_0000118798 http://togogenome.org/gene/10090:Atcay ^@ http://purl.uniprot.org/uniprot/Q8BHE3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site ^@ Basic and acidic residues|||CRAL-TRIO|||Caytaxin|||Cleavage; by CASP3|||Disordered|||Mediates interaction with GLS|||Phosphoserine|||Required for interaction with KLC1 ^@ http://purl.uniprot.org/annotation/PRO_0000210769 http://togogenome.org/gene/10090:Ccl8 ^@ http://purl.uniprot.org/uniprot/Q149U7|||http://purl.uniprot.org/uniprot/Q9Z121 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ C-C motif chemokine|||C-C motif chemokine 8|||Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_0000005190|||http://purl.uniprot.org/annotation/PRO_5014205730 http://togogenome.org/gene/10090:Entpd2 ^@ http://purl.uniprot.org/uniprot/O55026|||http://purl.uniprot.org/uniprot/Q921R1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Ectonucleoside triphosphate diphosphohydrolase 2|||Extracellular|||Helical|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000209907|||http://purl.uniprot.org/annotation/PRO_5014312475|||http://purl.uniprot.org/annotation/VSP_003611|||http://purl.uniprot.org/annotation/VSP_003612 http://togogenome.org/gene/10090:Zfp959 ^@ http://purl.uniprot.org/uniprot/Q91VM8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Angptl6 ^@ http://purl.uniprot.org/uniprot/Q8R0Z6 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Angiopoietin-related protein 6|||Disordered|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009129 http://togogenome.org/gene/10090:Tarm1 ^@ http://purl.uniprot.org/uniprot/B6A8R8 ^@ 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|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||T-cell-interacting, activating receptor on myeloid cells protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000394232 http://togogenome.org/gene/10090:Copg2 ^@ http://purl.uniprot.org/uniprot/Q9QXK3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Modified Residue|||Region|||Repeat|||Splice Variant ^@ Coatomer subunit gamma-2|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000193863|||http://purl.uniprot.org/annotation/VSP_034480|||http://purl.uniprot.org/annotation/VSP_034481|||http://purl.uniprot.org/annotation/VSP_034482|||http://purl.uniprot.org/annotation/VSP_034483|||http://purl.uniprot.org/annotation/VSP_034484 http://togogenome.org/gene/10090:Acmsd ^@ http://purl.uniprot.org/uniprot/Q8R519 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase ^@ http://purl.uniprot.org/annotation/PRO_0000190980 http://togogenome.org/gene/10090:Hnrnpk ^@ http://purl.uniprot.org/uniprot/B2M1R6|||http://purl.uniprot.org/uniprot/P61979|||http://purl.uniprot.org/uniprot/Q3U9Q3|||http://purl.uniprot.org/uniprot/Q5FWJ5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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.|||In isoform 3.|||Interaction with ZIK1|||K Homology|||KH 1|||KH 2|||KH 3|||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_0000050097|||http://purl.uniprot.org/annotation/VSP_010622|||http://purl.uniprot.org/annotation/VSP_012581 http://togogenome.org/gene/10090:Foxo1 ^@ http://purl.uniprot.org/uniprot/Q9R1E0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Abolishes insulin-induced phosphorylation when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-316; A-462 and A-463.|||DNA-binding|||Decreased transcriptional activity by about 2-fold in the absence of serum; when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-253; A-316 and A-462.|||Decreased transcriptional activity by about 2-fold in the absence of serum; when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-253; A-316 and A-463.|||Decreases insulin-induced phosphorylation by approximately 30%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-253; A-462 and A-463.|||Decreases insulin-induced phosphorylation by approximately 30%. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-253; A-316; A-462 and A-463. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with Q-219; Q-242; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with R-219; R-242; R-245; R-259; R-262; R-271 and R-291.|||Decreases phosphorylation by NLK; when associated with A-284; A-295; A-326; A-380; A-391; A-399 and A-413.|||Decreases phosphorylation by NLK; when associated with A-284; A-295; A-326; A-380; A-391; A-399 and A-415.|||Decreases phosphorylation by NLK; when associated with A-284; A-295; A-326; A-380; A-391; A-413 and A-415.|||Decreases phosphorylation by NLK; when associated with A-284; A-295; A-326; A-380; A-399; A-413 and A-415.|||Decreases phosphorylation by NLK; when associated with A-284; A-295; A-326; A-391; A-399; A-413 and A-415.|||Decreases phosphorylation by NLK; when associated with A-284; A-295; A-380; A-391; A-399; A-413 and A-415.|||Decreases phosphorylation by NLK; when associated with A-284; A-326; A-380; A-391; A-399; A-413 and A-415.|||Decreases phosphorylation by NLK; when associated with A-295; A-326; A-380; A-391; A-399; A-413 and A-415.|||Disordered|||Fork-head|||Forkhead box protein O1|||Little change in levels of methylation; when associated with K-147; K-154; K-311 and K-313.|||Little change in levels of methylation; when associated with K-29; K-147; K-154 and K-311.|||Little change in levels of methylation; when associated with K-29; K-147; K-154 and K-313.|||Little change in levels of methylation; when associated with K-29; K-147; K-311 and K-313.|||Little change in levels of methylation; when associated with K-29; K-154; K-311 and K-313.|||Loss of interaction with CEBPA.|||Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-262 and Q-271. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24: Q-219; Q-242; Q-245; Q-259; Q-262 and Q-271.|||Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-262 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-262 and Q-291.|||Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-262; Q-271 and Q-291.|||Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-242; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-242; Q-245; Q-259; Q-262; Q-271 and Q-291.|||Mimics acetylation. Cytoplasmic location in absence or presence of insulin. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-245 or Q-245 and either A-262 or Q-262. either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291.|||Mimics acetylation. Decreased DNA-binding by about half and enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-245 or Q-245. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291.|||Mimics acetylation. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291.|||N6-acetyllysine|||No change in methylation levels.|||Nuclear localization signal|||Omega-N-methylarginine; by PRMT1|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by CK1|||Phosphoserine; by CK1 and SGK1|||Phosphoserine; by PKB/AKT1 and SGK1|||Phosphoserine; by PKB/AKT1 or PKB/AKT2|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1 or PKB/AKT2 and SGK1|||Polar residues|||Pro residues|||Reduced acetylation and transcriptional activity increased by about 1.5 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-245 and R-262. Transcriptional activity not inhibited by FCOR; when associated with R-245; R-259; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-245; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-245; R-259; R-262; R-271 and R-291.|||Reduced acetylation and transcriptional activity increased by about 1.5-fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-262. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-259; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-259; R-262; R-271 and R-291.|||Required for interaction with RUNX2|||Required for interaction with SIRT1|||Significant reduction in acetylation and transcriptional activity increased by about 2.0 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-245. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-271 and R-291.|||Some decrease in levels of methylation. Greatly decreased methylation levels; when associated with K-248.|||Some decrease in levels of methylation. Greatly decreased methylation levels; when associated with K-250.|||Sufficient for interaction with NLK|||Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-262 and R-271. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-262 and R-271. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-262 and R-271.|||Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-262 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-262 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-262 and R-291.|||Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-262; R-271 and R-291.|||Translocates to the cytoplasm after insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-242; R-245; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-242; R-245; R-259; R-262; R-271 and R-291. ^@ http://purl.uniprot.org/annotation/PRO_0000091873 http://togogenome.org/gene/10090:Lcp2 ^@ http://purl.uniprot.org/uniprot/Q60787 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict ^@ 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_0000084369 http://togogenome.org/gene/10090:Dmtn ^@ http://purl.uniprot.org/uniprot/Q9WV69 ^@ 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|||Dematin|||Disordered|||HP|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Interaction with RASGRF2|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000218756|||http://purl.uniprot.org/annotation/VSP_047491|||http://purl.uniprot.org/annotation/VSP_047492 http://togogenome.org/gene/10090:Otop3 ^@ http://purl.uniprot.org/uniprot/F8VQ32|||http://purl.uniprot.org/uniprot/Q80UF9|||http://purl.uniprot.org/uniprot/Q9D7E9 ^@ 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.|||Proton channel OTOP3 ^@ http://purl.uniprot.org/annotation/PRO_0000313823|||http://purl.uniprot.org/annotation/VSP_030162 http://togogenome.org/gene/10090:Micall2 ^@ http://purl.uniprot.org/uniprot/E9PZD2|||http://purl.uniprot.org/uniprot/Q3TN34 ^@ 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 ^@ BMERB|||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|||LIM zinc-binding|||MICAL-like protein 2|||Mediates interaction with RAB13 and is required for transition from the closed to the open conformation|||Mediates targeting to the cell plasma membrane|||Necessary and sufficient for interaction with actinins|||Phosphoserine|||Polar residues|||bMERB ^@ http://purl.uniprot.org/annotation/PRO_0000424227 http://togogenome.org/gene/10090:Klhl29 ^@ http://purl.uniprot.org/uniprot/Q80T74 ^@ 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 29|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000119087 http://togogenome.org/gene/10090:Lrit1 ^@ http://purl.uniprot.org/uniprot/Q8K099 ^@ 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|||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_0000014836 http://togogenome.org/gene/10090:Trim40 ^@ http://purl.uniprot.org/uniprot/B7ZWG4|||http://purl.uniprot.org/uniprot/Q3UWA4 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Zinc Finger ^@ B box-type|||Disordered|||E3 ubiquitin ligase TRIM40|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000307823 http://togogenome.org/gene/10090:Sbno1 ^@ http://purl.uniprot.org/uniprot/B2RRI2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Strawberry notch AAA|||Strawberry notch helicase C ^@ http://togogenome.org/gene/10090:Rtn4 ^@ http://purl.uniprot.org/uniprot/Q99P72 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Turn ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform B.|||In isoform B2.|||In isoform C.|||In isoform D.|||Lumenal|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Reticulon|||Reticulon-4 ^@ http://purl.uniprot.org/annotation/PRO_0000168166|||http://purl.uniprot.org/annotation/VSP_018088|||http://purl.uniprot.org/annotation/VSP_018089|||http://purl.uniprot.org/annotation/VSP_018090|||http://purl.uniprot.org/annotation/VSP_018091|||http://purl.uniprot.org/annotation/VSP_060062|||http://purl.uniprot.org/annotation/VSP_060063 http://togogenome.org/gene/10090:Astl ^@ http://purl.uniprot.org/uniprot/Q6HA09 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Splice Variant ^@ Astacin-like metalloendopeptidase|||Disordered|||In isoform 2, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5.|||Peptidase M12A|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000041965|||http://purl.uniprot.org/annotation/VSP_043997|||http://purl.uniprot.org/annotation/VSP_043998|||http://purl.uniprot.org/annotation/VSP_043999|||http://purl.uniprot.org/annotation/VSP_051832 http://togogenome.org/gene/10090:Galns ^@ http://purl.uniprot.org/uniprot/Q571E4|||http://purl.uniprot.org/uniprot/Q8CC47 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 3-oxoalanine (Cys)|||Catalytic domain|||N-acetylgalactosamine-6-sulfatase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Sulfatase N-terminal|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000273148|||http://purl.uniprot.org/annotation/PRO_5015099029 http://togogenome.org/gene/10090:Snx30 ^@ http://purl.uniprot.org/uniprot/Q8CE50 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ BAR|||Disordered|||PX|||Phosphoserine|||Phosphothreonine|||Sorting nexin-30 ^@ http://purl.uniprot.org/annotation/PRO_0000284534 http://togogenome.org/gene/10090:Gm2663 ^@ http://purl.uniprot.org/uniprot/F6R7E8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5012384217 http://togogenome.org/gene/10090:Slc25a26 ^@ http://purl.uniprot.org/uniprot/Q5U680 ^@ 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|||Mitochondrial S-adenosylmethionine carrier protein|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000317588 http://togogenome.org/gene/10090:Trpm5 ^@ http://purl.uniprot.org/uniprot/Q9JJH7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Reduces sensitivity to block by extracellular acidification. Sensitivity to block by low extracellular pH is nearly abolished; when associated with N-935.|||Reduces sensitivity to block by extracellular acidification. Sensitivity to block by low extracellular pH is nearly abolished; when associated with Q-831.|||Shows normal sensitivity to acid block and significant recovery from acid-enhanced inactivation.|||Transient receptor potential cation channel subfamily M member 5 ^@ http://purl.uniprot.org/annotation/PRO_0000328934|||http://purl.uniprot.org/annotation/VSP_052744|||http://purl.uniprot.org/annotation/VSP_052745|||http://purl.uniprot.org/annotation/VSP_052746|||http://purl.uniprot.org/annotation/VSP_052747 http://togogenome.org/gene/10090:Prr5l ^@ http://purl.uniprot.org/uniprot/A2AVJ5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Proline-rich protein 5-like ^@ http://purl.uniprot.org/annotation/PRO_0000332710 http://togogenome.org/gene/10090:Ssx9 ^@ http://purl.uniprot.org/uniprot/Q6XAS3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB-related ^@ http://togogenome.org/gene/10090:Med13l ^@ http://purl.uniprot.org/uniprot/A0A0J9YUA8|||http://purl.uniprot.org/uniprot/E9QLJ3|||http://purl.uniprot.org/uniprot/Q6GQS5|||http://purl.uniprot.org/uniprot/Q6JPI3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||LXXLL motif 1|||LXXLL motif 2|||Leucine-zipper|||MID|||Mediator complex subunit Med13 C-terminal|||Mediator complex subunit Med13 N-terminal|||Mediator of RNA polymerase II transcription subunit 13-like|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000076353 http://togogenome.org/gene/10090:Gm45927 ^@ http://purl.uniprot.org/uniprot/B2M0S2 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site|||Transmembrane ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||Protein kinase ^@ http://togogenome.org/gene/10090:Or9a7 ^@ http://purl.uniprot.org/uniprot/Q8VF30 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ccbe1 ^@ http://purl.uniprot.org/uniprot/Q3MI99 ^@ 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 ^@ Basic and acidic residues|||Collagen and calcium-binding EGF domain-containing protein 1|||Collagen-like 1|||Collagen-like 2|||Disordered|||EGF-like; calcium-binding|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000279517 http://togogenome.org/gene/10090:Pkia ^@ http://purl.uniprot.org/uniprot/P63248 ^@ Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site ^@ Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Site ^@ Disordered|||Important for inhibition|||N-acetylthreonine|||Polar residues|||Removed|||cAMP-dependent protein kinase inhibitor alpha ^@ http://purl.uniprot.org/annotation/PRO_0000154533 http://togogenome.org/gene/10090:Id4 ^@ http://purl.uniprot.org/uniprot/P41139|||http://purl.uniprot.org/uniprot/Q544D2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ BHLH|||DNA-binding protein inhibitor ID-4|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127251 http://togogenome.org/gene/10090:Rnpc3 ^@ http://purl.uniprot.org/uniprot/Q3UZ01 ^@ 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 ^@ Acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Pro residues|||RNA-binding region-containing protein 3|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000311113|||http://purl.uniprot.org/annotation/VSP_029402 http://togogenome.org/gene/10090:Or4k36 ^@ http://purl.uniprot.org/uniprot/Q8VGG8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfc3h1 ^@ http://purl.uniprot.org/uniprot/B2RT41|||http://purl.uniprot.org/uniprot/Q6A049 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Putative zinc-finger|||TPR ^@ http://togogenome.org/gene/10090:Dcbld2 ^@ http://purl.uniprot.org/uniprot/Q91ZV3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ CUB|||Cytoplasmic|||Discoidin, CUB and LCCL domain-containing protein 2|||Disordered|||Extracellular|||F5/8 type C|||Helical|||LCCL|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000021079 http://togogenome.org/gene/10090:Cxcr1 ^@ http://purl.uniprot.org/uniprot/Q810W6 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ 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_0000277473 http://togogenome.org/gene/10090:Eef1akmt3 ^@ http://purl.uniprot.org/uniprot/D3YWP0 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ EEF1A lysine methyltransferase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000439952 http://togogenome.org/gene/10090:Bcl6 ^@ http://purl.uniprot.org/uniprot/P41183|||http://purl.uniprot.org/uniprot/Q544F9 ^@ 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 ^@ Abolishes interaction with NCOR2; mice have impaired GC formation and immunoglobulin affinity maturation with lower proliferation and survival of GCB-cells but normal differentiation of helper T-cell subsets and inflammatory response; in macrophages, no effect on transcriptional repression of genes encoding inflammatory molecules; when associated with A-116. In macrophages, no effect on competition with STAT5 for DNA-binding and transcriptional repression of genes encoding inflammatory molecules; when associated with A-116 and 377-Q--Q-380.|||Abolishes interaction with NCOR2; mice have impaired GC formation and immunoglobulin affinity maturation with lower proliferation and survival of GCB-cells but normal differentiation of helper T-cell subsets and inflammatory response; in macrophages, no effect on transcriptional repression of genes encoding inflammatory molecules; when associated with K-21. In macrophages, no effect on competition with STAT5 for DNA-binding and transcriptional repression of genes encoding inflammatory molecules; when associated with K-21 and 377-Q--Q-380.|||B-cell lymphoma 6 protein homolog|||BTB|||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|||In macrophages, inhibits competition with STAT5 for DNA-binding and abolishes transcriptional repression of genes encoding inflammatory molecules.|||In macrophages, no effect on transcriptional repression of genes encoding inflammatory molecules. In macrophages, no effect on competition with STAT5 for DNA-binding and transcriptional repression of genes encoding inflammatory molecules; when associated with K-21 and A-116.|||N6-acetyllysine; by EP300|||Phosphoserine|||Phosphoserine; by MAPK1|||Polar residues|||Required for interaction with NuRD complex and for transcriptional repressor activity ^@ http://purl.uniprot.org/annotation/PRO_0000047099 http://togogenome.org/gene/10090:Iqca1l ^@ http://purl.uniprot.org/uniprot/A6H690 ^@ 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|||IQ|||IQ and AAA domain-containing protein 1-like|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000341250|||http://purl.uniprot.org/annotation/VSP_034231 http://togogenome.org/gene/10090:Khnyn ^@ http://purl.uniprot.org/uniprot/Q80U38 ^@ 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 KHNYN|||RNase NYN ^@ http://purl.uniprot.org/annotation/PRO_0000084291 http://togogenome.org/gene/10090:Rab11fip2 ^@ http://purl.uniprot.org/uniprot/G3UW57|||http://purl.uniprot.org/uniprot/G3XA57 ^@ 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|||C2|||Disordered|||FIP-RBD|||In isoform 2.|||NPF 1|||NPF 2|||Necessary for interaction with AP2A1, RAB11A, subcellular location, endocytosis activity and homooligomerization|||Necessary for its cellular translocation to the plasma membrane|||Phosphoserine|||Phosphoserine; by MARK2|||Polar residues|||Rab11 family-interacting protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000424063|||http://purl.uniprot.org/annotation/VSP_053310 http://togogenome.org/gene/10090:Nkapl ^@ http://purl.uniprot.org/uniprot/Q5SZT7 ^@ 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|||Basic residues|||Disordered|||NKAP-like protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000437458 http://togogenome.org/gene/10090:Nsg2 ^@ http://purl.uniprot.org/uniprot/P47759|||http://purl.uniprot.org/uniprot/Q5SS02 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Neuronal vesicle trafficking-associated protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000164367 http://togogenome.org/gene/10090:2010003K11Rik ^@ http://purl.uniprot.org/uniprot/A0A678XUL2|||http://purl.uniprot.org/uniprot/Q8VC23 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Uncharacterized protein C11orf86 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000328810 http://togogenome.org/gene/10090:Il1rl1 ^@ http://purl.uniprot.org/uniprot/P14719|||http://purl.uniprot.org/uniprot/Q5D095 ^@ Active 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 Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Complete loss of FBXL19-mediated polyubiquitination.|||Complete loss of phosphorylation by GSK3B.|||Cytoplasmic|||Extracellular|||Flexible linker|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform B.|||In strain: C3H/He.|||Interleukin-1 receptor-like 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by GSK3-beta|||TIR ^@ http://purl.uniprot.org/annotation/PRO_0000015443|||http://purl.uniprot.org/annotation/PRO_5014309738|||http://purl.uniprot.org/annotation/VSP_002668|||http://purl.uniprot.org/annotation/VSP_002669 http://togogenome.org/gene/10090:Smim3 ^@ http://purl.uniprot.org/uniprot/Q3U1M0|||http://purl.uniprot.org/uniprot/Q99PE5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Chain|||Sequence Conflict|||Site|||Transmembrane ^@ Cleavage|||Helical|||Small integral membrane protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000096817 http://togogenome.org/gene/10090:Emsy ^@ http://purl.uniprot.org/uniprot/Q8BMB0 ^@ 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 ^@ BRCA2-interacting transcriptional repressor EMSY|||Basic and acidic residues|||Disordered|||ENT|||In isoform 2.|||In isoform 3.|||Interaction with BRCA2|||Interaction with ZMYND11|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000086969|||http://purl.uniprot.org/annotation/VSP_010432|||http://purl.uniprot.org/annotation/VSP_010433|||http://purl.uniprot.org/annotation/VSP_010434 http://togogenome.org/gene/10090:Fli1 ^@ http://purl.uniprot.org/uniprot/P26323|||http://purl.uniprot.org/uniprot/Q544B3|||http://purl.uniprot.org/uniprot/Q8BZ56 ^@ Chain|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||ETS|||Friend leukemia integration 1 transcription factor|||PNT|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000204125 http://togogenome.org/gene/10090:Ulk4 ^@ http://purl.uniprot.org/uniprot/E9Q2P5|||http://purl.uniprot.org/uniprot/Q3V129 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant ^@ Disordered|||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.|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase ULK4 ^@ http://purl.uniprot.org/annotation/PRO_0000250154|||http://purl.uniprot.org/annotation/VSP_020605|||http://purl.uniprot.org/annotation/VSP_020606|||http://purl.uniprot.org/annotation/VSP_020607|||http://purl.uniprot.org/annotation/VSP_020608|||http://purl.uniprot.org/annotation/VSP_020609|||http://purl.uniprot.org/annotation/VSP_020610|||http://purl.uniprot.org/annotation/VSP_020611|||http://purl.uniprot.org/annotation/VSP_020612|||http://purl.uniprot.org/annotation/VSP_020613 http://togogenome.org/gene/10090:Mpp3 ^@ http://purl.uniprot.org/uniprot/Q6XE40 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Guanylate kinase-like|||L27|||PDZ|||SH3 ^@ http://togogenome.org/gene/10090:Cdk15 ^@ http://purl.uniprot.org/uniprot/Q3V3A1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Basic and acidic residues|||Cyclin-dependent kinase 15|||Disordered|||In isoform 2.|||In isoform 3.|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000283822|||http://purl.uniprot.org/annotation/VSP_038766|||http://purl.uniprot.org/annotation/VSP_052350|||http://purl.uniprot.org/annotation/VSP_052351 http://togogenome.org/gene/10090:4930449I24Rik ^@ http://purl.uniprot.org/uniprot/Q9D5E3 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Pdgfb ^@ http://purl.uniprot.org/uniprot/A0A0R4IZW4|||http://purl.uniprot.org/uniprot/P31240 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Disordered|||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_0000023374|||http://purl.uniprot.org/annotation/PRO_0000023375|||http://purl.uniprot.org/annotation/PRO_0000023376|||http://purl.uniprot.org/annotation/PRO_5006451930 http://togogenome.org/gene/10090:Klf4 ^@ http://purl.uniprot.org/uniprot/Q60793 ^@ Chain|||Compositionally Biased Region|||Crosslink|||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|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||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)|||Increased cell reprogramming and pluripotency. No change in promoter-binding of target genes.|||Interaction with ZNF296|||Interaction with target DNA|||Krueppel-like factor 4|||Loss of polyglutamylation, reduced cell reprogramming and pluripotency maintenance. Forms heterodimer with KLF5. No change in promoter-binding of target genes. Embryo lethality in mutant homozygous mice.|||No change in KLF4 polyglutamylation.|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000047168 http://togogenome.org/gene/10090:Tex35 ^@ http://purl.uniprot.org/uniprot/A0A0R4J070|||http://purl.uniprot.org/uniprot/A0A0R4J1P6|||http://purl.uniprot.org/uniprot/D3Z4U7|||http://purl.uniprot.org/uniprot/D3Z652|||http://purl.uniprot.org/uniprot/Q14BK3 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Testis-expressed protein 35 ^@ http://purl.uniprot.org/annotation/PRO_0000251188|||http://purl.uniprot.org/annotation/VSP_020742 http://togogenome.org/gene/10090:Lhx3 ^@ http://purl.uniprot.org/uniprot/A2ALD8|||http://purl.uniprot.org/uniprot/P50481 ^@ 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|||Turn ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Homeobox|||In isoform LIM3B.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx3|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000075782|||http://purl.uniprot.org/annotation/VSP_003108 http://togogenome.org/gene/10090:Ceacam16 ^@ http://purl.uniprot.org/uniprot/E9QA28 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide ^@ Carcinoembryonic antigen-related cell adhesion molecule 16|||Disordered|||Does not affect the interaction with TECTA nor subcellular localization.|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000417874 http://togogenome.org/gene/10090:Tyro3 ^@ http://purl.uniprot.org/uniprot/P55144 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase receptor TYRO3 ^@ http://purl.uniprot.org/annotation/PRO_0000024479|||http://purl.uniprot.org/annotation/VSP_012548|||http://purl.uniprot.org/annotation/VSP_012549 http://togogenome.org/gene/10090:Or14j3 ^@ http://purl.uniprot.org/uniprot/Q923Q8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Snrnp27 ^@ http://purl.uniprot.org/uniprot/Q8K194 ^@ 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|||U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein ^@ http://purl.uniprot.org/annotation/PRO_0000223966|||http://purl.uniprot.org/annotation/VSP_017317 http://togogenome.org/gene/10090:Cpm ^@ http://purl.uniprot.org/uniprot/Q80V42 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide|||Splice Variant ^@ Carboxypeptidase M|||GPI-anchor amidated serine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000004392|||http://purl.uniprot.org/annotation/PRO_0000251911|||http://purl.uniprot.org/annotation/VSP_014606|||http://purl.uniprot.org/annotation/VSP_014607 http://togogenome.org/gene/10090:Ptgs2 ^@ http://purl.uniprot.org/uniprot/Q05769 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Aspirin-acetylated serine|||Decreases acetylation by SPHK1.|||EGF-like|||For cyclooxygenase activity|||Impairs peroxidase and cyclooxygenase activities toward 2-arachidonoyl glycerol.|||Loss of glycosylation site.|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||O-acetylserine; by SPHK1|||Prostaglandin G/H synthase 2|||Proton acceptor|||S-nitrosocysteine|||Slightly reduced activity.|||axial binding residue ^@ http://purl.uniprot.org/annotation/CAR_000222|||http://purl.uniprot.org/annotation/CAR_000223|||http://purl.uniprot.org/annotation/CAR_000224|||http://purl.uniprot.org/annotation/CAR_000225|||http://purl.uniprot.org/annotation/PRO_0000023876 http://togogenome.org/gene/10090:Gm5934 ^@ http://purl.uniprot.org/uniprot/D3Z4U6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Scgb1b29 ^@ http://purl.uniprot.org/uniprot/D2XZ31 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Signal Peptide ^@ Chain|||Non-terminal Residue|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015088473 http://togogenome.org/gene/10090:Cutal ^@ http://purl.uniprot.org/uniprot/A0A0J9YUN0|||http://purl.uniprot.org/uniprot/Q9D1U5 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Galntl6 ^@ http://purl.uniprot.org/uniprot/E5D8G1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Ricin B lectin ^@ http://togogenome.org/gene/10090:Il36rn ^@ http://purl.uniprot.org/uniprot/Q9QYY1 ^@ Chain|||Disulfide Bond|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Sequence Conflict|||Strand|||Turn ^@ Interleukin-36 receptor antagonist protein|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000153643 http://togogenome.org/gene/10090:Akap11 ^@ http://purl.uniprot.org/uniprot/E9Q777|||http://purl.uniprot.org/uniprot/Q8BSJ2 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ A-kinase anchor 110kDa C-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Zfp316 ^@ http://purl.uniprot.org/uniprot/G3XA34|||http://purl.uniprot.org/uniprot/Q6PGE4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Acidic residues|||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 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; degenerate|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 316 ^@ http://purl.uniprot.org/annotation/PRO_0000348943 http://togogenome.org/gene/10090:Mpdu1 ^@ http://purl.uniprot.org/uniprot/Q8R0J2 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Gnb4 ^@ http://purl.uniprot.org/uniprot/P29387 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ Guanine nucleotide-binding protein subunit beta-4|||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_0000127703 http://togogenome.org/gene/10090:Sephs1 ^@ http://purl.uniprot.org/uniprot/Q6NZN9|||http://purl.uniprot.org/uniprot/Q6P1B6|||http://purl.uniprot.org/uniprot/Q8BH69 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Site ^@ Important for catalytic activity|||N-acetylserine|||PurM-like C-terminal|||PurM-like N-terminal|||Removed|||Selenide, water dikinase 1|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000127649 http://togogenome.org/gene/10090:Cit ^@ http://purl.uniprot.org/uniprot/D3YU89|||http://purl.uniprot.org/uniprot/D3Z1U0|||http://purl.uniprot.org/uniprot/E9QL53|||http://purl.uniprot.org/uniprot/F6SBR5|||http://purl.uniprot.org/uniprot/P49025 ^@ Active Site|||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|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ AGC-kinase C-terminal|||Basic and acidic residues|||CNH|||Citron Rho-interacting kinase|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with Rho/Rac|||Loss of phosphorylation.|||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_0000085909|||http://purl.uniprot.org/annotation/VSP_012436|||http://purl.uniprot.org/annotation/VSP_012437|||http://purl.uniprot.org/annotation/VSP_012438|||http://purl.uniprot.org/annotation/VSP_012439|||http://purl.uniprot.org/annotation/VSP_016093|||http://purl.uniprot.org/annotation/VSP_016094|||http://purl.uniprot.org/annotation/VSP_016095 http://togogenome.org/gene/10090:Smad4 ^@ http://purl.uniprot.org/uniprot/P97471 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||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 ubiquitin)|||MH1|||MH2|||Mediates interaction with ZBTB7A|||Mothers against decapentaplegic homolog 4|||N6-acetyllysine|||Necessary for heterotrimerization|||Polar residues|||Required for interaction with TSC22D1|||SAD ^@ http://purl.uniprot.org/annotation/PRO_0000090862 http://togogenome.org/gene/10090:Tmem41a ^@ http://purl.uniprot.org/uniprot/Q9CUY8|||http://purl.uniprot.org/uniprot/Q9D8U2 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane ^@ Helical|||Transmembrane protein 41A|||VTT domain ^@ http://purl.uniprot.org/annotation/PRO_0000271776 http://togogenome.org/gene/10090:Grpel2 ^@ http://purl.uniprot.org/uniprot/O88396|||http://purl.uniprot.org/uniprot/Q0VB85 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Coiled-Coil|||Modified Residue|||Transit Peptide ^@ GrpE protein homolog 2, mitochondrial|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000013053 http://togogenome.org/gene/10090:Or5b96 ^@ http://purl.uniprot.org/uniprot/Q8VFX4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Erf ^@ http://purl.uniprot.org/uniprot/A0A0R4J0I0|||http://purl.uniprot.org/uniprot/P70459 ^@ 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 ^@ Acidic residues|||Disordered|||ETS|||ETS domain-containing transcription factor ERF|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000204102 http://togogenome.org/gene/10090:Plb1 ^@ http://purl.uniprot.org/uniprot/Q3TTY0|||http://purl.uniprot.org/uniprot/Q8K255 ^@ Active Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ 1|||2|||3|||4|||4 X 308-326 AA approximate repeats|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Necessary for membrane localization|||Phospholipase B1, membrane-associated ^@ http://purl.uniprot.org/annotation/PRO_0000324385|||http://purl.uniprot.org/annotation/VSP_032233|||http://purl.uniprot.org/annotation/VSP_032234|||http://purl.uniprot.org/annotation/VSP_032235|||http://purl.uniprot.org/annotation/VSP_032236|||http://purl.uniprot.org/annotation/VSP_032237|||http://purl.uniprot.org/annotation/VSP_032238 http://togogenome.org/gene/10090:Madd ^@ http://purl.uniprot.org/uniprot/A0A0R4J1F4|||http://purl.uniprot.org/uniprot/A2AGR0|||http://purl.uniprot.org/uniprot/E9QN47|||http://purl.uniprot.org/uniprot/Q80U28 ^@ 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|||Death|||Disordered|||In isoform 10 and isoform 12.|||In isoform 12.|||In isoform 13.|||In isoform 14.|||In isoform 15.|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 7, isoform 8, isoform 11 and isoform 14.|||In isoform 2, isoform 4, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11.|||In isoform 2, isoform 4, isoform 7, isoform 8 and isoform 11.|||In isoform 3, isoform 5, isoform 6, isoform 8, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13 and isoform 14.|||In isoform 4, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11.|||In isoform 4, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10, isoform 11 and isoform 12.|||In isoform 5, isoform 6, isoform 9 and isoform 10.|||In isoform 5, isoform 6, isoform 9, isoform 10 and isoform 12.|||In isoform 6.|||In isoform 7 and isoform 11.|||In isoform 9.|||MAP kinase-activating death domain protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||UDENN|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000278139|||http://purl.uniprot.org/annotation/VSP_052299|||http://purl.uniprot.org/annotation/VSP_052300|||http://purl.uniprot.org/annotation/VSP_052301|||http://purl.uniprot.org/annotation/VSP_052302|||http://purl.uniprot.org/annotation/VSP_052303|||http://purl.uniprot.org/annotation/VSP_052304|||http://purl.uniprot.org/annotation/VSP_052305|||http://purl.uniprot.org/annotation/VSP_052306|||http://purl.uniprot.org/annotation/VSP_052307|||http://purl.uniprot.org/annotation/VSP_052308|||http://purl.uniprot.org/annotation/VSP_052309|||http://purl.uniprot.org/annotation/VSP_052310|||http://purl.uniprot.org/annotation/VSP_052311|||http://purl.uniprot.org/annotation/VSP_052312|||http://purl.uniprot.org/annotation/VSP_052313|||http://purl.uniprot.org/annotation/VSP_052314|||http://purl.uniprot.org/annotation/VSP_052315 http://togogenome.org/gene/10090:Or51a8 ^@ http://purl.uniprot.org/uniprot/Q8VH12 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pfdn1 ^@ http://purl.uniprot.org/uniprot/Q9CQF7 ^@ Coiled-Coil|||Region ^@ Coiled-Coil ^@ ^@ http://togogenome.org/gene/10090:Defb40 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0U1|||http://purl.uniprot.org/uniprot/Q70KL2 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ Beta-defensin 40 ^@ http://purl.uniprot.org/annotation/PRO_0000006952|||http://purl.uniprot.org/annotation/PRO_5006451981 http://togogenome.org/gene/10090:Fam111a ^@ http://purl.uniprot.org/uniprot/D3YYD2|||http://purl.uniprot.org/uniprot/Q3UQF7|||http://purl.uniprot.org/uniprot/Q9D2L9 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||Charge relay system|||Cleavage; by autolysis|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Serine protease FAM111A ^@ http://purl.uniprot.org/annotation/PRO_0000274408 http://togogenome.org/gene/10090:Rabepk ^@ http://purl.uniprot.org/uniprot/Q8VCH5 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Rab9 effector protein with kelch motifs ^@ http://purl.uniprot.org/annotation/PRO_0000280617 http://togogenome.org/gene/10090:Or5h18 ^@ http://purl.uniprot.org/uniprot/Q8VEX5 ^@ 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 5H18 ^@ http://purl.uniprot.org/annotation/PRO_0000269658 http://togogenome.org/gene/10090:Mycl ^@ http://purl.uniprot.org/uniprot/P10166|||http://purl.uniprot.org/uniprot/Q3UIE0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||BHLH|||Basic and acidic residues|||Disordered|||Leucine-zipper|||Polar residues|||Protein L-Myc|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127334 http://togogenome.org/gene/10090:Naa38 ^@ http://purl.uniprot.org/uniprot/Q9D2U5 ^@ 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 ^@ Disordered|||In isoform 2.|||N-acetylalanine|||N-alpha-acetyltransferase 38, NatC auxiliary subunit|||Phosphoserine|||Polar residues|||Removed|||Sm ^@ http://purl.uniprot.org/annotation/PRO_0000299156|||http://purl.uniprot.org/annotation/VSP_027567 http://togogenome.org/gene/10090:Klhl1 ^@ http://purl.uniprot.org/uniprot/Q9JI74 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000119100 http://togogenome.org/gene/10090:Tbc1d10b ^@ http://purl.uniprot.org/uniprot/Q8BHL3 ^@ 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|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rab-GAP TBC|||TBC1 domain family member 10B ^@ http://purl.uniprot.org/annotation/PRO_0000315717 http://togogenome.org/gene/10090:Btg3 ^@ http://purl.uniprot.org/uniprot/P50615|||http://purl.uniprot.org/uniprot/Q52L83 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Anti-proliferative protein|||Disordered|||Protein BTG3 ^@ http://purl.uniprot.org/annotation/PRO_0000143808 http://togogenome.org/gene/10090:Morc1 ^@ http://purl.uniprot.org/uniprot/Q9WVL5 ^@ Binding Site|||Chain|||Coiled-Coil|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Region|||Zinc Finger ^@ CW-type|||Disordered|||MORC family CW-type zinc finger protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000248242 http://togogenome.org/gene/10090:Rnase1 ^@ http://purl.uniprot.org/uniprot/Q8C6G3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_5015020119 http://togogenome.org/gene/10090:Myo18a ^@ http://purl.uniprot.org/uniprot/A0A1C7ZN10|||http://purl.uniprot.org/uniprot/B2RRE2|||http://purl.uniprot.org/uniprot/E9Q405|||http://purl.uniprot.org/uniprot/E9QAX2|||http://purl.uniprot.org/uniprot/Q3UIM4|||http://purl.uniprot.org/uniprot/Q9JMH9 ^@ 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|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Disordered|||IQ|||In isoform 1, isoform 4, isoform 5 and isoform 7.|||In isoform 2 and isoform 5.|||In isoform 2, isoform 5 and isoform 7.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||Interaction with actin|||Loss of function.|||Mediates nucleotide-independent binding to F-actin and interaction with GOLPH3|||Myosin N-terminal SH3-like|||Myosin motor|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Unconventional myosin-XVIIIa ^@ http://purl.uniprot.org/annotation/PRO_0000123477|||http://purl.uniprot.org/annotation/VSP_007873|||http://purl.uniprot.org/annotation/VSP_007874|||http://purl.uniprot.org/annotation/VSP_023059|||http://purl.uniprot.org/annotation/VSP_023060|||http://purl.uniprot.org/annotation/VSP_023061|||http://purl.uniprot.org/annotation/VSP_023062 http://togogenome.org/gene/10090:Clcf1 ^@ http://purl.uniprot.org/uniprot/Q3TM06|||http://purl.uniprot.org/uniprot/Q9QZM3 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Signal Peptide ^@ Cardiotrophin-like cytokine factor 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015617|||http://purl.uniprot.org/annotation/PRO_5004229623 http://togogenome.org/gene/10090:Siah1a ^@ http://purl.uniprot.org/uniprot/P61092 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase SIAH1A|||Loss of interaction with AXIN1. Loss of function in AXIN1 degradation. Loss of function in Wnt signaling.|||Minor effect on binding and degradation of target proteins.|||Phosphoserine; by ATM and ATR|||RING-type|||SBD|||SIAH-type|||Strongly reduced binding and degradation of target proteins; when associated with D-158.|||Strongly reduced binding of target proteins. Strongly reduced degradation of target proteins. ^@ http://purl.uniprot.org/annotation/PRO_0000056164 http://togogenome.org/gene/10090:Tpk1 ^@ http://purl.uniprot.org/uniprot/Q9R0M5 ^@ 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.|||In isoform 3.|||Thiamin pyrophosphokinase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072648|||http://purl.uniprot.org/annotation/VSP_009595|||http://purl.uniprot.org/annotation/VSP_009596|||http://purl.uniprot.org/annotation/VSP_009597 http://togogenome.org/gene/10090:Or1p1 ^@ http://purl.uniprot.org/uniprot/B1ARL3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Katnip ^@ http://purl.uniprot.org/uniprot/F6XQI1|||http://purl.uniprot.org/uniprot/Q8C753 ^@ 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|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KATNIP|||Katanin-interacting protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000313091|||http://purl.uniprot.org/annotation/VSP_030009|||http://purl.uniprot.org/annotation/VSP_030010|||http://purl.uniprot.org/annotation/VSP_030011|||http://purl.uniprot.org/annotation/VSP_030012|||http://purl.uniprot.org/annotation/VSP_030013 http://togogenome.org/gene/10090:Defb19 ^@ http://purl.uniprot.org/uniprot/Q8K3I8 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Signal Peptide ^@ Beta-defensin 19 ^@ http://purl.uniprot.org/annotation/PRO_0000006944 http://togogenome.org/gene/10090:Palmd ^@ http://purl.uniprot.org/uniprot/A0A0R4J0J0|||http://purl.uniprot.org/uniprot/Q3UVT7|||http://purl.uniprot.org/uniprot/Q9JHU2 ^@ 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|||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-acetylmethionine|||Palmdelphin|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000262529 http://togogenome.org/gene/10090:Aldh6a1 ^@ http://purl.uniprot.org/uniprot/Q8K0L1|||http://purl.uniprot.org/uniprot/Q9EQ20 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Aldehyde dehydrogenase|||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_0000320299 http://togogenome.org/gene/10090:Speer2 ^@ http://purl.uniprot.org/uniprot/E9Q9U2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Eef1a2 ^@ http://purl.uniprot.org/uniprot/P62631 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 5-glutamyl glycerylphosphorylethanolamine|||Disordered|||Elongation factor 1-alpha 2|||G1|||G2|||G3|||G4|||G5|||N,N,N-trimethylglycine|||N6,N6,N6-trimethyllysine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3|||N6,N6-dimethyllysine|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||N6-methyllysine; alternate|||Phosphoserine|||Removed|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000090892 http://togogenome.org/gene/10090:Vwce ^@ http://purl.uniprot.org/uniprot/Q3U515 ^@ 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 ^@ Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||N-linked (GlcNAc...) asparagine|||Polar 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_0000318581 http://togogenome.org/gene/10090:Rgp1 ^@ http://purl.uniprot.org/uniprot/Q8BHT7 ^@ Chain|||Molecule Processing ^@ Chain ^@ RAB6A-GEF complex partner protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000274475 http://togogenome.org/gene/10090:Jam3 ^@ http://purl.uniprot.org/uniprot/Q9D8B7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreased binding to JAM2.|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||Junctional adhesion molecule C|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Soluble form of JAM-C ^@ http://purl.uniprot.org/annotation/PRO_0000015072|||http://purl.uniprot.org/annotation/PRO_0000445337 http://togogenome.org/gene/10090:Slc4a7 ^@ http://purl.uniprot.org/uniprot/F8VQC9|||http://purl.uniprot.org/uniprot/U3RF68 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Band 3 cytoplasmic|||Basic residues|||Bicarbonate transporter-like transmembrane|||Disordered|||Helical|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Pianp ^@ http://purl.uniprot.org/uniprot/Q6P1B3 ^@ 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|||O-linked (GalNAc...) threonine|||PILR alpha-associated neural protein|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000285966 http://togogenome.org/gene/10090:Or10al5 ^@ http://purl.uniprot.org/uniprot/Q5CZY0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or4a71 ^@ http://purl.uniprot.org/uniprot/Q8VGM7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dhrs7 ^@ http://purl.uniprot.org/uniprot/Q9CXR1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Signal Peptide ^@ Dehydrogenase/reductase SDR family member 7|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000031969 http://togogenome.org/gene/10090:Rfx3 ^@ http://purl.uniprot.org/uniprot/G5E890|||http://purl.uniprot.org/uniprot/P48381 ^@ 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|||In isoform 2.|||RFX-type winged-helix|||Transcription factor RFX3 ^@ http://purl.uniprot.org/annotation/PRO_0000215291|||http://purl.uniprot.org/annotation/VSP_007628|||http://purl.uniprot.org/annotation/VSP_007629|||http://purl.uniprot.org/annotation/VSP_007630 http://togogenome.org/gene/10090:Tnfsf8 ^@ http://purl.uniprot.org/uniprot/P32972|||http://purl.uniprot.org/uniprot/Q544U1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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_0000185500 http://togogenome.org/gene/10090:Pabpn1 ^@ http://purl.uniprot.org/uniprot/Q8CCS6 ^@ 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 ^@ Acidic residues|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Disordered|||In isoform 2.|||Interaction with PAPOLA|||Interaction with SKIP|||N-acetylalanine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polyadenylate-binding protein 2|||RRM|||Removed|||Stimulates PAPOLA|||Strong poly(A) affinity and self-association ^@ http://purl.uniprot.org/annotation/PRO_0000081712|||http://purl.uniprot.org/annotation/VSP_009849|||http://purl.uniprot.org/annotation/VSP_009850 http://togogenome.org/gene/10090:Agpat2 ^@ http://purl.uniprot.org/uniprot/Q059U0|||http://purl.uniprot.org/uniprot/Q8K3K7|||http://purl.uniprot.org/uniprot/Q9CWA8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Motif|||Non-terminal Residue|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 1-acyl-sn-glycerol-3-phosphate acyltransferase|||1-acyl-sn-glycerol-3-phosphate acyltransferase beta|||Cytoplasmic|||EGTR motif|||HXXXXD motif|||Helical|||Lumenal|||Phospholipid/glycerol acyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000208193|||http://purl.uniprot.org/annotation/PRO_5014306687 http://togogenome.org/gene/10090:Zscan5b ^@ http://purl.uniprot.org/uniprot/B2RTN3|||http://purl.uniprot.org/uniprot/Q9ES79 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues|||SCAN box ^@ http://togogenome.org/gene/10090:G6pc2 ^@ http://purl.uniprot.org/uniprot/Q9Z186 ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Motif|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Glucose-6-phosphatase 2|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Prevents secretion from ER|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000334510|||http://purl.uniprot.org/annotation/VSP_033650|||http://purl.uniprot.org/annotation/VSP_033651 http://togogenome.org/gene/10090:Purg ^@ http://purl.uniprot.org/uniprot/Q8R4E6 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Purine-rich element-binding protein gamma ^@ http://purl.uniprot.org/annotation/PRO_0000255953|||http://purl.uniprot.org/annotation/VSP_021320 http://togogenome.org/gene/10090:Mtg2 ^@ http://purl.uniprot.org/uniprot/A2AFK4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ OBG-type G|||Obg ^@ http://togogenome.org/gene/10090:Scrn2 ^@ http://purl.uniprot.org/uniprot/Q8VCA8 ^@ Active Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Chain ^@ Secernin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000262553 http://togogenome.org/gene/10090:Sh3rf1 ^@ http://purl.uniprot.org/uniprot/E9QQ33|||http://purl.uniprot.org/uniprot/Q69ZI1 ^@ 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|||E3 ubiquitin-protein ligase SH3RF1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with AKT2|||Interaction with RAC1|||Loss of binding to AKT2 and enhanced binding to MAP3K11.|||Loss of binding to AKT2.|||Phosphoserine|||Polar residues|||RING-type|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 4 ^@ http://purl.uniprot.org/annotation/PRO_0000334152|||http://purl.uniprot.org/annotation/VSP_033624|||http://purl.uniprot.org/annotation/VSP_033625|||http://purl.uniprot.org/annotation/VSP_033626|||http://purl.uniprot.org/annotation/VSP_033627|||http://purl.uniprot.org/annotation/VSP_033628 http://togogenome.org/gene/10090:Cdc37l1 ^@ http://purl.uniprot.org/uniprot/Q9CZP7 ^@ 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|||Hsp90 co-chaperone Cdc37-like 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with Hsp70|||Phosphoserine|||Required for interaction with STIP1|||Self-association|||Self-association and interaction with Hsp90 ^@ http://purl.uniprot.org/annotation/PRO_0000318522|||http://purl.uniprot.org/annotation/VSP_031213|||http://purl.uniprot.org/annotation/VSP_031214|||http://purl.uniprot.org/annotation/VSP_031215|||http://purl.uniprot.org/annotation/VSP_031216|||http://purl.uniprot.org/annotation/VSP_031217|||http://purl.uniprot.org/annotation/VSP_031218 http://togogenome.org/gene/10090:Ttc16 ^@ http://purl.uniprot.org/uniprot/E9PZ84|||http://purl.uniprot.org/uniprot/Q3TV33|||http://purl.uniprot.org/uniprot/Q3V0B6|||http://purl.uniprot.org/uniprot/Q8BTM2|||http://purl.uniprot.org/uniprot/Q8C1F5 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||Tetratricopeptide repeat protein 16 ^@ http://purl.uniprot.org/annotation/PRO_0000106405 http://togogenome.org/gene/10090:Rxra ^@ http://purl.uniprot.org/uniprot/A2AJP1|||http://purl.uniprot.org/uniprot/P28700|||http://purl.uniprot.org/uniprot/Q3UMU4|||http://purl.uniprot.org/uniprot/Q6LC96 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn|||Zinc Finger ^@ Abolishes interaction with ASXL1 and NCOA1.|||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)|||Hinge|||Loss of constituitive phosphorylation. No effect on RXRA transcriptional activity.|||Modulating domain|||N6-acetyllysine|||NR C4-type|||NR LBD|||No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-61 and A-75. phosphorylation. No effect on RXRA transcriptional activity.|||No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-61 and A-87.|||No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-75 and A-87. No effect on RXRA transcriptional activity.|||No effect on constituitive phosphorylation.|||No effect on constiuitive phosphorylation but loss of stress-induced phosphorylation. No effect on RXRA transcriptional activity.|||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_0000053567 http://togogenome.org/gene/10090:Oaz1 ^@ http://purl.uniprot.org/uniprot/P54369 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Ornithine decarboxylase antizyme 1 ^@ http://purl.uniprot.org/annotation/PRO_0000220851 http://togogenome.org/gene/10090:Clcnkb ^@ http://purl.uniprot.org/uniprot/Q9WUB6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ CBS 1|||CBS 2|||Chloride channel protein ClC-Kb|||Cytoplasmic|||Helical|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000094460|||http://purl.uniprot.org/annotation/VSP_011757|||http://purl.uniprot.org/annotation/VSP_011758 http://togogenome.org/gene/10090:Slc30a1 ^@ http://purl.uniprot.org/uniprot/Q3UM63|||http://purl.uniprot.org/uniprot/Q60738 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ 6 X 2 AA approximate repeats of H-G|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Proton-coupled zinc antiporter SLC30A1 ^@ http://purl.uniprot.org/annotation/PRO_0000206092 http://togogenome.org/gene/10090:Tmem150b ^@ http://purl.uniprot.org/uniprot/Q8R218 ^@ 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.|||Modulator of macroautophagy TMEM150B|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000349285|||http://purl.uniprot.org/annotation/VSP_035310|||http://purl.uniprot.org/annotation/VSP_035311 http://togogenome.org/gene/10090:Mbd3l2 ^@ http://purl.uniprot.org/uniprot/Q3UXB0|||http://purl.uniprot.org/uniprot/Q6P237 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Methyl-CpG binding protein 2/3 C-terminal|||Methyl-CpG-binding ^@ http://togogenome.org/gene/10090:Apobec2 ^@ http://purl.uniprot.org/uniprot/Q9WV35 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Strand ^@ C->U-editing enzyme APOBEC-2|||CMP/dCMP-type deaminase|||Disordered|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000171750 http://togogenome.org/gene/10090:Ppp1r21 ^@ http://purl.uniprot.org/uniprot/Q3TDD9 ^@ 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.|||Phosphothreonine|||Protein phosphatase 1 regulatory subunit 21 ^@ http://purl.uniprot.org/annotation/PRO_0000286099|||http://purl.uniprot.org/annotation/VSP_024988|||http://purl.uniprot.org/annotation/VSP_024990 http://togogenome.org/gene/10090:Wasf3 ^@ http://purl.uniprot.org/uniprot/Q8VHI6 ^@ 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 ^@ Actin-binding protein WASF3|||Basic and acidic residues|||Disordered|||Phosphotyrosine; by ABL1|||Polar residues|||Pro residues|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000188997 http://togogenome.org/gene/10090:Akap12 ^@ http://purl.uniprot.org/uniprot/B2RRE0|||http://purl.uniprot.org/uniprot/Q9WTQ5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Splice Variant ^@ A kinase-anchoring proteins AKAP-5 and AKAP-12 calmodulin (CaM)-binding|||A-kinase anchor protein 12|||AKAP CaM-binding|||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 isoform 2.|||Involved in PKC-binding|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RII-binding|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000304941|||http://purl.uniprot.org/annotation/VSP_028135 http://togogenome.org/gene/10090:Itga7 ^@ http://purl.uniprot.org/uniprot/G3X9Q1|||http://purl.uniprot.org/uniprot/Q3TZS3 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Transmembrane ^@ Basic and acidic residues|||Disordered|||FG-GAP|||Helical|||Integrin alpha-2|||Polar residues ^@ http://togogenome.org/gene/10090:Lig4 ^@ http://purl.uniprot.org/uniprot/Q8BTF7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ BRCT 1|||BRCT 2|||DNA ligase 4|||N6-AMP-lysine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000059577 http://togogenome.org/gene/10090:Gm10375 ^@ http://purl.uniprot.org/uniprot/Q5EBJ2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rc3h2 ^@ http://purl.uniprot.org/uniprot/A2AVP4|||http://purl.uniprot.org/uniprot/P0C090|||http://purl.uniprot.org/uniprot/Q148V4|||http://purl.uniprot.org/uniprot/Q148V5 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Site|||Zinc Finger ^@ C3H1-type|||Cleavage; by MALT1|||Disordered|||HEPN-C|||HEPN-N|||Phosphoserine|||RING-type|||RING-type; degenerate|||ROQ|||Roquin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000055969 http://togogenome.org/gene/10090:Agpat3 ^@ http://purl.uniprot.org/uniprot/Q9D517 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Motif|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma|||Cytoplasmic|||HXXXXD motif|||Helical|||Loss of LPA acyltransferase and LPI acyltransferase activities.|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000208195 http://togogenome.org/gene/10090:Sohlh1 ^@ http://purl.uniprot.org/uniprot/Q6IUP1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 1|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000315699 http://togogenome.org/gene/10090:Zfp91 ^@ http://purl.uniprot.org/uniprot/Q62511 ^@ 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 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000047313|||http://purl.uniprot.org/annotation/VSP_025759|||http://purl.uniprot.org/annotation/VSP_025760 http://togogenome.org/gene/10090:Vmn1r28 ^@ http://purl.uniprot.org/uniprot/Q8R2C9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pnpla1 ^@ http://purl.uniprot.org/uniprot/B2KF06|||http://purl.uniprot.org/uniprot/Q3V1D5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Basic and acidic residues|||DGA/G|||Disordered|||GXSXG|||Nucleophile|||Omega-hydroxyceramide transacylase|||PNPLA|||Polar residues|||Pro residues|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000292020 http://togogenome.org/gene/10090:Stk11ip ^@ http://purl.uniprot.org/uniprot/Q3TAA7 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||Phosphoserine|||Polar residues|||Serine/threonine-protein kinase 11-interacting protein ^@ http://purl.uniprot.org/annotation/PRO_0000317463 http://togogenome.org/gene/10090:Prkag3 ^@ http://purl.uniprot.org/uniprot/Q8BGM7 ^@ 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 ^@ 5'-AMP-activated protein kinase subunit gamma-3|||AMPK pseudosubstrate|||CBS 1|||CBS 2|||CBS 3|||CBS 4|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204385|||http://purl.uniprot.org/annotation/VSP_015588 http://togogenome.org/gene/10090:Lrrc52 ^@ http://purl.uniprot.org/uniprot/Q5M8M9 ^@ 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|||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_0000226827 http://togogenome.org/gene/10090:Or5ae2 ^@ http://purl.uniprot.org/uniprot/Q8VF60 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ttc24 ^@ http://purl.uniprot.org/uniprot/B9EJT8|||http://purl.uniprot.org/uniprot/Q8BYG0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Splice Variant ^@ Disordered|||In isoform 2.|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||Tetratricopeptide repeat protein 24 ^@ http://purl.uniprot.org/annotation/PRO_0000307772|||http://purl.uniprot.org/annotation/VSP_028823 http://togogenome.org/gene/10090:Tsga13 ^@ http://purl.uniprot.org/uniprot/Q9DA17 ^@ Chain|||Molecule Processing ^@ Chain ^@ Testis-specific gene 13 protein ^@ http://purl.uniprot.org/annotation/PRO_0000286346 http://togogenome.org/gene/10090:Sval1 ^@ http://purl.uniprot.org/uniprot/Q9D2X6 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Signal Peptide ^@ Prolactin-induced protein|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_5015099677 http://togogenome.org/gene/10090:Fam81a ^@ http://purl.uniprot.org/uniprot/Q3UXZ6 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict ^@ Disordered|||Protein FAM81A ^@ http://purl.uniprot.org/annotation/PRO_0000265120 http://togogenome.org/gene/10090:Tenm2 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ92|||http://purl.uniprot.org/uniprot/A0A0A0MQB7|||http://purl.uniprot.org/uniprot/B9EJ72 ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||EGF-like|||Helical|||Polar residues|||Teneurin N-terminal ^@ http://togogenome.org/gene/10090:B4galt2 ^@ http://purl.uniprot.org/uniprot/B1ASJ2|||http://purl.uniprot.org/uniprot/Q9Z2Y2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Beta-1,4-galactosyltransferase 2|||Cytoplasmic|||Disordered|||Galactosyltransferase C-terminal|||Galactosyltransferase N-terminal|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080534 http://togogenome.org/gene/10090:Zdhhc15 ^@ http://purl.uniprot.org/uniprot/Q8BGJ0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Disordered|||Fails to enhance DLG4 palmitoylation.|||Helical|||Lumenal|||Palmitoyltransferase ZDHHC15|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212894 http://togogenome.org/gene/10090:Gngt2 ^@ http://purl.uniprot.org/uniprot/A2A614|||http://purl.uniprot.org/uniprot/Q61017|||http://purl.uniprot.org/uniprot/Q6P8Y9 ^@ 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-T2|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000012647|||http://purl.uniprot.org/annotation/PRO_0000012648 http://togogenome.org/gene/10090:Dido1 ^@ http://purl.uniprot.org/uniprot/Q8C9B9 ^@ Chain|||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|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Death-inducer obliterator 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000059325|||http://purl.uniprot.org/annotation/VSP_012363|||http://purl.uniprot.org/annotation/VSP_012364|||http://purl.uniprot.org/annotation/VSP_026606|||http://purl.uniprot.org/annotation/VSP_026607 http://togogenome.org/gene/10090:Or8b49 ^@ http://purl.uniprot.org/uniprot/E9Q716 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rbms2 ^@ http://purl.uniprot.org/uniprot/E9Q7G6|||http://purl.uniprot.org/uniprot/Q3UGN4|||http://purl.uniprot.org/uniprot/Q8VC70 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Phosphoserine|||Polar residues|||RNA-binding motif, single-stranded-interacting protein 2|||RRM|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081801 http://togogenome.org/gene/10090:Il23r ^@ http://purl.uniprot.org/uniprot/G5E8U4|||http://purl.uniprot.org/uniprot/Q8K4B4 ^@ 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|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Interleukin-23 receptor|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000268663 http://togogenome.org/gene/10090:Vmn1r2 ^@ http://purl.uniprot.org/uniprot/A2AMT6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nck1 ^@ http://purl.uniprot.org/uniprot/Q8BH99|||http://purl.uniprot.org/uniprot/Q99M51 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Cytoplasmic protein NCK1|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Removed|||SH2|||SH3|||SH3 1|||SH3 2|||SH3 3 ^@ http://purl.uniprot.org/annotation/PRO_0000413801 http://togogenome.org/gene/10090:Magea13 ^@ http://purl.uniprot.org/uniprot/Q99PA7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Vmn1r232 ^@ http://purl.uniprot.org/uniprot/A2RTT5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp12 ^@ http://purl.uniprot.org/uniprot/Q6PB81|||http://purl.uniprot.org/uniprot/Q7TSI0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||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|||FYVE-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000402833|||http://purl.uniprot.org/annotation/VSP_040336 http://togogenome.org/gene/10090:Anp32e ^@ http://purl.uniprot.org/uniprot/P97822 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Acidic leucine-rich nuclear phosphoprotein 32 family member E|||Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000137600|||http://purl.uniprot.org/annotation/VSP_007373|||http://purl.uniprot.org/annotation/VSP_059599 http://togogenome.org/gene/10090:Flrt1 ^@ http://purl.uniprot.org/uniprot/A0A452J8F8|||http://purl.uniprot.org/uniprot/Q6RKD8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreases phosphorylation. Nearly abolishes phosphorylation; when associated with F-572 and F-605.|||Decreases phosphorylation. Nearly abolishes phosphorylation; when associated with F-572 and F-643.|||Decreases phosphorylation. Nearly abolishes phosphorylation; when associated with F-605 and F-643.|||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|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000434522 http://togogenome.org/gene/10090:Chd9 ^@ http://purl.uniprot.org/uniprot/Q8BYH8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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.|||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_0000233173|||http://purl.uniprot.org/annotation/VSP_018087 http://togogenome.org/gene/10090:1700001J03Rik ^@ http://purl.uniprot.org/uniprot/Q80ZR8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Sectm1b ^@ http://purl.uniprot.org/uniprot/Q8CE38|||http://purl.uniprot.org/uniprot/Q9D966 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||Secreted and transmembrane protein 1b ^@ http://purl.uniprot.org/annotation/PRO_5004304428|||http://purl.uniprot.org/annotation/PRO_5015099694 http://togogenome.org/gene/10090:Zfp605 ^@ http://purl.uniprot.org/uniprot/E9QAH2|||http://purl.uniprot.org/uniprot/Q8BRQ8 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Hoxa5 ^@ http://purl.uniprot.org/uniprot/P09021 ^@ 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|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000200058 http://togogenome.org/gene/10090:Dennd6b ^@ http://purl.uniprot.org/uniprot/Q9D9V7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||Protein DENND6B|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000264991 http://togogenome.org/gene/10090:Mbp ^@ http://purl.uniprot.org/uniprot/P04370|||http://purl.uniprot.org/uniprot/Q3UGF3|||http://purl.uniprot.org/uniprot/Q542T4|||http://purl.uniprot.org/uniprot/Q5D096 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand ^@ Basic and acidic residues|||Citrulline|||Cleavage; by CTSG|||Deamidated glutamine|||Disordered|||In isoform 10.|||In isoform 11.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10, isoform 11, isoform 12 and isoform 13.|||In isoform 4, isoform 6, isoform 9, isoform 11 and isoform 12.|||In isoform 6 and isoform 8.|||In isoform 7 and isoform 9.|||Myelin basic protein|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by UHMK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000158991|||http://purl.uniprot.org/annotation/VSP_003312|||http://purl.uniprot.org/annotation/VSP_003313|||http://purl.uniprot.org/annotation/VSP_003314|||http://purl.uniprot.org/annotation/VSP_003315|||http://purl.uniprot.org/annotation/VSP_003316|||http://purl.uniprot.org/annotation/VSP_003317|||http://purl.uniprot.org/annotation/VSP_003318|||http://purl.uniprot.org/annotation/VSP_003319|||http://purl.uniprot.org/annotation/VSP_003320 http://togogenome.org/gene/10090:Dao ^@ http://purl.uniprot.org/uniprot/A0A0R4J203|||http://purl.uniprot.org/uniprot/P18894|||http://purl.uniprot.org/uniprot/Q91WH3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict|||Sequence Variant ^@ Abolishes activity.|||D-amino-acid oxidase|||FAD dependent oxidoreductase|||Microbody targeting signal ^@ http://purl.uniprot.org/annotation/PRO_0000162762 http://togogenome.org/gene/10090:Ogt ^@ http://purl.uniprot.org/uniprot/Q8CGY8 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Impaired interaction with HOXA1. Loss of glycosylation of HOXA1.|||In isoform 2.|||Interacts with HOXA1. Interaction is localized to the nucleus.|||Loss of interaction with HOXA1. Loss of glycosylation of HOXA1.|||N-acetylalanine|||Nuclear localization signal|||O-linked (GlcNAc) serine; alternate|||Phosphoserine|||Phosphoserine; by GSK3-beta; alternate|||Phosphotyrosine|||Proton acceptor|||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_0000285216|||http://purl.uniprot.org/annotation/VSP_024844 http://togogenome.org/gene/10090:Bzw2 ^@ http://purl.uniprot.org/uniprot/Q91VK1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N6-acetyllysine|||Phosphoserine|||W2|||eIF5-mimic protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000254620 http://togogenome.org/gene/10090:Kif21a ^@ http://purl.uniprot.org/uniprot/F8WGN6|||http://purl.uniprot.org/uniprot/Q3TQJ5|||http://purl.uniprot.org/uniprot/Q3UHE7|||http://purl.uniprot.org/uniprot/Q3V416|||http://purl.uniprot.org/uniprot/Q9QXL2 ^@ 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|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with KANK1 and KANK2|||Kinesin motor|||Kinesin-like protein KIF21A|||N-acetylmethionine|||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_0000125463|||http://purl.uniprot.org/annotation/VSP_010873|||http://purl.uniprot.org/annotation/VSP_010874|||http://purl.uniprot.org/annotation/VSP_010875|||http://purl.uniprot.org/annotation/VSP_010876|||http://purl.uniprot.org/annotation/VSP_010877 http://togogenome.org/gene/10090:Ccdc22 ^@ http://purl.uniprot.org/uniprot/Q9JIG7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict ^@ Coiled-coil domain-containing protein 22|||Phosphoserine|||Sufficicient and required for interaction with CCDC93|||Sufficient for interaction with COMMD1 ^@ http://purl.uniprot.org/annotation/PRO_0000076200 http://togogenome.org/gene/10090:Tmem200c ^@ http://purl.uniprot.org/uniprot/J3QK46 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Rnf145 ^@ http://purl.uniprot.org/uniprot/Q3UTM8|||http://purl.uniprot.org/uniprot/Q5SWK7|||http://purl.uniprot.org/uniprot/Q8BU61 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transmembrane|||Zinc Finger ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Abolishes E3 ubiquitin ligase activity. Impairs ubiquitination of SCAP and functional regulation of cholesterol biosynthesis. Impairs sterol-induced ubiquitination and degradation of HMGCR.|||Disordered|||Helical|||Impairs interaction with INSIG1.|||Polar residues|||RING finger protein 145|||RING-type; atypical|||TRC8-like N-terminal|||YLYF motif ^@ http://purl.uniprot.org/annotation/PRO_0000294025 http://togogenome.org/gene/10090:Ncoa6 ^@ http://purl.uniprot.org/uniprot/F6M2J9|||http://purl.uniprot.org/uniprot/Q5XJV5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Nuclear receptor coactivator 6 TRADD-N|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Cyp2j6 ^@ http://purl.uniprot.org/uniprot/O54750 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Cytochrome P450 2J6|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051772 http://togogenome.org/gene/10090:Ano10 ^@ http://purl.uniprot.org/uniprot/Q8BH79 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Splice Variant|||Topological Domain|||Transmembrane ^@ Anoctamin-10|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4. ^@ http://purl.uniprot.org/annotation/PRO_0000289958|||http://purl.uniprot.org/annotation/VSP_026034|||http://purl.uniprot.org/annotation/VSP_026035|||http://purl.uniprot.org/annotation/VSP_026036|||http://purl.uniprot.org/annotation/VSP_026037 http://togogenome.org/gene/10090:Fbxw22 ^@ http://purl.uniprot.org/uniprot/Q3TSG7|||http://purl.uniprot.org/uniprot/Q5XG67 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ F-box ^@ http://togogenome.org/gene/10090:Tnfrsf23 ^@ http://purl.uniprot.org/uniprot/A0A140LIU0|||http://purl.uniprot.org/uniprot/Q3U3F7|||http://purl.uniprot.org/uniprot/Q9ER63 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Repeat|||Signal Peptide ^@ GPI-anchor amidated cysteine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 23 ^@ http://purl.uniprot.org/annotation/PRO_0000034604|||http://purl.uniprot.org/annotation/PRO_0000034605|||http://purl.uniprot.org/annotation/PRO_5014309182|||http://purl.uniprot.org/annotation/PRO_5015050599 http://togogenome.org/gene/10090:Chit1 ^@ http://purl.uniprot.org/uniprot/B2RS82|||http://purl.uniprot.org/uniprot/Q9D7Q1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant ^@ Chitin-binding type-2|||Chitotriosidase-1|||Disordered|||GH18|||In isoform 2.|||Loss of activity; when associated with N-136.|||Loss of activity; when associated with Q-140.|||Pro residues|||Proton donor|||chitinase ^@ http://purl.uniprot.org/annotation/PRO_0000011942|||http://purl.uniprot.org/annotation/PRO_5014298304|||http://purl.uniprot.org/annotation/VSP_020143|||http://purl.uniprot.org/annotation/VSP_020144 http://togogenome.org/gene/10090:Uqcrq ^@ http://purl.uniprot.org/uniprot/Q9CQ69 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Helix|||Modified Residue|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytochrome b-c1 complex subunit 8|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000193545 http://togogenome.org/gene/10090:Sirpb1a ^@ http://purl.uniprot.org/uniprot/Q6F5F2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Ig-like ^@ http://togogenome.org/gene/10090:Btbd2 ^@ http://purl.uniprot.org/uniprot/Q7TNF6 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ BTB ^@ http://togogenome.org/gene/10090:Lsm14b ^@ http://purl.uniprot.org/uniprot/Q4KL69|||http://purl.uniprot.org/uniprot/Q8CGC4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ DFDF|||Disordered|||FFD box|||FFD box profile|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylserine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Protein LSM14 homolog B|||Removed|||Sm|||TFG box|||TFG box profile ^@ http://purl.uniprot.org/annotation/PRO_0000187094 http://togogenome.org/gene/10090:Gm1553 ^@ http://purl.uniprot.org/uniprot/Q66VB7 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015098136 http://togogenome.org/gene/10090:Skp2 ^@ http://purl.uniprot.org/uniprot/A0A087WQ11|||http://purl.uniprot.org/uniprot/Q569Z9|||http://purl.uniprot.org/uniprot/Q9Z0Z3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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|||N6-acetyllysine; by p300/EP300|||Nuclear localization signal|||Phosphoserine|||S-phase kinase-associated protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000119955|||http://purl.uniprot.org/annotation/VSP_008433|||http://purl.uniprot.org/annotation/VSP_008434 http://togogenome.org/gene/10090:Pcif1 ^@ http://purl.uniprot.org/uniprot/P59114|||http://purl.uniprot.org/uniprot/Q542C3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||WW|||mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000076088 http://togogenome.org/gene/10090:Tbp ^@ http://purl.uniprot.org/uniprot/P29037|||http://purl.uniprot.org/uniprot/Q6RI65 ^@ 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|||Disordered|||In strain: TW18/TW5.|||Pro residues|||TATA-box-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000153958 http://togogenome.org/gene/10090:Zfp677 ^@ http://purl.uniprot.org/uniprot/Q6PEP4|||http://purl.uniprot.org/uniprot/Q8BI85 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Or11g26 ^@ http://purl.uniprot.org/uniprot/A2RTP5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mrps26 ^@ http://purl.uniprot.org/uniprot/Q80ZS3 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Transit Peptide ^@ Disordered|||Mitochondrion|||N6-acetyllysine|||Small ribosomal subunit protein mS26 ^@ http://purl.uniprot.org/annotation/PRO_0000283815 http://togogenome.org/gene/10090:Aldh5a1 ^@ http://purl.uniprot.org/uniprot/B2RS41|||http://purl.uniprot.org/uniprot/Q8BWF0 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Site|||Transit Peptide ^@ Aldehyde dehydrogenase|||In inhibited form|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Phosphoserine|||Proton acceptor|||Succinate-semialdehyde dehydrogenase, mitochondrial|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000007185 http://togogenome.org/gene/10090:Dmac2l ^@ http://purl.uniprot.org/uniprot/Q9CRA7 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Region|||Repeat|||Sequence Conflict|||Transit Peptide ^@ ATP synthase subunit s, mitochondrial|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||Mitochondrion|||N-terminal domain ^@ http://purl.uniprot.org/annotation/PRO_0000002539 http://togogenome.org/gene/10090:Zfp804b ^@ http://purl.uniprot.org/uniprot/A0A0G2JGH6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Arsi ^@ http://purl.uniprot.org/uniprot/Q32KI9 ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide ^@ 3-oxoalanine (Cys)|||Arylsulfatase I|||Disordered|||N-linked (GlcNAc...) asparagine|||Nucleophile|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000356284 http://togogenome.org/gene/10090:St6gal1 ^@ http://purl.uniprot.org/uniprot/Q64685|||http://purl.uniprot.org/uniprot/Q8BM62 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Beta-galactoside alpha-2,6-sialyltransferase 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Loss of enzyme activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on enzyme activity.|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000149250 http://togogenome.org/gene/10090:Prkcd ^@ http://purl.uniprot.org/uniprot/P28867|||http://purl.uniprot.org/uniprot/Q3TGE4|||http://purl.uniprot.org/uniprot/Q53YN4 ^@ 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|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ AGC-kinase C-terminal|||C2|||Cleavage; by caspase-3|||In isoform 2.|||Interaction with phosphotyrosine-containing peptide|||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_0000055695|||http://purl.uniprot.org/annotation/PRO_0000421669|||http://purl.uniprot.org/annotation/PRO_0000421670|||http://purl.uniprot.org/annotation/VSP_004741 http://togogenome.org/gene/10090:Mblac2 ^@ http://purl.uniprot.org/uniprot/Q8BL86 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict ^@ Acyl-coenzyme A thioesterase MBLAC2|||N-acetylserine|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000325936 http://togogenome.org/gene/10090:Leng1 ^@ http://purl.uniprot.org/uniprot/Q9DB98 ^@ 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|||Leukocyte receptor cluster member 1 homolog|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000254628 http://togogenome.org/gene/10090:Gsg1l2 ^@ http://purl.uniprot.org/uniprot/M0QWL6 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5004003693 http://togogenome.org/gene/10090:Or8b47 ^@ http://purl.uniprot.org/uniprot/A0A140T8K0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dpysl5 ^@ http://purl.uniprot.org/uniprot/Q9EQF6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Dihydropyrimidinase-related protein 5|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000165925 http://togogenome.org/gene/10090:Fam131c ^@ http://purl.uniprot.org/uniprot/A2ADB2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cblb ^@ http://purl.uniprot.org/uniprot/B9EKI5|||http://purl.uniprot.org/uniprot/Q3TTA7 ^@ 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|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ 4H|||Cbl-PTB|||Disordered|||E3 ubiquitin-protein ligase CBL-B|||EF-hand-like|||In isoform 2.|||Interaction with SH3KBP1|||Interaction with VAV1|||Linker|||Phosphoserine|||Phosphoserine; by PKC/PRKCQ|||Phosphotyrosine|||Polar residues|||Pro residues|||RING-type|||SH2-like|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000055861|||http://purl.uniprot.org/annotation/VSP_017222 http://togogenome.org/gene/10090:Mmd ^@ http://purl.uniprot.org/uniprot/Q9CQY7 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Monocyte to macrophage differentiation factor ^@ http://purl.uniprot.org/annotation/PRO_0000218855 http://togogenome.org/gene/10090:H2bc15 ^@ http://purl.uniprot.org/uniprot/P10853 ^@ 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-F/J/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-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_0000071839 http://togogenome.org/gene/10090:H1f6 ^@ http://purl.uniprot.org/uniprot/Q07133 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Citrulline|||Disordered|||H15|||Histone H1t|||Important for nucleosome binding properties|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000195919 http://togogenome.org/gene/10090:Ccdc148 ^@ http://purl.uniprot.org/uniprot/Q6P5U8 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Splice Variant ^@ Coiled-coil domain-containing protein 148|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000326065|||http://purl.uniprot.org/annotation/VSP_032537|||http://purl.uniprot.org/annotation/VSP_032538 http://togogenome.org/gene/10090:Tradd ^@ http://purl.uniprot.org/uniprot/B2RRZ7|||http://purl.uniprot.org/uniprot/Q3U0V2 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region ^@ (Microbial infection) N-beta-linked (GlcNAc) arginine|||Death|||Dominant-negative mutant, leading to enhanced ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A.|||Interaction with KRT14 and KRT18|||Nuclear export signal|||Nuclear localization signal|||Tumor necrosis factor receptor type 1-associated DEATH domain protein ^@ http://purl.uniprot.org/annotation/PRO_0000291660 http://togogenome.org/gene/10090:Mst1 ^@ http://purl.uniprot.org/uniprot/P26928|||http://purl.uniprot.org/uniprot/Q3UZ05 ^@ 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 ^@ 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|||N-linked (GlcNAc...) asparagine|||PAN|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000028088|||http://purl.uniprot.org/annotation/PRO_0000028089|||http://purl.uniprot.org/annotation/PRO_0000028090|||http://purl.uniprot.org/annotation/PRO_5004230299 http://togogenome.org/gene/10090:Ido2 ^@ http://purl.uniprot.org/uniprot/Q8R0V5 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Indoleamine 2,3-dioxygenase 2|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000285263 http://togogenome.org/gene/10090:Nox4 ^@ http://purl.uniprot.org/uniprot/B2RSM1|||http://purl.uniprot.org/uniprot/Q9JHI8 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||FAD-binding FR-type|||Ferric oxidoreductase|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mediates interaction with TLR4|||N-linked (GlcNAc...) asparagine|||NADPH oxidase 4 ^@ http://purl.uniprot.org/annotation/PRO_0000238981|||http://purl.uniprot.org/annotation/VSP_019060|||http://purl.uniprot.org/annotation/VSP_019061|||http://purl.uniprot.org/annotation/VSP_019062|||http://purl.uniprot.org/annotation/VSP_019063|||http://purl.uniprot.org/annotation/VSP_019064 http://togogenome.org/gene/10090:Vti1a ^@ http://purl.uniprot.org/uniprot/O89116|||http://purl.uniprot.org/uniprot/Q5FWJ7 ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Helical|||Helical; Anchor for type IV membrane protein|||T-SNARE coiled-coil homology|||Vesicle transport through interaction with t-SNAREs homolog 1A|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000218226 http://togogenome.org/gene/10090:Car15 ^@ http://purl.uniprot.org/uniprot/Q99N23 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Alpha-carbonic anhydrase|||Carbonic anhydrase 15|||Disordered|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004253 http://togogenome.org/gene/10090:Ntn1 ^@ http://purl.uniprot.org/uniprot/O09118 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Cell attachment site|||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_0000017083 http://togogenome.org/gene/10090:Cntn6 ^@ http://purl.uniprot.org/uniprot/Q9JMB8 ^@ 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|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Contactin-6|||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.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000014729|||http://purl.uniprot.org/annotation/PRO_0000014730|||http://purl.uniprot.org/annotation/VSP_011968 http://togogenome.org/gene/10090:Abhd11 ^@ http://purl.uniprot.org/uniprot/D3YYK0|||http://purl.uniprot.org/uniprot/Q8K4F5 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue ^@ AB hydrolase-1|||Charge relay system|||N6-succinyllysine|||Protein ABHD11 ^@ http://purl.uniprot.org/annotation/PRO_0000281004 http://togogenome.org/gene/10090:Hipk1 ^@ http://purl.uniprot.org/uniprot/O88904 ^@ 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|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes enzymatic 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|||Homeodomain-interacting protein kinase 1|||In isoform 2.|||In isoform 3.|||Interaction with TP53|||Nuclear localization signal 1 (NLS1)|||Phosphoserine|||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_0000085994|||http://purl.uniprot.org/annotation/VSP_013132|||http://purl.uniprot.org/annotation/VSP_013133|||http://purl.uniprot.org/annotation/VSP_013134 http://togogenome.org/gene/10090:Ubox5 ^@ http://purl.uniprot.org/uniprot/Q3TZ72|||http://purl.uniprot.org/uniprot/Q543N0|||http://purl.uniprot.org/uniprot/Q925F4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Loss of E3 ubiquitin-protein ligase activity.|||No effect on E3 ubiquitin-protein ligase activity.|||Polar residues|||RING finger protein 37|||RING-type|||U-box ^@ http://purl.uniprot.org/annotation/PRO_0000056077 http://togogenome.org/gene/10090:Arf5 ^@ http://purl.uniprot.org/uniprot/P84084 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding ^@ ADP-ribosylation factor 5|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207397 http://togogenome.org/gene/10090:Sh2d3c ^@ http://purl.uniprot.org/uniprot/Q9QZS8 ^@ 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 ^@ Abolishes interaction with NEDD9. Abolishes interaction with BCAR1. Abolishes phosphorylation of NEDD9. Abolishes promotion of migration and adhesion in T cells.|||Basic and acidic residues|||Disordered|||Disrupts binding to BCAR1 and inhibits EGF-induced tyrosine phosphorylation.|||In isoform 2.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Ras-GEF|||SH2|||SH2 domain-containing protein 3C ^@ http://purl.uniprot.org/annotation/PRO_0000228834|||http://purl.uniprot.org/annotation/VSP_017709 http://togogenome.org/gene/10090:Aipl1 ^@ http://purl.uniprot.org/uniprot/Q924K1|||http://purl.uniprot.org/uniprot/Q9CTQ3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Non-terminal Residue|||Repeat|||Sequence Conflict ^@ Aryl-hydrocarbon-interacting protein-like 1|||PPIase FKBP-type|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000075344 http://togogenome.org/gene/10090:Spint4 ^@ http://purl.uniprot.org/uniprot/Q9D263 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ BPTI/Kunitz inhibitor|||Kunitz-type protease inhibitor 4 ^@ http://purl.uniprot.org/annotation/PRO_0000308328 http://togogenome.org/gene/10090:Luzp2 ^@ http://purl.uniprot.org/uniprot/Q8BGY3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Leucine zipper protein 2|||Leucine-zipper|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000315275 http://togogenome.org/gene/10090:Wnt9b ^@ http://purl.uniprot.org/uniprot/O35468|||http://purl.uniprot.org/uniprot/Q2TBA6|||http://purl.uniprot.org/uniprot/Q8C718 ^@ 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|||Protein Wnt-9b ^@ http://purl.uniprot.org/annotation/PRO_0000041459|||http://purl.uniprot.org/annotation/PRO_5004304353|||http://purl.uniprot.org/annotation/PRO_5014308783 http://togogenome.org/gene/10090:Rassf7 ^@ http://purl.uniprot.org/uniprot/Q9DD19 ^@ 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 ^@ Disordered|||Pro residues|||Ras association domain-containing protein 7|||Ras-associating ^@ http://purl.uniprot.org/annotation/PRO_0000097174 http://togogenome.org/gene/10090:Foxq1 ^@ http://purl.uniprot.org/uniprot/O70220 ^@ 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 Q1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000091891 http://togogenome.org/gene/10090:Fxr1 ^@ http://purl.uniprot.org/uniprot/A0A0G2JEP0|||http://purl.uniprot.org/uniprot/Q61584 ^@ 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 ^@ Abolished ability to undergo liquid-liquid phase separation and promote translation of target mRNAs. Male infertility in knokin mice.|||Agenet-like|||Agenet-like 1|||Agenet-like 2|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Decreased phosphorylation by GSK3B.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform A and isoform B.|||In isoform A, isoform D and isoform F.|||In isoform A.|||In isoform C and isoform D.|||In isoform G.|||KH 1|||KH 2|||N-acetylalanine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RNA-binding RGG-box|||RNA-binding protein FXR1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000050107|||http://purl.uniprot.org/annotation/VSP_002836|||http://purl.uniprot.org/annotation/VSP_002837|||http://purl.uniprot.org/annotation/VSP_002838|||http://purl.uniprot.org/annotation/VSP_002839|||http://purl.uniprot.org/annotation/VSP_002840 http://togogenome.org/gene/10090:Exosc4 ^@ http://purl.uniprot.org/uniprot/Q542B0|||http://purl.uniprot.org/uniprot/Q921I9 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Exoribonuclease phosphorolytic|||Exosome complex component RRP41|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000139959 http://togogenome.org/gene/10090:Prmt5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J049|||http://purl.uniprot.org/uniprot/Q8CIG8 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Beta barrel|||Critical for specifying symmetric addition of methyl groups|||Dimerization|||N-acetylalanine|||PRMT5 TIM barrel|||PRMT5 arginine-N-methyltransferase|||PRMT5 oligomerisation|||Protein arginine N-methyltransferase 5|||Proton donor/acceptor|||Removed|||SAM-dependent MTase PRMT-type|||TIM barrel ^@ http://purl.uniprot.org/annotation/PRO_0000212344 http://togogenome.org/gene/10090:Pprc1 ^@ http://purl.uniprot.org/uniprot/Q6NZN1 ^@ 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 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||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_0000296667|||http://purl.uniprot.org/annotation/VSP_027232|||http://purl.uniprot.org/annotation/VSP_027233|||http://purl.uniprot.org/annotation/VSP_027234|||http://purl.uniprot.org/annotation/VSP_027235|||http://purl.uniprot.org/annotation/VSP_027236|||http://purl.uniprot.org/annotation/VSP_027237 http://togogenome.org/gene/10090:Sly ^@ http://purl.uniprot.org/uniprot/A0A087WRK1|||http://purl.uniprot.org/uniprot/Q810R0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Lrrc15 ^@ http://purl.uniprot.org/uniprot/Q80X72|||http://purl.uniprot.org/uniprot/Q9D3K0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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|||LRRNT|||Leucine-rich repeat-containing protein 15|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000021606|||http://purl.uniprot.org/annotation/PRO_5004324657 http://togogenome.org/gene/10090:Or6c74 ^@ http://purl.uniprot.org/uniprot/Q8VG45 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or8g26 ^@ http://purl.uniprot.org/uniprot/Q9EQ92 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Etv1 ^@ http://purl.uniprot.org/uniprot/E0CZ54|||http://purl.uniprot.org/uniprot/P41164|||http://purl.uniprot.org/uniprot/Q549J8|||http://purl.uniprot.org/uniprot/Q8CCR6 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||ETS|||ETS translocation variant 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphoserine; by RPS6KA1 and RPS6KA5 ^@ http://purl.uniprot.org/annotation/PRO_0000204111 http://togogenome.org/gene/10090:Pcdha6 ^@ http://purl.uniprot.org/uniprot/Q91Y14 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Cadherin|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099520 http://togogenome.org/gene/10090:Camsap2 ^@ http://purl.uniprot.org/uniprot/A0A0A6YY67|||http://purl.uniprot.org/uniprot/Q8C1B1 ^@ 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|||CKK|||Calmodulin-regulated spectrin-associated protein 2|||Calponin-homology (CH)|||Disordered|||In isoform 2.|||MBD region|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000316833|||http://purl.uniprot.org/annotation/VSP_030807 http://togogenome.org/gene/10090:Plet1 ^@ http://purl.uniprot.org/uniprot/Q8VEN2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||GPI-anchor amidated serine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Placenta-expressed transcript 1 protein|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000320954|||http://purl.uniprot.org/annotation/PRO_0000424669|||http://purl.uniprot.org/annotation/VSP_031770 http://togogenome.org/gene/10090:Ybx3 ^@ http://purl.uniprot.org/uniprot/Q68G78|||http://purl.uniprot.org/uniprot/Q9JKB3 ^@ 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 ^@ CSD|||Disordered|||In isoform 2.|||N-acetylserine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Removed|||Y-box-binding protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000100215|||http://purl.uniprot.org/annotation/VSP_013051 http://togogenome.org/gene/10090:Atraid ^@ http://purl.uniprot.org/uniprot/A8C1S6|||http://purl.uniprot.org/uniprot/Q6PGD0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ All-trans retinoic acid-induced differentiation factor|||Cytoplasmic|||EGF-like|||Extracellular|||Helical|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000020753|||http://purl.uniprot.org/annotation/PRO_5015086598|||http://purl.uniprot.org/annotation/VSP_039970 http://togogenome.org/gene/10090:Prl7a2 ^@ http://purl.uniprot.org/uniprot/A0A0M6L0L8|||http://purl.uniprot.org/uniprot/O54831 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prolactin-7A2 ^@ http://purl.uniprot.org/annotation/PRO_0000045130|||http://purl.uniprot.org/annotation/PRO_5015043311 http://togogenome.org/gene/10090:Vmn1r59 ^@ http://purl.uniprot.org/uniprot/Q8R2B9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nr1i2 ^@ http://purl.uniprot.org/uniprot/O54915|||http://purl.uniprot.org/uniprot/Q0P525 ^@ Binding Site|||Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||DNA Binding|||Domain Extent|||Motif|||Region|||Splice Variant|||Zinc Finger ^@ Bipartite nuclear localization signal|||Hinge|||In isoform 2.|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 1 group I member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000053549|||http://purl.uniprot.org/annotation/VSP_003670 http://togogenome.org/gene/10090:Bcdin3d ^@ http://purl.uniprot.org/uniprot/Q91YP1 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Bin3-type SAM|||RNA 5'-monophosphate methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000289266 http://togogenome.org/gene/10090:Vmn1r130 ^@ http://purl.uniprot.org/uniprot/D3YTY1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Acbd6 ^@ http://purl.uniprot.org/uniprot/Q14BV7|||http://purl.uniprot.org/uniprot/Q9D061 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ ACB|||ANK|||ANK 1|||ANK 2|||Acyl-CoA-binding domain-containing protein 6|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000232880|||http://purl.uniprot.org/annotation/VSP_018002|||http://purl.uniprot.org/annotation/VSP_018003|||http://purl.uniprot.org/annotation/VSP_018004|||http://purl.uniprot.org/annotation/VSP_018005 http://togogenome.org/gene/10090:Cdc25c ^@ http://purl.uniprot.org/uniprot/P48967|||http://purl.uniprot.org/uniprot/Q3UR74 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||M-phase inducer phosphatase 3|||N-acetylserine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by PLK3|||Phosphothreonine|||Phosphothreonine; by CDK1|||Polar residues|||Removed|||Rhodanese ^@ http://purl.uniprot.org/annotation/PRO_0000198648 http://togogenome.org/gene/10090:Tlr9 ^@ http://purl.uniprot.org/uniprot/Q9EQU3 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Highly susceptible to mouse cytomegalovirus infection. Shows low level of cytokine induction and natural killer activation on viral infection.|||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|||Loss of NF-kappa-B activation.|||N-linked (GlcNAc...) asparagine|||Significantly decreased NF-kappa-B activation.|||TIR|||Toll-like receptor 9 ^@ http://purl.uniprot.org/annotation/PRO_0000034738 http://togogenome.org/gene/10090:Elp1 ^@ http://purl.uniprot.org/uniprot/Q7TT37 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Elongator complex protein 1|||Mediates dimerization|||Phosphoserine|||Polar residues|||Required for binding to tRNA ^@ http://purl.uniprot.org/annotation/PRO_0000283995 http://togogenome.org/gene/10090:Grik2 ^@ http://purl.uniprot.org/uniprot/A0A1W2P6S5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding ^@ http://togogenome.org/gene/10090:Shisa6 ^@ http://purl.uniprot.org/uniprot/Q3UH99 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Loss of interaction with PDZ-domain of DLG4.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein shisa-6 ^@ http://purl.uniprot.org/annotation/PRO_0000326155|||http://purl.uniprot.org/annotation/VSP_059384 http://togogenome.org/gene/10090:Sdhd ^@ http://purl.uniprot.org/uniprot/Q9CXV1 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Binding Site|||Chain|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000006488 http://togogenome.org/gene/10090:Khdc1a ^@ http://purl.uniprot.org/uniprot/Q3UWR2 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ KH homology domain-containing protein 1A|||KH; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000311433 http://togogenome.org/gene/10090:Kcnn2 ^@ http://purl.uniprot.org/uniprot/A0A1B0GT12|||http://purl.uniprot.org/uniprot/B4YDY0|||http://purl.uniprot.org/uniprot/P58390|||http://purl.uniprot.org/uniprot/Q8C7F3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||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|||Phosphotyrosine|||Polar residues|||Pore-forming; Name=Segment H5|||Small conductance calcium-activated potassium channel protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000155011 http://togogenome.org/gene/10090:Prr9 ^@ http://purl.uniprot.org/uniprot/Q8BV84 ^@ Chain|||Molecule Processing ^@ Chain ^@ Proline-rich protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000334689 http://togogenome.org/gene/10090:Rsbn1 ^@ http://purl.uniprot.org/uniprot/Q80T69 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Lysine-specific demethylase 9|||Nuclear localization signal|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000299413 http://togogenome.org/gene/10090:Ch25h ^@ http://purl.uniprot.org/uniprot/Q9Z0F5 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Transmembrane ^@ Cholesterol 25-hydroxylase|||Fatty acid hydroxylase|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Loss of function.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000226802 http://togogenome.org/gene/10090:Sptlc3 ^@ http://purl.uniprot.org/uniprot/Q8BG54 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||N6-(pyridoxal phosphate)lysine|||Serine palmitoyltransferase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000304978 http://togogenome.org/gene/10090:Mrps5 ^@ http://purl.uniprot.org/uniprot/Q99N87 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||S5 DRBM|||Small ribosomal subunit protein uS5m ^@ http://purl.uniprot.org/annotation/PRO_0000131686 http://togogenome.org/gene/10090:Scarf2 ^@ http://purl.uniprot.org/uniprot/P59222|||http://purl.uniprot.org/uniprot/Q58A84 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Scavenger receptor class F member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000007740|||http://purl.uniprot.org/annotation/PRO_5014309705 http://togogenome.org/gene/10090:Crls1 ^@ http://purl.uniprot.org/uniprot/A0A0C3SFZ5|||http://purl.uniprot.org/uniprot/Q80ZM8 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Cardiolipin synthase (CMP-forming)|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000056817 http://togogenome.org/gene/10090:Vps25 ^@ http://purl.uniprot.org/uniprot/Q9CQ80 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||Vacuolar protein-sorting-associated protein 25 ^@ http://purl.uniprot.org/annotation/PRO_0000215217|||http://purl.uniprot.org/annotation/VSP_015341 http://togogenome.org/gene/10090:Tmbim7 ^@ http://purl.uniprot.org/uniprot/Q9D561|||http://purl.uniprot.org/uniprot/Q9D592 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Fbxo15 ^@ http://purl.uniprot.org/uniprot/Q3TJW2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Gltp ^@ http://purl.uniprot.org/uniprot/Q9JL62 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||2 X 12 AA approximate tandem repeats|||Glycolipid transfer protein|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000148916 http://togogenome.org/gene/10090:Mfsd6 ^@ http://purl.uniprot.org/uniprot/D3Z183|||http://purl.uniprot.org/uniprot/Q8CBH5 ^@ 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 ^@ Disordered|||Helical|||In isoform 2.|||Major facilitator superfamily associated|||Major facilitator superfamily domain-containing protein 6|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000321941|||http://purl.uniprot.org/annotation/VSP_031836 http://togogenome.org/gene/10090:Or7e170 ^@ http://purl.uniprot.org/uniprot/Q8VFJ1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ramp3 ^@ http://purl.uniprot.org/uniprot/Q9WUP1 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Receptor activity-modifying protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000030177 http://togogenome.org/gene/10090:Amz1 ^@ http://purl.uniprot.org/uniprot/A1L312|||http://purl.uniprot.org/uniprot/Q3UTF6|||http://purl.uniprot.org/uniprot/Q8BVF9 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Region|||Signal Peptide ^@ Archaemetzincin-1|||Disordered|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000159615|||http://purl.uniprot.org/annotation/PRO_5004230332 http://togogenome.org/gene/10090:Card6 ^@ http://purl.uniprot.org/uniprot/E9PWH2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ CARD|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rhox3g ^@ http://purl.uniprot.org/uniprot/B9EJQ9 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Nipal3 ^@ http://purl.uniprot.org/uniprot/A2A987|||http://purl.uniprot.org/uniprot/Q8BGN5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||NIPA-like protein 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000242151 http://togogenome.org/gene/10090:Ccdc174 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0L8|||http://purl.uniprot.org/uniprot/Q3U155 ^@ 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|||Coiled-coil domain-containing protein 174|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000251957 http://togogenome.org/gene/10090:Zmynd8 ^@ http://purl.uniprot.org/uniprot/A2A482|||http://purl.uniprot.org/uniprot/A2A483|||http://purl.uniprot.org/uniprot/A2A484|||http://purl.uniprot.org/uniprot/E9Q8D1|||http://purl.uniprot.org/uniprot/Q3U1M7|||http://purl.uniprot.org/uniprot/Q3UH28|||http://purl.uniprot.org/uniprot/Q3V1I9|||http://purl.uniprot.org/uniprot/Q80Y82 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Bromo|||Disordered|||MYND-type|||PHD-type|||PWWP|||Polar residues ^@ http://togogenome.org/gene/10090:Atxn1l ^@ http://purl.uniprot.org/uniprot/P0C7T6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ 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_0000343710 http://togogenome.org/gene/10090:Tcf7l2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1G0|||http://purl.uniprot.org/uniprot/D3YWT3|||http://purl.uniprot.org/uniprot/E9Q990|||http://purl.uniprot.org/uniprot/E9QQ90|||http://purl.uniprot.org/uniprot/E9QQ91|||http://purl.uniprot.org/uniprot/F6WBK9|||http://purl.uniprot.org/uniprot/F6WPX2|||http://purl.uniprot.org/uniprot/Q8BS68|||http://purl.uniprot.org/uniprot/Q8CAI6|||http://purl.uniprot.org/uniprot/Q924A0 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ 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 isoform 2 and isoform 8.|||In isoform 2.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Mediates interaction with MAD2L2|||Nuclear localization signal|||Phosphothreonine; by NLK|||Polar residues|||Transcription factor 7-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000048624|||http://purl.uniprot.org/annotation/VSP_006973|||http://purl.uniprot.org/annotation/VSP_006974|||http://purl.uniprot.org/annotation/VSP_006975|||http://purl.uniprot.org/annotation/VSP_006976|||http://purl.uniprot.org/annotation/VSP_006977|||http://purl.uniprot.org/annotation/VSP_006978|||http://purl.uniprot.org/annotation/VSP_006979|||http://purl.uniprot.org/annotation/VSP_006980|||http://purl.uniprot.org/annotation/VSP_006981|||http://purl.uniprot.org/annotation/VSP_043205 http://togogenome.org/gene/10090:Stom ^@ http://purl.uniprot.org/uniprot/P54116 ^@ Chain|||Experimental Information|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain ^@ Chain|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Topological Domain ^@ Abolishes homodimerization and oligomerization. Abolishes regulation of ASIC2 and ASIC3 channel activity.|||Cytoplasmic|||Does not abolish interaction with ASIC3, but abolishes regulation of ASIC2 and ASIC3 channel activity.|||Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-109 and D-145.|||Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-97 and D-109.|||Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-97 and D-145.|||Interaction with LANCL1|||Phosphoserine|||Required for homooligomerization|||Required for lipid raft association|||S-palmitoyl cysteine|||Stomatin ^@ http://purl.uniprot.org/annotation/PRO_0000094028 http://togogenome.org/gene/10090:Nlrp9c ^@ http://purl.uniprot.org/uniprot/Q66X01 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||NACHT|||NACHT, LRR and PYD domains-containing protein 9C|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000286337|||http://purl.uniprot.org/annotation/VSP_025027|||http://purl.uniprot.org/annotation/VSP_025028|||http://purl.uniprot.org/annotation/VSP_025029 http://togogenome.org/gene/10090:Clk2 ^@ http://purl.uniprot.org/uniprot/F8WHX0|||http://purl.uniprot.org/uniprot/O35491 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||Disordered|||Dual specificity protein kinase CLK2|||Loss of phosphorylation.|||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_0000085869 http://togogenome.org/gene/10090:Ms4a6b ^@ http://purl.uniprot.org/uniprot/Q99N09 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Membrane-spanning 4-domains subfamily A member 6B ^@ http://purl.uniprot.org/annotation/PRO_0000158639 http://togogenome.org/gene/10090:Htr1b ^@ http://purl.uniprot.org/uniprot/P28334|||http://purl.uniprot.org/uniprot/Q0VES5 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ 5-hydroxytryptamine receptor 1B|||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|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000068917 http://togogenome.org/gene/10090:Glipr1l1 ^@ http://purl.uniprot.org/uniprot/Q9DAG6 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ GLIPR1-like protein 1|||N-linked (GlcNAc...) asparagine|||SCP ^@ http://purl.uniprot.org/annotation/PRO_5009348226 http://togogenome.org/gene/10090:Kif2c ^@ http://purl.uniprot.org/uniprot/Q3TTL2|||http://purl.uniprot.org/uniprot/Q3UD72|||http://purl.uniprot.org/uniprot/Q922S8 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Strand|||Turn ^@ Disordered|||Globular|||Kinesin motor|||Kinesin-like protein KIF2C|||Loss of microtubule depolymerization activity.|||Microtubule tip localization signal|||Negative regulator of microtubule-binding|||Phosphoserine|||Phosphoserine; by AURKB ^@ http://purl.uniprot.org/annotation/PRO_0000125420 http://togogenome.org/gene/10090:Frs3 ^@ http://purl.uniprot.org/uniprot/Q91WJ0 ^@ 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 ^@ Disordered|||Fibroblast growth factor receptor substrate 3|||IRS-type PTB|||N-myristoyl glycine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087347 http://togogenome.org/gene/10090:Adrb2 ^@ http://purl.uniprot.org/uniprot/P18762 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 4-hydroxyproline|||Beta-2 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|||PDZ-binding|||Phosphoserine|||Phosphoserine; by BARK|||Phosphoserine; by PKA|||Phosphotyrosine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069134 http://togogenome.org/gene/10090:Slc35a5 ^@ http://purl.uniprot.org/uniprot/Q921R7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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_0000309356 http://togogenome.org/gene/10090:AY761185 ^@ http://purl.uniprot.org/uniprot/Q5ERI8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Alpha-defensin N-terminal|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015097872 http://togogenome.org/gene/10090:Papss1 ^@ http://purl.uniprot.org/uniprot/Q3TUA8|||http://purl.uniprot.org/uniprot/Q60967|||http://purl.uniprot.org/uniprot/Q6NZM8 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ ATP-sulfurylase PUA-like|||Adenylyl-sulfate kinase|||Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1|||N-acetylmethionine|||N6-acetyllysine|||Sulfate adenylyltransferase|||Sulphate adenylyltransferase catalytic ^@ http://purl.uniprot.org/annotation/PRO_0000105960 http://togogenome.org/gene/10090:Neurl3 ^@ http://purl.uniprot.org/uniprot/Q8CJC5 ^@ 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 ^@ E3 ubiquitin-protein ligase NEURL3|||In isoform 2.|||NHR|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000325772|||http://purl.uniprot.org/annotation/VSP_032400|||http://purl.uniprot.org/annotation/VSP_032401 http://togogenome.org/gene/10090:Nol6 ^@ http://purl.uniprot.org/uniprot/Q8R5K4 ^@ 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.|||Nucleolar protein 6|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000215648|||http://purl.uniprot.org/annotation/VSP_013533|||http://purl.uniprot.org/annotation/VSP_013534 http://togogenome.org/gene/10090:Tnk2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1L0|||http://purl.uniprot.org/uniprot/A0A5F8MPC4|||http://purl.uniprot.org/uniprot/D3Z3U6|||http://purl.uniprot.org/uniprot/D3Z3U7|||http://purl.uniprot.org/uniprot/G3X9X7|||http://purl.uniprot.org/uniprot/O54967 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Activated CDC42 kinase 1|||Basic and acidic residues|||CRIB|||Disordered|||EBD domain|||In isoform 2 and isoform 3.|||In isoform 2.|||Increase in autophosphorylation activity.|||Loss of CDC42-binding and impairment of autophosphorylation.|||Loss of interaction with NEDD4 and drastic reduction in its ubiquitination.|||Loss of kinase activity.|||Mig-6|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||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_0000088059|||http://purl.uniprot.org/annotation/VSP_008657|||http://purl.uniprot.org/annotation/VSP_008658 http://togogenome.org/gene/10090:Masp2 ^@ http://purl.uniprot.org/uniprot/Q91WP0 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ (3R)-3-hydroxyasparagine|||CUB 1|||CUB 2|||Charge relay system|||Cleavage|||EGF-like; calcium-binding|||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|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi 1|||Sushi 2 ^@ http://purl.uniprot.org/annotation/PRO_0000027601|||http://purl.uniprot.org/annotation/PRO_0000027602|||http://purl.uniprot.org/annotation/PRO_0000027603|||http://purl.uniprot.org/annotation/VSP_014636|||http://purl.uniprot.org/annotation/VSP_014637 http://togogenome.org/gene/10090:Slc35e1 ^@ http://purl.uniprot.org/uniprot/Q8CD26 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Transmembrane ^@ Helical|||Phosphoserine|||Solute carrier family 35 member E1 ^@ http://purl.uniprot.org/annotation/PRO_0000071942 http://togogenome.org/gene/10090:Scoc ^@ http://purl.uniprot.org/uniprot/Q78YZ6 ^@ 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 and isoform 3.|||In isoform 3.|||Short coiled-coil protein ^@ http://purl.uniprot.org/annotation/PRO_0000334165|||http://purl.uniprot.org/annotation/VSP_033646|||http://purl.uniprot.org/annotation/VSP_033647 http://togogenome.org/gene/10090:Sfpq ^@ http://purl.uniprot.org/uniprot/Q8VIJ6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||3 X 3 AA repeats of R-G-G|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||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|||N6,N6-dimethyllysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by MKNK2|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ALK|||Pro residues|||RRM 1|||RRM 2|||Splicing factor, proline- and glutamine-rich ^@ http://purl.uniprot.org/annotation/PRO_0000081910 http://togogenome.org/gene/10090:Arhgdia ^@ http://purl.uniprot.org/uniprot/Q99PT1 ^@ Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||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|||Loss of interaction with CDC42, RHOA and RAC1.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Removed|||Rho GDP-dissociation inhibitor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000219014 http://togogenome.org/gene/10090:Sun2 ^@ http://purl.uniprot.org/uniprot/Q8BJS4 ^@ 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|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Disordered|||Disrupts homotrimerization; disrupts interaction with SYNE2; when associated with A-432.|||Disrupts homotrimerization; disrupts interaction with SYNE2; when associated with A-435.|||Helical|||In isoform 2.|||In isoform 3.|||Interchain (with C-6851 in SYNE2)|||LMNA-binding|||N-linked (GlcNAc...) asparagine|||Nuclear|||Perinuclear space|||Phosphoserine|||Phosphothreonine|||Polar residues|||SUN|||SUN domain-containing protein 2|||Stabilizes homotrimerization; no effect on interaction with SYNE2.|||Sufficient for interaction with SYNE1 and SYNE2 ^@ http://purl.uniprot.org/annotation/PRO_0000218914|||http://purl.uniprot.org/annotation/VSP_039553|||http://purl.uniprot.org/annotation/VSP_039554 http://togogenome.org/gene/10090:Cyp2u1 ^@ http://purl.uniprot.org/uniprot/Q9CX98 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Splice Variant|||Transmembrane ^@ Cytochrome P450 2U1|||Helical|||In isoform 2.|||In isoform 3.|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000291757|||http://purl.uniprot.org/annotation/VSP_026224|||http://purl.uniprot.org/annotation/VSP_026225|||http://purl.uniprot.org/annotation/VSP_026226|||http://purl.uniprot.org/annotation/VSP_026227|||http://purl.uniprot.org/annotation/VSP_026228 http://togogenome.org/gene/10090:Tbc1d2 ^@ http://purl.uniprot.org/uniprot/B1AVH7 ^@ 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.|||Interaction with CADH1|||Interaction with RAC1|||PH|||Phosphoserine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 2A ^@ http://purl.uniprot.org/annotation/PRO_0000395194|||http://purl.uniprot.org/annotation/VSP_039384 http://togogenome.org/gene/10090:Cyp4f37 ^@ http://purl.uniprot.org/uniprot/Q3V1F1 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Nxnl2 ^@ http://purl.uniprot.org/uniprot/Q9D531 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ In isoform 2.|||Nucleoredoxin-like protein 2|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000229736|||http://purl.uniprot.org/annotation/VSP_053273|||http://purl.uniprot.org/annotation/VSP_053274 http://togogenome.org/gene/10090:Ulbp1 ^@ http://purl.uniprot.org/uniprot/Q8HWA3 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099156 http://togogenome.org/gene/10090:Armc6 ^@ http://purl.uniprot.org/uniprot/Q8BNU0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||Armadillo repeat-containing protein 6|||In isoform 2.|||Phosphoserine|||Pros-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000242661|||http://purl.uniprot.org/annotation/VSP_019462|||http://purl.uniprot.org/annotation/VSP_019463 http://togogenome.org/gene/10090:Ing2 ^@ http://purl.uniprot.org/uniprot/Q9ESK4 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Region|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Histone H3K4me3 binding|||Inhibitor of growth protein 2|||PBR|||PHD-type ^@ http://purl.uniprot.org/annotation/PRO_0000212664 http://togogenome.org/gene/10090:Prss22 ^@ http://purl.uniprot.org/uniprot/Q9ER10 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Brain-specific serine protease 4|||Charge relay system|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027505 http://togogenome.org/gene/10090:Cnot10 ^@ http://purl.uniprot.org/uniprot/Q8BH15 ^@ 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 ^@ CCR4-NOT transcription complex subunit 10|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylalanine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000314581|||http://purl.uniprot.org/annotation/VSP_030315|||http://purl.uniprot.org/annotation/VSP_030316|||http://purl.uniprot.org/annotation/VSP_030317|||http://purl.uniprot.org/annotation/VSP_030318|||http://purl.uniprot.org/annotation/VSP_030319|||http://purl.uniprot.org/annotation/VSP_030320 http://togogenome.org/gene/10090:Slc35g2 ^@ http://purl.uniprot.org/uniprot/D3YVE8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Transmembrane ^@ EamA 1|||EamA 2|||Helical|||Phosphoserine|||Solute carrier family 35 member G2 ^@ http://purl.uniprot.org/annotation/PRO_0000416119 http://togogenome.org/gene/10090:Herc3 ^@ http://purl.uniprot.org/uniprot/A6H6S0|||http://purl.uniprot.org/uniprot/Q8CFQ0 ^@ Active Site|||Domain Extent|||Region|||Repeat|||Site ^@ Active Site|||Domain Extent|||Repeat ^@ Glycyl thioester intermediate|||HECT|||RCC1 ^@ http://togogenome.org/gene/10090:Pgm3 ^@ http://purl.uniprot.org/uniprot/Q8BLS4|||http://purl.uniprot.org/uniprot/Q8BWW3|||http://purl.uniprot.org/uniprot/Q9CYR6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Strand ^@ Alpha-D-phosphohexomutase C-terminal|||Alpha-D-phosphohexomutase alpha/beta/alpha|||N-acetylmethionine|||Phosphoacetylglucosamine mutase|||Phosphoserine|||Phosphoserine intermediate|||Phosphothreonine|||via phosphate group ^@ http://purl.uniprot.org/annotation/PRO_0000148014 http://togogenome.org/gene/10090:Cd200l1 ^@ http://purl.uniprot.org/uniprot/E9Q573 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Immunoglobulin V-set|||Immunoglobulin subtype|||Polar residues ^@ http://togogenome.org/gene/10090:Nlrp10 ^@ http://purl.uniprot.org/uniprot/Q3V3Z6|||http://purl.uniprot.org/uniprot/Q6JGS9|||http://purl.uniprot.org/uniprot/Q8CCN1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||NACHT|||NACHT, LRR and PYD domains-containing protein 10|||Polar residues|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000080897 http://togogenome.org/gene/10090:Rras ^@ http://purl.uniprot.org/uniprot/P10833|||http://purl.uniprot.org/uniprot/Q3U1N3 ^@ 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|||Disordered|||Effector region|||Ras-related protein R-Ras|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000082651|||http://purl.uniprot.org/annotation/PRO_0000281301 http://togogenome.org/gene/10090:Or2l13b ^@ http://purl.uniprot.org/uniprot/Q8VF05 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Xpo4 ^@ http://purl.uniprot.org/uniprot/Q9ESJ0 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn ^@ Abolished binding to and nuclear export of hypusinated EIF5A.|||Abolished binding to hypusinated EIF5A.|||Exportin-4|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000204712 http://togogenome.org/gene/10090:Dot1l ^@ http://purl.uniprot.org/uniprot/Q6XZL8 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Basic residues|||DOT1|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Drgx ^@ http://purl.uniprot.org/uniprot/Q8BYH0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Splice Variant ^@ Disordered|||Dorsal root ganglia homeobox protein|||Homeobox|||In isoform 2.|||OAR|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000248487|||http://purl.uniprot.org/annotation/VSP_040392 http://togogenome.org/gene/10090:Il1b ^@ http://purl.uniprot.org/uniprot/P10749 ^@ Chain|||Helix|||Molecule Processing|||Propeptide|||Secondary Structure|||Site|||Strand|||Turn ^@ Chain|||Helix|||Propeptide|||Site|||Strand|||Turn ^@ Important for interaction with integrin|||Interleukin-1 beta ^@ http://purl.uniprot.org/annotation/PRO_0000015311|||http://purl.uniprot.org/annotation/PRO_0000015312 http://togogenome.org/gene/10090:Lrrc23 ^@ http://purl.uniprot.org/uniprot/O35125 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Acidic residues|||Basic and acidic residues|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||Leucine-rich repeat-containing protein 23 ^@ http://purl.uniprot.org/annotation/PRO_0000264237 http://togogenome.org/gene/10090:Bpi ^@ http://purl.uniprot.org/uniprot/Q67E05 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ Bactericidal permeability-increasing protein|||C-terminal barrel|||Central sheet, part 1|||Central sheet, part 2|||Central sheet, part 3|||Cleavage sites for elastase|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||N-terminal barrel ^@ http://purl.uniprot.org/annotation/PRO_0000358332|||http://purl.uniprot.org/annotation/VSP_036069|||http://purl.uniprot.org/annotation/VSP_036070 http://togogenome.org/gene/10090:Ocm ^@ http://purl.uniprot.org/uniprot/P51879 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||EF-hand 1|||EF-hand 2|||N-acetylserine|||Oncomodulin|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073583 http://togogenome.org/gene/10090:Crisp2 ^@ http://purl.uniprot.org/uniprot/P16563 ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Strand ^@ Cysteine-rich secretory protein 2|||SCP|||ShKT ^@ http://purl.uniprot.org/annotation/PRO_0000006266 http://togogenome.org/gene/10090:Abhd15 ^@ http://purl.uniprot.org/uniprot/B6DQM2|||http://purl.uniprot.org/uniprot/Q5F2F2 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Phosphoserine|||Protein ABHD15 ^@ http://purl.uniprot.org/annotation/PRO_0000345396|||http://purl.uniprot.org/annotation/PRO_5015087356 http://togogenome.org/gene/10090:Tead3 ^@ http://purl.uniprot.org/uniprot/F8VPU0|||http://purl.uniprot.org/uniprot/P70210 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant ^@ Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||TEA|||Transcriptional activation|||Transcriptional enhancer factor TEF-5 ^@ http://purl.uniprot.org/annotation/PRO_0000205935 http://togogenome.org/gene/10090:Ptk2 ^@ http://purl.uniprot.org/uniprot/P34152 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes interaction with GRB2.|||Disordered|||FERM|||Focal adhesion kinase 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5 and isoform 7.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Interaction with ARHGEF28|||Interaction with TGFB1I1|||Loss of interaction with ARHGEF28.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by RET and SRC|||Phosphotyrosine; by SRC|||Phosphotyrosine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Removed|||Strongly reduced enzyme activity; when associated with 576-F-F-577. Abolishes activation of MAPK1/ERK2 in response to integrin signaling. Abolishes activation of SRC. Abolishes interaction with PIK3R1.|||Strongly reduced enzyme activity; when associated with F-397. ^@ http://purl.uniprot.org/annotation/PRO_0000088078|||http://purl.uniprot.org/annotation/VSP_060034|||http://purl.uniprot.org/annotation/VSP_060035|||http://purl.uniprot.org/annotation/VSP_060036|||http://purl.uniprot.org/annotation/VSP_060037|||http://purl.uniprot.org/annotation/VSP_060038|||http://purl.uniprot.org/annotation/VSP_060039|||http://purl.uniprot.org/annotation/VSP_060040|||http://purl.uniprot.org/annotation/VSP_060041|||http://purl.uniprot.org/annotation/VSP_060042|||http://purl.uniprot.org/annotation/VSP_060043|||http://purl.uniprot.org/annotation/VSP_060044 http://togogenome.org/gene/10090:Zbtb11 ^@ http://purl.uniprot.org/uniprot/G5E8B9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ BTB|||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|||Polar residues|||Zinc finger and BTB domain-containing protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000447988 http://togogenome.org/gene/10090:Ms4a2 ^@ http://purl.uniprot.org/uniprot/A0A087WPM9|||http://purl.uniprot.org/uniprot/A0A0B4J1P0|||http://purl.uniprot.org/uniprot/B2RTF7|||http://purl.uniprot.org/uniprot/P20490|||http://purl.uniprot.org/uniprot/Q3UNT6 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||High affinity immunoglobulin epsilon receptor subunit beta|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000158630 http://togogenome.org/gene/10090:Casp12 ^@ http://purl.uniprot.org/uniprot/E9Q575|||http://purl.uniprot.org/uniprot/O08736 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Propeptide|||Region ^@ Basic and acidic residues|||CARD|||Caspase family p10|||Caspase family p20|||Caspase-12|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000004647|||http://purl.uniprot.org/annotation/PRO_0000004648 http://togogenome.org/gene/10090:Rheb ^@ http://purl.uniprot.org/uniprot/Q921J2 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Site|||Strand ^@ Binding Site|||Chain|||Crosslink|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Site|||Strand ^@ Abolished farnesylation, impairing localization to endomembrane system.|||Abolishes phosphorylation by MAPKAPK5 and impairs GTP-binding.|||Cysteine methyl ester|||Effector region|||GTP-binding protein Rheb|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired localization to endomembrane system.|||Impairs GTPase activity and increases stimulation of the protein kinase activity of mTORC1.|||Important for autoinhibition of GTPase activity|||Increased affinity for GTP.|||Phosphoserine; by MAPKAPK5|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000082709|||http://purl.uniprot.org/annotation/PRO_0000281366 http://togogenome.org/gene/10090:Pwp1 ^@ http://purl.uniprot.org/uniprot/Q99LL5 ^@ 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 ^@ Acidic residues|||Disordered|||Periodic tryptophan protein 1 homolog|||Phosphoserine|||Phosphothreonine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000051172 http://togogenome.org/gene/10090:Pgap4 ^@ http://purl.uniprot.org/uniprot/Q91YV9 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DXD motif|||Helical|||Lumenal|||Post-GPI attachment to proteins factor 4 ^@ http://purl.uniprot.org/annotation/PRO_0000089732 http://togogenome.org/gene/10090:Or2b2b ^@ http://purl.uniprot.org/uniprot/A2BDD3|||http://purl.uniprot.org/uniprot/K9J6X0 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Domain Extent|||Non-terminal Residue|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trpv5 ^@ http://purl.uniprot.org/uniprot/P69744 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Abolishes interaction with S100A10, plasma membrane localization and channel activity.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Induces faster Ca(2+)-dependent channel inactivation.|||Interaction with S100A10|||Involved in Ca(2+)-dependent inactivation|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pore-forming|||Transient receptor potential cation channel subfamily V member 5 ^@ http://purl.uniprot.org/annotation/PRO_0000215351 http://togogenome.org/gene/10090:Cd300a ^@ http://purl.uniprot.org/uniprot/Q6SJQ0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes internalization after cross-linking.|||CMRF35-like molecule 8|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000320132|||http://purl.uniprot.org/annotation/VSP_031608 http://togogenome.org/gene/10090:Rps27 ^@ http://purl.uniprot.org/uniprot/Q6ZWU9 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Modified Residue|||Region|||Zinc Finger ^@ C4-type|||Disordered|||Phosphoserine|||Small ribosomal subunit protein eS27 ^@ http://purl.uniprot.org/annotation/PRO_0000149052 http://togogenome.org/gene/10090:Grin2a ^@ http://purl.uniprot.org/uniprot/P35436 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Functional determinant of NMDA receptors|||Glutamate receptor ionotropic, NMDA 2A|||Helical|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Pore-forming ^@ http://purl.uniprot.org/annotation/PRO_0000011574 http://togogenome.org/gene/10090:Atp8b1 ^@ http://purl.uniprot.org/uniprot/Q148W0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Acidic residues|||Cytoplasmic|||Disordered|||Exoplasmic loop|||Helical|||Markly decreased expression, hearing loss associated with degeneration of cochlear hair cells and spiral ganglion cells.|||Phospholipid-transporting ATPase IC|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000370862 http://togogenome.org/gene/10090:Gfra4 ^@ http://purl.uniprot.org/uniprot/A2AP45|||http://purl.uniprot.org/uniprot/Q8C1V7|||http://purl.uniprot.org/uniprot/Q9JJT2 ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||GDNF family receptor alpha-4|||GDNF/GAS1|||GPI-anchor amidated threonine|||In isoform a2 and isoform b2.|||In isoform a3 and isoform b3.|||In isoform b1, isoform b2 and isoform b3.|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000010795|||http://purl.uniprot.org/annotation/PRO_0000010796|||http://purl.uniprot.org/annotation/VSP_007226|||http://purl.uniprot.org/annotation/VSP_007227|||http://purl.uniprot.org/annotation/VSP_007228|||http://purl.uniprot.org/annotation/VSP_007229 http://togogenome.org/gene/10090:Sec23a ^@ http://purl.uniprot.org/uniprot/Q01405|||http://purl.uniprot.org/uniprot/Q8C1E4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ Gelsolin-like|||N-acetylthreonine|||Phosphothreonine|||Protein transport protein Sec23A|||Removed|||Sec23/Sec24 beta-sandwich|||Sec23/Sec24 helical|||Sec23/Sec24 trunk|||Zinc finger Sec23/Sec24-type ^@ http://purl.uniprot.org/annotation/PRO_0000205147 http://togogenome.org/gene/10090:Gca ^@ http://purl.uniprot.org/uniprot/Q8VC88 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Grancalcin ^@ http://purl.uniprot.org/annotation/PRO_0000073722 http://togogenome.org/gene/10090:Rps8 ^@ http://purl.uniprot.org/uniprot/P62242|||http://purl.uniprot.org/uniprot/Q497E9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ 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_0000122241 http://togogenome.org/gene/10090:D7Ertd443e ^@ http://purl.uniprot.org/uniprot/D2J0Y4|||http://purl.uniprot.org/uniprot/G3UZF7|||http://purl.uniprot.org/uniprot/Q9D4E0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region ^@ (E2-independent) E3 ubiquitin-conjugating enzyme FATS|||ALMS motif|||Abolishes p53/TP53 polyubiquitination. No effect on interaction with p53/TP53.|||Basic and acidic residues|||Centrosomal protein C10orf90 N-terminal|||Disordered|||No effect on p53/TP53 polyubiquitination.|||Polar residues|||Required for interaction with HDAC1|||Required for interaction with p53/TP53 ^@ http://purl.uniprot.org/annotation/PRO_0000413487 http://togogenome.org/gene/10090:Adgrl2 ^@ http://purl.uniprot.org/uniprot/A0A0G2JGM8 ^@ 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 ^@ Disordered|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Helical|||Olfactomedin-like|||Polar residues|||SUEL-type lectin ^@ http://purl.uniprot.org/annotation/PRO_5002546583 http://togogenome.org/gene/10090:Snap23 ^@ http://purl.uniprot.org/uniprot/A2AKH4|||http://purl.uniprot.org/uniprot/O09044|||http://purl.uniprot.org/uniprot/Q9D3L3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA)|||(Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E)|||Disordered|||Inhibits interaction with ZDHHC13 and ZDHHC17.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||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_0000213599 http://togogenome.org/gene/10090:Sfxn2 ^@ http://purl.uniprot.org/uniprot/Q3UC14|||http://purl.uniprot.org/uniprot/Q925N2 ^@ 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_0000177036 http://togogenome.org/gene/10090:Tsen54 ^@ http://purl.uniprot.org/uniprot/Q8C2A2 ^@ 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.|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||tRNA-splicing endonuclease subunit Sen54 ^@ http://purl.uniprot.org/annotation/PRO_0000194030|||http://purl.uniprot.org/annotation/VSP_010990 http://togogenome.org/gene/10090:Plk5 ^@ http://purl.uniprot.org/uniprot/G3X967|||http://purl.uniprot.org/uniprot/Q4FZD7 ^@ 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|||Inactive serine/threonine-protein kinase PLK5|||Induces cell cycle arrest and neurite differentiation.|||Induces cell cycle arrest.|||POLO box|||POLO box 1|||POLO box 2|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000274545 http://togogenome.org/gene/10090:Hs6st1 ^@ http://purl.uniprot.org/uniprot/Q9QYK5 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Heparan-sulfate 6-O-sulfotransferase 1|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000190802 http://togogenome.org/gene/10090:Plcxd3 ^@ http://purl.uniprot.org/uniprot/G3X9A7|||http://purl.uniprot.org/uniprot/Q8BLJ3 ^@ 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_0000305694 http://togogenome.org/gene/10090:Or52e15 ^@ http://purl.uniprot.org/uniprot/Q8VG28 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Itprid2 ^@ http://purl.uniprot.org/uniprot/Q922B9 ^@ 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.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein ITPRID2 ^@ http://purl.uniprot.org/annotation/PRO_0000072212|||http://purl.uniprot.org/annotation/VSP_023868|||http://purl.uniprot.org/annotation/VSP_023869 http://togogenome.org/gene/10090:Elavl4 ^@ http://purl.uniprot.org/uniprot/Q61701|||http://purl.uniprot.org/uniprot/Q80XH9|||http://purl.uniprot.org/uniprot/Q9CXQ0 ^@ 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 ^@ Asymmetric dimethylarginine; by CARM1; alternate|||Decreased dendritic localization and decreased translation of reporter mRNA, when associated with Ala-149.|||Decreased dendritic localization and decreased translation of reporter mRNA, when associated with Ala-165.|||Disordered|||Disrupts interaction with EIF4A and fails to stimulate translation.|||ELAV-like protein 4|||In isoform 10.|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4, isoform 6, isoform 8 and isoform 9.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Loss of association with polysomes and loss of translation stimulation.|||No impact on interaction with EIF4A.|||Omega-N-methylarginine; by CARM1; alternate|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||RRM 3|||Reduced association with polysomes and reduced stimulation of translation. ^@ http://purl.uniprot.org/annotation/PRO_0000081584|||http://purl.uniprot.org/annotation/VSP_005792|||http://purl.uniprot.org/annotation/VSP_060284|||http://purl.uniprot.org/annotation/VSP_060285|||http://purl.uniprot.org/annotation/VSP_060286|||http://purl.uniprot.org/annotation/VSP_060287|||http://purl.uniprot.org/annotation/VSP_060288|||http://purl.uniprot.org/annotation/VSP_060289|||http://purl.uniprot.org/annotation/VSP_060290|||http://purl.uniprot.org/annotation/VSP_060291 http://togogenome.org/gene/10090:Pdp1 ^@ http://purl.uniprot.org/uniprot/A2AJP9|||http://purl.uniprot.org/uniprot/A8Y5Q0|||http://purl.uniprot.org/uniprot/A8Y5Q1|||http://purl.uniprot.org/uniprot/Q3UV70 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||N6-acetyllysine|||PPM-type phosphatase|||[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000045808 http://togogenome.org/gene/10090:Or5d43 ^@ http://purl.uniprot.org/uniprot/Q7TR24 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ndufc2 ^@ http://purl.uniprot.org/uniprot/Q9CQ54 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane|||Turn ^@ Chain|||Helix|||Strand|||Transmembrane|||Turn ^@ Helical|||NADH dehydrogenase [ubiquinone] 1 subunit C2 ^@ http://purl.uniprot.org/annotation/PRO_0000118839 http://togogenome.org/gene/10090:Epha2 ^@ http://purl.uniprot.org/uniprot/Q03145 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Abolishes interaction with INPPL1 SAM domain.|||Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 2|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells. Inhibits kinase activity. Loss of binding to VAV3 and PI3-kinase p85 subunit.|||Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells. No significant effect on kinase activity. Loss of binding to PI3-kinase p85 subunit.|||Inhibits EFNA1-induced vascular assembly and abolishes kinase activity.|||Inhibits EFNA1-induced vascular assembly and kinase activity.|||Loss of kinase activity and binding to VAV3.|||Mediates interaction with ARHGEF16|||Mediates interaction with CLDN4|||N-linked (GlcNAc...) asparagine|||Negatively regulates interaction with ARHGEF16|||No significant effect on kinase activity and loss of binding to VAV2 and VAV3. Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells, no significant effect on kinase activity, significant reduction in phosphorylation and binding to VAV3; when associated with E-589.|||No significant effect on kinase activity and loss of binding to VAV2 and VAV3. Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells, no significant effect on kinase activity, significant reduction in phosphorylation and binding to VAV3; when associated with E-595.|||No significant effect on kinase activity. Significant reduction in phosphorylation.|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM|||Strongly reduced binding affinity for INPPL1 SAM domain. ^@ http://purl.uniprot.org/annotation/PRO_0000016801 http://togogenome.org/gene/10090:Zfp965 ^@ http://purl.uniprot.org/uniprot/A2BE20 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Itgb2 ^@ http://purl.uniprot.org/uniprot/P11835|||http://purl.uniprot.org/uniprot/Q542I8 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||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-2|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Phosphothreonine|||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_0000016342|||http://purl.uniprot.org/annotation/PRO_5015097760 http://togogenome.org/gene/10090:Iqub ^@ http://purl.uniprot.org/uniprot/Q8CDK3 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||IQ|||IQ and ubiquitin-like domain-containing protein|||Male infertility due to asthenospermia; leads to radial spoke defects, and increased levels of phosphorylated MAPK1/ERK2 and MAPK3/ERK1.|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000274603 http://togogenome.org/gene/10090:Atf7 ^@ http://purl.uniprot.org/uniprot/Q3TZR9|||http://purl.uniprot.org/uniprot/V9GXN6 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ BZIP|||Basic and acidic residues|||C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Rasl10a ^@ http://purl.uniprot.org/uniprot/Q8K5A4 ^@ 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|||Ras-like protein family member 10A|||Removed in mature form|||S-farnesyl cysteine|||Small GTPase-like ^@ http://purl.uniprot.org/annotation/PRO_0000082707|||http://purl.uniprot.org/annotation/PRO_0000281361 http://togogenome.org/gene/10090:Nacc2 ^@ http://purl.uniprot.org/uniprot/Q9DCM7 ^@ 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 ^@ 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_0000263669 http://togogenome.org/gene/10090:Vmn1r117 ^@ http://purl.uniprot.org/uniprot/L7N2C9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Veph1 ^@ http://purl.uniprot.org/uniprot/A1A535 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ In isoform B.|||Interaction with TGFBR1|||PH|||Ventricular zone-expressed PH domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000297956|||http://purl.uniprot.org/annotation/VSP_027434 http://togogenome.org/gene/10090:Cep295nl ^@ http://purl.uniprot.org/uniprot/Q497N6 ^@ 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|||CEP295 N-terminal-like protein|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000422184 http://togogenome.org/gene/10090:Lgals1 ^@ http://purl.uniprot.org/uniprot/P16045 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand ^@ Galectin|||Galectin-1|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000076918 http://togogenome.org/gene/10090:Zfp593 ^@ http://purl.uniprot.org/uniprot/Q9DB42 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||C2H2-type|||Disordered|||Zinc finger protein 593 ^@ http://purl.uniprot.org/annotation/PRO_0000047685 http://togogenome.org/gene/10090:Prpf4b ^@ http://purl.uniprot.org/uniprot/Q61136|||http://purl.uniprot.org/uniprot/Q8C5G1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Acidic residues|||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|||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_0000086587 http://togogenome.org/gene/10090:Grb14 ^@ http://purl.uniprot.org/uniprot/A2ASX2|||http://purl.uniprot.org/uniprot/Q9JLM9 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Growth factor receptor-bound protein 14|||N-acetylthreonine|||PH|||Phosphoserine|||Ras-associating|||Removed|||SH2 ^@ http://purl.uniprot.org/annotation/PRO_0000150349 http://togogenome.org/gene/10090:Trim46 ^@ http://purl.uniprot.org/uniprot/D3YXA6|||http://purl.uniprot.org/uniprot/Q3TC52|||http://purl.uniprot.org/uniprot/Q7TNM2 ^@ 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.|||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_0000056269|||http://purl.uniprot.org/annotation/VSP_011985|||http://purl.uniprot.org/annotation/VSP_011986|||http://purl.uniprot.org/annotation/VSP_011987 http://togogenome.org/gene/10090:Sbspon ^@ http://purl.uniprot.org/uniprot/Q3UPR9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||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_0000332159 http://togogenome.org/gene/10090:Aanat ^@ http://purl.uniprot.org/uniprot/O88816|||http://purl.uniprot.org/uniprot/Q14A64 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Site ^@ Important for the catalytic mechanism; involved in substrate deprotonation|||N-acetyltransferase|||Phosphoserine|||Phosphothreonine; by PKA|||Serotonin N-acetyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000074583 http://togogenome.org/gene/10090:Pgp ^@ http://purl.uniprot.org/uniprot/Q8CHP8 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Site|||Strand ^@ Abolishes phosphatase activity.|||Abolishes phosphatase activity. Abolishes phosphatase activity; when associated with S-67 and R-72. Strongly reduces phosphatase activity; when associated with S-67; R-71 and R-72. Mildly reduces phosphatase activity; when associated with R-71 and R-72.|||Glycerol-3-phosphate phosphatase|||Important for substrate specificity|||Mildly reduces phosphatase activity; when associated with R-71 and A-73. Strongly reduces phosphatase activity; when associated with S-67; R-71 and A-73. Abolishes phosphatase activity; when associated with S-67 and A-73.|||Mildly reduces phosphatase activity; when associated with R-72 and A-73. Strongly reduces phosphatase activity; when associated with S-67; R-72 and A-73.|||Nucleophile|||Proton donor|||Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with N-41 and I-45.|||Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with N-41 and R-44.|||Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with R-44 and I-45.|||Strongly increases activity with pyridoxal phosphate.|||Strongly reduces phosphatase activity; when associated with R-71; R-72 and A-73. Abolishes phosphatase activity; when associated with R-72 and A-73. ^@ http://purl.uniprot.org/annotation/PRO_0000316889 http://togogenome.org/gene/10090:Vmn2r34 ^@ http://purl.uniprot.org/uniprot/E9PVI0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245612 http://togogenome.org/gene/10090:Csf2ra ^@ http://purl.uniprot.org/uniprot/Q00941 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Granulocyte-macrophage colony-stimulating factor receptor subunit alpha|||Helical|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010873 http://togogenome.org/gene/10090:Slco1a5 ^@ http://purl.uniprot.org/uniprot/A0A0G2JDD1|||http://purl.uniprot.org/uniprot/Q91YY5 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||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|||Kazal-like|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Solute carrier organic anion transporter family member 1A5 ^@ http://purl.uniprot.org/annotation/PRO_0000191043 http://togogenome.org/gene/10090:Ankrd10 ^@ http://purl.uniprot.org/uniprot/Q8BG46|||http://purl.uniprot.org/uniprot/Q8BYG1|||http://purl.uniprot.org/uniprot/Q99LW0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 10|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000066906 http://togogenome.org/gene/10090:Zfp397 ^@ http://purl.uniprot.org/uniprot/Q7TNK4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||SCAN box ^@ http://togogenome.org/gene/10090:Smarca1 ^@ http://purl.uniprot.org/uniprot/Q6PGB8 ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ DEAH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Phosphoserine|||Phosphotyrosine|||Probable global transcription activator SNF2L1|||SANT 1|||SANT 2 ^@ http://purl.uniprot.org/annotation/PRO_0000249246|||http://purl.uniprot.org/annotation/VSP_020378 http://togogenome.org/gene/10090:Smchd1 ^@ http://purl.uniprot.org/uniprot/Q6P5D8 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ ATPase activity domain|||Abolishes ATPase activity.|||Abolishes ability to bind DNA without altering the ability of the SMC hinge domain to mediate homodimerization.|||Abolishes homodimerization.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000332145 http://togogenome.org/gene/10090:Pkmyt1 ^@ http://purl.uniprot.org/uniprot/Q9ESG9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Interaction with CDC2-CCNB1|||Interaction with PIN1|||Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase|||Membrane-association motif|||Phosphoserine|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphothreonine; by PLK1|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086574 http://togogenome.org/gene/10090:Ifi30 ^@ http://purl.uniprot.org/uniprot/Q9ESY9 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand ^@ Gamma-interferon-inducible lysosomal thiol reductase|||N-linked (GlcNAc...) asparagine|||Redox-active|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000406221|||http://purl.uniprot.org/annotation/PRO_0000406222|||http://purl.uniprot.org/annotation/PRO_0000406223 http://togogenome.org/gene/10090:Psmd4 ^@ http://purl.uniprot.org/uniprot/O35226|||http://purl.uniprot.org/uniprot/Q3ULG4 ^@ 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 ^@ 26S proteasome non-ATPase regulatory subunit 4|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform Rpn10B and isoform Rpn10C.|||In isoform Rpn10C.|||In isoform Rpn10D.|||In isoform Rpn10E.|||Interaction with UBQLN1|||Phosphoserine|||Phosphothreonine|||UIM 1|||UIM 2|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000173829|||http://purl.uniprot.org/annotation/VSP_005293|||http://purl.uniprot.org/annotation/VSP_005294|||http://purl.uniprot.org/annotation/VSP_005295|||http://purl.uniprot.org/annotation/VSP_005296|||http://purl.uniprot.org/annotation/VSP_005297|||http://purl.uniprot.org/annotation/VSP_005298|||http://purl.uniprot.org/annotation/VSP_005299 http://togogenome.org/gene/10090:Tecrl ^@ http://purl.uniprot.org/uniprot/Q8BFZ1|||http://purl.uniprot.org/uniprot/Q8BWI9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Phosphoserine|||Steroid 5-alpha reductase C-terminal|||Trans-2,3-enoyl-CoA reductase-like ^@ http://purl.uniprot.org/annotation/PRO_0000317714 http://togogenome.org/gene/10090:Scgb3a1 ^@ http://purl.uniprot.org/uniprot/Q5NCL1|||http://purl.uniprot.org/uniprot/Q920D7 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Interchain|||Secretoglobin family 3A member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000036384|||http://purl.uniprot.org/annotation/PRO_5014309902 http://togogenome.org/gene/10090:Or4k48 ^@ http://purl.uniprot.org/uniprot/Q8VGE6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Efcab12 ^@ http://purl.uniprot.org/uniprot/I6L9E6|||http://purl.uniprot.org/uniprot/V9GXH0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||EF-hand|||Polar residues ^@ http://togogenome.org/gene/10090:Mbl1 ^@ http://purl.uniprot.org/uniprot/P39039 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant ^@ 4-hydroxyproline|||5-hydroxylysine|||C-type lectin|||Calcium-dependent carbohydrate binding|||Collagen-like|||Disordered|||In isoform 2.|||Mannose-binding protein A|||O-linked (Gal...) hydroxylysine ^@ http://purl.uniprot.org/annotation/PRO_0000017413|||http://purl.uniprot.org/annotation/VSP_038477 http://togogenome.org/gene/10090:Tas2r143 ^@ http://purl.uniprot.org/uniprot/Q7TQB9 ^@ 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 143 ^@ http://purl.uniprot.org/annotation/PRO_0000082307 http://togogenome.org/gene/10090:Bco1 ^@ http://purl.uniprot.org/uniprot/E9Q321|||http://purl.uniprot.org/uniprot/Q05AC0|||http://purl.uniprot.org/uniprot/Q9JJS6 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Beta,beta-carotene 15,15'-dioxygenase|||Decreased beta-carotene 15,15'-monooxygenase activity.|||Decreased beta-carotene 15,15'-monooxygenase activity. Decreased catalytic efficiency. Loss of beta-carotene 15,15'-monooxygenase activity; when associated with A-140.|||Decreased beta-carotene 15,15'-monooxygenase activity. Decreased catalytic efficiency. Loss of beta-carotene 15,15'-monooxygenase activity; when associated with A-52.|||Disordered|||Loss of beta-carotene 15,15'-monooxygenase activity.|||No effect on protein abundance. Loss of beta-carotene 15,15'-monooxygenase activity. Decreased iron binding.|||No effect on protein abundance. Loss of beta-carotene 15,15'-monooxygenase activity. Loss of iron binding.|||No significant effect on beta-carotene 15,15'-monooxygenase activity.|||No significant effect on beta-carotene 15,15'-monooxygenase activity. Decreased catalytic efficiency.|||No significant effect on beta-carotene 15,15'-monooxygenase activity. Decreased stability. ^@ http://purl.uniprot.org/annotation/PRO_0000143934 http://togogenome.org/gene/10090:Rab17 ^@ http://purl.uniprot.org/uniprot/P35292|||http://purl.uniprot.org/uniprot/Q0PD39 ^@ 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 ^@ Disordered|||Effector region|||Loss of association with membranes and redistribution to the cytosol.|||Phosphoserine|||Probable constitutively active mutant unable to hydrolyze GTP; increases dendrite number and length.|||Ras-related protein Rab-17|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121192 http://togogenome.org/gene/10090:St3gal2 ^@ http://purl.uniprot.org/uniprot/Q11204 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000149259 http://togogenome.org/gene/10090:Nkx2-4 ^@ http://purl.uniprot.org/uniprot/Q9EQM3 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Disordered|||Homeobox|||Homeobox protein Nkx-2.4|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000048936 http://togogenome.org/gene/10090:2300009A05Rik ^@ http://purl.uniprot.org/uniprot/Q0VG49 ^@ Chain|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||Uncharacterized protein C15orf61 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000332741|||http://purl.uniprot.org/annotation/VSP_038577 http://togogenome.org/gene/10090:Snx18 ^@ http://purl.uniprot.org/uniprot/Q8C788 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PX|||Pro residues|||SH3 ^@ http://togogenome.org/gene/10090:Flot1 ^@ http://purl.uniprot.org/uniprot/O08917|||http://purl.uniprot.org/uniprot/Q540I4 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Band 7|||Flotillin-1|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000094045 http://togogenome.org/gene/10090:Cdk5rap3 ^@ http://purl.uniprot.org/uniprot/Q99LM2 ^@ Chain|||Crosslink|||Modification|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Region ^@ CDK5 regulatory subunit-associated protein 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Required for interaction with UFL1 and mediates interaction with CHEK1 ^@ http://purl.uniprot.org/annotation/PRO_0000220517 http://togogenome.org/gene/10090:Mpped2 ^@ http://purl.uniprot.org/uniprot/B1APT2|||http://purl.uniprot.org/uniprot/Q9CZJ0 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Calcineurin-like phosphoesterase|||Metallophosphoesterase MPPED2 ^@ http://purl.uniprot.org/annotation/PRO_0000053406 http://togogenome.org/gene/10090:4930562C15Rik ^@ http://purl.uniprot.org/uniprot/E9QMW4 ^@ 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.|||Uncharacterized protein C16orf96 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000413539|||http://purl.uniprot.org/annotation/VSP_042127 http://togogenome.org/gene/10090:Nudt4 ^@ http://purl.uniprot.org/uniprot/Q4FJR0|||http://purl.uniprot.org/uniprot/Q8R2U6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Strand|||Turn ^@ Diphosphoinositol polyphosphate phosphohydrolase 2|||Nudix box|||Nudix hydrolase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000057059 http://togogenome.org/gene/10090:Xrra1 ^@ http://purl.uniprot.org/uniprot/Q3U3V8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Polar residues|||X-ray radiation resistance-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000318132 http://togogenome.org/gene/10090:Spi1 ^@ http://purl.uniprot.org/uniprot/P17433|||http://purl.uniprot.org/uniprot/Q3U5L4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||ETS|||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_0000204133 http://togogenome.org/gene/10090:Cebpz ^@ http://purl.uniprot.org/uniprot/A0A0R4J046|||http://purl.uniprot.org/uniprot/P53569 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||CCAAT-binding factor|||CCAAT/enhancer-binding protein zeta|||Disordered|||In isoform CBF2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000173471|||http://purl.uniprot.org/annotation/VSP_000853|||http://purl.uniprot.org/annotation/VSP_000854 http://togogenome.org/gene/10090:Tyw5 ^@ http://purl.uniprot.org/uniprot/A2RSX7 ^@ 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 ^@ In isoform 2.|||JmjC|||tRNA wybutosine-synthesizing protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000309275|||http://purl.uniprot.org/annotation/VSP_029107|||http://purl.uniprot.org/annotation/VSP_029108 http://togogenome.org/gene/10090:Adgrl4 ^@ http://purl.uniprot.org/uniprot/Q923X1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Adhesion G protein-coupled receptor L4|||Cleavage|||Cytoplasmic|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; 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_0000012871 http://togogenome.org/gene/10090:Zfp142 ^@ http://purl.uniprot.org/uniprot/G5E869 ^@ 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 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger protein 142 ^@ http://purl.uniprot.org/annotation/PRO_0000447987|||http://purl.uniprot.org/annotation/VSP_060316|||http://purl.uniprot.org/annotation/VSP_060317 http://togogenome.org/gene/10090:Cpt1a ^@ http://purl.uniprot.org/uniprot/P97742|||http://purl.uniprot.org/uniprot/Q3UGT1|||http://purl.uniprot.org/uniprot/Q7TQD5 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 3'-nitrotyrosine|||Carnitine O-palmitoyltransferase 1, liver isoform|||Carnitine O-palmitoyltransferase N-terminal|||Choline/carnitine acyltransferase|||Cytoplasmic|||Helical|||Mitochondrial intermembrane|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000210160 http://togogenome.org/gene/10090:Hus1 ^@ http://purl.uniprot.org/uniprot/Q8BQY8 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ Checkpoint protein HUS1|||In isoform 2 and isoform 3.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000225004|||http://purl.uniprot.org/annotation/VSP_017332|||http://purl.uniprot.org/annotation/VSP_017333 http://togogenome.org/gene/10090:Gpi1 ^@ http://purl.uniprot.org/uniprot/P06745 ^@ 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 ^@ Glucose-6-phosphate isomerase|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000180538 http://togogenome.org/gene/10090:Adat1 ^@ http://purl.uniprot.org/uniprot/Q9JHI2 ^@ 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 ^@ A to I editase|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Proton donor|||tRNA-specific adenosine deaminase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000287648|||http://purl.uniprot.org/annotation/VSP_025580|||http://purl.uniprot.org/annotation/VSP_025581 http://togogenome.org/gene/10090:Gm6040 ^@ http://purl.uniprot.org/uniprot/Q4QY32 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015097641 http://togogenome.org/gene/10090:Ptprb ^@ http://purl.uniprot.org/uniprot/A0A1W2P7W3|||http://purl.uniprot.org/uniprot/B2RU80 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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|||Loss of activity and dephosphorylation of CDH5.|||Loss of tyrosine phosphorylation. Abolishes interaction with FYN and GRB2.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphotyrosine|||Polar residues|||Receptor-type tyrosine-protein phosphatase beta|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||protein-tyrosine-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000390401|||http://purl.uniprot.org/annotation/PRO_5015071728 http://togogenome.org/gene/10090:Cwc27 ^@ http://purl.uniprot.org/uniprot/Q3TKY6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||N-acetylserine|||PPIase cyclophilin-type|||Polar residues|||Removed|||Spliceosome-associated protein CWC27 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000313649 http://togogenome.org/gene/10090:Gars ^@ http://purl.uniprot.org/uniprot/Q9CZD3 ^@ 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|||Sequence Conflict|||Sequence Variant|||Transit Peptide ^@ Found in Nmf249 mice, a Charcot-Marie-Tooth 2D model; involved in neuromuscular dysfunction; contrary to the wild-type protein, strongly interacts with NRP1 and competes with VEGFA for NRP1-binding; no effect on subcellular location.|||Glycine--tRNA ligase|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||WHEP-TRS ^@ http://purl.uniprot.org/annotation/PRO_0000072999 http://togogenome.org/gene/10090:Il6ra ^@ http://purl.uniprot.org/uniprot/A0A0G2JGF1|||http://purl.uniprot.org/uniprot/P22272|||http://purl.uniprot.org/uniprot/Q3URV7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cleavage; by ADAM10 and ADAM17|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like|||Ig-like C2-type|||Interleukin-6 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Soluble interleukin-6 receptor subunit alpha|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010896|||http://purl.uniprot.org/annotation/PRO_0000450731|||http://purl.uniprot.org/annotation/PRO_5002546578|||http://purl.uniprot.org/annotation/PRO_5004230307 http://togogenome.org/gene/10090:Akap5 ^@ http://purl.uniprot.org/uniprot/D3YVF0|||http://purl.uniprot.org/uniprot/H3BIV5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Motif|||Region|||Repeat ^@ 10|||11|||12|||13|||14; approximate|||15; approximate|||16|||17|||18|||19|||1; approximate|||20; approximate|||21|||22; approximate|||23; approximate|||24; approximate|||25|||26; approximate|||27; approximate|||28 X 8 AA repeats of V-G-Q-A-E-E-A-T|||28; approximate|||2; approximate|||3; approximate|||4; approximate|||5; approximate|||6; approximate|||7; approximate|||8; approximate|||9|||A kinase-anchoring proteins AKAP-5 and AKAP-12 calmodulin (CaM)-binding|||A-kinase anchor protein 5|||AKAP CaM-binding|||Basic and acidic residues|||Basic residues|||Disordered|||Essential to the intracellular anchoring function|||Phosphoserine|||Polar residues|||RII-beta subunit binding domain|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000414750 http://togogenome.org/gene/10090:Tinagl1 ^@ http://purl.uniprot.org/uniprot/Q99JR5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Alternate|||N-linked (GlcNAc...) asparagine|||SMB|||Tubulointerstitial nephritis antigen-like ^@ http://purl.uniprot.org/annotation/PRO_0000026483 http://togogenome.org/gene/10090:Rgs12 ^@ http://purl.uniprot.org/uniprot/D3Z0G5|||http://purl.uniprot.org/uniprot/E9Q1K7|||http://purl.uniprot.org/uniprot/E9Q652|||http://purl.uniprot.org/uniprot/Q3TTW9|||http://purl.uniprot.org/uniprot/Q8BPL6|||http://purl.uniprot.org/uniprot/Q8CGE9|||http://purl.uniprot.org/uniprot/Q9D677 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||GoLoco|||Omega-N-methylarginine|||PDZ|||PID|||Phosphoserine|||Polar residues|||Pro residues|||RBD|||RBD 1|||RBD 2|||RGS|||Regulator of G-protein signaling 12 ^@ http://purl.uniprot.org/annotation/PRO_0000408474 http://togogenome.org/gene/10090:Atp5e ^@ http://purl.uniprot.org/uniprot/P56382 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ ATP synthase subunit epsilon, mitochondrial|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000071663 http://togogenome.org/gene/10090:Spef2 ^@ http://purl.uniprot.org/uniprot/Q8C9J3 ^@ 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|||Calponin-homology (CH)|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with IFT20|||Sperm flagellar protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000299030|||http://purl.uniprot.org/annotation/VSP_027526|||http://purl.uniprot.org/annotation/VSP_027527|||http://purl.uniprot.org/annotation/VSP_027528|||http://purl.uniprot.org/annotation/VSP_027529|||http://purl.uniprot.org/annotation/VSP_059848|||http://purl.uniprot.org/annotation/VSP_059849 http://togogenome.org/gene/10090:Clcn6 ^@ http://purl.uniprot.org/uniprot/O35454|||http://purl.uniprot.org/uniprot/Q3UM91 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Site|||Topological Domain|||Transmembrane ^@ CBS|||CBS 1|||CBS 2|||Cytoplasmic|||H(+)/Cl(-) exchange transporter 6|||Helical|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000094450 http://togogenome.org/gene/10090:Or5t18 ^@ http://purl.uniprot.org/uniprot/A0A1L1STV1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ggt1 ^@ http://purl.uniprot.org/uniprot/Q4FK56|||http://purl.uniprot.org/uniprot/Q60928 ^@ 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|||Extracellular|||Glutathione hydrolase 1 heavy chain|||Glutathione hydrolase 1 light chain|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000011060|||http://purl.uniprot.org/annotation/PRO_0000011061 http://togogenome.org/gene/10090:Cldn24 ^@ http://purl.uniprot.org/uniprot/D3YXJ9 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Set ^@ http://purl.uniprot.org/uniprot/Q3T9S3|||http://purl.uniprot.org/uniprot/Q9EQU5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Almost abolishes N-terminal methylation at A-2.|||Basic and acidic residues|||Dimerization|||Disordered|||Earmuff domain|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||N,N,N-trimethylalanine; by NTM1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Protein SET|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000185663|||http://purl.uniprot.org/annotation/VSP_009869|||http://purl.uniprot.org/annotation/VSP_009870|||http://purl.uniprot.org/annotation/VSP_009871 http://togogenome.org/gene/10090:Snx19 ^@ http://purl.uniprot.org/uniprot/Q6P4T1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand ^@ Abolishes interaction with membranes enriched in phosphatidylinositol 3-phosphate.|||Abolishes interaction with membranes enriched in phosphatidylinositol 3-phosphate. Abolishes location on endosome membranes.|||Abolishes location on endosome membranes.|||Basic and acidic residues|||Disordered|||PX|||PXA|||Sorting nexin-19 ^@ http://purl.uniprot.org/annotation/PRO_0000434599 http://togogenome.org/gene/10090:Plcd1 ^@ http://purl.uniprot.org/uniprot/G5DDB7|||http://purl.uniprot.org/uniprot/Q8R3B1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1|||C2|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||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_0000088505 http://togogenome.org/gene/10090:Ergic3 ^@ http://purl.uniprot.org/uniprot/Q9CQE7 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endoplasmic reticulum-Golgi intermediate compartment protein 3|||Helical|||In isoform 2.|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Required for MARCHF2-mediated degradation|||Ubiquitinated; by MARCHF2 ^@ http://purl.uniprot.org/annotation/PRO_0000097641|||http://purl.uniprot.org/annotation/VSP_019209|||http://purl.uniprot.org/annotation/VSP_019210 http://togogenome.org/gene/10090:Ebpl ^@ http://purl.uniprot.org/uniprot/Q9D0P0 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ EXPERA|||Emopamil-binding protein-like|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000174348 http://togogenome.org/gene/10090:Magea10 ^@ http://purl.uniprot.org/uniprot/A2AMW4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Pga5 ^@ http://purl.uniprot.org/uniprot/Q9D106 ^@ 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-5|||Peptidase A1 ^@ http://purl.uniprot.org/annotation/PRO_0000436776|||http://purl.uniprot.org/annotation/PRO_0000436777 http://togogenome.org/gene/10090:Or51ag1 ^@ http://purl.uniprot.org/uniprot/E9Q598 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Acsm1 ^@ http://purl.uniprot.org/uniprot/Q91VA0 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ 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_0000306092|||http://purl.uniprot.org/annotation/VSP_028392 http://togogenome.org/gene/10090:Gm6460 ^@ http://purl.uniprot.org/uniprot/Q2TB45 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Ddx39b ^@ http://purl.uniprot.org/uniprot/Q9Z1N5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Acidic residues|||DECD box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||N-acetylalanine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Q motif|||Removed|||Spliceosome RNA helicase Ddx39b ^@ http://purl.uniprot.org/annotation/PRO_0000055073 http://togogenome.org/gene/10090:Rabggtb ^@ http://purl.uniprot.org/uniprot/P53612 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ Geranylgeranyl transferase type-2 subunit beta|||PFTB 1|||PFTB 2|||PFTB 3|||PFTB 4|||PFTB 5|||PFTB 6|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000119773 http://togogenome.org/gene/10090:Upk1b ^@ http://purl.uniprot.org/uniprot/Q9Z2C6 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Uroplakin-1b ^@ http://purl.uniprot.org/annotation/PRO_0000219290 http://togogenome.org/gene/10090:Myh15 ^@ http://purl.uniprot.org/uniprot/E9Q264 ^@ Binding Site|||Coiled-Coil|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Domain Extent|||Region ^@ Actin-binding|||Disordered|||Myosin N-terminal SH3-like|||Myosin motor ^@ http://togogenome.org/gene/10090:Tedc1 ^@ http://purl.uniprot.org/uniprot/Q3UK37 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict ^@ Disordered|||Tubulin epsilon and delta complex protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000330693 http://togogenome.org/gene/10090:Zfp444 ^@ http://purl.uniprot.org/uniprot/Q3TDV8 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||SCAN box ^@ http://togogenome.org/gene/10090:Defa39 ^@ http://purl.uniprot.org/uniprot/Q9D848 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ Alpha-defensin N-terminal|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015099693 http://togogenome.org/gene/10090:Dusp28 ^@ http://purl.uniprot.org/uniprot/Q8BTR5 ^@ Active Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand ^@ Active Site|||Chain|||Domain Extent|||Helix|||Strand ^@ Dual specificity phosphatase 28|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000302841 http://togogenome.org/gene/10090:Stx16 ^@ http://purl.uniprot.org/uniprot/Q0VGN4|||http://purl.uniprot.org/uniprot/Q8BVI5|||http://purl.uniprot.org/uniprot/Q8C0W8 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Helical; Anchor for type IV membrane protein|||Phosphoserine|||Syntaxin-16|||T-SNARE coiled-coil homology|||Vesicular|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000210227 http://togogenome.org/gene/10090:Aqp9 ^@ http://purl.uniprot.org/uniprot/D3YYD6|||http://purl.uniprot.org/uniprot/Q4FK77|||http://purl.uniprot.org/uniprot/Q9JJJ3 ^@ Chain|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Motif|||Topological Domain|||Transmembrane ^@ Aquaporin-9|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||NPA 1|||NPA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000063965 http://togogenome.org/gene/10090:Rock1 ^@ http://purl.uniprot.org/uniprot/P70335|||http://purl.uniprot.org/uniprot/Q3UE22 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Zinc Finger ^@ AGC-kinase C-terminal|||Auto-inhibitory|||Cleavage; by caspase-3|||Disordered|||In isoform 2.|||Interaction with FHOD1|||N-acetylserine|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Protein kinase|||Proton acceptor|||REM-1|||RHOA binding|||Removed|||Rho-associated protein kinase 1|||RhoBD|||SHROOM3 binding ^@ http://purl.uniprot.org/annotation/PRO_0000086620|||http://purl.uniprot.org/annotation/VSP_010448 http://togogenome.org/gene/10090:Clcn7 ^@ http://purl.uniprot.org/uniprot/E9PYL4|||http://purl.uniprot.org/uniprot/O70496|||http://purl.uniprot.org/uniprot/Q6RUT9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||CBS|||CBS 1|||CBS 2|||Cytoplasmic|||Disordered|||H(+)/Cl(-) exchange transporter 7|||Helical|||Increased cytoplasmic vacuole size. Knockin mice develop albinism and lysosomal-storage disease.|||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_0000094453 http://togogenome.org/gene/10090:Zfp819 ^@ http://purl.uniprot.org/uniprot/Q80V81|||http://purl.uniprot.org/uniprot/Q9D4A7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Iqcf3 ^@ http://purl.uniprot.org/uniprot/A0A571BEE9|||http://purl.uniprot.org/uniprot/Q9D498 ^@ 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|||IQ|||IQ domain-containing protein F3 ^@ http://purl.uniprot.org/annotation/PRO_0000339382 http://togogenome.org/gene/10090:Erlin2 ^@ http://purl.uniprot.org/uniprot/Q8BFZ9 ^@ 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|||Erlin-2|||Helical|||Interaction with ERLIN1|||Lumenal|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000002788 http://togogenome.org/gene/10090:Cacna1c ^@ http://purl.uniprot.org/uniprot/A0A087WS40|||http://purl.uniprot.org/uniprot/A0A087WSE7|||http://purl.uniprot.org/uniprot/C7TQ57|||http://purl.uniprot.org/uniprot/C7TQ58|||http://purl.uniprot.org/uniprot/C7TQ59|||http://purl.uniprot.org/uniprot/C7TQ60|||http://purl.uniprot.org/uniprot/C7TQ61|||http://purl.uniprot.org/uniprot/C7TQ62|||http://purl.uniprot.org/uniprot/F7C376|||http://purl.uniprot.org/uniprot/F8WJL1|||http://purl.uniprot.org/uniprot/Q01815|||http://purl.uniprot.org/uniprot/Q0PCR6 ^@ 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|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ AID/alpha-interaction domain; mediates interaction with the beta subunit|||Basic and acidic residues|||Calmodulin-binding|||Calmodulin-binding IQ region|||Cytoplasmic|||Dihydropyridine binding|||Disordered|||Expected to abolish a phosphorylation site. Decreased channel activity. No effect on phosphorylation at S-1897. Causes heart hypertrophy and decreased exercise tolerance in adult mice.|||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|||Important for interaction with STAC1, STAC2 and STAC3|||Important for localization in at the junctional membrane|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Interaction with STAC2|||Loss of phosphorylation site. Abolishes increased vasoconstriction in response to elevated blood glucose.|||N-linked (GlcNAc...) asparagine|||Phenylalkylamine binding|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Pore-forming|||Pro residues|||Selectivity filter of repeat I|||Selectivity filter of repeat II|||Selectivity filter of repeat III|||Selectivity filter of repeat IV|||Strongly decreased channel activity due to decreased expression at the cell membrane, leading to hypertrophy of the right heart ventricle, heart failure and perinatal death; when associated with 1794-L--K-1796.|||Strongly decreased channel activity due to decreased expression at the cell membrane, leading to hypertrophy of the right heart ventricle, heart failure and perinatal death; when associated with 1797-P--L-2139 DEL.|||Voltage-dependent L-type calcium channel subunit alpha-1C|||Voltage-dependent calcium channel alpha-1 subunit IQ ^@ http://purl.uniprot.org/annotation/PRO_0000053929|||http://purl.uniprot.org/annotation/VSP_000896|||http://purl.uniprot.org/annotation/VSP_000897|||http://purl.uniprot.org/annotation/VSP_000898|||http://purl.uniprot.org/annotation/VSP_000899|||http://purl.uniprot.org/annotation/VSP_000900|||http://purl.uniprot.org/annotation/VSP_000901 http://togogenome.org/gene/10090:Or2ag2b ^@ http://purl.uniprot.org/uniprot/Q9D3U9|||http://purl.uniprot.org/uniprot/Q9D4F9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kbtbd3 ^@ http://purl.uniprot.org/uniprot/Q8BHI4 ^@ 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 repeat and BTB domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000119079 http://togogenome.org/gene/10090:Lin7c ^@ http://purl.uniprot.org/uniprot/O88952 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif ^@ Kinase interacting site|||L27|||N-acetylalanine|||PDZ|||Protein lin-7 homolog C|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000189630 http://togogenome.org/gene/10090:Tmem79 ^@ http://purl.uniprot.org/uniprot/Q9D709 ^@ 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|||Polar residues|||Transmembrane protein 79 ^@ http://purl.uniprot.org/annotation/PRO_0000254119 http://togogenome.org/gene/10090:Lpin3 ^@ http://purl.uniprot.org/uniprot/Q149B0|||http://purl.uniprot.org/uniprot/Q571G1|||http://purl.uniprot.org/uniprot/Q99PI4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||C-LIP|||DXDXT motif|||Disordered|||LNS2/PITP|||LXXIL motif|||N-LIP|||Nuclear localization signal|||Phosphatidate phosphatase LPIN3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000209884 http://togogenome.org/gene/10090:Dhx8 ^@ http://purl.uniprot.org/uniprot/A2A4P0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region ^@ ATP-dependent RNA helicase DHX8|||Basic and acidic residues|||Basic residues|||DEAH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||S1 motif ^@ http://purl.uniprot.org/annotation/PRO_0000330831 http://togogenome.org/gene/10090:Rpl21 ^@ http://purl.uniprot.org/uniprot/O09167 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Large ribosomal subunit protein eL21 ^@ http://purl.uniprot.org/annotation/PRO_0000149670 http://togogenome.org/gene/10090:Pappa ^@ http://purl.uniprot.org/uniprot/Q8R4K8 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||Interchain|||Interchain (with C-170 in PRG2 proform)|||Interchain (with C-49 in PRG2 proform)|||Metalloprotease|||N-linked (GlcNAc...) asparagine|||Or C-580 with C-609|||Or C-584 with C-597|||Pappalysin-1|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5 ^@ http://purl.uniprot.org/annotation/PRO_0000029247|||http://purl.uniprot.org/annotation/PRO_0000029248|||http://purl.uniprot.org/annotation/VSP_012193 http://togogenome.org/gene/10090:Efs ^@ http://purl.uniprot.org/uniprot/Q64355 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Diminishes the ability to induce SRC-mediated activation of luciferase.|||Disordered|||Divergent helix-loop-helix motif|||Embryonal Fyn-associated substrate|||Phosphotyrosine; by SRC|||Polar residues|||Pro residues|||SH3|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000086941 http://togogenome.org/gene/10090:Rhox11 ^@ http://purl.uniprot.org/uniprot/Q810N8 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Gm14295 ^@ http://purl.uniprot.org/uniprot/A2BG90 ^@ Domain Extent|||Region ^@ Domain Extent ^@ KRAB ^@ http://togogenome.org/gene/10090:Cpeb1 ^@ http://purl.uniprot.org/uniprot/P70166|||http://purl.uniprot.org/uniprot/Q059Z2 ^@ 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|||Site ^@ Cytoplasmic polyadenylation element-binding protein 1|||Disordered|||Important for the positionning of RRM1 relative to RRM2|||Inhibits CPE-containing cytoplasmic polyadenylation and translation activation.|||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_0000269252 http://togogenome.org/gene/10090:Vegfb ^@ http://purl.uniprot.org/uniprot/P49766 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform VEGF-B167.|||Interchain|||Vascular endothelial growth factor B ^@ http://purl.uniprot.org/annotation/PRO_0000023399|||http://purl.uniprot.org/annotation/VSP_004641 http://togogenome.org/gene/10090:Ngly1 ^@ http://purl.uniprot.org/uniprot/Q9JI78 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn ^@ Abolishes enzyme activity.|||Abolishes interaction with VCP.|||Does not affect the interaction with VCP.|||N-acetylalanine|||Nucleophile|||PAW|||PUB|||Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000248973 http://togogenome.org/gene/10090:4930596D02Rik ^@ http://purl.uniprot.org/uniprot/Q3V0H9 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Tesc ^@ http://purl.uniprot.org/uniprot/D0EM45|||http://purl.uniprot.org/uniprot/Q9JKL5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes calcium-binding. Does not alter subcellular localization and does not prevent inhibition of calcineurin activity.|||Calcineurin B homologous protein 3|||Disordered|||EF-hand|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073860 http://togogenome.org/gene/10090:Galk1 ^@ http://purl.uniprot.org/uniprot/Q9CXZ9|||http://purl.uniprot.org/uniprot/Q9R0N0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site ^@ GHMP kinase C-terminal|||GHMP kinase N-terminal|||Galactokinase|||Galactokinase N-terminal|||Phosphoserine|||Proton acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000184646 http://togogenome.org/gene/10090:Acer1 ^@ http://purl.uniprot.org/uniprot/Q8R4X1 ^@ 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_0000247746 http://togogenome.org/gene/10090:Sgo2b ^@ http://purl.uniprot.org/uniprot/J3QMK1 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gpr61 ^@ http://purl.uniprot.org/uniprot/Q8C010 ^@ 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|||Extracellular|||G-protein coupled receptor 61|||Helical; 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_0000069579 http://togogenome.org/gene/10090:P3r3urf ^@ http://purl.uniprot.org/uniprot/B1AUF7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||PIK3R3 upstream open reading frame protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000446329 http://togogenome.org/gene/10090:Diablo ^@ http://purl.uniprot.org/uniprot/Q9JIQ3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Basic and acidic residues|||Cleavage; by PARL|||Diablo IAP-binding mitochondrial protein|||Diablo IAP-binding mitochondrial protein, cleaved form|||Disordered|||IAP-binding|||Mitochondrion|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000021073|||http://purl.uniprot.org/annotation/PRO_0000458410 http://togogenome.org/gene/10090:Impg2 ^@ http://purl.uniprot.org/uniprot/Q80XH2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Decreased-binding affinity to hyaluronan.|||Disordered|||EGF-like 1|||EGF-like 2|||Extracellular|||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|||Important decrease in binding affinity to hyaluronan.|||In isoform 2.|||Interphotoreceptor matrix proteoglycan 2|||Most important decrease in binding affinity to hyaluronan.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Polar residues|||SEA 1|||SEA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000320150|||http://purl.uniprot.org/annotation/VSP_031612 http://togogenome.org/gene/10090:Tnni3 ^@ http://purl.uniprot.org/uniprot/P48787|||http://purl.uniprot.org/uniprot/Q497F1 ^@ Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site ^@ Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Site ^@ Disordered|||Involved in TNI-TNT interactions|||Involved in binding TNC|||Involved in binding TNC and actin|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by PKA and PKD/PRKD1|||Phosphoserine; by PKC/PRKCE|||Phosphothreonine|||Phosphothreonine; by STK4/MST1|||Phosphotyrosine|||Removed|||Troponin I, cardiac muscle ^@ http://purl.uniprot.org/annotation/PRO_0000186153 http://togogenome.org/gene/10090:Mfsd6l ^@ http://purl.uniprot.org/uniprot/Q8R3N2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Major facilitator superfamily domain-containing protein 6-like|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000321945 http://togogenome.org/gene/10090:Dnpep ^@ http://purl.uniprot.org/uniprot/Q9Z2W0 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Aspartyl aminopeptidase|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000173452 http://togogenome.org/gene/10090:Zdhhc22 ^@ http://purl.uniprot.org/uniprot/A0PK84 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Helical|||Lumenal|||Palmitoyltransferase ZDHHC22|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000278772 http://togogenome.org/gene/10090:Gk2 ^@ http://purl.uniprot.org/uniprot/Q9WU65 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Glycerol kinase 2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000343678 http://togogenome.org/gene/10090:Atl2 ^@ http://purl.uniprot.org/uniprot/E9QND8|||http://purl.uniprot.org/uniprot/Q6PA06|||http://purl.uniprot.org/uniprot/Q8BYP9|||http://purl.uniprot.org/uniprot/Q8C081|||http://purl.uniprot.org/uniprot/Q9D873 ^@ 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|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Atlastin-2|||Cytoplasmic|||Disordered|||GB1/RHD3-type G|||Helical|||In isoform 2.|||Lumenal|||N6-methyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000287107|||http://purl.uniprot.org/annotation/VSP_025311 http://togogenome.org/gene/10090:Fam98a ^@ http://purl.uniprot.org/uniprot/Q3TJZ6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Protein FAM98A ^@ http://purl.uniprot.org/annotation/PRO_0000187185 http://togogenome.org/gene/10090:Ppp2r5c ^@ http://purl.uniprot.org/uniprot/Q60996|||http://purl.uniprot.org/uniprot/Q6ZQK4 ^@ 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|||Basic residues|||Disordered|||In isoform 1.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Polar residues|||Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform ^@ http://purl.uniprot.org/annotation/PRO_0000071458|||http://purl.uniprot.org/annotation/VSP_014718|||http://purl.uniprot.org/annotation/VSP_014719|||http://purl.uniprot.org/annotation/VSP_014720|||http://purl.uniprot.org/annotation/VSP_038641|||http://purl.uniprot.org/annotation/VSP_038642 http://togogenome.org/gene/10090:Meis2 ^@ http://purl.uniprot.org/uniprot/A0A0A7EPH8|||http://purl.uniprot.org/uniprot/B1AWK4|||http://purl.uniprot.org/uniprot/P97367|||http://purl.uniprot.org/uniprot/Q3TY73|||http://purl.uniprot.org/uniprot/Q3TYM2|||http://purl.uniprot.org/uniprot/Q3UJ35|||http://purl.uniprot.org/uniprot/Q6GU28 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Homeobox|||Homeobox protein Meis2|||Homeobox; TALE-type|||In isoform Meis2A and isoform Meis2B.|||In isoform Meis2B and isoform Meis2D.|||Interaction with DNA|||MEIS N-terminal|||Polar residues|||Required for interaction with PBX1|||Transcriptional activation domain ^@ http://purl.uniprot.org/annotation/PRO_0000049109|||http://purl.uniprot.org/annotation/VSP_002247|||http://purl.uniprot.org/annotation/VSP_002248|||http://purl.uniprot.org/annotation/VSP_002249 http://togogenome.org/gene/10090:Or6c217 ^@ http://purl.uniprot.org/uniprot/Q8VFU0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nid2 ^@ http://purl.uniprot.org/uniprot/O88322|||http://purl.uniprot.org/uniprot/Q3TPN0|||http://purl.uniprot.org/uniprot/Q8C6Z2|||http://purl.uniprot.org/uniprot/Q8R5G0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Cell attachment site|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5; calcium-binding|||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|||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|||Thyroglobulin type-1 1|||Thyroglobulin type-1 2 ^@ http://purl.uniprot.org/annotation/PRO_0000007672|||http://purl.uniprot.org/annotation/PRO_5004229649|||http://purl.uniprot.org/annotation/PRO_5004304350|||http://purl.uniprot.org/annotation/PRO_5004313914 http://togogenome.org/gene/10090:Tmem158 ^@ http://purl.uniprot.org/uniprot/B2RTM1 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015087157 http://togogenome.org/gene/10090:Calml4 ^@ http://purl.uniprot.org/uniprot/A0A1L1SR54|||http://purl.uniprot.org/uniprot/E9Q1L1|||http://purl.uniprot.org/uniprot/Q91WQ9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ Calmodulin-like protein 4|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000314934|||http://purl.uniprot.org/annotation/VSP_030437|||http://purl.uniprot.org/annotation/VSP_030438 http://togogenome.org/gene/10090:Btbd35f23 ^@ http://purl.uniprot.org/uniprot/A0A0R4J2B9|||http://purl.uniprot.org/uniprot/Q99N64 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Motif|||Sequence Conflict ^@ BTB|||Germ cell-less protein-like 2|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000087522 http://togogenome.org/gene/10090:Ppp2ca ^@ http://purl.uniprot.org/uniprot/P63330 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ Leucine methyl ester|||Loss of binding to PP2AB-alpha regulatory subunit.|||Loss of trimeric subunit ABC assembly.|||Phosphotyrosine|||Proton donor|||Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform ^@ http://purl.uniprot.org/annotation/PRO_0000058840 http://togogenome.org/gene/10090:Akr1c21 ^@ http://purl.uniprot.org/uniprot/Q91WR5 ^@ 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|||Site|||Strand|||Turn ^@ Aldo-keto reductase family 1 member C21|||Decreases affinity for NADP. Changes enzyme activity, leading to the production of testosterone and concomitantly reducing the production of epi-testosterone.|||Lowers pKa of active site Tyr|||No effect on affinity for androstenedione. Slight increase of catalytic activity.|||No effect on enzyme activity. Decreases affinity for NADP.|||Proton donor|||Reduces enzyme activity and affinity for substrate. Alters the stereospecificity, so that androstenedione is converted to testosterone. ^@ http://purl.uniprot.org/annotation/PRO_0000326222 http://togogenome.org/gene/10090:Limch1 ^@ http://purl.uniprot.org/uniprot/Q3UH68 ^@ 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|||Calponin-homology (CH)|||Disordered|||In isoform 2.|||In isoform 3.|||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_0000293620|||http://purl.uniprot.org/annotation/VSP_026551|||http://purl.uniprot.org/annotation/VSP_026552|||http://purl.uniprot.org/annotation/VSP_026553|||http://purl.uniprot.org/annotation/VSP_026554 http://togogenome.org/gene/10090:Rcbtb2 ^@ http://purl.uniprot.org/uniprot/Q99LJ7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant ^@ BTB|||In isoform 2.|||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_0000206645|||http://purl.uniprot.org/annotation/VSP_016724 http://togogenome.org/gene/10090:Spic ^@ http://purl.uniprot.org/uniprot/Q6P3D7 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||DNA Binding|||Sequence Conflict|||Splice Variant ^@ ETS|||In isoform 2.|||Transcription factor Spi-C ^@ http://purl.uniprot.org/annotation/PRO_0000204141|||http://purl.uniprot.org/annotation/VSP_037734|||http://purl.uniprot.org/annotation/VSP_037735 http://togogenome.org/gene/10090:Or10ak14 ^@ http://purl.uniprot.org/uniprot/A0A1L1SSB4|||http://purl.uniprot.org/uniprot/A2ACY7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hps4 ^@ http://purl.uniprot.org/uniprot/Q541V2|||http://purl.uniprot.org/uniprot/Q99KG7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant ^@ BLOC-3 complex member HPS4|||CCZ1/INTU/HPS4 third Longin|||CCZ1/INTU/HSP4 first Longin|||Disordered|||In Le.|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000084053 http://togogenome.org/gene/10090:Vmn1r36 ^@ http://purl.uniprot.org/uniprot/Q8R2E3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Stmn1 ^@ http://purl.uniprot.org/uniprot/P54227|||http://purl.uniprot.org/uniprot/Q545B6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||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_0000182390 http://togogenome.org/gene/10090:Ttll6 ^@ http://purl.uniprot.org/uniprot/A4Q9E8 ^@ 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 ^@ Decreased alpha-tubulin alpha-elongation step of polyglutamylase activity.|||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.|||Increased alpha-tubulin initiation step of polyglutamylase activity. Increased alpha-tubulin initiation step of polyglutamylase activity; when associated with I-362. Strong increase in alpha-tubulin initiation step of polyglutamylase activity; when associated with A-179 and I-362. Strong increase in alpha-tubulin initiation step of polyglutamylase activity; when associated with A-179, I-182, I-362 and H-367.|||Loss of alpha-tubulin alpha-elongation polyglutamylase activity.|||Loss of alpha-tubulin alpha-elongation step of polyglutamylase activity.|||Polar residues|||Small increase in alpha-tubulin initiation step of polyglutamylase activity. Increased alpha-tubulin initiation step of polyglutamylase activity; when associated with R-180. Strong increase in alpha-tubulin initiation step of polyglutamylase activity; when associated with A-179 and R-180. Strong increase in alpha-tubulin initiation step of polyglutamylase activity; when associated with A-179, R-180, I-362 and H-367.|||Strong increase in alpha-tubulin initiation step of polyglutamylase activity; when associated with A-179, R-180, I-182 and I-262.|||Strong increase in alpha-tubulin initiation step of polyglutamylase activity; when associated with A-179, R-180, I-362 and H-367.|||Strong increase in alpha-tubulin initiation step of polyglutamylase activity; when associated with R-180 and I-362. Strong increase in alpha-tubulin initiation step of polyglutamylase activity; when associated with R-180, I-182, I-362 and H-367.|||TTL|||Tubulin polyglutamylase TTLL6|||c-MTBD region ^@ http://purl.uniprot.org/annotation/PRO_0000326161|||http://purl.uniprot.org/annotation/VSP_052729 http://togogenome.org/gene/10090:Abcd4 ^@ http://purl.uniprot.org/uniprot/O89016 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ ABC transmembrane type-1|||ABC transporter|||Helical|||Lysosomal cobalamin transporter ABCD4 ^@ http://purl.uniprot.org/annotation/PRO_0000093313 http://togogenome.org/gene/10090:Slc25a25 ^@ http://purl.uniprot.org/uniprot/A2ASZ8 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-terminal transmembrane transporter domain|||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 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||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_0000317603|||http://purl.uniprot.org/annotation/VSP_031071|||http://purl.uniprot.org/annotation/VSP_031072|||http://purl.uniprot.org/annotation/VSP_031073 http://togogenome.org/gene/10090:9930012K11Rik ^@ http://purl.uniprot.org/uniprot/Q66JV7 ^@ 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.|||Uncharacterized protein C8orf58 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000285641|||http://purl.uniprot.org/annotation/VSP_024877 http://togogenome.org/gene/10090:Syap1 ^@ http://purl.uniprot.org/uniprot/Q9D5V6 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ BSD|||Disordered|||Phosphoserine|||Phosphothreonine|||Synapse-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000072356 http://togogenome.org/gene/10090:Fancd2os ^@ http://purl.uniprot.org/uniprot/Q9D4K4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ FANCD2 opposite strand protein ^@ http://purl.uniprot.org/annotation/PRO_0000235344 http://togogenome.org/gene/10090:Or1j17 ^@ http://purl.uniprot.org/uniprot/Q8VGJ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gnptab ^@ http://purl.uniprot.org/uniprot/Q69ZN6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Cleavage; by MBTPS1|||DMAP1-binding|||Disordered|||EF-hand|||Helical|||In isoform 2.|||LNR 1|||LNR 2|||N-acetylglucosamine-1-phosphotransferase subunit alpha|||N-acetylglucosamine-1-phosphotransferase subunit beta|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000225010|||http://purl.uniprot.org/annotation/PRO_0000225011|||http://purl.uniprot.org/annotation/VSP_017340|||http://purl.uniprot.org/annotation/VSP_017341 http://togogenome.org/gene/10090:Dipk2a ^@ http://purl.uniprot.org/uniprot/Q3USZ8 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Sequence Conflict|||Signal Peptide ^@ Divergent protein kinase domain 2A ^@ http://purl.uniprot.org/annotation/PRO_0000226038 http://togogenome.org/gene/10090:Or8g52 ^@ http://purl.uniprot.org/uniprot/Q7TRA7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Irf2bpl ^@ http://purl.uniprot.org/uniprot/Q8K3X4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Pro residues|||Probable E3 ubiquitin-protein ligase IRF2BPL|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000056412 http://togogenome.org/gene/10090:Magea5 ^@ http://purl.uniprot.org/uniprot/O89009 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Fnip1 ^@ http://purl.uniprot.org/uniprot/Q68FD7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Abolished recognition by the CRL2(FEM1B) complex and subsequent ubiquitination.|||Abolished recognition by the CRL2(FEM1B) complex and subsequent ubiquitination. Reduced zinc-binding.|||Basic and acidic residues|||Cys degron|||Disordered|||Does not affect recognition by the CRL2(FEM1B) complex and subsequent ubiquitination.|||Folliculin-interacting protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with HSP90AA1|||KY-finger|||O-linked (GlcNAc) serine; alternate|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by AMPK|||Phosphothreonine|||Reduced but not abolished recognition by the CRL2(FEM1B) complex.|||cDENN FNIP1/2-type|||dDENN FNIP1/2-type|||uDENN FNIP1/2-type ^@ http://purl.uniprot.org/annotation/PRO_0000308485 http://togogenome.org/gene/10090:Sp3 ^@ http://purl.uniprot.org/uniprot/O70494 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 9aaTAD|||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|||In isoform 2.|||In isoform 3.|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||Repressor domain|||Transactivation domain (Gln-rich)|||Transcription factor Sp3 ^@ http://purl.uniprot.org/annotation/PRO_0000047142|||http://purl.uniprot.org/annotation/VSP_016782|||http://purl.uniprot.org/annotation/VSP_016783|||http://purl.uniprot.org/annotation/VSP_016784 http://togogenome.org/gene/10090:Poldip3 ^@ http://purl.uniprot.org/uniprot/Q3UDD3|||http://purl.uniprot.org/uniprot/Q8BG81 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polymerase delta-interacting protein 3|||RRM|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000081723 http://togogenome.org/gene/10090:Vmn2r104 ^@ http://purl.uniprot.org/uniprot/E9Q2J5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003244382 http://togogenome.org/gene/10090:Arpin ^@ http://purl.uniprot.org/uniprot/Q9D0A3 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Arpin|||Disordered|||Necessary and sufficient fopr interaction with ARPC2 ^@ http://purl.uniprot.org/annotation/PRO_0000244266 http://togogenome.org/gene/10090:Hoxb5 ^@ http://purl.uniprot.org/uniprot/P09079 ^@ 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-B5|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000200129 http://togogenome.org/gene/10090:Tob2 ^@ http://purl.uniprot.org/uniprot/Q543X9|||http://purl.uniprot.org/uniprot/Q9JM55 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Region ^@ Anti-proliferative protein|||Disordered|||Phosphoserine|||Protein Tob2 ^@ http://purl.uniprot.org/annotation/PRO_0000143816 http://togogenome.org/gene/10090:Cbx1 ^@ http://purl.uniprot.org/uniprot/P83917 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn ^@ Abolishes homodimer formation.|||Abolishes interaction with SUV39H1.|||Basic and acidic residues|||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_0000080200 http://togogenome.org/gene/10090:Mcat ^@ http://purl.uniprot.org/uniprot/Q8R3F5 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Active Site|||Chain|||Modified Residue|||Transit Peptide ^@ Malonyl-CoA-acyl carrier protein transacylase, mitochondrial|||Mitochondrion|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000042239 http://togogenome.org/gene/10090:Fbxo24 ^@ http://purl.uniprot.org/uniprot/Q9D417 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Region|||Repeat ^@ Disordered|||F-box|||F-box only protein 24|||RCC1 ^@ http://purl.uniprot.org/annotation/PRO_0000119910 http://togogenome.org/gene/10090:Myl2 ^@ http://purl.uniprot.org/uniprot/P51667 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||Loss of cardiac myofibril assembly; when associated with A-14 and A-15. Loss of phosphorylation; when associated with A-14 and A-15. Loss of calcium sensitivity of force development; when associated with A-14 and A-15.|||Loss of cardiac myofibril assembly; when associated with A-14 and A-19. Loss of phosphorylation; when associated with A-14 and A-19. Loss of calcium sensitivity of force development; when associated with A-14 and A-19. Increase of phosphorylation. Phosphorylation at Ser-14 and at Ser-19. Phosphorylation at Ser-19; when associated with A-14. Significant decrease in phosphorylation by MLCK; when associated with A-14. Adult lethality associated with early defects in cardiac twitch relaxation and torsion leading to dilated cardiomyopathy, heart failure and premature death; when associated with A-14. Significant acceleration of twitch relaxation in absence of changes in calcium transients; when associated with A-14. Absence of transmural phosphorylation gradient leading to alteration of torsion; when associated with A-14.|||Loss of cardiac myofibril assembly; when associated with A-15 and A-19. Loss of phosphorylation; when associated with A-15 and A-19. Loss of calcium sensitivity of force development; when associated with A-15 and A-19. Phosphorylation at Ser-19; when associated with A-15. Significant decrease in phosphorylation by MLCK; when associated with A-15. Adult lethality associated with early defects in cardiac twitch relaxation and torsion leading to dilated cardiomyopathy, heart failure and premature death; when associated with A-15.Significant acceleration of twitch relaxation in absence of changes in calcium transients; when associated with A-15. Absence of transmural phosphorylation gradient leading to alteration of torsion; when associated with A-14.|||Myosin regulatory light chain 2, ventricular/cardiac muscle isoform|||N,N,N-trimethylalanine|||Phosphoserine|||Phosphoserine; by MLCK|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000198728 http://togogenome.org/gene/10090:C1ra ^@ http://purl.uniprot.org/uniprot/Q8CG16|||http://purl.uniprot.org/uniprot/Q9CTX0 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide ^@ (3R)-3-hydroxyasparagine|||CUB 1|||CUB 2|||Charge relay system|||Complement C1r-A subcomponent|||Complement C1r-A subcomponent heavy chain|||Complement C1r-A subcomponent light chain|||EGF-like; calcium-binding|||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_0000027580|||http://purl.uniprot.org/annotation/PRO_0000027581|||http://purl.uniprot.org/annotation/PRO_0000027582 http://togogenome.org/gene/10090:Gxylt1 ^@ http://purl.uniprot.org/uniprot/Q3UHH8 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||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_0000288535|||http://purl.uniprot.org/annotation/VSP_025710 http://togogenome.org/gene/10090:Tmem208 ^@ http://purl.uniprot.org/uniprot/Q9CR96|||http://purl.uniprot.org/uniprot/S4R1H6 ^@ 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.|||N-acetylmethionine|||Transmembrane protein 208 ^@ http://purl.uniprot.org/annotation/PRO_0000325968|||http://purl.uniprot.org/annotation/VSP_032506 http://togogenome.org/gene/10090:Rnf166 ^@ http://purl.uniprot.org/uniprot/A2RS02|||http://purl.uniprot.org/uniprot/Q3U9F6 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Zinc Finger ^@ C2HC RNF-type|||E3 ubiquitin-protein ligase RNF166|||RING-type|||UIM ^@ http://purl.uniprot.org/annotation/PRO_0000245589 http://togogenome.org/gene/10090:Nde1 ^@ http://purl.uniprot.org/uniprot/Q9CZA6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with CENPF|||Interaction with PAFAH1B1|||Nuclear distribution protein nudE homolog 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7|||Self-association ^@ http://purl.uniprot.org/annotation/PRO_0000240203|||http://purl.uniprot.org/annotation/VSP_019306|||http://purl.uniprot.org/annotation/VSP_019307|||http://purl.uniprot.org/annotation/VSP_019308|||http://purl.uniprot.org/annotation/VSP_019309 http://togogenome.org/gene/10090:Hsh2d ^@ http://purl.uniprot.org/uniprot/Q6VYH9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||Hematopoietic SH2 domain-containing protein|||Polar residues|||SH2 ^@ http://purl.uniprot.org/annotation/PRO_0000233130 http://togogenome.org/gene/10090:Chmp6 ^@ http://purl.uniprot.org/uniprot/B1AZ39|||http://purl.uniprot.org/uniprot/P0C0A3 ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region ^@ Charged multivesicular body protein 6|||Disordered|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Removed|||Type-2 MIT-interacting motif ^@ http://purl.uniprot.org/annotation/PRO_0000211509 http://togogenome.org/gene/10090:Uri1 ^@ http://purl.uniprot.org/uniprot/Q3TLD5 ^@ 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|||Phosphoserine; by RPS6KB1|||Polar residues|||Unconventional prefoldin RPB5 interactor ^@ http://purl.uniprot.org/annotation/PRO_0000328753|||http://purl.uniprot.org/annotation/VSP_032774 http://togogenome.org/gene/10090:Ndufa7 ^@ http://purl.uniprot.org/uniprot/Q9Z1P6 ^@ 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|||N6-acetyllysine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118835 http://togogenome.org/gene/10090:Bnip3 ^@ http://purl.uniprot.org/uniprot/O55003 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Transmembrane ^@ BCL2/adenovirus E1B 19 kDa protein-interacting protein 3|||BH3|||Disordered|||Helical|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064965 http://togogenome.org/gene/10090:Sirt2 ^@ http://purl.uniprot.org/uniprot/Q8VDQ8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||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|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes deacetylation of FOXO3. Does not inhibit interaction with FOXO3.|||Deacetylase sirtuin-type|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||NAD-dependent protein deacetylase sirtuin-2|||Nuclear export signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000110259|||http://purl.uniprot.org/annotation/VSP_008729|||http://purl.uniprot.org/annotation/VSP_055329|||http://purl.uniprot.org/annotation/VSP_055330 http://togogenome.org/gene/10090:Anxa11 ^@ http://purl.uniprot.org/uniprot/P97384 ^@ 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 ^@ Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A11|||Disordered|||N6-acetyllysine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000067511 http://togogenome.org/gene/10090:Pcdhb16 ^@ http://purl.uniprot.org/uniprot/Q8CB45|||http://purl.uniprot.org/uniprot/Q91Y03 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Cadherin domain-containing protein|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5004307381|||http://purl.uniprot.org/annotation/PRO_5015099531 http://togogenome.org/gene/10090:1700024G13Rik ^@ http://purl.uniprot.org/uniprot/Q3KNL4 ^@ Chain|||Molecule Processing ^@ Chain ^@ UPF0728 protein C10orf53 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000351543 http://togogenome.org/gene/10090:Kcnab2 ^@ http://purl.uniprot.org/uniprot/A0A571BF54|||http://purl.uniprot.org/uniprot/P62482|||http://purl.uniprot.org/uniprot/Q3UPV6 ^@ 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|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine; alternate|||Disordered|||N6-acetyllysine|||NADP-dependent oxidoreductase|||No detectable phenotype.|||Omega-N-methylarginine; alternate|||Phosphoserine|||Proton donor/acceptor|||Voltage-gated potassium channel subunit beta-2 ^@ http://purl.uniprot.org/annotation/PRO_0000148747 http://togogenome.org/gene/10090:Fgfr2 ^@ http://purl.uniprot.org/uniprot/E9Q5C2|||http://purl.uniprot.org/uniprot/E9Q7C7|||http://purl.uniprot.org/uniprot/E9QK53|||http://purl.uniprot.org/uniprot/P21803 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Abolishes phosphorylation of FRS2 and activation of MAP kinases.|||Cytoplasmic|||Disordered|||Extracellular|||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 isoform Short.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000016784|||http://purl.uniprot.org/annotation/VSP_002985|||http://purl.uniprot.org/annotation/VSP_002986|||http://purl.uniprot.org/annotation/VSP_002987 http://togogenome.org/gene/10090:Slamf1 ^@ http://purl.uniprot.org/uniprot/Q544K1|||http://purl.uniprot.org/uniprot/Q9QUM4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes SLAMF1:SH2D1A-mediated intracellular tyrosine phosphorylation, no effect on interaction with SH2D1A; when associated with A-315.|||Abolishes SLAMF1:SH2D1A-mediated intracellular tyrosine phosphorylation, no effect on interaction with SH2D1A; when associated with A-335.|||Cytoplasmic|||Disordered|||Extracellular|||Greatly reduces SLAMF1:SH2D1A-mediated intracellular tyrosine phosphorylation.|||Helical|||ITSM 1|||ITSM 2|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by FYN|||Polar residues|||SH2-binding|||Signaling lymphocytic activation molecule ^@ http://purl.uniprot.org/annotation/PRO_0000014960|||http://purl.uniprot.org/annotation/PRO_5014309580|||http://purl.uniprot.org/annotation/VSP_002570 http://togogenome.org/gene/10090:Rnf135 ^@ http://purl.uniprot.org/uniprot/B2RRA5|||http://purl.uniprot.org/uniprot/Q9CWS1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Splice Variant|||Zinc Finger ^@ B30.2/SPRY|||Disordered|||E3 ubiquitin-protein ligase RNF135|||In isoform 2.|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000280558|||http://purl.uniprot.org/annotation/VSP_023787 http://togogenome.org/gene/10090:Pcnp ^@ http://purl.uniprot.org/uniprot/Q3KQH9|||http://purl.uniprot.org/uniprot/Q3UCC5|||http://purl.uniprot.org/uniprot/Q6P8I4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||N-acetylalanine|||N6-acetyllysine|||PEST proteolytic signal-containing nuclear protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000058254 http://togogenome.org/gene/10090:Ppm1h ^@ http://purl.uniprot.org/uniprot/Q3UYC0 ^@ 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.|||Omega-N-methylarginine|||PPM-type phosphatase|||Phosphoserine|||Phosphothreonine|||Protein phosphatase 1H ^@ http://purl.uniprot.org/annotation/PRO_0000286604|||http://purl.uniprot.org/annotation/VSP_025121|||http://purl.uniprot.org/annotation/VSP_025122 http://togogenome.org/gene/10090:Olfr209 ^@ http://purl.uniprot.org/uniprot/L7N1X3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rnasek ^@ http://purl.uniprot.org/uniprot/Q8K3C0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Ribonuclease kappa ^@ http://purl.uniprot.org/annotation/PRO_0000344222 http://togogenome.org/gene/10090:Or11j4 ^@ http://purl.uniprot.org/uniprot/Q8VFT6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rnf19b ^@ http://purl.uniprot.org/uniprot/E9Q2L7 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||Helical|||Pro residues|||RING-type ^@ http://togogenome.org/gene/10090:Or5w11 ^@ http://purl.uniprot.org/uniprot/Q7TR45 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dmd ^@ http://purl.uniprot.org/uniprot/A0A023ZT56|||http://purl.uniprot.org/uniprot/A0A023ZTV5|||http://purl.uniprot.org/uniprot/A2A9Z1|||http://purl.uniprot.org/uniprot/A2A9Z2|||http://purl.uniprot.org/uniprot/P11531|||http://purl.uniprot.org/uniprot/Q3TWL4|||http://purl.uniprot.org/uniprot/Q8BHM1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ ANK2- and ANK-3 binding|||Actin-binding|||Binds to SNTB1|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Dystrophin|||Interaction with SYNM|||Phosphoserine|||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_0000076076 http://togogenome.org/gene/10090:Cnih4 ^@ http://purl.uniprot.org/uniprot/Q9CX13 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Protein cornichon homolog 4 ^@ http://purl.uniprot.org/annotation/PRO_0000122231 http://togogenome.org/gene/10090:St7 ^@ http://purl.uniprot.org/uniprot/Q99M95|||http://purl.uniprot.org/uniprot/Q99M96 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||In isoform 3, isoform 4, isoform 7 and isoform 9.|||In isoform 4 and isoform 5.|||In isoform 6 and isoform 7.|||In isoform 8 and isoform 9.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Suppressor of tumorigenicity 7 protein ^@ http://purl.uniprot.org/annotation/PRO_0000339207|||http://purl.uniprot.org/annotation/VSP_034118|||http://purl.uniprot.org/annotation/VSP_034119|||http://purl.uniprot.org/annotation/VSP_034120|||http://purl.uniprot.org/annotation/VSP_034121|||http://purl.uniprot.org/annotation/VSP_034122|||http://purl.uniprot.org/annotation/VSP_034123|||http://purl.uniprot.org/annotation/VSP_034124 http://togogenome.org/gene/10090:Anxa6 ^@ http://purl.uniprot.org/uniprot/F8WIT2|||http://purl.uniprot.org/uniprot/P14824|||http://purl.uniprot.org/uniprot/Q3TUI1 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin 5|||Annexin 6|||Annexin 7|||Annexin 8|||Annexin A6|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067495 http://togogenome.org/gene/10090:Prkcz ^@ http://purl.uniprot.org/uniprot/Q02956|||http://purl.uniprot.org/uniprot/Q3V341 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ AGC-kinase C-terminal|||Disordered|||In isoform 2.|||Interaction with SQSTM1|||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_0000055702|||http://purl.uniprot.org/annotation/VSP_059934 http://togogenome.org/gene/10090:Mcemp1 ^@ http://purl.uniprot.org/uniprot/Q9D8U6 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Mast cell-expressed membrane protein 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000358923 http://togogenome.org/gene/10090:Rgs16 ^@ http://purl.uniprot.org/uniprot/P97428|||http://purl.uniprot.org/uniprot/Q542U0 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Turn ^@ Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Turn ^@ Disordered|||Phosphotyrosine|||Phosphotyrosine; by EGFR|||RGS|||Regulator of G-protein signaling 16|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000204222 http://togogenome.org/gene/10090:Or8b54 ^@ http://purl.uniprot.org/uniprot/Q7TRC0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ctdsp2 ^@ http://purl.uniprot.org/uniprot/Q8BX07|||http://purl.uniprot.org/uniprot/Q8R3B3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Site ^@ 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_0000212575 http://togogenome.org/gene/10090:Xlr3c ^@ http://purl.uniprot.org/uniprot/B1B0S0 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Fam13c ^@ http://purl.uniprot.org/uniprot/G3X9S1|||http://purl.uniprot.org/uniprot/Q5DTU9|||http://purl.uniprot.org/uniprot/Q6NXX8|||http://purl.uniprot.org/uniprot/Q8BLV7|||http://purl.uniprot.org/uniprot/Q9DBR2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Protein FAM13C ^@ http://purl.uniprot.org/annotation/PRO_0000058923 http://togogenome.org/gene/10090:H2al3 ^@ http://purl.uniprot.org/uniprot/Q9D4U4 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Mmp16 ^@ http://purl.uniprot.org/uniprot/Q9WTR0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cysteine switch|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Matrix metalloproteinase-16|||N-linked (GlcNAc...) asparagine|||Pro residues|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028814|||http://purl.uniprot.org/annotation/PRO_0000028815 http://togogenome.org/gene/10090:Nfam1 ^@ http://purl.uniprot.org/uniprot/Q3TCT5|||http://purl.uniprot.org/uniprot/Q8R4V1 ^@ 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|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||ITAM|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||NFAT activation molecule 1|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000015047|||http://purl.uniprot.org/annotation/PRO_5004229529|||http://purl.uniprot.org/annotation/VSP_008043|||http://purl.uniprot.org/annotation/VSP_008044 http://togogenome.org/gene/10090:Vmn2r20 ^@ http://purl.uniprot.org/uniprot/L7N2B1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982277 http://togogenome.org/gene/10090:1810024B03Rik ^@ http://purl.uniprot.org/uniprot/Q8BWE1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Slc7a9 ^@ http://purl.uniprot.org/uniprot/Q3UQE3|||http://purl.uniprot.org/uniprot/Q9QXA6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interchain (with C-113 in SLC3A1)|||Phosphoserine|||b(0,+)-type amino acid transporter 1 ^@ http://purl.uniprot.org/annotation/PRO_0000054259 http://togogenome.org/gene/10090:Dydc1 ^@ http://purl.uniprot.org/uniprot/Q9D9T0 ^@ 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|||DPY30 domain-containing protein 1|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000247557|||http://purl.uniprot.org/annotation/VSP_020012 http://togogenome.org/gene/10090:Pcyox1 ^@ http://purl.uniprot.org/uniprot/Q3UYP2|||http://purl.uniprot.org/uniprot/Q9CQF9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prenylcysteine lyase|||Prenylcysteine lyase domain-containing protein|||Prenylcysteine oxidase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000023300|||http://purl.uniprot.org/annotation/PRO_5004230445 http://togogenome.org/gene/10090:Mt2 ^@ http://purl.uniprot.org/uniprot/P02798 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Alpha|||Beta|||Metallothionein-2|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000197207 http://togogenome.org/gene/10090:Ccdc154 ^@ http://purl.uniprot.org/uniprot/Q6RUT8 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Splice Variant ^@ Coiled-coil domain-containing protein 154|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000332271|||http://purl.uniprot.org/annotation/VSP_060241 http://togogenome.org/gene/10090:Or12k7 ^@ http://purl.uniprot.org/uniprot/Q8VFP3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vwa7 ^@ http://purl.uniprot.org/uniprot/B2RQ76|||http://purl.uniprot.org/uniprot/B9EJA5|||http://purl.uniprot.org/uniprot/Q9JHA8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Polar residues|||VWFA|||von Willebrand factor A domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000231632|||http://purl.uniprot.org/annotation/PRO_5014298300|||http://purl.uniprot.org/annotation/PRO_5015087496 http://togogenome.org/gene/10090:Npat ^@ http://purl.uniprot.org/uniprot/Q8BMA5 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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_0000318164 http://togogenome.org/gene/10090:Catsperg2 ^@ http://purl.uniprot.org/uniprot/C6KI89 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cation channel sperm-associated auxiliary subunit gamma 2|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000388712 http://togogenome.org/gene/10090:Zfp853 ^@ http://purl.uniprot.org/uniprot/A0A1D5RM95 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Asb11 ^@ http://purl.uniprot.org/uniprot/Q9CQ31 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Repeat|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankyrin repeat and SOCS box protein 11|||In isoform 2.|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066945|||http://purl.uniprot.org/annotation/VSP_013946 http://togogenome.org/gene/10090:Taar9 ^@ http://purl.uniprot.org/uniprot/Q5QD04 ^@ 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|||Trace amine-associated receptor 9 ^@ http://purl.uniprot.org/annotation/PRO_0000070182 http://togogenome.org/gene/10090:A530032D15Rik ^@ http://purl.uniprot.org/uniprot/E9PV05|||http://purl.uniprot.org/uniprot/Q8BS13 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||HSR ^@ http://togogenome.org/gene/10090:Cntrl ^@ http://purl.uniprot.org/uniprot/R4GML3 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Abhd16a ^@ http://purl.uniprot.org/uniprot/Q9Z1Q2 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Topological Domain|||Transmembrane ^@ AB hydrolase-1|||Charge relay system|||Cytoplasmic|||Helical|||Phosphatidylserine lipase ABHD16A ^@ http://purl.uniprot.org/annotation/PRO_0000064834 http://togogenome.org/gene/10090:Hk1 ^@ http://purl.uniprot.org/uniprot/B4YB29|||http://purl.uniprot.org/uniprot/G3UVV4|||http://purl.uniprot.org/uniprot/P17710|||http://purl.uniprot.org/uniprot/Q3TTB4|||http://purl.uniprot.org/uniprot/Q6GQU1 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Disrupts targeting to membrane; when associated with A-67; N-68; P-73; A-74 and Q-75.|||Disrupts targeting to membrane; when associated with A-67; N-68; Q-70; A-74 and Q-75.|||Disrupts targeting to membrane; when associated with A-67; N-68; Q-70; P-73 and A-74.|||Disrupts targeting to membrane; when associated with A-67; N-68; Q-70; P-73 and Q-75.|||Disrupts targeting to membrane; when associated with A-67; Q-70; P-73; A-74 and Q-75.|||Disrupts targeting to membrane; when associated with N-68; Q-70; P-73; A-74 and Q-75.|||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 isoform HK1-SB and isoform HK1-SC.|||In isoform HK1-SB.|||In isoform HK1.|||Mitochondrial-binding peptide (MBP)|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000013399|||http://purl.uniprot.org/annotation/VSP_007327|||http://purl.uniprot.org/annotation/VSP_007328|||http://purl.uniprot.org/annotation/VSP_018747 http://togogenome.org/gene/10090:Klrg2 ^@ http://purl.uniprot.org/uniprot/G5E8L6 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||C-type lectin|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Tank ^@ http://purl.uniprot.org/uniprot/P70347|||http://purl.uniprot.org/uniprot/Q3TNB4|||http://purl.uniprot.org/uniprot/Q3UGW0|||http://purl.uniprot.org/uniprot/Q8C2D3 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with TBK1 and IKBKE|||Necessary for interaction with TRAF6|||Necessary for interaction with ZC3H12A|||Phosphoserine|||Phosphothreonine|||TRAF family member interaction|||TRAF family member-associated NF-kappa-B activator|||UBZ1-type ^@ http://purl.uniprot.org/annotation/PRO_0000072428|||http://purl.uniprot.org/annotation/VSP_004444|||http://purl.uniprot.org/annotation/VSP_004445|||http://purl.uniprot.org/annotation/VSP_004446|||http://purl.uniprot.org/annotation/VSP_004447|||http://purl.uniprot.org/annotation/VSP_004448 http://togogenome.org/gene/10090:Qsox1 ^@ http://purl.uniprot.org/uniprot/Q8BND5 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Causes local perturbations of protein folding; when associated with T-122.|||Disordered|||ERV/ALR sulfhydryl oxidase|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Redox-active|||Sulfhydryl oxidase 1|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000249534|||http://purl.uniprot.org/annotation/VSP_020491|||http://purl.uniprot.org/annotation/VSP_020492|||http://purl.uniprot.org/annotation/VSP_020493|||http://purl.uniprot.org/annotation/VSP_020494|||http://purl.uniprot.org/annotation/VSP_020495|||http://purl.uniprot.org/annotation/VSP_020496 http://togogenome.org/gene/10090:Arsa ^@ http://purl.uniprot.org/uniprot/P50428 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ 3-oxoalanine (Cys)|||Arylsulfatase A|||N-linked (GlcNAc...) asparagine|||Nucleophile|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000033420 http://togogenome.org/gene/10090:Cdk20 ^@ http://purl.uniprot.org/uniprot/Q9JHU3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Cyclin-dependent kinase 20|||Disordered|||In isoform 2.|||Pro residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085703|||http://purl.uniprot.org/annotation/VSP_016753|||http://purl.uniprot.org/annotation/VSP_016754 http://togogenome.org/gene/10090:Slc5a2 ^@ http://purl.uniprot.org/uniprot/Q923I7 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Sodium/glucose cotransporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000105373 http://togogenome.org/gene/10090:Lysmd1 ^@ http://purl.uniprot.org/uniprot/A6H624|||http://purl.uniprot.org/uniprot/Q9D0E3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||LysM|||LysM and putative peptidoglycan-binding domain-containing protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247998 http://togogenome.org/gene/10090:Fkbp6 ^@ http://purl.uniprot.org/uniprot/Q91XW8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant ^@ Abolishes interaction with HSP90.|||In isoform 2 and isoform 3.|||In isoform 2.|||Inactive peptidyl-prolyl cis-trans isomerase FKBP6|||PPIase FKBP-type|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000075330|||http://purl.uniprot.org/annotation/VSP_005185|||http://purl.uniprot.org/annotation/VSP_005186 http://togogenome.org/gene/10090:Trappc2 ^@ http://purl.uniprot.org/uniprot/Q9CQP2 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand ^@ Aberrant protein folding and increased proteasomal degradation.|||Increased interaction with TRAPPC3.|||Trafficking protein particle complex subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000211567 http://togogenome.org/gene/10090:Samd10 ^@ http://purl.uniprot.org/uniprot/Q3TBN2|||http://purl.uniprot.org/uniprot/Q7TST3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||SAM|||Sterile alpha motif domain-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000097569 http://togogenome.org/gene/10090:Rbm12 ^@ http://purl.uniprot.org/uniprot/Q8R4X3 ^@ 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 ^@ Disordered|||Phosphoserine|||Pro residues|||RNA-binding protein 12|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000081772 http://togogenome.org/gene/10090:Rpl41 ^@ http://purl.uniprot.org/uniprot/P62947 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Large ribosomal subunit protein eL41 ^@ http://purl.uniprot.org/annotation/PRO_0000198056 http://togogenome.org/gene/10090:Fpr1 ^@ http://purl.uniprot.org/uniprot/P33766 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||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|||fMet-Leu-Phe receptor ^@ http://purl.uniprot.org/annotation/PRO_0000069446 http://togogenome.org/gene/10090:Artn ^@ http://purl.uniprot.org/uniprot/Q9Z0L2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Artemin|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) asparagine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000240288|||http://purl.uniprot.org/annotation/PRO_0000240289|||http://purl.uniprot.org/annotation/VSP_019337|||http://purl.uniprot.org/annotation/VSP_019338|||http://purl.uniprot.org/annotation/VSP_019339|||http://purl.uniprot.org/annotation/VSP_019340 http://togogenome.org/gene/10090:Fyb2 ^@ http://purl.uniprot.org/uniprot/E9PZ08 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||SH3 ^@ http://togogenome.org/gene/10090:Or10ag54 ^@ http://purl.uniprot.org/uniprot/E9PXB8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Prob1 ^@ http://purl.uniprot.org/uniprot/A0A087WR45|||http://purl.uniprot.org/uniprot/Q3UKG2 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||DUF4585|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Smim5 ^@ http://purl.uniprot.org/uniprot/Q8BT42 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Small integral membrane protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000410868 http://togogenome.org/gene/10090:Ciapin1 ^@ http://purl.uniprot.org/uniprot/Q8WTY4 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Region ^@ Anamorsin|||Cx2C motif 1|||Cx2C motif 2|||Fe-S binding site A|||Fe-S binding site B|||Linker|||N-terminal SAM-like domain|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000079289 http://togogenome.org/gene/10090:Tpo ^@ http://purl.uniprot.org/uniprot/P35419 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EGF-like; calcium-binding|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Sushi|||Thyroid peroxidase|||Transition state stabilizer|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000023663 http://togogenome.org/gene/10090:Whrn ^@ http://purl.uniprot.org/uniprot/Q80VW5 ^@ 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 ^@ Disordered|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 7 and isoform 8.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 8.|||In isoform 9.|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Polar residues|||Pro residues|||Whirlin ^@ http://purl.uniprot.org/annotation/PRO_0000065969|||http://purl.uniprot.org/annotation/VSP_029934|||http://purl.uniprot.org/annotation/VSP_029935|||http://purl.uniprot.org/annotation/VSP_029936|||http://purl.uniprot.org/annotation/VSP_029937|||http://purl.uniprot.org/annotation/VSP_029938|||http://purl.uniprot.org/annotation/VSP_029939|||http://purl.uniprot.org/annotation/VSP_029940|||http://purl.uniprot.org/annotation/VSP_029941|||http://purl.uniprot.org/annotation/VSP_029942|||http://purl.uniprot.org/annotation/VSP_029943|||http://purl.uniprot.org/annotation/VSP_045293|||http://purl.uniprot.org/annotation/VSP_045294|||http://purl.uniprot.org/annotation/VSP_045295 http://togogenome.org/gene/10090:Cuedc1 ^@ http://purl.uniprot.org/uniprot/A2RS63|||http://purl.uniprot.org/uniprot/Q8R3V6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ CUE|||CUE domain-containing protein 1|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079560 http://togogenome.org/gene/10090:Or8g34 ^@ http://purl.uniprot.org/uniprot/Q9EQB6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bltp1 ^@ http://purl.uniprot.org/uniprot/A2AAE1|||http://purl.uniprot.org/uniprot/Q8CDG7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Bridge-like lipid transfer protein family member 1|||Bridge-like lipid transfer protein family member 1 N-terminal|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317556|||http://purl.uniprot.org/annotation/VSP_031032|||http://purl.uniprot.org/annotation/VSP_031033|||http://purl.uniprot.org/annotation/VSP_031034|||http://purl.uniprot.org/annotation/VSP_031035|||http://purl.uniprot.org/annotation/VSP_031036|||http://purl.uniprot.org/annotation/VSP_031037|||http://purl.uniprot.org/annotation/VSP_031038 http://togogenome.org/gene/10090:Ak1 ^@ http://purl.uniprot.org/uniprot/Q9R0Y5 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Region|||Splice Variant ^@ Adenylate kinase isoenzyme 1|||In isoform 2.|||LID|||N-acetylmethionine|||NMP|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000158911|||http://purl.uniprot.org/annotation/VSP_024843 http://togogenome.org/gene/10090:Pik3cg ^@ http://purl.uniprot.org/uniprot/Q3UVA4|||http://purl.uniprot.org/uniprot/Q8C5Q7|||http://purl.uniprot.org/uniprot/Q9JHG7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Activation loop|||C2 PI3K-type|||Catalytic loop|||G-loop|||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_0000088793 http://togogenome.org/gene/10090:Pcp4 ^@ http://purl.uniprot.org/uniprot/P63054 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Acidic; binds calcium and is required for modulating the calcium-binding kinetics of calmodulin|||Basic and acidic residues|||Calmodulin regulator protein PCP4|||Disordered|||IQ|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000058307 http://togogenome.org/gene/10090:Hmg20a ^@ http://purl.uniprot.org/uniprot/Q9DC33 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||HMG box|||High mobility group protein 20A|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000238650|||http://purl.uniprot.org/annotation/VSP_018623|||http://purl.uniprot.org/annotation/VSP_018624|||http://purl.uniprot.org/annotation/VSP_018625|||http://purl.uniprot.org/annotation/VSP_018626|||http://purl.uniprot.org/annotation/VSP_018627 http://togogenome.org/gene/10090:Yy1 ^@ http://purl.uniprot.org/uniprot/Q00899 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Acidic residues|||Basic residues|||Binding to DNA|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Cleavage; by caspase-7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with the SMAD1/SMAD4 complex|||Involved in masking transactivation domain|||Involved in nuclear matrix association|||Involved in repression of activated transcription|||Phosphoserine|||Phosphothreonine|||Transcriptional repressor protein YY1 ^@ http://purl.uniprot.org/annotation/PRO_0000047191 http://togogenome.org/gene/10090:Or4c11b ^@ http://purl.uniprot.org/uniprot/Q8VGF5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:E2f1 ^@ http://purl.uniprot.org/uniprot/Q547J6|||http://purl.uniprot.org/uniprot/Q61501|||http://purl.uniprot.org/uniprot/Q9CYB4 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Signal Peptide ^@ Cyclin A:CDK2 binding|||DEF box|||Dimerization|||Disordered|||E2F/DP family winged-helix DNA-binding|||Interaction with BIRC2/c-IAP1|||Leucine-zipper|||N6-acetyllysine|||N6-methyllysine; by SETD7|||Phosphoserine|||Phosphothreonine|||Polar residues|||RB1 binding|||Required for interaction with TRIM28|||Transactivation|||Transcription factor E2F1 ^@ http://purl.uniprot.org/annotation/PRO_0000219462|||http://purl.uniprot.org/annotation/PRO_5015099706 http://togogenome.org/gene/10090:Baiap2 ^@ http://purl.uniprot.org/uniprot/B1AZ46|||http://purl.uniprot.org/uniprot/Q3UKP6|||http://purl.uniprot.org/uniprot/Q8BKX1 ^@ 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 ^@ Brain-specific angiogenesis inhibitor 1-associated protein 2|||Disordered|||IMD|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000064817|||http://purl.uniprot.org/annotation/VSP_015507|||http://purl.uniprot.org/annotation/VSP_015508|||http://purl.uniprot.org/annotation/VSP_015509 http://togogenome.org/gene/10090:Zfp81 ^@ http://purl.uniprot.org/uniprot/B8JJZ7|||http://purl.uniprot.org/uniprot/Q3UX68 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Zfp64 ^@ http://purl.uniprot.org/uniprot/A2AQR4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type ^@ http://togogenome.org/gene/10090:Hoxc6 ^@ http://purl.uniprot.org/uniprot/B2RUB8|||http://purl.uniprot.org/uniprot/P10629|||http://purl.uniprot.org/uniprot/Q543H4 ^@ 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 ^@ Antp-type hexapeptide|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Hox-C6|||In isoform PRI. ^@ http://purl.uniprot.org/annotation/PRO_0000200175|||http://purl.uniprot.org/annotation/VSP_002393 http://togogenome.org/gene/10090:Suv39h1 ^@ http://purl.uniprot.org/uniprot/A2AC19|||http://purl.uniprot.org/uniprot/O54864 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Chromo|||Histone-lysine N-methyltransferase SUV39H1|||In isoform 2.|||In isoform 3.|||Interaction with SIRT1|||Mediates interaction with MECOM|||N6-acetyllysine|||No effect on rates of development into blastocysts.|||Phosphoserine|||Post-SET|||Pre-SET|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000186058|||http://purl.uniprot.org/annotation/VSP_002208|||http://purl.uniprot.org/annotation/VSP_024029|||http://purl.uniprot.org/annotation/VSP_024030 http://togogenome.org/gene/10090:Bckdhb ^@ http://purl.uniprot.org/uniprot/Q6P3A8 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Splice Variant|||Transit Peptide ^@ 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000312367|||http://purl.uniprot.org/annotation/VSP_029841 http://togogenome.org/gene/10090:Tshz3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J017|||http://purl.uniprot.org/uniprot/Q8CGV9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||Disordered|||Homeobox|||Homeobox; atypical|||Phosphoserine|||Polar residues|||Teashirt homolog 3 ^@ http://purl.uniprot.org/annotation/PRO_0000047067 http://togogenome.org/gene/10090:Cdh20 ^@ http://purl.uniprot.org/uniprot/Q9Z0M3 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-20|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000320096|||http://purl.uniprot.org/annotation/PRO_0000320097 http://togogenome.org/gene/10090:Itln1 ^@ http://purl.uniprot.org/uniprot/D9J349|||http://purl.uniprot.org/uniprot/O88310 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Lipid Binding|||Mass|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Mass|||Propeptide|||Signal Peptide ^@ Fibrinogen C-terminal|||GPI-anchor amidated serine|||Intelectin-1a ^@ http://purl.uniprot.org/annotation/PRO_0000009145|||http://purl.uniprot.org/annotation/PRO_0000009146|||http://purl.uniprot.org/annotation/PRO_5009952922 http://togogenome.org/gene/10090:Ush2a ^@ http://purl.uniprot.org/uniprot/Q2QI47|||http://purl.uniprot.org/uniprot/Q9D1Z8 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||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 14|||Fibronectin type-III 15|||Fibronectin type-III 16|||Fibronectin type-III 17|||Fibronectin type-III 18|||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 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.|||LamG-like jellyroll fold|||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|||Polar residues|||Usherin ^@ http://purl.uniprot.org/annotation/PRO_0000229805|||http://purl.uniprot.org/annotation/VSP_017774|||http://purl.uniprot.org/annotation/VSP_017775|||http://purl.uniprot.org/annotation/VSP_017776 http://togogenome.org/gene/10090:Pdha2 ^@ http://purl.uniprot.org/uniprot/P35487 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||Phosphoserine|||Phosphoserine; by PDK1, PDK2, PDK3 and PDK4|||Phosphoserine; by PDK3|||Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000020448 http://togogenome.org/gene/10090:Ttpa ^@ http://purl.uniprot.org/uniprot/A8Y5N9|||http://purl.uniprot.org/uniprot/Q499J3|||http://purl.uniprot.org/uniprot/Q8BWP5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Strand|||Turn ^@ Abolishes binding to phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate.|||Alpha-tocopherol transfer protein|||CRAL-TRIO|||Loss of tocopherol secretion (in vivo). No effect on tocopherol binding and intermembrane transfer (in vitro). ^@ http://purl.uniprot.org/annotation/PRO_0000210765 http://togogenome.org/gene/10090:Cdhr5 ^@ http://purl.uniprot.org/uniprot/A0PJK7|||http://purl.uniprot.org/uniprot/Q8VHF2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||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|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ 1|||2|||3 X 31 AA approximate tandem repeats|||3; truncated|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin-related family member 5|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||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_0000004013|||http://purl.uniprot.org/annotation/PRO_5015085864|||http://purl.uniprot.org/annotation/VSP_050689 http://togogenome.org/gene/10090:Sec61a1 ^@ http://purl.uniprot.org/uniprot/P61620 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Fails to rescue pronephric kidney tubule atrophy in zebrafish morpholino knockdown.|||Helical|||Lumenal|||Protein transport protein Sec61 subunit alpha isoform 1|||Rescued partially pronephric kidney tubule atrophy in zebrafish morpholino knockdown. ^@ http://purl.uniprot.org/annotation/PRO_0000131792 http://togogenome.org/gene/10090:Prss42 ^@ http://purl.uniprot.org/uniprot/Q8VIF2 ^@ 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 42 ^@ http://purl.uniprot.org/annotation/PRO_0000349279 http://togogenome.org/gene/10090:Satb2 ^@ http://purl.uniprot.org/uniprot/Q546B3|||http://purl.uniprot.org/uniprot/Q8VI24 ^@ 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 ^@ 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|||ULD ^@ http://purl.uniprot.org/annotation/PRO_0000202401|||http://purl.uniprot.org/annotation/VSP_008967 http://togogenome.org/gene/10090:Rslcan18 ^@ http://purl.uniprot.org/uniprot/Q7M6X5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Fgb ^@ http://purl.uniprot.org/uniprot/Q3TGR2|||http://purl.uniprot.org/uniprot/Q8K0E8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Peptide|||Region|||Signal Peptide|||Site ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Peptide|||Region|||Signal Peptide|||Site ^@ Basic and acidic residues|||Beta-chain polymerization, binding distal domain of another fibrin|||Cleavage; by thrombin; to release fibrinopeptide B|||Disordered|||Fibrinogen C-terminal|||Fibrinogen C-terminal domain-containing protein|||Fibrinogen beta chain|||Fibrinopeptide B|||Interchain (with alpha chain)|||Interchain (with gamma chain)|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000009077|||http://purl.uniprot.org/annotation/PRO_0000009078|||http://purl.uniprot.org/annotation/PRO_5014309133 http://togogenome.org/gene/10090:Chct1 ^@ http://purl.uniprot.org/uniprot/Q9D979 ^@ 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|||CHD1 helical C-terminal domain (CHCT)|||CHD1 helical C-terminal domain containing protein 1|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000287175|||http://purl.uniprot.org/annotation/VSP_039026 http://togogenome.org/gene/10090:Crot ^@ http://purl.uniprot.org/uniprot/Q9DC50 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn ^@ Increases activity with octanoyl-CoA.|||Loss of activity with octanoyl-CoA and myristoyl-CoA.|||Microbody targeting signal|||N-acetylmethionine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Peroxisomal carnitine O-octanoyltransferase|||Proton acceptor|||Slightly decreases activity with octanoyl-CoA.|||Strongly decreases activity with octanoyl-CoA. ^@ http://purl.uniprot.org/annotation/PRO_0000210170 http://togogenome.org/gene/10090:Vps36 ^@ http://purl.uniprot.org/uniprot/Q3TSR1|||http://purl.uniprot.org/uniprot/Q91XD6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Strand|||Turn ^@ GLUE C-terminal|||GLUE N-terminal|||Vacuolar protein-sorting-associated protein 36 ^@ http://purl.uniprot.org/annotation/PRO_0000215223 http://togogenome.org/gene/10090:Cdk5r2 ^@ http://purl.uniprot.org/uniprot/O35926 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict ^@ Cyclin-dependent kinase 5 activator 2|||Disordered|||N-myristoyl glycine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000004802|||http://purl.uniprot.org/annotation/PRO_0000004803 http://togogenome.org/gene/10090:Tmed11 ^@ http://purl.uniprot.org/uniprot/A2RTW8|||http://purl.uniprot.org/uniprot/Q9D2R4|||http://purl.uniprot.org/uniprot/Q9D941 ^@ Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Motif|||Signal Peptide|||Topological Domain|||Transmembrane ^@ COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||GOLD|||GOLD domain-containing protein|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Transmembrane emp24 domain-containing protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000010379|||http://purl.uniprot.org/annotation/PRO_5004325094|||http://purl.uniprot.org/annotation/PRO_5014296825 http://togogenome.org/gene/10090:Gmpr ^@ http://purl.uniprot.org/uniprot/Q9DCZ1 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ GMP reductase 1|||Phosphoserine|||Proton donor/acceptor|||Thioimidate intermediate|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000093724 http://togogenome.org/gene/10090:Ankhd1 ^@ http://purl.uniprot.org/uniprot/E9PUR0|||http://purl.uniprot.org/uniprot/Q5BJ28|||http://purl.uniprot.org/uniprot/Q8BXZ6|||http://purl.uniprot.org/uniprot/Q8C103 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat ^@ ANK|||Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||K Homology|||Polar residues ^@ http://togogenome.org/gene/10090:Epb41 ^@ http://purl.uniprot.org/uniprot/A0A068WAQ5|||http://purl.uniprot.org/uniprot/A0A068WAZ7|||http://purl.uniprot.org/uniprot/A0A571BEG4|||http://purl.uniprot.org/uniprot/P48193 ^@ 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|||C-terminal (CTD)|||Disordered|||FERM|||Hydrophilic|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein 4.1|||Spectrin--actin-binding ^@ http://purl.uniprot.org/annotation/PRO_0000219391|||http://purl.uniprot.org/annotation/VSP_012874 http://togogenome.org/gene/10090:Or4f7 ^@ http://purl.uniprot.org/uniprot/A2AVW1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tsg101 ^@ http://purl.uniprot.org/uniprot/Q3UCW0|||http://purl.uniprot.org/uniprot/Q61187 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Disordered|||Interaction with CEP55|||N-acetylalanine|||PTAP/PSAP motif|||Phosphothreonine|||Polar residues|||Removed|||SB|||Tumor susceptibility gene 101 protein|||UEV ^@ http://purl.uniprot.org/annotation/PRO_0000082607 http://togogenome.org/gene/10090:Dsc3 ^@ http://purl.uniprot.org/uniprot/P55850 ^@ 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|||Cytoplasmic|||Desmocollin-3|||Extracellular|||Helical|||In isoform 3B.|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000003877|||http://purl.uniprot.org/annotation/PRO_0000003878|||http://purl.uniprot.org/annotation/VSP_000665|||http://purl.uniprot.org/annotation/VSP_000666 http://togogenome.org/gene/10090:Znrf1 ^@ http://purl.uniprot.org/uniprot/E9PWL2|||http://purl.uniprot.org/uniprot/E9PZB7|||http://purl.uniprot.org/uniprot/Q91V17 ^@ 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 ^@ Delays neurite degeneration and inhibits DPYSL2/CRMP2 phosphorylation.|||Disordered|||Dominant negative mutant; can prevent Wallerian degeneration when overexpressed.|||E3 ubiquitin-protein ligase ZNRF1|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RING-type|||RING-type; atypical|||Removed|||Required for endosomal and lysosomal localization and myristoylation ^@ http://purl.uniprot.org/annotation/PRO_0000277800 http://togogenome.org/gene/10090:Krt17 ^@ http://purl.uniprot.org/uniprot/Q9QWL7 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Causes twisted hair shafts, broken hair follicles at sebaceous gland level and occasional rupture of the hair bulb or epidermal cyst-like changes.|||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|||Keratin, type I cytoskeletal 17|||Linker 1|||Linker 12|||Phosphoserine|||Phosphoserine; by RPS6KA1|||Phosphothreonine|||Reduces binding to SNF.|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063665 http://togogenome.org/gene/10090:Tcl1b4 ^@ http://purl.uniprot.org/uniprot/P56844 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein TCL1B4 ^@ http://purl.uniprot.org/annotation/PRO_0000184494 http://togogenome.org/gene/10090:Atxn7l2 ^@ http://purl.uniprot.org/uniprot/Q8C8K6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||SCA7 ^@ http://togogenome.org/gene/10090:Msmo1 ^@ http://purl.uniprot.org/uniprot/Q9CRA4 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Motif|||Transmembrane ^@ Fatty acid hydroxylase|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Methylsterol monooxygenase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000117034 http://togogenome.org/gene/10090:Kifap3 ^@ http://purl.uniprot.org/uniprot/P70188|||http://purl.uniprot.org/uniprot/Q3UZA5|||http://purl.uniprot.org/uniprot/Q9CRX5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Chain|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ ARM|||ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||Disordered|||In isoform KAP3B.|||Kinesin-associated protein 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000084303|||http://purl.uniprot.org/annotation/VSP_003899 http://togogenome.org/gene/10090:Fbxo40 ^@ http://purl.uniprot.org/uniprot/P62932|||http://purl.uniprot.org/uniprot/Q3KN92 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Zinc Finger ^@ Disordered|||F-box|||F-box only protein 40|||TRAF-type ^@ http://purl.uniprot.org/annotation/PRO_0000119939 http://togogenome.org/gene/10090:Rapsn ^@ http://purl.uniprot.org/uniprot/P12672 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Repeat|||Sequence Conflict|||Zinc Finger ^@ 43 kDa receptor-associated protein of the synapse|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||RING-type|||Removed|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7 ^@ http://purl.uniprot.org/annotation/PRO_0000167592 http://togogenome.org/gene/10090:Ccr9 ^@ http://purl.uniprot.org/uniprot/Q9WUT7 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ C-C chemokine receptor type 9|||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_0000069292 http://togogenome.org/gene/10090:Ifnl2 ^@ http://purl.uniprot.org/uniprot/Q4VK74 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Interferon lambda-2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000345632 http://togogenome.org/gene/10090:Snrk ^@ http://purl.uniprot.org/uniprot/B9EK90|||http://purl.uniprot.org/uniprot/Q8VDU5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine; by LKB1|||Polar residues|||Protein kinase|||Proton acceptor|||SNF-related serine/threonine-protein kinase|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000225606 http://togogenome.org/gene/10090:Slc35g1 ^@ http://purl.uniprot.org/uniprot/Q8BY79 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Transmembrane ^@ EamA 1|||EamA 2|||Helical|||Solute carrier family 35 member G1 ^@ http://purl.uniprot.org/annotation/PRO_0000244464 http://togogenome.org/gene/10090:Tnnt2 ^@ http://purl.uniprot.org/uniprot/P50752|||http://purl.uniprot.org/uniprot/Q3TH80|||http://purl.uniprot.org/uniprot/Q3TQ90|||http://purl.uniprot.org/uniprot/Q54AB6|||http://purl.uniprot.org/uniprot/Q6P3Z7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform A1.|||In isoform A2 and isoform A3B.|||In isoform A3B.|||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_0000186174|||http://purl.uniprot.org/annotation/VSP_006649|||http://purl.uniprot.org/annotation/VSP_006650|||http://purl.uniprot.org/annotation/VSP_007913 http://togogenome.org/gene/10090:Matcap1 ^@ http://purl.uniprot.org/uniprot/Q810A5 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict ^@ Disordered|||Microtubule-associated tyrosine carboxypeptidase|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000320620 http://togogenome.org/gene/10090:Sct ^@ http://purl.uniprot.org/uniprot/A0A1B0GS37|||http://purl.uniprot.org/uniprot/Q08535|||http://purl.uniprot.org/uniprot/Q3UKU8|||http://purl.uniprot.org/uniprot/Q80ZS9 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide ^@ Glucagon / GIP / secretin / VIP family|||Phosphoserine|||Secretin|||Valine amide ^@ http://purl.uniprot.org/annotation/PRO_0000011426|||http://purl.uniprot.org/annotation/PRO_0000011427|||http://purl.uniprot.org/annotation/PRO_0000011428|||http://purl.uniprot.org/annotation/PRO_5008408596|||http://purl.uniprot.org/annotation/PRO_5009970836|||http://purl.uniprot.org/annotation/PRO_5015098935 http://togogenome.org/gene/10090:Sftpa1 ^@ http://purl.uniprot.org/uniprot/Q9CQI1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Region|||Signal Peptide ^@ C-type lectin|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015099664 http://togogenome.org/gene/10090:Cypt12 ^@ http://purl.uniprot.org/uniprot/Q9DAR6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered ^@ http://togogenome.org/gene/10090:Or13c7 ^@ http://purl.uniprot.org/uniprot/Q9QZ22 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nyap1 ^@ http://purl.uniprot.org/uniprot/Q6PFX7 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes binding to PIK3R2. Slight reduction of phosphorylation in HEK293T cells. Abolishes phosphorylation in HEK293T cells and in neurons; when associated with F-257.|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Involved in CYFIP1- and NCKAP1-binding|||Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 1|||Polar residues|||Pro residues|||Reduced binding to PIK3R2. Slight reduction of phosphorylation in HEK293T cells. Abolishes phosphorylation in HEK293T cells and neurons; when associated with F-212. ^@ http://purl.uniprot.org/annotation/PRO_0000320930|||http://purl.uniprot.org/annotation/VSP_031747|||http://purl.uniprot.org/annotation/VSP_031748 http://togogenome.org/gene/10090:Cypt3 ^@ http://purl.uniprot.org/uniprot/B1AY64|||http://purl.uniprot.org/uniprot/Q80ZR9 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic residues|||Disordered ^@ http://togogenome.org/gene/10090:Dio2 ^@ http://purl.uniprot.org/uniprot/Q9QXV5|||http://purl.uniprot.org/uniprot/Q9Z1Y9 ^@ Active Site|||Chain|||Modification|||Molecule Processing|||Non standard residue|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Non standard residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Selenocysteine|||Type II iodothyronine deiodinase ^@ http://purl.uniprot.org/annotation/PRO_0000154318 http://togogenome.org/gene/10090:Upk3a ^@ http://purl.uniprot.org/uniprot/Q9JKX8 ^@ 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|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Uroplakin-3a ^@ http://purl.uniprot.org/annotation/PRO_0000022638 http://togogenome.org/gene/10090:Atp12a ^@ http://purl.uniprot.org/uniprot/Q9Z1W8 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Phosphoserine; by PKA|||Potassium-transporting ATPase alpha chain 2 ^@ http://purl.uniprot.org/annotation/PRO_0000046261 http://togogenome.org/gene/10090:Maoa ^@ http://purl.uniprot.org/uniprot/Q3TPD9|||http://purl.uniprot.org/uniprot/Q3UJ53|||http://purl.uniprot.org/uniprot/Q64133 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Amine oxidase|||Amine oxidase [flavin-containing] A|||Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Important for catalytic activity|||Important for substrate specificity|||Interaction with membrane phospholipid headgroups|||Mitochondrial intermembrane|||N-acetylmethionine|||Phosphoserine|||S-8alpha-FAD cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000099851 http://togogenome.org/gene/10090:Ino80b ^@ http://purl.uniprot.org/uniprot/A0A0R4J0C7|||http://purl.uniprot.org/uniprot/Q99PT3 ^@ 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 ^@ Basic residues|||Disordered|||HIT-type|||INO80 complex subunit B|||INO80 complex subunit B-like conserved region|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000173555 http://togogenome.org/gene/10090:Coa4 ^@ http://purl.uniprot.org/uniprot/Q8BT51 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ CHCH|||Cx9C motif 1|||Cx9C motif 2|||Cytochrome c oxidase assembly factor 4 homolog, mitochondrial|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000314909 http://togogenome.org/gene/10090:Slc37a3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J133|||http://purl.uniprot.org/uniprot/Q3TIT8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Sugar phosphate exchanger 3 ^@ http://purl.uniprot.org/annotation/PRO_0000309279 http://togogenome.org/gene/10090:Hes3 ^@ http://purl.uniprot.org/uniprot/A0A1W2P7Y8|||http://purl.uniprot.org/uniprot/Q61657 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ BHLH|||Disordered|||Orange|||Transcription factor HES-3|||WRPW motif|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127209 http://togogenome.org/gene/10090:Phactr4 ^@ http://purl.uniprot.org/uniprot/Q501J7 ^@ 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 humdy; failure to close the neural tube and optic fissure, causing exencephaly and retinal coloboma and common birth defects. Specifically disrupts interaction with PPP1CA while it does not affect interaction with actin.|||In isoform 2.|||In isoform 3.|||Phosphatase and actin regulator 4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RPEL 1|||RPEL 2|||RPEL 3 ^@ http://purl.uniprot.org/annotation/PRO_0000287307|||http://purl.uniprot.org/annotation/VSP_025439|||http://purl.uniprot.org/annotation/VSP_025440 http://togogenome.org/gene/10090:Nmur2 ^@ http://purl.uniprot.org/uniprot/Q8BZ39 ^@ 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|||Neuromedin-U receptor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000069911 http://togogenome.org/gene/10090:Or2o1 ^@ http://purl.uniprot.org/uniprot/Q8VET2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ugt3a2 ^@ http://purl.uniprot.org/uniprot/Q8JZZ0 ^@ 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 3A2 ^@ http://purl.uniprot.org/annotation/PRO_0000299154 http://togogenome.org/gene/10090:Elf5 ^@ http://purl.uniprot.org/uniprot/Q3ULZ4|||http://purl.uniprot.org/uniprot/Q3V1F7|||http://purl.uniprot.org/uniprot/Q8VDK3 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Sequence Conflict ^@ ETS|||ETS-related transcription factor Elf-5|||PNT ^@ http://purl.uniprot.org/annotation/PRO_0000204093 http://togogenome.org/gene/10090:Dcaf6 ^@ http://purl.uniprot.org/uniprot/Q9DC22 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Basic and acidic residues|||DDB1- and CUL4-associated factor 6|||Disordered|||IQ|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000304402 http://togogenome.org/gene/10090:Lrrc36 ^@ http://purl.uniprot.org/uniprot/B7ZWL7|||http://purl.uniprot.org/uniprot/F8WI85|||http://purl.uniprot.org/uniprot/Q3V0M2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant ^@ Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRRCT|||Leucine-rich repeat-containing protein 36|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000275856|||http://purl.uniprot.org/annotation/VSP_022965|||http://purl.uniprot.org/annotation/VSP_022966 http://togogenome.org/gene/10090:Bpifb4 ^@ http://purl.uniprot.org/uniprot/A2BGH0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ BPI fold-containing family B member 4|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000355589|||http://purl.uniprot.org/annotation/VSP_052985|||http://purl.uniprot.org/annotation/VSP_052986 http://togogenome.org/gene/10090:Il4i1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0C2|||http://purl.uniprot.org/uniprot/O09046 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Amine oxidase|||Disordered|||In isoform 2.|||L-amino-acid oxidase|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000001711|||http://purl.uniprot.org/annotation/PRO_5006451949|||http://purl.uniprot.org/annotation/VSP_017174 http://togogenome.org/gene/10090:Tgm2 ^@ http://purl.uniprot.org/uniprot/P21981 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site ^@ Alternate|||Important for catalytic activity|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)|||N-acetylalanine|||N6-acetyllysine|||Protein-glutamine gamma-glutamyltransferase 2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213708 http://togogenome.org/gene/10090:Mms19 ^@ http://purl.uniprot.org/uniprot/Q9D071 ^@ Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Turn ^@ HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||In isoform 2.|||In isoform 3.|||MMS19 nucleotide excision repair protein homolog|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000096515|||http://purl.uniprot.org/annotation/VSP_015569|||http://purl.uniprot.org/annotation/VSP_015570|||http://purl.uniprot.org/annotation/VSP_044184 http://togogenome.org/gene/10090:Ogfr ^@ http://purl.uniprot.org/uniprot/Q99PG2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 1|||10|||11|||12|||13|||14|||14 X approximate tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Acidic residues|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||In isoform 2.|||N-acetylmethionine|||Opioid growth factor receptor|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000058031|||http://purl.uniprot.org/annotation/VSP_004061|||http://purl.uniprot.org/annotation/VSP_004062 http://togogenome.org/gene/10090:Acadsb ^@ http://purl.uniprot.org/uniprot/Q9DBL1 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Proton acceptor|||Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000000520 http://togogenome.org/gene/10090:Zbtb34 ^@ http://purl.uniprot.org/uniprot/A2ATY4 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ BTB|||C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Tecta ^@ http://purl.uniprot.org/uniprot/O08523 ^@ 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 ^@ Alpha-tectorin|||GPI-anchor amidated asparagine|||In isoform 2.|||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_0000041737|||http://purl.uniprot.org/annotation/PRO_0000041738|||http://purl.uniprot.org/annotation/VSP_010557 http://togogenome.org/gene/10090:Fsd1l ^@ http://purl.uniprot.org/uniprot/A1L3T0|||http://purl.uniprot.org/uniprot/Q8BYN5 ^@ 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 ^@ B-box C-terminal|||B30.2/SPRY|||Basic and acidic residues|||COS|||Disordered|||FSD1-like protein|||Fibronectin type-III|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089406|||http://purl.uniprot.org/annotation/VSP_039648|||http://purl.uniprot.org/annotation/VSP_039649|||http://purl.uniprot.org/annotation/VSP_039650 http://togogenome.org/gene/10090:Ptp4a2 ^@ http://purl.uniprot.org/uniprot/O70274 ^@ 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|||Strand|||Turn ^@ Cysteine methyl ester|||Locates in the nucleus.|||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_0000094786|||http://purl.uniprot.org/annotation/PRO_0000396732 http://togogenome.org/gene/10090:Zc2hc1a ^@ http://purl.uniprot.org/uniprot/Q8BJH1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C2HC/C3H-type 1|||C2HC/C3H-type 2|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger C2HC domain-containing protein 1A ^@ http://purl.uniprot.org/annotation/PRO_0000280247|||http://purl.uniprot.org/annotation/VSP_023580 http://togogenome.org/gene/10090:Msantd1 ^@ http://purl.uniprot.org/uniprot/A0A0J9YU52|||http://purl.uniprot.org/uniprot/A0A1D5RLV8|||http://purl.uniprot.org/uniprot/Q8BIL2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ 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_0000321820 http://togogenome.org/gene/10090:Npm1 ^@ http://purl.uniprot.org/uniprot/Q5BL09|||http://purl.uniprot.org/uniprot/Q5SQB7|||http://purl.uniprot.org/uniprot/Q61937|||http://purl.uniprot.org/uniprot/Q9DAY9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Site|||Strand|||Turn ^@ ADP-ribosylserine|||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|||Interaction between pentamers|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Necessary for interaction with APEX1|||Nuclear localization signal|||Nucleophosmin|||Nucleophosmin C-terminal|||Nucleoplasmin core|||Phosphoserine|||Phosphoserine; by PLK1 and PLK2|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphothreonine; by CDK1 and CDK2|||Phosphotyrosine|||Polar residues|||Required for interaction with SENP3|||Required for nucleolar localization ^@ http://purl.uniprot.org/annotation/PRO_0000219482 http://togogenome.org/gene/10090:Coq4 ^@ http://purl.uniprot.org/uniprot/Q8BGB8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Transit Peptide ^@ Chain|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||Phosphoserine|||Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000320291 http://togogenome.org/gene/10090:Srsf1 ^@ http://purl.uniprot.org/uniprot/Q6PDM2 ^@ 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 ^@ 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 isoform 2.|||In isoform 3.|||Interaction with SAFB1|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||RRM 1|||RRM 2|||Removed|||Serine/arginine-rich splicing factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000081912|||http://purl.uniprot.org/annotation/VSP_013770|||http://purl.uniprot.org/annotation/VSP_013771|||http://purl.uniprot.org/annotation/VSP_013772|||http://purl.uniprot.org/annotation/VSP_013773 http://togogenome.org/gene/10090:Lypd5 ^@ http://purl.uniprot.org/uniprot/Q9D7Z7 ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated serine|||Ly6/PLAUR domain-containing protein 5|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000226765|||http://purl.uniprot.org/annotation/PRO_0000226766 http://togogenome.org/gene/10090:Tsacc ^@ http://purl.uniprot.org/uniprot/Q9DA44 ^@ Chain|||Molecule Processing ^@ Chain ^@ TSSK6-activating co-chaperone protein ^@ http://purl.uniprot.org/annotation/PRO_0000271075 http://togogenome.org/gene/10090:Cd300lf ^@ http://purl.uniprot.org/uniprot/A0A1C9ZQ14|||http://purl.uniprot.org/uniprot/A2A6Z2|||http://purl.uniprot.org/uniprot/Q6SJQ7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ CMRF35-like molecule 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||Immunoglobulin subtype|||In isoform 2.|||In isoform 3.|||Phosphatase-binding|||Plays an important role in murine norovirus (MNV) binding|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247826|||http://purl.uniprot.org/annotation/PRO_5002641834|||http://purl.uniprot.org/annotation/PRO_5008896853|||http://purl.uniprot.org/annotation/VSP_020066|||http://purl.uniprot.org/annotation/VSP_020067 http://togogenome.org/gene/10090:Prss3 ^@ http://purl.uniprot.org/uniprot/Q792Z0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015098646 http://togogenome.org/gene/10090:Grhl3 ^@ http://purl.uniprot.org/uniprot/Q5FWH3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Grainyhead-like protein 3 homolog|||Grh/CP2 DB|||Transcription activation ^@ http://purl.uniprot.org/annotation/PRO_0000227998 http://togogenome.org/gene/10090:Iigp1 ^@ http://purl.uniprot.org/uniprot/J7NNX8|||http://purl.uniprot.org/uniprot/Q9QZ85 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn ^@ Abrogates interaction with HOOK3. Greatly reduces binding affinity for GDP and GTP. Abolishes GTP-dependent oligomer formation.|||Constitutively active. Binds GTP but fails to hydrolyze it. Does not localize to the parasitophorous vacuole membrane following T.gondii infection.|||IRG-type G|||Interferon-inducible GTPase 1|||N-myristoyl glycine|||Protein is detected exclusively in the aqueous phase.|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000223527 http://togogenome.org/gene/10090:Extl2 ^@ http://purl.uniprot.org/uniprot/Q3TSR0|||http://purl.uniprot.org/uniprot/Q8C089|||http://purl.uniprot.org/uniprot/Q9ES89 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||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|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes enzyme activity.|||Cytoplasmic|||Exostosin-like 2|||Glycosyl transferase 64|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Reduced activity. ^@ http://purl.uniprot.org/annotation/PRO_0000149656|||http://purl.uniprot.org/annotation/PRO_5015097457 http://togogenome.org/gene/10090:Tmbim6 ^@ http://purl.uniprot.org/uniprot/Q9D2C7 ^@ Chain|||Crosslink|||Experimental Information|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||INTRAMEM|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Bax inhibitor 1|||Cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000179079 http://togogenome.org/gene/10090:Poldip2 ^@ http://purl.uniprot.org/uniprot/Q91VA6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ ApaG|||Mitochondrion|||Phosphothreonine|||Polymerase delta-interacting protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000197976 http://togogenome.org/gene/10090:Vps4b ^@ http://purl.uniprot.org/uniprot/P46467|||http://purl.uniprot.org/uniprot/Q3TN07|||http://purl.uniprot.org/uniprot/Q8BM73 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ AAA+ ATPase|||Abolishes ATP-dependent oligomerization.|||Basic and acidic residues|||Defective in ATP-binding. Causes membrane association. Induces vacuolation of endosomal compartments and impairs cholesterol sorting.|||Defective in ATP-hydrolysis. Causes membrane-association. Induces vacuolation of endosomal compartments and impairs cholesterol and protein sorting. Increased perinuclear localization.|||Disordered|||MIT|||Phosphoserine|||Spastin/Vps4 C-terminal|||Vacuolar protein sorting-associated protein 4B ^@ http://purl.uniprot.org/annotation/PRO_0000084768 http://togogenome.org/gene/10090:Col4a6 ^@ http://purl.uniprot.org/uniprot/B1AVK5|||http://purl.uniprot.org/uniprot/Q9ESQ1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Collagen IV NC1|||Disordered|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5002761940|||http://purl.uniprot.org/annotation/PRO_5004324970 http://togogenome.org/gene/10090:Or2j3 ^@ http://purl.uniprot.org/uniprot/Q8VFC2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ldhc ^@ http://purl.uniprot.org/uniprot/P00342|||http://purl.uniprot.org/uniprot/Q548Z6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ Blocked amino end (Ser)|||L-lactate dehydrogenase C chain|||Lactate/malate dehydrogenase C-terminal|||Lactate/malate dehydrogenase N-terminal|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000168480 http://togogenome.org/gene/10090:Gimap7 ^@ http://purl.uniprot.org/uniprot/Q8R379 ^@ Domain Extent|||Region ^@ Domain Extent ^@ AIG1-type G ^@ http://togogenome.org/gene/10090:Glis3 ^@ http://purl.uniprot.org/uniprot/Q0GE24|||http://purl.uniprot.org/uniprot/Q6XP49 ^@ 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 ^@ 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_0000047212|||http://purl.uniprot.org/annotation/VSP_012281|||http://purl.uniprot.org/annotation/VSP_012282|||http://purl.uniprot.org/annotation/VSP_012283 http://togogenome.org/gene/10090:Rbfox2 ^@ http://purl.uniprot.org/uniprot/A0A2K6EDK7|||http://purl.uniprot.org/uniprot/Q8BP71 ^@ 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 ^@ Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Disordered|||In isoform 2, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 2.|||In isoform 3, isoform 4, isoform 6, isoform 7, isoform 8 and isoform 9.|||In isoform 4 and isoform 8.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 9.|||Interaction with RNA|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Polar residues|||Pro residues|||RNA binding protein fox-1 homolog 2|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000317115|||http://purl.uniprot.org/annotation/VSP_030892|||http://purl.uniprot.org/annotation/VSP_030893|||http://purl.uniprot.org/annotation/VSP_030894|||http://purl.uniprot.org/annotation/VSP_030895|||http://purl.uniprot.org/annotation/VSP_030896|||http://purl.uniprot.org/annotation/VSP_030897|||http://purl.uniprot.org/annotation/VSP_030898|||http://purl.uniprot.org/annotation/VSP_030899|||http://purl.uniprot.org/annotation/VSP_030900 http://togogenome.org/gene/10090:Ccl11 ^@ http://purl.uniprot.org/uniprot/P48298 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Eotaxin|||O-linked (GalNAc...) threonine ^@ http://purl.uniprot.org/annotation/PRO_0000005197 http://togogenome.org/gene/10090:Snapc3 ^@ http://purl.uniprot.org/uniprot/Q9D2C9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||snRNA-activating protein complex subunit 3 ^@ http://purl.uniprot.org/annotation/PRO_0000072026 http://togogenome.org/gene/10090:Spock2 ^@ http://purl.uniprot.org/uniprot/Q9ER58 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide ^@ Acidic residues|||Disordered|||Kazal-like|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Phosphoserine|||Testican-2|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000026702 http://togogenome.org/gene/10090:Adipor1 ^@ http://purl.uniprot.org/uniprot/Q3UPA4|||http://purl.uniprot.org/uniprot/Q53YY4|||http://purl.uniprot.org/uniprot/Q91VH1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane ^@ Adiponectin receptor protein 1|||Basic and acidic residues|||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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000218828 http://togogenome.org/gene/10090:Vmn1r198 ^@ http://purl.uniprot.org/uniprot/Q8R263 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Plpp2 ^@ http://purl.uniprot.org/uniprot/A0A1W2P7I9|||http://purl.uniprot.org/uniprot/G3XA61|||http://purl.uniprot.org/uniprot/Q9DAX2 ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Phosphatidic acid phosphatase type 2/haloperoxidase|||Phospholipid phosphatase 2|||Proton donors|||Stabilizes the active site histidine for nucleophilic attack ^@ http://purl.uniprot.org/annotation/PRO_0000220910|||http://purl.uniprot.org/annotation/VSP_009654|||http://purl.uniprot.org/annotation/VSP_009655 http://togogenome.org/gene/10090:Plekhm1 ^@ http://purl.uniprot.org/uniprot/Q7TSI1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Decreases interaction with RAB7A.|||Disordered|||Interaction with RAB7A|||LIR|||No change in osteoclast formation and bone resorption.|||PH 1|||PH 2|||Phorbol-ester/DAG-type|||Phosphoserine|||Pleckstrin homology domain-containing family M member 1|||Polar residues|||Pro residues|||RUN ^@ http://purl.uniprot.org/annotation/PRO_0000309336 http://togogenome.org/gene/10090:Gm10230 ^@ http://purl.uniprot.org/uniprot/Q62478 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Mrpl47 ^@ http://purl.uniprot.org/uniprot/Q8K2Y7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Large ribosomal subunit protein uL29m|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000030568 http://togogenome.org/gene/10090:Cmklr2 ^@ http://purl.uniprot.org/uniprot/Q8K087 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||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_0000069508 http://togogenome.org/gene/10090:Or52e7 ^@ http://purl.uniprot.org/uniprot/Q8VGZ9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Serpina3k ^@ http://purl.uniprot.org/uniprot/A0A0R4J0I1|||http://purl.uniprot.org/uniprot/P07759 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond|||Serine protease inhibitor A3K|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_0000032417|||http://purl.uniprot.org/annotation/PRO_5015044311 http://togogenome.org/gene/10090:Tns4 ^@ http://purl.uniprot.org/uniprot/Q8BZ33 ^@ 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 ^@ Disordered|||PTB|||Phosphoserine|||Polar residues|||SH2|||Tensin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000248214 http://togogenome.org/gene/10090:Mrps6 ^@ http://purl.uniprot.org/uniprot/P58064 ^@ Chain|||Molecule Processing ^@ Chain ^@ Small ribosomal subunit protein bS6m ^@ http://purl.uniprot.org/annotation/PRO_0000176893 http://togogenome.org/gene/10090:Stag3 ^@ http://purl.uniprot.org/uniprot/O70576 ^@ 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|||Cohesin subunit SA-3|||Disordered|||Phosphoserine|||Polar residues|||SCD ^@ http://purl.uniprot.org/annotation/PRO_0000120189 http://togogenome.org/gene/10090:Etnk1 ^@ http://purl.uniprot.org/uniprot/Q9D4V0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Ethanolamine kinase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000206228 http://togogenome.org/gene/10090:Muc15 ^@ http://purl.uniprot.org/uniprot/A2AHK7|||http://purl.uniprot.org/uniprot/Q0VEM9|||http://purl.uniprot.org/uniprot/Q8C6Z1 ^@ 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|||Mucin-15|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000019289|||http://purl.uniprot.org/annotation/PRO_5002641907|||http://purl.uniprot.org/annotation/PRO_5009969498 http://togogenome.org/gene/10090:Upp1 ^@ http://purl.uniprot.org/uniprot/P52624|||http://purl.uniprot.org/uniprot/Q5SUC8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Nucleoside phosphorylase|||Uridine phosphorylase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000063192 http://togogenome.org/gene/10090:Gm906 ^@ http://purl.uniprot.org/uniprot/Q3V0M1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||SPATA31 ^@ http://togogenome.org/gene/10090:Depp1 ^@ http://purl.uniprot.org/uniprot/Q8K2F3 ^@ 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 DEPP1 ^@ http://purl.uniprot.org/annotation/PRO_0000079868 http://togogenome.org/gene/10090:Or5d14 ^@ http://purl.uniprot.org/uniprot/Q7TR28 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rassf3 ^@ http://purl.uniprot.org/uniprot/Q99P51 ^@ 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 ^@ Disordered|||N-acetylserine|||Ras association domain-containing protein 3|||Ras-associating|||Removed|||SARAH ^@ http://purl.uniprot.org/annotation/PRO_0000240397 http://togogenome.org/gene/10090:Gpx6 ^@ http://purl.uniprot.org/uniprot/Q91WR8 ^@ Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Glutathione peroxidase 6 ^@ http://purl.uniprot.org/annotation/PRO_0000013082 http://togogenome.org/gene/10090:Naga ^@ http://purl.uniprot.org/uniprot/Q3U6T2|||http://purl.uniprot.org/uniprot/Q9QWR8 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Alpha galactosidase A C-terminal beta-sandwich|||Alpha-N-acetylgalactosaminidase|||Alpha-galactosidase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000001019|||http://purl.uniprot.org/annotation/PRO_5004229969 http://togogenome.org/gene/10090:Vmn1r185 ^@ http://purl.uniprot.org/uniprot/Q8R299 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zcchc2 ^@ http://purl.uniprot.org/uniprot/Q69ZB8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||CCHC-type|||Disordered|||In isoform 2.|||Polar residues|||Pro residues|||Zinc finger CCHC domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000150950|||http://purl.uniprot.org/annotation/VSP_013721 http://togogenome.org/gene/10090:Fam83a ^@ http://purl.uniprot.org/uniprot/Q8K2P2 ^@ 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 FAM83A ^@ http://purl.uniprot.org/annotation/PRO_0000286814|||http://purl.uniprot.org/annotation/VSP_025192|||http://purl.uniprot.org/annotation/VSP_025193 http://togogenome.org/gene/10090:Cep89 ^@ http://purl.uniprot.org/uniprot/Q9CZX2 ^@ 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|||Centrosomal protein of 89 kDa|||Disordered|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000288810 http://togogenome.org/gene/10090:Fgf15 ^@ http://purl.uniprot.org/uniprot/O35622|||http://purl.uniprot.org/uniprot/Q790L8 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Fibroblast growth factor|||Fibroblast growth factor 15 ^@ http://purl.uniprot.org/annotation/PRO_0000008984|||http://purl.uniprot.org/annotation/PRO_5014205957 http://togogenome.org/gene/10090:Zfp773 ^@ http://purl.uniprot.org/uniprot/Q149T8|||http://purl.uniprot.org/uniprot/Q3V3V8|||http://purl.uniprot.org/uniprot/Q9CZ29 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Jade2 ^@ http://purl.uniprot.org/uniprot/Q6ZQF7 ^@ 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|||C2HC pre-PHD-type|||Disordered|||E3 ubiquitin-protein ligase Jade-2|||In isoform 2.|||N6-acetyllysine|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000253533|||http://purl.uniprot.org/annotation/VSP_021052|||http://purl.uniprot.org/annotation/VSP_021053 http://togogenome.org/gene/10090:Marchf9 ^@ http://purl.uniprot.org/uniprot/Q3TZ87 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Transmembrane|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase MARCHF9|||Helical|||Pro residues|||RING-CH-type ^@ http://purl.uniprot.org/annotation/PRO_0000274283 http://togogenome.org/gene/10090:Or8b36 ^@ http://purl.uniprot.org/uniprot/Q8VF64 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Naif1 ^@ http://purl.uniprot.org/uniprot/Q6PFD7 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Nuclear apoptosis-inducing factor 1|||Required for nuclear localization and apoptosis-inducing activity ^@ http://purl.uniprot.org/annotation/PRO_0000089726 http://togogenome.org/gene/10090:Tmem134 ^@ http://purl.uniprot.org/uniprot/Q8R0J4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||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_0000279486|||http://purl.uniprot.org/annotation/VSP_023455|||http://purl.uniprot.org/annotation/VSP_023456 http://togogenome.org/gene/10090:Ripor2 ^@ http://purl.uniprot.org/uniprot/Q80U16 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2, isoform 5 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||Inhibits interaction with RHOC. Reduces homooligomerization activity. Inhibits RHOC-dependent homooligomerization activity. Abolishes ability to rescue the morphological hair bundle defect in hair cell of RIPOR2-deficient mice.|||Involved in cell filopodia formation|||Loss of retention in the stereocilia, but does not visibly affect the stereocilia structure in the short term. 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.|||Phosphoserine|||Polar residues|||Rho family-interacting cell polarization regulator 2 ^@ http://purl.uniprot.org/annotation/PRO_0000289115|||http://purl.uniprot.org/annotation/VSP_025907|||http://purl.uniprot.org/annotation/VSP_025908|||http://purl.uniprot.org/annotation/VSP_025909|||http://purl.uniprot.org/annotation/VSP_025910|||http://purl.uniprot.org/annotation/VSP_025911|||http://purl.uniprot.org/annotation/VSP_025912|||http://purl.uniprot.org/annotation/VSP_025913|||http://purl.uniprot.org/annotation/VSP_025914|||http://purl.uniprot.org/annotation/VSP_025915|||http://purl.uniprot.org/annotation/VSP_025916|||http://purl.uniprot.org/annotation/VSP_025917 http://togogenome.org/gene/10090:Phex ^@ http://purl.uniprot.org/uniprot/P70669|||http://purl.uniprot.org/uniprot/Q3TYM9 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||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_0000078229 http://togogenome.org/gene/10090:Cst7 ^@ http://purl.uniprot.org/uniprot/O89098|||http://purl.uniprot.org/uniprot/Q9QWL5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Signal Peptide|||Site ^@ Cystatin|||Cystatin-F|||N-linked (GlcNAc...) asparagine|||Reactive site|||Secondary area of contact ^@ http://purl.uniprot.org/annotation/PRO_0000006647|||http://purl.uniprot.org/annotation/PRO_5014313159 http://togogenome.org/gene/10090:Gdnf ^@ http://purl.uniprot.org/uniprot/P48540 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Disordered|||Glial cell line-derived neurotrophic factor|||In isoform 2 and isoform 3.|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000034006|||http://purl.uniprot.org/annotation/PRO_0000034007|||http://purl.uniprot.org/annotation/VSP_006421|||http://purl.uniprot.org/annotation/VSP_026367 http://togogenome.org/gene/10090:Smim23 ^@ http://purl.uniprot.org/uniprot/Q9DAL0 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Small integral membrane protein 23 ^@ http://purl.uniprot.org/annotation/PRO_0000341238 http://togogenome.org/gene/10090:Psmf1 ^@ http://purl.uniprot.org/uniprot/A0A1S6GWI1|||http://purl.uniprot.org/uniprot/A2AU35|||http://purl.uniprot.org/uniprot/Q8BHL8 ^@ 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 ^@ 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|||Proteasome inhibitor PI31 subunit|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000220921 http://togogenome.org/gene/10090:Tepsin ^@ http://purl.uniprot.org/uniprot/B2RPS6|||http://purl.uniprot.org/uniprot/Q3U3N6 ^@ 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 ^@ AP-4 complex accessory subunit Tepsin|||Disordered|||ENTH|||Interaction with AP4B1|||Interaction with AP4E1|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000286679 http://togogenome.org/gene/10090:Sil1 ^@ http://purl.uniprot.org/uniprot/Q9EPK6 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Interaction with HSPA5 and localization to the endoplasmic reticulum|||N-linked (GlcNAc...) asparagine|||Nucleotide exchange factor SIL1 ^@ http://purl.uniprot.org/annotation/PRO_0000223355 http://togogenome.org/gene/10090:Pate7 ^@ http://purl.uniprot.org/uniprot/E9Q4V7 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5003245706 http://togogenome.org/gene/10090:Edf1 ^@ http://purl.uniprot.org/uniprot/Q9JMG1 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Endothelial differentiation-related factor 1|||H-T-H motif|||HTH cro/C1-type|||IQ motif|||Interaction with NR5A2, PPARG and NR1H3|||Interaction with TBP and NR5A1|||N-acetylalanine|||N6-methyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000149796 http://togogenome.org/gene/10090:Or10aa1 ^@ http://purl.uniprot.org/uniprot/Q3U4A2|||http://purl.uniprot.org/uniprot/Q7TRV9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:St8sia1 ^@ http://purl.uniprot.org/uniprot/Q3V3B1|||http://purl.uniprot.org/uniprot/Q64687 ^@ 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|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000149283 http://togogenome.org/gene/10090:Iqcf4 ^@ http://purl.uniprot.org/uniprot/Q6P8Y2 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Dhx15 ^@ http://purl.uniprot.org/uniprot/O35286|||http://purl.uniprot.org/uniprot/Q3UDX4|||http://purl.uniprot.org/uniprot/Q3UKJ6|||http://purl.uniprot.org/uniprot/Q497W9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ ATP-dependent RNA helicase DHX15|||Basic and acidic residues|||DEAH box|||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_0000055140 http://togogenome.org/gene/10090:Zfp668 ^@ http://purl.uniprot.org/uniprot/Q8K2R5 ^@ 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 ^@ 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 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|||Phosphoserine|||Zinc finger protein 668 ^@ http://purl.uniprot.org/annotation/PRO_0000251480 http://togogenome.org/gene/10090:Arid4a ^@ http://purl.uniprot.org/uniprot/F8VPQ2 ^@ 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 ^@ ARID|||AT-rich interactive domain-containing protein 4A|||Acidic residues|||Basic and acidic residues|||DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Retinoblastoma protein binding|||Tudor-knot ^@ http://purl.uniprot.org/annotation/PRO_0000444995 http://togogenome.org/gene/10090:Krtap5-4 ^@ http://purl.uniprot.org/uniprot/Q62220 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1|||10|||11|||12|||13|||14|||14 X 4 AA repeats of C-C-X-P|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 5-4 ^@ http://purl.uniprot.org/annotation/PRO_0000361660 http://togogenome.org/gene/10090:Nufip2 ^@ http://purl.uniprot.org/uniprot/Q5F2E7 ^@ 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|||FMR1-interacting protein NUFIP2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000245522|||http://purl.uniprot.org/annotation/VSP_019729 http://togogenome.org/gene/10090:Yeats2 ^@ http://purl.uniprot.org/uniprot/B9EKJ4|||http://purl.uniprot.org/uniprot/Q3TUF7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||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 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|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||YEATS|||YEATS domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000076367|||http://purl.uniprot.org/annotation/VSP_017006|||http://purl.uniprot.org/annotation/VSP_017007|||http://purl.uniprot.org/annotation/VSP_017008 http://togogenome.org/gene/10090:Foxd2 ^@ http://purl.uniprot.org/uniprot/O35392 ^@ Chain|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Modified Residue|||Region ^@ Disordered|||Fork-head|||Forkhead box protein D2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000091816 http://togogenome.org/gene/10090:Spin2d ^@ http://purl.uniprot.org/uniprot/B1B0R2 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Ahsa1 ^@ http://purl.uniprot.org/uniprot/Q8BK64 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Crosslink|||Modified Residue|||Sequence Conflict ^@ Activator of 90 kDa heat shock protein ATPase homolog 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine; by ABL ^@ http://purl.uniprot.org/annotation/PRO_0000215821 http://togogenome.org/gene/10090:Acsbg3 ^@ http://purl.uniprot.org/uniprot/Q08EE8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ AMP-dependent synthetase/ligase ^@ http://togogenome.org/gene/10090:Gpr33 ^@ http://purl.uniprot.org/uniprot/D8VER2|||http://purl.uniprot.org/uniprot/O88416 ^@ 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 33 ^@ http://purl.uniprot.org/annotation/PRO_0000069554 http://togogenome.org/gene/10090:Adcy4 ^@ http://purl.uniprot.org/uniprot/Q91WF3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Adenylate cyclase type 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000195691 http://togogenome.org/gene/10090:Tex46 ^@ http://purl.uniprot.org/uniprot/Q9CPU3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Meltf ^@ http://purl.uniprot.org/uniprot/Q544J8|||http://purl.uniprot.org/uniprot/Q9R0R1 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated cysteine|||Melanotransferrin|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Removed in mature form|||Transferrin-like|||Transferrin-like 1|||Transferrin-like 2|||Transferrin-like domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000035741|||http://purl.uniprot.org/annotation/PRO_0000035742|||http://purl.uniprot.org/annotation/PRO_5015097764 http://togogenome.org/gene/10090:Thrap3 ^@ http://purl.uniprot.org/uniprot/Q569Z6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region ^@ 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|||Removed|||Required for mRNA decay activity|||Required for mRNA splicing activation|||Thyroid hormone receptor-associated protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000235980 http://togogenome.org/gene/10090:Catsperg1 ^@ http://purl.uniprot.org/uniprot/E9Q355 ^@ 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 ^@ Cation channel sperm-associated protein subunit gamma 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000416886|||http://purl.uniprot.org/annotation/VSP_042983|||http://purl.uniprot.org/annotation/VSP_042984|||http://purl.uniprot.org/annotation/VSP_042985|||http://purl.uniprot.org/annotation/VSP_042986|||http://purl.uniprot.org/annotation/VSP_042987|||http://purl.uniprot.org/annotation/VSP_042988|||http://purl.uniprot.org/annotation/VSP_042989|||http://purl.uniprot.org/annotation/VSP_042990|||http://purl.uniprot.org/annotation/VSP_042991|||http://purl.uniprot.org/annotation/VSP_042992|||http://purl.uniprot.org/annotation/VSP_042993|||http://purl.uniprot.org/annotation/VSP_042994 http://togogenome.org/gene/10090:Pwp2 ^@ http://purl.uniprot.org/uniprot/Q8BU03 ^@ 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|||N6-acetyllysine|||Periodic tryptophan protein 2 homolog|||Phosphoserine|||Phosphothreonine|||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_0000051176 http://togogenome.org/gene/10090:Lrch1 ^@ http://purl.uniprot.org/uniprot/A0A2I3BQ16|||http://purl.uniprot.org/uniprot/P62046|||http://purl.uniprot.org/uniprot/Q3TU52|||http://purl.uniprot.org/uniprot/Q3UP01 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||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|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000084479 http://togogenome.org/gene/10090:Tirap ^@ http://purl.uniprot.org/uniprot/H3BKL1|||http://purl.uniprot.org/uniprot/Q3UB38|||http://purl.uniprot.org/uniprot/Q542S6|||http://purl.uniprot.org/uniprot/Q99JY1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Polar residues|||TIR|||Toll/interleukin-1 receptor domain-containing adapter protein ^@ http://purl.uniprot.org/annotation/PRO_0000072548 http://togogenome.org/gene/10090:Rgs20 ^@ http://purl.uniprot.org/uniprot/E9Q720|||http://purl.uniprot.org/uniprot/Q8C5J7|||http://purl.uniprot.org/uniprot/Q9QZB1 ^@ 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|||In strain: BALB/c.|||RGS|||Regulator of G-protein signaling 20 ^@ http://purl.uniprot.org/annotation/PRO_0000204234 http://togogenome.org/gene/10090:Sdf2 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZW9|||http://purl.uniprot.org/uniprot/Q6P5I1|||http://purl.uniprot.org/uniprot/Q9DCT5 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ MIR|||MIR 1|||MIR 2|||MIR 3|||Stromal cell-derived factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000031956|||http://purl.uniprot.org/annotation/PRO_5004278844|||http://purl.uniprot.org/annotation/PRO_5006451936 http://togogenome.org/gene/10090:Gpr151 ^@ http://purl.uniprot.org/uniprot/Q7TSN6 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 151 protein|||Helical; 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_0000069633 http://togogenome.org/gene/10090:Ghdc ^@ http://purl.uniprot.org/uniprot/Q99J23 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||GH3 domain-containing protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000021594 http://togogenome.org/gene/10090:Mrpl16 ^@ http://purl.uniprot.org/uniprot/Q99N93 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Large ribosomal subunit protein uL16m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000239842 http://togogenome.org/gene/10090:Ubap1 ^@ http://purl.uniprot.org/uniprot/Q8BH48 ^@ 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.|||Interaction with ESCRT-I|||Interaction with PTPN23|||Phosphoserine|||Polar residues|||UBA 1|||UBA 2|||UMA|||Ubiquitin-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000211018|||http://purl.uniprot.org/annotation/VSP_013651 http://togogenome.org/gene/10090:Cldn34b2 ^@ http://purl.uniprot.org/uniprot/Q9D9N2 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099713 http://togogenome.org/gene/10090:Ambp ^@ http://purl.uniprot.org/uniprot/Q07456 ^@ 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|||Site ^@ Alpha-1-microglobulin|||BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||Inhibitory (P1) (chymotrypsin, elastase)|||Inhibitory (P1) (trypsin)|||Inter-alpha-trypsin inhibitor light chain|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Trypstatin|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000017893|||http://purl.uniprot.org/annotation/PRO_0000017894|||http://purl.uniprot.org/annotation/PRO_0000318928 http://togogenome.org/gene/10090:Setd6 ^@ http://purl.uniprot.org/uniprot/Q9CWY3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-lysine methyltransferase SETD6|||N6-methylated lysine; by autocatalysis|||Phosphoserine|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000281890 http://togogenome.org/gene/10090:Socs6 ^@ http://purl.uniprot.org/uniprot/Q9JLY0 ^@ 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|||SH2|||SOCS box|||Suppressor of cytokine signaling 6 ^@ http://purl.uniprot.org/annotation/PRO_0000181252 http://togogenome.org/gene/10090:Qng1 ^@ http://purl.uniprot.org/uniprot/G3X8U3 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue ^@ N-acetylmethionine|||Nucleophile or transition state stabilizer|||Queuosine 5'-phosphate N-glycosylase/hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000458146 http://togogenome.org/gene/10090:Pabpc1l ^@ http://purl.uniprot.org/uniprot/A2A5N3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ PABC|||RRM ^@ http://togogenome.org/gene/10090:Ddx49 ^@ http://purl.uniprot.org/uniprot/Q4FZF3 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Region ^@ DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Probable ATP-dependent RNA helicase DDX49|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000055053 http://togogenome.org/gene/10090:Plscr1 ^@ http://purl.uniprot.org/uniprot/Q9JJ00 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Breakpoint for translocation to form MMTRA1A|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Nuclear localization signal|||PPxY motif|||Phospholipid scramblase 1|||Phosphothreonine; by PKC/PRKCD|||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_0000100785 http://togogenome.org/gene/10090:Mindy1 ^@ http://purl.uniprot.org/uniprot/B7ZMR0|||http://purl.uniprot.org/uniprot/Q76LS9 ^@ 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|||Site|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||MINDY deubiquitinase|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||Ubiquitin carboxyl-terminal hydrolase MINDY-1|||Ubiquitin-binding|||Ubiquitin-binding domain (UBD) ^@ http://purl.uniprot.org/annotation/PRO_0000344038|||http://purl.uniprot.org/annotation/VSP_034716|||http://purl.uniprot.org/annotation/VSP_034717|||http://purl.uniprot.org/annotation/VSP_034718 http://togogenome.org/gene/10090:Tmod3 ^@ http://purl.uniprot.org/uniprot/Q9JHJ0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Phosphoserine|||Tropomodulin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000186135 http://togogenome.org/gene/10090:Map7d2 ^@ http://purl.uniprot.org/uniprot/A2AG50|||http://purl.uniprot.org/uniprot/Q3TS73 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||MAP7 domain-containing protein 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000306810|||http://purl.uniprot.org/annotation/VSP_028494|||http://purl.uniprot.org/annotation/VSP_028495|||http://purl.uniprot.org/annotation/VSP_028496|||http://purl.uniprot.org/annotation/VSP_028497 http://togogenome.org/gene/10090:Or52n20 ^@ http://purl.uniprot.org/uniprot/Q8VGV6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp454 ^@ http://purl.uniprot.org/uniprot/Q80Y34 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Defb18 ^@ http://purl.uniprot.org/uniprot/Q30KP5 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Beta-defensin 18 ^@ http://purl.uniprot.org/annotation/PRO_0000352703 http://togogenome.org/gene/10090:Arc ^@ http://purl.uniprot.org/uniprot/Q9WV31 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region ^@ Abolished palmitoylation, leading to impaired ability mediate synaptic long-term depression (LTD).|||Abolished phosphorylation by CaMK2; knockin mice display normal baseline synaptic transmission and long-term potentiation (LTP) in the hippocampus, but metabotropic receptor-LTD is increased; when associated with A-278.|||Activity-regulated cytoskeleton-associated protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired ability to homooligomerize at 30 degrees Celsius.|||Interaction with DNM2|||Interaction with SH3GL1 or SH3GL3|||Phosphomimetic mutant; does not affect ability to homooligomerize.|||Phosphomimetic mutant; impaired ability to homooligomerize at 30 degrees Celsius.|||Phosphoserine; by CaMK2|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000273286 http://togogenome.org/gene/10090:Stx4a ^@ http://purl.uniprot.org/uniprot/P70452 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical; Anchor for type IV membrane protein|||Interaction with CENPF|||Phosphoserine|||Required for neurite tip localization|||Syntaxin-4|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000210203 http://togogenome.org/gene/10090:Ell ^@ http://purl.uniprot.org/uniprot/O08856 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylalanine|||OCEL|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RNA polymerase II elongation factor ELL|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000146734 http://togogenome.org/gene/10090:E230025N22Rik ^@ http://purl.uniprot.org/uniprot/G5E8S3|||http://purl.uniprot.org/uniprot/Q8BU60 ^@ Coiled-Coil|||Region ^@ Coiled-Coil|||Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Ppp1r12c ^@ http://purl.uniprot.org/uniprot/Q3UMT1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Basic and acidic residues|||Disordered|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein phosphatase 1 regulatory subunit 12C|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000315864 http://togogenome.org/gene/10090:Brd2 ^@ http://purl.uniprot.org/uniprot/B2RS09|||http://purl.uniprot.org/uniprot/Q7JJ13 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Bromo|||Bromo 1|||Bromo 2|||Bromodomain-containing protein 2|||Disordered|||In isoform 2.|||N-acetylmethionine|||NET|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000274005|||http://purl.uniprot.org/annotation/VSP_022601 http://togogenome.org/gene/10090:Lce1l ^@ http://purl.uniprot.org/uniprot/Q9D1G7 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Or5w18 ^@ http://purl.uniprot.org/uniprot/Q8VEU8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vit ^@ http://purl.uniprot.org/uniprot/A0A3B2WCI9|||http://purl.uniprot.org/uniprot/Q8VHI5 ^@ 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.|||LCCL|||N-linked (GlcNAc...) asparagine|||Polar residues|||VWFA|||VWFA 1|||VWFA 2|||Vitrin ^@ http://purl.uniprot.org/annotation/PRO_0000248211|||http://purl.uniprot.org/annotation/VSP_020212 http://togogenome.org/gene/10090:Tubb2b ^@ http://purl.uniprot.org/uniprot/B2RSN3|||http://purl.uniprot.org/uniprot/Q9CWF2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 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|||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_0000262652 http://togogenome.org/gene/10090:Ermp1 ^@ http://purl.uniprot.org/uniprot/Q3UVK0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Endoplasmic reticulum metallopeptidase 1|||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_0000259493|||http://purl.uniprot.org/annotation/VSP_021393|||http://purl.uniprot.org/annotation/VSP_021394 http://togogenome.org/gene/10090:Or52a5b ^@ http://purl.uniprot.org/uniprot/E9Q7C5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cacna1s ^@ http://purl.uniprot.org/uniprot/Q02789 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 isoform 2 and isoform 3.|||In isoform 3.|||Interaction with calmodulin|||N-linked (GlcNAc...) asparagine|||Phenylalkylamine binding|||Phosphoserine|||Phosphoserine; by PKA|||Phosphoserine; by PKA and CAMK2|||Phosphothreonine|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000053944|||http://purl.uniprot.org/annotation/VSP_050420|||http://purl.uniprot.org/annotation/VSP_061231 http://togogenome.org/gene/10090:Nap1l4 ^@ http://purl.uniprot.org/uniprot/A2RSB1|||http://purl.uniprot.org/uniprot/B7ZNL2|||http://purl.uniprot.org/uniprot/Q78ZA7 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Acidic residues|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Nucleosome assembly protein 1-like 4|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000236213 http://togogenome.org/gene/10090:Hbp1 ^@ http://purl.uniprot.org/uniprot/E9Q1A8|||http://purl.uniprot.org/uniprot/E9Q469|||http://purl.uniprot.org/uniprot/Q8R316 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn ^@ AXH|||Basic and acidic residues|||Disordered|||HMG box|||HMG box-containing protein 1|||In isoform 2.|||Strongly reduces Sin3A binding. ^@ http://purl.uniprot.org/annotation/PRO_0000048547|||http://purl.uniprot.org/annotation/VSP_014657 http://togogenome.org/gene/10090:Slc25a53 ^@ http://purl.uniprot.org/uniprot/A2AF28|||http://purl.uniprot.org/uniprot/E9PZF7 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Region|||Repeat|||Signal Peptide ^@ Disordered|||Solcar ^@ http://purl.uniprot.org/annotation/PRO_5015086019 http://togogenome.org/gene/10090:Loxl1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Q4|||http://purl.uniprot.org/uniprot/P97873 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ 2',4',5'-topaquinone|||Disordered|||Lysine tyrosylquinone (Lys-Tyr)|||Lysyl oxidase homolog|||Lysyl oxidase homolog 1|||Lysyl-oxidase like|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000018530|||http://purl.uniprot.org/annotation/PRO_0000018531|||http://purl.uniprot.org/annotation/PRO_5015044313 http://togogenome.org/gene/10090:Tmem8b ^@ http://purl.uniprot.org/uniprot/B1AWJ5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 8B ^@ http://purl.uniprot.org/annotation/PRO_0000333040 http://togogenome.org/gene/10090:Rpl31 ^@ http://purl.uniprot.org/uniprot/P62900 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Large ribosomal subunit protein eL31|||N-acetylmethionine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000153764 http://togogenome.org/gene/10090:Prr36 ^@ http://purl.uniprot.org/uniprot/E9PV26|||http://purl.uniprot.org/uniprot/Q6NVE5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB/POZ|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Atp6v0e ^@ http://purl.uniprot.org/uniprot/Q9CQD8 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||V-type proton ATPase subunit e 1 ^@ http://purl.uniprot.org/annotation/PRO_0000270196 http://togogenome.org/gene/10090:Dolpp1 ^@ http://purl.uniprot.org/uniprot/A0A140T8S3|||http://purl.uniprot.org/uniprot/A2AWJ3|||http://purl.uniprot.org/uniprot/Q9JMF7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ Dolichyldiphosphatase 1|||Helical|||Phosphatidic acid phosphatase type 2/haloperoxidase ^@ http://purl.uniprot.org/annotation/PRO_0000215627 http://togogenome.org/gene/10090:Zfp474 ^@ http://purl.uniprot.org/uniprot/Q6V5K9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger ^@ C2HC/C3H-type 1|||C2HC/C3H-type 2|||C2HC/C3H-type 3|||C2HC/C3H-type 4|||Disordered|||Polar residues|||Zinc finger protein 474 ^@ http://purl.uniprot.org/annotation/PRO_0000353099 http://togogenome.org/gene/10090:Or51v8 ^@ http://purl.uniprot.org/uniprot/F8VQI7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Styk1 ^@ http://purl.uniprot.org/uniprot/Q6J9G1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Polar residues|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase STYK1 ^@ http://purl.uniprot.org/annotation/PRO_0000088164|||http://purl.uniprot.org/annotation/VSP_013427 http://togogenome.org/gene/10090:Gm14325 ^@ http://purl.uniprot.org/uniprot/A2AW67 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Nr0b1 ^@ http://purl.uniprot.org/uniprot/Q53ZY9|||http://purl.uniprot.org/uniprot/Q61066 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Repeat ^@ 1|||2|||3|||4 X 67 AA tandem repeats|||4; truncated|||AF-2 motif|||Disordered|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||NR LBD|||Nuclear receptor subfamily 0 group B member 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053749 http://togogenome.org/gene/10090:Vgll1 ^@ http://purl.uniprot.org/uniprot/Q99NC0 ^@ Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Compositionally Biased Region|||Helix|||Region|||Strand ^@ Basic and acidic residues|||Disordered|||Polar residues|||Transcription cofactor vestigial-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000191348 http://togogenome.org/gene/10090:Cplane1 ^@ http://purl.uniprot.org/uniprot/Q8CE72 ^@ 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|||Ciliogenesis and planar polarity effector 1|||Disordered|||Helical|||In Hug.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000344366 http://togogenome.org/gene/10090:Ccna2 ^@ http://purl.uniprot.org/uniprot/P51943 ^@ 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 ^@ Cyclin-A2|||Disordered|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000080340 http://togogenome.org/gene/10090:4933402N22Rik ^@ http://purl.uniprot.org/uniprot/A3KN63 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered ^@ http://togogenome.org/gene/10090:Tex15 ^@ http://purl.uniprot.org/uniprot/F8VPN2 ^@ 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|||Testis-expressed protein 15 ^@ http://purl.uniprot.org/annotation/PRO_0000435484|||http://purl.uniprot.org/annotation/VSP_058101 http://togogenome.org/gene/10090:Gxylt2 ^@ http://purl.uniprot.org/uniprot/Q810K9 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Glucoside xylosyltransferase 2|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000288540 http://togogenome.org/gene/10090:Irak2 ^@ http://purl.uniprot.org/uniprot/Q8CFA1 ^@ 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 ^@ Death|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interleukin-1 receptor-associated kinase-like 2|||Polar residues|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000277560|||http://purl.uniprot.org/annotation/VSP_023025|||http://purl.uniprot.org/annotation/VSP_023026|||http://purl.uniprot.org/annotation/VSP_023027|||http://purl.uniprot.org/annotation/VSP_023028 http://togogenome.org/gene/10090:Farsb ^@ http://purl.uniprot.org/uniprot/Q9CZU5|||http://purl.uniprot.org/uniprot/Q9WUA2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ B5|||Phenylalanine--tRNA ligase beta subunit ^@ http://purl.uniprot.org/annotation/PRO_0000127017 http://togogenome.org/gene/10090:Psma3 ^@ http://purl.uniprot.org/uniprot/O70435|||http://purl.uniprot.org/uniprot/Q58EV4 ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn ^@ N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Proteasome alpha-type subunits|||Proteasome subunit alpha type-3|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000124092 http://togogenome.org/gene/10090:Gpr84 ^@ http://purl.uniprot.org/uniprot/A0A0R4J100|||http://purl.uniprot.org/uniprot/Q8CIM5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 84|||G-protein coupled receptors family 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 ^@ http://purl.uniprot.org/annotation/PRO_0000069590 http://togogenome.org/gene/10090:Sgsm3 ^@ http://purl.uniprot.org/uniprot/Q8VCZ6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand ^@ Phosphoserine|||RUN|||Rab-GAP TBC|||SH3|||Small G protein signaling modulator 3 ^@ http://purl.uniprot.org/annotation/PRO_0000307811 http://togogenome.org/gene/10090:Phyhip ^@ http://purl.uniprot.org/uniprot/B9EIC7|||http://purl.uniprot.org/uniprot/Q8K0S0 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Glycosylation Site ^@ Fibronectin type-III|||N-linked (GlcNAc...) asparagine|||Phytanoyl-CoA hydroxylase-interacting protein ^@ http://purl.uniprot.org/annotation/PRO_0000058417 http://togogenome.org/gene/10090:Ruvbl1 ^@ http://purl.uniprot.org/uniprot/P60122|||http://purl.uniprot.org/uniprot/Q3U1C2 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue ^@ AAA+ ATPase|||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|||RuvB-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000165640 http://togogenome.org/gene/10090:Insyn1 ^@ http://purl.uniprot.org/uniprot/Q8CD60 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Inhibitory synaptic factor 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000337046 http://togogenome.org/gene/10090:Pnma3 ^@ http://purl.uniprot.org/uniprot/Q8JZW8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Zinc Finger ^@ Basic and acidic residues|||CCHC-type|||Disordered|||Paraneoplastic antigen Ma3 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000280216 http://togogenome.org/gene/10090:Trmt11 ^@ http://purl.uniprot.org/uniprot/E9QKG3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ UPF0020 ^@ http://togogenome.org/gene/10090:Ccndbp1 ^@ http://purl.uniprot.org/uniprot/Q3TVC7 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant ^@ Cyclin-D1-binding protein 1|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with RPLP0|||Interaction with TCF3|||N-acetylalanine|||Removed|||Required for interaction with CCND1 ^@ http://purl.uniprot.org/annotation/PRO_0000323374|||http://purl.uniprot.org/annotation/VSP_032017|||http://purl.uniprot.org/annotation/VSP_032018 http://togogenome.org/gene/10090:Rplp2 ^@ http://purl.uniprot.org/uniprot/P99027 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Large ribosomal subunit protein P2|||N-acetylmethionine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000157641 http://togogenome.org/gene/10090:Glud1 ^@ http://purl.uniprot.org/uniprot/P26443|||http://purl.uniprot.org/uniprot/Q3TSQ7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Transit Peptide ^@ ADP-ribosylcysteine|||Glutamate dehydrogenase 1, mitochondrial|||Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase C-terminal|||Mitochondrion|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000007212 http://togogenome.org/gene/10090:Cela3b ^@ http://purl.uniprot.org/uniprot/Q9CQ52 ^@ 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|||Charge relay system|||Chymotrypsin-like elastase family member 3B|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000416105|||http://purl.uniprot.org/annotation/PRO_0000416106 http://togogenome.org/gene/10090:Cps1 ^@ http://purl.uniprot.org/uniprot/Q8C196 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ ATP-grasp 1|||ATP-grasp 2|||Anthranilate phosphoribosyltransferase homolog|||Carbamoyl-phosphate synthase [ammonia], mitochondrial|||Glutamine amidotransferase type-1|||MGS-like|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) serine; alternate|||O-linked (GlcNAc) threonine|||Phosphoserine|||Phosphoserine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000029898 http://togogenome.org/gene/10090:Vmn2r68 ^@ http://purl.uniprot.org/uniprot/L7N2B3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982396 http://togogenome.org/gene/10090:Fance ^@ http://purl.uniprot.org/uniprot/B8JJD3|||http://purl.uniprot.org/uniprot/F7DAL6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Fanconi Anaemia group E protein C-terminal ^@ http://togogenome.org/gene/10090:Ppp3r2 ^@ http://purl.uniprot.org/uniprot/Q497S1|||http://purl.uniprot.org/uniprot/Q63811 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Site ^@ Calcineurin A binding|||Calcineurin subunit B type 2|||EF-hand|||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_0000073500 http://togogenome.org/gene/10090:Mest ^@ http://purl.uniprot.org/uniprot/D3Z383|||http://purl.uniprot.org/uniprot/Q07646 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ AB hydrolase-1|||Helical|||In isoform 2.|||Mesoderm-specific transcript protein|||N-linked (GlcNAc...) asparagine|||RVIALD ^@ http://purl.uniprot.org/annotation/PRO_0000284419|||http://purl.uniprot.org/annotation/VSP_024534 http://togogenome.org/gene/10090:Or6c35 ^@ http://purl.uniprot.org/uniprot/Q8VFZ8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r98 ^@ http://purl.uniprot.org/uniprot/E9PZ56 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003244335 http://togogenome.org/gene/10090:Adamts19 ^@ http://purl.uniprot.org/uniprot/P59509 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Signal Peptide ^@ A disintegrin and metalloproteinase with thrombospondin motifs 19|||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|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029204|||http://purl.uniprot.org/annotation/PRO_0000029205 http://togogenome.org/gene/10090:Smim24 ^@ http://purl.uniprot.org/uniprot/Q0VG18 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Small integral membrane protein 24 ^@ http://purl.uniprot.org/annotation/PRO_0000322599 http://togogenome.org/gene/10090:2610028H24Rik ^@ http://purl.uniprot.org/uniprot/E9Q7R5|||http://purl.uniprot.org/uniprot/G5E8K1|||http://purl.uniprot.org/uniprot/Q3TT67|||http://purl.uniprot.org/uniprot/Q80X27 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ DUF4587|||Disordered ^@ http://togogenome.org/gene/10090:Adamts7 ^@ http://purl.uniprot.org/uniprot/F6UD05|||http://purl.uniprot.org/uniprot/Q68SA9|||http://purl.uniprot.org/uniprot/Q6PD18 ^@ 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|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ A disintegrin and metalloproteinase with thrombospondin motifs 7|||Basic and acidic residues|||Cysteine switch|||Disintegrin|||Disordered|||In isoform 2.|||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_0000348234|||http://purl.uniprot.org/annotation/PRO_0000348235|||http://purl.uniprot.org/annotation/PRO_5003343911|||http://purl.uniprot.org/annotation/VSP_035113 http://togogenome.org/gene/10090:C1qb ^@ http://purl.uniprot.org/uniprot/P14106 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 4-hydroxyproline|||5-hydroxylysine|||C1q|||Collagen-like|||Complement C1q subcomponent subunit B|||Disordered|||Interchain (with C-26 in chain A)|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000003522 http://togogenome.org/gene/10090:Camk2a ^@ http://purl.uniprot.org/uniprot/F8WHB5|||http://purl.uniprot.org/uniprot/P11798 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn ^@ Abolishes autophosphorylation. Loss of FOXO3 activation. Reduces association with DAGLA. Enhances DAGLA enzymatic activity with an increase of 2-AG levels in dorsolateral striatal tissue of knockin mice. Inhibition of 2-AG breakdown using JZL-184 decreased locomotor activity in knockin mice.|||Basic and acidic residues|||Calcium/calmodulin-dependent protein kinase II association-domain|||Calcium/calmodulin-dependent protein kinase type II subunit alpha|||Calmodulin-binding|||Decreased protein abundance. Decreased autophosphorylation. Changed subcellular localization. Homozygous mice for that mutation are hyperactive and display repetitive behaviors. They also display social deficits and decreased exploratory behavior.|||Disordered|||In isoform Alpha KAP.|||Interaction with BAALC|||Phosphomimetic mutant. Enhanced FOXO3 activation.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086092|||http://purl.uniprot.org/annotation/PRO_5003379505|||http://purl.uniprot.org/annotation/VSP_004767|||http://purl.uniprot.org/annotation/VSP_004768|||http://purl.uniprot.org/annotation/VSP_004769 http://togogenome.org/gene/10090:Nkx1-1 ^@ http://purl.uniprot.org/uniprot/G3UXB3 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox|||NK1 transcription factor-related protein 1|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000452744 http://togogenome.org/gene/10090:Hecw1 ^@ http://purl.uniprot.org/uniprot/Q8K4P8 ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||C2|||Disordered|||E3 ubiquitin-protein ligase HECW1|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Phosphoserine|||Polar residues|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000277666|||http://purl.uniprot.org/annotation/VSP_023074|||http://purl.uniprot.org/annotation/VSP_023075|||http://purl.uniprot.org/annotation/VSP_023076 http://togogenome.org/gene/10090:Ei24 ^@ http://purl.uniprot.org/uniprot/A0A0R4J250|||http://purl.uniprot.org/uniprot/Q61070 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Etoposide-induced protein 2.4|||Helical|||Interaction with BH3 domain of BCL2|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000086946 http://togogenome.org/gene/10090:Zfr ^@ http://purl.uniprot.org/uniprot/O88532 ^@ 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|||DZF|||Disordered|||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_0000312720 http://togogenome.org/gene/10090:Atp23 ^@ http://purl.uniprot.org/uniprot/G3UW46|||http://purl.uniprot.org/uniprot/Q9CWQ3 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Region ^@ Disordered|||Mitochondrial inner membrane protease ATP23 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000330345 http://togogenome.org/gene/10090:Tbc1d9 ^@ http://purl.uniprot.org/uniprot/Q3UYK3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Arginine finger|||Basic and acidic residues|||Disordered|||EF-hand|||GRAM 1|||GRAM 2|||Glutamine finger|||In isoform 2.|||Rab-GAP TBC|||TBC1 domain family member 9 ^@ http://purl.uniprot.org/annotation/PRO_0000288500|||http://purl.uniprot.org/annotation/VSP_025698 http://togogenome.org/gene/10090:Sprr1b ^@ http://purl.uniprot.org/uniprot/Q62267 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Region|||Repeat ^@ 1|||10|||11|||12|||13|||14|||14 X 8 AA approximate tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Cornifin-B|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000150000 http://togogenome.org/gene/10090:Nhsl1 ^@ http://purl.uniprot.org/uniprot/Q8CAF4 ^@ 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 3.|||NHS-like protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000341354|||http://purl.uniprot.org/annotation/VSP_034261|||http://purl.uniprot.org/annotation/VSP_034263 http://togogenome.org/gene/10090:Or10x1 ^@ http://purl.uniprot.org/uniprot/F8VQB1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Leap2 ^@ http://purl.uniprot.org/uniprot/Q91V13 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Propeptide|||Signal Peptide ^@ Liver-expressed antimicrobial peptide 2 ^@ http://purl.uniprot.org/annotation/PRO_0000017359|||http://purl.uniprot.org/annotation/PRO_0000017360 http://togogenome.org/gene/10090:Kdm3b ^@ http://purl.uniprot.org/uniprot/Q6ZPY7 ^@ 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|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C6-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||JmjC|||LXXLL motif|||Lysine-specific demethylase 3B|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000234374|||http://purl.uniprot.org/annotation/VSP_061228|||http://purl.uniprot.org/annotation/VSP_061229|||http://purl.uniprot.org/annotation/VSP_061230 http://togogenome.org/gene/10090:Fntb ^@ http://purl.uniprot.org/uniprot/Q8K2I1 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Modified Residue|||Repeat|||Site ^@ Important for selectivity against geranylgeranyl diphosphate|||PFTB 1|||PFTB 2|||PFTB 3|||PFTB 4|||PFTB 5|||Phosphoserine|||Phosphothreonine|||Protein farnesyltransferase subunit beta ^@ http://purl.uniprot.org/annotation/PRO_0000119762 http://togogenome.org/gene/10090:Acadl ^@ http://purl.uniprot.org/uniprot/A0A0R4J083|||http://purl.uniprot.org/uniprot/P51174 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transit Peptide ^@ Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA dehydrogenase/oxidase N-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||Disordered|||Long-chain specific acyl-CoA dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Proton acceptor|||Reduces activity by 23%; reduces activity by 80% when associated with R-318.|||Reduces activity by 37%; reduces activity by 80% when associated with R-322.|||Reduces activity by 90% when associated with R-318 and R-322. ^@ http://purl.uniprot.org/annotation/PRO_0000000511 http://togogenome.org/gene/10090:A1cf ^@ http://purl.uniprot.org/uniprot/Q5YD48 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ APOBEC1 complementation factor|||In isoform 2.|||In isoform 3.|||RRM 1|||RRM 2|||RRM 3|||Required for nuclear localization ^@ http://purl.uniprot.org/annotation/PRO_0000081483|||http://purl.uniprot.org/annotation/VSP_051930|||http://purl.uniprot.org/annotation/VSP_051931|||http://purl.uniprot.org/annotation/VSP_051932 http://togogenome.org/gene/10090:Tpcn2 ^@ http://purl.uniprot.org/uniprot/Q8BWC0 ^@ Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Complete loss of selectivity for calcium over monocovalent cations.|||Cytoplasmic|||Extracellular|||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.|||Interaction with phosphatidylinositol 3,5-bisphosphate|||Loss of N-glycosylation; when associated with N-594.|||Loss of N-glycosylation; when associated with N-601.|||N-linked (GlcNAc...) asparagine|||Partial loss of selectivity for calcium over monocovalent cations.|||Two pore channel protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000276857|||http://purl.uniprot.org/annotation/VSP_023008|||http://purl.uniprot.org/annotation/VSP_023009|||http://purl.uniprot.org/annotation/VSP_023010 http://togogenome.org/gene/10090:Frmd5 ^@ http://purl.uniprot.org/uniprot/Q6P5H6 ^@ 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|||FERM|||FERM domain-containing protein 5|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ROCK1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247447|||http://purl.uniprot.org/annotation/VSP_019983|||http://purl.uniprot.org/annotation/VSP_019984|||http://purl.uniprot.org/annotation/VSP_019985|||http://purl.uniprot.org/annotation/VSP_019986 http://togogenome.org/gene/10090:Sh3bgrl2 ^@ http://purl.uniprot.org/uniprot/Q8BG73 ^@ Chain|||Molecule Processing|||Motif|||Region ^@ Chain|||Motif ^@ SH3 domain-binding glutamic acid-rich-like protein 2|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000220748 http://togogenome.org/gene/10090:Cep152 ^@ http://purl.uniprot.org/uniprot/A2AUM9 ^@ 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|||Centrosomal protein of 152 kDa|||Disordered|||Interaction with PLK4|||N6-acetyllysine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000424820 http://togogenome.org/gene/10090:Ppic ^@ http://purl.uniprot.org/uniprot/P30412|||http://purl.uniprot.org/uniprot/Q3UC73 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Signal Peptide|||Strand|||Turn ^@ PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase|||Peptidyl-prolyl cis-trans isomerase C ^@ http://purl.uniprot.org/annotation/PRO_0000064148|||http://purl.uniprot.org/annotation/PRO_5014205831 http://togogenome.org/gene/10090:Prelid2 ^@ http://purl.uniprot.org/uniprot/Q0VBB0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ PRELI domain-containing protein 2|||PRELI/MSF1 ^@ http://purl.uniprot.org/annotation/PRO_0000307774 http://togogenome.org/gene/10090:Otop1 ^@ http://purl.uniprot.org/uniprot/Q80VM9 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In mlh (mergulhador phenotype); affected mice have defects in the formation of otoconia in the inner ear, but do not suffer from deafness or other inner ear defects. They cannot perceive gravity and have problems with spatial orientation and with keeping their equilibrium. They show typical head-tilting behavior and are unable to swim. Impaired subcellular localization to the plasma membrane.|||In tlt (tilted phenotype); affected mice have defects in the formation of otoconia in the inner ear, but do not suffer from deafness or other inner ear defects. They cannot perceive gravity and have problems with spatial orientation and with keeping their equilibrium. They show typical head-tilting behavior and are unable to swim. Impaired subcellular localization to the plasma membrane. Effects may be due to dysregulation of pH.|||Proton channel OTOP1 ^@ http://purl.uniprot.org/annotation/PRO_0000313817|||http://purl.uniprot.org/annotation/VSP_030160|||http://purl.uniprot.org/annotation/VSP_030161 http://togogenome.org/gene/10090:Gm3336 ^@ http://purl.uniprot.org/uniprot/J3QMQ6 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003777309 http://togogenome.org/gene/10090:Ugt1a2 ^@ http://purl.uniprot.org/uniprot/P70691 ^@ 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|||UDP-glucuronosyltransferase 1-2 ^@ http://purl.uniprot.org/annotation/PRO_0000036012 http://togogenome.org/gene/10090:Nudt10 ^@ http://purl.uniprot.org/uniprot/P0C027|||http://purl.uniprot.org/uniprot/P0C028 ^@ 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-alpha|||Diphosphoinositol polyphosphate phosphohydrolase 3-beta|||Disordered|||Nudix box|||Nudix hydrolase|||Polar residues|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000057063|||http://purl.uniprot.org/annotation/PRO_0000057066 http://togogenome.org/gene/10090:Cyp1a1 ^@ http://purl.uniprot.org/uniprot/P00184 ^@ Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Glycosylation Site|||Region ^@ Cytochrome P450 1A1|||Mitochondrial targeting signal|||O-linked (GlcNAc) serine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051631 http://togogenome.org/gene/10090:Acbd3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J079|||http://purl.uniprot.org/uniprot/Q6P9T6|||http://purl.uniprot.org/uniprot/Q8BMP6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ ACB|||Basic and acidic residues|||Disordered|||GOLD|||Golgi resident protein GCP60|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Q domain; Interaction with PI4KB, TBC1D22A and TBC1D22B|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000436450 http://togogenome.org/gene/10090:Vhl ^@ http://purl.uniprot.org/uniprot/P40338|||http://purl.uniprot.org/uniprot/Q3TTE7 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure ^@ Chain|||Domain Extent|||Helix|||Region ^@ Disordered|||Interaction with Elongin BC complex|||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_0000065810 http://togogenome.org/gene/10090:Vmn2r109 ^@ http://purl.uniprot.org/uniprot/K7N747 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003911220 http://togogenome.org/gene/10090:Col16a1 ^@ http://purl.uniprot.org/uniprot/Q8BLX7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||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|||Collagen-like 9|||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_0000282960|||http://purl.uniprot.org/annotation/VSP_052375 http://togogenome.org/gene/10090:Arxes1 ^@ http://purl.uniprot.org/uniprot/C0HK79|||http://purl.uniprot.org/uniprot/C0HK80 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Adipocyte-related X-chromosome expressed sequence 1|||Adipocyte-related X-chromosome expressed sequence 2|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000438510|||http://purl.uniprot.org/annotation/PRO_0000438511 http://togogenome.org/gene/10090:Col7a1 ^@ http://purl.uniprot.org/uniprot/Q63870 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ 4-hydroxyproline|||5-hydroxylysine|||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|||Interchain|||Interrupted collagenous region|||N-linked (GlcNAc...) asparagine|||Nonhelical region (NC1)|||Nonhelical region (NC2)|||Pro residues|||Reactive bond|||Triple-helical region|||VWFA 1|||VWFA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000282951 http://togogenome.org/gene/10090:Cenatac ^@ http://purl.uniprot.org/uniprot/Q4VA36 ^@ 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|||Centrosomal AT-AC splicing factor|||Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Polar residues|||Required for centrosome location ^@ http://purl.uniprot.org/annotation/PRO_0000271023|||http://purl.uniprot.org/annotation/VSP_022266|||http://purl.uniprot.org/annotation/VSP_022267|||http://purl.uniprot.org/annotation/VSP_022268|||http://purl.uniprot.org/annotation/VSP_022269 http://togogenome.org/gene/10090:Fbxw9 ^@ http://purl.uniprot.org/uniprot/F8VPX2|||http://purl.uniprot.org/uniprot/Q6PAS7 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Domain Extent|||Non-terminal Residue|||Region|||Repeat ^@ Disordered|||F-box|||WD ^@ http://togogenome.org/gene/10090:Mylk ^@ http://purl.uniprot.org/uniprot/B1B1A8 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Fibronectin type-III|||Ig-like|||Polar residues|||Protein kinase ^@ http://togogenome.org/gene/10090:2610524H06Rik ^@ http://purl.uniprot.org/uniprot/Q9CZU9 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099669 http://togogenome.org/gene/10090:Gzmm ^@ http://purl.uniprot.org/uniprot/B7ZP17|||http://purl.uniprot.org/uniprot/O08643 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5002867028|||http://purl.uniprot.org/annotation/PRO_5015096735 http://togogenome.org/gene/10090:Bicd1 ^@ http://purl.uniprot.org/uniprot/B2KG46|||http://purl.uniprot.org/uniprot/G3UXK5|||http://purl.uniprot.org/uniprot/Q8BR07 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Splice Variant ^@ 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_0000205358|||http://purl.uniprot.org/annotation/VSP_007965|||http://purl.uniprot.org/annotation/VSP_007966|||http://purl.uniprot.org/annotation/VSP_007967|||http://purl.uniprot.org/annotation/VSP_007968 http://togogenome.org/gene/10090:Loxhd1 ^@ http://purl.uniprot.org/uniprot/C8YR32 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant ^@ Chain|||Domain Extent|||Sequence Variant ^@ In the samba murine model of hearing loss.|||Lipoxygenase homology domain-containing protein 1|||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_0000393330 http://togogenome.org/gene/10090:Ibsp ^@ http://purl.uniprot.org/uniprot/Q61711 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||Bone sialoprotein 2|||Cell attachment site|||Disordered|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000020331 http://togogenome.org/gene/10090:Tacc1 ^@ http://purl.uniprot.org/uniprot/F8VQ95|||http://purl.uniprot.org/uniprot/Q6Y685 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Splice Variant ^@ Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||In isoform 2.|||Interaction with CH-TOG|||Interaction with LSM7 and SNRPG|||Interaction with TDRD7|||Interaction with YEATS4|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by AURKC|||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_0000179987|||http://purl.uniprot.org/annotation/VSP_012650|||http://purl.uniprot.org/annotation/VSP_012651 http://togogenome.org/gene/10090:Ndufaf5 ^@ http://purl.uniprot.org/uniprot/A2APY7 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant|||Transit Peptide ^@ Chain|||Splice Variant|||Transit Peptide ^@ Arginine-hydroxylase NDUFAF5, mitochondrial|||In isoform 2.|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000307214|||http://purl.uniprot.org/annotation/VSP_028638 http://togogenome.org/gene/10090:Brca1 ^@ http://purl.uniprot.org/uniprot/P48754|||http://purl.uniprot.org/uniprot/Q6NV63 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ BRCT|||BRCT 1|||BRCT 2|||Basic and acidic residues|||Breast cancer type 1 susceptibility protein homolog|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with PALB2|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by CHEK2|||Phosphothreonine|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055832 http://togogenome.org/gene/10090:Kcnc4 ^@ http://purl.uniprot.org/uniprot/A0A571BG98|||http://purl.uniprot.org/uniprot/Q8R1C0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Topological Domain|||Transmembrane ^@ BTB|||Basic and acidic residues|||Cytoplasmic|||Disordered|||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|||Inactivation gate|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Potassium voltage-gated channel subfamily C member 4|||Pro residues|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054059 http://togogenome.org/gene/10090:Fhdc1 ^@ http://purl.uniprot.org/uniprot/Q3ULZ2 ^@ 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|||FH2|||FH2 domain-containing protein 1|||MTBD; microtubule-binding domain|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000317281 http://togogenome.org/gene/10090:Tpp2 ^@ http://purl.uniprot.org/uniprot/Q64514 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Basic and acidic residues|||Charge relay system|||Disordered|||In isoform Short.|||N-acetylalanine|||N6-acetyllysine|||No effect on adipogenesis.|||Peptidase S8|||Phosphoserine|||Removed|||Tripeptidyl-peptidase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000076423|||http://purl.uniprot.org/annotation/VSP_005446 http://togogenome.org/gene/10090:Rnf186 ^@ http://purl.uniprot.org/uniprot/A2ALL3|||http://purl.uniprot.org/uniprot/Q9D241 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNF186|||Helical|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000261625 http://togogenome.org/gene/10090:Rnf150 ^@ http://purl.uniprot.org/uniprot/Q5DTZ6 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PA|||RING finger protein 150|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000280698|||http://purl.uniprot.org/annotation/VSP_023848|||http://purl.uniprot.org/annotation/VSP_023849|||http://purl.uniprot.org/annotation/VSP_023850 http://togogenome.org/gene/10090:Mab21l4 ^@ http://purl.uniprot.org/uniprot/Q8CEZ4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Protein mab-21-like 4 ^@ http://purl.uniprot.org/annotation/PRO_0000288450 http://togogenome.org/gene/10090:Rnf212b ^@ http://purl.uniprot.org/uniprot/D3Z423 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Zinc Finger ^@ Disordered|||Polar residues|||RING finger protein 212B|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000395110 http://togogenome.org/gene/10090:Rpp21 ^@ http://purl.uniprot.org/uniprot/Q8R040 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylalanine|||Removed|||Ribonuclease P protein subunit p21 ^@ http://purl.uniprot.org/annotation/PRO_0000153846 http://togogenome.org/gene/10090:Cnrip1 ^@ http://purl.uniprot.org/uniprot/Q5M8N0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ CB1 cannabinoid receptor-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000089362 http://togogenome.org/gene/10090:Slc22a8 ^@ http://purl.uniprot.org/uniprot/O88909 ^@ 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|||N-linked (GlcNAc...) asparagine|||Organic anion transporter 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000273441 http://togogenome.org/gene/10090:Gbp8 ^@ http://purl.uniprot.org/uniprot/Q2V6D6 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ GB1/RHD3-type G ^@ http://togogenome.org/gene/10090:Ctla2a ^@ http://purl.uniprot.org/uniprot/P12399 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Region|||Repeat|||Signal Peptide ^@ 1|||2|||2 X 3 AA tandem repeats of E-W-K|||Disordered|||Protein CTLA-2-alpha ^@ http://purl.uniprot.org/annotation/PRO_0000026485 http://togogenome.org/gene/10090:Tox4 ^@ http://purl.uniprot.org/uniprot/Q3UVQ1|||http://purl.uniprot.org/uniprot/Q6A006|||http://purl.uniprot.org/uniprot/Q8BU11 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Disordered|||HMG box|||Loss of transcriptional regulation of gluconeogenic genes expression.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TOX high mobility group box family member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000048569 http://togogenome.org/gene/10090:Pacsin1 ^@ http://purl.uniprot.org/uniprot/Q3TYF2|||http://purl.uniprot.org/uniprot/Q543Y7|||http://purl.uniprot.org/uniprot/Q61644 ^@ 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 ^@ Abolishes interaction with DNM1, MAPT, SYNJ1 and WASL.|||Abolishes membrane tubulation.|||Abolishes membrane tubulation. No effect on phospholipid binding.|||Abolishes membrane tubulation; when associated with E-127.|||Abolishes membrane tubulation; when associated with E-130.|||Basic and acidic residues|||Disordered|||F-BAR|||Impairs interaction with DNM1.|||Increases membrane tubulation.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase C and casein kinase substrate in neurons protein 1|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000161793 http://togogenome.org/gene/10090:Haao ^@ http://purl.uniprot.org/uniprot/Q78JT3 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Region ^@ 3-hydroxyanthranilate 3,4-dioxygenase|||Domain A (catalytic)|||Domain B|||Linker ^@ http://purl.uniprot.org/annotation/PRO_0000064373 http://togogenome.org/gene/10090:Knl1 ^@ http://purl.uniprot.org/uniprot/A3KGI3 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Knl1 C-terminal RWD ^@ http://togogenome.org/gene/10090:Mmp1a ^@ http://purl.uniprot.org/uniprot/Q9EPL5 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Activation peptide|||Cysteine switch|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Interstitial collagenase A|||Metalloprotease|||N-linked (GlcNAc...) asparagine|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000042645|||http://purl.uniprot.org/annotation/PRO_0000042646 http://togogenome.org/gene/10090:Vmn2r25 ^@ http://purl.uniprot.org/uniprot/W4VSP2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015102296 http://togogenome.org/gene/10090:Nfatc2ip ^@ http://purl.uniprot.org/uniprot/O09130 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||NFATC2-interacting protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000281009 http://togogenome.org/gene/10090:Crp ^@ http://purl.uniprot.org/uniprot/P14847 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ C-reactive protein|||Pentraxin (PTX) ^@ http://purl.uniprot.org/annotation/PRO_0000023529 http://togogenome.org/gene/10090:Boc ^@ http://purl.uniprot.org/uniprot/D3Z763|||http://purl.uniprot.org/uniprot/Q6AZB0 ^@ 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|||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 isoform 2.|||In isoform 3.|||In isoform 4.|||In strain: C57BL/6.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000234053|||http://purl.uniprot.org/annotation/PRO_5009688663|||http://purl.uniprot.org/annotation/VSP_018197|||http://purl.uniprot.org/annotation/VSP_018198|||http://purl.uniprot.org/annotation/VSP_018199|||http://purl.uniprot.org/annotation/VSP_018200 http://togogenome.org/gene/10090:Dync1li2 ^@ http://purl.uniprot.org/uniprot/Q6PDL0 ^@ 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 ^@ Cytoplasmic dynein 1 light intermediate chain 2|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000114672 http://togogenome.org/gene/10090:Pdc ^@ http://purl.uniprot.org/uniprot/Q9QW08 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosducin|||Phosphoserine; by PKA|||Thioredoxin fold ^@ http://purl.uniprot.org/annotation/PRO_0000163753 http://togogenome.org/gene/10090:Or13a19 ^@ http://purl.uniprot.org/uniprot/Q8VGL5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slx1b ^@ http://purl.uniprot.org/uniprot/Q3TQB5|||http://purl.uniprot.org/uniprot/Q8BX32 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Splice Variant|||Zinc Finger ^@ Disordered|||GIY-YIG|||In isoform 2.|||SLX1-type|||Structure-specific endonuclease subunit SLX1 ^@ http://purl.uniprot.org/annotation/PRO_0000332121|||http://purl.uniprot.org/annotation/VSP_033332|||http://purl.uniprot.org/annotation/VSP_033333 http://togogenome.org/gene/10090:Zfp872 ^@ http://purl.uniprot.org/uniprot/Q3UVL3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ik ^@ http://purl.uniprot.org/uniprot/Q9Z1M8 ^@ 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 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000097236 http://togogenome.org/gene/10090:Hlx ^@ http://purl.uniprot.org/uniprot/Q549B7|||http://purl.uniprot.org/uniprot/Q61670|||http://purl.uniprot.org/uniprot/Q6P3B7|||http://purl.uniprot.org/uniprot/Q80YV1 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||H2.0-like homeobox protein|||Homeobox|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000048979 http://togogenome.org/gene/10090:Hydin ^@ http://purl.uniprot.org/uniprot/Q80W93 ^@ 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|||Disordered|||Hydrocephalus-inducing protein|||In isoform 2.|||In isoform 3.|||Interaction with KIF9|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000284845|||http://purl.uniprot.org/annotation/VSP_024701|||http://purl.uniprot.org/annotation/VSP_024702|||http://purl.uniprot.org/annotation/VSP_040915|||http://purl.uniprot.org/annotation/VSP_040916|||http://purl.uniprot.org/annotation/VSP_040917 http://togogenome.org/gene/10090:Asb2 ^@ http://purl.uniprot.org/uniprot/Q8K0L0 ^@ 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 ^@ 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 SOCS box protein 2|||Disordered|||In isoform 2.|||Loss of E3 ubiquitin-protein ligase complex association and loss of activity of the complex. Does not affect localization of isoform 1 to the Z line or its interaction with DES.|||Phosphoserine|||Polar residues|||SOCS box|||UIM ^@ http://purl.uniprot.org/annotation/PRO_0000233303|||http://purl.uniprot.org/annotation/VSP_052025|||http://purl.uniprot.org/annotation/VSP_052026 http://togogenome.org/gene/10090:Ccdc88b ^@ http://purl.uniprot.org/uniprot/Q4QRL3 ^@ 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|||Coiled-coil domain-containing protein 88B|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317455|||http://purl.uniprot.org/annotation/VSP_030966 http://togogenome.org/gene/10090:Mettl21c ^@ http://purl.uniprot.org/uniprot/Q8BLU2 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Protein-lysine methyltransferase METTL21C ^@ http://purl.uniprot.org/annotation/PRO_0000319591 http://togogenome.org/gene/10090:Wdsub1 ^@ http://purl.uniprot.org/uniprot/A2AUX8|||http://purl.uniprot.org/uniprot/Q9D0I6 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict ^@ 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_0000278609 http://togogenome.org/gene/10090:Cd274 ^@ http://purl.uniprot.org/uniprot/Q3U472|||http://purl.uniprot.org/uniprot/Q9EP73 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes the binding to PDCD1.|||Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells.|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||No effect on PDCD1 binding.|||PDCD1 binding.|||Programmed cell death 1 ligand 1|||Significantly reduces the binding to PDCD1. ^@ http://purl.uniprot.org/annotation/PRO_0000014554|||http://purl.uniprot.org/annotation/PRO_5014309187 http://togogenome.org/gene/10090:Tapbp ^@ http://purl.uniprot.org/uniprot/Q3TCU5|||http://purl.uniprot.org/uniprot/Q3U9A3|||http://purl.uniprot.org/uniprot/Q8C6N4|||http://purl.uniprot.org/uniprot/Q9D679|||http://purl.uniprot.org/uniprot/Q9R233 ^@ 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|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Ig-like|||Ig-like C1-type|||Ig-like domain-containing protein|||In isoform Short.|||Interchain (with C-57 in PDIA3)|||Lumenal|||May be involved in interaction with TAP|||N-linked (GlcNAc...) asparagine|||Tapasin ^@ http://purl.uniprot.org/annotation/PRO_0000014991|||http://purl.uniprot.org/annotation/PRO_5004325084|||http://purl.uniprot.org/annotation/PRO_5010843385|||http://purl.uniprot.org/annotation/PRO_5015097435|||http://purl.uniprot.org/annotation/VSP_002578 http://togogenome.org/gene/10090:Kmt2b ^@ http://purl.uniprot.org/uniprot/F8WJ40|||http://purl.uniprot.org/uniprot/O08550|||http://purl.uniprot.org/uniprot/Q6PHU4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ A.T hook 1|||A.T hook 2|||A.T hook 3|||Acidic residues|||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|||Menin-binding motif (MBM)|||N-acetylalanine|||PHD-type|||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_0000124882 http://togogenome.org/gene/10090:Ykt6 ^@ http://purl.uniprot.org/uniprot/Q9CQW1 ^@ Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict ^@ Cysteine methyl ester|||Longin|||Phosphoserine|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine|||Synaptobrevin homolog YKT6|||v-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000280710|||http://purl.uniprot.org/annotation/PRO_0000396662 http://togogenome.org/gene/10090:R3hdm2 ^@ http://purl.uniprot.org/uniprot/E9Q9D6|||http://purl.uniprot.org/uniprot/Q148X5|||http://purl.uniprot.org/uniprot/Q80TM6 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Polar residues|||R3H|||R3H domain-containing protein 2|||SUZ ^@ http://purl.uniprot.org/annotation/PRO_0000050788|||http://purl.uniprot.org/annotation/VSP_010553|||http://purl.uniprot.org/annotation/VSP_010554|||http://purl.uniprot.org/annotation/VSP_010555|||http://purl.uniprot.org/annotation/VSP_010556 http://togogenome.org/gene/10090:Tsr1 ^@ http://purl.uniprot.org/uniprot/Q5SWD9 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Bms1-type G|||Disordered|||In isoform 2.|||In isoform 3.|||Pre-rRNA-processing protein TSR1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000311275|||http://purl.uniprot.org/annotation/VSP_029504|||http://purl.uniprot.org/annotation/VSP_029505|||http://purl.uniprot.org/annotation/VSP_029506 http://togogenome.org/gene/10090:Slc6a20a ^@ http://purl.uniprot.org/uniprot/Q8VDB9 ^@ 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=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 transporter XTRP3A ^@ http://purl.uniprot.org/annotation/PRO_0000343522 http://togogenome.org/gene/10090:Diaph2 ^@ http://purl.uniprot.org/uniprot/K4PWM5|||http://purl.uniprot.org/uniprot/O70566|||http://purl.uniprot.org/uniprot/Q6W4W7 ^@ 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|||DAD|||Disordered|||FH1|||FH2|||GBD/FH3|||N-acetylmethionine|||Pro residues|||Protein diaphanous homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000194896 http://togogenome.org/gene/10090:Flacc1 ^@ http://purl.uniprot.org/uniprot/A0A087WNN1|||http://purl.uniprot.org/uniprot/Q8BVM7 ^@ 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 ^@ Disordered|||Flagellum-associated coiled-coil domain-containing protein 1|||In isoform 2.|||N6-acetyllysine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000344494|||http://purl.uniprot.org/annotation/VSP_058875|||http://purl.uniprot.org/annotation/VSP_058876 http://togogenome.org/gene/10090:Trappc8 ^@ http://purl.uniprot.org/uniprot/A0A286YCX6|||http://purl.uniprot.org/uniprot/E9PY51|||http://purl.uniprot.org/uniprot/Q69ZT3|||http://purl.uniprot.org/uniprot/Q8BJI6 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Non-terminal Residue|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Samd3 ^@ http://purl.uniprot.org/uniprot/E9Q3G4|||http://purl.uniprot.org/uniprot/Q8C4H2 ^@ 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.|||Polar residues|||SAM|||Sterile alpha motif domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000279497|||http://purl.uniprot.org/annotation/VSP_041628|||http://purl.uniprot.org/annotation/VSP_041629 http://togogenome.org/gene/10090:Ephb4 ^@ http://purl.uniprot.org/uniprot/P54761|||http://purl.uniprot.org/uniprot/Q3V1K8|||http://purl.uniprot.org/uniprot/Q8C7S3|||http://purl.uniprot.org/uniprot/Q8C8K1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Eph LBD|||Ephrin type-B receptor 4|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Protein kinase|||Proton acceptor|||SAM|||receptor protein-tyrosine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000016835|||http://purl.uniprot.org/annotation/PRO_5012181179|||http://purl.uniprot.org/annotation/PRO_5012542522|||http://purl.uniprot.org/annotation/PRO_5015099027 http://togogenome.org/gene/10090:Mob3c ^@ http://purl.uniprot.org/uniprot/Q8BJG4 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ MOB kinase activator 3C ^@ http://purl.uniprot.org/annotation/PRO_0000193575 http://togogenome.org/gene/10090:Sbf2 ^@ http://purl.uniprot.org/uniprot/E9PXF8 ^@ 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|||GRAM|||In isoform 2.|||Myotubularin phosphatase|||Myotubularin-related protein 13|||PH|||Phosphoserine|||Required for homodimerization and interaction with MTMR2|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000446366|||http://purl.uniprot.org/annotation/VSP_060070 http://togogenome.org/gene/10090:Pdcl ^@ http://purl.uniprot.org/uniprot/Q9DBX2 ^@ 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|||Disordered|||N-acetylthreonine|||Phosducin-like protein|||Phosphoserine|||Removed|||Thioredoxin fold ^@ http://purl.uniprot.org/annotation/PRO_0000163756 http://togogenome.org/gene/10090:Per3 ^@ http://purl.uniprot.org/uniprot/O70361 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolishes homodimerization.|||Basic and acidic residues|||CRY binding domain|||CSNK1E binding domain|||Disordered|||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 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000162634 http://togogenome.org/gene/10090:Myo3b ^@ http://purl.uniprot.org/uniprot/F8VQ79|||http://purl.uniprot.org/uniprot/Q1EG27 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant ^@ Actin-binding|||Basic and acidic residues|||Disordered|||IQ 1|||IQ 2|||In isoform 2.|||Myosin motor|||Myosin-IIIb|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000277830|||http://purl.uniprot.org/annotation/VSP_023112|||http://purl.uniprot.org/annotation/VSP_036028 http://togogenome.org/gene/10090:Lkaaear1 ^@ http://purl.uniprot.org/uniprot/Q8BIG2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Protein LKAAEAR1 ^@ http://purl.uniprot.org/annotation/PRO_0000329280 http://togogenome.org/gene/10090:Clp1 ^@ http://purl.uniprot.org/uniprot/Q99LI9 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict ^@ Polyribonucleotide 5'-hydroxyl-kinase Clp1|||Progressive loss of motor neurons, axonal motor neuropathy, and muscle paralysis leading to death within hours of birth. Mice exhibit microcephaly due to reduced numbers of cortical neurons. Embryos have normal numbers and proliferation of neuronal progenitors, but neuronal progenitor cells undergo enhanced cell death, resulting in reduced numbers of cortical neurons. ^@ http://purl.uniprot.org/annotation/PRO_0000089864 http://togogenome.org/gene/10090:Gapvd1 ^@ http://purl.uniprot.org/uniprot/Q6PAR5 ^@ 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 4 and isoform 5.|||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_0000324772|||http://purl.uniprot.org/annotation/VSP_032363|||http://purl.uniprot.org/annotation/VSP_032364|||http://purl.uniprot.org/annotation/VSP_032365|||http://purl.uniprot.org/annotation/VSP_032366|||http://purl.uniprot.org/annotation/VSP_032367|||http://purl.uniprot.org/annotation/VSP_032368 http://togogenome.org/gene/10090:Traf5 ^@ http://purl.uniprot.org/uniprot/P70191|||http://purl.uniprot.org/uniprot/Q3UMS9 ^@ 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 ^@ Abolished ubiquitination by the SCF(FBXL2) complex.|||Decreased interaction with FBXL2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with EIF2AK2/PKR|||MATH|||RING-type|||TNF receptor-associated factor 5|||TRAF-type|||TRAF-type 1|||TRAF-type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000056406 http://togogenome.org/gene/10090:Cul4a ^@ http://purl.uniprot.org/uniprot/Q3TCH7 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Modified Residue|||Region|||Sequence Conflict ^@ Cullin-4A|||Disordered|||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)|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000236184 http://togogenome.org/gene/10090:Or1x6 ^@ http://purl.uniprot.org/uniprot/A0A0N4SUP0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:D17H6S53E ^@ http://purl.uniprot.org/uniprot/B2RS43|||http://purl.uniprot.org/uniprot/Q9Z1R4 ^@ 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 C6orf47 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089505 http://togogenome.org/gene/10090:Slc9a1 ^@ http://purl.uniprot.org/uniprot/Q3UDC9|||http://purl.uniprot.org/uniprot/Q61165 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Cation/H+ exchanger|||Channel pore-lining|||Confers pH-dependent PI(4,5)P2 binding|||Cytoplasmic|||Disordered|||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 swe.|||Interaction with CALM1|||Interaction with CHP2|||Interaction with PPP3CA|||Interaction with TESC|||PI(4,5)P2-binding region|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sodium/hydrogen exchanger 1|||Sodium/hydrogen exchanger regulatory region ^@ http://purl.uniprot.org/annotation/PRO_0000052348 http://togogenome.org/gene/10090:Ak8 ^@ http://purl.uniprot.org/uniprot/Q32M07 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Region|||Sequence Conflict ^@ Adenylate kinase 1|||Adenylate kinase 2|||Adenylate kinase 8|||LID 1|||LID 2|||NMP 1|||NMP 2 ^@ http://purl.uniprot.org/annotation/PRO_0000279385 http://togogenome.org/gene/10090:Pikfyve ^@ http://purl.uniprot.org/uniprot/D3Z5N5|||http://purl.uniprot.org/uniprot/Q9Z1T6 ^@ Binding 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|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 1-phosphatidylinositol 3-phosphate 5-kinase|||Basic and acidic residues|||Catalytic|||Chaperonin-like domain|||DEP|||Disordered|||FYVE-type|||In isoform 2.|||In isoform 3.|||Loss of kinase activity. Decreases RABEPK location to membranes. Abolishes EGFR translocation to the nucleus.|||N-acetylalanine|||PIPK|||Phosphoserine|||Phosphoserine; by PKB/AKT1 or PKB/AKT2|||Phosphoserine; by autocatalysis|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000185453|||http://purl.uniprot.org/annotation/VSP_034953|||http://purl.uniprot.org/annotation/VSP_034954|||http://purl.uniprot.org/annotation/VSP_034955|||http://purl.uniprot.org/annotation/VSP_034956 http://togogenome.org/gene/10090:Prss33 ^@ http://purl.uniprot.org/uniprot/Q80WM7 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Splice Variant ^@ Charge relay system|||In isoform 2.|||Peptidase S1|||Serine protease 33 ^@ http://purl.uniprot.org/annotation/PRO_0000299317|||http://purl.uniprot.org/annotation/VSP_027609 http://togogenome.org/gene/10090:Suox ^@ http://purl.uniprot.org/uniprot/Q8R086 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Cytochrome b5 heme-binding|||Hinge|||Homodimerization|||Mitochondrion|||Moco domain|||Phosphoserine|||Sulfite oxidase, mitochondrial|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000006483 http://togogenome.org/gene/10090:Usp39 ^@ http://purl.uniprot.org/uniprot/Q3TIX9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||UBP-type; degenerate|||USP|||Ubiquitin carboxyl-terminal hydrolase 39 ^@ http://purl.uniprot.org/annotation/PRO_0000223963 http://togogenome.org/gene/10090:Or4c122 ^@ http://purl.uniprot.org/uniprot/Q8VGM9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or9r7 ^@ http://purl.uniprot.org/uniprot/Q8VFU4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Banp ^@ http://purl.uniprot.org/uniprot/Q8VBU8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ BEN|||DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs TP53 activation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interaction with CUX1 and HDAC1|||N6-acetyllysine|||No effect on TP53 activation.|||Phosphoserine|||Polar residues|||Protein BANP|||Required for TP53 activation ^@ http://purl.uniprot.org/annotation/PRO_0000297911|||http://purl.uniprot.org/annotation/VSP_027403|||http://purl.uniprot.org/annotation/VSP_027404|||http://purl.uniprot.org/annotation/VSP_027405 http://togogenome.org/gene/10090:Mrpl10 ^@ http://purl.uniprot.org/uniprot/Q3TBW2 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Large ribosomal subunit protein uL10m|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000273076 http://togogenome.org/gene/10090:Gpatch2l ^@ http://purl.uniprot.org/uniprot/Q6PE65 ^@ 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|||G patch domain-containing protein 2-like|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089928|||http://purl.uniprot.org/annotation/VSP_014717 http://togogenome.org/gene/10090:Serpind1 ^@ http://purl.uniprot.org/uniprot/P49182 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Site ^@ 1|||2|||2 X 11 AA approximate repeats, Asp/Glu-rich (acidic) (hirudin-like)|||Glycosaminoglycan-binding site|||Heparin cofactor 2|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000032495 http://togogenome.org/gene/10090:Hoxd11 ^@ http://purl.uniprot.org/uniprot/A2ASM7|||http://purl.uniprot.org/uniprot/P23813 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Homeobox protein Hox-D11|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000200232 http://togogenome.org/gene/10090:Nt5c2 ^@ http://purl.uniprot.org/uniprot/A0A494B9X3|||http://purl.uniprot.org/uniprot/E9Q9M1|||http://purl.uniprot.org/uniprot/Q3V1L4 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Cytosolic purine 5'-nucleotidase|||Disordered|||Nucleophile|||Phosphoserine|||Proton donor|||Required for tetramer assembly ^@ http://purl.uniprot.org/annotation/PRO_0000310264 http://togogenome.org/gene/10090:Wnt7b ^@ http://purl.uniprot.org/uniprot/P28047|||http://purl.uniprot.org/uniprot/Q6PDY6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Disordered linker|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-7b ^@ http://purl.uniprot.org/annotation/PRO_0000041445 http://togogenome.org/gene/10090:Spata3 ^@ http://purl.uniprot.org/uniprot/Q3V2M5|||http://purl.uniprot.org/uniprot/Q6P8X3|||http://purl.uniprot.org/uniprot/Q9D9T6 ^@ 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 and isoform 3.|||In isoform 3.|||In isoform 4.|||Polar residues|||Pro residues|||Spermatogenesis-associated protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000072175|||http://purl.uniprot.org/annotation/VSP_008523|||http://purl.uniprot.org/annotation/VSP_008524|||http://purl.uniprot.org/annotation/VSP_008525|||http://purl.uniprot.org/annotation/VSP_008526|||http://purl.uniprot.org/annotation/VSP_008527 http://togogenome.org/gene/10090:Usp38 ^@ http://purl.uniprot.org/uniprot/Q8BW70 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 38 ^@ http://purl.uniprot.org/annotation/PRO_0000080669 http://togogenome.org/gene/10090:Per2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0U3|||http://purl.uniprot.org/uniprot/O54943|||http://purl.uniprot.org/uniprot/Q3TW41|||http://purl.uniprot.org/uniprot/Q8C8R0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolishes dimerization.|||Abolishes interaction with NR1D1.|||Abolishes interaction with PPARA and NR1D1. No effect on interaction with CRY1. Abolishes interaction with PPARA and NR1D1 as well as reduces the amplitude of BMAL1 expression; when associated with 1052-E--A-1055.|||Accumulates in the nucleus. Exlcusively nuclear; when associated with 113-A--A-116 and 985-A--A-990.|||Accumulates in the nucleus. Exlcusively nuclear; when associated with 464-A--A-467 and 985-A--A-990.|||CRY binding domain|||CSNK1E binding domain|||Disordered|||Important for protein stability|||Interaction with PPARG|||LXXLL|||No effect on interaction with NR1D1.|||No effect on interaction with PPARA. Abolishes interaction with PPARA and NR1D1 as well as reduces the amplitude of BMAL1 expression; when associated with 306-A--A-310.|||Nuclear export signal 1|||Nuclear export signal 2|||Nuclear export signal 3|||Nuclear localization signal|||PAC|||PAS|||PAS 1|||PAS 2|||Period circadian protein homolog 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Slightly accumulates in the nucleus. Exlcusively nuclear; when associated with 464-A--A-467 and 985-A--A-990. ^@ http://purl.uniprot.org/annotation/PRO_0000162631 http://togogenome.org/gene/10090:Tubal3 ^@ http://purl.uniprot.org/uniprot/Q3UX10 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Motif|||Sequence Conflict ^@ MREC motif|||Tubulin alpha chain-like 3 ^@ http://purl.uniprot.org/annotation/PRO_0000313710 http://togogenome.org/gene/10090:Cdk11b ^@ http://purl.uniprot.org/uniprot/A2A9P6|||http://purl.uniprot.org/uniprot/P24788 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||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|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ 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.|||Phosphoserine|||Phosphoserine; by CDK7|||Phosphothreonine|||Phosphothreonine; by CDK7|||Phosphotyrosine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000024313|||http://purl.uniprot.org/annotation/VSP_018835 http://togogenome.org/gene/10090:Acy1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J050|||http://purl.uniprot.org/uniprot/Q99JW2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Aminoacylase-1|||Peptidase M20 dimerisation|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000274007 http://togogenome.org/gene/10090:Hsbp1l1 ^@ http://purl.uniprot.org/uniprot/B2RXB2 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Heat shock factor-binding protein 1-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000394663 http://togogenome.org/gene/10090:Fam20b ^@ http://purl.uniprot.org/uniprot/Q8VCS3 ^@ 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_0000008746 http://togogenome.org/gene/10090:Ppid ^@ http://purl.uniprot.org/uniprot/Q9CR16 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Chaperone activity|||Interaction with HSP90AB1|||N6-acetyllysine|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase D|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000064154 http://togogenome.org/gene/10090:Gm525 ^@ http://purl.uniprot.org/uniprot/Q3V3I5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Uncharacterized protein C17orf67 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000287180 http://togogenome.org/gene/10090:Or5p79 ^@ http://purl.uniprot.org/uniprot/Q8VG13 ^@ 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 5P79 ^@ http://purl.uniprot.org/annotation/PRO_0000150854 http://togogenome.org/gene/10090:Prr23a3 ^@ http://purl.uniprot.org/uniprot/Q9CWP9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Pro residues|||Proline-rich protein 23A3 ^@ http://purl.uniprot.org/annotation/PRO_0000332253 http://togogenome.org/gene/10090:Pcdhb9 ^@ http://purl.uniprot.org/uniprot/E9Q5G2|||http://purl.uniprot.org/uniprot/Q8CCK1|||http://purl.uniprot.org/uniprot/Q91XZ1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Cadherin|||Cadherin domain-containing protein|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5004304051|||http://purl.uniprot.org/annotation/PRO_5014312433 http://togogenome.org/gene/10090:Cables1 ^@ http://purl.uniprot.org/uniprot/Q3TYS6|||http://purl.uniprot.org/uniprot/Q3U148|||http://purl.uniprot.org/uniprot/Q9ESJ1 ^@ 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 ^@ CDK5 and ABL1 enzyme substrate 1|||Cyclin N-terminal|||Disordered|||Efficiently phosphorylated in vitro.|||Interaction with CDK3|||Interaction with TDRD7|||Less efficiently phosphorylated in vitro.|||Phosphoserine|||Phosphoserine; by CDK2 and CDK3|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000080511 http://togogenome.org/gene/10090:Them7 ^@ http://purl.uniprot.org/uniprot/Q9DCP4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Thioesterase ^@ http://togogenome.org/gene/10090:Pcdh20 ^@ http://purl.uniprot.org/uniprot/Q68FM5|||http://purl.uniprot.org/uniprot/Q8BIZ0 ^@ 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|||Sequence Conflict|||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|||Protocadherin-20 ^@ http://purl.uniprot.org/annotation/PRO_0000004006 http://togogenome.org/gene/10090:Repin1 ^@ http://purl.uniprot.org/uniprot/A0A0R3P9D3|||http://purl.uniprot.org/uniprot/D3YY67|||http://purl.uniprot.org/uniprot/Q5U4E2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||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 1; atypical|||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|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Replication initiator 1 ^@ http://purl.uniprot.org/annotation/PRO_0000274913 http://togogenome.org/gene/10090:Arl6ip6 ^@ http://purl.uniprot.org/uniprot/Q8BH07 ^@ 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_0000307325 http://togogenome.org/gene/10090:Cdx1 ^@ http://purl.uniprot.org/uniprot/P18111 ^@ 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 CDX-1|||Interaction with 5-mCpG DNA|||Interaction with DNA|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000048847 http://togogenome.org/gene/10090:Wipi1 ^@ http://purl.uniprot.org/uniprot/Q8R3E3 ^@ Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Motif|||Region|||Repeat|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||L/FRRG motif|||Nuclear receptor interaction|||WD 1|||WD 2|||WD 3|||WD repeat domain phosphoinositide-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000051438|||http://purl.uniprot.org/annotation/VSP_016967|||http://purl.uniprot.org/annotation/VSP_016968|||http://purl.uniprot.org/annotation/VSP_016969 http://togogenome.org/gene/10090:Gcat ^@ http://purl.uniprot.org/uniprot/E9PWY6|||http://purl.uniprot.org/uniprot/O88986|||http://purl.uniprot.org/uniprot/Q9CZ08 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial|||Aminotransferase class I/classII|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000001247 http://togogenome.org/gene/10090:Slfn2 ^@ http://purl.uniprot.org/uniprot/Q9Z0I6 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Mutagenesis Site ^@ Abolished tRNA-binding.|||In elektra mutation; impaired T-cell quiescence. Mice show elevated susceptibility to bacterial and viral infections and to diminished numbers of T-cells that fail to proliferate in response to infection and diverse proliferative stimuli. T-cells display chronic endoplasmic reticulum (ER) stress under steady state conditions. T-cells also show elevated de novo sterol synthesis.|||Schlafen family member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000457109 http://togogenome.org/gene/10090:Cib3 ^@ http://purl.uniprot.org/uniprot/Q0P523 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Calcium and integrin-binding family member 3|||EF-hand 1|||EF-hand 2|||EF-hand 3 ^@ http://purl.uniprot.org/annotation/PRO_0000425745 http://togogenome.org/gene/10090:Mlkl ^@ http://purl.uniprot.org/uniprot/Q9D2Y4 ^@ Binding Site|||Chain|||Coiled-Coil|||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|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn ^@ Abolishes ATP-binding and induces necroptosis in absence of exogeous stimuli and independently of RIPK3.|||Impaired ability to induce necroptosis.|||Impairs interaction with RIPK3.|||In isoform 2.|||Mimics phosphorylation state and induces necroptosis in absence of exogeous stimuli and independently of RIPK3.e.|||Mixed lineage kinase domain-like protein|||N-terminal bundle and brace (NBB); mediates INSP6 binding|||No effect.|||Phosphoserine|||Phosphoserine; by RIPK3|||Phosphothreonine; by RIPK3|||Protein kinase|||Retains ATP-binding ability and induces necroptosis in absence of exogeous stimuli and independently of RIPK3.|||Retains ATP-binding ability. ^@ http://purl.uniprot.org/annotation/PRO_0000248240|||http://purl.uniprot.org/annotation/VSP_052132 http://togogenome.org/gene/10090:Tshz1 ^@ http://purl.uniprot.org/uniprot/Q5DTH5 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||Disordered|||Homeobox; atypical|||Phosphoserine|||Polar residues|||Teashirt homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000047063 http://togogenome.org/gene/10090:Krt33b ^@ http://purl.uniprot.org/uniprot/Q61897 ^@ 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_0000063690 http://togogenome.org/gene/10090:Ddrgk1 ^@ http://purl.uniprot.org/uniprot/Q80WW9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Signal Peptide|||Strand ^@ Basic and acidic residues|||DDRGK domain-containing protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)|||Mediates interaction with CDK5RAP3|||Mediates interaction with TRIP4|||Mediates interaction with UFL1|||PCI|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000021034 http://togogenome.org/gene/10090:Zfp280c ^@ http://purl.uniprot.org/uniprot/Q6P3Y5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Region|||Splice Variant|||Zinc Finger ^@ 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.|||In isoform 3.|||Polar residues|||Zinc finger protein 280C ^@ http://purl.uniprot.org/annotation/PRO_0000227976|||http://purl.uniprot.org/annotation/VSP_017619|||http://purl.uniprot.org/annotation/VSP_017620|||http://purl.uniprot.org/annotation/VSP_017621 http://togogenome.org/gene/10090:Doc2b ^@ http://purl.uniprot.org/uniprot/P70169 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ C2 1|||C2 2|||Disordered|||Double C2-like domain-containing protein beta|||Loss of interaction with STX4 and insulin-dependent translocation to the cell membrane; when associated with N-157, N-163 and N-297.|||Loss of interaction with STX4 and insulin-dependent translocation to the cell membrane; when associated with N-157, N-163 and N-303.|||Loss of interaction with STX4 and insulin-dependent translocation to the cell membrane; when associated with N-157, N-297 and N-303.|||Loss of interaction with STX4 and insulin-dependent translocation to the cell membrane; when associated with N-163, N-297 and N-303.|||Mediates interaction with DYNLT1|||Mediates interaction with STXBP3|||Negatively regulates targeting to plasma membrane|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000079969 http://togogenome.org/gene/10090:Stil ^@ http://purl.uniprot.org/uniprot/A2AD39|||http://purl.uniprot.org/uniprot/Q60988|||http://purl.uniprot.org/uniprot/Q8BQI9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Abolishes mitotic phosphorylation and decreases mitotic index as well as CDK1 activity; when associated with A-574; A-643; A-656; A-664; A-686 and A-699.|||Abolishes mitotic phosphorylation and decreases mitotic index as well as CDK1 activity; when associated with A-574; A-643; A-656; A-664; A-686 and A-760.|||Abolishes mitotic phosphorylation and decreases mitotic index as well as CDK1 activity; when associated with A-574; A-643; A-656; A-664; A-699 and A-760.|||Abolishes mitotic phosphorylation and decreases mitotic index as well as CDK1 activity; when associated with A-574; A-643; A-656; A-686; A-699 and A-760.|||Abolishes mitotic phosphorylation and decreases mitotic index as well as CDK1 activity; when associated with A-574; A-643; A-664; A-686; A-699 and A-760.|||Abolishes mitotic phosphorylation and decreases mitotic index as well as CDK1 activity; when associated with A-574; A-656; A-664; A-686; A-699 and A-760.|||Abolishes mitotic phosphorylation and decreases mitotic index as well as CDK1 activity; when associated with A-643; A-656; A-664; A-686; A-699 and A-760.|||Basic and acidic residues|||Disordered|||Interaction with CENPJ|||Interaction with RBM14|||PIN1-binding|||Phosphoserine|||Polar residues|||SCL-interrupting locus protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000271333 http://togogenome.org/gene/10090:Calml3 ^@ http://purl.uniprot.org/uniprot/Q9D6P8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Calmodulin-like protein 3|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4 ^@ http://purl.uniprot.org/annotation/PRO_0000284521 http://togogenome.org/gene/10090:Apbb3 ^@ http://purl.uniprot.org/uniprot/Q3UR23|||http://purl.uniprot.org/uniprot/Q8R1C9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Amyloid-beta A4 precursor protein-binding family B member 3|||Disordered|||PID|||PID 1|||PID 2|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000076055 http://togogenome.org/gene/10090:Rasl2-9 ^@ http://purl.uniprot.org/uniprot/Q61820 ^@ Binding Site|||Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ GTP-binding nuclear protein Ran, testis-specific isoform|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000208699 http://togogenome.org/gene/10090:Inpp4b ^@ http://purl.uniprot.org/uniprot/E9PVM1|||http://purl.uniprot.org/uniprot/E9PVM3|||http://purl.uniprot.org/uniprot/Q1A6U9|||http://purl.uniprot.org/uniprot/Q1A6V0|||http://purl.uniprot.org/uniprot/Q1A6V1|||http://purl.uniprot.org/uniprot/Q3URI3|||http://purl.uniprot.org/uniprot/Q6P1Y8 ^@ 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 ^@ Basic and acidic residues|||C2|||Disordered|||Helical|||Type II inositol 3,4-bisphosphate 4-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000190237 http://togogenome.org/gene/10090:Sntb1 ^@ http://purl.uniprot.org/uniprot/Q99L88 ^@ 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 ^@ Beta-1-syntrophin|||Calmodulin-binding|||Disordered|||In isoform 2.|||N-acetylalanine|||PDZ|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Removed|||SU ^@ http://purl.uniprot.org/annotation/PRO_0000184010|||http://purl.uniprot.org/annotation/VSP_006356|||http://purl.uniprot.org/annotation/VSP_006357 http://togogenome.org/gene/10090:Ift52 ^@ http://purl.uniprot.org/uniprot/Q62559 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Helix|||Sequence Conflict|||Strand|||Turn ^@ Intraflagellar transport protein 52 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000084168 http://togogenome.org/gene/10090:Ablim3 ^@ http://purl.uniprot.org/uniprot/Q69ZX8 ^@ 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 ^@ Actin-binding LIM protein 3|||Basic and acidic residues|||Disordered|||HP|||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_0000075703 http://togogenome.org/gene/10090:Elovl3 ^@ http://purl.uniprot.org/uniprot/O35949 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Elongation of very long chain fatty acids protein 3|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000207541 http://togogenome.org/gene/10090:Krtap15 ^@ http://purl.uniprot.org/uniprot/Q9QZU5 ^@ Chain|||Molecule Processing ^@ Chain ^@ Keratin-associated protein 15-1 ^@ http://purl.uniprot.org/annotation/PRO_0000271177 http://togogenome.org/gene/10090:Or13j1 ^@ http://purl.uniprot.org/uniprot/Q9QZ18 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dlx4 ^@ http://purl.uniprot.org/uniprot/P70436 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Region|||Sequence Conflict ^@ Disordered|||Homeobox|||Homeobox protein DLX-4 ^@ http://purl.uniprot.org/annotation/PRO_0000049029 http://togogenome.org/gene/10090:Slc30a7 ^@ http://purl.uniprot.org/uniprot/Q9JKN1 ^@ 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|||Helical|||His-rich loop|||Lumenal|||Zinc transporter 7 ^@ http://purl.uniprot.org/annotation/PRO_0000314300 http://togogenome.org/gene/10090:Map6d1 ^@ http://purl.uniprot.org/uniprot/Q14BB9 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||MAP6 domain-containing protein 1|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000271916 http://togogenome.org/gene/10090:Gm128 ^@ http://purl.uniprot.org/uniprot/G9MDF2|||http://purl.uniprot.org/uniprot/Q569E4 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Protein MENT ^@ http://purl.uniprot.org/annotation/PRO_0000304970|||http://purl.uniprot.org/annotation/PRO_5009956038 http://togogenome.org/gene/10090:Colgalt1 ^@ http://purl.uniprot.org/uniprot/Q8K297 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Procollagen galactosyltransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000309537 http://togogenome.org/gene/10090:Col22a1 ^@ http://purl.uniprot.org/uniprot/A0A2R8W6Z9|||http://purl.uniprot.org/uniprot/E9Q7P1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Pro residues|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5003243106 http://togogenome.org/gene/10090:Sox14 ^@ http://purl.uniprot.org/uniprot/Q04892|||http://purl.uniprot.org/uniprot/Q3UUP3|||http://purl.uniprot.org/uniprot/Q497H4|||http://purl.uniprot.org/uniprot/Q7TNS9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||HMG box|||Transcription factor SOX-14 ^@ http://purl.uniprot.org/annotation/PRO_0000048760 http://togogenome.org/gene/10090:Slc7a14 ^@ http://purl.uniprot.org/uniprot/Q8BXR1 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier family 7 member 14 ^@ http://purl.uniprot.org/annotation/PRO_0000307361 http://togogenome.org/gene/10090:Cfap99 ^@ http://purl.uniprot.org/uniprot/A0A140LIX9 ^@ Coiled-Coil|||Region ^@ Coiled-Coil|||Region ^@ Disordered ^@ http://togogenome.org/gene/10090:B4galnt2 ^@ http://purl.uniprot.org/uniprot/A2A615|||http://purl.uniprot.org/uniprot/Q09199 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Beta-1,4 N-acetylgalactosaminyltransferase 2|||Cytoplasmic|||Glycosyltransferase 2-like|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000059104 http://togogenome.org/gene/10090:1110059E24Rik ^@ http://purl.uniprot.org/uniprot/Q9CQ90 ^@ 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|||Disordered|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||Uncharacterized protein C9orf85 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089721 http://togogenome.org/gene/10090:Dcst1 ^@ http://purl.uniprot.org/uniprot/Q059Y8 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||E3 ubiquitin-protein ligase DCST1|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000278825 http://togogenome.org/gene/10090:Moap1 ^@ http://purl.uniprot.org/uniprot/Q9ERH6 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Motif|||Region|||Sequence Conflict ^@ BH3-like|||LIR|||Modulator of apoptosis 1|||RASSF1-binding ^@ http://purl.uniprot.org/annotation/PRO_0000155207 http://togogenome.org/gene/10090:D11Wsu47e ^@ http://purl.uniprot.org/uniprot/Q6PIX9 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Polar residues|||Uncharacterized protein C17orf80 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000284613|||http://purl.uniprot.org/annotation/VSP_024575 http://togogenome.org/gene/10090:Zbtb42 ^@ http://purl.uniprot.org/uniprot/Q811H0 ^@ 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|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In isoform 2.|||Polar residues|||Zinc finger and BTB domain-containing protein 42 ^@ http://purl.uniprot.org/annotation/PRO_0000391930|||http://purl.uniprot.org/annotation/VSP_038770 http://togogenome.org/gene/10090:Galc ^@ http://purl.uniprot.org/uniprot/P54818 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Galactocerebrosidase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000012232 http://togogenome.org/gene/10090:Ltc4s ^@ http://purl.uniprot.org/uniprot/Q60860|||http://purl.uniprot.org/uniprot/Q8K355 ^@ Active Site|||Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Leukotriene C4 synthase|||Lumenal|||Phosphoserine|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000217749 http://togogenome.org/gene/10090:Npr3 ^@ http://purl.uniprot.org/uniprot/A0A2I3BPR9|||http://purl.uniprot.org/uniprot/P70180|||http://purl.uniprot.org/uniprot/Q7TMG7 ^@ 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 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Atrial natriuretic peptide receptor 3|||Cytoplasmic|||Extracellular|||Helical|||In Lgj-2J.|||In Lgj.|||Interchain|||N-linked (GlcNAc...) asparagine|||Receptor ligand binding region ^@ http://purl.uniprot.org/annotation/PRO_0000012371|||http://purl.uniprot.org/annotation/PRO_0000012372|||http://purl.uniprot.org/annotation/PRO_5015098851 http://togogenome.org/gene/10090:Cox14 ^@ http://purl.uniprot.org/uniprot/Q8BH51 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytochrome c oxidase assembly protein COX14|||Cytoplasmic|||Helical|||Mitochondrial intermembrane ^@ http://purl.uniprot.org/annotation/PRO_0000263678 http://togogenome.org/gene/10090:Srsf5 ^@ http://purl.uniprot.org/uniprot/O35326|||http://purl.uniprot.org/uniprot/Q9D8S5 ^@ 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 residues|||Disordered|||N6-acetyllysine|||Phosphoserine|||Polar residues|||RRM|||RRM 1|||RRM 2|||Serine/arginine-rich splicing factor 5 ^@ http://purl.uniprot.org/annotation/PRO_0000081928 http://togogenome.org/gene/10090:Ankrd37 ^@ http://purl.uniprot.org/uniprot/Q569N2 ^@ Chain|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Motif|||Repeat ^@ ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat domain-containing protein 37|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000244362 http://togogenome.org/gene/10090:Gh ^@ http://purl.uniprot.org/uniprot/A0A0M6L0K7|||http://purl.uniprot.org/uniprot/P06880 ^@ Binding Site|||Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Signal Peptide ^@ Phosphoserine|||Somatotropin ^@ http://purl.uniprot.org/annotation/PRO_0000032992|||http://purl.uniprot.org/annotation/PRO_5014234056 http://togogenome.org/gene/10090:Bbs1 ^@ http://purl.uniprot.org/uniprot/Q3V3N7 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site ^@ Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site ^@ Bardet-Biedl syndrome 1 protein homolog|||Knockin mice exhibit olfaction deficits, male infertility, ventriculomegaly, retinopathy and obesity.|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000441016 http://togogenome.org/gene/10090:Tfb2m ^@ http://purl.uniprot.org/uniprot/B2RSE6|||http://purl.uniprot.org/uniprot/Q3TL26 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Transit Peptide ^@ DNA-binding|||Dimethyladenosine transferase 2, mitochondrial|||Disordered|||Mitochondrion|||Ribosomal RNA adenine methylase transferase N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000273180 http://togogenome.org/gene/10090:Zfp947 ^@ http://purl.uniprot.org/uniprot/Q8BIQ6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:1700011L22Rik ^@ http://purl.uniprot.org/uniprot/Q9DAF8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Uncharacterized protein C4orf51 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000392539 http://togogenome.org/gene/10090:Ikzf2 ^@ http://purl.uniprot.org/uniprot/A0A087WNY4|||http://purl.uniprot.org/uniprot/P81183 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform A.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Zinc finger protein Helios ^@ http://purl.uniprot.org/annotation/PRO_0000047093|||http://purl.uniprot.org/annotation/VSP_006846 http://togogenome.org/gene/10090:Eya4 ^@ http://purl.uniprot.org/uniprot/A0A1W2P721|||http://purl.uniprot.org/uniprot/Q8BY78|||http://purl.uniprot.org/uniprot/Q9Z191 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Eyes absent homolog 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Nucleophile|||Phosphoserine|||Polar residues|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000218652 http://togogenome.org/gene/10090:Naip6 ^@ http://purl.uniprot.org/uniprot/Q9JIB6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ BIR 1|||BIR 2|||BIR 3|||Baculoviral IAP repeat-containing protein 1f|||NACHT ^@ http://purl.uniprot.org/annotation/PRO_0000122345 http://togogenome.org/gene/10090:Tmcc3 ^@ http://purl.uniprot.org/uniprot/Q8R310 ^@ 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|||Polar residues|||Transmembrane and coiled-coil domain protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000184600|||http://purl.uniprot.org/annotation/VSP_025999 http://togogenome.org/gene/10090:Brd8 ^@ http://purl.uniprot.org/uniprot/D3YZC7|||http://purl.uniprot.org/uniprot/Q8R3B7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Bromo|||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|||In isoform 2.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000211186|||http://purl.uniprot.org/annotation/VSP_038218 http://togogenome.org/gene/10090:Polr2f ^@ http://purl.uniprot.org/uniprot/P61219 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ Acidic residues|||DNA-directed RNA polymerases I, II, and III subunit RPABC2|||Disordered|||N-acetylserine|||Phosphoserine; by CK2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000133800 http://togogenome.org/gene/10090:Or2y3 ^@ http://purl.uniprot.org/uniprot/Q8VGC8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ldlrad4 ^@ http://purl.uniprot.org/uniprot/Q4VAH9|||http://purl.uniprot.org/uniprot/Q8BWJ4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||LDL-receptor class A|||Low-density lipoprotein receptor class A domain-containing protein 4|||Lumenal|||PPxY motif 1|||PPxY motif 2|||Polar residues|||SMAD interaction motif (SIM) ^@ http://purl.uniprot.org/annotation/PRO_0000185445 http://togogenome.org/gene/10090:Glra2 ^@ http://purl.uniprot.org/uniprot/Q3UTL8|||http://purl.uniprot.org/uniprot/Q7TNC8 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Glycine receptor subunit alpha-2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Important for obstruction of the ion pore in the closed conformation|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000417|||http://purl.uniprot.org/annotation/PRO_5022248775 http://togogenome.org/gene/10090:Rbl2 ^@ http://purl.uniprot.org/uniprot/A0A1B0GR06|||http://purl.uniprot.org/uniprot/A0A1B0GRM0|||http://purl.uniprot.org/uniprot/Q64700 ^@ 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 ^@ Cyclin-like|||Disordered|||Domain A|||Domain B|||Phosphoserine|||Phosphothreonine|||Pocket; binds E1A|||Polar residues|||Pro residues|||Retinoblastoma-associated protein A-box|||Retinoblastoma-associated protein C-terminal|||Retinoblastoma-associated protein N-terminal|||Retinoblastoma-like protein 2|||Spacer ^@ http://purl.uniprot.org/annotation/PRO_0000167842 http://togogenome.org/gene/10090:Gtf3c1 ^@ http://purl.uniprot.org/uniprot/Q8K284 ^@ 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|||General transcription factor 3C polypeptide 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000209711|||http://purl.uniprot.org/annotation/VSP_010573|||http://purl.uniprot.org/annotation/VSP_010574|||http://purl.uniprot.org/annotation/VSP_010575|||http://purl.uniprot.org/annotation/VSP_010576 http://togogenome.org/gene/10090:Serf2 ^@ http://purl.uniprot.org/uniprot/A2ARQ4|||http://purl.uniprot.org/uniprot/P84102 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Small EDRK-rich factor 2|||Small EDRK-rich factor-like N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000050713 http://togogenome.org/gene/10090:Vmn1r203 ^@ http://purl.uniprot.org/uniprot/Q8R273 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp712 ^@ http://purl.uniprot.org/uniprot/E9PXJ4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dock8 ^@ http://purl.uniprot.org/uniprot/Q8C147 ^@ 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 ^@ C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 8|||Disordered|||In an experimental autoimmune encephalomyelitis (EAE) disease model, 50 percent of animals have no EAE symptoms. In the remaining animals, EAE is less severe with a reduction in the demyelination of the spinal cord and in the number of CD4(+) T-cells infiltrating the central nervous system. In addition, CD4(+) T-cell proliferation and apoptosis are increased. Reduced CD4(+) T-cell transmigration towards chemokine CXCL12 and CCL5.|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000189998|||http://purl.uniprot.org/annotation/VSP_027374|||http://purl.uniprot.org/annotation/VSP_027375|||http://purl.uniprot.org/annotation/VSP_027376 http://togogenome.org/gene/10090:Tox3 ^@ http://purl.uniprot.org/uniprot/Q80W03 ^@ 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|||HMG box|||Polar residues|||TOX high mobility group box family member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000286354 http://togogenome.org/gene/10090:Cnbp ^@ http://purl.uniprot.org/uniprot/P53996|||http://purl.uniprot.org/uniprot/Q3U5V2|||http://purl.uniprot.org/uniprot/Q3U935|||http://purl.uniprot.org/uniprot/Q3ULK8|||http://purl.uniprot.org/uniprot/Q5QJQ9 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified 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 and isoform 3.|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; by PRMT1|||Phosphoserine|||RNA-binding Arg/Gly-rich region (RGG-box)|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089966|||http://purl.uniprot.org/annotation/VSP_010983|||http://purl.uniprot.org/annotation/VSP_010984 http://togogenome.org/gene/10090:Serpinb9 ^@ http://purl.uniprot.org/uniprot/O08797 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Steep1 ^@ http://purl.uniprot.org/uniprot/Q8VDP2 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||STING ER exit protein ^@ http://purl.uniprot.org/annotation/PRO_0000287610|||http://purl.uniprot.org/annotation/VSP_025569 http://togogenome.org/gene/10090:Or10w1 ^@ http://purl.uniprot.org/uniprot/Q7TQQ5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dcpp1 ^@ http://purl.uniprot.org/uniprot/L7N1X9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Jacalin-type lectin ^@ http://purl.uniprot.org/annotation/PRO_5003982279 http://togogenome.org/gene/10090:F12 ^@ http://purl.uniprot.org/uniprot/Q80YC5 ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Coagulation factor XIIa heavy chain|||Coagulation factor XIIa light chain|||Disordered|||EGF-like 1|||EGF-like 2|||Fibronectin type-I|||Fibronectin type-II|||Kringle|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc) threonine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Peptidase S1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000394555|||http://purl.uniprot.org/annotation/PRO_0000394556 http://togogenome.org/gene/10090:Cpa5 ^@ http://purl.uniprot.org/uniprot/B2RQW9|||http://purl.uniprot.org/uniprot/Q8R4H4 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Signal Peptide ^@ Activation peptide|||Carboxypeptidase A5|||Peptidase M14 carboxypeptidase A|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004363|||http://purl.uniprot.org/annotation/PRO_0000004364 http://togogenome.org/gene/10090:Mucl3 ^@ http://purl.uniprot.org/uniprot/Q3TNW5 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Mucin-like protein 3|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000318687 http://togogenome.org/gene/10090:Klhl30 ^@ http://purl.uniprot.org/uniprot/Q8C3F7 ^@ 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 30 ^@ http://purl.uniprot.org/annotation/PRO_0000274595 http://togogenome.org/gene/10090:Desi1 ^@ http://purl.uniprot.org/uniprot/Q9CQT7 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Strand|||Turn ^@ Desumoylating isopeptidase 1|||Nuclear export signal 1|||Nuclear export signal 2|||PPPDE ^@ http://purl.uniprot.org/annotation/PRO_0000318151 http://togogenome.org/gene/10090:Or5m11 ^@ http://purl.uniprot.org/uniprot/Q7TR89 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pip4k2c ^@ http://purl.uniprot.org/uniprot/Q91XU3 ^@ 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 ^@ N-acetylalanine|||PIPK|||Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma|||Phosphoserine|||Removed|||Required for interaction with PIP5K1A ^@ http://purl.uniprot.org/annotation/PRO_0000285751 http://togogenome.org/gene/10090:Or5an10 ^@ http://purl.uniprot.org/uniprot/A0PK57 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tox2 ^@ http://purl.uniprot.org/uniprot/E9Q0B9 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||HMG box|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:H1f3 ^@ http://purl.uniprot.org/uniprot/P43277|||http://purl.uniprot.org/uniprot/Q149Z9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.3|||N-acetylserine|||N6-(beta-hydroxybutyryl)lysine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000195916 http://togogenome.org/gene/10090:Rmnd5b ^@ http://purl.uniprot.org/uniprot/Q91YQ7 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Zinc Finger ^@ CTLH|||E3 ubiquitin-protein transferase RMND5B|||LisH|||N-acetylmethionine|||RING-Gid-type ^@ http://purl.uniprot.org/annotation/PRO_0000065710 http://togogenome.org/gene/10090:Arl10 ^@ http://purl.uniprot.org/uniprot/Q9QXJ4 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ ADP-ribosylation factor-like protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000207477 http://togogenome.org/gene/10090:Fgf6 ^@ http://purl.uniprot.org/uniprot/P21658|||http://purl.uniprot.org/uniprot/Q8C399 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Non-terminal Residue|||Signal Peptide ^@ Fibroblast growth factor|||Fibroblast growth factor 6|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000008962|||http://purl.uniprot.org/annotation/PRO_5005144434 http://togogenome.org/gene/10090:Fat4 ^@ http://purl.uniprot.org/uniprot/Q2PZL6 ^@ 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|||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 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5|||EGF-like 6|||Extracellular|||Helical|||In isoform 2.|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Necessary and sufficient for interaction with MPDZ|||Phosphoserine|||Polar residues|||Protocadherin Fat 4 ^@ http://purl.uniprot.org/annotation/PRO_0000324638|||http://purl.uniprot.org/annotation/VSP_032339|||http://purl.uniprot.org/annotation/VSP_032340 http://togogenome.org/gene/10090:Gm20906 ^@ http://purl.uniprot.org/uniprot/A0A087WRK1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Lypla2 ^@ http://purl.uniprot.org/uniprot/Q9WTL7 ^@ Active Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Chain|||Lipid Binding|||Modified Residue ^@ Acyl-protein thioesterase 2|||Charge relay system|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000102272 http://togogenome.org/gene/10090:Cnih3 ^@ http://purl.uniprot.org/uniprot/G3XA11|||http://purl.uniprot.org/uniprot/Q6ZWS4|||http://purl.uniprot.org/uniprot/Q9D6E1 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Topological Domain|||Transmembrane ^@ Chain|||Helix|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Protein cornichon homolog 3 ^@ http://purl.uniprot.org/annotation/PRO_0000122229 http://togogenome.org/gene/10090:Vmn1r245 ^@ http://purl.uniprot.org/uniprot/K9J7G9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Anks4b ^@ http://purl.uniprot.org/uniprot/Q8K3X6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn ^@ ANK 1|||ANK 2|||ANK 3|||Acidic residues|||Ankyrin repeat and SAM domain-containing protein 4B|||Disordered|||Mediates interaction with MYO7B|||Mediates localization to microvilli|||PDZ-binding; mediates interaction with USH1C|||Polar residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000066997 http://togogenome.org/gene/10090:Tmem242 ^@ http://purl.uniprot.org/uniprot/Q8VCR3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylmethionine|||Transmembrane protein 242 ^@ http://purl.uniprot.org/annotation/PRO_0000295849|||http://purl.uniprot.org/annotation/VSP_027110|||http://purl.uniprot.org/annotation/VSP_027111|||http://purl.uniprot.org/annotation/VSP_027112 http://togogenome.org/gene/10090:Mapk11 ^@ http://purl.uniprot.org/uniprot/Q9WUI1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||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_0000186281 http://togogenome.org/gene/10090:Mark4 ^@ http://purl.uniprot.org/uniprot/Q8CIP4 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||KA1|||MAP/microtubule affinity-regulating kinase 4|||Phosphoserine|||Phosphothreonine; by LKB1|||Polar residues|||Protein kinase|||Proton acceptor|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000086308|||http://purl.uniprot.org/annotation/VSP_058199 http://togogenome.org/gene/10090:Mup17 ^@ http://purl.uniprot.org/uniprot/B5X0G2 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Major urinary protein 17 ^@ http://purl.uniprot.org/annotation/PRO_0000415145 http://togogenome.org/gene/10090:Arl4c ^@ http://purl.uniprot.org/uniprot/P61208 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding ^@ ADP-ribosylation factor-like protein 4C|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000207463 http://togogenome.org/gene/10090:Gstt1 ^@ http://purl.uniprot.org/uniprot/Q64471|||http://purl.uniprot.org/uniprot/Q9DCY6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase theta-1|||Strongly reduced catalytic activity. ^@ http://purl.uniprot.org/annotation/PRO_0000185940 http://togogenome.org/gene/10090:Tmem144 ^@ http://purl.uniprot.org/uniprot/Q8VEH0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 144 ^@ http://purl.uniprot.org/annotation/PRO_0000288972 http://togogenome.org/gene/10090:Rit1 ^@ http://purl.uniprot.org/uniprot/P70426 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ GTP-binding protein Rit1 ^@ http://purl.uniprot.org/annotation/PRO_0000082726 http://togogenome.org/gene/10090:2610318N02Rik ^@ http://purl.uniprot.org/uniprot/Q80VT5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gucy2d ^@ http://purl.uniprot.org/uniprot/A0A0U1RPR8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Guanylate cyclase|||Guanylate cyclase D|||Helical|||Interaction with NCALD|||Interchain|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000448832 http://togogenome.org/gene/10090:Serpina12 ^@ http://purl.uniprot.org/uniprot/Q7TMF5 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage|||N-linked (GlcNAc...) asparagine|||Reactive center loop|||Serpin A12 ^@ http://purl.uniprot.org/annotation/PRO_0000041977 http://togogenome.org/gene/10090:Zyg11b ^@ http://purl.uniprot.org/uniprot/Q3UFS0 ^@ 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.|||LRR 1|||LRR 2|||LRR 3|||Protein zyg-11 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000305088|||http://purl.uniprot.org/annotation/VSP_028225|||http://purl.uniprot.org/annotation/VSP_028226|||http://purl.uniprot.org/annotation/VSP_028227|||http://purl.uniprot.org/annotation/VSP_028228 http://togogenome.org/gene/10090:Dusp22 ^@ http://purl.uniprot.org/uniprot/Q99N11 ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Splice Variant ^@ Dual specificity protein phosphatase 22|||In isoform 2.|||N-myristoyl glycine|||Phosphocysteine intermediate|||Removed|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000244752|||http://purl.uniprot.org/annotation/VSP_019615 http://togogenome.org/gene/10090:H3c6 ^@ http://purl.uniprot.org/uniprot/B9EI85|||http://purl.uniprot.org/uniprot/P84228 ^@ Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||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 H2A/H2B/H3|||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; 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_0000221250 http://togogenome.org/gene/10090:Myl7 ^@ http://purl.uniprot.org/uniprot/Q5SVI8|||http://purl.uniprot.org/uniprot/Q9QVP4 ^@ 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|||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_0000198726 http://togogenome.org/gene/10090:Afdn ^@ http://purl.uniprot.org/uniprot/E9Q9C3|||http://purl.uniprot.org/uniprot/Q9QZQ1 ^@ 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|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Afadin|||Basic and acidic residues|||Dilute|||Disordered|||FHA|||In isoform 1.|||N6-acetyllysine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Ras-associating|||Ras-associating 1|||Ras-associating 2 ^@ http://purl.uniprot.org/annotation/PRO_0000215919|||http://purl.uniprot.org/annotation/VSP_026731 http://togogenome.org/gene/10090:Osm ^@ http://purl.uniprot.org/uniprot/P53347 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Oncostatin-M ^@ http://purl.uniprot.org/annotation/PRO_0000017722|||http://purl.uniprot.org/annotation/PRO_0000408764 http://togogenome.org/gene/10090:Hjurp ^@ http://purl.uniprot.org/uniprot/E9Q4T0|||http://purl.uniprot.org/uniprot/E9QKG8|||http://purl.uniprot.org/uniprot/Q6PG16 ^@ 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)|||Holliday junction recognition protein|||Holliday junction recognition protein HJURP central|||Holliday junction regulator protein family C-terminal|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000378154|||http://purl.uniprot.org/annotation/VSP_037515|||http://purl.uniprot.org/annotation/VSP_037516 http://togogenome.org/gene/10090:Jkamp ^@ http://purl.uniprot.org/uniprot/Q8BI36 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform 2.|||JNK1/MAPK8-associated membrane protein|||Loss of glycosylation.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000089904|||http://purl.uniprot.org/annotation/VSP_008813 http://togogenome.org/gene/10090:Fchsd1 ^@ http://purl.uniprot.org/uniprot/Q6PFY1 ^@ 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 ^@ Disordered|||F-BAR|||F-BAR and double SH3 domains protein 1|||In isoform 2.|||Phosphoserine|||Pro residues|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000278213|||http://purl.uniprot.org/annotation/VSP_023166 http://togogenome.org/gene/10090:Larp7 ^@ http://purl.uniprot.org/uniprot/Q05CL8 ^@ 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)|||HTH La-type RNA-binding|||In isoform 2.|||La-related protein 7|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||Reduced binding to U6 snRNA without affecting binding to 7SKRNA. Reduced 2'-O-methylation of U6 snRNAs.|||xRRM ^@ http://purl.uniprot.org/annotation/PRO_0000281144|||http://purl.uniprot.org/annotation/VSP_024022|||http://purl.uniprot.org/annotation/VSP_024023 http://togogenome.org/gene/10090:Sipa1l1 ^@ http://purl.uniprot.org/uniprot/Q8C0T5 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In isoform 2.|||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_0000056747|||http://purl.uniprot.org/annotation/VSP_010918|||http://purl.uniprot.org/annotation/VSP_010919 http://togogenome.org/gene/10090:Popdc2 ^@ http://purl.uniprot.org/uniprot/Q6P3F7|||http://purl.uniprot.org/uniprot/Q9ES82 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Transmembrane ^@ Almost abolishes cAMP-binding.|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues|||Popeye domain-containing protein 2|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000046794 http://togogenome.org/gene/10090:Or10ag57 ^@ http://purl.uniprot.org/uniprot/Q8VGT9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdc14b ^@ http://purl.uniprot.org/uniprot/Q6PFY9 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ A|||B|||Disordered|||Dual specificity protein phosphatase CDC14B|||In isoform 2.|||Linker|||Nucleolar localization signal|||Phosphocysteine intermediate|||Polar residues|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094879|||http://purl.uniprot.org/annotation/VSP_012325 http://togogenome.org/gene/10090:Ovgp1 ^@ http://purl.uniprot.org/uniprot/Q54AJ4|||http://purl.uniprot.org/uniprot/Q62010 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide ^@ 1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||21 X 7 AA tandem repeats of S-K-[TAI]-[TI]-[TAP]-[GED]-[IVM]|||3|||4|||5|||6|||7|||8|||9|||Disordered|||GH18|||N-linked (GlcNAc...) asparagine|||Oviduct-specific glycoprotein ^@ http://purl.uniprot.org/annotation/PRO_0000011975|||http://purl.uniprot.org/annotation/PRO_5010139401 http://togogenome.org/gene/10090:Rab8b ^@ http://purl.uniprot.org/uniprot/P61028 ^@ 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|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-8B|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121135|||http://purl.uniprot.org/annotation/PRO_0000370801 http://togogenome.org/gene/10090:Ireb2 ^@ http://purl.uniprot.org/uniprot/Q811J3 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Iron-responsive element-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000076685 http://togogenome.org/gene/10090:Or5l13 ^@ http://purl.uniprot.org/uniprot/A2AVC3|||http://purl.uniprot.org/uniprot/Q8VG81 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dhx57 ^@ http://purl.uniprot.org/uniprot/Q6P5D3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Putative ATP-dependent RNA helicase DHX57|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000233152|||http://purl.uniprot.org/annotation/VSP_018061|||http://purl.uniprot.org/annotation/VSP_018062|||http://purl.uniprot.org/annotation/VSP_018063|||http://purl.uniprot.org/annotation/VSP_018064|||http://purl.uniprot.org/annotation/VSP_018065|||http://purl.uniprot.org/annotation/VSP_018066 http://togogenome.org/gene/10090:Cir1 ^@ http://purl.uniprot.org/uniprot/Q9DA19 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ 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_0000247985|||http://purl.uniprot.org/annotation/VSP_020093 http://togogenome.org/gene/10090:Mdn1 ^@ http://purl.uniprot.org/uniprot/A2ANY6|||http://purl.uniprot.org/uniprot/J3QMC5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||VWFA ^@ http://togogenome.org/gene/10090:Gm4513 ^@ http://purl.uniprot.org/uniprot/A0A140LJ87 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Csmd3 ^@ http://purl.uniprot.org/uniprot/Q80T79 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||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|||Helical|||In isoform 2.|||In isoform 3.|||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_0000079406|||http://purl.uniprot.org/annotation/VSP_009053|||http://purl.uniprot.org/annotation/VSP_009054|||http://purl.uniprot.org/annotation/VSP_009055|||http://purl.uniprot.org/annotation/VSP_009056|||http://purl.uniprot.org/annotation/VSP_027009 http://togogenome.org/gene/10090:Foxj1 ^@ http://purl.uniprot.org/uniprot/Q61660|||http://purl.uniprot.org/uniprot/Q640Q8 ^@ 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 ^@ Disordered|||Fork-head|||Forkhead box protein J1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000091851 http://togogenome.org/gene/10090:Xkr8 ^@ http://purl.uniprot.org/uniprot/Q8C0T0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Mutagenesis Site|||Site|||Topological Domain|||Transmembrane ^@ Abolished ability to promote phosphatidylserine exposure.|||Abolished ability to promote phosphatidylserine exposure. Promotes localization to the cytoplasm.|||Cleavage; by caspase-3|||Cytoplasmic|||Decreased phosphorylation; does not affect the phospholipid scramblase activity.|||Decreased phosphorylation; impairs the phospholipid scramblase activity.|||Does not affect ability to promote phosphatidylserine exposure.|||Extracellular|||Helical|||In 2DA mutant; abolished cleavage by CASP3 and ability to promote phosphatidylserine exposure.|||Mimics phosphorylation status; activation of the phospholipid scramblase activity.|||Mimics phosphorylation status; does not affect the phospholipid scramblase activity.|||Phosphoserine|||Phosphothreonine|||XK-related protein 8|||XK-related protein 8, processed form ^@ http://purl.uniprot.org/annotation/PRO_0000415854|||http://purl.uniprot.org/annotation/PRO_0000423985 http://togogenome.org/gene/10090:Vmn1r91 ^@ http://purl.uniprot.org/uniprot/E9PZR7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ndufv3 ^@ http://purl.uniprot.org/uniprot/Q3U422|||http://purl.uniprot.org/uniprot/Q8BK30 ^@ Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Strand|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||Mitochondrion|||NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000251883 http://togogenome.org/gene/10090:Ccr8 ^@ http://purl.uniprot.org/uniprot/P56484|||http://purl.uniprot.org/uniprot/Q3ZB17 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ C-C chemokine receptor type 8|||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_0000069290 http://togogenome.org/gene/10090:Slc47a2 ^@ http://purl.uniprot.org/uniprot/Q3V050 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Multidrug and toxin extrusion protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000312852 http://togogenome.org/gene/10090:Actl11 ^@ http://purl.uniprot.org/uniprot/Q9D5V1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Tfec ^@ http://purl.uniprot.org/uniprot/Q9WTW4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Necessary for transcriptional transactivation|||Transcription factor EC|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000313565 http://togogenome.org/gene/10090:Mertk ^@ http://purl.uniprot.org/uniprot/Q60805 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Loss of GRB2 binding.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase Mer ^@ http://purl.uniprot.org/annotation/PRO_0000024444 http://togogenome.org/gene/10090:Msln ^@ http://purl.uniprot.org/uniprot/Q61468 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated serine|||Megakaryocyte-potentiating factor|||Mesothelin|||Mesothelin, cleaved form|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000253562|||http://purl.uniprot.org/annotation/PRO_0000253563|||http://purl.uniprot.org/annotation/PRO_0000253564|||http://purl.uniprot.org/annotation/PRO_0000253565 http://togogenome.org/gene/10090:Gpx1 ^@ http://purl.uniprot.org/uniprot/P11352 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Non standard residue|||Site ^@ Active Site|||Chain|||Modified Residue|||Non standard residue|||Site ^@ Glutathione peroxidase 1|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Selenocysteine|||Subject to oxidation and hydroselenide loss to dehydroalanine ^@ http://purl.uniprot.org/annotation/PRO_0000066613 http://togogenome.org/gene/10090:H2ax ^@ http://purl.uniprot.org/uniprot/P27661 ^@ Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Complete loss of ubiquitination and increased radiosensitivity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Histone H2AX|||Increased genomic instability and radiosensitivity; when associated with A-137. Reduced homologous recombination. No effect on Lys-40 acetylation. Further increase in radiosensitivity; when associated with R-37.|||Increased genomic instability and radiosensitivity; when associated with A-140.|||Increased radiosensitivity. No effect on phosphorylation after DNA damage. No effect on Ser-140 phosphorylation, nor on TP53BP1 recruitment to DNA double-strand breaks.|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; by CREBBP and EP300|||N6-lactoyllysine; alternate|||No effect on phosphorylation after DNA damage, but increased radiosensitivity. Further increase in radiosensitivity; when associated with A-140.|||No effect on radiosensitivity; when associated with A-10, A-14 and A-16.|||No effect on radiosensitivity; when associated with A-6, A-10 and A-14.|||No effect on radiosensitivity; when associated with A-6, A-10 and A-16.|||No effect on radiosensitivity; when associated with A-6, A-14 and A-16.|||Phosphoserine|||Phosphoserine; by ATM, ATR and PRKDC|||Phosphotyrosine; by WSTF|||Removed|||[ST]-Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000055243 http://togogenome.org/gene/10090:Cylc1 ^@ http://purl.uniprot.org/uniprot/Q9CUM9 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Cylicin N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Sdr16c6 ^@ http://purl.uniprot.org/uniprot/Q05A13 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Proton acceptor|||Short-chain dehydrogenase/reductase family 16C member 6 ^@ http://purl.uniprot.org/annotation/PRO_0000386458 http://togogenome.org/gene/10090:Gpr18 ^@ http://purl.uniprot.org/uniprot/Q8K1Z6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||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-arachidonyl glycine receptor|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000278174 http://togogenome.org/gene/10090:Taar6 ^@ http://purl.uniprot.org/uniprot/Q5QD13 ^@ 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|||Trace amine-associated receptor 6 ^@ http://purl.uniprot.org/annotation/PRO_0000070159 http://togogenome.org/gene/10090:Klhl14 ^@ http://purl.uniprot.org/uniprot/Q69ZK5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ BACK|||BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 14|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000409552 http://togogenome.org/gene/10090:Ptrhd1 ^@ http://purl.uniprot.org/uniprot/D3Z4S3 ^@ Chain|||Molecule Processing ^@ Chain ^@ Putative peptidyl-tRNA hydrolase PTRHD1 ^@ http://purl.uniprot.org/annotation/PRO_0000412069 http://togogenome.org/gene/10090:Mrpl24 ^@ http://purl.uniprot.org/uniprot/Q9CQ06 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ KOW|||Large ribosomal subunit protein uL24m|||Mitochondrion|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000270489 http://togogenome.org/gene/10090:Ang2 ^@ http://purl.uniprot.org/uniprot/Q64438|||http://purl.uniprot.org/uniprot/W0UV59 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Angiogenin-2|||Critical for catalytic activity|||Nucleolar localization signal|||Proton acceptor|||Proton donor|||Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_0000030858|||http://purl.uniprot.org/annotation/PRO_5007751492 http://togogenome.org/gene/10090:Pomk ^@ http://purl.uniprot.org/uniprot/Q3TUA9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein O-mannose kinase|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000262998 http://togogenome.org/gene/10090:Rpp40 ^@ http://purl.uniprot.org/uniprot/Q8R1F9 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Ribonuclease P protein subunit p40 ^@ http://purl.uniprot.org/annotation/PRO_0000354076 http://togogenome.org/gene/10090:Bltp3b ^@ http://purl.uniprot.org/uniprot/A2RSJ4|||http://purl.uniprot.org/uniprot/Q9D574 ^@ 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 ^@ Bridge-like lipid transfer protein family member 3B|||Chorein N-terminal|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295720 http://togogenome.org/gene/10090:Fat1 ^@ http://purl.uniprot.org/uniprot/A0A087WRT4|||http://purl.uniprot.org/uniprot/A0A1L1SQU7|||http://purl.uniprot.org/uniprot/F2Z4A3 ^@ 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 ^@ Cadherin|||Disordered|||EGF-like|||Helical|||Laminin G|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5008198974|||http://purl.uniprot.org/annotation/PRO_5009681955|||http://purl.uniprot.org/annotation/PRO_5015091000 http://togogenome.org/gene/10090:Fgf12 ^@ http://purl.uniprot.org/uniprot/A0A338P752|||http://purl.uniprot.org/uniprot/A0A7U3JW65|||http://purl.uniprot.org/uniprot/P61329|||http://purl.uniprot.org/uniprot/Q3UFZ2 ^@ 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|||Bipartite nuclear localization signal|||Disordered|||Fibroblast growth factor 12|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000147605|||http://purl.uniprot.org/annotation/VSP_010223 http://togogenome.org/gene/10090:Ptdss1 ^@ http://purl.uniprot.org/uniprot/Q99LH2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Basic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylalanine|||Phosphatidylserine synthase 1|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056830 http://togogenome.org/gene/10090:Rab12 ^@ http://purl.uniprot.org/uniprot/P35283 ^@ 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 ^@ Disordered|||Effector region|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by LRRK2|||Probable constitutively active mutant unable to hydrolyze GTP; increases degradation of the transferrin receptor.|||Ras-related protein Rab-12|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121180 http://togogenome.org/gene/10090:Plxdc1 ^@ http://purl.uniprot.org/uniprot/Q91ZV7 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Plexin domain-containing protein 1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000232752|||http://purl.uniprot.org/annotation/VSP_017975 http://togogenome.org/gene/10090:Mapk14 ^@ http://purl.uniprot.org/uniprot/P47811|||http://purl.uniprot.org/uniprot/Q5U421 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitogen-activated protein kinase 14|||N-acetylserine|||N6-acetyllysine|||Phosphorylation blocked.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis|||Phosphotyrosine|||Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis|||Phosphotyrosine; by ZAP70|||Protein kinase|||Proton acceptor|||Removed|||TXY ^@ http://purl.uniprot.org/annotation/PRO_0000186292|||http://purl.uniprot.org/annotation/VSP_004846|||http://purl.uniprot.org/annotation/VSP_007544|||http://purl.uniprot.org/annotation/VSP_007545|||http://purl.uniprot.org/annotation/VSP_022359 http://togogenome.org/gene/10090:Tmprss12 ^@ http://purl.uniprot.org/uniprot/Q3V0Q7 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Charge relay system|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Transmembrane protease serine 12 ^@ http://purl.uniprot.org/annotation/PRO_0000290439 http://togogenome.org/gene/10090:Plcz1 ^@ http://purl.uniprot.org/uniprot/Q8K4D7 ^@ 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|||Sequence Conflict|||Splice Variant ^@ 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1|||Abolishes nuclear translocation.|||Abolishes nuclear translocation. Prolongs Ca(2+) oscillations allowing them to occur during interphase.|||C2|||Defective in Ca(2+) oscillation activity and loss of nuclear translocation.|||Defective in Ca(2+) oscillation activity and shows slower nuclear translocation.|||EF-hand|||In isoform 2.|||PI-PLC X-box|||PI-PLC Y-box ^@ http://purl.uniprot.org/annotation/PRO_0000347246|||http://purl.uniprot.org/annotation/VSP_052863 http://togogenome.org/gene/10090:Or52n5 ^@ http://purl.uniprot.org/uniprot/Q8VGU9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Card10 ^@ http://purl.uniprot.org/uniprot/E9PUV9|||http://purl.uniprot.org/uniprot/P58660 ^@ 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 ^@ CARD|||Caspase recruitment domain-containing protein 10|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000144085 http://togogenome.org/gene/10090:Fahd2a ^@ http://purl.uniprot.org/uniprot/A0A0R4J094|||http://purl.uniprot.org/uniprot/Q3TC72 ^@ 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 ^@ Fumarylacetoacetase-like C-terminal|||Fumarylacetoacetate hydrolase domain-containing protein 2A|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000289797 http://togogenome.org/gene/10090:Rarres2 ^@ http://purl.uniprot.org/uniprot/A0A0N4SVV4|||http://purl.uniprot.org/uniprot/Q9DD06 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide ^@ Chain|||Disulfide Bond|||Propeptide|||Sequence Variant|||Signal Peptide ^@ In strain: FVB/N.|||Retinoic acid receptor responder protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000022530|||http://purl.uniprot.org/annotation/PRO_0000424871|||http://purl.uniprot.org/annotation/PRO_5015043362 http://togogenome.org/gene/10090:Timm13 ^@ http://purl.uniprot.org/uniprot/P62075 ^@ 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_0000193624 http://togogenome.org/gene/10090:Vmn1r1 ^@ http://purl.uniprot.org/uniprot/E9PVR6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ct45a ^@ http://purl.uniprot.org/uniprot/Q3UJ22 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||INTS6/SAGE1/DDX26B/CT45 C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Abcc12 ^@ http://purl.uniprot.org/uniprot/Q80WJ6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||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.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000253579|||http://purl.uniprot.org/annotation/VSP_021093|||http://purl.uniprot.org/annotation/VSP_021094|||http://purl.uniprot.org/annotation/VSP_021095|||http://purl.uniprot.org/annotation/VSP_021096|||http://purl.uniprot.org/annotation/VSP_021097|||http://purl.uniprot.org/annotation/VSP_021098 http://togogenome.org/gene/10090:Cyp2a5 ^@ http://purl.uniprot.org/uniprot/Q80XK1|||http://purl.uniprot.org/uniprot/Q91X75 ^@ Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Non-terminal Residue|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Tusc1 ^@ http://purl.uniprot.org/uniprot/Q673H1 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Tumor suppressor candidate gene 1 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000312285 http://togogenome.org/gene/10090:Or7e165 ^@ http://purl.uniprot.org/uniprot/Q7TRF6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nat14 ^@ http://purl.uniprot.org/uniprot/Q8BVG8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Transmembrane ^@ Helical|||N-acetyltransferase|||Probable N-acetyltransferase 14 ^@ http://purl.uniprot.org/annotation/PRO_0000307788 http://togogenome.org/gene/10090:Hcfc1r1 ^@ http://purl.uniprot.org/uniprot/Q9CYQ5 ^@ Chain|||Molecule Processing|||Motif|||Region ^@ Chain|||Motif|||Region ^@ Disordered|||Host cell factor C1 regulator 1|||Interaction with HCFC1|||Nuclear export signal ^@ http://purl.uniprot.org/annotation/PRO_0000338979 http://togogenome.org/gene/10090:Slc27a1 ^@ http://purl.uniprot.org/uniprot/Q544D7|||http://purl.uniprot.org/uniprot/Q60714 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Abolishes very-long-chain acyl-CoA synthetase activity.|||Cytoplasmic|||Diminishes LCFA import and decreases nucleotide binding. No effect on localization to the cell membrane.|||Extracellular|||Helical|||Long-chain fatty acid transport protein 1|||Sufficient for oligomerization ^@ http://purl.uniprot.org/annotation/PRO_0000193202 http://togogenome.org/gene/10090:Ssc4d ^@ http://purl.uniprot.org/uniprot/A1L0T3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4|||Scavenger receptor cysteine-rich domain-containing group B protein ^@ http://purl.uniprot.org/annotation/PRO_0000322582 http://togogenome.org/gene/10090:Slc15a5 ^@ http://purl.uniprot.org/uniprot/Q8CBB2 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Solute carrier family 15 member 5 ^@ http://purl.uniprot.org/annotation/PRO_0000332234|||http://purl.uniprot.org/annotation/VSP_033358 http://togogenome.org/gene/10090:Septin5 ^@ http://purl.uniprot.org/uniprot/Q9Z2Q6 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region ^@ G1 motif|||G3 motif|||G4 motif|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Septin-5|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173523 http://togogenome.org/gene/10090:Or52e19 ^@ http://purl.uniprot.org/uniprot/F8VQ26 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp513 ^@ http://purl.uniprot.org/uniprot/Q6PD29 ^@ 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 ^@ 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 isoform 2.|||Phosphoserine|||Zinc finger protein 513 ^@ http://purl.uniprot.org/annotation/PRO_0000353093|||http://purl.uniprot.org/annotation/VSP_035626 http://togogenome.org/gene/10090:Hdgfl1 ^@ http://purl.uniprot.org/uniprot/Q2VPR5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PWWP ^@ http://togogenome.org/gene/10090:Suclg2 ^@ http://purl.uniprot.org/uniprot/Q9Z2I8 ^@ 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|||Site|||Splice Variant|||Transit Peptide ^@ ATP-grasp|||Important for substrate specificity|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000033357|||http://purl.uniprot.org/annotation/VSP_016905 http://togogenome.org/gene/10090:Fbxo4 ^@ http://purl.uniprot.org/uniprot/Q8CHQ0 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ F-box|||F-box only protein 4|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000119880 http://togogenome.org/gene/10090:Rflna ^@ http://purl.uniprot.org/uniprot/Q7TS73 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Disordered|||Refilin-A ^@ http://purl.uniprot.org/annotation/PRO_0000274332 http://togogenome.org/gene/10090:H2-M10.4 ^@ http://purl.uniprot.org/uniprot/Q85ZW8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015098996 http://togogenome.org/gene/10090:Irf5 ^@ http://purl.uniprot.org/uniprot/F6Z6C6|||http://purl.uniprot.org/uniprot/P56477|||http://purl.uniprot.org/uniprot/Q3U169 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Abolished homodimerization and subsequent activation.|||Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||IRF tryptophan pentad repeat|||Interferon regulatory factor 5|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by IKKB|||Phosphoserine; by TBK1|||Reduced homodimerization and subsequent activation. ^@ http://purl.uniprot.org/annotation/PRO_0000154559 http://togogenome.org/gene/10090:Ank1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1N7|||http://purl.uniprot.org/uniprot/B7ZW98|||http://purl.uniprot.org/uniprot/D3YTV8|||http://purl.uniprot.org/uniprot/D3Z5M4|||http://purl.uniprot.org/uniprot/E9QNT8|||http://purl.uniprot.org/uniprot/G5E8J2|||http://purl.uniprot.org/uniprot/Q02357|||http://purl.uniprot.org/uniprot/Q0VGY9 ^@ 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 ^@ (3S)-3-hydroxyasparagine; by HIF1AN|||(3S)-3-hydroxyasparagine; by HIF1AN; partial|||(3S)-3-hydroxyaspartate; by HIF1AN|||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|||Ankyrin-1|||Basic and acidic residues|||Death|||Disordered|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform Br2 and isoform 6.|||In isoform Br2.|||In isoform Br4.|||In isoform Er3 and isoform Mu8.|||In isoform Mu7 and isoform Mu8.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||UPA domain|||ZU5|||ZU5 1|||ZU5 2 ^@ http://purl.uniprot.org/annotation/PRO_0000066884|||http://purl.uniprot.org/annotation/VSP_018452|||http://purl.uniprot.org/annotation/VSP_018453|||http://purl.uniprot.org/annotation/VSP_018454|||http://purl.uniprot.org/annotation/VSP_018455|||http://purl.uniprot.org/annotation/VSP_018456|||http://purl.uniprot.org/annotation/VSP_018457|||http://purl.uniprot.org/annotation/VSP_018458|||http://purl.uniprot.org/annotation/VSP_018459|||http://purl.uniprot.org/annotation/VSP_018460 http://togogenome.org/gene/10090:Uba5 ^@ http://purl.uniprot.org/uniprot/Q8VE47 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict ^@ Abolished ability to catalyze the first step in ufmylation.|||Glycyl thioester intermediate|||Phosphoserine|||UFM1-interacting sequence (UIS)|||Ubiquitin-like modifier-activating enzyme 5 ^@ http://purl.uniprot.org/annotation/PRO_0000194971 http://togogenome.org/gene/10090:Psmb9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J256|||http://purl.uniprot.org/uniprot/P28076 ^@ 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 LMP-2b and LMP-2q.|||In LMP-2b.|||N6-acetyllysine|||Nucleophile|||Proteasome subunit beta type-9|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000026621|||http://purl.uniprot.org/annotation/PRO_0000026622 http://togogenome.org/gene/10090:Fosb ^@ http://purl.uniprot.org/uniprot/A2RSD4|||http://purl.uniprot.org/uniprot/P13346 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ BZIP|||Basic and acidic residues|||Basic motif|||Disordered|||In isoform 2.|||Increased degradation by the proteasome and a decrease in isoform 2/deltaFosB transactivation activity.|||Increased protein stability.|||Interchain (with C-279 in JUND)|||Leucine-zipper|||Phosphoserine|||Polar residues|||Pro residues|||Protein FosB|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076477|||http://purl.uniprot.org/annotation/VSP_061375 http://togogenome.org/gene/10090:Rmnd5a ^@ http://purl.uniprot.org/uniprot/Q80YQ8 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger ^@ CTLH|||E3 ubiquitin-protein ligase RMND5A|||LisH|||N-acetylmethionine|||RING-Gid-type ^@ http://purl.uniprot.org/annotation/PRO_0000272649 http://togogenome.org/gene/10090:Pla1a ^@ http://purl.uniprot.org/uniprot/Q8VI78 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phospholipase A1 member A ^@ http://purl.uniprot.org/annotation/PRO_0000273331 http://togogenome.org/gene/10090:Nmral1 ^@ http://purl.uniprot.org/uniprot/D3YU12|||http://purl.uniprot.org/uniprot/G5E8S7|||http://purl.uniprot.org/uniprot/Q8K2T1 ^@ 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 ^@ In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Interaction with ASS1|||NmrA-like|||NmrA-like family domain-containing protein 1|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000278205|||http://purl.uniprot.org/annotation/VSP_023151|||http://purl.uniprot.org/annotation/VSP_023153|||http://purl.uniprot.org/annotation/VSP_023154|||http://purl.uniprot.org/annotation/VSP_027873|||http://purl.uniprot.org/annotation/VSP_027874 http://togogenome.org/gene/10090:Ryr2 ^@ http://purl.uniprot.org/uniprot/E9Q401|||http://purl.uniprot.org/uniprot/Q60835|||http://purl.uniprot.org/uniprot/Q80ZZ5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 1|||2|||3|||4|||4 X approximate repeats|||Abolishes phosphorylation by CaMK2D. Tendency to tachycardia and subsequent death due to heart failure.|||B30.2/SPRY|||B30.2/SPRY 1|||B30.2/SPRY 2|||B30.2/SPRY 3|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Interaction with CALM|||Ion transport|||MIR|||MIR 1|||MIR 2|||MIR 3|||MIR 4|||MIR 5|||Mutant mice show systolic arrhythmogenic abnormalities. Spontaneous Ca(2+) release from the sarcoplasmic reticulum in the heart is diminished.|||No change to global protein fold or protein stability. Alters local protein folding.|||No effect on calcium channel activity. Abolishes ryanodine binding.|||Phosphoserine|||Phosphoserine; by CaMK2D|||Phosphoserine; by CaMK2D and PKA|||Phosphoserine; by PKA|||Pore-forming|||Protects against tachycardia and subsequent death due to heart failure.|||Reduced calcium channel activity. Reduces single channel conductance by 97%. No effect on ryaodine binding.|||Ryanodine receptor 2|||Strongly reduced calcium channel activity. Abolishes ryanodine binding. ^@ http://purl.uniprot.org/annotation/PRO_0000415582 http://togogenome.org/gene/10090:Cgas ^@ http://purl.uniprot.org/uniprot/Q8BSY1|||http://purl.uniprot.org/uniprot/Q8C6L5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||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|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ 5-glutamyl glutamate|||5-glutamyl polyglutamate|||Abolished homodimerization and subsequent activation. Does not affect nuclear localization and tethering to chromatin.|||Abolished interaction with nucleosomes.|||Abolished monomethylation, promoting interaction with PARP1.|||Abolished nucleotidyltransferase activity. Does not affect nuclear localization and tethering to chromatin.|||Abolished poly-ADP-ribosylation by PARP1, stimulating interferon production in knockin mice.|||Abolished tethering to chromatin, leading to strong constitutive activation in the absence of DNA.|||Abolished ubiquitination by TRIM56, leading to impaired homodimerization and activation. Does not affect sumoylation. Strongly reduced sumoylation; when associated with R-372 and R-382.|||Abolishes ability to promote type-I interferon production.|||Abolishes stimulation of interferon production; when associated with A-199.|||Arginine-anchor|||Basic and acidic residues|||Cleavage; by CASP3|||Cyclic GMP-AMP synthase|||DNA-binding|||Decreased DNA-binding and abolished homodimerization. Does not affect nuclear localization and tethering to chromatin.|||Decreased DNA-binding and subsequent activation. Does not affect nuclear localization and tethering to chromatin.|||Decreased cyclic GMP-AMP synthase activity.|||Disordered|||Does not affect ability to bind poly-ADP-ribosylated PARP1.|||Does not affect deubiquitination by USP29. Reduced sumoylation.|||Does not affect interaction with nucleosomes.|||Does not affect ubiquitination by TRIM56.|||Enhanced stimulation of interferon production.|||Gains susceptibility to mouse-specific RU.521; when associated with N-467.|||Gains susceptibility to mouse-specific RU.521; when associated with S-419.|||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|||Impaired ability to bind poly-ADP-ribosylated PARP1.|||Impaired deubiquitination by USP29. Does not affect sumoylation.|||Impaired tethering to chromatin, leading to constitutive activation in the absence of DNA.|||Increased DNA-binding activity.|||Increased nucleotidyltransferase activity.|||Induces alteration of the DNA-binding surface and leads to decreased synthesis of cyclic GMP-AMP (cGAMP); when associated with K-182.|||Induces alteration of the DNA-binding surface and leads to decreased synthesis of cyclic GMP-AMP (cGAMP); when associated with L-180.|||Interaction with collided ribosomes|||Mab-21-like nucleotidyltransferase|||N6-acetyllysine|||N6-methyllysine|||Nuclear export signal|||Nuclear localization signal|||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|||PolyADP-ribosyl glutamic acid|||Reduced sumoylation.|||Required for activation upon DNA viral infection|||Required for association with the cell membrane|||S-palmitoyl cysteine|||Slightly decreased interaction with nucleosomes.|||Slightly decreased tethering to chromatin, leading to mild constitutive activation in the absence of DNA.|||Slightly decreased tethering to chromatin. Does not affect interaction with nucleosomes.|||Strongly decreased interaction with nucleosomes.|||Strongly reduced interaction with nucleosomes.|||Strongly reduced sumoylation; when associated with R-335 and R-372.|||Strongly reduced sumoylation; when associated with R-335 and R-382. ^@ http://purl.uniprot.org/annotation/PRO_0000421764 http://togogenome.org/gene/10090:Pomt2 ^@ http://purl.uniprot.org/uniprot/Q8BGQ4 ^@ 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 and isoform 3.|||In isoform 2.|||MIR 1|||MIR 2|||MIR 3|||N-linked (GlcNAc...) asparagine|||Protein O-mannosyl-transferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000121489|||http://purl.uniprot.org/annotation/VSP_007597|||http://purl.uniprot.org/annotation/VSP_007598|||http://purl.uniprot.org/annotation/VSP_007599 http://togogenome.org/gene/10090:Trmt5 ^@ http://purl.uniprot.org/uniprot/Q9D0C4 ^@ 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.|||tRNA (guanine(37)-N1)-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000256515|||http://purl.uniprot.org/annotation/VSP_021355 http://togogenome.org/gene/10090:Ccnl1 ^@ http://purl.uniprot.org/uniprot/Q52KE7 ^@ 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.|||Phosphoserine|||Phosphothreonine|||RS ^@ http://purl.uniprot.org/annotation/PRO_0000080481|||http://purl.uniprot.org/annotation/VSP_016126|||http://purl.uniprot.org/annotation/VSP_016127 http://togogenome.org/gene/10090:Rprd2 ^@ http://purl.uniprot.org/uniprot/Q6NXI6 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||CID|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Regulation of nuclear pre-mRNA domain-containing protein 2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000244356|||http://purl.uniprot.org/annotation/VSP_019548 http://togogenome.org/gene/10090:Cenps ^@ http://purl.uniprot.org/uniprot/Q9D084 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Basic and acidic residues|||Centromere protein S|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000249478|||http://purl.uniprot.org/annotation/VSP_020435|||http://purl.uniprot.org/annotation/VSP_020436 http://togogenome.org/gene/10090:Gm20874 ^@ http://purl.uniprot.org/uniprot/J3QNI1 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Zhx1 ^@ http://purl.uniprot.org/uniprot/P70121|||http://purl.uniprot.org/uniprot/Q5DTL2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox|||Homeobox 1|||Homeobox 2|||Homeobox 3|||Homeobox 4|||Homeobox 5|||Phosphoserine|||Phosphothreonine|||Polar residues|||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_0000049389 http://togogenome.org/gene/10090:Gpsm2 ^@ http://purl.uniprot.org/uniprot/Q3UPG3|||http://purl.uniprot.org/uniprot/Q8VDU0 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Site|||Strand ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Strand ^@ Abolishes interaction with INSC.|||Abolishes interaction with NUMA1; when associated with A-228. Abolishes interaction with FRMPD1; when associated with A-228.|||Abolishes interaction with NUMA1; when associated with A-243. Abolishes interaction with FRMPD1; when associated with A-243.|||Disrupts one GNAI3 binding site.|||G-protein-signaling modulator 2|||GoLoco 1|||GoLoco 2|||GoLoco 3|||GoLoco 4|||Important for interaction with NUMA1; INSC and FRMPD1|||Nearly abolishes interaction with NUMA1.|||Phosphoserine|||Phosphothreonine|||Reduces affinity for GDP-bound GNAI3 50-fold. Reduces affinity for GDP-bound GNAI3 500-fold; when associated with A-647.|||Reduces affinity for GDP-bound GNAI3 500-fold; when associated with A-642.|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8 ^@ http://purl.uniprot.org/annotation/PRO_0000106359 http://togogenome.org/gene/10090:Uox ^@ http://purl.uniprot.org/uniprot/P25688|||http://purl.uniprot.org/uniprot/Q543J0 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif ^@ Charge relay system|||Microbody targeting signal|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphotyrosine|||Removed|||Uricase ^@ http://purl.uniprot.org/annotation/PRO_0000165986 http://togogenome.org/gene/10090:Vmn2r73 ^@ http://purl.uniprot.org/uniprot/D3Z7M3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015088528 http://togogenome.org/gene/10090:Cpsf6 ^@ http://purl.uniprot.org/uniprot/H3BJ30|||http://purl.uniprot.org/uniprot/H3BJW3|||http://purl.uniprot.org/uniprot/Q6NVF9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Arg/Ser-rich domain|||Basic and acidic residues|||Cleavage and polyadenylation specificity factor subunit 6|||Disordered|||GAR|||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|||Sufficient for nuclear speckle localization|||Sufficient for nuclear targeting ^@ http://purl.uniprot.org/annotation/PRO_0000081522 http://togogenome.org/gene/10090:Pbx1 ^@ http://purl.uniprot.org/uniprot/D9J2V6|||http://purl.uniprot.org/uniprot/P41778|||http://purl.uniprot.org/uniprot/Q71VB4 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand|||Turn ^@ Disordered|||Homeobox|||Homeobox; TALE-type|||In isoform PBX1b.|||PBC|||PBC-A|||PBC-B|||Polar residues|||Pre-B-cell leukemia transcription factor 1|||Required for binding to the NFIL3 promoter|||Significantly reduced binding to NFIL3 promoter.|||Slightly reduced binding to NFIL3 promoter. ^@ http://purl.uniprot.org/annotation/PRO_0000049236|||http://purl.uniprot.org/annotation/VSP_002273|||http://purl.uniprot.org/annotation/VSP_002274 http://togogenome.org/gene/10090:Lamtor4 ^@ http://purl.uniprot.org/uniprot/Q8CF66 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ N-acetylmethionine|||N-acetylthreonine; in Ragulator complex protein LAMTOR4, N-terminally processed|||Phosphoserine|||Ragulator complex protein LAMTOR4|||Ragulator complex protein LAMTOR4, N-terminally processed|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000325842|||http://purl.uniprot.org/annotation/PRO_0000424499 http://togogenome.org/gene/10090:Or10d3 ^@ http://purl.uniprot.org/uniprot/Q8VEY3 ^@ 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 10D3 ^@ http://purl.uniprot.org/annotation/PRO_0000326026 http://togogenome.org/gene/10090:Vpreb3 ^@ http://purl.uniprot.org/uniprot/Q61243 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015098096 http://togogenome.org/gene/10090:C3 ^@ http://purl.uniprot.org/uniprot/P01027 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ Acylation stimulating protein|||Anaphylatoxin-like|||C3-beta-c|||C3a anaphylatoxin|||Cleavage; by C3 convertase|||Cleavage; by carboxypeptidases|||Cleavage; by factor I|||Complement C3|||Complement C3 alpha chain|||Complement C3 beta chain|||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|||In isoform Short.|||Interaction with CFP/properdin|||Interchain (between beta and alpha chains)|||Isoglutamyl cysteine thioester (Cys-Gln)|||N-linked (GlcNAc...) asparagine|||NTR|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000005917|||http://purl.uniprot.org/annotation/PRO_0000005918|||http://purl.uniprot.org/annotation/PRO_0000005919|||http://purl.uniprot.org/annotation/PRO_0000005920|||http://purl.uniprot.org/annotation/PRO_0000005921|||http://purl.uniprot.org/annotation/PRO_0000005922|||http://purl.uniprot.org/annotation/PRO_0000005923|||http://purl.uniprot.org/annotation/PRO_0000005924|||http://purl.uniprot.org/annotation/PRO_0000005925|||http://purl.uniprot.org/annotation/PRO_0000005927|||http://purl.uniprot.org/annotation/PRO_0000273949|||http://purl.uniprot.org/annotation/PRO_0000419936|||http://purl.uniprot.org/annotation/PRO_0000430431|||http://purl.uniprot.org/annotation/VSP_018708 http://togogenome.org/gene/10090:Adap2 ^@ http://purl.uniprot.org/uniprot/Q5SSK2|||http://purl.uniprot.org/uniprot/Q8R2V5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Zinc Finger ^@ Arf-GAP|||Arf-GAP with dual PH domain-containing protein 2|||C4-type|||PH|||PH 1|||PH 2 ^@ http://purl.uniprot.org/annotation/PRO_0000074207 http://togogenome.org/gene/10090:Adamtsl5 ^@ http://purl.uniprot.org/uniprot/D3Z689|||http://purl.uniprot.org/uniprot/Q9CRC7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ ADAMTS/ADAMTS-like cysteine-rich|||NTR ^@ http://purl.uniprot.org/annotation/PRO_5015088522|||http://purl.uniprot.org/annotation/PRO_5015099702 http://togogenome.org/gene/10090:Armc2 ^@ http://purl.uniprot.org/uniprot/Q3URY6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||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 isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000325090|||http://purl.uniprot.org/annotation/VSP_024495|||http://purl.uniprot.org/annotation/VSP_024496 http://togogenome.org/gene/10090:Syngap1 ^@ http://purl.uniprot.org/uniprot/F6SEU4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||C2|||Disordered|||PH|||Phosphoserine|||Phosphoserine; by PLK2|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Ras-GAP|||Ras/Rap GTPase-activating protein SynGAP|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000414716 http://togogenome.org/gene/10090:Prdm8 ^@ http://purl.uniprot.org/uniprot/Q8BZ97 ^@ 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 ^@ C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||PR domain zinc finger protein 8|||Polar residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000047765 http://togogenome.org/gene/10090:Tmem139 ^@ http://purl.uniprot.org/uniprot/E9PX92|||http://purl.uniprot.org/uniprot/Q8C6T0 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Trp53bp1 ^@ http://purl.uniprot.org/uniprot/A0A5H1ZRL7|||http://purl.uniprot.org/uniprot/P70399|||http://purl.uniprot.org/uniprot/Q3V1P7|||http://purl.uniprot.org/uniprot/Q8BZ87 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ BRCT|||BRCT 1|||BRCT 2|||Basic and acidic residues|||Disordered|||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 isoform 2 and isoform 3.|||In isoform 3.|||Interaction with dimethylated histone H4|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||TP53-binding protein 1|||Tudor-like|||UDR ^@ http://purl.uniprot.org/annotation/PRO_0000072644|||http://purl.uniprot.org/annotation/VSP_058926|||http://purl.uniprot.org/annotation/VSP_058927 http://togogenome.org/gene/10090:Mib1 ^@ http://purl.uniprot.org/uniprot/Q80SY4 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||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|||MIB/HERC2 1|||MIB/HERC2 2|||Phosphoserine|||RING-type 1|||RING-type 2|||RING-type 3|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000055944 http://togogenome.org/gene/10090:Hepacam2 ^@ http://purl.uniprot.org/uniprot/Q4VAH7 ^@ 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|||HEPACAM family member 2|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000332221 http://togogenome.org/gene/10090:Speer4b ^@ http://purl.uniprot.org/uniprot/Q9D9F7 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Zfyve1 ^@ http://purl.uniprot.org/uniprot/Q810J8 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Region|||Sequence Conflict|||Zinc Finger ^@ FYVE-type 1|||FYVE-type 2|||Required for localization in the lipid droplets|||Zinc finger FYVE domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000098714 http://togogenome.org/gene/10090:Dpep1 ^@ http://purl.uniprot.org/uniprot/P31428|||http://purl.uniprot.org/uniprot/Q3V175 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Dipeptidase 1|||GPI-anchor amidated serine|||Interchain|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000018654|||http://purl.uniprot.org/annotation/PRO_0000018655 http://togogenome.org/gene/10090:Kif15 ^@ http://purl.uniprot.org/uniprot/Q6P9L6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Kinesin motor|||Kinesin-like protein KIF15|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000328685 http://togogenome.org/gene/10090:Tbck ^@ http://purl.uniprot.org/uniprot/E9Q1W7|||http://purl.uniprot.org/uniprot/Q8BM85 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ In isoform 2.|||Protein kinase|||Rab-GAP TBC|||Rhodanese|||TBC domain-containing protein kinase-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000273279|||http://purl.uniprot.org/annotation/VSP_052276|||http://purl.uniprot.org/annotation/VSP_052277 http://togogenome.org/gene/10090:Atp2b3 ^@ http://purl.uniprot.org/uniprot/A2ALL9|||http://purl.uniprot.org/uniprot/Q0VF55|||http://purl.uniprot.org/uniprot/Q8C048 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Cation-transporting P-type ATPase N-terminal|||Disordered|||Helical ^@ http://togogenome.org/gene/10090:Caskin1 ^@ http://purl.uniprot.org/uniprot/Q6P9K8 ^@ 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 ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||CASK-binding|||Caskin-1|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SAM 1|||SAM 2|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000066981|||http://purl.uniprot.org/annotation/VSP_013121|||http://purl.uniprot.org/annotation/VSP_013122|||http://purl.uniprot.org/annotation/VSP_013123|||http://purl.uniprot.org/annotation/VSP_013124 http://togogenome.org/gene/10090:Gm7609 ^@ http://purl.uniprot.org/uniprot/A0A668KL92 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kdm5c ^@ http://purl.uniprot.org/uniprot/P41230 ^@ Binding Site|||Chain|||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|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ARID|||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.|||JmjC|||JmjN|||Lysine-specific demethylase 5C|||PHD-type 1|||PHD-type 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000200587|||http://purl.uniprot.org/annotation/VSP_000316|||http://purl.uniprot.org/annotation/VSP_026411 http://togogenome.org/gene/10090:Runx1t1 ^@ http://purl.uniprot.org/uniprot/B1AXH8|||http://purl.uniprot.org/uniprot/B1AXH9|||http://purl.uniprot.org/uniprot/Q3UQX8|||http://purl.uniprot.org/uniprot/Q61909|||http://purl.uniprot.org/uniprot/Q8C066 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Important for oligomerization|||MYND-type|||Nervy homology region 2 (NHR2)|||Nervy homology region 3 (NHR3)|||Phosphoserine|||Polar residues|||Protein CBFA2T1|||TAFH ^@ http://purl.uniprot.org/annotation/PRO_0000218300 http://togogenome.org/gene/10090:Zbtb17 ^@ http://purl.uniprot.org/uniprot/A6H6B9|||http://purl.uniprot.org/uniprot/Q60821 ^@ 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 ^@ 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)|||Interaction with HCFC1|||Interaction with MYC|||Polar residues|||Zinc finger and BTB domain-containing protein 17 ^@ http://purl.uniprot.org/annotation/PRO_0000047731 http://togogenome.org/gene/10090:Esrp2 ^@ http://purl.uniprot.org/uniprot/Q8K0G8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||Epithelial splicing regulatory protein 2|||Phosphoserine|||Pro residues|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000273051 http://togogenome.org/gene/10090:Hycc1 ^@ http://purl.uniprot.org/uniprot/Q6P9N1 ^@ 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|||Hyccin|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080006|||http://purl.uniprot.org/annotation/VSP_058130|||http://purl.uniprot.org/annotation/VSP_058131|||http://purl.uniprot.org/annotation/VSP_058132|||http://purl.uniprot.org/annotation/VSP_058133 http://togogenome.org/gene/10090:Notch1 ^@ http://purl.uniprot.org/uniprot/Q01705 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||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|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ (3S)-3-hydroxyasparagine; by HIF1AN; partial|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Cleavage; by ADAM17|||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; calcium-binding|||EGF-like 19; calcium-binding|||EGF-like 2|||EGF-like 20; calcium-binding|||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; 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 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|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HIF1AN-binding|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with DLL4|||Interaction with PSEN1|||LNR 1|||LNR 2|||LNR 3|||N-linked (GlcNAc...) asparagine|||NICD processing severely reduced.|||Neurogenic locus notch homolog protein 1|||No effect on localization to the plasma membrane. No effect on binding and activation by DLL1. Decreased localization to the plasma membrane; when associated with V-311.|||No effect.|||No significant effect on its binding and activation by DLL1 or JAG1. No effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. Decrease in LFNG- and MFNG-mediated inhibition of its activation by JAG1. Significant decrease in LFNG- and MFNG-mediated inhibition of its activation by JAG1; when associated with V-232.|||No significant effect on its binding and activation by DLL1 or JAG1. No effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. No effect on LFNG- and MFNG-mediated inhibition of its activation by JAG1.|||No significant effect on its binding and activation by DLL1 or JAG1. No significant effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. Decrease in LFNG- and MFNG-mediated inhibition of its activation by JAG1. Significant decrease in LFNG- and MFNG-mediated inhibition of its activation by JAG1; when associated with V-1402.|||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; alternate|||O-linked (Glc...) serine|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||O-linked (GlcNAc...) threonine|||Phosphothreonine|||Polar residues|||Processing by furin-like convertase abolished.|||Produces an activated, ligand-independent molecule; when associated with S-1675.|||Produces an activated, ligand-independent molecule; when associated with S-1682.|||Reduced ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation and greatly reduced transactivation capacity. Abolished ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation; when associated with G-2012. Almost abolished transactivation capacity; when associated with A-2012.|||Reduced ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. Abolished ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation; when associated with A-1945.|||Reduced activity.|||Reduced binding and activation by DLL1 but not JAG1. Decrease in RFNG- and LFNG-mediated enhancement of its activation by DLL1. Loss of RFNG-mediated enhancement of its activation by JAG1. Significant loss of binding and activation by DLL1 or JAG1 and complete loss of RFNG- and LFNG-mediated enhancement of its activation by DLL1; when associated with V-311.|||Reduced binding and activation by DLL1 but not JAG1. No effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. No effect on LFNG- and MFNG-mediated inhibition of its activation by JAG1.|||Reduced binding and activation by JAG1 but not DLL1. Decrease in MFNG-mediated enhancement of its activation by DLL1.|||Reduced binding and activation by JAG1 but not DLL1. No effect on RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. No effect on LFNG- and MFNG-mediated inhibition of its activation by JAG1.|||Significant loss of binding and activation by DLL1 or JAG1. Decrease in RFNG-, LFNG- and MFNG-mediated enhancement of its activation by DLL1. Decrease in LFNG-mediated inhibition of its activation by JAG1. Significant loss of binding and activation by DLL1 or JAG1 and complete loss of RFNG- and LFNG-mediated enhancement of its activation by DLL1; when associated with V-466. Decreased localization to the plasma membrane; when associated with A-435.|||Slightly reduced ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. Abolished ability to promote HIF1AN-dependent 2-oxoglutarate decarboxylation and almost abolished transactivation capacity; when associated with A-1945. ^@ http://purl.uniprot.org/annotation/PRO_0000007677|||http://purl.uniprot.org/annotation/PRO_0000007678|||http://purl.uniprot.org/annotation/PRO_0000007679|||http://purl.uniprot.org/annotation/VSP_001402|||http://purl.uniprot.org/annotation/VSP_001403|||http://purl.uniprot.org/annotation/VSP_001404|||http://purl.uniprot.org/annotation/VSP_043064|||http://purl.uniprot.org/annotation/VSP_043065 http://togogenome.org/gene/10090:Shfl ^@ http://purl.uniprot.org/uniprot/Q3U076|||http://purl.uniprot.org/uniprot/Q8CAK3 ^@ 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.|||Interaction with PABPC1|||Nuclear export signal|||Nuclear localization signal|||Shiftless antiviral inhibitor of ribosomal frameshifting protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000318702|||http://purl.uniprot.org/annotation/VSP_031275 http://togogenome.org/gene/10090:Scgb2b15 ^@ http://purl.uniprot.org/uniprot/A0A089N3E7|||http://purl.uniprot.org/uniprot/S4R2V3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5001847728|||http://purl.uniprot.org/annotation/PRO_5015101141 http://togogenome.org/gene/10090:Aars2 ^@ http://purl.uniprot.org/uniprot/Q14CH7 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Sequence Conflict|||Transit Peptide ^@ Alanine--tRNA ligase, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000250726 http://togogenome.org/gene/10090:Tdrd9 ^@ http://purl.uniprot.org/uniprot/Q14BI7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Splice Variant ^@ ATP-dependent RNA helicase TDRD9|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In Tdrd9(KI); heterozygous and homozygous knockin male mice are infertile due to derepression of transposable elements. PiRNA biogenesis in not affected but piRNAs fail to accumulate in the nucleus.|||In isoform 2.|||In isoform 3.|||Polar residues|||Tudor ^@ http://purl.uniprot.org/annotation/PRO_0000333814|||http://purl.uniprot.org/annotation/VSP_033553|||http://purl.uniprot.org/annotation/VSP_033554|||http://purl.uniprot.org/annotation/VSP_033555 http://togogenome.org/gene/10090:Eif2b3 ^@ http://purl.uniprot.org/uniprot/B1AUN2|||http://purl.uniprot.org/uniprot/Q3UKV0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Nucleotidyl transferase ^@ http://togogenome.org/gene/10090:Cyp2a22 ^@ http://purl.uniprot.org/uniprot/B2RXZ2 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Cytochrome P450 ^@ http://purl.uniprot.org/annotation/PRO_5015087167 http://togogenome.org/gene/10090:Nudt16l1 ^@ http://purl.uniprot.org/uniprot/Q8VHN8 ^@ Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Chain|||Crosslink|||Helix|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||Interaction with PXN|||Required for interaction with TP53BP1|||Tudor-interacting repair regulator protein ^@ http://purl.uniprot.org/annotation/PRO_0000097649|||http://purl.uniprot.org/annotation/VSP_014277|||http://purl.uniprot.org/annotation/VSP_014278|||http://purl.uniprot.org/annotation/VSP_014279 http://togogenome.org/gene/10090:Phlpp2 ^@ http://purl.uniprot.org/uniprot/J3QM82|||http://purl.uniprot.org/uniprot/Q8BXA7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||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|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000057785 http://togogenome.org/gene/10090:Adam34 ^@ http://purl.uniprot.org/uniprot/A2RSG8 ^@ Active Site|||Binding Site|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Disulfide Bond|||Domain Extent|||Transmembrane ^@ Disintegrin|||EGF-like|||Helical|||Peptidase M12B ^@ http://togogenome.org/gene/10090:Tm4sf1 ^@ http://purl.uniprot.org/uniprot/Q64302 ^@ 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 1 ^@ http://purl.uniprot.org/annotation/PRO_0000219297 http://togogenome.org/gene/10090:Lman1l ^@ http://purl.uniprot.org/uniprot/Q8VCD3 ^@ 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|||Helical|||In isoform 2.|||L-type lectin-like|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein ERGIC-53-like ^@ http://purl.uniprot.org/annotation/PRO_0000017664|||http://purl.uniprot.org/annotation/VSP_039811|||http://purl.uniprot.org/annotation/VSP_039812 http://togogenome.org/gene/10090:Efhc2 ^@ http://purl.uniprot.org/uniprot/Q059K2|||http://purl.uniprot.org/uniprot/Q9D485 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ DM10|||DM10 1|||DM10 2|||DM10 3|||EF-hand|||EF-hand domain-containing family member C2 ^@ http://purl.uniprot.org/annotation/PRO_0000251704 http://togogenome.org/gene/10090:Vmn1r45 ^@ http://purl.uniprot.org/uniprot/Q8VIC7 ^@ 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|||Vomeronasal type-1 receptor 45 ^@ http://purl.uniprot.org/annotation/PRO_0000239957 http://togogenome.org/gene/10090:Or3a4 ^@ http://purl.uniprot.org/uniprot/Q7TRX3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cep135 ^@ http://purl.uniprot.org/uniprot/Q6P5D4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region ^@ Centrosomal protein of 135 kDa|||Disordered|||Interchain|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089492 http://togogenome.org/gene/10090:Cops6 ^@ http://purl.uniprot.org/uniprot/O88545|||http://purl.uniprot.org/uniprot/Q3UIT2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ COP9 signalosome complex subunit 6|||MPN ^@ http://purl.uniprot.org/annotation/PRO_0000194861 http://togogenome.org/gene/10090:B3gnt2 ^@ http://purl.uniprot.org/uniprot/Q9Z222 ^@ 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-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219171 http://togogenome.org/gene/10090:Lct ^@ http://purl.uniprot.org/uniprot/F8VPT3 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Chain|||Signal Peptide|||Transmembrane ^@ Helical|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_5003379233 http://togogenome.org/gene/10090:Cep76 ^@ http://purl.uniprot.org/uniprot/Q0VEJ0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Centrosomal protein of 76 kDa|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000378949 http://togogenome.org/gene/10090:Ube3a ^@ http://purl.uniprot.org/uniprot/O08759|||http://purl.uniprot.org/uniprot/Q5DTH1 ^@ 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|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Abolishes catalytic activity. Abolishes ability to ubiquitinate ARC and LAMTOR1.|||Basic and acidic residues|||C4-type; atypical|||Disordered|||Glycyl thioester intermediate|||HECT|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphotyrosine; by ABL1|||Polar residues|||Ubiquitin-protein ligase E3A ^@ http://purl.uniprot.org/annotation/PRO_0000194981|||http://purl.uniprot.org/annotation/VSP_057563|||http://purl.uniprot.org/annotation/VSP_057564 http://togogenome.org/gene/10090:Eif1ad2 ^@ http://purl.uniprot.org/uniprot/Q3UT53 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||S1-like ^@ http://togogenome.org/gene/10090:Idua ^@ http://purl.uniprot.org/uniprot/Q3U1Z0|||http://purl.uniprot.org/uniprot/Q8BLF6|||http://purl.uniprot.org/uniprot/Q8BMG0 ^@ Active Site|||Chain|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Signal Peptide ^@ Alpha-L-iduronidase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_5004229919|||http://purl.uniprot.org/annotation/PRO_5015099016|||http://purl.uniprot.org/annotation/PRO_5015099040 http://togogenome.org/gene/10090:Bin1 ^@ http://purl.uniprot.org/uniprot/A0A3Q4EBK4|||http://purl.uniprot.org/uniprot/O08539|||http://purl.uniprot.org/uniprot/Q6P1B9 ^@ 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 ^@ BAR|||Clathrin-binding|||Disordered|||In isoform 2.|||Interaction with BIN2|||Myc box-dependent-interacting protein 1|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000192952|||http://purl.uniprot.org/annotation/VSP_000254|||http://purl.uniprot.org/annotation/VSP_000255 http://togogenome.org/gene/10090:Tmx3 ^@ http://purl.uniprot.org/uniprot/Q8BXZ1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Di-lysine motif|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein disulfide-isomerase TMX3|||Redox-active|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000034186 http://togogenome.org/gene/10090:Mitf ^@ http://purl.uniprot.org/uniprot/Q08874|||http://purl.uniprot.org/uniprot/Q32MU7|||http://purl.uniprot.org/uniprot/Q8C6Y4 ^@ 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|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand ^@ BHLH|||Changes the structure of the leucine zipper and thereby confers the ability to form heterodimers with MAX.|||DNA-binding regulation|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform A1 and isoform H3.|||In isoform A2 and isoform M1.|||In isoform A2.|||In isoform H, isoform H1, isoform H2 and isoform H3.|||In isoform H1 and isoform H2.|||In isoform H2.|||In isoform M and isoform M1.|||In microphthalmia-black and white spot/mi-bws.|||In microphthalmia-cloudy-eyed/mi-ce and microphthalmia-defective iris/mi-di.|||In microphthalmia-eyeless-white/mi-ew.|||In microphthalmia-red-eyed white/mi-rw.|||In microphthalmia-spotted/mi-sp.|||In microphthalmia-vitiligo/mi-vi.|||In microphthalmia-white spot/mi-ws.|||In microphthalmia-white/mi-wh.|||In microphthalmia/mi.|||Leucine-zipper|||Microphthalmia-associated transcription factor|||Phosphoserine|||Phosphoserine; by GSK3|||Phosphoserine; by MAPK|||Phosphoserine; by MTOR|||Phosphoserine; by RPS6KA1|||Polar residues|||Transactivation|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127277|||http://purl.uniprot.org/annotation/VSP_002129|||http://purl.uniprot.org/annotation/VSP_002130|||http://purl.uniprot.org/annotation/VSP_002131|||http://purl.uniprot.org/annotation/VSP_002132|||http://purl.uniprot.org/annotation/VSP_002133|||http://purl.uniprot.org/annotation/VSP_002134|||http://purl.uniprot.org/annotation/VSP_002135|||http://purl.uniprot.org/annotation/VSP_002136 http://togogenome.org/gene/10090:Il17a ^@ http://purl.uniprot.org/uniprot/Q544E6|||http://purl.uniprot.org/uniprot/Q62386 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ Interleukin-17A|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015424|||http://purl.uniprot.org/annotation/PRO_5014309618 http://togogenome.org/gene/10090:Tmem51 ^@ http://purl.uniprot.org/uniprot/Q99LG1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Polar residues|||Transmembrane protein 51 ^@ http://purl.uniprot.org/annotation/PRO_0000072578 http://togogenome.org/gene/10090:Cox8b ^@ http://purl.uniprot.org/uniprot/P48772|||http://purl.uniprot.org/uniprot/Q545U6 ^@ Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn ^@ Chain|||Helix|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn ^@ Cytochrome c oxidase subunit 8B, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000006178 http://togogenome.org/gene/10090:Spry1 ^@ http://purl.uniprot.org/uniprot/Q53ZU1|||http://purl.uniprot.org/uniprot/Q9QXV9 ^@ 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_0000076899 http://togogenome.org/gene/10090:Ppp1cc ^@ http://purl.uniprot.org/uniprot/P63087|||http://purl.uniprot.org/uniprot/Q6ZWM8 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Disordered|||In isoform 2.|||N-acetylalanine|||Phosphothreonine|||Proton donor|||Removed|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase PP1-gamma catalytic subunit ^@ http://purl.uniprot.org/annotation/PRO_0000058788|||http://purl.uniprot.org/annotation/VSP_005095 http://togogenome.org/gene/10090:Tas2r120 ^@ http://purl.uniprot.org/uniprot/Q7M721 ^@ 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 120 ^@ http://purl.uniprot.org/annotation/PRO_0000248479 http://togogenome.org/gene/10090:Nop14 ^@ http://purl.uniprot.org/uniprot/Q8C539|||http://purl.uniprot.org/uniprot/Q8R3N1 ^@ 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|||Basic and acidic residues|||Disordered|||Nucleolar protein 14|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000137156 http://togogenome.org/gene/10090:C1ql3 ^@ http://purl.uniprot.org/uniprot/A0A3B0IT58|||http://purl.uniprot.org/uniprot/Q9ESN4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Turn ^@ C1q|||Collagen-like|||Complement C1q-like protein 3|||Disordered|||Does not affect heterooligomerization with C1QL2; when associated with S-28.|||Does not affect heterooligomerization with C1QL2; when associated with S-32.|||Does not affect heterooligomerization with C1QL4; when associated with A-28.|||Does not affect heterooligomerization with C1QL4; when associated with A-32.|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000003542|||http://purl.uniprot.org/annotation/PRO_5017371604 http://togogenome.org/gene/10090:Ifit1bl1 ^@ http://purl.uniprot.org/uniprot/D3Z6F0|||http://purl.uniprot.org/uniprot/E9PXF7 ^@ Region|||Repeat ^@ Repeat ^@ TPR ^@ http://togogenome.org/gene/10090:Esrrg ^@ http://purl.uniprot.org/uniprot/P62509 ^@ 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|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Disordered|||Estrogen-related receptor gamma|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||Loss of transcriptional activation; when associated with A-449.|||Loss of transcriptional activation; when associated with A-450.|||Loss of transcriptional activation; when associated with A-453.|||Loss of transcriptional activation; when associated with A-454.|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053666|||http://purl.uniprot.org/annotation/VSP_010766 http://togogenome.org/gene/10090:Slc24a3 ^@ http://purl.uniprot.org/uniprot/Q8VD29 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Acidic residues|||Disordered|||Helical|||Sodium/calcium exchanger membrane region ^@ http://togogenome.org/gene/10090:Onecut2 ^@ http://purl.uniprot.org/uniprot/Q6XBJ3 ^@ 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_0000202406 http://togogenome.org/gene/10090:Gcnt3 ^@ http://purl.uniprot.org/uniprot/Q5JCT0 ^@ 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 ^@ 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_0000288546 http://togogenome.org/gene/10090:Man1a ^@ http://purl.uniprot.org/uniprot/P45700|||http://purl.uniprot.org/uniprot/Q544T7 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000210309 http://togogenome.org/gene/10090:Dnase2b ^@ http://purl.uniprot.org/uniprot/Q9QY48 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Deoxyribonuclease-2-beta|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000007296 http://togogenome.org/gene/10090:Pafah2 ^@ http://purl.uniprot.org/uniprot/E9QNW6|||http://purl.uniprot.org/uniprot/Q8VDG7 ^@ 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_0000090384 http://togogenome.org/gene/10090:Cryzl1 ^@ http://purl.uniprot.org/uniprot/D3Z6I4|||http://purl.uniprot.org/uniprot/Q921W4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ Enoyl reductase (ER)|||In isoform 2.|||Quinone oxidoreductase-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000160914|||http://purl.uniprot.org/annotation/VSP_000209|||http://purl.uniprot.org/annotation/VSP_000210 http://togogenome.org/gene/10090:Gk5 ^@ http://purl.uniprot.org/uniprot/Q8BX05 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2 and isoform 3.|||In isoform 3.|||Putative glycerol kinase 5 ^@ http://purl.uniprot.org/annotation/PRO_0000323755|||http://purl.uniprot.org/annotation/VSP_032124|||http://purl.uniprot.org/annotation/VSP_032125 http://togogenome.org/gene/10090:S1pr3 ^@ http://purl.uniprot.org/uniprot/Q9Z0U9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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|||Phosphoserine|||Polar residues|||Sphingosine 1-phosphate receptor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000069422 http://togogenome.org/gene/10090:Clec9a ^@ http://purl.uniprot.org/uniprot/Q8BRU4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes the recruitment and activation of the tyrosine kinase Syk.|||C-type lectin|||C-type lectin domain family 9 member A|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||ITAM-like|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046638|||http://purl.uniprot.org/annotation/VSP_041500|||http://purl.uniprot.org/annotation/VSP_041501|||http://purl.uniprot.org/annotation/VSP_041502|||http://purl.uniprot.org/annotation/VSP_041503|||http://purl.uniprot.org/annotation/VSP_041504|||http://purl.uniprot.org/annotation/VSP_041505 http://togogenome.org/gene/10090:Mocs1 ^@ http://purl.uniprot.org/uniprot/Q5RKZ7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||For molybdenum cofactor biosynthesis protein C activity|||In isoform 3.|||In isoform Mocs1a.|||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_0000369400|||http://purl.uniprot.org/annotation/VSP_036849|||http://purl.uniprot.org/annotation/VSP_036850|||http://purl.uniprot.org/annotation/VSP_036851 http://togogenome.org/gene/10090:Mvd ^@ http://purl.uniprot.org/uniprot/Q3UYC1|||http://purl.uniprot.org/uniprot/Q99JF5 ^@ 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 ^@ Diphosphomevalonate decarboxylase|||GHMP kinase N-terminal|||Mvd1 C-terminal|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087013 http://togogenome.org/gene/10090:Sema7a ^@ http://purl.uniprot.org/uniprot/Q9QUR8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Asymmetric dimethylarginine|||Cell attachment site|||GPI-anchor amidated alanine|||Homozygous mutant mice show signs of hepatocytes degeneration associated with elevated serum levels of total bile acid, alanine transaminase and aspartate transaminase. Levels of the canalicular bile acid transporters ABCB11 and ABCC2 are reduced.|||Ig-like C2-type|||Interaction with integrins|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Sema|||Semaphorin-7A ^@ http://purl.uniprot.org/annotation/PRO_0000032349|||http://purl.uniprot.org/annotation/PRO_0000032350 http://togogenome.org/gene/10090:Tut4 ^@ http://purl.uniprot.org/uniprot/A2A8R7|||http://purl.uniprot.org/uniprot/B2RX14|||http://purl.uniprot.org/uniprot/Q3V3D5|||http://purl.uniprot.org/uniprot/Q9EQN6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||CCHC-type|||CCHC-type 1|||CCHC-type 2|||CCHC-type 3|||Disordered|||Loss of nucleotidyltransferase activity and oocytes are unable to support early embryonic development; when associated with A-1026.|||Loss of nucleotidyltransferase activity and oocytes are unable to support early embryonic development; when associated with A-1028.|||Matrin-type|||No effect on basal uridylation activity, but loss of LIN28A-enhanced uridylation; when associated with A-326.|||No effect on basal uridylation activity, but loss of LIN28A-enhanced uridylation; when associated with A-329.|||Omega-N-methylarginine|||PAP-associated 1|||PAP-associated 2|||Phosphoserine|||Polar residues|||Pro residues|||Required for interaction with LIN28A and pre-let-7 RNA|||Sufficient for monouridylation activity|||TUTase nucleotidyltransferase|||Terminal uridylyltransferase 4 ^@ http://purl.uniprot.org/annotation/PRO_0000385330 http://togogenome.org/gene/10090:Mtcp1 ^@ http://purl.uniprot.org/uniprot/Q60945 ^@ Chain|||Molecule Processing ^@ Chain ^@ Protein p13 MTCP-1 ^@ http://purl.uniprot.org/annotation/PRO_0000184487 http://togogenome.org/gene/10090:Adipoq ^@ http://purl.uniprot.org/uniprot/Q60994 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ 4-hydroxyproline|||5-hydroxylysine|||5-hydroxylysine; alternate|||Adiponectin|||Basic and acidic residues|||C1q|||Collagen-like|||Disordered|||Impaired formation of HMW multimers; when associated with R-68; R-71 and R-104.|||Impaired formation of HMW multimers; when associated with R-68; R-71 and R-80.|||Impaired formation of HMW multimers; when associated with R-68; R-80 and R-104.|||Impaired formation of HMW multimers; when associated with R-71; R-80 and R-104.|||Interchain|||No change in the interaction with CTRP9.|||Not glycosylated|||Not hydroxylated|||O-linked (Gal...) hydroxylysine; alternate|||O-linked (GalNAc...) threonine|||S-(2-succinyl)cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000003544 http://togogenome.org/gene/10090:Smarcd3 ^@ http://purl.uniprot.org/uniprot/Q6P9Z1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||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_0000071989 http://togogenome.org/gene/10090:Ccdc92 ^@ http://purl.uniprot.org/uniprot/Q8VDN4 ^@ 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 92|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000274501 http://togogenome.org/gene/10090:Mettl6 ^@ http://purl.uniprot.org/uniprot/Q8BVH9 ^@ Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant ^@ Binding Site|||Chain|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||tRNA N(3)-methylcytidine methyltransferase METTL6 ^@ http://purl.uniprot.org/annotation/PRO_0000204455|||http://purl.uniprot.org/annotation/VSP_008481|||http://purl.uniprot.org/annotation/VSP_008482 http://togogenome.org/gene/10090:Gm5617 ^@ http://purl.uniprot.org/uniprot/Q91VN2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Uncharacterized protein C11orf71 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000274326 http://togogenome.org/gene/10090:Wfdc13 ^@ http://purl.uniprot.org/uniprot/Q5DQQ6 ^@ 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 13 ^@ http://purl.uniprot.org/annotation/PRO_0000415848 http://togogenome.org/gene/10090:Etv2 ^@ http://purl.uniprot.org/uniprot/P41163|||http://purl.uniprot.org/uniprot/Q5EP41 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||ETS|||ETS translocation variant 2 ^@ http://purl.uniprot.org/annotation/PRO_0000204113 http://togogenome.org/gene/10090:Cda ^@ http://purl.uniprot.org/uniprot/P56389 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Strand|||Turn ^@ CMP/dCMP-type deaminase|||Cytidine deaminase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000171683 http://togogenome.org/gene/10090:Zbtb8a ^@ http://purl.uniprot.org/uniprot/Q9CWH1 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 8A ^@ http://purl.uniprot.org/annotation/PRO_0000378509 http://togogenome.org/gene/10090:Nfkbie ^@ http://purl.uniprot.org/uniprot/A0A3B2WAY2|||http://purl.uniprot.org/uniprot/O54910 ^@ 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|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Disordered|||NF-kappa-B inhibitor epsilon|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000067008 http://togogenome.org/gene/10090:Dleu7 ^@ http://purl.uniprot.org/uniprot/Q8CHZ8 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Leukemia-associated protein 7 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000281768 http://togogenome.org/gene/10090:Hoxb3 ^@ http://purl.uniprot.org/uniprot/P09026 ^@ 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-B3|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000200118 http://togogenome.org/gene/10090:Krtap3-3 ^@ http://purl.uniprot.org/uniprot/Q9D638 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||3 X 5 AA repeats of C-C-X(3)|||Keratin-associated protein 3-2|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000358595 http://togogenome.org/gene/10090:Tbx20 ^@ http://purl.uniprot.org/uniprot/Q9ES03 ^@ 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|||In isoform 2.|||Polar residues|||T-box|||T-box transcription factor TBX20 ^@ http://purl.uniprot.org/annotation/PRO_0000184452|||http://purl.uniprot.org/annotation/VSP_021730 http://togogenome.org/gene/10090:Rad51c ^@ http://purl.uniprot.org/uniprot/Q924H5 ^@ 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|||Region|||Sequence Conflict|||Splice Variant ^@ DNA repair protein RAD51 homolog 3|||Disordered|||In isoform 2.|||Interaction with RAD51B, RAD51D and XRCC3|||Nuclear localization signal|||Phosphoserine|||Required for Holliday junction resolution activity ^@ http://purl.uniprot.org/annotation/PRO_0000401939|||http://purl.uniprot.org/annotation/VSP_040206 http://togogenome.org/gene/10090:Ntsr1 ^@ http://purl.uniprot.org/uniprot/A2ACT4|||http://purl.uniprot.org/uniprot/O88319 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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|||N-linked (GlcNAc...) asparagine|||Neurotensin binding|||Neurotensin receptor type 1|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069947 http://togogenome.org/gene/10090:Vmn1r46 ^@ http://purl.uniprot.org/uniprot/Q9EQ45 ^@ 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|||Vomeronasal type-1 receptor 46 ^@ http://purl.uniprot.org/annotation/PRO_0000239980 http://togogenome.org/gene/10090:Hsd3b1 ^@ http://purl.uniprot.org/uniprot/P24815|||http://purl.uniprot.org/uniprot/Q3UI20|||http://purl.uniprot.org/uniprot/Q3UJ12 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Transmembrane ^@ 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1|||3-beta hydroxysteroid dehydrogenase/isomerase|||Helical|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000087780 http://togogenome.org/gene/10090:Ephx4 ^@ http://purl.uniprot.org/uniprot/Q6IE26 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||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_0000281379 http://togogenome.org/gene/10090:Mrgpra3 ^@ http://purl.uniprot.org/uniprot/H3BKL3|||http://purl.uniprot.org/uniprot/Q91WW3 ^@ 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|||Mas-related G-protein coupled receptor member A3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069749 http://togogenome.org/gene/10090:Foxo3 ^@ http://purl.uniprot.org/uniprot/Q9WVH4 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Abolishes phosphorylation by CAMK2A. Loss of transcriptional activity.|||Acidic residues|||Disordered|||Fork-head|||Forkhead box protein O3|||Mediates interaction with CHUK/IKKA and IKBKB/IKKB|||N6-acetyllysine|||N6-methyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by AMPK and MAPKAPK5|||Phosphoserine; by CaMK2A|||Phosphoserine; by IKKB|||Phosphoserine; by MAPKAPK5|||Phosphoserine; by SGK1|||Phosphothreonine|||Polar residues|||Required for mitochondrial import ^@ http://purl.uniprot.org/annotation/PRO_0000415334 http://togogenome.org/gene/10090:Cenpa ^@ http://purl.uniprot.org/uniprot/O35216 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region ^@ CATD|||Disordered|||H3-like|||Histone H3-like centromeric protein A|||Important for flexibility of DNA ends that protrude from nucleosomes|||N,N,N-trimethylglycine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000221374 http://togogenome.org/gene/10090:Pdgfrl ^@ http://purl.uniprot.org/uniprot/A0A0R4J0C9|||http://purl.uniprot.org/uniprot/Q6PE55 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Platelet-derived growth factor receptor-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000233092|||http://purl.uniprot.org/annotation/PRO_5006451969 http://togogenome.org/gene/10090:Sap30 ^@ http://purl.uniprot.org/uniprot/O88574 ^@ Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Zinc Finger ^@ Chain|||Crosslink|||Helix|||Modified Residue|||Region|||Strand|||Zinc Finger ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000097583 http://togogenome.org/gene/10090:Pex10 ^@ http://purl.uniprot.org/uniprot/B1AUE5 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Region|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||Disordered|||Helical; Name=TM1|||Helical; Name=TM2|||Helical; Name=TM3|||Helical; Name=TM4|||Helical; Name=TM5|||Peroxisomal matrix|||Peroxisome biogenesis factor 10|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000346862 http://togogenome.org/gene/10090:Mzt1 ^@ http://purl.uniprot.org/uniprot/Q8BUR9 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Mitotic-spindle organizing protein 1|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000337016 http://togogenome.org/gene/10090:Kras ^@ http://purl.uniprot.org/uniprot/P32883|||http://purl.uniprot.org/uniprot/Q5J7N1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Splice Variant ^@ Basic residues|||Cysteine methyl ester|||Disordered|||Effector region|||GTPase KRas|||GTPase KRas, N-terminally processed|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hypervariable region|||In isoform 2B.|||N-acetylmethionine|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000082643|||http://purl.uniprot.org/annotation/PRO_0000281293|||http://purl.uniprot.org/annotation/PRO_0000326482|||http://purl.uniprot.org/annotation/VSP_011142|||http://purl.uniprot.org/annotation/VSP_011143 http://togogenome.org/gene/10090:Garin2 ^@ http://purl.uniprot.org/uniprot/D3YV92|||http://purl.uniprot.org/uniprot/Q80W24 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ Golgi associated RAB2 interactor protein-like Rab2B-binding|||Golgi-associated RAB2 interactor protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000455124 http://togogenome.org/gene/10090:Or2a5 ^@ http://purl.uniprot.org/uniprot/Q8VES9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or2r2 ^@ http://purl.uniprot.org/uniprot/B2RT27 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp366 ^@ http://purl.uniprot.org/uniprot/Q6NS86 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Zinc Finger ^@ Acidic residues|||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|||Interaction with NRIP1|||PXDLS|||Polar residues|||Zinc finger protein 366 ^@ http://purl.uniprot.org/annotation/PRO_0000439856 http://togogenome.org/gene/10090:Cwc15 ^@ http://purl.uniprot.org/uniprot/Q9JHS9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 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_0000291544 http://togogenome.org/gene/10090:Prss41 ^@ http://purl.uniprot.org/uniprot/Q920S2 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Charge relay system|||GPI-anchor amidated asparagine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Removed in mature form|||Serine protease 41 ^@ http://purl.uniprot.org/annotation/PRO_0000345422|||http://purl.uniprot.org/annotation/PRO_0000345423|||http://purl.uniprot.org/annotation/PRO_0000345424|||http://purl.uniprot.org/annotation/VSP_034949|||http://purl.uniprot.org/annotation/VSP_034950 http://togogenome.org/gene/10090:Reg2 ^@ http://purl.uniprot.org/uniprot/Q08731|||http://purl.uniprot.org/uniprot/Q545J0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ C-type lectin|||Lithostathine-2 ^@ http://purl.uniprot.org/annotation/PRO_0000017427|||http://purl.uniprot.org/annotation/PRO_5014309592 http://togogenome.org/gene/10090:Usp45 ^@ http://purl.uniprot.org/uniprot/Q8K387 ^@ 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|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with ERCC1|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 45 ^@ http://purl.uniprot.org/annotation/PRO_0000280562|||http://purl.uniprot.org/annotation/VSP_023794 http://togogenome.org/gene/10090:Synb ^@ http://purl.uniprot.org/uniprot/Q8BI41 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ CX6CC|||CXXC|||Cleavage|||Cytoplasmic|||Extracellular|||Fusion peptide|||Helical|||Immunosuppression|||Interchain (between SU and TM chains, or C-47 with C-507); in linked form|||Loss of immunosuppressive activity. No effect on fusogenic activity.|||N-linked (GlcNAc...) asparagine|||Surface protein|||Syncytin-B|||Transmembrane protein ^@ http://purl.uniprot.org/annotation/PRO_0000440575|||http://purl.uniprot.org/annotation/PRO_0000440576|||http://purl.uniprot.org/annotation/PRO_5009346813 http://togogenome.org/gene/10090:Dync2i1 ^@ http://purl.uniprot.org/uniprot/Q8C761 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Binding to the DYNLT2B-DYNLT1/DYNLT3 dimer|||Cytoplasmic dynein 2 intermediate chain 1|||Disordered|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000242143 http://togogenome.org/gene/10090:Or9s27 ^@ http://purl.uniprot.org/uniprot/Q8VET3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cyp2c68 ^@ http://purl.uniprot.org/uniprot/K7N6C2 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5003910730 http://togogenome.org/gene/10090:Dppa2 ^@ http://purl.uniprot.org/uniprot/B2RQ54|||http://purl.uniprot.org/uniprot/Q9CWH0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Developmental pluripotency-associated protein 2|||Developmental pluripotency-associated protein 2/4 C-terminal|||Developmental pluripotency-associated protein 2/4 central|||Disordered|||Polar residues|||SAP ^@ http://purl.uniprot.org/annotation/PRO_0000239264 http://togogenome.org/gene/10090:Ints13 ^@ http://purl.uniprot.org/uniprot/Q8QZV7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Integrator complex subunit 13|||Loss of nuclear location. Location is mainly cytoplasmic or diffuse.|||Nuclear localization signal (NLS)|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000089846 http://togogenome.org/gene/10090:Alkbh8 ^@ http://purl.uniprot.org/uniprot/Q80Y20 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes hydroxylation of 5-methylcarboxymethyl uridine.|||Alkylated DNA repair protein alkB homolog 8|||Fe2OG dioxygenase|||In isoform 2.|||In isoform 3.|||Methyltransferase domain|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000337127|||http://purl.uniprot.org/annotation/VSP_033929|||http://purl.uniprot.org/annotation/VSP_033930|||http://purl.uniprot.org/annotation/VSP_033931 http://togogenome.org/gene/10090:Ift70a1 ^@ http://purl.uniprot.org/uniprot/Q99J38 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Repeat|||Sequence Conflict ^@ Intraflagellar transport protein 70A1|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8 ^@ http://purl.uniprot.org/annotation/PRO_0000333202 http://togogenome.org/gene/10090:Mrpl23 ^@ http://purl.uniprot.org/uniprot/O35972 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Large ribosomal subunit protein uL23m ^@ http://purl.uniprot.org/annotation/PRO_0000129485 http://togogenome.org/gene/10090:Gpc2 ^@ http://purl.uniprot.org/uniprot/Q8BKV1 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||GPI-anchor amidated serine|||Glypican-2|||O-linked (Xyl...) (heparan sulfate) serine|||Removed in mature form|||Secreted glypican-2 ^@ http://purl.uniprot.org/annotation/PRO_0000012305|||http://purl.uniprot.org/annotation/PRO_0000012306|||http://purl.uniprot.org/annotation/PRO_0000333842 http://togogenome.org/gene/10090:Sertad2 ^@ http://purl.uniprot.org/uniprot/Q3UGZ1|||http://purl.uniprot.org/uniprot/Q9JJG5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Nuclear export signal (NES)|||Polar residues|||Required for transactivation activity|||SERTA|||SERTA domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000191614 http://togogenome.org/gene/10090:Peak1 ^@ http://purl.uniprot.org/uniprot/Q69Z38 ^@ 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|||Inactive tyrosine-protein kinase PEAK1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Required for homodimerization ^@ http://purl.uniprot.org/annotation/PRO_0000250590 http://togogenome.org/gene/10090:Lmntd2 ^@ http://purl.uniprot.org/uniprot/B7ZMW1|||http://purl.uniprot.org/uniprot/Q0VET5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||LTD|||Lamin tail domain-containing protein 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000251930 http://togogenome.org/gene/10090:Nt5m ^@ http://purl.uniprot.org/uniprot/Q8VCE6 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Transit Peptide ^@ 5'(3')-deoxyribonucleotidase, mitochondrial|||Mitochondrion|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000000012 http://togogenome.org/gene/10090:Wtap ^@ http://purl.uniprot.org/uniprot/E0CYH0|||http://purl.uniprot.org/uniprot/Q9ER69 ^@ 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.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pre-mRNA-splicing regulator WTAP ^@ http://purl.uniprot.org/annotation/PRO_0000065984|||http://purl.uniprot.org/annotation/VSP_010280|||http://purl.uniprot.org/annotation/VSP_010281 http://togogenome.org/gene/10090:Fcna ^@ http://purl.uniprot.org/uniprot/O70165|||http://purl.uniprot.org/uniprot/Q4FJM1 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Site ^@ A domain; contributes to trimerization|||B domain; contributes to trimerization|||Collagen-like|||Disordered|||Fibrinogen C-terminal|||Ficolin-1|||Mediates specificity for sialic acids|||N-linked (GlcNAc...) asparagine|||P domain ^@ http://purl.uniprot.org/annotation/PRO_0000009137|||http://purl.uniprot.org/annotation/PRO_5014309350 http://togogenome.org/gene/10090:Spata48 ^@ http://purl.uniprot.org/uniprot/Q5NC83 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||Protein SPMIP7 ^@ http://purl.uniprot.org/annotation/PRO_0000331496|||http://purl.uniprot.org/annotation/VSP_033234 http://togogenome.org/gene/10090:Gm13276 ^@ http://purl.uniprot.org/uniprot/A0A087WR18 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5039969353 http://togogenome.org/gene/10090:Plbd1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0B2|||http://purl.uniprot.org/uniprot/Q8VCI0 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) (high mannose) asparagine; alternate|||N-linked (GlcNAc...) (hybrid) asparagine; alternate|||Phospholipase B-like|||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_0000286107|||http://purl.uniprot.org/annotation/PRO_0000425425|||http://purl.uniprot.org/annotation/PRO_0000425426|||http://purl.uniprot.org/annotation/PRO_0000425427|||http://purl.uniprot.org/annotation/PRO_0000425428|||http://purl.uniprot.org/annotation/PRO_5011330537 http://togogenome.org/gene/10090:Vars2 ^@ http://purl.uniprot.org/uniprot/Q3U2A8 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Transit Peptide ^@ 'HIGH' region|||'KMSKS' region|||Disordered|||Mitochondrion|||N6-acetyllysine|||Valine--tRNA ligase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000338002 http://togogenome.org/gene/10090:5530400C23Rik ^@ http://purl.uniprot.org/uniprot/Q9D3I0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099678 http://togogenome.org/gene/10090:Inppl1 ^@ http://purl.uniprot.org/uniprot/Q6P549 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes both enzyme activity and ability to inhibit PKB activity.|||Abolishes interaction with EPHA2 SAM domain.|||Basic and acidic residues|||Disordered|||Does not affect the ability to inhibit PKB activity.|||Induces little effect.|||NPXY motif|||Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pro residues|||SAM|||SH2|||SH3-binding|||Still partially active. ^@ http://purl.uniprot.org/annotation/PRO_0000302871 http://togogenome.org/gene/10090:Adam11 ^@ http://purl.uniprot.org/uniprot/Q3TZE2|||http://purl.uniprot.org/uniprot/Q7TQG7|||http://purl.uniprot.org/uniprot/Q9R1V4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 11|||Disordered|||EGF-like|||Extracellular|||Helical|||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_0000029076|||http://purl.uniprot.org/annotation/PRO_0000029077|||http://purl.uniprot.org/annotation/PRO_5004229701|||http://purl.uniprot.org/annotation/PRO_5015098856 http://togogenome.org/gene/10090:Tbx19 ^@ http://purl.uniprot.org/uniprot/Q99ME7 ^@ Chain|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||DNA Binding ^@ T-box|||T-box transcription factor TBX19 ^@ http://purl.uniprot.org/annotation/PRO_0000184450 http://togogenome.org/gene/10090:Fam221a ^@ http://purl.uniprot.org/uniprot/Q8C790 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Polar residues|||Protein FAM221A ^@ http://purl.uniprot.org/annotation/PRO_0000295140|||http://purl.uniprot.org/annotation/VSP_026740|||http://purl.uniprot.org/annotation/VSP_026741 http://togogenome.org/gene/10090:Rap1gds1 ^@ http://purl.uniprot.org/uniprot/E9Q912 ^@ 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|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Prevents binding to prenylated RHOA|||Rap1 GTPase-GDP dissociation stimulator 1 ^@ http://purl.uniprot.org/annotation/PRO_0000452472|||http://purl.uniprot.org/annotation/VSP_061008|||http://purl.uniprot.org/annotation/VSP_061009 http://togogenome.org/gene/10090:Wdr24 ^@ http://purl.uniprot.org/uniprot/Q8CFJ9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Zinc Finger ^@ Basic and acidic residues|||C4-type|||Disordered|||GATOR2 complex protein WDR24|||In delta-Ring; knockin mice show embryonic lethality due to impaired mTORC1 activation.|||Knockin mice display higher mTORC1 activity under fasting.|||Mimics phosphorylation; knockin mice are lethal due to decreased mTOC1 activity.|||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_0000051376 http://togogenome.org/gene/10090:Mrpl58 ^@ http://purl.uniprot.org/uniprot/Q8R035 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Modified Residue|||Splice Variant|||Strand|||Transit Peptide|||Turn ^@ In isoform 2.|||Large ribosomal subunit protein mL62|||Mitochondrion|||N5-methylglutamine ^@ http://purl.uniprot.org/annotation/PRO_0000030340|||http://purl.uniprot.org/annotation/VSP_014374 http://togogenome.org/gene/10090:Or5t7 ^@ http://purl.uniprot.org/uniprot/Q8VFL9 ^@ 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 5T7 ^@ http://purl.uniprot.org/annotation/PRO_0000150866 http://togogenome.org/gene/10090:Pcdhga2 ^@ http://purl.uniprot.org/uniprot/Q91XY6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099538 http://togogenome.org/gene/10090:Gpr108 ^@ http://purl.uniprot.org/uniprot/Q91WD0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||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|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein GPR108 ^@ http://purl.uniprot.org/annotation/PRO_0000045084|||http://purl.uniprot.org/annotation/VSP_016607 http://togogenome.org/gene/10090:AI467606 ^@ http://purl.uniprot.org/uniprot/Q8C708 ^@ 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|||Phosphothreonine|||Polar residues|||Transmembrane protein C16orf54 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000279443 http://togogenome.org/gene/10090:Tspan10 ^@ http://purl.uniprot.org/uniprot/Q3UFS7|||http://purl.uniprot.org/uniprot/Q3UGA5 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Cabyr ^@ http://purl.uniprot.org/uniprot/Q3KNH8|||http://purl.uniprot.org/uniprot/Q9D424 ^@ 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 ^@ Calcium-binding tyrosine phosphorylation-regulated protein|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Pro residues|||RIIa ^@ http://purl.uniprot.org/annotation/PRO_0000089270|||http://purl.uniprot.org/annotation/VSP_016252|||http://purl.uniprot.org/annotation/VSP_016253|||http://purl.uniprot.org/annotation/VSP_016254|||http://purl.uniprot.org/annotation/VSP_016255 http://togogenome.org/gene/10090:Thnsl2 ^@ http://purl.uniprot.org/uniprot/Q80W22 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ N6-(pyridoxal phosphate)lysine|||Threonine synthase-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000306408 http://togogenome.org/gene/10090:Lman1 ^@ http://purl.uniprot.org/uniprot/Q9D0F3 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||ER export motif|||Helical|||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_0000017661 http://togogenome.org/gene/10090:Rerg ^@ http://purl.uniprot.org/uniprot/Q8R367 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Ras-related and estrogen-regulated growth inhibitor ^@ http://purl.uniprot.org/annotation/PRO_0000082724 http://togogenome.org/gene/10090:Scgb2b7 ^@ http://purl.uniprot.org/uniprot/D3YYY1 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015088514 http://togogenome.org/gene/10090:Yars ^@ http://purl.uniprot.org/uniprot/A2A7S7|||http://purl.uniprot.org/uniprot/Q91WQ3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ 'HIGH' region|||'KMSKS' region|||Disordered|||N-acetylglycine; in Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Removed; alternate|||TRNA-binding|||Tyrosine--tRNA ligase, cytoplasmic|||Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed|||tRNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000055674|||http://purl.uniprot.org/annotation/PRO_0000423286 http://togogenome.org/gene/10090:Ghsr ^@ http://purl.uniprot.org/uniprot/Q0VBE5|||http://purl.uniprot.org/uniprot/Q99P50 ^@ 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|||Growth hormone secretagogue receptor type 1|||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_0000069480 http://togogenome.org/gene/10090:Gcnt1 ^@ http://purl.uniprot.org/uniprot/Q09324 ^@ 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|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase|||Catalytic|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Loss of catalytic activity; when associated with S-217 and A-378. Abolishes binding to UDP-GlcNAc; when associated with S-217.|||Loss of catalytic activity; when associated with S-217 and A-401. Reduces the affinity for UDP-GlcNAc; when associated with S-217.|||Lumenal|||Mediates interaction with GOLPH3 and is necessary and sufficient for localization to the Golgi|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Protects from inactivation caused by air oxidation or thiol-reactive agents. Reduces the affinity for UDP-GlcNAc; when associated with A-378. Abolishes binding to UDP-GlcNAc; when associated with A-401. Loss of catalytic activity; when associated with A-378 and A-401.|||Stem region ^@ http://purl.uniprot.org/annotation/PRO_0000191396 http://togogenome.org/gene/10090:Mipep ^@ http://purl.uniprot.org/uniprot/A6H611 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Mitochondrial intermediate peptidase|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000319045 http://togogenome.org/gene/10090:Cidec ^@ http://purl.uniprot.org/uniprot/P56198 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolished ability to bind acidic phospholipids and inhibit lipid droplet fusion.|||Abolished ability to mediate lipid droplet fusion.|||Abolished ability to undergo liquid-liquid phase separation (LLPS).|||Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits and inhibits lipid droplet enlargement. No effect on homodimerization.|||Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits.|||Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-182 and A-186.|||Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-182 and A-190.|||Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-186 and A-190.|||CIDE-N|||Does not affect ability to mediate lipid droplet fusion.|||Inhibits interaction with PLIN1; when associated with A-75.|||Inhibits interaction with PLIN1; when associated with A-77.|||Lipid transferase CIDEC|||No effect on protein stability. Drastically increased protein stability and decreased ubiquitination; when associated with A-224 and A-226.|||No effect on protein stability; when associated with A-226. Drastically increased protein stability and decreased ubiquitination; when associated with A-224 and A-236.|||No effect on protein stability; when associated with A-226. Drastically increased protein stability and decreased ubiquitination; when associated with A-226 and A-236.|||RKKR polybasic motif|||Reduces CIDE-N/CIDE-N interaction between the 2 homodimer subunits and inhibits lipid droplet enlargement.|||Required for liquid-liquid phase separation (LLPS)|||Slightly inhibits interaction with PLIN1.|||Slightly inhibits interaction with PLIN1; when associated with A-112 or A-117.|||Slightly inhibits interaction with PLIN1; when associated with A-115. ^@ http://purl.uniprot.org/annotation/PRO_0000144723 http://togogenome.org/gene/10090:Smcp ^@ http://purl.uniprot.org/uniprot/P15265 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Phosphoserine|||Sperm mitochondrial-associated cysteine-rich protein ^@ http://purl.uniprot.org/annotation/PRO_0000096308 http://togogenome.org/gene/10090:Or4p7 ^@ http://purl.uniprot.org/uniprot/Q7TR20 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kcnk15 ^@ http://purl.uniprot.org/uniprot/B2RVL1 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Potassium channel ^@ http://togogenome.org/gene/10090:Evi2 ^@ http://purl.uniprot.org/uniprot/Q8VD58 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein EVI2B ^@ http://purl.uniprot.org/annotation/PRO_0000021214 http://togogenome.org/gene/10090:Otof ^@ http://purl.uniprot.org/uniprot/A0A0R4J1K2|||http://purl.uniprot.org/uniprot/A0A2Z2CEU0|||http://purl.uniprot.org/uniprot/E9PYR6|||http://purl.uniprot.org/uniprot/Q9ESF1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||C2|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||C2 6|||C2 7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||Otoferlin ^@ http://purl.uniprot.org/annotation/PRO_0000057882|||http://purl.uniprot.org/annotation/VSP_001512|||http://purl.uniprot.org/annotation/VSP_001513|||http://purl.uniprot.org/annotation/VSP_001514 http://togogenome.org/gene/10090:Amy2a5 ^@ http://purl.uniprot.org/uniprot/P00688 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ In A1 and B(C).|||In A1, B(A) and B(C).|||In A1, B(A) and B(C); requires 2 nucleotide substitutions.|||In A1, B(C) and AMY-2.2Y.|||In AMY-2.2Y.|||In B(A).|||In B(C).|||In B1.|||Nucleophile|||Pancreatic alpha-amylase 2a5|||Proton donor|||Pyrrolidone carboxylic acid|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000001398 http://togogenome.org/gene/10090:Plekha1 ^@ http://purl.uniprot.org/uniprot/Q8BUL6 ^@ 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.|||PH 1|||PH 2|||Phosphoserine|||Pleckstrin homology domain-containing family A member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000053874|||http://purl.uniprot.org/annotation/VSP_009764|||http://purl.uniprot.org/annotation/VSP_009767 http://togogenome.org/gene/10090:Lgi3 ^@ http://purl.uniprot.org/uniprot/Q3V1R3|||http://purl.uniprot.org/uniprot/Q8K406 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide ^@ EAR|||EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||EAR 7|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||LRRCT domain-containing protein|||LRRNT|||Leucine-rich repeat LGI family member 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017711|||http://purl.uniprot.org/annotation/PRO_5004230475 http://togogenome.org/gene/10090:Tmem276 ^@ http://purl.uniprot.org/uniprot/P0DW86 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||Transmembrane protein 276 ^@ http://purl.uniprot.org/annotation/PRO_0000456484 http://togogenome.org/gene/10090:Maip1 ^@ http://purl.uniprot.org/uniprot/Q8BHE8 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Mitochondrion|||m-AAA protease-interacting protein 1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000301946 http://togogenome.org/gene/10090:Hells ^@ http://purl.uniprot.org/uniprot/Q60848 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Lymphocyte-specific helicase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000260052|||http://purl.uniprot.org/annotation/VSP_052235 http://togogenome.org/gene/10090:S100a7a ^@ http://purl.uniprot.org/uniprot/Q6S5I3 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ EF-hand|||Protein S100-A15A ^@ http://purl.uniprot.org/annotation/PRO_0000320087 http://togogenome.org/gene/10090:Bmp2k ^@ http://purl.uniprot.org/uniprot/Q91Z96 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Acidic residues|||BMP-2-inducible protein kinase|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085664|||http://purl.uniprot.org/annotation/VSP_008094|||http://purl.uniprot.org/annotation/VSP_008095 http://togogenome.org/gene/10090:Zfp30 ^@ http://purl.uniprot.org/uniprot/Q60585|||http://purl.uniprot.org/uniprot/Q78FW7 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000047292 http://togogenome.org/gene/10090:Ddx23 ^@ http://purl.uniprot.org/uniprot/D3Z0M9 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Basic and acidic residues|||Basic residues|||DEAD-box RNA helicase Q|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Q motif ^@ http://togogenome.org/gene/10090:Or51h1 ^@ http://purl.uniprot.org/uniprot/E9Q547 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Drd5 ^@ http://purl.uniprot.org/uniprot/B2RQS5|||http://purl.uniprot.org/uniprot/Q8BLD9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||D(1B) dopamine receptor|||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|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069407 http://togogenome.org/gene/10090:Aph1c ^@ http://purl.uniprot.org/uniprot/Q9DCZ9 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Putative gamma-secretase subunit APH-1C ^@ http://purl.uniprot.org/annotation/PRO_0000221055 http://togogenome.org/gene/10090:Blm ^@ http://purl.uniprot.org/uniprot/E9PZ97|||http://purl.uniprot.org/uniprot/O88700 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ 3' overhang DNA-binding|||3' overhang DNA-binding; via amide nitrogen|||Acidic residues|||Basic residues|||DEAH box|||DNA Holliday junction binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HRDC|||Helicase ATP-binding|||Helicase C-terminal|||N6-acetyllysine|||Necessary for dimerization and homooligomerization|||Necessary for ssDNA and DNA Holliday junction binding|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||RecQ-like DNA helicase BLM|||Reduced ATPase and helicase activities.|||Reduces TRIM25-mediated ubiquitination in response to DNA damage. Reduces recruitment of BLM to replication forks and impairs the restart of stalled replication forks. ^@ http://purl.uniprot.org/annotation/PRO_0000205040 http://togogenome.org/gene/10090:Map3k9 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VKX4|||http://purl.uniprot.org/uniprot/Q3U1V8 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Leucine-zipper 1|||Leucine-zipper 2|||Mitogen-activated protein kinase kinase kinase 9|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000277825 http://togogenome.org/gene/10090:Gm21992 ^@ http://purl.uniprot.org/uniprot/B0LM42|||http://purl.uniprot.org/uniprot/F7BGR7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ CCHC-type|||RRM ^@ http://togogenome.org/gene/10090:Trnau1ap ^@ http://purl.uniprot.org/uniprot/Q80VC6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ RRM 1|||RRM 2|||tRNA selenocysteine 1-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000304918 http://togogenome.org/gene/10090:Rhox2c ^@ http://purl.uniprot.org/uniprot/A2AWL9|||http://purl.uniprot.org/uniprot/V9GXB9 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Myrfl ^@ http://purl.uniprot.org/uniprot/Q3UN70 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Myelin regulatory factor-like protein|||NDT80|||Peptidase S74|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000420956 http://togogenome.org/gene/10090:H2al1i ^@ http://purl.uniprot.org/uniprot/Q5M8Q2 ^@ Chain|||Molecule Processing ^@ Chain ^@ Histone H2A-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000440627 http://togogenome.org/gene/10090:Slc22a21 ^@ http://purl.uniprot.org/uniprot/A2RSK7|||http://purl.uniprot.org/uniprot/Q9WTN6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||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|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Polar residues|||Solute carrier family 22 member 21 ^@ http://purl.uniprot.org/annotation/PRO_0000220506 http://togogenome.org/gene/10090:Krtap8-1 ^@ http://purl.uniprot.org/uniprot/O08633 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ 11 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 8-1 ^@ http://purl.uniprot.org/annotation/PRO_0000185186 http://togogenome.org/gene/10090:Slc35f4 ^@ http://purl.uniprot.org/uniprot/B2RSS2|||http://purl.uniprot.org/uniprot/Q8BZK4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||EamA|||Helical|||In isoform 2.|||In isoform 3.|||Solute carrier family 35 member F4 ^@ http://purl.uniprot.org/annotation/PRO_0000311966|||http://purl.uniprot.org/annotation/VSP_029670|||http://purl.uniprot.org/annotation/VSP_029671|||http://purl.uniprot.org/annotation/VSP_029672|||http://purl.uniprot.org/annotation/VSP_029673 http://togogenome.org/gene/10090:Dnajc22 ^@ http://purl.uniprot.org/uniprot/Q8CHS2 ^@ 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_0000325863 http://togogenome.org/gene/10090:Sap30l ^@ http://purl.uniprot.org/uniprot/Q5SQF8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Modified Residue|||Motif|||Region|||Zinc Finger ^@ Atypical|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone deacetylase complex subunit SAP30L|||Important for DNA and phosphoinositide binding|||N-acetylmethionine|||Nuclear localization signal (NLS)|||Phosphoserine|||Redox-active ^@ http://purl.uniprot.org/annotation/PRO_0000309501 http://togogenome.org/gene/10090:Opn4 ^@ http://purl.uniprot.org/uniprot/Q9QXZ9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||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|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000197816|||http://purl.uniprot.org/annotation/VSP_045928 http://togogenome.org/gene/10090:Gpd1l ^@ http://purl.uniprot.org/uniprot/B2RSR7|||http://purl.uniprot.org/uniprot/Q3ULJ0 ^@ 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 ^@ Glycerol-3-phosphate dehydrogenase 1-like protein|||Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal|||Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal|||In isoform 2.|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000286512|||http://purl.uniprot.org/annotation/VSP_025062 http://togogenome.org/gene/10090:Fbxw19 ^@ http://purl.uniprot.org/uniprot/Q8C2W8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Prrg1 ^@ http://purl.uniprot.org/uniprot/A2BFE8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||Gla|||Helical ^@ http://togogenome.org/gene/10090:Nek9 ^@ http://purl.uniprot.org/uniprot/Q69Z43|||http://purl.uniprot.org/uniprot/Q8K1R7 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Interaction with NEK6|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||RCC1|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||Removed|||Serine/threonine-protein kinase Nek9 ^@ http://purl.uniprot.org/annotation/PRO_0000086436 http://togogenome.org/gene/10090:Sox7 ^@ http://purl.uniprot.org/uniprot/P40646|||http://purl.uniprot.org/uniprot/Q3U1W5 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Mutagenesis Site|||Region ^@ Disordered|||HMG box|||Loss of beta-catenin-binding.|||Required for beta-catenin-binding|||Sox C-terminal|||Transcription factor SOX-7 ^@ http://purl.uniprot.org/annotation/PRO_0000048732 http://togogenome.org/gene/10090:Bard1 ^@ http://purl.uniprot.org/uniprot/O70445 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Zinc Finger ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4; degenerate|||BRCA1-associated RING domain protein 1|||BRCT 1|||BRCT 2|||Basic and acidic residues|||Disordered|||Flexible linker|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type|||Required for BRCA1 binding ^@ http://purl.uniprot.org/annotation/PRO_0000055820 http://togogenome.org/gene/10090:Or9g4b ^@ http://purl.uniprot.org/uniprot/Q7TR94 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pdzph1 ^@ http://purl.uniprot.org/uniprot/Q8BGR1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||PDZ|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Aqp3 ^@ http://purl.uniprot.org/uniprot/Q8R2N1 ^@ Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Aquaporin-3|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000063944 http://togogenome.org/gene/10090:Klk5 ^@ http://purl.uniprot.org/uniprot/Q9D140 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Peptidase S1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015099671 http://togogenome.org/gene/10090:Trim36 ^@ http://purl.uniprot.org/uniprot/E9Q3A0|||http://purl.uniprot.org/uniprot/Q80WG7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||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 Trim36|||Fibronectin type-III|||RING-type|||RING-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000056253 http://togogenome.org/gene/10090:Ccdc78 ^@ http://purl.uniprot.org/uniprot/D3Z5T1 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil ^@ Coiled-coil domain-containing protein 78 ^@ http://purl.uniprot.org/annotation/PRO_0000415805 http://togogenome.org/gene/10090:Ndufa4 ^@ http://purl.uniprot.org/uniprot/Q62425 ^@ 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_0000118822 http://togogenome.org/gene/10090:Gast ^@ http://purl.uniprot.org/uniprot/P48757 ^@ Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Compositionally Biased Region|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Big gastrin|||Disordered|||Gastrin|||Gastrin-71|||Phenylalanine amide|||Phosphoserine|||Polar residues|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000010640|||http://purl.uniprot.org/annotation/PRO_0000010641|||http://purl.uniprot.org/annotation/PRO_0000010642|||http://purl.uniprot.org/annotation/PRO_0000010643 http://togogenome.org/gene/10090:Pip5kl1 ^@ http://purl.uniprot.org/uniprot/Q6U7H8 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||No effect on lipid kinase activity observed when the protein is purified from mammalian cell extracts; when associated with R-155.|||No effect on lipid kinase activity when the protein is purified from mammalian cell extracts. No effect on lipid kinase activity when the protein is purified from mammalian cell extracts; when associated with A-281.|||PIPK|||Phosphatidylinositol 4-phosphate 5-kinase-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000285759|||http://purl.uniprot.org/annotation/VSP_024905|||http://purl.uniprot.org/annotation/VSP_024906|||http://purl.uniprot.org/annotation/VSP_024907|||http://purl.uniprot.org/annotation/VSP_024908|||http://purl.uniprot.org/annotation/VSP_024909 http://togogenome.org/gene/10090:Ly6a ^@ http://purl.uniprot.org/uniprot/P05533 ^@ 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 glycine|||In Ly-6E.1.|||Lymphocyte antigen 6A-2/6E-1|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036130|||http://purl.uniprot.org/annotation/PRO_0000036131 http://togogenome.org/gene/10090:Or4d5 ^@ http://purl.uniprot.org/uniprot/Q8VFN1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bbx ^@ http://purl.uniprot.org/uniprot/Q8VBW5 ^@ 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|||Strand ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand ^@ 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.|||In isoform 4.|||In strain: C3H/He.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000232886|||http://purl.uniprot.org/annotation/VSP_018007|||http://purl.uniprot.org/annotation/VSP_018008|||http://purl.uniprot.org/annotation/VSP_018009|||http://purl.uniprot.org/annotation/VSP_018010|||http://purl.uniprot.org/annotation/VSP_018011|||http://purl.uniprot.org/annotation/VSP_018012 http://togogenome.org/gene/10090:Tfeb ^@ http://purl.uniprot.org/uniprot/Q3UKG7|||http://purl.uniprot.org/uniprot/Q6P203|||http://purl.uniprot.org/uniprot/Q8C5F1|||http://purl.uniprot.org/uniprot/Q9R210 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Abolished alkylation in knockin mice. Mice display elevated susceptibility to S.typhimurium infection.|||BHLH|||Disordered|||Leucine-zipper|||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_0000127474 http://togogenome.org/gene/10090:Zgrf1 ^@ http://purl.uniprot.org/uniprot/Q0VGT4|||http://purl.uniprot.org/uniprot/Q8BQU5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Basic and acidic residues|||DNA2/NAM7 helicase helicase|||DNA2/NAM7 helicase-like C-terminal|||Disordered|||GRF-type|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein ZGRF1 ^@ http://purl.uniprot.org/annotation/PRO_0000286627|||http://purl.uniprot.org/annotation/VSP_053245|||http://purl.uniprot.org/annotation/VSP_053246 http://togogenome.org/gene/10090:Unc5c ^@ http://purl.uniprot.org/uniprot/O08747|||http://purl.uniprot.org/uniprot/Q3UQ08|||http://purl.uniprot.org/uniprot/Q3URW2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes interaction with PTPN11, leading to an increased level of phosphorylation.|||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 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_0000036076|||http://purl.uniprot.org/annotation/PRO_5004230271|||http://purl.uniprot.org/annotation/PRO_5014309223|||http://purl.uniprot.org/annotation/VSP_011702 http://togogenome.org/gene/10090:Bcl2a1a ^@ http://purl.uniprot.org/uniprot/Q07440 ^@ Chain|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Turn ^@ Chain|||Helix|||Motif|||Turn ^@ BH1|||BH2|||Bcl-2-related protein A1 ^@ http://purl.uniprot.org/annotation/PRO_0000143095 http://togogenome.org/gene/10090:1700017B05Rik ^@ http://purl.uniprot.org/uniprot/Q3TEI4 ^@ 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.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Uncharacterized protein C15orf39 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000244344|||http://purl.uniprot.org/annotation/VSP_019542 http://togogenome.org/gene/10090:Actr1b ^@ http://purl.uniprot.org/uniprot/Q8R5C5 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ 3'-nitrotyrosine|||Beta-centractin|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000089061 http://togogenome.org/gene/10090:Tmem30c ^@ http://purl.uniprot.org/uniprot/Q9D4D7 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cell cycle control protein 50C|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000292847 http://togogenome.org/gene/10090:Nbn ^@ http://purl.uniprot.org/uniprot/Q9R207 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ BRCT|||Basic and acidic residues|||Disordered|||EEXXXDDL motif|||FHA|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with MTOR, MAPKAP1 and RICTOR|||Mediates interaction with SP100|||Nibrin|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000231044 http://togogenome.org/gene/10090:Med28 ^@ http://purl.uniprot.org/uniprot/Q920D3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Mediator of RNA polymerase II transcription subunit 28|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000113982 http://togogenome.org/gene/10090:Has3 ^@ http://purl.uniprot.org/uniprot/O08650 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis 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|||Hyaluronan synthase 3|||N-linked (GlcNAc...) asparagine|||Not detectable on the plasma membrane. Abolishes hyaluronan synthase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000197179 http://togogenome.org/gene/10090:Rcc2 ^@ http://purl.uniprot.org/uniprot/Q8BK67 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Region|||Repeat ^@ Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Protein RCC2|||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_0000206653 http://togogenome.org/gene/10090:Ifna15 ^@ http://purl.uniprot.org/uniprot/Q61718 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015098101 http://togogenome.org/gene/10090:Serpina10 ^@ http://purl.uniprot.org/uniprot/Q8R121 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn ^@ 2-fold decrease in rates of factor Xa inhibition.|||400-fold decrease in rates of factor Xa inhibition.|||5-fold decrease in rates of factor Xa inhibition.|||50-fold decrease in rates of factor Xa inhibition.|||Acidic residues|||Disordered|||Essential for interaction with PROZ|||Heparin-binding|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No change in rates of factor Xa inhibition.|||Protein Z-dependent protease inhibitor|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000032483|||http://purl.uniprot.org/annotation/VSP_014439 http://togogenome.org/gene/10090:Zfp729b ^@ http://purl.uniprot.org/uniprot/Q80VN4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Hspe1 ^@ http://purl.uniprot.org/uniprot/Q64433 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ 10 kDa heat shock protein, mitochondrial|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000174918 http://togogenome.org/gene/10090:Ssr1 ^@ http://purl.uniprot.org/uniprot/Q9CY50 ^@ 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 ^@ Acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Translocon-associated protein subunit alpha ^@ http://purl.uniprot.org/annotation/PRO_0000033282 http://togogenome.org/gene/10090:H4c18 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Psca ^@ http://purl.uniprot.org/uniprot/P57096 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ GPI-anchor amidated asparagine|||N-linked (GlcNAc...) asparagine|||Prostate stem cell antigen|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036164|||http://purl.uniprot.org/annotation/PRO_0000036165 http://togogenome.org/gene/10090:Dctd ^@ http://purl.uniprot.org/uniprot/G3X908|||http://purl.uniprot.org/uniprot/Q8K2D6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ CMP/dCMP-type deaminase|||Deoxycytidylate deaminase|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000171692 http://togogenome.org/gene/10090:Ccdc13 ^@ http://purl.uniprot.org/uniprot/D3YV10|||http://purl.uniprot.org/uniprot/Q3TYG3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Coiled-coil domain-containing protein 13|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000431958 http://togogenome.org/gene/10090:Fabp5 ^@ http://purl.uniprot.org/uniprot/Q05816|||http://purl.uniprot.org/uniprot/Q497I3 ^@ 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|||Strand ^@ Cytosolic fatty-acid binding proteins|||Fatty acid-binding protein 5|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067378 http://togogenome.org/gene/10090:Pla2r1 ^@ http://purl.uniprot.org/uniprot/Q62028|||http://purl.uniprot.org/uniprot/Q8CB47 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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|||Disordered|||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_0000311251|||http://purl.uniprot.org/annotation/PRO_5000139804|||http://purl.uniprot.org/annotation/VSP_029495|||http://purl.uniprot.org/annotation/VSP_029496 http://togogenome.org/gene/10090:Rex1bd ^@ http://purl.uniprot.org/uniprot/Q9CYZ6 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Required for excision 1-B domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000305286 http://togogenome.org/gene/10090:Nek5 ^@ http://purl.uniprot.org/uniprot/Q7TSC3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek5 ^@ http://purl.uniprot.org/annotation/PRO_0000259766|||http://purl.uniprot.org/annotation/VSP_021531|||http://purl.uniprot.org/annotation/VSP_021532|||http://purl.uniprot.org/annotation/VSP_021533 http://togogenome.org/gene/10090:Zfp282 ^@ http://purl.uniprot.org/uniprot/E9PVC2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Potefam3a ^@ http://purl.uniprot.org/uniprot/E9Q637 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ ANK|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Taco1 ^@ http://purl.uniprot.org/uniprot/Q8K0Z7 ^@ Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ N6-acetyllysine|||Translational activator of cytochrome c oxidase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000175943 http://togogenome.org/gene/10090:Or5b101 ^@ http://purl.uniprot.org/uniprot/Q8VFX0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tpd52l1 ^@ http://purl.uniprot.org/uniprot/O54818 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tumor protein D53 ^@ http://purl.uniprot.org/annotation/PRO_0000185742 http://togogenome.org/gene/10090:Cited1 ^@ http://purl.uniprot.org/uniprot/P97769|||http://purl.uniprot.org/uniprot/Q3UGA1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Motif|||Region ^@ Cbp/p300-interacting transactivator 1|||Disordered|||Nuclear export signal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000144725 http://togogenome.org/gene/10090:Usp7 ^@ http://purl.uniprot.org/uniprot/E9PXY8|||http://purl.uniprot.org/uniprot/F8VPX1|||http://purl.uniprot.org/uniprot/Q6A4J8 ^@ Active 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 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ 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 isoform 2.|||In isoform 3.|||Interaction with TSPYL5|||Interaction with p53/TP53 and MDM2|||Loss of p53/TP53-deubiquitinating activity.|||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_0000268006|||http://purl.uniprot.org/annotation/VSP_021952|||http://purl.uniprot.org/annotation/VSP_021953|||http://purl.uniprot.org/annotation/VSP_021954 http://togogenome.org/gene/10090:Or5m3 ^@ http://purl.uniprot.org/uniprot/A2ATE5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:4921524L21Rik ^@ http://purl.uniprot.org/uniprot/Q9D5T2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF3496|||Disordered ^@ http://togogenome.org/gene/10090:Dsn1 ^@ http://purl.uniprot.org/uniprot/Q9CYC5 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Kinetochore-associated protein DSN1 homolog|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000079482 http://togogenome.org/gene/10090:Lysmd4 ^@ http://purl.uniprot.org/uniprot/Q8CC84 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||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_0000248014|||http://purl.uniprot.org/annotation/VSP_020129 http://togogenome.org/gene/10090:C1qtnf5 ^@ http://purl.uniprot.org/uniprot/Q4ZJN4|||http://purl.uniprot.org/uniprot/Q8K479|||http://purl.uniprot.org/uniprot/Q8K480 ^@ 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 ^@ Basic and acidic residues|||C1q|||CUB 1|||CUB 2|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 5|||Cytoplasmic|||Disordered|||Extracellular|||FZ|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||LDL-receptor class A 1|||LDL-receptor class A 2|||Membrane frizzled-related protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000003536|||http://purl.uniprot.org/annotation/PRO_0000228133|||http://purl.uniprot.org/annotation/PRO_5011946675|||http://purl.uniprot.org/annotation/VSP_017664 http://togogenome.org/gene/10090:Tyrobp ^@ http://purl.uniprot.org/uniprot/O54885|||http://purl.uniprot.org/uniprot/Q3U419 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Abolishes phosphorylation and ability to regulate cytoskeletal organization; when associated with F-103.|||Abolishes phosphorylation and ability to regulate cytoskeletal organization; when associated with F-92.|||Cytoplasmic|||Disordered|||Extracellular|||Failure to rescue cytoskeletal defects when introduced into TYROBP-deficient cells.|||Helical|||ITAM|||Important for interaction with transmembrane receptors|||Interchain|||Phosphotyrosine|||Polar residues|||TYRO protein tyrosine kinase-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000022605|||http://purl.uniprot.org/annotation/PRO_5014309174 http://togogenome.org/gene/10090:Vmn1r250 ^@ http://purl.uniprot.org/uniprot/K7N6B8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnnm2 ^@ http://purl.uniprot.org/uniprot/Q3TWN3 ^@ Chain|||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|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ CBS 1|||CBS 2|||CNNM transmembrane|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Impairs N-terminal cleavage.|||In isoform 2.|||Loss of N-glycosylation; 90% decrease of plasma membrane expression.|||Metal transporter CNNM2|||N-linked (GlcNAc...) asparagine|||No effect on N-glycosylation.|||No effect on N-terminal cleavage.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000295761|||http://purl.uniprot.org/annotation/VSP_027081 http://togogenome.org/gene/10090:Chrne ^@ http://purl.uniprot.org/uniprot/P20782|||http://purl.uniprot.org/uniprot/Q5SXG9 ^@ 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 ^@ Acetylcholine receptor subunit epsilon|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000330|||http://purl.uniprot.org/annotation/PRO_5022270154 http://togogenome.org/gene/10090:Ap3b2 ^@ http://purl.uniprot.org/uniprot/A0A571BES1|||http://purl.uniprot.org/uniprot/Q9JME5 ^@ 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 ^@ AP-3 complex subunit beta C-terminal|||AP-3 complex subunit beta-2|||Acidic residues|||Basic and acidic residues|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000193749 http://togogenome.org/gene/10090:Or52e3 ^@ http://purl.uniprot.org/uniprot/Q7TRR4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mup21 ^@ http://purl.uniprot.org/uniprot/Q80YX8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5015098931 http://togogenome.org/gene/10090:Gtf2e1 ^@ http://purl.uniprot.org/uniprot/Q9D0D5 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Zinc Finger ^@ 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_0000211223 http://togogenome.org/gene/10090:Slc4a2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J101|||http://purl.uniprot.org/uniprot/A0A0R4J1K4|||http://purl.uniprot.org/uniprot/A0A0R4J1K9|||http://purl.uniprot.org/uniprot/P13808|||http://purl.uniprot.org/uniprot/Q3UKP0|||http://purl.uniprot.org/uniprot/Q7TPS4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Anion exchange protein 2|||Band 3 cytoplasmic|||Basic and acidic residues|||Bicarbonate transporter-like transmembrane|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform B1.|||In isoform B2.|||In isoform C1.|||In isoform C2.|||Loss of activity but no effect on localization to basolateral cell membrane.|||Membrane (anion exchange)|||N-linked (GlcNAc...) asparagine|||N6-methyllysine|||Phosphoserine|||Phosphothreonine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000079216|||http://purl.uniprot.org/annotation/VSP_000457|||http://purl.uniprot.org/annotation/VSP_000458|||http://purl.uniprot.org/annotation/VSP_000459|||http://purl.uniprot.org/annotation/VSP_000460|||http://purl.uniprot.org/annotation/VSP_000461 http://togogenome.org/gene/10090:Apobec3 ^@ http://purl.uniprot.org/uniprot/E9QMH1|||http://purl.uniprot.org/uniprot/Q3TI69|||http://purl.uniprot.org/uniprot/Q3U5C5|||http://purl.uniprot.org/uniprot/Q99J72 ^@ 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 ^@ CMP/dCMP-type deaminase|||CMP/dCMP-type deaminase 1|||CMP/dCMP-type deaminase 2|||DNA dC->dU-editing enzyme APOBEC-3|||Decrease in cytidine deaminase and antiviral activity.|||Decrease in cytidine deaminase and antiviral activity; when associated with A-301.|||Decrease in cytidine deaminase and antiviral activity; when associated with A-84.|||In cell line 3T3.|||In cell line EL4.|||In cell line L1.2.|||In cell line MDTF.|||In cell line MDTF; requires 2 nucleotide substitutions.|||In cell lines L1.2 and 3T3.|||In cell lines MDTF and 3T3.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In splenocytes.|||No effect on cytidine deaminase and antiviral activity.|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000171772|||http://purl.uniprot.org/annotation/VSP_009831|||http://purl.uniprot.org/annotation/VSP_009832|||http://purl.uniprot.org/annotation/VSP_009833 http://togogenome.org/gene/10090:Stk38 ^@ http://purl.uniprot.org/uniprot/Q91VJ4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ AGC-kinase C-terminal|||Interaction with S100B|||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_0000086719 http://togogenome.org/gene/10090:Prpf18 ^@ http://purl.uniprot.org/uniprot/Q8BM39 ^@ 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|||Pre-mRNA-splicing factor 18 ^@ http://purl.uniprot.org/annotation/PRO_0000058583|||http://purl.uniprot.org/annotation/VSP_008329|||http://purl.uniprot.org/annotation/VSP_008330 http://togogenome.org/gene/10090:Sowahb ^@ http://purl.uniprot.org/uniprot/Q8BZW2 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein SOWAHB|||Basic and acidic residues|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000317241 http://togogenome.org/gene/10090:2900026A02Rik ^@ http://purl.uniprot.org/uniprot/A0A1B0GR85|||http://purl.uniprot.org/uniprot/A0A1D5RLN6|||http://purl.uniprot.org/uniprot/Q8BRV5 ^@ 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|||Pro residues|||Tankyrase 1-binding protein C-terminal|||Uncharacterized protein KIAA1671 ^@ http://purl.uniprot.org/annotation/PRO_0000287146 http://togogenome.org/gene/10090:Gusb ^@ http://purl.uniprot.org/uniprot/P12265 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Active Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ Beta-glucuronidase|||In allele GUS-SA.|||In allele W26; reduced retention in the endoplasmic reticulum.|||In strain: C3H/HeJ.|||N-linked (GlcNAc...) asparagine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000012162 http://togogenome.org/gene/10090:Or8j3c ^@ http://purl.uniprot.org/uniprot/Q7TR71 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dut ^@ http://purl.uniprot.org/uniprot/Q9CQ43 ^@ 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 ^@ Deoxyuridine 5'-triphosphate nucleotidohydrolase|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000454313|||http://purl.uniprot.org/annotation/VSP_061339 http://togogenome.org/gene/10090:Synj2bp ^@ http://purl.uniprot.org/uniprot/Q9D6K5 ^@ 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; Anchor for type IV membrane protein|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Mitochondrial intermembrane|||PDZ|||Synaptojanin-2-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000375982|||http://purl.uniprot.org/annotation/VSP_053101|||http://purl.uniprot.org/annotation/VSP_053102|||http://purl.uniprot.org/annotation/VSP_053103|||http://purl.uniprot.org/annotation/VSP_053104 http://togogenome.org/gene/10090:Fam240a ^@ http://purl.uniprot.org/uniprot/J3QNP9 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Mzb1 ^@ http://purl.uniprot.org/uniprot/Q9D8I1 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Marginal zone B- and B1-cell-specific protein|||Prevents secretion from ER|||Reduced electrophoretic mobility; when associated with A-170.|||Reduced electrophoretic mobility; when associated with A-177.|||Reduced electrophoretic mobility; when associated with A-49.|||Reduced electrophoretic mobility; when associated with A-52.|||Small loss of electrophoretic mobility. ^@ http://purl.uniprot.org/annotation/PRO_0000318741 http://togogenome.org/gene/10090:Tmem232 ^@ http://purl.uniprot.org/uniprot/A0A3B2W4C3|||http://purl.uniprot.org/uniprot/Q5K6N0 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Transmembrane protein 232 ^@ http://purl.uniprot.org/annotation/PRO_0000395036|||http://purl.uniprot.org/annotation/VSP_039353|||http://purl.uniprot.org/annotation/VSP_039354 http://togogenome.org/gene/10090:Hpse ^@ http://purl.uniprot.org/uniprot/Q6YGZ1 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Heparanase 50 kDa subunit|||Heparanase 8 kDa subunit|||Linker peptide|||N-linked (GlcNAc...) asparagine|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000042263|||http://purl.uniprot.org/annotation/PRO_0000042264|||http://purl.uniprot.org/annotation/PRO_0000042265 http://togogenome.org/gene/10090:Josd2 ^@ http://purl.uniprot.org/uniprot/Q9CR30 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ Josephin|||Josephin-2|||Nucleophile|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000053844 http://togogenome.org/gene/10090:Fcrl2 ^@ http://purl.uniprot.org/uniprot/Q9EQY5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Ig-like|||SRCR ^@ http://purl.uniprot.org/annotation/PRO_5015099715 http://togogenome.org/gene/10090:Gm11757 ^@ http://purl.uniprot.org/uniprot/A2BEI8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Robo3 ^@ http://purl.uniprot.org/uniprot/D3Z4M6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Fibronectin type-III|||Ig-like|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Nrcam ^@ http://purl.uniprot.org/uniprot/Q6QRP1|||http://purl.uniprot.org/uniprot/Q810U4 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||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.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Neurofascin/L1/NrCAM C-terminal|||Neuronal cell adhesion molecule|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000015058|||http://purl.uniprot.org/annotation/VSP_008921|||http://purl.uniprot.org/annotation/VSP_008922|||http://purl.uniprot.org/annotation/VSP_008923|||http://purl.uniprot.org/annotation/VSP_008924|||http://purl.uniprot.org/annotation/VSP_008925|||http://purl.uniprot.org/annotation/VSP_008926|||http://purl.uniprot.org/annotation/VSP_008927|||http://purl.uniprot.org/annotation/VSP_008930 http://togogenome.org/gene/10090:Wdr70 ^@ http://purl.uniprot.org/uniprot/G3X934|||http://purl.uniprot.org/uniprot/Q3TWF6 ^@ 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 SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD|||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_0000305145 http://togogenome.org/gene/10090:Atoh8 ^@ http://purl.uniprot.org/uniprot/Q99NA2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ Basic motif; degenerate|||Disordered|||Helix-loop-helix motif|||Polar residues|||Pro residues|||Transcription factor Atoh8|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000323752 http://togogenome.org/gene/10090:Ccny ^@ http://purl.uniprot.org/uniprot/Q8BGU5 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Cyclin N-terminal|||Cyclin-Y|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Phosphoserine; by CDK14|||Phosphothreonine|||Phosphothreonine; by CDK14|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000080515|||http://purl.uniprot.org/annotation/VSP_014835 http://togogenome.org/gene/10090:Rars2 ^@ http://purl.uniprot.org/uniprot/Q3U186 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Transit Peptide ^@ 'HIGH' region|||Mitochondrion|||N6-acetyllysine|||Probable arginine--tRNA ligase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000250732 http://togogenome.org/gene/10090:Cdc26 ^@ http://purl.uniprot.org/uniprot/Q99JP4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region ^@ Anaphase-promoting complex subunit CDC26|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000271195 http://togogenome.org/gene/10090:Pa2g4 ^@ http://purl.uniprot.org/uniprot/P50580|||http://purl.uniprot.org/uniprot/Q3TGU7 ^@ 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 ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with RNA|||N-acetylserine|||Necessary for nucleolar localization|||No effect on RNA-binding.|||Peptidase M24|||Phosphoserine|||Phosphoserine; by PKC/PRKCD|||Phosphothreonine|||Proliferation-associated protein 2G4|||RNA-binding|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000148990|||http://purl.uniprot.org/annotation/VSP_057326 http://togogenome.org/gene/10090:Cops5 ^@ http://purl.uniprot.org/uniprot/O35864 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site ^@ Abolishes ability to deneddylate cullins, but keeps ability to stabilize HIF1A protein.|||COP9 signalosome complex subunit 5|||JAMM motif|||MPN|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000194836 http://togogenome.org/gene/10090:Acot3 ^@ http://purl.uniprot.org/uniprot/Q53YL1|||http://purl.uniprot.org/uniprot/Q9QYR7 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Domain Extent|||Motif|||Splice Variant ^@ Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase|||Acyl-coenzyme A thioesterase 3|||BAAT/Acyl-CoA thioester hydrolase C-terminal|||Charge relay system|||In isoform 2.|||Microbody targeting signal ^@ http://purl.uniprot.org/annotation/PRO_0000202148|||http://purl.uniprot.org/annotation/VSP_010994 http://togogenome.org/gene/10090:Slc12a7 ^@ http://purl.uniprot.org/uniprot/B9EIV8|||http://purl.uniprot.org/uniprot/Q9WVL3 ^@ 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 ^@ Amino acid permease/ SLC12A|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) (high mannose) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SLC12A transporter C-terminal|||Solute carrier family 12 member 7 ^@ http://purl.uniprot.org/annotation/PRO_0000178040|||http://purl.uniprot.org/annotation/VSP_027770 http://togogenome.org/gene/10090:Hnrnpul2 ^@ http://purl.uniprot.org/uniprot/Q00PI9 ^@ 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 ^@ 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_0000278143 http://togogenome.org/gene/10090:Fryl ^@ http://purl.uniprot.org/uniprot/F8VQ05|||http://purl.uniprot.org/uniprot/Q80XD5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Cell morphogenesis central region|||Cell morphogenesis protein C-terminal|||Cell morphogenesis protein N-terminal|||Disordered|||Polar residues|||Protein furry C-terminal ^@ http://togogenome.org/gene/10090:Tesk1 ^@ http://purl.uniprot.org/uniprot/O70146 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Dual specificity testis-specific protein kinase 1|||Omega-N-methylarginine|||Phosphoserine; by autocatalysis|||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_0000086747 http://togogenome.org/gene/10090:Csn3 ^@ http://purl.uniprot.org/uniprot/P06796 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage; by chymosin/rennin|||Kappa-casein|||O-linked (GalNAc...) serine; alternate|||O-linked (GalNAc...) threonine|||Phosphoserine|||Phosphoserine; alternate|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000004499 http://togogenome.org/gene/10090:Dnaaf5 ^@ http://purl.uniprot.org/uniprot/B9EJR8 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat ^@ Dynein axonemal assembly factor 5|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000431656 http://togogenome.org/gene/10090:Otud6a ^@ http://purl.uniprot.org/uniprot/Q6IE21 ^@ 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_0000076278 http://togogenome.org/gene/10090:Klhl4 ^@ http://purl.uniprot.org/uniprot/B1AZQ9|||http://purl.uniprot.org/uniprot/B1AZR0|||http://purl.uniprot.org/uniprot/Q8BLJ6|||http://purl.uniprot.org/uniprot/Q8BUX1 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ BTB|||Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Lrrc4 ^@ http://purl.uniprot.org/uniprot/Q99PH1 ^@ 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|||Helical|||Ig-like|||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_0000014834 http://togogenome.org/gene/10090:Vmn2r100 ^@ http://purl.uniprot.org/uniprot/E9QAZ9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003243148 http://togogenome.org/gene/10090:Nedd4 ^@ http://purl.uniprot.org/uniprot/B2RSC8|||http://purl.uniprot.org/uniprot/P46935 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Basic and acidic residues|||C2|||Disordered|||E3 ubiquitin-protein ligase NEDD4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl thioester intermediate|||HECT|||Loss of ubiquitin-ligase activity. No effect on VEGFR-2/KDFR degradation.|||Mediates interaction with TNIK|||Nuclear export signal|||Phosphoserine|||Phosphothreonine|||WW|||WW 1|||WW 2|||WW 3 ^@ http://purl.uniprot.org/annotation/PRO_0000120320 http://togogenome.org/gene/10090:Cct8 ^@ http://purl.uniprot.org/uniprot/P42932|||http://purl.uniprot.org/uniprot/Q3UL22|||http://purl.uniprot.org/uniprot/Q8BVY8 ^@ Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed|||T-complex protein 1 subunit theta ^@ http://purl.uniprot.org/annotation/PRO_0000128374 http://togogenome.org/gene/10090:Asb16 ^@ http://purl.uniprot.org/uniprot/Q8VHS5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankyrin repeat and SOCS box protein 16|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066957 http://togogenome.org/gene/10090:Gch1 ^@ http://purl.uniprot.org/uniprot/Q05915|||http://purl.uniprot.org/uniprot/Q3U7P6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Disordered|||GTP cyclohydrolase 1|||GTP cyclohydrolase I|||Involved in pterin ring binding|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000010718|||http://purl.uniprot.org/annotation/PRO_0000010719 http://togogenome.org/gene/10090:Atad2 ^@ http://purl.uniprot.org/uniprot/G3X963|||http://purl.uniprot.org/uniprot/Q6IQY4|||http://purl.uniprot.org/uniprot/Q8CDM1 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant ^@ ATPase family AAA domain-containing protein 2|||Acidic residues|||Basic and acidic residues|||Basic residues|||Bromo|||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_0000084797|||http://purl.uniprot.org/annotation/VSP_035804|||http://purl.uniprot.org/annotation/VSP_035805|||http://purl.uniprot.org/annotation/VSP_035806|||http://purl.uniprot.org/annotation/VSP_035807 http://togogenome.org/gene/10090:Galnt6 ^@ http://purl.uniprot.org/uniprot/Q8C7U7 ^@ 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 6|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059115 http://togogenome.org/gene/10090:Ttc28 ^@ http://purl.uniprot.org/uniprot/Q80XJ3 ^@ 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|||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_0000106428 http://togogenome.org/gene/10090:Slc25a5 ^@ http://purl.uniprot.org/uniprot/P51881|||http://purl.uniprot.org/uniprot/Q545A2 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||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_0000090580|||http://purl.uniprot.org/annotation/PRO_0000423221 http://togogenome.org/gene/10090:Hadh ^@ http://purl.uniprot.org/uniprot/Q61425 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial|||Important for catalytic activity|||Mitochondrion|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000007407 http://togogenome.org/gene/10090:Stard8 ^@ http://purl.uniprot.org/uniprot/Q8K031 ^@ 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 ^@ Acidic residues|||Asymmetric dimethylarginine|||Disordered|||Phosphoserine|||Polar residues|||Rho-GAP|||START|||StAR-related lipid transfer protein 8 ^@ http://purl.uniprot.org/annotation/PRO_0000220677 http://togogenome.org/gene/10090:Med20 ^@ http://purl.uniprot.org/uniprot/Q9R0X0 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||Mediator of RNA polymerase II transcription subunit 20 ^@ http://purl.uniprot.org/annotation/PRO_0000065732|||http://purl.uniprot.org/annotation/VSP_028987|||http://purl.uniprot.org/annotation/VSP_028988|||http://purl.uniprot.org/annotation/VSP_028989|||http://purl.uniprot.org/annotation/VSP_028990 http://togogenome.org/gene/10090:Ccdc172 ^@ http://purl.uniprot.org/uniprot/Q810N9 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Splice Variant ^@ Coiled-coil domain-containing protein 172|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000344514|||http://purl.uniprot.org/annotation/VSP_034843 http://togogenome.org/gene/10090:Klhl22 ^@ http://purl.uniprot.org/uniprot/Q99JN2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||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 22|||N-acetylalanine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000242156|||http://purl.uniprot.org/annotation/VSP_019452 http://togogenome.org/gene/10090:Sac3d1 ^@ http://purl.uniprot.org/uniprot/A6H687|||http://purl.uniprot.org/uniprot/G5E8Q7 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||PCI|||Phosphoserine|||SAC3 domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000308205 http://togogenome.org/gene/10090:Popdc3 ^@ http://purl.uniprot.org/uniprot/Q9ES81 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Popeye domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000046796 http://togogenome.org/gene/10090:Bmyc ^@ http://purl.uniprot.org/uniprot/A0PJL6|||http://purl.uniprot.org/uniprot/Q6P8Z1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site ^@ Loss of phosphorylation.|||Phosphoserine|||Protein B-Myc|||Transcription regulator Myc N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000127339 http://togogenome.org/gene/10090:Cyp4a12a ^@ http://purl.uniprot.org/uniprot/Q91WL5 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Sequence Conflict|||Signal Peptide ^@ Cytochrome P450 4A12A|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000051817 http://togogenome.org/gene/10090:Fgf8 ^@ http://purl.uniprot.org/uniprot/D3Z207|||http://purl.uniprot.org/uniprot/P37237|||http://purl.uniprot.org/uniprot/Q3V279|||http://purl.uniprot.org/uniprot/Q80ZL6 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Fibroblast growth factor|||Fibroblast growth factor 8|||In isoform FGF-8A.|||In isoform FGF-8B.|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000008971|||http://purl.uniprot.org/annotation/PRO_5005143200|||http://purl.uniprot.org/annotation/PRO_5015019508|||http://purl.uniprot.org/annotation/PRO_5015020109|||http://purl.uniprot.org/annotation/VSP_001527|||http://purl.uniprot.org/annotation/VSP_001528 http://togogenome.org/gene/10090:Ptgfr ^@ http://purl.uniprot.org/uniprot/P43117|||http://purl.uniprot.org/uniprot/Q60I90|||http://purl.uniprot.org/uniprot/Q8BNT7 ^@ 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 ^@ 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|||Prostaglandin F2-alpha receptor ^@ http://purl.uniprot.org/annotation/PRO_0000070071 http://togogenome.org/gene/10090:Nsrp1 ^@ http://purl.uniprot.org/uniprot/Q5NCR9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Necessary for alternative splicing activity|||Nuclear speckle splicing regulatory protein 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000240435 http://togogenome.org/gene/10090:Eng ^@ http://purl.uniprot.org/uniprot/F7A1B4|||http://purl.uniprot.org/uniprot/Q3UAM9|||http://purl.uniprot.org/uniprot/Q63961 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Endoglin|||Essential for interaction with GDF2|||Extracellular|||Helical|||Interchain|||N-linked (GlcNAc...) asparagine|||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_0000021157|||http://purl.uniprot.org/annotation/PRO_5003347284|||http://purl.uniprot.org/annotation/PRO_5015097477 http://togogenome.org/gene/10090:Pdia2 ^@ http://purl.uniprot.org/uniprot/D3Z6P0 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Contributes to redox potential value|||Disordered|||In isoform 2.|||Lowers pKa of C-terminal Cys of second active site|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Prevents secretion from ER|||Protein disulfide-isomerase A2|||Redox-active|||Thioredoxin 1|||Thioredoxin 2 ^@ http://purl.uniprot.org/annotation/PRO_0000394671|||http://purl.uniprot.org/annotation/VSP_039293 http://togogenome.org/gene/10090:Zkscan2 ^@ http://purl.uniprot.org/uniprot/G3X952 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||SCAN box ^@ http://togogenome.org/gene/10090:Klk1b16 ^@ http://purl.uniprot.org/uniprot/A0A1R3UCH4|||http://purl.uniprot.org/uniprot/P04071 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Charge relay system|||Kallikrein 1-related peptidase b16|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027985|||http://purl.uniprot.org/annotation/PRO_0000027986|||http://purl.uniprot.org/annotation/PRO_5010243664 http://togogenome.org/gene/10090:Lif ^@ http://purl.uniprot.org/uniprot/P09056 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Signal Peptide|||Strand ^@ Leukemia inhibitory factor|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017716 http://togogenome.org/gene/10090:Minar1 ^@ http://purl.uniprot.org/uniprot/Q8K3V7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Major intrinsically disordered Notch2-binding receptor 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000157134|||http://purl.uniprot.org/annotation/VSP_013706 http://togogenome.org/gene/10090:Fam166a ^@ http://purl.uniprot.org/uniprot/Q9D4K5 ^@ Chain|||Molecule Processing ^@ Chain ^@ Ciliary microtubule inner protein 2A ^@ http://purl.uniprot.org/annotation/PRO_0000325901 http://togogenome.org/gene/10090:Or1ad8 ^@ http://purl.uniprot.org/uniprot/Q8VGG9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tinag ^@ http://purl.uniprot.org/uniprot/Q9WUR0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ SMB ^@ http://purl.uniprot.org/annotation/PRO_5015020188 http://togogenome.org/gene/10090:Cyp2d10 ^@ http://purl.uniprot.org/uniprot/P24456 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Cytochrome P450 2D10|||Phosphoserine|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051735 http://togogenome.org/gene/10090:Kif12 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VK29|||http://purl.uniprot.org/uniprot/Q9D2Z8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Kinesin motor|||Kinesin-like protein KIF12|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000125445 http://togogenome.org/gene/10090:Ptpn14 ^@ http://purl.uniprot.org/uniprot/Q62130|||http://purl.uniprot.org/uniprot/Q8CAV9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Disordered|||FERM|||Phosphocysteine intermediate|||Phosphoserine|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 14 ^@ http://purl.uniprot.org/annotation/PRO_0000219438 http://togogenome.org/gene/10090:Uqcc3 ^@ http://purl.uniprot.org/uniprot/Q8K2T4 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Helical|||Mediates lipid-binding|||Mitochondrial intermembrane|||Mitochondrial matrix|||Ubiquinol-cytochrome-c reductase complex assembly factor 3 ^@ http://purl.uniprot.org/annotation/PRO_0000022612 http://togogenome.org/gene/10090:Luc7l ^@ http://purl.uniprot.org/uniprot/A0A0R4J047|||http://purl.uniprot.org/uniprot/Q3TV90|||http://purl.uniprot.org/uniprot/Q9CYI4 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Putative RNA-binding protein Luc7-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000187281|||http://purl.uniprot.org/annotation/VSP_010216 http://togogenome.org/gene/10090:Slc17a9 ^@ http://purl.uniprot.org/uniprot/Q8VCL5|||http://purl.uniprot.org/uniprot/Q9DA66 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||Voltage-gated purine nucleotide uniporter SLC17A9 ^@ http://purl.uniprot.org/annotation/PRO_0000084850 http://togogenome.org/gene/10090:Mphosph9 ^@ http://purl.uniprot.org/uniprot/A0A8Q0L6P9|||http://purl.uniprot.org/uniprot/A6H5Y1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with CEP97|||Interaction with KIF24|||M-phase phosphoprotein 9|||Phosphoserine|||Phosphoserine; by TTBK2|||Polar residues|||Required for its centrosomal localization ^@ http://purl.uniprot.org/annotation/PRO_0000355083 http://togogenome.org/gene/10090:Gng2 ^@ http://purl.uniprot.org/uniprot/P63213 ^@ 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_0000012613|||http://purl.uniprot.org/annotation/PRO_0000012614 http://togogenome.org/gene/10090:Septin2 ^@ http://purl.uniprot.org/uniprot/E9Q3V6|||http://purl.uniprot.org/uniprot/P42208 ^@ 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|||Region|||Site|||Strand|||Turn ^@ G1 motif|||G3 motif|||G4 motif|||Important for dimerization|||Loss of GTP-binding activity.|||Loss of GTP-binding.|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Reduces affinity for GTP 20-fold.|||Septin-2|||Septin-type G ^@ http://purl.uniprot.org/annotation/PRO_0000173516 http://togogenome.org/gene/10090:Hey1 ^@ http://purl.uniprot.org/uniprot/Q9QUM5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Disordered|||Orange|||Polar residues ^@ http://togogenome.org/gene/10090:Tmem70 ^@ http://purl.uniprot.org/uniprot/A0A0R4J272|||http://purl.uniprot.org/uniprot/Q921N7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Transmembrane protein 70, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000251473 http://togogenome.org/gene/10090:Gsdmc4 ^@ http://purl.uniprot.org/uniprot/A0A679B0N4|||http://purl.uniprot.org/uniprot/Q3TR54 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Site ^@ Cleavage; by CASP8|||Gasdermin PUB|||Gasdermin pore forming|||Gasdermin-C4|||Gasdermin-C4, C-terminal|||Gasdermin-C4, N-terminal|||Triggers pyroptosis ^@ http://purl.uniprot.org/annotation/PRO_0000347333|||http://purl.uniprot.org/annotation/PRO_0000451682|||http://purl.uniprot.org/annotation/PRO_0000451683 http://togogenome.org/gene/10090:Rgs7bp ^@ http://purl.uniprot.org/uniprot/Q8BQP9 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Lipid Binding|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes nuclear localization and palmitoylation.|||Abolishes nuclear localization; when associated with E-243.|||Abolishes nuclear localization; when associated with E-246.|||Abolishes palmitoylation.|||Disordered|||Nuclear localization signal|||Regulator of G-protein signaling 7-binding protein|||S-palmitoyl cysteine|||Strongly reduces palmitoylation and its ability to regulate GPCR signaling. Abolishes palmitoylation and its ability to regulate GPCR signaling; when associated with S-252.|||Strongly reduces palmitoylation and its ability to regulate GPCR signaling. Abolishes palmitoylation and its ability to regulate GPCR signaling; when associated with S-253. ^@ http://purl.uniprot.org/annotation/PRO_0000287596 http://togogenome.org/gene/10090:Ube2c ^@ http://purl.uniprot.org/uniprot/A2A4Z0|||http://purl.uniprot.org/uniprot/Q9D1C1 ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Glycyl thioester intermediate|||N-acetylalanine|||Phosphoserine|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 C ^@ http://purl.uniprot.org/annotation/PRO_0000082561 http://togogenome.org/gene/10090:Rnase6 ^@ http://purl.uniprot.org/uniprot/Q3V3L3|||http://purl.uniprot.org/uniprot/Q9D244 ^@ 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|||Sequence Conflict|||Signal Peptide|||Site ^@ Critical for catalytic activity|||Facilitates cleavage of polynucleotide substrates|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Proton donor|||Ribonuclease A-domain|||Ribonuclease K6 ^@ http://purl.uniprot.org/annotation/PRO_0000030900|||http://purl.uniprot.org/annotation/PRO_5015020017 http://togogenome.org/gene/10090:Krt78 ^@ http://purl.uniprot.org/uniprot/E9Q0F0|||http://purl.uniprot.org/uniprot/Q6IFT3 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent|||Region ^@ Disordered|||IF rod ^@ http://togogenome.org/gene/10090:Nnmt ^@ http://purl.uniprot.org/uniprot/D3YX59|||http://purl.uniprot.org/uniprot/O55239 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Citrulline; alternate|||Disordered|||Loss of N-methyltransferase activity.|||Nicotinamide N-methyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000159707 http://togogenome.org/gene/10090:Chrnb4 ^@ http://purl.uniprot.org/uniprot/Q3USV2|||http://purl.uniprot.org/uniprot/Q8R493 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||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|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000390|||http://purl.uniprot.org/annotation/PRO_5014309181 http://togogenome.org/gene/10090:Nanp ^@ http://purl.uniprot.org/uniprot/Q9CPT3 ^@ Binding Site|||Chain|||Helix|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Strand|||Turn ^@ N-acylneuraminate-9-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000083939 http://togogenome.org/gene/10090:Btbd35f8 ^@ http://purl.uniprot.org/uniprot/A0A571BG86 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Lrp1b ^@ http://purl.uniprot.org/uniprot/A2API5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Repeat|||Signal Peptide|||Transmembrane ^@ EGF-like|||Helical|||LDL-receptor class B ^@ http://purl.uniprot.org/annotation/PRO_5005898203 http://togogenome.org/gene/10090:Siah1b ^@ http://purl.uniprot.org/uniprot/A2AHZ2|||http://purl.uniprot.org/uniprot/Q06985 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase SIAH1B|||Phosphoserine; by ATM and ATR|||RING-type|||SBD|||SIAH-type ^@ http://purl.uniprot.org/annotation/PRO_0000056165 http://togogenome.org/gene/10090:Parp8 ^@ http://purl.uniprot.org/uniprot/F8WIK2|||http://purl.uniprot.org/uniprot/Q3UD82 ^@ 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 ^@ ADP-ribosylcysteine|||Disordered|||PARP catalytic|||Polar residues|||Pro residues|||Protein mono-ADP-ribosyltransferase PARP8 ^@ http://purl.uniprot.org/annotation/PRO_0000252434 http://togogenome.org/gene/10090:Krr1 ^@ http://purl.uniprot.org/uniprot/Q8BGA5 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KH|||KRR1 small subunit processome component homolog|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000050115 http://togogenome.org/gene/10090:Grifin ^@ http://purl.uniprot.org/uniprot/Q9D1U0 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ Galectin|||Grifin|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000315763 http://togogenome.org/gene/10090:Mrc2 ^@ http://purl.uniprot.org/uniprot/Q14AX9|||http://purl.uniprot.org/uniprot/Q64449 ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||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|||C-type mannose receptor 2|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-II|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000046079|||http://purl.uniprot.org/annotation/PRO_5014306929|||http://purl.uniprot.org/annotation/VSP_017223|||http://purl.uniprot.org/annotation/VSP_017224 http://togogenome.org/gene/10090:Rhox9 ^@ http://purl.uniprot.org/uniprot/Q9EQM5 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Pcbp3 ^@ http://purl.uniprot.org/uniprot/P57722 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||KH 1|||KH 2|||KH 3|||Poly(rC)-binding protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000050093|||http://purl.uniprot.org/annotation/VSP_010015 http://togogenome.org/gene/10090:Chrm3 ^@ http://purl.uniprot.org/uniprot/Q542R4|||http://purl.uniprot.org/uniprot/Q9ERZ3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Basolateral sorting signal|||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 M3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069030 http://togogenome.org/gene/10090:Larp4 ^@ http://purl.uniprot.org/uniprot/A0A2R8VKL5|||http://purl.uniprot.org/uniprot/E9Q066|||http://purl.uniprot.org/uniprot/G3X9Q6|||http://purl.uniprot.org/uniprot/Q3UT02|||http://purl.uniprot.org/uniprot/Q8BWW4 ^@ 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|||Interaction with PABPC1|||Interaction with the poly-A tract of mRNA|||La-related protein 4|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000207612 http://togogenome.org/gene/10090:Sim2 ^@ http://purl.uniprot.org/uniprot/Q61079 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Nuclear localization signal|||PAC|||PAS 1|||PAS 2|||Polar residues|||Single-minded C-terminal|||Single-minded homolog 2|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127442 http://togogenome.org/gene/10090:Mcrs1 ^@ http://purl.uniprot.org/uniprot/Q3TJY1|||http://purl.uniprot.org/uniprot/Q3TYU7|||http://purl.uniprot.org/uniprot/Q99L90 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||FHA|||Microspherule protein 1|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000096306 http://togogenome.org/gene/10090:Or10g1b ^@ http://purl.uniprot.org/uniprot/E9PWU0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Armcx1 ^@ http://purl.uniprot.org/uniprot/Q9CX83 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||Acidic residues|||Armadillo repeat-containing X-linked protein 1|||Basic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor|||Mitochondrial intermembrane|||Mitochondrion outer membrane (MOM)-targeting sequence ^@ http://purl.uniprot.org/annotation/PRO_0000191362 http://togogenome.org/gene/10090:Prdx6 ^@ http://purl.uniprot.org/uniprot/D3Z0Y2|||http://purl.uniprot.org/uniprot/O08709|||http://purl.uniprot.org/uniprot/Q6GT24 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site ^@ Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity|||For phospholipase activity|||Important for phospholipase activity|||In strain: C57BL/6, C57BL/6J and FVB/N.|||Loss of lysophosphatidylcholine acyltransferase activity, but no effect on phospholipase activity.|||Loss of phospholipase activity, but no effect on lysophosphatidylcholine acyltransferase activity.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||No loss of phospholipase or lysophosphatidylcholine acyltransferase activity.|||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_0000135103 http://togogenome.org/gene/10090:Tmem18 ^@ http://purl.uniprot.org/uniprot/Q3TUD9 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Motif|||Region|||Topological Domain|||Transmembrane ^@ DNA-binding|||Helical|||Nuclear|||Nuclear localization signal|||Perinuclear space|||Transmembrane protein 18 ^@ http://purl.uniprot.org/annotation/PRO_0000284370 http://togogenome.org/gene/10090:Trp53rka ^@ http://purl.uniprot.org/uniprot/Q5U452 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Protein kinase ^@ http://togogenome.org/gene/10090:Micos10 ^@ http://purl.uniprot.org/uniprot/Q7TNS2 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Topological Domain|||Transmembrane ^@ Helical|||MICOS complex subunit Mic10|||Mitochondrial intermembrane|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000221635 http://togogenome.org/gene/10090:Or7g35 ^@ http://purl.uniprot.org/uniprot/Q7TRF8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Wbp1 ^@ http://purl.uniprot.org/uniprot/P97764|||http://purl.uniprot.org/uniprot/Q8C5Y4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Abolishes interaction with NEDD4.|||Disordered|||Helical|||In isoform 2.|||PPxY motif 1|||PPxY motif 2|||Polar residues|||WW domain-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000065949|||http://purl.uniprot.org/annotation/VSP_004022 http://togogenome.org/gene/10090:Aebp2 ^@ http://purl.uniprot.org/uniprot/Q9Z248 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Abrogates transcriptional repression but does not affect DNA-binding.|||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, isoform 4 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||Interaction with RBBP4|||Interaction with SUZ12|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Zinc finger protein AEBP2 ^@ http://purl.uniprot.org/annotation/PRO_0000341591|||http://purl.uniprot.org/annotation/VSP_034360|||http://purl.uniprot.org/annotation/VSP_034361|||http://purl.uniprot.org/annotation/VSP_034362|||http://purl.uniprot.org/annotation/VSP_034363 http://togogenome.org/gene/10090:Wbp4 ^@ http://purl.uniprot.org/uniprot/Q61048 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Interaction with SNRNP200|||Matrin-type|||Phosphoserine|||Polar residues|||WW 1|||WW 2|||WW domain-binding protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000076066 http://togogenome.org/gene/10090:Casp8ap2 ^@ http://purl.uniprot.org/uniprot/Q3UQU1|||http://purl.uniprot.org/uniprot/Q9WUF3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000076189 http://togogenome.org/gene/10090:Jph1 ^@ http://purl.uniprot.org/uniprot/Q9ET80 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||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_0000159845 http://togogenome.org/gene/10090:Hmgb1 ^@ http://purl.uniprot.org/uniprot/P63158|||http://purl.uniprot.org/uniprot/Q58EV5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ ADP-ribosylserine|||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|||Disordered|||HMG box|||HMG box 1|||HMG box 2|||High mobility group protein B1|||In disulfide HMGB1; alternate|||Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)|||LPS binding (Lipid A)|||LPS binding (delipidated)|||N6-acetyllysine|||NLS 1|||NLS 2|||Nuclear localization signal (NLS) 1|||Nuclear localization signal (NLS) 2|||Phosphoserine|||Sufficient for interaction with HAVCR2 ^@ http://purl.uniprot.org/annotation/PRO_0000048528 http://togogenome.org/gene/10090:Slc5a10 ^@ http://purl.uniprot.org/uniprot/Q5SWY8 ^@ 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|||Phosphothreonine|||Sodium/mannose cotransporter SLC5A10 ^@ http://purl.uniprot.org/annotation/PRO_0000311212 http://togogenome.org/gene/10090:Pid1 ^@ http://purl.uniprot.org/uniprot/Q3UBG2 ^@ 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.|||PID|||PTB-containing, cubilin and LRP1-interacting protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000274901|||http://purl.uniprot.org/annotation/VSP_022913 http://togogenome.org/gene/10090:Or10q12 ^@ http://purl.uniprot.org/uniprot/Q8VEZ4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rusf1 ^@ http://purl.uniprot.org/uniprot/Q91W34 ^@ 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|||RUS family member 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000282931|||http://purl.uniprot.org/annotation/VSP_024257|||http://purl.uniprot.org/annotation/VSP_024258 http://togogenome.org/gene/10090:Or4a77 ^@ http://purl.uniprot.org/uniprot/Q8VGM3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Exoc3 ^@ http://purl.uniprot.org/uniprot/Q6KAR6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Exocyst complex component 3|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000118926 http://togogenome.org/gene/10090:Smim9 ^@ http://purl.uniprot.org/uniprot/Q3V0X1 ^@ 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_0000348248 http://togogenome.org/gene/10090:Ibtk ^@ http://purl.uniprot.org/uniprot/Q6ZPR6 ^@ 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 ^@ ANK 1|||ANK 2|||BTB 1|||BTB 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||Inhibitor of Bruton tyrosine kinase|||Phosphoserine|||RCC1 1|||RCC1 2|||RCC1 3 ^@ http://purl.uniprot.org/annotation/PRO_0000280277|||http://purl.uniprot.org/annotation/VSP_023605 http://togogenome.org/gene/10090:Ptpra ^@ http://purl.uniprot.org/uniprot/P18052|||http://purl.uniprot.org/uniprot/Q3TRY9|||http://purl.uniprot.org/uniprot/Q91V35 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Receptor-type tyrosine-protein phosphatase alpha|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000025434|||http://purl.uniprot.org/annotation/PRO_5015099518|||http://purl.uniprot.org/annotation/VSP_005146|||http://purl.uniprot.org/annotation/VSP_011880 http://togogenome.org/gene/10090:Tmem30b ^@ http://purl.uniprot.org/uniprot/Q0VEI2|||http://purl.uniprot.org/uniprot/Q8BHG3 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cell cycle control protein 50B|||Cytoplasmic|||Exoplasmic loop|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000244475 http://togogenome.org/gene/10090:Pagr1a ^@ http://purl.uniprot.org/uniprot/Q99L02 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||PAXIP1-associated glutamate-rich protein 1A|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sufficient for interaction with ESR1|||Sufficient for interaction with NCOA1 ^@ http://purl.uniprot.org/annotation/PRO_0000248335 http://togogenome.org/gene/10090:Ahcy ^@ http://purl.uniprot.org/uniprot/P50247|||http://purl.uniprot.org/uniprot/Q3TF14|||http://purl.uniprot.org/uniprot/Q5M9P0 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ Adenosylhomocysteinase|||N-acetylserine|||N6-(2-hydroxyisobutyryl)lysine|||NAD binding|||Phosphoserine|||Phosphotyrosine|||Removed|||S-adenosyl-L-homocysteine hydrolase NAD binding ^@ http://purl.uniprot.org/annotation/PRO_0000116903 http://togogenome.org/gene/10090:Eif3d ^@ http://purl.uniprot.org/uniprot/O70194 ^@ 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|||Eukaryotic translation initiation factor 3 subunit D|||N6-acetyllysine|||Phosphoserine|||RNA gate ^@ http://purl.uniprot.org/annotation/PRO_0000123521 http://togogenome.org/gene/10090:Gabbr2 ^@ http://purl.uniprot.org/uniprot/Q80T41 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Gamma-aminobutyric acid type B receptor subunit 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|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000306250 http://togogenome.org/gene/10090:Pvalb ^@ http://purl.uniprot.org/uniprot/P32848|||http://purl.uniprot.org/uniprot/Q545M7 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Mass|||Modified Residue|||Sequence Conflict ^@ EF-hand|||EF-hand 1|||EF-hand 2|||N-acetylserine|||Parvalbumin alpha|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073590 http://togogenome.org/gene/10090:Mthfsl ^@ http://purl.uniprot.org/uniprot/L7N466 ^@ Binding Site|||Site ^@ Binding Site ^@ ^@ http://togogenome.org/gene/10090:Sec14l2 ^@ http://purl.uniprot.org/uniprot/Q99J08 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Modified Residue ^@ CRAL-TRIO|||GOLD|||N6-succinyllysine|||SEC14-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000210756 http://togogenome.org/gene/10090:Phyhipl ^@ http://purl.uniprot.org/uniprot/F7D3N3|||http://purl.uniprot.org/uniprot/Q8BGT8 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant ^@ Fibronectin type-III|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phytanoyl-CoA hydroxylase-interacting protein-like ^@ http://purl.uniprot.org/annotation/PRO_0000338642|||http://purl.uniprot.org/annotation/VSP_034070 http://togogenome.org/gene/10090:Siglece ^@ http://purl.uniprot.org/uniprot/Q91Y57 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Abolishes binding to PTPN6 and PTPN11.|||Cytoplasmic|||Extracellular|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Reduces binding to PTPN6.|||SLAM-like motif|||Sialic acid-binding Ig-like lectin 12 ^@ http://purl.uniprot.org/annotation/PRO_0000014954 http://togogenome.org/gene/10090:Lrfn3 ^@ http://purl.uniprot.org/uniprot/Q8BLY3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||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|||LRRCT|||LRRNT|||Leucine-rich repeat and fibronectin type-III domain-containing protein 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014842 http://togogenome.org/gene/10090:Or4a66 ^@ http://purl.uniprot.org/uniprot/Q7TR14 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdc42se1 ^@ http://purl.uniprot.org/uniprot/Q8BHL7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region ^@ Basic and acidic residues|||CDC42 small effector protein 1|||CRIB|||Disordered|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000334630 http://togogenome.org/gene/10090:Ryr3 ^@ http://purl.uniprot.org/uniprot/A0A140LJK7|||http://purl.uniprot.org/uniprot/A2AGL3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ 1|||2|||3|||4|||4 X approximate repeats|||Acidic residues|||B30.2/SPRY|||B30.2/SPRY 1|||B30.2/SPRY 2|||B30.2/SPRY 3|||Cytoplasmic|||Disordered|||EF-hand|||Helical|||Important for activation by Ca(2+)|||In isoform 2.|||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_0000415648|||http://purl.uniprot.org/annotation/VSP_042304 http://togogenome.org/gene/10090:Obscn ^@ http://purl.uniprot.org/uniprot/E9QQ96|||http://purl.uniprot.org/uniprot/H7BX05 ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DH|||Disordered|||Fibronectin type-III|||Ig-like|||PH|||Polar residues|||Protein kinase|||SH3 ^@ http://togogenome.org/gene/10090:B3gnt9 ^@ http://purl.uniprot.org/uniprot/Q8VI16 ^@ 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|||UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 9 ^@ http://purl.uniprot.org/annotation/PRO_0000352763 http://togogenome.org/gene/10090:Ldb3 ^@ http://purl.uniprot.org/uniprot/E9PYJ9|||http://purl.uniprot.org/uniprot/Q9JKS4 ^@ 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 6.|||In isoform 3 and isoform 4.|||In isoform 5 and isoform 6.|||LIM domain-binding protein 3|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000075768|||http://purl.uniprot.org/annotation/VSP_051903|||http://purl.uniprot.org/annotation/VSP_051904|||http://purl.uniprot.org/annotation/VSP_051905|||http://purl.uniprot.org/annotation/VSP_051906 http://togogenome.org/gene/10090:Cldn23 ^@ http://purl.uniprot.org/uniprot/Q3ULX4|||http://purl.uniprot.org/uniprot/Q9D7D7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane ^@ Claudin-23|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000144788 http://togogenome.org/gene/10090:Bpifb5 ^@ http://purl.uniprot.org/uniprot/Q3UQ05 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipid-binding serum glycoprotein N-terminal ^@ http://purl.uniprot.org/annotation/PRO_5015097490 http://togogenome.org/gene/10090:Ubl5 ^@ http://purl.uniprot.org/uniprot/Q9EPV8 ^@ Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Helix|||Strand ^@ Ubiquitin-like|||Ubiquitin-like protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000114868 http://togogenome.org/gene/10090:Cerkl ^@ http://purl.uniprot.org/uniprot/A2AQH1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ DAGKc|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cspp1 ^@ http://purl.uniprot.org/uniprot/B2RX88 ^@ 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|||Centrosome and spindle pole associated protein 1|||Disordered|||In isoform 2.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 3.|||In isoform 5 and isoform 6.|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000401192|||http://purl.uniprot.org/annotation/VSP_040073|||http://purl.uniprot.org/annotation/VSP_040074|||http://purl.uniprot.org/annotation/VSP_040075|||http://purl.uniprot.org/annotation/VSP_040076|||http://purl.uniprot.org/annotation/VSP_040077|||http://purl.uniprot.org/annotation/VSP_040078|||http://purl.uniprot.org/annotation/VSP_040079 http://togogenome.org/gene/10090:Itgal ^@ http://purl.uniprot.org/uniprot/B7ZN92|||http://purl.uniprot.org/uniprot/P24063|||http://purl.uniprot.org/uniprot/Q3TB85 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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.|||Integrin alpha-L|||N-linked (GlcNAc...) asparagine|||VWFA|||VWFA domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000016293|||http://purl.uniprot.org/annotation/PRO_5001423992|||http://purl.uniprot.org/annotation/PRO_5010754652|||http://purl.uniprot.org/annotation/VSP_061239 http://togogenome.org/gene/10090:Mkrn1 ^@ http://purl.uniprot.org/uniprot/E9QAG7|||http://purl.uniprot.org/uniprot/Q8C5V4 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger ^@ C3H1-type|||Disordered|||Polar residues|||RING-type ^@ http://togogenome.org/gene/10090:Agtrap ^@ http://purl.uniprot.org/uniprot/Q9WVK0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Interaction with AGTR1|||Phosphoserine|||Phosphothreonine|||Type-1 angiotensin II receptor-associated protein ^@ http://purl.uniprot.org/annotation/PRO_0000064736 http://togogenome.org/gene/10090:Sorl1 ^@ http://purl.uniprot.org/uniprot/O88307 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ BNR 1|||BNR 2|||BNR 3|||BNR 4|||BNR 5|||Cytoplasmic|||DXXLL motif involved in the interaction with GGA1|||Disordered|||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|||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|||Lumenal|||N-linked (GlcNAc...) asparagine|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000033166|||http://purl.uniprot.org/annotation/PRO_0000033167 http://togogenome.org/gene/10090:Podn ^@ http://purl.uniprot.org/uniprot/Q7TQ62 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ Acidic residues|||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 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_0000262525|||http://purl.uniprot.org/annotation/VSP_021785 http://togogenome.org/gene/10090:Prpf38a ^@ http://purl.uniprot.org/uniprot/B2RTE3|||http://purl.uniprot.org/uniprot/Q4FK66 ^@ 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|||Basic residues|||Disordered|||In isoform 2.|||N-terminal protein interaction domain|||Phosphoserine|||Pre-mRNA-splicing factor 38 C-terminal|||Pre-mRNA-splicing factor 38A ^@ http://purl.uniprot.org/annotation/PRO_0000287274|||http://purl.uniprot.org/annotation/VSP_025425|||http://purl.uniprot.org/annotation/VSP_025426|||http://purl.uniprot.org/annotation/VSP_025427 http://togogenome.org/gene/10090:Lrrc63 ^@ http://purl.uniprot.org/uniprot/A6H694 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Leucine-rich repeat-containing protein 63|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000320629 http://togogenome.org/gene/10090:Wdr5 ^@ http://purl.uniprot.org/uniprot/P61965 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Site|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Site|||Strand|||Turn ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Important for interaction with histone H3|||N-acetylalanine|||N6-acetyllysine|||Polar residues|||Removed|||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_0000051351 http://togogenome.org/gene/10090:Zbtb24 ^@ http://purl.uniprot.org/uniprot/Q80X44 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand|||Turn|||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 isoform 2.|||In isoform 3.|||Zinc finger and BTB domain-containing protein 24 ^@ http://purl.uniprot.org/annotation/PRO_0000047735|||http://purl.uniprot.org/annotation/VSP_016223|||http://purl.uniprot.org/annotation/VSP_016224|||http://purl.uniprot.org/annotation/VSP_016225 http://togogenome.org/gene/10090:Or5ak25 ^@ http://purl.uniprot.org/uniprot/Q8VF74 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cpox ^@ http://purl.uniprot.org/uniprot/P36552 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Disordered|||Important for dimerization|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial|||Phosphoserine|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000006030 http://togogenome.org/gene/10090:Spsb3 ^@ http://purl.uniprot.org/uniprot/D3YW96|||http://purl.uniprot.org/uniprot/Q571F5 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ B30.2/SPRY|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||SOCS box|||SPRY domain-containing SOCS box protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000278779|||http://purl.uniprot.org/annotation/VSP_023378|||http://purl.uniprot.org/annotation/VSP_023379|||http://purl.uniprot.org/annotation/VSP_023380 http://togogenome.org/gene/10090:Anapc15 ^@ http://purl.uniprot.org/uniprot/G5E8M3|||http://purl.uniprot.org/uniprot/H3BIU1|||http://purl.uniprot.org/uniprot/P60007|||http://purl.uniprot.org/uniprot/Q9D3A0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Acidic residues|||Anaphase-promoting complex subunit 15|||Disordered|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000084073|||http://purl.uniprot.org/annotation/VSP_043771 http://togogenome.org/gene/10090:BC004004 ^@ http://purl.uniprot.org/uniprot/Q99KU6 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Bombesin receptor-activated protein C6orf89 homolog|||Cytoplasmic|||Extracellular|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000237622 http://togogenome.org/gene/10090:Tent4b ^@ http://purl.uniprot.org/uniprot/B7ZMU2|||http://purl.uniprot.org/uniprot/E9QJT6|||http://purl.uniprot.org/uniprot/F8WI26|||http://purl.uniprot.org/uniprot/Q68ED3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic, involved in binding of the RNA primer|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||PAP-associated|||Phosphoserine|||Polar residues|||Polymerase nucleotidyl transferase|||Terminal nucleotidyltransferase 4B ^@ http://purl.uniprot.org/annotation/PRO_0000120311 http://togogenome.org/gene/10090:Noxred1 ^@ http://purl.uniprot.org/uniprot/Q9D3S5 ^@ Chain|||Molecule Processing ^@ Chain ^@ NADP-dependent oxidoreductase domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000280280 http://togogenome.org/gene/10090:Tas2r126 ^@ http://purl.uniprot.org/uniprot/P59532 ^@ 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 41 ^@ http://purl.uniprot.org/annotation/PRO_0000082300 http://togogenome.org/gene/10090:Zfp160 ^@ http://purl.uniprot.org/uniprot/E9Q459|||http://purl.uniprot.org/uniprot/Q3UPQ5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ifitm10 ^@ http://purl.uniprot.org/uniprot/Q8BR26 ^@ Chain|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Lipid Binding|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Interferon-induced transmembrane protein 10|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000332962|||http://purl.uniprot.org/annotation/VSP_033398|||http://purl.uniprot.org/annotation/VSP_041596 http://togogenome.org/gene/10090:Ethe1 ^@ http://purl.uniprot.org/uniprot/Q9DCM0 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Persulfide dioxygenase ETHE1, mitochondrial|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000012290 http://togogenome.org/gene/10090:Rbp4 ^@ http://purl.uniprot.org/uniprot/H7BWY6|||http://purl.uniprot.org/uniprot/Q00724 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding|||Omega-N-methylarginine|||Retinol-binding protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000017966 http://togogenome.org/gene/10090:Ncoa1 ^@ http://purl.uniprot.org/uniprot/P70365 ^@ 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|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Abolishes the interactions with estrogen and retinoid-acids receptors.|||Asymmetric dimethylarginine|||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.|||In isoform 3.|||In isoform 4.|||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|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000094401|||http://purl.uniprot.org/annotation/VSP_011740|||http://purl.uniprot.org/annotation/VSP_011741|||http://purl.uniprot.org/annotation/VSP_027855|||http://purl.uniprot.org/annotation/VSP_027856 http://togogenome.org/gene/10090:Vmn1r221 ^@ http://purl.uniprot.org/uniprot/A0A494B935 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r53 ^@ http://purl.uniprot.org/uniprot/A2RS76 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r237 ^@ http://purl.uniprot.org/uniprot/Q8R296 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Map1b ^@ http://purl.uniprot.org/uniprot/P14873|||http://purl.uniprot.org/uniprot/Q3UF78|||http://purl.uniprot.org/uniprot/Q8CFR9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||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|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000018606|||http://purl.uniprot.org/annotation/PRO_0000018607|||http://purl.uniprot.org/annotation/PRO_0000418380 http://togogenome.org/gene/10090:Opcml ^@ http://purl.uniprot.org/uniprot/G5E8G3|||http://purl.uniprot.org/uniprot/Q6DFY2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015091906|||http://purl.uniprot.org/annotation/PRO_5015098188 http://togogenome.org/gene/10090:Chfr ^@ http://purl.uniprot.org/uniprot/Q810L3 ^@ 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 ^@ Disordered|||E3 ubiquitin-protein ligase CHFR|||FHA|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PBZ-type|||Phosphothreonine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055873|||http://purl.uniprot.org/annotation/VSP_009351|||http://purl.uniprot.org/annotation/VSP_038128|||http://purl.uniprot.org/annotation/VSP_038129 http://togogenome.org/gene/10090:Selenop ^@ http://purl.uniprot.org/uniprot/P70274 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non standard residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Non standard residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Selenocysteine|||Selenoprotein P ^@ http://purl.uniprot.org/annotation/PRO_0000022314 http://togogenome.org/gene/10090:Zfp616 ^@ http://purl.uniprot.org/uniprot/J3QN14 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type ^@ http://togogenome.org/gene/10090:Dhdh ^@ http://purl.uniprot.org/uniprot/Q9DBB8 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Chain|||Sequence Conflict|||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_0000315364 http://togogenome.org/gene/10090:Cst10 ^@ http://purl.uniprot.org/uniprot/Q9JM84 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Splice Variant ^@ Cystatin 10|||Cystatin kininogen-type|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_5006993922|||http://purl.uniprot.org/annotation/VSP_058422 http://togogenome.org/gene/10090:Glg1 ^@ http://purl.uniprot.org/uniprot/Q53WR6|||http://purl.uniprot.org/uniprot/Q61543 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cys-rich GLG1|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000011121|||http://purl.uniprot.org/annotation/PRO_5014309557 http://togogenome.org/gene/10090:Samd9l ^@ http://purl.uniprot.org/uniprot/E9PX59|||http://purl.uniprot.org/uniprot/Q8BZG4 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||SAM ^@ http://togogenome.org/gene/10090:Clip2 ^@ http://purl.uniprot.org/uniprot/Q9Z0H8 ^@ 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 ^@ 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_0000083516|||http://purl.uniprot.org/annotation/VSP_015683 http://togogenome.org/gene/10090:Dapp1 ^@ http://purl.uniprot.org/uniprot/Q3TEK6|||http://purl.uniprot.org/uniprot/Q3UK44|||http://purl.uniprot.org/uniprot/Q3UL29|||http://purl.uniprot.org/uniprot/Q9QXT1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide|||PH|||Phosphoserine|||Phosphotyrosine|||SH2 ^@ http://purl.uniprot.org/annotation/PRO_0000079786 http://togogenome.org/gene/10090:Serpina1c ^@ http://purl.uniprot.org/uniprot/A0A0R4J0X5|||http://purl.uniprot.org/uniprot/Q00896 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Alpha-1-antitrypsin 1-3|||N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_0000032390|||http://purl.uniprot.org/annotation/PRO_5006451980 http://togogenome.org/gene/10090:Cd209d ^@ http://purl.uniprot.org/uniprot/Q3UW57|||http://purl.uniprot.org/uniprot/Q91ZW8 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-type lectin|||CD209 antigen-like protein D|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046607|||http://purl.uniprot.org/annotation/VSP_010071 http://togogenome.org/gene/10090:Adra1d ^@ http://purl.uniprot.org/uniprot/A2ANQ2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r87 ^@ http://purl.uniprot.org/uniprot/E9PZX4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245765 http://togogenome.org/gene/10090:Cyp4a10 ^@ http://purl.uniprot.org/uniprot/O88833 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Cytochrome P450 4A10|||Helical|||Phosphoserine|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000051815 http://togogenome.org/gene/10090:Smg7 ^@ http://purl.uniprot.org/uniprot/Q5RJH6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Nonsense-mediated mRNA decay factor SMG7|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||TPR 1|||TPR 2 ^@ http://purl.uniprot.org/annotation/PRO_0000076325|||http://purl.uniprot.org/annotation/VSP_016577|||http://purl.uniprot.org/annotation/VSP_016578|||http://purl.uniprot.org/annotation/VSP_016579 http://togogenome.org/gene/10090:Ano6 ^@ http://purl.uniprot.org/uniprot/A0A2I3BPX3|||http://purl.uniprot.org/uniprot/Q6P9J9 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Anoctamin dimerisation|||Anoctamin-6|||Constitutive lipid scramblase activity at basal cytosolic calcium levels.|||Cytoplasmic|||Decreased lipid scramblase activity.|||Decreased lipid scramblase and ion channel activity. Requires lower calcium levels for activation of ion channel activity.|||Expected to disrupt calcium binding. Loss of scramblase activity.|||Expected to disrupt calcium binding. Loss of scramblase and ion channel activity.|||Extracellular|||Helical|||In isoform 2.|||Increased speed of phospholipid scrambling.|||Increased speed of phospholipid scrambling. Constitutive scramblase activity at basal cytosolic calcium levels; when associated with A-518 and A-563.|||Increased speed of phospholipid scrambling. Constitutive scramblase activity at basal cytosolic calcium levels; when associated with A-563 and A-612.|||Increased speed of phospholipid scrambling. Requires lower calcium levels for activation of scramblase and ion channel activity. Constitutive scramblase activity at basal cytosolic calcium levels; when associated with A-518 and A-612.|||Loss of lipid scramblase activity.|||Moderately decreased sensitivity to activation by calcium.|||N-linked (GlcNAc...) asparagine|||No effect on lipid scramblase activity.|||Reduced channel activity and sensitivity to Ca(2+).|||Requires lower calcium levels for activation of scramblase and ion channel activity.|||Requires much higher calcium levels for the activation of scramblase and ion channel activity.|||Slightly increased lipid scramblase activity.|||Slower channel activation. Increased permeability to chloride ions. ^@ http://purl.uniprot.org/annotation/PRO_0000191758|||http://purl.uniprot.org/annotation/VSP_015654|||http://purl.uniprot.org/annotation/VSP_015655 http://togogenome.org/gene/10090:Tnfsfm13 ^@ http://purl.uniprot.org/uniprot/Q5F2A1|||http://purl.uniprot.org/uniprot/Q8BXS2 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||TNF family profile ^@ http://togogenome.org/gene/10090:Ezr ^@ http://purl.uniprot.org/uniprot/P26040|||http://purl.uniprot.org/uniprot/Q3UL48|||http://purl.uniprot.org/uniprot/Q4KML7|||http://purl.uniprot.org/uniprot/Q8CBU4 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ 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_0000219409 http://togogenome.org/gene/10090:Spacdr ^@ http://purl.uniprot.org/uniprot/Q9EQN3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Leucine-zipper|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TSC22 domain family protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000219375 http://togogenome.org/gene/10090:Kcna1 ^@ http://purl.uniprot.org/uniprot/P16388 ^@ Chain|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence 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|||In RNA edited version.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphoserine; by PKA|||Potassium voltage-gated channel subfamily A member 1|||S-palmitoyl cysteine|||S4-S5 linker|||Selectivity filter|||Tetramerization domain ^@ http://purl.uniprot.org/annotation/PRO_0000053969 http://togogenome.org/gene/10090:Lsmem1 ^@ http://purl.uniprot.org/uniprot/B2RVW5|||http://purl.uniprot.org/uniprot/Q3UQS2 ^@ 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_0000309273|||http://purl.uniprot.org/annotation/VSP_029105 http://togogenome.org/gene/10090:Btbd35f13 ^@ http://purl.uniprot.org/uniprot/B8JKF6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Tcaf1 ^@ http://purl.uniprot.org/uniprot/Q8BNE1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Peptidase M60|||TRPM8 channel-associated factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000320183|||http://purl.uniprot.org/annotation/VSP_031632|||http://purl.uniprot.org/annotation/VSP_031633|||http://purl.uniprot.org/annotation/VSP_031634 http://togogenome.org/gene/10090:Rad9b ^@ http://purl.uniprot.org/uniprot/Q6WBX7|||http://purl.uniprot.org/uniprot/Q8VC54 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Cell cycle checkpoint control protein RAD9B|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000226700 http://togogenome.org/gene/10090:Nudt19 ^@ http://purl.uniprot.org/uniprot/P11930 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ 2-fold increase in Km for CoA. Reduced affinity for CoA.|||3- to 4-fold increase in Km for CoA. Reduced affinity for CoA.|||3-fold increase in Km for CoA.|||4-fold increase in Km for CoA. Reduced affinity for CoA.|||Acyl-coenzyme A diphosphatase NUDT19|||Disordered|||Important for coenzyme A binding|||Loss of fatty acyl-coenzyme A diphosphatase activity.|||Microbody targeting signal|||N6-succinyllysine|||No significant effect on Km for CoA.|||Nudix box|||Nudix hydrolase|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000057119 http://togogenome.org/gene/10090:Tbx5 ^@ http://purl.uniprot.org/uniprot/P70326|||http://purl.uniprot.org/uniprot/Q5CZX7 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Basic and acidic residues|||Disordered|||N6-acetyllysine|||Polar residues|||T-box|||T-box transcription factor TBX5 ^@ http://purl.uniprot.org/annotation/PRO_0000184436 http://togogenome.org/gene/10090:Zfp759 ^@ http://purl.uniprot.org/uniprot/Q7M6X3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Alx1 ^@ http://purl.uniprot.org/uniprot/Q8C8B0 ^@ Chain|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||DNA Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ ALX homeobox protein 1|||Homeobox|||Loss of acetylation. Decreased binding affinity to EP300. Loss of EP300-mediated transcriptional coactivation.|||N6-acetyllysine; by EP300|||OAR|||Phosphoserine|||Transactivation domain ^@ http://purl.uniprot.org/annotation/PRO_0000048856 http://togogenome.org/gene/10090:Tmem82 ^@ http://purl.uniprot.org/uniprot/Q8R115 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Pro residues|||Transmembrane protein 82 ^@ http://purl.uniprot.org/annotation/PRO_0000309237 http://togogenome.org/gene/10090:Foxr1 ^@ http://purl.uniprot.org/uniprot/Q3UTB7 ^@ Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||DNA Binding|||Region|||Splice Variant ^@ Disordered|||Fork-head|||Forkhead box protein R1|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000253779|||http://purl.uniprot.org/annotation/VSP_021113|||http://purl.uniprot.org/annotation/VSP_021114 http://togogenome.org/gene/10090:Lhfpl5 ^@ http://purl.uniprot.org/uniprot/B2RWL4|||http://purl.uniprot.org/uniprot/Q4KL25 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In hscy.|||LHFPL tetraspan subfamily member 5 protein ^@ http://purl.uniprot.org/annotation/PRO_0000285923 http://togogenome.org/gene/10090:1700012B07Rik ^@ http://purl.uniprot.org/uniprot/Q3V0S8|||http://purl.uniprot.org/uniprot/Q9DAE9 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gss ^@ http://purl.uniprot.org/uniprot/P51855|||http://purl.uniprot.org/uniprot/Q3UEE2|||http://purl.uniprot.org/uniprot/Q541E2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue ^@ Glutathione synthase substrate-binding|||Glutathione synthetase|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000211262 http://togogenome.org/gene/10090:Sart1 ^@ http://purl.uniprot.org/uniprot/Q9Z315 ^@ 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|||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|||U4/U6.U5 tri-snRNP-associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000223309 http://togogenome.org/gene/10090:Drc7 ^@ http://purl.uniprot.org/uniprot/Q6V3W6 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Dynein regulatory complex subunit 7|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000279436|||http://purl.uniprot.org/annotation/VSP_023440|||http://purl.uniprot.org/annotation/VSP_023441 http://togogenome.org/gene/10090:Or2w3b ^@ http://purl.uniprot.org/uniprot/Q5NCD6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp382 ^@ http://purl.uniprot.org/uniprot/B2RXC5 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||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|||Disordered|||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_0000361567 http://togogenome.org/gene/10090:H2-Eb1 ^@ http://purl.uniprot.org/uniprot/O78196 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015096816 http://togogenome.org/gene/10090:Cxcl14 ^@ http://purl.uniprot.org/uniprot/Q6AXC2|||http://purl.uniprot.org/uniprot/Q9WUQ5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Motif|||Sequence Conflict|||Signal Peptide ^@ C-X-C motif chemokine 14|||Chemokine interleukin-8-like|||D-box ^@ http://purl.uniprot.org/annotation/PRO_0000005116|||http://purl.uniprot.org/annotation/PRO_5015098166 http://togogenome.org/gene/10090:Efcab7 ^@ http://purl.uniprot.org/uniprot/Q8VDY4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand calcium-binding domain-containing protein 7|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317267 http://togogenome.org/gene/10090:Il17c ^@ http://purl.uniprot.org/uniprot/Q8K4C5 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Interleukin-17C ^@ http://purl.uniprot.org/annotation/PRO_0000421684 http://togogenome.org/gene/10090:Cyp2j11 ^@ http://purl.uniprot.org/uniprot/Q3UNV2 ^@ Binding Site|||Site ^@ Binding Site ^@ ^@ http://togogenome.org/gene/10090:Alpk2 ^@ http://purl.uniprot.org/uniprot/Q91ZB0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict ^@ Alpha-protein kinase 2|||Alpha-type protein kinase|||Basic and acidic residues|||Disordered|||Ig-like 1|||Ig-like 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000291383 http://togogenome.org/gene/10090:Ints7 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0E4|||http://purl.uniprot.org/uniprot/Q7TQK1 ^@ 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.|||Integrator complex subunit 7|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000259550|||http://purl.uniprot.org/annotation/VSP_021465|||http://purl.uniprot.org/annotation/VSP_021466 http://togogenome.org/gene/10090:Nufip1 ^@ http://purl.uniprot.org/uniprot/Q9QXX8 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Zinc Finger ^@ Basic residues|||Bipartite nuclear localization signal|||C2H2-type|||Disordered|||FMR1-interacting protein NUFIP1|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000245519 http://togogenome.org/gene/10090:Igf2bp3 ^@ http://purl.uniprot.org/uniprot/Q9CPN8 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Insulin-like growth factor 2 mRNA-binding protein 3|||KH 1|||KH 2|||KH 3|||KH 4|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000282539 http://togogenome.org/gene/10090:Pfdn6 ^@ http://purl.uniprot.org/uniprot/Q03958|||http://purl.uniprot.org/uniprot/Q792E4 ^@ 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_0000124851 http://togogenome.org/gene/10090:Phf11a ^@ http://purl.uniprot.org/uniprot/Q8BVM9 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Region|||Zinc Finger ^@ C2HC pre-PHD-type|||Disordered|||PHD finger protein 11A|||PHD-type; degenerate ^@ http://purl.uniprot.org/annotation/PRO_0000385017 http://togogenome.org/gene/10090:Lmo7 ^@ http://purl.uniprot.org/uniprot/A0T1J8|||http://purl.uniprot.org/uniprot/E9PYF4|||http://purl.uniprot.org/uniprot/E9PYI7|||http://purl.uniprot.org/uniprot/Q6ZQ32 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||LIM zinc-binding|||PDZ|||Polar residues ^@ http://togogenome.org/gene/10090:Ubr3 ^@ http://purl.uniprot.org/uniprot/Q5U430|||http://purl.uniprot.org/uniprot/Q8CAW0 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase UBR3|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||RING-type; degenerate|||UBR-type ^@ http://purl.uniprot.org/annotation/PRO_0000278185|||http://purl.uniprot.org/annotation/VSP_023143|||http://purl.uniprot.org/annotation/VSP_023144|||http://purl.uniprot.org/annotation/VSP_023145 http://togogenome.org/gene/10090:Fes ^@ http://purl.uniprot.org/uniprot/P16879|||http://purl.uniprot.org/uniprot/Q8CGG9 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Disordered|||F-BAR|||Important for interaction with membranes containing phosphoinositides|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SH2|||Tyrosine-protein kinase Fes/Fps ^@ http://purl.uniprot.org/annotation/PRO_0000088089 http://togogenome.org/gene/10090:Sh3bp2 ^@ http://purl.uniprot.org/uniprot/E9QJU7|||http://purl.uniprot.org/uniprot/Q3UD40|||http://purl.uniprot.org/uniprot/Q5U3L0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||PH|||Polar residues|||Pro residues|||SH2 ^@ http://togogenome.org/gene/10090:Sppl3 ^@ http://purl.uniprot.org/uniprot/Q9CUS9 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Motif|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Does not inhibit NFAT-induced transcription activation.|||Helical|||Lumenal|||PAL|||Signal peptide peptidase-like 3 ^@ http://purl.uniprot.org/annotation/PRO_0000073913 http://togogenome.org/gene/10090:Blzf1 ^@ http://purl.uniprot.org/uniprot/Q3V485|||http://purl.uniprot.org/uniprot/Q8R2X8 ^@ 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 ^@ Disordered|||Essential for interaction with GORASP2|||Golgin-45|||In isoform 2.|||Phosphoserine|||Polar residues|||Reduced interaction with GORASP2.|||Reduced interaction with GORASP2; when associated with A-393.|||Reduced interaction with GORASP2; when associated with A-396.|||Tankyrase-binding motif ^@ http://purl.uniprot.org/annotation/PRO_0000087540|||http://purl.uniprot.org/annotation/VSP_011188 http://togogenome.org/gene/10090:Gm13285 ^@ http://purl.uniprot.org/uniprot/B1AYI3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015087047 http://togogenome.org/gene/10090:Vmn1r183 ^@ http://purl.uniprot.org/uniprot/Q8K3N5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Plekha2 ^@ http://purl.uniprot.org/uniprot/Q9ERS5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||PH 1|||PH 2|||Phosphoserine|||Pleckstrin homology domain-containing family A member 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053877 http://togogenome.org/gene/10090:Cat ^@ http://purl.uniprot.org/uniprot/P24270 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Acatalasemia.|||Basic and acidic residues|||Catalase|||Disordered|||Microbody targeting signal; atypical|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000084902 http://togogenome.org/gene/10090:9130401M01Rik ^@ http://purl.uniprot.org/uniprot/Q9D2X8 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Uncharacterized protein C8orf76 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000225636 http://togogenome.org/gene/10090:Tchhl1 ^@ http://purl.uniprot.org/uniprot/Q9D3P1 ^@ 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|||EF-hand|||Polar residues|||Trichohyalin-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000341544 http://togogenome.org/gene/10090:Rapgef4 ^@ http://purl.uniprot.org/uniprot/A2ASW4|||http://purl.uniprot.org/uniprot/A2ASW8|||http://purl.uniprot.org/uniprot/Q571A8|||http://purl.uniprot.org/uniprot/Q9CS95|||http://purl.uniprot.org/uniprot/Q9EQZ6 ^@ 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|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ 2-fold reduction in maximal activity.|||Cyclic nucleotide-binding|||DEP|||In isoform 2.|||In isoform 3.|||Less than 10% of the wild-type maximal activity.|||N-terminal Ras-GEF|||Rap guanine nucleotide exchange factor 4|||Ras-GEF ^@ http://purl.uniprot.org/annotation/PRO_0000068871|||http://purl.uniprot.org/annotation/VSP_007614|||http://purl.uniprot.org/annotation/VSP_007615 http://togogenome.org/gene/10090:Wee2 ^@ http://purl.uniprot.org/uniprot/Q66JT0 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes nuclear localization.|||Abolishes phosphorylation and impairs ability to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage and metaphase II exit during egg activation.|||Abolishes the cytoplasmic localization; when associated with A-311; A-316 and A-320.|||Abolishes the cytoplasmic localization; when associated with A-311; A-316 and A-322.|||Abolishes the cytoplasmic localization; when associated with A-311; A-320 and A-322.|||Abolishes the cytoplasmic localization; when associated with A-316; A-320 and A-322.|||Basic and acidic residues|||Disordered|||Loss of function.|||Mimicks phosphorylation state, lesading to enhance kinase activity and promote pronuclear formation.|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CaMK2 and PKA|||Polar residues|||Protein kinase|||Proton acceptor|||Wee1-like protein kinase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000248080 http://togogenome.org/gene/10090:Mrps14 ^@ http://purl.uniprot.org/uniprot/Q9CR88 ^@ Chain|||Molecule Processing ^@ Chain ^@ Small ribosomal subunit protein uS14m ^@ http://purl.uniprot.org/annotation/PRO_0000131014 http://togogenome.org/gene/10090:Cenpj ^@ http://purl.uniprot.org/uniprot/Q569L8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Alpha/beta-tubulin binding|||Basic and acidic residues|||Centromere protein J|||Disordered|||Interaction with STIL|||Phosphoserine|||Phosphoserine; by PLK2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000286053 http://togogenome.org/gene/10090:Aaas ^@ http://purl.uniprot.org/uniprot/P58742|||http://purl.uniprot.org/uniprot/Q8BU75 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat ^@ Aladin|||Disordered|||Microbody targeting signal|||N-acetylcysteine|||Phosphoserine|||Polar residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000050829 http://togogenome.org/gene/10090:Gpr146 ^@ http://purl.uniprot.org/uniprot/Q99LE2 ^@ 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|||Probable G-protein coupled receptor 146 ^@ http://purl.uniprot.org/annotation/PRO_0000069623 http://togogenome.org/gene/10090:Tubg2 ^@ http://purl.uniprot.org/uniprot/Q6F4J0|||http://purl.uniprot.org/uniprot/Q8VCK3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site ^@ Phosphomimetic mutant that lead to increased centrosome number.|||Phosphoserine; by BRSK1|||Tubulin gamma-2 chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase|||Weak effect possibly due to low expression of this mutant. ^@ http://purl.uniprot.org/annotation/PRO_0000048469 http://togogenome.org/gene/10090:Fads1 ^@ http://purl.uniprot.org/uniprot/Q920L1 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Acyl-CoA (8-3)-desaturase|||Cytochrome b5 heme-binding|||Cytoplasmic|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Lumenal|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000307097 http://togogenome.org/gene/10090:Lrrc42 ^@ http://purl.uniprot.org/uniprot/Q8R2U7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ 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_0000223471 http://togogenome.org/gene/10090:Sclt1 ^@ http://purl.uniprot.org/uniprot/G5E861 ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Splice Variant ^@ In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||Sodium channel and clathrin linker 1 ^@ http://purl.uniprot.org/annotation/PRO_0000422822|||http://purl.uniprot.org/annotation/VSP_047144|||http://purl.uniprot.org/annotation/VSP_047145 http://togogenome.org/gene/10090:Or6d14 ^@ http://purl.uniprot.org/uniprot/Q8VG27 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp960 ^@ http://purl.uniprot.org/uniprot/L7N267|||http://purl.uniprot.org/uniprot/Q3ULR3 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Dnajc5b ^@ http://purl.uniprot.org/uniprot/Q9CQ94 ^@ 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_0000071056 http://togogenome.org/gene/10090:Gjd3 ^@ http://purl.uniprot.org/uniprot/A0A654IET7|||http://purl.uniprot.org/uniprot/Q91YD1 ^@ 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 delta-3 protein|||Gap junction protein cysteine-rich|||Helical|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000313009 http://togogenome.org/gene/10090:Etv6 ^@ http://purl.uniprot.org/uniprot/P97360|||http://purl.uniprot.org/uniprot/Q80WR3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ 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|||N6-acetyllysine; alternate|||PNT|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription factor ETV6 ^@ http://purl.uniprot.org/annotation/PRO_0000204122 http://togogenome.org/gene/10090:Canx ^@ http://purl.uniprot.org/uniprot/P35564|||http://purl.uniprot.org/uniprot/Q5SUC3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||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|||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_0000004199|||http://purl.uniprot.org/annotation/PRO_5014205900 http://togogenome.org/gene/10090:Mkrn2 ^@ http://purl.uniprot.org/uniprot/Q9ERV1 ^@ 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|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||Disordered|||E3 ubiquitin-protein ligase makorin-2|||Makorin-type Cys-His|||Phosphoserine|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055956 http://togogenome.org/gene/10090:Rhbdf2 ^@ http://purl.uniprot.org/uniprot/Q80WQ6 ^@ 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|||Helical|||Inactive rhomboid protein 2|||Lumenal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000341939 http://togogenome.org/gene/10090:Plpp6 ^@ http://purl.uniprot.org/uniprot/Q9D4F2 ^@ Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Modified Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Nucleophile|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Phosphoserine|||Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6|||Proton donors|||Stabilizes the active site histidine for nucleophilic attack ^@ http://purl.uniprot.org/annotation/PRO_0000239397 http://togogenome.org/gene/10090:Or51aa2 ^@ http://purl.uniprot.org/uniprot/L7N462 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Avl9 ^@ http://purl.uniprot.org/uniprot/Q80U56 ^@ 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|||Late secretory pathway protein AVL9 homolog|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000247179 http://togogenome.org/gene/10090:Kcnma1 ^@ http://purl.uniprot.org/uniprot/A0A087WQ41|||http://purl.uniprot.org/uniprot/A0A087WQN5|||http://purl.uniprot.org/uniprot/A0A087WRS4|||http://purl.uniprot.org/uniprot/A0A286YD35|||http://purl.uniprot.org/uniprot/A0A286YDM6|||http://purl.uniprot.org/uniprot/Q08460|||http://purl.uniprot.org/uniprot/Q3UXG3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes sensitivity to Mg(2+), but not sensitivity to Ca(2+).|||Alters calcium binding.|||Alters the voltage-dependent gating.|||Alters the voltage-dependent gating; when associated with K-284.|||Alters the voltage-dependent gating; when associated with R-287.|||Basic and acidic residues|||Calcium bowl|||Calcium-activated potassium channel BK alpha subunit|||Calcium-activated potassium channel subunit alpha-1|||Cytoplasmic|||Disordered|||Does not affect sensitivity to Ca(2+).|||Extracellular|||Helical|||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|||Heme-binding motif|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Ion transport|||Loss of phosphorylation-independent activation of channel activity by ethanol. CaMK2-dependent phosphorylation leads to populations of partially phosphorylated tetramers with a range of responses to ethanol from activation to inhibition.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pore-forming; Name=P region|||RCK N-terminal|||Reduced sensitivity to Ca(2+).|||Reduces sensitivity to Mg(2+), but not sensitivity to Ca(2+).|||Remains sensitive to Mg(2+).|||S-palmitoyl cysteine|||Segment S10|||Segment S7|||Segment S8|||Segment S9|||Selectivity for potassium ^@ http://purl.uniprot.org/annotation/PRO_0000054134|||http://purl.uniprot.org/annotation/VSP_009959|||http://purl.uniprot.org/annotation/VSP_009960|||http://purl.uniprot.org/annotation/VSP_009961|||http://purl.uniprot.org/annotation/VSP_009962|||http://purl.uniprot.org/annotation/VSP_009963|||http://purl.uniprot.org/annotation/VSP_009964|||http://purl.uniprot.org/annotation/VSP_009965 http://togogenome.org/gene/10090:Fam47c ^@ http://purl.uniprot.org/uniprot/Q14BE7 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Prodh ^@ http://purl.uniprot.org/uniprot/Q9WU79 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrion|||N6-acetyllysine|||Proline dehydrogenase 1, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000025801 http://togogenome.org/gene/10090:Fam151a ^@ http://purl.uniprot.org/uniprot/Q8QZW3 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Region|||Transmembrane ^@ Disordered|||Helical|||Protein FAM151A ^@ http://purl.uniprot.org/annotation/PRO_0000310956 http://togogenome.org/gene/10090:Naa35 ^@ http://purl.uniprot.org/uniprot/Q6PHQ8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-alpha-acetyltransferase 35, NatC auxiliary subunit|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000308616 http://togogenome.org/gene/10090:Bet1l ^@ http://purl.uniprot.org/uniprot/O35153 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ BET1-like protein|||Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Lumenal|||Phosphoserine|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000233057 http://togogenome.org/gene/10090:Plekhb1 ^@ http://purl.uniprot.org/uniprot/D3YV71|||http://purl.uniprot.org/uniprot/Q3TP62|||http://purl.uniprot.org/uniprot/Q9QYE9 ^@ 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 and isoform 4.|||In isoform 3 and isoform 4.|||PH|||Pleckstrin homology domain-containing family B member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000053887|||http://purl.uniprot.org/annotation/VSP_009781|||http://purl.uniprot.org/annotation/VSP_009782 http://togogenome.org/gene/10090:Nedd8 ^@ http://purl.uniprot.org/uniprot/P29595|||http://purl.uniprot.org/uniprot/Q3UI46 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Site ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Propeptide|||Region|||Site ^@ Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Interaction with UBE1C|||N6-acetyllysine|||NEDD8|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000042769|||http://purl.uniprot.org/annotation/PRO_0000042770 http://togogenome.org/gene/10090:Tmem38a ^@ http://purl.uniprot.org/uniprot/Q3TMP8 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||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_0000271069 http://togogenome.org/gene/10090:Malt1 ^@ http://purl.uniprot.org/uniprot/Q2TBA3 ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Caspase-like|||Death|||Disordered|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog|||N-acetylserine|||Nuclear export signal|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000272961|||http://purl.uniprot.org/annotation/VSP_052279 http://togogenome.org/gene/10090:Samm50 ^@ http://purl.uniprot.org/uniprot/Q8BGH2 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict ^@ N6-methyllysine|||POTRA|||Sorting and assembly machinery component 50 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000286399 http://togogenome.org/gene/10090:Cln5 ^@ http://purl.uniprot.org/uniprot/B2RUP8|||http://purl.uniprot.org/uniprot/Q3UMW8 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Ceroid-lipofuscinosis neuronal protein 5 homolog|||Ceroid-lipofuscinosis neuronal protein 5 homolog, secreted form|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Membrane-anchoring|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000330471|||http://purl.uniprot.org/annotation/PRO_0000438010|||http://purl.uniprot.org/annotation/PRO_5014298311 http://togogenome.org/gene/10090:Vmn1r138 ^@ http://purl.uniprot.org/uniprot/D3YTY2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cd248 ^@ http://purl.uniprot.org/uniprot/Q91V98 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||Disordered|||EGF-like; calcium-binding|||Endosialin|||Extracellular|||Helical|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues|||Pro residues|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_0000045800 http://togogenome.org/gene/10090:Or51k2 ^@ http://purl.uniprot.org/uniprot/Q8VF02 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tm7sf2 ^@ http://purl.uniprot.org/uniprot/Q3V3I6|||http://purl.uniprot.org/uniprot/Q71KT5 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Delta(14)-sterol reductase TM7SF2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000331121 http://togogenome.org/gene/10090:Enkur ^@ http://purl.uniprot.org/uniprot/Q4KL11|||http://purl.uniprot.org/uniprot/Q6SP97 ^@ 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_0000086976 http://togogenome.org/gene/10090:Map4k4 ^@ http://purl.uniprot.org/uniprot/A0A0A6YW53|||http://purl.uniprot.org/uniprot/A0A0A6YWM8|||http://purl.uniprot.org/uniprot/A0A0A6YWR8|||http://purl.uniprot.org/uniprot/B2RUE8|||http://purl.uniprot.org/uniprot/B7ZNR8|||http://purl.uniprot.org/uniprot/B7ZNR9|||http://purl.uniprot.org/uniprot/P97820|||http://purl.uniprot.org/uniprot/Q3UTY9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||CNH|||Disordered|||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_0000086281 http://togogenome.org/gene/10090:Grin3a ^@ http://purl.uniprot.org/uniprot/A2AIR5 ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||GIT1-binding|||Glutamate receptor ionotropic, NMDA 3A|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PPP2CB binding site ^@ http://purl.uniprot.org/annotation/PRO_5027148248|||http://purl.uniprot.org/annotation/VSP_061048 http://togogenome.org/gene/10090:Shisal2a ^@ http://purl.uniprot.org/uniprot/A2A9G7 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||Protein shisa-like-2A ^@ http://purl.uniprot.org/annotation/PRO_0000317721 http://togogenome.org/gene/10090:Defb45 ^@ http://purl.uniprot.org/uniprot/Q3V490 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Beta-defensin ^@ http://purl.uniprot.org/annotation/PRO_5015020019 http://togogenome.org/gene/10090:Kirrel2 ^@ http://purl.uniprot.org/uniprot/A0A4X8|||http://purl.uniprot.org/uniprot/Q7TSU7 ^@ 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 ^@ Basic and acidic residues|||Cell attachment site|||Cytoplasmic|||Disordered|||Does not modify the structure of cell contacts. No effect on localization at the plasma membrane. No change in shedding activity.|||Enhances stability. Modifies the structure of cell contacts. Localization at the plasma membrane is increased. Does not affect dimerization. No change in shedding activity.|||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 domain-containing protein|||In isoform 2.|||Kin of IRRE-like protein 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000015097|||http://purl.uniprot.org/annotation/PRO_5002621994|||http://purl.uniprot.org/annotation/VSP_011786 http://togogenome.org/gene/10090:Kcnq5 ^@ http://purl.uniprot.org/uniprot/E9Q9F1|||http://purl.uniprot.org/uniprot/G3UYG5|||http://purl.uniprot.org/uniprot/Q9JK45 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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|||Ion transport|||Phosphoserine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium channel voltage dependent KCNQ C-terminal|||Potassium voltage-gated channel subfamily KQT member 5|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000054041 http://togogenome.org/gene/10090:Arhgap10 ^@ http://purl.uniprot.org/uniprot/Q6Y5D8|||http://purl.uniprot.org/uniprot/Q8C9L7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant ^@ BAR|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inactive. Abolishes GTPase activity in vitro. Greatly diminishes cytoskeletal reorganization.|||PH|||Polar residues|||Pro residues|||Rho GTPase-activating protein 10|||Rho-GAP|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000304915|||http://purl.uniprot.org/annotation/VSP_028127|||http://purl.uniprot.org/annotation/VSP_028128|||http://purl.uniprot.org/annotation/VSP_028129 http://togogenome.org/gene/10090:Mzt2 ^@ http://purl.uniprot.org/uniprot/Q9CQ25 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||Mitotic-spindle organizing protein 2|||Omega-N-methylarginine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000338986 http://togogenome.org/gene/10090:H2al2b ^@ http://purl.uniprot.org/uniprot/A9Z055 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Transcription factor CBF/NF-Y/archaeal histone ^@ http://togogenome.org/gene/10090:Slc22a29 ^@ http://purl.uniprot.org/uniprot/Q8BWG6 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:Sra1 ^@ http://purl.uniprot.org/uniprot/A0A8Q0Q6H9|||http://purl.uniprot.org/uniprot/Q80VJ2 ^@ 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|||Pro residues|||SRA1/Sec31|||Steroid receptor RNA activator 1 ^@ http://purl.uniprot.org/annotation/PRO_0000234106 http://togogenome.org/gene/10090:Scx ^@ http://purl.uniprot.org/uniprot/Q53ZC3|||http://purl.uniprot.org/uniprot/Q64124 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Basic and acidic residues|||Basic helix-loop-helix transcription factor scleraxis|||Disordered|||Pro residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127436 http://togogenome.org/gene/10090:Fbxo25 ^@ http://purl.uniprot.org/uniprot/Q9D2Y6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ F-box|||F-box only protein 25|||Interaction with beta-actin ^@ http://purl.uniprot.org/annotation/PRO_0000119912 http://togogenome.org/gene/10090:Prdm11 ^@ http://purl.uniprot.org/uniprot/A2AGX3 ^@ 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)|||PR domain-containing protein 11|||Phosphoserine|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000416113 http://togogenome.org/gene/10090:Mgat4c ^@ http://purl.uniprot.org/uniprot/Q9D306 ^@ 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 C|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000288598 http://togogenome.org/gene/10090:Or7e177 ^@ http://purl.uniprot.org/uniprot/Q8VFJ0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rasd2 ^@ http://purl.uniprot.org/uniprot/P63032 ^@ 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_0000082721|||http://purl.uniprot.org/annotation/PRO_0000281376 http://togogenome.org/gene/10090:Gpr135 ^@ http://purl.uniprot.org/uniprot/A7E1Z8|||http://purl.uniprot.org/uniprot/Q7TQP2 ^@ 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 receptor 135|||G-protein coupled receptors family 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_0000069613 http://togogenome.org/gene/10090:Flii ^@ http://purl.uniprot.org/uniprot/Q9JJ28 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||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|||Phosphoserine|||Phosphoserine; by SGK3|||Protein flightless-1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000218751 http://togogenome.org/gene/10090:Prrt3 ^@ http://purl.uniprot.org/uniprot/A0A0N4SVB5|||http://purl.uniprot.org/uniprot/Q6PE13 ^@ 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 ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Proline-rich transmembrane protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000251979|||http://purl.uniprot.org/annotation/PRO_5015043365 http://togogenome.org/gene/10090:Rhox4f ^@ http://purl.uniprot.org/uniprot/Q2MDF8 ^@ DNA Binding|||Domain Extent|||Region ^@ DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox ^@ http://togogenome.org/gene/10090:Or9m1 ^@ http://purl.uniprot.org/uniprot/L7MU57 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nkain3 ^@ http://purl.uniprot.org/uniprot/Q3URJ8 ^@ 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.|||Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000263094|||http://purl.uniprot.org/annotation/VSP_021858|||http://purl.uniprot.org/annotation/VSP_029300 http://togogenome.org/gene/10090:Peli1 ^@ http://purl.uniprot.org/uniprot/Q8C669 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ E3 ubiquitin-protein ligase pellino homolog 1|||FHA; atypical|||Ring-like domain; necessary for ubiquitination of RIPK3 ^@ http://purl.uniprot.org/annotation/PRO_0000194173 http://togogenome.org/gene/10090:Ccdc32 ^@ http://purl.uniprot.org/uniprot/Q3UHY7 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Arid5b ^@ http://purl.uniprot.org/uniprot/Q8BM75 ^@ 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 5B|||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_0000200582|||http://purl.uniprot.org/annotation/VSP_009357|||http://purl.uniprot.org/annotation/VSP_009358|||http://purl.uniprot.org/annotation/VSP_009359|||http://purl.uniprot.org/annotation/VSP_009360 http://togogenome.org/gene/10090:Ccdc85a ^@ http://purl.uniprot.org/uniprot/E0CX32|||http://purl.uniprot.org/uniprot/Q5SP85 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Coiled-coil domain-containing protein 85A|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000271105|||http://purl.uniprot.org/annotation/VSP_022280|||http://purl.uniprot.org/annotation/VSP_022283 http://togogenome.org/gene/10090:Plek2 ^@ http://purl.uniprot.org/uniprot/Q9WV52 ^@ Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Strand ^@ DEP|||N-acetylmethionine|||PH 1|||PH 2|||Phosphoserine|||Pleckstrin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000053863 http://togogenome.org/gene/10090:Sult2a2 ^@ http://purl.uniprot.org/uniprot/Q3UEP5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Sulfotransferase ^@ http://togogenome.org/gene/10090:Nme2 ^@ http://purl.uniprot.org/uniprot/Q01768|||http://purl.uniprot.org/uniprot/Q5NC82 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region ^@ Interaction with AKAP13|||Nucleoside diphosphate kinase B|||Nucleoside diphosphate kinase-like|||Pros-phosphohistidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000137118 http://togogenome.org/gene/10090:Crkl ^@ http://purl.uniprot.org/uniprot/A0A338P6Q0|||http://purl.uniprot.org/uniprot/A2RS58|||http://purl.uniprot.org/uniprot/P47941 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Crk-like protein|||Disordered|||Phosphotyrosine|||SH2|||SH3|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000079348 http://togogenome.org/gene/10090:Htr6 ^@ http://purl.uniprot.org/uniprot/Q14AW8|||http://purl.uniprot.org/uniprot/Q9R1C8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ 5-hydroxytryptamine receptor 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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000068975 http://togogenome.org/gene/10090:Glp1r ^@ http://purl.uniprot.org/uniprot/O35659 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ ADP-ribosylarginine|||ADP-ribosylcysteine|||Cytoplasmic|||Extracellular|||Glucagon-like peptide 1 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|||Interaction with the endogenous ligand GLP-1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000012836 http://togogenome.org/gene/10090:Trim25 ^@ http://purl.uniprot.org/uniprot/Q3TU94|||http://purl.uniprot.org/uniprot/Q61510 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ B30.2/SPRY|||Disordered|||E3 ubiquitin/ISG15 ligase TRIM25|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056234 http://togogenome.org/gene/10090:Aadacl4 ^@ http://purl.uniprot.org/uniprot/B1AVU5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Alpha/beta hydrolase fold-3|||Helical ^@ http://togogenome.org/gene/10090:Slc35d1 ^@ http://purl.uniprot.org/uniprot/A2AKQ0 ^@ 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.|||Nucleotide sugar transporter SLC35D1 ^@ http://purl.uniprot.org/annotation/PRO_0000440990|||http://purl.uniprot.org/annotation/VSP_059020 http://togogenome.org/gene/10090:Paqr7 ^@ http://purl.uniprot.org/uniprot/Q3TT73|||http://purl.uniprot.org/uniprot/Q80ZE4 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||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 alpha ^@ http://purl.uniprot.org/annotation/PRO_0000218836 http://togogenome.org/gene/10090:Nsun2 ^@ http://purl.uniprot.org/uniprot/Q1HFZ0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||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|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ 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.|||Loss of RNA 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_0000289224|||http://purl.uniprot.org/annotation/VSP_025969 http://togogenome.org/gene/10090:Bcl6b ^@ http://purl.uniprot.org/uniprot/O88282|||http://purl.uniprot.org/uniprot/Q5BKP3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||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|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000047101 http://togogenome.org/gene/10090:Arhgef11 ^@ http://purl.uniprot.org/uniprot/Q68FM7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DH|||Disordered|||PDZ|||PH|||Polar residues|||Pro residues|||RGS ^@ http://togogenome.org/gene/10090:Supt5 ^@ http://purl.uniprot.org/uniprot/O55201 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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; 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with RNA polymerase II|||Interaction with SUPT4H1 and SUPT4H2|||KOW 1|||KOW 2|||KOW 3|||KOW 4|||KOW 5|||N6-acetyllysine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK9|||Polar residues|||Pro residues|||Symmetric dimethylarginine; alternate|||Transcription elongation factor SPT5 ^@ http://purl.uniprot.org/annotation/PRO_0000208469|||http://purl.uniprot.org/annotation/VSP_016283 http://togogenome.org/gene/10090:Gsc ^@ http://purl.uniprot.org/uniprot/Q02591 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein goosecoid ^@ http://purl.uniprot.org/annotation/PRO_0000048886 http://togogenome.org/gene/10090:Meikin ^@ http://purl.uniprot.org/uniprot/Q5F2C3|||http://purl.uniprot.org/uniprot/Q9D5P1 ^@ 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.|||Meiosis-specific kinetochore protein|||POLO box domain (PBD)-binding|||Polar residues|||Required for localization to kinetochores ^@ http://purl.uniprot.org/annotation/PRO_0000432391|||http://purl.uniprot.org/annotation/VSP_057509 http://togogenome.org/gene/10090:Tcerg1l ^@ http://purl.uniprot.org/uniprot/Q3B807 ^@ 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|||FF 1|||FF 2|||In isoform 2.|||In isoform 3.|||Transcription elongation regulator 1-like protein|||WW 1|||WW 2 ^@ http://purl.uniprot.org/annotation/PRO_0000312873|||http://purl.uniprot.org/annotation/VSP_029925|||http://purl.uniprot.org/annotation/VSP_029926|||http://purl.uniprot.org/annotation/VSP_029927 http://togogenome.org/gene/10090:Spdya ^@ http://purl.uniprot.org/uniprot/B2RWC8|||http://purl.uniprot.org/uniprot/Q5IBH7 ^@ 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 ^@ Abolishes interaction with CDK2.|||Basic and acidic residues|||Disordered|||In isoform 1.|||No effect on CDK2-binding.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Speedy protein A|||Speedy/Ringo box; Required for CDK-binding ^@ http://purl.uniprot.org/annotation/PRO_0000234113|||http://purl.uniprot.org/annotation/VSP_052029|||http://purl.uniprot.org/annotation/VSP_052030 http://togogenome.org/gene/10090:Pparg ^@ http://purl.uniprot.org/uniprot/M1VPI1|||http://purl.uniprot.org/uniprot/P37238|||http://purl.uniprot.org/uniprot/Q6GU14 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||DNA Binding|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 9aaTAD|||In isoform 1.|||Increases basal and ligand-induced adipogenic activity. Abolishes repression by PER2 on transactivation activity.|||Interaction with FAM120B|||NR C4-type|||NR LBD|||No effect on repression by PER2 on transactivation activity.|||No loss of ubiquitination by FBXO9.|||Nuclear receptor|||O-linked (GlcNAc) threonine|||Peroxisome proliferator-activated receptor gamma|||Phosphoserine; by MAPK ^@ http://purl.uniprot.org/annotation/PRO_0000053494|||http://purl.uniprot.org/annotation/VSP_003647 http://togogenome.org/gene/10090:Reep1 ^@ http://purl.uniprot.org/uniprot/Q8BGH4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Polar residues|||Receptor expression-enhancing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000101822 http://togogenome.org/gene/10090:Gm6370 ^@ http://purl.uniprot.org/uniprot/L7N250 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Fxyd7 ^@ http://purl.uniprot.org/uniprot/P59648 ^@ 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_0000148191 http://togogenome.org/gene/10090:Rrp1b ^@ http://purl.uniprot.org/uniprot/Q91YK2 ^@ 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|||Basic residues|||Citrulline|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ribosomal RNA processing protein 1 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000340116 http://togogenome.org/gene/10090:Psmd12 ^@ http://purl.uniprot.org/uniprot/Q9D8W5 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ 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|||N-acetylalanine|||N6-acetyllysine|||PCI|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000173862 http://togogenome.org/gene/10090:Xrcc5 ^@ http://purl.uniprot.org/uniprot/P27641 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||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|||X-ray repair cross-complementing protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000084341 http://togogenome.org/gene/10090:Ccdc18 ^@ http://purl.uniprot.org/uniprot/Q640L5 ^@ 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|||Coiled-coil domain-containing protein 18|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000284776|||http://purl.uniprot.org/annotation/VSP_024637|||http://purl.uniprot.org/annotation/VSP_024638|||http://purl.uniprot.org/annotation/VSP_024639|||http://purl.uniprot.org/annotation/VSP_024640|||http://purl.uniprot.org/annotation/VSP_024641|||http://purl.uniprot.org/annotation/VSP_024642|||http://purl.uniprot.org/annotation/VSP_024643 http://togogenome.org/gene/10090:Dsg1c ^@ http://purl.uniprot.org/uniprot/Q7TSF0 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cytoplasmic|||Desmoglein repeat 1|||Desmoglein repeat 2|||Desmoglein repeat 3|||Desmoglein repeat 4|||Desmoglein repeat 5; truncated|||Desmoglein-1-gamma|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000003843|||http://purl.uniprot.org/annotation/PRO_0000003844|||http://purl.uniprot.org/annotation/VSP_012903|||http://purl.uniprot.org/annotation/VSP_012904 http://togogenome.org/gene/10090:Rfc1 ^@ http://purl.uniprot.org/uniprot/A0A0N5E9G7|||http://purl.uniprot.org/uniprot/G3X8Z6|||http://purl.uniprot.org/uniprot/P35601|||http://purl.uniprot.org/uniprot/Q5U4B1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||BRCT|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interferon-stimulated-response-element binding region|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Replication factor C subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000121773|||http://purl.uniprot.org/annotation/VSP_008444 http://togogenome.org/gene/10090:Nelfe ^@ http://purl.uniprot.org/uniprot/P19426|||http://purl.uniprot.org/uniprot/Q3UIA1 ^@ 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 ^@ 1|||10; approximate|||11|||12|||13|||14|||15|||16|||17|||18; approximate|||19; approximate|||2|||20|||21|||22|||23|||24; approximate|||25|||26|||27|||28|||29|||3|||30|||31|||32|||32 X 2 AA approximate tandem repeats of R-[DSE]|||4|||5; approximate|||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|||In isoform 2.|||In strain: 129/Sv.|||In strain: LP.RIII/Sn.|||Negative elongation factor E|||Phosphoserine|||Phosphothreonine|||Polar residues|||PolyADP-ribosyl glutamic acid|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081803|||http://purl.uniprot.org/annotation/VSP_008960 http://togogenome.org/gene/10090:Zfp622 ^@ http://purl.uniprot.org/uniprot/Q91VY9 ^@ 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_0000191816 http://togogenome.org/gene/10090:Taf13 ^@ http://purl.uniprot.org/uniprot/P61216 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Disordered|||Histone-fold|||Transcription initiation factor TFIID subunit 13 ^@ http://purl.uniprot.org/annotation/PRO_0000118911 http://togogenome.org/gene/10090:Ckmt1 ^@ http://purl.uniprot.org/uniprot/P30275|||http://purl.uniprot.org/uniprot/Q545N7 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Transit Peptide ^@ Cardiolipin-binding|||Creatine kinase U-type, mitochondrial|||Mitochondrion|||Phosphagen kinase C-terminal|||Phosphagen kinase N-terminal|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000016591 http://togogenome.org/gene/10090:Utp14b ^@ http://purl.uniprot.org/uniprot/E9Q9S3|||http://purl.uniprot.org/uniprot/Q6EJB6 ^@ 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|||U3 small nucleolar RNA-associated protein 14 homolog B ^@ http://purl.uniprot.org/annotation/PRO_0000065735 http://togogenome.org/gene/10090:4930407I10Rik ^@ http://purl.uniprot.org/uniprot/D3Z5T8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Selenof ^@ http://purl.uniprot.org/uniprot/Q9ERR7 ^@ Chain|||Experimental Information|||Modification|||Molecule Processing|||Non standard residue|||Sequence Conflict|||Signal Peptide ^@ Chain|||Non standard residue|||Sequence Conflict|||Signal Peptide ^@ Selenocysteine|||Selenoprotein F ^@ http://purl.uniprot.org/annotation/PRO_0000022308 http://togogenome.org/gene/10090:Duoxa2 ^@ http://purl.uniprot.org/uniprot/Q9D311 ^@ 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|||Dual oxidase maturation factor 2|||Extracellular|||Helical|||Interchain (with C-568 in DUXA2)|||Interchain (with C-582 in DUXA2)|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000264246 http://togogenome.org/gene/10090:Or2f1b ^@ http://purl.uniprot.org/uniprot/Q8VGP4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trim12a ^@ http://purl.uniprot.org/uniprot/A0A0R4J1B5|||http://purl.uniprot.org/uniprot/D3YVI1|||http://purl.uniprot.org/uniprot/Q99PQ1 ^@ 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|||RING-type|||Tripartite motif-containing protein 12A ^@ http://purl.uniprot.org/annotation/PRO_0000056217 http://togogenome.org/gene/10090:Ucp3 ^@ http://purl.uniprot.org/uniprot/B2RTM2|||http://purl.uniprot.org/uniprot/P56501 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Changed proton transmembrane transport. Decreased inhibition by ATP and ADP. No effect on AMP-mediated inhibition.|||Changed proton transmembrane transport. Loss of inhibition by the purine nucleotides ATP, ADP and AMP.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial intermembrane|||Mitochondrial matrix|||No effect on proton transmembrane transport. No effect on inhibition by ATP, ADP and AMP.|||Purine nucleotide binding|||Putative mitochondrial transporter UCP3|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090673 http://togogenome.org/gene/10090:Cited2 ^@ http://purl.uniprot.org/uniprot/O35740 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant ^@ Cbp/p300-interacting transactivator 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000144727|||http://purl.uniprot.org/annotation/VSP_001090|||http://purl.uniprot.org/annotation/VSP_001091|||http://purl.uniprot.org/annotation/VSP_001092 http://togogenome.org/gene/10090:Rpusd4 ^@ http://purl.uniprot.org/uniprot/Q9CWX4 ^@ Active Site|||Chain|||Molecule Processing|||Site|||Transit Peptide ^@ Active Site|||Chain|||Transit Peptide ^@ Mitochondrion|||Pseudouridylate synthase RPUSD4, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000300826 http://togogenome.org/gene/10090:Zfp235 ^@ http://purl.uniprot.org/uniprot/Q499D5 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Atpaf1 ^@ http://purl.uniprot.org/uniprot/H3BLL2 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Klhl7 ^@ http://purl.uniprot.org/uniprot/G3UW75|||http://purl.uniprot.org/uniprot/Q8BUL5 ^@ 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 7 ^@ http://purl.uniprot.org/annotation/PRO_0000228989 http://togogenome.org/gene/10090:Or5ac17 ^@ http://purl.uniprot.org/uniprot/F6ZUS0|||http://purl.uniprot.org/uniprot/Q7TS39 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rpe ^@ http://purl.uniprot.org/uniprot/B2KGF0|||http://purl.uniprot.org/uniprot/Q8VEE0 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||Proton acceptor|||Proton donor|||Removed|||Ribulose-phosphate 3-epimerase ^@ http://purl.uniprot.org/annotation/PRO_0000171588 http://togogenome.org/gene/10090:Apoc3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1N3|||http://purl.uniprot.org/uniprot/E9QP56|||http://purl.uniprot.org/uniprot/P33622 ^@ Chain|||Experimental Information|||Glycosylation Site|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Apolipoprotein C-III|||Disordered|||Lipid-binding|||May interact with the LDL receptor|||Methionine sulfoxide|||O-linked (GalNAc...) threonine|||Strain BALB/c. Without methionine sulfoxide.|||Strain C57BL/6. Without methionine sulfoxide. ^@ http://purl.uniprot.org/annotation/PRO_0000002033|||http://purl.uniprot.org/annotation/PRO_5015044300 http://togogenome.org/gene/10090:Stmn4 ^@ http://purl.uniprot.org/uniprot/D3Z4C2|||http://purl.uniprot.org/uniprot/G3X9Z6|||http://purl.uniprot.org/uniprot/P63042|||http://purl.uniprot.org/uniprot/Q05DI3 ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Strand ^@ Disordered|||Phosphoserine|||S-palmitoyl cysteine|||SLD|||Stathmin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000182407 http://togogenome.org/gene/10090:Tril ^@ http://purl.uniprot.org/uniprot/Q9DBY4 ^@ 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 ^@ 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|||Polar residues|||TLR4 interactor with leucine rich repeats ^@ http://purl.uniprot.org/annotation/PRO_0000349256 http://togogenome.org/gene/10090:Prpf39 ^@ http://purl.uniprot.org/uniprot/E9QJV4 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Spag11a ^@ http://purl.uniprot.org/uniprot/Q0VB31|||http://purl.uniprot.org/uniprot/Q8K4N2 ^@ 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 ^@ In isoform 2.|||Sperm-associated antigen 11A ^@ http://purl.uniprot.org/annotation/PRO_0000006955|||http://purl.uniprot.org/annotation/PRO_5014306858|||http://purl.uniprot.org/annotation/VSP_020138 http://togogenome.org/gene/10090:Mcub ^@ http://purl.uniprot.org/uniprot/Q810S1 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide|||Transmembrane ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Transit Peptide|||Transmembrane ^@ Calcium uniporter regulatory subunit MCUb, mitochondrial|||Helical|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000282981 http://togogenome.org/gene/10090:Or8k22 ^@ http://purl.uniprot.org/uniprot/Q8VGS7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Htr5a ^@ http://purl.uniprot.org/uniprot/P30966|||http://purl.uniprot.org/uniprot/Q3UVG4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 5-hydroxytryptamine receptor 5A|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||G-protein coupled receptors family 1 profile domain-containing protein|||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_0000068970|||http://purl.uniprot.org/annotation/PRO_5004230347 http://togogenome.org/gene/10090:Tsnaxip1 ^@ http://purl.uniprot.org/uniprot/Q99P25 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Translin-associated factor X-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000323609 http://togogenome.org/gene/10090:C7 ^@ http://purl.uniprot.org/uniprot/D3YXF5 ^@ 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 ^@ Basic and acidic residues|||Disordered|||MACPF|||Sushi ^@ http://purl.uniprot.org/annotation/PRO_5003052732 http://togogenome.org/gene/10090:Tmem237 ^@ http://purl.uniprot.org/uniprot/Q3V0J1 ^@ 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 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Transmembrane protein 237 ^@ http://purl.uniprot.org/annotation/PRO_0000076170|||http://purl.uniprot.org/annotation/VSP_042384|||http://purl.uniprot.org/annotation/VSP_042385|||http://purl.uniprot.org/annotation/VSP_042386 http://togogenome.org/gene/10090:Echdc2 ^@ http://purl.uniprot.org/uniprot/Q3TLP5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Chain|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Enoyl-CoA hydratase domain-containing protein 2, mitochondrial|||Important for catalytic activity|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000309460|||http://purl.uniprot.org/annotation/VSP_029178|||http://purl.uniprot.org/annotation/VSP_029179 http://togogenome.org/gene/10090:Pds5a ^@ http://purl.uniprot.org/uniprot/E9QPI5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Rora ^@ http://purl.uniprot.org/uniprot/P51448|||http://purl.uniprot.org/uniprot/Q3U1P4|||http://purl.uniprot.org/uniprot/Q8C3F5 ^@ 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 ^@ AF-2|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In SG; disturbance of Purkinje cell and muscle development, lipid metabolism, circadian behavior and immune system functioning.|||In isoform 4.|||N6-methyllysine|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor ROR-alpha|||Phosphothreonine; by MAPK1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053513|||http://purl.uniprot.org/annotation/VSP_003658 http://togogenome.org/gene/10090:Or1e33 ^@ http://purl.uniprot.org/uniprot/Q8VGR6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nrg1 ^@ http://purl.uniprot.org/uniprot/A0A140LHZ9|||http://purl.uniprot.org/uniprot/A0A5F8MPT8|||http://purl.uniprot.org/uniprot/Q6DR99 ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Transmembrane ^@ Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Transmembrane ^@ Disordered|||EGF-like|||Helical|||Ig-like|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Or6b9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0M0|||http://purl.uniprot.org/uniprot/P34986 ^@ 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 6B9 ^@ http://purl.uniprot.org/annotation/PRO_0000150806 http://togogenome.org/gene/10090:Nectin3 ^@ http://purl.uniprot.org/uniprot/Q9JLB9 ^@ 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 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_0000226373|||http://purl.uniprot.org/annotation/VSP_017437|||http://purl.uniprot.org/annotation/VSP_017438|||http://purl.uniprot.org/annotation/VSP_017439|||http://purl.uniprot.org/annotation/VSP_017440 http://togogenome.org/gene/10090:Cd200r1 ^@ http://purl.uniprot.org/uniprot/Q9ES57 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 7-fold reduction in binding to CD200.|||Cell surface glycoprotein CD200 receptor 1|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015129 http://togogenome.org/gene/10090:Atp8b5 ^@ http://purl.uniprot.org/uniprot/A3FIN4 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Helical|||In isoform 2.|||In isoform 3.|||Phospholipid-transporting ATPase FetA ^@ http://purl.uniprot.org/annotation/PRO_0000321955|||http://purl.uniprot.org/annotation/VSP_031844|||http://purl.uniprot.org/annotation/VSP_031845|||http://purl.uniprot.org/annotation/VSP_031846|||http://purl.uniprot.org/annotation/VSP_031847 http://togogenome.org/gene/10090:Zfp970 ^@ http://purl.uniprot.org/uniprot/Q08BU3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Atg16l1 ^@ http://purl.uniprot.org/uniprot/G9M4M6|||http://purl.uniprot.org/uniprot/Q3TDQ5|||http://purl.uniprot.org/uniprot/Q8C0J2 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Turn ^@ Autophagy-related protein 16|||Autophagy-related protein 16-1|||Caspase cleavage|||Disordered|||Impaired non-canonical autophagy, leading to susceptibility to influenza A virus (IAV) infection in mice.|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Interaction with ATG5|||No effect on the stability of the protein under normal conditions. Enhances cleavage and degradation mediated by activated CASP3 and CASP7. Results in reduced autophagy and defective clearance of intestinal pathogens. Increases secretion of pro-inflammatory cytokine IL1B and type IIFN.|||Phosphoserine|||Prevents cleavage by activated CASP3.|||RB1CC1-binding|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WIPI2-binding ^@ http://purl.uniprot.org/annotation/PRO_0000050849|||http://purl.uniprot.org/annotation/VSP_013391|||http://purl.uniprot.org/annotation/VSP_013392|||http://purl.uniprot.org/annotation/VSP_013393|||http://purl.uniprot.org/annotation/VSP_013394|||http://purl.uniprot.org/annotation/VSP_013395 http://togogenome.org/gene/10090:Itga11 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1F0|||http://purl.uniprot.org/uniprot/Q7TQC3|||http://purl.uniprot.org/uniprot/Q8CE84 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Non-terminal Residue|||Repeat|||Signal Peptide|||Transmembrane ^@ FG-GAP|||Helical|||Integrin alpha-2|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5001423000|||http://purl.uniprot.org/annotation/PRO_5001426184 http://togogenome.org/gene/10090:Coq10a ^@ http://purl.uniprot.org/uniprot/E9Q3H6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Coenzyme Q-binding protein COQ10 START ^@ http://togogenome.org/gene/10090:2310039H08Rik ^@ http://purl.uniprot.org/uniprot/Q9D727 ^@ 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|||Uncharacterized protein C6orf226 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000371343 http://togogenome.org/gene/10090:Slc14a2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J213|||http://purl.uniprot.org/uniprot/A0A494BAL3|||http://purl.uniprot.org/uniprot/G5E849|||http://purl.uniprot.org/uniprot/Q8BMD1|||http://purl.uniprot.org/uniprot/Q8R4T9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Important for channel permeability|||In isoform A2.|||In isoform A3 and isoform A5.|||In isoform A5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Urea transporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000392531|||http://purl.uniprot.org/annotation/VSP_038809|||http://purl.uniprot.org/annotation/VSP_038810|||http://purl.uniprot.org/annotation/VSP_038811|||http://purl.uniprot.org/annotation/VSP_038812 http://togogenome.org/gene/10090:Acot9 ^@ http://purl.uniprot.org/uniprot/Q9R0X4 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Acyl-coenzyme A thioesterase 9, mitochondrial|||HotDog ACOT-type 1|||HotDog ACOT-type 2|||Mitochondrion|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000000870 http://togogenome.org/gene/10090:Lhx4 ^@ http://purl.uniprot.org/uniprot/P53776 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Homeobox|||Interaction with 5-mCpG DNA|||Interaction with DNA|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000075788 http://togogenome.org/gene/10090:Ftmt ^@ http://purl.uniprot.org/uniprot/Q9D5H4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide ^@ Ferritin, mitochondrial|||Ferritin-like diiron|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000008851 http://togogenome.org/gene/10090:Mpv17l ^@ http://purl.uniprot.org/uniprot/Q99MS3 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Mpv17-like protein|||Targeting to peroxisomes ^@ http://purl.uniprot.org/annotation/PRO_0000333179|||http://purl.uniprot.org/annotation/VSP_033464|||http://purl.uniprot.org/annotation/VSP_033465|||http://purl.uniprot.org/annotation/VSP_033466 http://togogenome.org/gene/10090:Dnah17 ^@ http://purl.uniprot.org/uniprot/A2A520|||http://purl.uniprot.org/uniprot/E9Q7P0 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ 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|||Dynein heavy chain tail ^@ http://togogenome.org/gene/10090:Otx2 ^@ http://purl.uniprot.org/uniprot/Q8R0B5|||http://purl.uniprot.org/uniprot/Q8VD35 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Commd9 ^@ http://purl.uniprot.org/uniprot/Q8K2Q0 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ COMM|||COMM domain-containing protein 9|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000077404 http://togogenome.org/gene/10090:Tfap2b ^@ http://purl.uniprot.org/uniprot/E9Q5N4|||http://purl.uniprot.org/uniprot/Q61313|||http://purl.uniprot.org/uniprot/Q8CCV4|||http://purl.uniprot.org/uniprot/Q8CE69 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||H-S-H (helix-span-helix), dimerization|||Phosphoserine; by PKA|||Polar residues|||Pro residues|||Transcription factor AP-2 C-terminal|||Transcription factor AP-2-beta ^@ http://purl.uniprot.org/annotation/PRO_0000184802 http://togogenome.org/gene/10090:Lilra5 ^@ http://purl.uniprot.org/uniprot/D3Z7A9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5003053114 http://togogenome.org/gene/10090:Lss ^@ http://purl.uniprot.org/uniprot/Q8BLN5 ^@ Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ Lanosterol synthase|||N-acetylthreonine|||PFTB 1|||PFTB 2|||PFTB 3|||PFTB 4|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000072660 http://togogenome.org/gene/10090:Trim58 ^@ http://purl.uniprot.org/uniprot/Q5NCC9 ^@ 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|||E3 ubiquitin-protein ligase TRIM58|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000272302 http://togogenome.org/gene/10090:Scamp1 ^@ http://purl.uniprot.org/uniprot/Q3TD71|||http://purl.uniprot.org/uniprot/Q3TSA8|||http://purl.uniprot.org/uniprot/Q3UY11|||http://purl.uniprot.org/uniprot/Q8K021 ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||Secretory carrier-associated membrane protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000191251 http://togogenome.org/gene/10090:Nrp1 ^@ http://purl.uniprot.org/uniprot/P97333 ^@ 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 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ CUB 1|||CUB 2|||Cytoplasmic|||Disordered|||Extracellular|||F5/8 type C 1|||F5/8 type C 2|||Helical|||MAM|||N-linked (GlcNAc...) asparagine|||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_0000021860 http://togogenome.org/gene/10090:Gdap1 ^@ http://purl.uniprot.org/uniprot/O88741 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Transmembrane ^@ 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|||In isoform 2.|||N6-acetyllysine; alternate|||Required for mitochondrial localization ^@ http://purl.uniprot.org/annotation/PRO_0000186039|||http://purl.uniprot.org/annotation/VSP_008791|||http://purl.uniprot.org/annotation/VSP_008792 http://togogenome.org/gene/10090:Atf1 ^@ http://purl.uniprot.org/uniprot/P81269|||http://purl.uniprot.org/uniprot/Q9CWS2 ^@ 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 ^@ BZIP|||Basic and acidic residues|||Basic motif|||Cyclic AMP-dependent transcription factor ATF-1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KID|||Leucine-zipper|||Phosphoserine; by CaMK1, CDK3, RPS6KA4 and RPS6KA5|||Phosphoserine; by HIPK2|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076576 http://togogenome.org/gene/10090:Gan ^@ http://purl.uniprot.org/uniprot/Q8CA72 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ BACK|||BTB|||Gigaxonin|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6 ^@ http://purl.uniprot.org/annotation/PRO_0000358592 http://togogenome.org/gene/10090:Rrp1 ^@ http://purl.uniprot.org/uniprot/P56183 ^@ 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|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Ribosomal RNA processing protein 1 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000096888|||http://purl.uniprot.org/annotation/VSP_004335|||http://purl.uniprot.org/annotation/VSP_004336|||http://purl.uniprot.org/annotation/VSP_004337 http://togogenome.org/gene/10090:Ttc41 ^@ http://purl.uniprot.org/uniprot/A0A1W2P894|||http://purl.uniprot.org/uniprot/F8VPV8|||http://purl.uniprot.org/uniprot/Q692V3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||NACHT|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||Tetratricopeptide repeat protein 41 ^@ http://purl.uniprot.org/annotation/PRO_0000342550|||http://purl.uniprot.org/annotation/VSP_034497|||http://purl.uniprot.org/annotation/VSP_034498|||http://purl.uniprot.org/annotation/VSP_034499|||http://purl.uniprot.org/annotation/VSP_034500|||http://purl.uniprot.org/annotation/VSP_034501 http://togogenome.org/gene/10090:Abcb1b ^@ http://purl.uniprot.org/uniprot/B2RUR3|||http://purl.uniprot.org/uniprot/P06795 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ 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|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000093334 http://togogenome.org/gene/10090:Slc29a3 ^@ http://purl.uniprot.org/uniprot/Q99P65 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Motif|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dileucine internalization motif|||Equilibrative nucleoside transporter 3|||Extracellular|||Helical|||Important for acidic pH-dependent nucleoside transporter activity. Acts as pH sensor|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000209344 http://togogenome.org/gene/10090:Slco4a1 ^@ http://purl.uniprot.org/uniprot/Q8K078 ^@ 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|||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.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier organic anion transporter family member 4A1 ^@ http://purl.uniprot.org/annotation/PRO_0000191068|||http://purl.uniprot.org/annotation/VSP_006157|||http://purl.uniprot.org/annotation/VSP_006158 http://togogenome.org/gene/10090:Zfp518a ^@ http://purl.uniprot.org/uniprot/B2RRF6 ^@ 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 ^@ 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)|||Phosphoserine|||Polar residues|||Zinc finger protein 518A ^@ http://purl.uniprot.org/annotation/PRO_0000349265 http://togogenome.org/gene/10090:Ccdc190 ^@ http://purl.uniprot.org/uniprot/H3BLK0|||http://purl.uniprot.org/uniprot/Q3URK1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-coil domain-containing protein 190|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000274499 http://togogenome.org/gene/10090:Med27 ^@ http://purl.uniprot.org/uniprot/Q9DB40 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ In isoform 2.|||Mediator of RNA polymerase II transcription subunit 27|||N6-methyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000079362|||http://purl.uniprot.org/annotation/VSP_051870|||http://purl.uniprot.org/annotation/VSP_051871 http://togogenome.org/gene/10090:Stoml3 ^@ http://purl.uniprot.org/uniprot/B2RS16|||http://purl.uniprot.org/uniprot/Q6PE84 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Abolishes STOML3 modulation of mechanosensitive currents.|||Abolishes the activity of STOML3.|||Band 7|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type III membrane protein|||Mis-localization predominantly to the cytoplasmic compartment.|||Phosphoserine|||Reduced oligomerization. Does not sensitize mechanically gated currents.|||Stomatin-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000094034 http://togogenome.org/gene/10090:Gm4847 ^@ http://purl.uniprot.org/uniprot/G3X946 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Nup62 ^@ http://purl.uniprot.org/uniprot/Q5FWJ9|||http://purl.uniprot.org/uniprot/Q63850 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||4|||5|||5 X 2 AA repeats of F-G|||Disordered|||Interchain (with NUP155)|||Loss of reduction of influx rate of NLS cargo upon oxidative stress; when associated with S-478.|||Loss of reduction of influx rate of NLS cargo upon oxidative stress; when associated with S-509.|||N-acetylserine|||Nuclear pore glycoprotein p62|||Nucleoporin NSP1-like C-terminal|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||Phosphoserine|||Removed|||Required for centrosome localization ^@ http://purl.uniprot.org/annotation/PRO_0000204881 http://togogenome.org/gene/10090:Smarcc1 ^@ http://purl.uniprot.org/uniprot/P97496|||http://purl.uniprot.org/uniprot/Q3UPK0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ 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 isoform 2.|||MarR-like|||MarR-like, BRCT and chromo domains module|||Myb-like|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SANT|||SWI/SNF complex subunit SMARCC1|||SWIRM ^@ http://purl.uniprot.org/annotation/PRO_0000197116|||http://purl.uniprot.org/annotation/VSP_012489 http://togogenome.org/gene/10090:Pkp3 ^@ http://purl.uniprot.org/uniprot/Q9QY23 ^@ 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 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Plakophilin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000064288|||http://purl.uniprot.org/annotation/VSP_026139 http://togogenome.org/gene/10090:Ifitm2 ^@ http://purl.uniprot.org/uniprot/Q99J93 ^@ Chain|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||INTRAMEM|||Lipid Binding|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Interferon-induced transmembrane protein 2|||N-acetylmethionine|||Phosphotyrosine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000398566 http://togogenome.org/gene/10090:Or4k6 ^@ http://purl.uniprot.org/uniprot/F8VQB9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dclre1c ^@ http://purl.uniprot.org/uniprot/Q32MX8|||http://purl.uniprot.org/uniprot/Q8K4J0 ^@ 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 ^@ DNA repair metallo-beta-lactamase|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues|||Protein artemis ^@ http://purl.uniprot.org/annotation/PRO_0000209124|||http://purl.uniprot.org/annotation/VSP_014893|||http://purl.uniprot.org/annotation/VSP_014894|||http://purl.uniprot.org/annotation/VSP_014895|||http://purl.uniprot.org/annotation/VSP_014896 http://togogenome.org/gene/10090:D630039A03Rik ^@ http://purl.uniprot.org/uniprot/Q8K0M7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||TBC1 ^@ http://togogenome.org/gene/10090:Bdh1 ^@ http://purl.uniprot.org/uniprot/Q80XN0 ^@ 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_0000031961 http://togogenome.org/gene/10090:Tasp1 ^@ http://purl.uniprot.org/uniprot/Q3UJT0|||http://purl.uniprot.org/uniprot/Q8R1G1 ^@ Active Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Region|||Site|||Splice Variant ^@ Cleavage; by autolysis|||Disordered|||In isoform 2.|||Nucleophile|||Polar residues|||Threonine aspartase subunit alpha|||Threonine aspartase subunit beta ^@ http://purl.uniprot.org/annotation/PRO_0000002352|||http://purl.uniprot.org/annotation/PRO_0000002353|||http://purl.uniprot.org/annotation/VSP_000334|||http://purl.uniprot.org/annotation/VSP_000335 http://togogenome.org/gene/10090:Rab28 ^@ http://purl.uniprot.org/uniprot/Q99KL7 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Propeptide ^@ Cysteine methyl ester|||Effector region|||N-acetylserine|||Phosphoserine|||Ras-related protein Rab-28|||Removed|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121228|||http://purl.uniprot.org/annotation/PRO_0000396722 http://togogenome.org/gene/10090:Nme4 ^@ http://purl.uniprot.org/uniprot/Q9WV84 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Transit Peptide ^@ Mitochondrion|||Nucleoside diphosphate kinase, mitochondrial|||Pros-phosphohistidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000019433 http://togogenome.org/gene/10090:Atp5l ^@ http://purl.uniprot.org/uniprot/Q9CPQ8 ^@ 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_0000071692 http://togogenome.org/gene/10090:Hook2 ^@ http://purl.uniprot.org/uniprot/Q3TKK8|||http://purl.uniprot.org/uniprot/Q7TMK6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Calponin-homology (CH)|||Phosphoserine|||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_0000219195 http://togogenome.org/gene/10090:Spata20 ^@ http://purl.uniprot.org/uniprot/Q80YT5 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Spermatogenesis-associated protein 20 ^@ http://purl.uniprot.org/annotation/PRO_0000278451 http://togogenome.org/gene/10090:Eno3 ^@ http://purl.uniprot.org/uniprot/P21550 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Beta-enolase|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor|||Proton donor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000134108 http://togogenome.org/gene/10090:Flvcr1 ^@ http://purl.uniprot.org/uniprot/A0A0A6YWJ7|||http://purl.uniprot.org/uniprot/B2RXV4 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Heme transporter FLVCR1|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000423424|||http://purl.uniprot.org/annotation/VSP_047867 http://togogenome.org/gene/10090:Cdkl4 ^@ http://purl.uniprot.org/uniprot/Q3TZA2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Motif|||Region ^@ Cyclin-dependent kinase-like 4|||Disordered|||Protein kinase|||Proton acceptor|||[NKR]KIAxRE ^@ http://purl.uniprot.org/annotation/PRO_0000085825 http://togogenome.org/gene/10090:Myh7b ^@ http://purl.uniprot.org/uniprot/A2AQP0 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Actin-binding|||Basic and acidic residues|||Disordered|||IQ|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-7B ^@ http://purl.uniprot.org/annotation/PRO_0000349313 http://togogenome.org/gene/10090:Pdlim2 ^@ http://purl.uniprot.org/uniprot/Q8R1G6 ^@ 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 ^@ Disordered|||LIM zinc-binding|||PDZ|||PDZ and LIM domain protein 2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000075864 http://togogenome.org/gene/10090:Mmrn2 ^@ http://purl.uniprot.org/uniprot/A6H6E2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ C1q|||Disordered|||EMI|||In isoform 2.|||Multimerin-2|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000367040|||http://purl.uniprot.org/annotation/VSP_053050 http://togogenome.org/gene/10090:Klk1b3 ^@ http://purl.uniprot.org/uniprot/A0A1R3UHM9|||http://purl.uniprot.org/uniprot/P00756 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand ^@ Activation peptide|||Charge relay system|||Kallikrein 1-related peptidase b3|||N-linked (GlcNAc...) asparagine|||Nerve growth factor gamma chain 1|||Nerve growth factor gamma chain 2|||Peptidase S1|||Segment A|||Segment B1|||Segment B2|||Segment C ^@ http://purl.uniprot.org/annotation/PRO_0000027968|||http://purl.uniprot.org/annotation/PRO_0000027969|||http://purl.uniprot.org/annotation/PRO_0000027970|||http://purl.uniprot.org/annotation/PRO_0000027971|||http://purl.uniprot.org/annotation/PRO_5010250888 http://togogenome.org/gene/10090:Pms2 ^@ http://purl.uniprot.org/uniprot/P54279 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Mismatch repair endonuclease PMS2|||Nuclear localization signal|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000178006 http://togogenome.org/gene/10090:Uaca ^@ http://purl.uniprot.org/uniprot/A0A0R4J0S7|||http://purl.uniprot.org/uniprot/Q8CGB3 ^@ 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|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||T-SNARE coiled-coil homology|||Uveal autoantigen with coiled-coil domains and ankyrin repeats ^@ http://purl.uniprot.org/annotation/PRO_0000231651|||http://purl.uniprot.org/annotation/VSP_017874|||http://purl.uniprot.org/annotation/VSP_017875 http://togogenome.org/gene/10090:Or1e19 ^@ http://purl.uniprot.org/uniprot/Q8VGT2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Celf2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J2B0|||http://purl.uniprot.org/uniprot/E9QA47|||http://purl.uniprot.org/uniprot/Q9Z0H4|||http://purl.uniprot.org/uniprot/S4R1S7 ^@ 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 ^@ CUGBP Elav-like family member 2|||Disordered|||In isoform 11.|||In isoform 2 and isoform 6.|||In isoform 3, isoform 5, isoform 6, isoform 8 and isoform 11.|||In isoform 3.|||In isoform 4, isoform 5 and isoform 7.|||In isoform 4.|||In isoform 9.|||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_0000295190|||http://purl.uniprot.org/annotation/VSP_026801|||http://purl.uniprot.org/annotation/VSP_026802|||http://purl.uniprot.org/annotation/VSP_026803|||http://purl.uniprot.org/annotation/VSP_026804|||http://purl.uniprot.org/annotation/VSP_026805|||http://purl.uniprot.org/annotation/VSP_026806|||http://purl.uniprot.org/annotation/VSP_026808 http://togogenome.org/gene/10090:Or11n2 ^@ http://purl.uniprot.org/uniprot/Q7TQW3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp174 ^@ http://purl.uniprot.org/uniprot/B9EJW5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||SCAN box ^@ http://togogenome.org/gene/10090:Crct1 ^@ http://purl.uniprot.org/uniprot/Q6PAI5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Crygb ^@ http://purl.uniprot.org/uniprot/P04344 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ 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_0000057596 http://togogenome.org/gene/10090:Ptx3 ^@ http://purl.uniprot.org/uniprot/P48759 ^@ 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 ^@ Interchain|||N-linked (GlcNAc...) asparagine|||Pentraxin (PTX)|||Pentraxin-related protein PTX3 ^@ http://purl.uniprot.org/annotation/PRO_0000023546 http://togogenome.org/gene/10090:Cxcr4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0N8|||http://purl.uniprot.org/uniprot/P70658 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-X-C chemokine receptor type 4|||Chemokine binding|||Chemokine binding, important for signaling|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||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|||Important for chemokine binding and signaling|||Important for signaling|||In isoform CXCR4-A.|||Involved in dimerization|||Involved in dimerization; when bound to chemokine|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Phosphoserine; by GRK6|||Phosphoserine; by PKC and GRK6|||Polar residues|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000069355|||http://purl.uniprot.org/annotation/VSP_001891 http://togogenome.org/gene/10090:Akna ^@ http://purl.uniprot.org/uniprot/Q80VW7 ^@ 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 ^@ A.T hook|||Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Microtubule organization protein AKNA|||PEST|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000289160|||http://purl.uniprot.org/annotation/VSP_025941|||http://purl.uniprot.org/annotation/VSP_025942|||http://purl.uniprot.org/annotation/VSP_025943|||http://purl.uniprot.org/annotation/VSP_025944|||http://purl.uniprot.org/annotation/VSP_025945 http://togogenome.org/gene/10090:Ildr2 ^@ http://purl.uniprot.org/uniprot/B5TVM2 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||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|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Ig-like V-type|||Immunoglobulin-like domain-containing receptor 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Lumenal|||Omega-N-methylarginine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000425154|||http://purl.uniprot.org/annotation/VSP_061354|||http://purl.uniprot.org/annotation/VSP_061355|||http://purl.uniprot.org/annotation/VSP_061356|||http://purl.uniprot.org/annotation/VSP_061357|||http://purl.uniprot.org/annotation/VSP_061358|||http://purl.uniprot.org/annotation/VSP_061359|||http://purl.uniprot.org/annotation/VSP_061360 http://togogenome.org/gene/10090:Gbp6 ^@ http://purl.uniprot.org/uniprot/A0A8Q0QEH4|||http://purl.uniprot.org/uniprot/Q3U8G5 ^@ Coiled-Coil|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Domain Extent|||Non-terminal Residue ^@ GB1/RHD3-type G ^@ http://togogenome.org/gene/10090:Mpp4 ^@ http://purl.uniprot.org/uniprot/D3Z0G8|||http://purl.uniprot.org/uniprot/Q6P7F1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||Guanylate kinase-like|||In isoform 3 and isoform 4.|||In isoform 4.|||L27|||L27 1|||L27 2|||MAGUK p55 subfamily member 4|||PDZ|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000094578|||http://purl.uniprot.org/annotation/VSP_013994|||http://purl.uniprot.org/annotation/VSP_013995|||http://purl.uniprot.org/annotation/VSP_013996|||http://purl.uniprot.org/annotation/VSP_013997 http://togogenome.org/gene/10090:Gnl3l ^@ http://purl.uniprot.org/uniprot/Q6PGG6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region ^@ Basic and acidic residues|||Basic residues|||CP-type G|||Disordered|||Guanine nucleotide-binding protein-like 3-like protein|||Mislocalized to the nucleoplasm. No effect on the reduction of MDM2 ubiquitination.|||No effect on TERF1-binding. Loss of ability to stabilize TERF1 protein.|||Polar residues|||Required for nucleolar localization ^@ http://purl.uniprot.org/annotation/PRO_0000284382 http://togogenome.org/gene/10090:Clec11a ^@ http://purl.uniprot.org/uniprot/O88200 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||C-type lectin|||C-type lectin domain family 11 member A|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000017469 http://togogenome.org/gene/10090:Tmem89 ^@ http://purl.uniprot.org/uniprot/Q9DA04 ^@ 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.|||Transmembrane protein 89 ^@ http://purl.uniprot.org/annotation/PRO_0000290068|||http://purl.uniprot.org/annotation/VSP_026116|||http://purl.uniprot.org/annotation/VSP_026117 http://togogenome.org/gene/10090:Or9i2 ^@ http://purl.uniprot.org/uniprot/Q8VFQ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Erich4 ^@ http://purl.uniprot.org/uniprot/A0A5F8MPB4|||http://purl.uniprot.org/uniprot/Q3UNU4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Glutamate-rich protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000340278 http://togogenome.org/gene/10090:Alpk3 ^@ http://purl.uniprot.org/uniprot/Q924C5 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Alpha-protein kinase 3|||Alpha-type protein kinase|||Basic and acidic residues|||Disordered|||Ig-like 1|||Ig-like 2|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000291531 http://togogenome.org/gene/10090:Or51e1 ^@ http://purl.uniprot.org/uniprot/Q8VGZ7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Mettl21e ^@ http://purl.uniprot.org/uniprot/Q8CDZ2 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Region ^@ Disordered|||Protein-lysine methyltransferase METTL21E ^@ http://purl.uniprot.org/annotation/PRO_0000329292 http://togogenome.org/gene/10090:Ptprj ^@ http://purl.uniprot.org/uniprot/A2AWF8|||http://purl.uniprot.org/uniprot/A2AWF9|||http://purl.uniprot.org/uniprot/E9Q4S7|||http://purl.uniprot.org/uniprot/Q64455 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 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|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Receptor-type tyrosine-protein phosphatase eta|||Substrate trapping with much higher affinity for substrate.|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000025445 http://togogenome.org/gene/10090:Rad1 ^@ http://purl.uniprot.org/uniprot/Q9QWZ1 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ Cell cycle checkpoint protein RAD1|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000225006|||http://purl.uniprot.org/annotation/VSP_017337 http://togogenome.org/gene/10090:Usp24 ^@ http://purl.uniprot.org/uniprot/B1AY13 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Proton acceptor|||UBA|||USP|||Ubiquitin carboxyl-terminal hydrolase 24 ^@ http://purl.uniprot.org/annotation/PRO_0000353213|||http://purl.uniprot.org/annotation/VSP_035661|||http://purl.uniprot.org/annotation/VSP_035662 http://togogenome.org/gene/10090:Narf ^@ http://purl.uniprot.org/uniprot/Q9CYQ7 ^@ 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|||Nuclear prelamin A recognition factor|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000288480 http://togogenome.org/gene/10090:1700001O22Rik ^@ http://purl.uniprot.org/uniprot/A2APZ1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DUF4685|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Mepe ^@ http://purl.uniprot.org/uniprot/Q8K4L6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ ASARM motif; interaction with PHEX|||Cell attachment site|||Dentonin|||Disordered|||Matrix extracellular phosphoglycoprotein|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5014107441 http://togogenome.org/gene/10090:Tm9sf4 ^@ http://purl.uniprot.org/uniprot/Q8BH24 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Phosphotyrosine|||Transmembrane 9 superfamily member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000311810 http://togogenome.org/gene/10090:Mstn ^@ http://purl.uniprot.org/uniprot/O08689|||http://purl.uniprot.org/uniprot/Q540E2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Signal Peptide|||Site|||Strand|||Turn ^@ Blocks proteolytic cleavage; increases muscle mass when injected into adult mice.|||Cleavage|||Growth/differentiation factor 8|||Interchain|||N-linked (GlcNAc...) asparagine|||No effect on proteolytic cleavage.|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033956|||http://purl.uniprot.org/annotation/PRO_0000033957|||http://purl.uniprot.org/annotation/PRO_5014309529 http://togogenome.org/gene/10090:Rpia ^@ http://purl.uniprot.org/uniprot/P47968 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Omega-N-methylarginine|||Phosphoserine|||Ribose-5-phosphate isomerase ^@ http://purl.uniprot.org/annotation/PRO_0000158522 http://togogenome.org/gene/10090:Cd72 ^@ http://purl.uniprot.org/uniprot/P21855|||http://purl.uniprot.org/uniprot/Q3UB58|||http://purl.uniprot.org/uniprot/Q3UNJ0|||http://purl.uniprot.org/uniprot/Q3UZ35 ^@ 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|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane ^@ B-cell differentiation antigen CD72|||C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In allele LYB-2A.2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by LYN ^@ http://purl.uniprot.org/annotation/PRO_0000046586 http://togogenome.org/gene/10090:Rilpl2 ^@ http://purl.uniprot.org/uniprot/Q99LE1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes homodimerization.|||Acidic residues|||Disordered|||In isoform 2.|||Loss of interaction with MYO5A.|||RH1|||RH2|||RILP-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000317006|||http://purl.uniprot.org/annotation/VSP_030853 http://togogenome.org/gene/10090:Zfp831 ^@ http://purl.uniprot.org/uniprot/A2ADM8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Chst12 ^@ http://purl.uniprot.org/uniprot/Q99LL3 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Carbohydrate sulfotransferase 12|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000189669 http://togogenome.org/gene/10090:Six6 ^@ http://purl.uniprot.org/uniprot/B2RSE8|||http://purl.uniprot.org/uniprot/Q9QZ28 ^@ 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 protein SIX6|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049308 http://togogenome.org/gene/10090:Or2b2 ^@ http://purl.uniprot.org/uniprot/Q7TQU5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clec4f ^@ http://purl.uniprot.org/uniprot/A0A0R4IZZ5|||http://purl.uniprot.org/uniprot/P70194 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Strand|||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|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000046623 http://togogenome.org/gene/10090:Kcmf1 ^@ http://purl.uniprot.org/uniprot/A0A0N4SV15|||http://purl.uniprot.org/uniprot/Q80UY2 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ C2H2-type|||Disordered|||E3 ubiquitin-protein ligase KCMF1|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000349220|||http://purl.uniprot.org/annotation/VSP_035227 http://togogenome.org/gene/10090:Dnah5 ^@ http://purl.uniprot.org/uniprot/Q8VHE6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Disordered|||Dynein axonemal heavy chain 5|||Polar residues|||Stalk|||Stem ^@ http://purl.uniprot.org/annotation/PRO_0000114631 http://togogenome.org/gene/10090:Wdfy4 ^@ http://purl.uniprot.org/uniprot/E9PV60|||http://purl.uniprot.org/uniprot/E9Q2M9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ BEACH|||BEACH-type PH|||Basic and acidic residues|||Disordered|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat- and FYVE domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000448268 http://togogenome.org/gene/10090:Alg2 ^@ http://purl.uniprot.org/uniprot/Q9DBE8 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Alpha-1,3/1,6-mannosyltransferase ALG2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000080261 http://togogenome.org/gene/10090:Aff3 ^@ http://purl.uniprot.org/uniprot/D3YYI6 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ AF4/FMR2 C-terminal homology|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Eif2ak1 ^@ http://purl.uniprot.org/uniprot/Q9Z2R9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site ^@ Abolishes kinase activity.|||Abolishes kinase activity. Impaired hemoglobin synthesis and proliferation of differentiating erythroid cells in knockin mice.|||Almost complete loss of kinase activity; even upon arsenite treatment.|||Constitutively active kinase; loss of regulation by heme and arsenite.|||Disordered|||Eukaryotic translation initiation factor 2-alpha kinase 1|||HRM 1|||HRM 2|||Heme-binding|||No effect on kinase activity.|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085942 http://togogenome.org/gene/10090:Wdr55 ^@ http://purl.uniprot.org/uniprot/Q9CX97 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Phosphoserine|||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_0000237599 http://togogenome.org/gene/10090:Gsto1 ^@ http://purl.uniprot.org/uniprot/O09131 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase omega-1|||N-acetylserine|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000185885 http://togogenome.org/gene/10090:Hmgcr ^@ http://purl.uniprot.org/uniprot/Q01237|||http://purl.uniprot.org/uniprot/Q8BV96 ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 3-hydroxy-3-methylglutaryl-coenzyme A reductase|||Charge relay system|||Cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||INSIG-binding motif|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Proton donor|||SSD ^@ http://purl.uniprot.org/annotation/PRO_0000114421 http://togogenome.org/gene/10090:Slc6a13 ^@ http://purl.uniprot.org/uniprot/P31649 ^@ 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=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|||Sodium- and chloride-dependent GABA transporter 2 ^@ http://purl.uniprot.org/annotation/PRO_0000214793 http://togogenome.org/gene/10090:Sts ^@ http://purl.uniprot.org/uniprot/P50427 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 3-oxoalanine (Cys)|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Steryl-sulfatase|||via 3-oxoalanine ^@ http://purl.uniprot.org/annotation/PRO_0000033415 http://togogenome.org/gene/10090:Or12d12 ^@ http://purl.uniprot.org/uniprot/Q920Z0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sema6a ^@ http://purl.uniprot.org/uniprot/D3YWM8|||http://purl.uniprot.org/uniprot/O35464|||http://purl.uniprot.org/uniprot/Q8BUT0|||http://purl.uniprot.org/uniprot/Q8BXZ7 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes homodimerization.|||Cytoplasmic|||Disordered|||Extracellular|||Formation of disulfide-linked homodimer.|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Sema|||Sema domain-containing protein|||Semaphorin-6A|||Strongly reduced affinity for PLXNA2. ^@ http://purl.uniprot.org/annotation/PRO_0000032340|||http://purl.uniprot.org/annotation/PRO_5003052950|||http://purl.uniprot.org/annotation/PRO_5004303874|||http://purl.uniprot.org/annotation/PRO_5004307238|||http://purl.uniprot.org/annotation/VSP_012097|||http://purl.uniprot.org/annotation/VSP_012098 http://togogenome.org/gene/10090:Dkk1 ^@ http://purl.uniprot.org/uniprot/O54908 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ 43% reduced binding to LRP6.|||50% reduced binding to LRP6.|||DKK-type Cys-1|||DKK-type Cys-2|||Dickkopf-related protein 1|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine ^@ http://purl.uniprot.org/annotation/PRO_0000007219 http://togogenome.org/gene/10090:Syt7 ^@ http://purl.uniprot.org/uniprot/A0A498WGM0|||http://purl.uniprot.org/uniprot/Q9R0N7 ^@ 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|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes palmitoylation. Impaired phagocytosis and localization to lysosomes.|||Asymmetric dimethylarginine|||C2|||C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||In C2A*; loss of function due to abolished Ca(2+)-binding to the first C2 domain. Impaired ability to mediate synaptic facilitation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of Ca(2+)-binding in the first C2 domain. Impaired delivery of lysosomal membrane to nascent phagosomes; when associated with 357-N--N-359. Impaired synaptic vesicle replenishment; when associated with 357-N--N-359.|||Loss of Ca(2+)-binding in the second C2 domain. Impaired delivery of lysosomal membrane to nascent phagosomes; when associated with 225-N--N-227. Impaired synaptic vesicle replenishment; when associated with 225-N--N-227.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Synaptotagmin-7|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000183958|||http://purl.uniprot.org/annotation/VSP_058235|||http://purl.uniprot.org/annotation/VSP_058236|||http://purl.uniprot.org/annotation/VSP_058237 http://togogenome.org/gene/10090:Top2b ^@ http://purl.uniprot.org/uniprot/Q64511 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Basic and acidic residues|||DNA topoisomerase 2-beta|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs B-cell development.|||Important for DNA bending; intercalates between base pairs of target DNA|||Interaction with DNA|||Interaction with PLSCR1|||N-acetylalanine|||N6-acetyllysine|||O-(5'-phospho-DNA)-tyrosine intermediate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Toprim|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000145370 http://togogenome.org/gene/10090:Tmem65 ^@ http://purl.uniprot.org/uniprot/Q4VAE3 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Mitochondrion|||Transmembrane protein 65 ^@ http://purl.uniprot.org/annotation/PRO_0000251405 http://togogenome.org/gene/10090:Pals1 ^@ http://purl.uniprot.org/uniprot/B2RRY4|||http://purl.uniprot.org/uniprot/Q9JLB2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand ^@ Basic and acidic residues|||Disordered|||Failure to restore localization of PALS1 and PATJ to cell-cell contacts and to restore tight junction and adherens junction formation in cells where PALS1 has been knocked down.|||Guanylate kinase-like|||Interaction with LIN7C|||Interaction with PARD6B|||L27|||L27 1|||L27 2|||No effect on PARD6B interaction. Prevents interaction with PATJ; when associated with G-150.|||No effect on PARD6B interaction. Prevents interaction with PATJ; when associated with G-154.|||No effect on interaction with LIN7C.|||No effect on interaction with PARD6B.|||PDZ|||Partially prevents interaction with LIN7C.|||Phosphoserine|||Prevents interaction with LIN7C.|||Prevents interaction with PARD6B.|||Prevents interaction with PARD6B. Does not affect localization to the tight junctions.|||Protein PALS1|||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_0000094581 http://togogenome.org/gene/10090:Akap13 ^@ http://purl.uniprot.org/uniprot/A0A140LJJ5|||http://purl.uniprot.org/uniprot/E9Q394 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ A-kinase anchor protein 13|||Basic and acidic residues|||DH|||Disordered|||Important for interaction with MAP2K3|||Important for interaction with PRKAR2A|||In isoform 2.|||Interaction with ESR1|||N6-methyllysine|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000436319|||http://purl.uniprot.org/annotation/VSP_058344|||http://purl.uniprot.org/annotation/VSP_058345 http://togogenome.org/gene/10090:Zdhhc6 ^@ http://purl.uniprot.org/uniprot/Q9CPV7 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Lipid Binding|||Motif|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Di-lysine motif|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||Palmitoyltransferase ZDHHC6|||S-palmitoyl cysteine|||S-palmitoyl cysteine intermediate|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000212872|||http://purl.uniprot.org/annotation/VSP_006939|||http://purl.uniprot.org/annotation/VSP_006940|||http://purl.uniprot.org/annotation/VSP_006941|||http://purl.uniprot.org/annotation/VSP_016270 http://togogenome.org/gene/10090:Wdr89 ^@ http://purl.uniprot.org/uniprot/Q9D0R9 ^@ 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_0000330845 http://togogenome.org/gene/10090:Pwwp4a ^@ http://purl.uniprot.org/uniprot/Q52KH6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Gabra4 ^@ http://purl.uniprot.org/uniprot/Q543Z0|||http://purl.uniprot.org/uniprot/Q9D6F4 ^@ 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 ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Gamma-aminobutyric acid receptor subunit alpha-4|||Helical|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000000442|||http://purl.uniprot.org/annotation/PRO_5014309554 http://togogenome.org/gene/10090:Kcnk7 ^@ http://purl.uniprot.org/uniprot/A0A494B9E8|||http://purl.uniprot.org/uniprot/Q9JJ14|||http://purl.uniprot.org/uniprot/Q9Z2T1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||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_0000101752 http://togogenome.org/gene/10090:Mtmr1 ^@ http://purl.uniprot.org/uniprot/Q9Z2C4 ^@ 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|||GRAM|||Myotubularin phosphatase|||Myotubularin-related protein 1|||N-acetylmethionine|||Phosphocysteine intermediate|||Phosphoserine|||Required for dimerization ^@ http://purl.uniprot.org/annotation/PRO_0000094933 http://togogenome.org/gene/10090:Sf3b3 ^@ http://purl.uniprot.org/uniprot/B2RSV4|||http://purl.uniprot.org/uniprot/Q921M3 ^@ 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 ^@ Cleavage/polyadenylation specificity factor A subunit C-terminal|||Cleavage/polyadenylation specificity factor A subunit N-terminal|||In isoform 2.|||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_0000276755|||http://purl.uniprot.org/annotation/VSP_022980 http://togogenome.org/gene/10090:Skap2 ^@ http://purl.uniprot.org/uniprot/Q3UND0 ^@ 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 FYN, phosphorylation by FYN, and effects on cell growth.|||Basic and acidic residues|||Disordered|||Homodimerization|||In isoform 2.|||PH|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by FYN|||SH3|||Src kinase-associated phosphoprotein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000270180|||http://purl.uniprot.org/annotation/VSP_022184 http://togogenome.org/gene/10090:Dcaf12l2 ^@ http://purl.uniprot.org/uniprot/Q8BGW4 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ DDB1- and CUL4-associated factor 12-like protein 2|||Disordered|||WD 1|||WD 2|||WD 3|||WD 4 ^@ http://purl.uniprot.org/annotation/PRO_0000306851 http://togogenome.org/gene/10090:Cdca4 ^@ http://purl.uniprot.org/uniprot/Q9CWM2 ^@ 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_0000191618 http://togogenome.org/gene/10090:S100a3 ^@ http://purl.uniprot.org/uniprot/P62818|||http://purl.uniprot.org/uniprot/Q496W1 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue ^@ Citrulline; by PAD3|||EF-hand 1|||EF-hand 2|||Protein S100-A3|||S100/CaBP-9k-type calcium binding subdomain ^@ http://purl.uniprot.org/annotation/PRO_0000143973 http://togogenome.org/gene/10090:Ociad2 ^@ http://purl.uniprot.org/uniprot/A0A0J9YU56|||http://purl.uniprot.org/uniprot/Q9D8W7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||N6-acetyllysine|||OCIA|||OCIA domain-containing protein 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000299393 http://togogenome.org/gene/10090:Fam124b ^@ http://purl.uniprot.org/uniprot/Q8BLQ0 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Protein FAM124B ^@ http://purl.uniprot.org/annotation/PRO_0000286385 http://togogenome.org/gene/10090:Dhx16 ^@ http://purl.uniprot.org/uniprot/G3X8X0|||http://purl.uniprot.org/uniprot/Q921Y1|||http://purl.uniprot.org/uniprot/Q9CRI3 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Helicase-associated ^@ http://togogenome.org/gene/10090:Btbd35f4 ^@ http://purl.uniprot.org/uniprot/A2CGC2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Tmem169 ^@ http://purl.uniprot.org/uniprot/Q8BG50 ^@ 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 169 ^@ http://purl.uniprot.org/annotation/PRO_0000271040 http://togogenome.org/gene/10090:Btbd10 ^@ http://purl.uniprot.org/uniprot/E9Q6L8|||http://purl.uniprot.org/uniprot/E9Q6Y9|||http://purl.uniprot.org/uniprot/Q80X66 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ BTB|||BTB/POZ domain-containing protein 10|||Basic and acidic residues|||Disordered|||Interaction with AKT family members|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000228986 http://togogenome.org/gene/10090:Parva ^@ http://purl.uniprot.org/uniprot/Q3UF75|||http://purl.uniprot.org/uniprot/Q9EPC1 ^@ 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 ^@ Alpha-parvin|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Interaction with ARHGAP31|||N-acetylalanine|||Phosphoserine|||Removed|||Required for interaction with TESK1 and ILK ^@ http://purl.uniprot.org/annotation/PRO_0000121581 http://togogenome.org/gene/10090:Olr1 ^@ http://purl.uniprot.org/uniprot/G4WK09|||http://purl.uniprot.org/uniprot/G4WK10|||http://purl.uniprot.org/uniprot/Q9EQ09 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 1|||2|||3|||Basic and acidic residues|||C-type lectin|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Neck|||Oxidized low-density lipoprotein receptor 1|||Oxidized low-density lipoprotein receptor 1, soluble form|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000017445|||http://purl.uniprot.org/annotation/PRO_0000017446 http://togogenome.org/gene/10090:Cst13 ^@ http://purl.uniprot.org/uniprot/Q80ZN5 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Cystatin-13|||Reactive site|||Secondary area of contact ^@ http://purl.uniprot.org/annotation/PRO_0000006661 http://togogenome.org/gene/10090:Zfp97 ^@ http://purl.uniprot.org/uniprot/E9PZP6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Aldh1b1 ^@ http://purl.uniprot.org/uniprot/Q9CZS1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ 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_0000271411 http://togogenome.org/gene/10090:Itgb3bp ^@ http://purl.uniprot.org/uniprot/Q9CQ82 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Centromere protein R|||DD1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||LXXIL motif|||Nuclear localization signal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000057950|||http://purl.uniprot.org/annotation/VSP_020453|||http://purl.uniprot.org/annotation/VSP_020454 http://togogenome.org/gene/10090:Cd81 ^@ http://purl.uniprot.org/uniprot/P35762 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ CD81 antigen|||Cytoplasmic|||Extracellular|||Helical|||Important for interaction with integrin ^@ http://purl.uniprot.org/annotation/PRO_0000219222 http://togogenome.org/gene/10090:Lims1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J005|||http://purl.uniprot.org/uniprot/A0A5F8MPJ3|||http://purl.uniprot.org/uniprot/E9QP62|||http://purl.uniprot.org/uniprot/Q99JW4|||http://purl.uniprot.org/uniprot/Q9D7B2 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ LIM and senescent cell antigen-like-containing domain protein 1|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||LIM zinc-binding 5|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000266009 http://togogenome.org/gene/10090:Kbtbd11 ^@ http://purl.uniprot.org/uniprot/Q8BNW9|||http://purl.uniprot.org/uniprot/Q9CUY6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ BTB|||Basic and acidic residues|||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_0000119091 http://togogenome.org/gene/10090:Gm10488 ^@ http://purl.uniprot.org/uniprot/Q4KL05 ^@ Domain Extent|||Region ^@ Domain Extent ^@ XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Ahcyl2 ^@ http://purl.uniprot.org/uniprot/F8WGT1|||http://purl.uniprot.org/uniprot/F8WI65|||http://purl.uniprot.org/uniprot/Q68FL4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||LISN domain, inhibits interaction with ITPR1|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Putative adenosylhomocysteinase 3|||Removed|||S-adenosyl-L-homocysteine hydrolase NAD binding ^@ http://purl.uniprot.org/annotation/PRO_0000230301|||http://purl.uniprot.org/annotation/VSP_017821 http://togogenome.org/gene/10090:Sox6 ^@ http://purl.uniprot.org/uniprot/A0A0U1RNW8|||http://purl.uniprot.org/uniprot/E9PUW0|||http://purl.uniprot.org/uniprot/P40645|||http://purl.uniprot.org/uniprot/Q3V1J7|||http://purl.uniprot.org/uniprot/Q8BSS6 ^@ 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|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Decreased localization to the nucleus. No effect on homodimerization. Decreased transcription cis-regulatory region binding. Loss of DNA-binding transcription factor activity. Acts as a dominant negative.|||Decreased localization to the nucleus. No effect on homodimerization. No effect on transcription cis-regulatory region binding. No effect on DNA-binding transcription factor activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||HMG box|||In isoform 2.|||Increased localization to the nucleus. Decreased transcription cis-regulatory region binding. No effect on DNA-binding transcription factor activity.|||Loss of localization to the nucleus. Loss of transcription cis-regulatory region binding. Loss of DNA-binding transcription factor activity. Acts as a dominant negative.|||Phosphoserine|||Phosphothreonine|||Transcription factor SOX-6 ^@ http://purl.uniprot.org/annotation/PRO_0000048730|||http://purl.uniprot.org/annotation/VSP_002198 http://togogenome.org/gene/10090:Cd5l ^@ http://purl.uniprot.org/uniprot/Q9QWK4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site ^@ CD5 antigen-like|||Decreased glycosylation.|||Does not affect glycosylation.|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||SRCR 1|||SRCR 2|||SRCR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000033226 http://togogenome.org/gene/10090:Pif1 ^@ http://purl.uniprot.org/uniprot/Q80SX8 ^@ Binding Site|||Chain|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ ATP-dependent DNA helicase PIF1|||Disordered|||In isoform 2.|||In isoform 3.|||PINT|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000295091|||http://purl.uniprot.org/annotation/VSP_026718|||http://purl.uniprot.org/annotation/VSP_026719|||http://purl.uniprot.org/annotation/VSP_047458 http://togogenome.org/gene/10090:Prrg4 ^@ http://purl.uniprot.org/uniprot/Q4KL73|||http://purl.uniprot.org/uniprot/Q8BGN6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Propeptide|||Sequence Conflict|||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|||Transmembrane gamma-carboxyglutamic acid protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000022553|||http://purl.uniprot.org/annotation/PRO_0000022554|||http://purl.uniprot.org/annotation/PRO_5014309396 http://togogenome.org/gene/10090:Lrrc74a ^@ http://purl.uniprot.org/uniprot/F6QBN8 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Or4b13 ^@ http://purl.uniprot.org/uniprot/Q60881 ^@ 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 4B13 ^@ http://purl.uniprot.org/annotation/PRO_0000150819 http://togogenome.org/gene/10090:Ttk ^@ http://purl.uniprot.org/uniprot/Q3TPW2|||http://purl.uniprot.org/uniprot/Q8BX21|||http://purl.uniprot.org/uniprot/Q8BY97 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Protein kinase ^@ http://togogenome.org/gene/10090:U2af1l4 ^@ http://purl.uniprot.org/uniprot/Q8BGJ9 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger ^@ C3H1-type 1|||C3H1-type 2|||Disordered|||Does not impair nuclear localization.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||RRM|||Removed|||Splicing factor U2AF 26 kDa subunit ^@ http://purl.uniprot.org/annotation/PRO_0000309741|||http://purl.uniprot.org/annotation/VSP_056874|||http://purl.uniprot.org/annotation/VSP_056875|||http://purl.uniprot.org/annotation/VSP_056876|||http://purl.uniprot.org/annotation/VSP_056877 http://togogenome.org/gene/10090:Sis ^@ http://purl.uniprot.org/uniprot/F8VQM5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||P-type ^@ http://togogenome.org/gene/10090:Syp ^@ http://purl.uniprot.org/uniprot/Q62277 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||MARVEL|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Repeats, Gly-rich|||Synaptophysin|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000179162 http://togogenome.org/gene/10090:BC031181 ^@ http://purl.uniprot.org/uniprot/Q91WE4 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Necessary for its localzation to the endoplasmic reticulum and lipid droplets|||UPF0729 protein C18orf32 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000321909 http://togogenome.org/gene/10090:Terf2 ^@ http://purl.uniprot.org/uniprot/D3YZ08|||http://purl.uniprot.org/uniprot/E9QM06|||http://purl.uniprot.org/uniprot/O35144 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes interaction with DCLRE1B/Apollo, leading to activate the ATM signaling pathway.|||Abolishes interaction with TERF2IP/RAP1 but does not affect protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair.|||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.|||Myb-like|||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_0000197132|||http://purl.uniprot.org/annotation/VSP_027086 http://togogenome.org/gene/10090:Fbxl17 ^@ http://purl.uniprot.org/uniprot/Q9QZN1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Disordered|||F-box|||F-box/LRR-repeat protein 17|||In isoform 2.|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000119866|||http://purl.uniprot.org/annotation/VSP_009477|||http://purl.uniprot.org/annotation/VSP_009478 http://togogenome.org/gene/10090:Zfp280b ^@ http://purl.uniprot.org/uniprot/Q505F4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Golga1 ^@ http://purl.uniprot.org/uniprot/Q3TR77|||http://purl.uniprot.org/uniprot/Q9CW79 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant ^@ Disordered|||GRIP|||Golgin subfamily A member 1|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000190053|||http://purl.uniprot.org/annotation/VSP_007726 http://togogenome.org/gene/10090:Tmc1 ^@ http://purl.uniprot.org/uniprot/Q8R4P5 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Disrupts interaction with CIB2 and CIB3.|||Extracellular|||Helical|||In BTH.|||In isoform 2.|||No impact on interaction with CIB2 and CIB3.|||Required for interaction with CIB2|||Transmembrane channel-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000185381|||http://purl.uniprot.org/annotation/VSP_006435|||http://purl.uniprot.org/annotation/VSP_006436|||http://purl.uniprot.org/annotation/VSP_006437 http://togogenome.org/gene/10090:Or8s16 ^@ http://purl.uniprot.org/uniprot/Q7TS17 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Disp1 ^@ http://purl.uniprot.org/uniprot/Q3TDN0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Basic and acidic residues|||Disordered|||Helical|||In icb; loss of function.|||In isoform 2.|||Loss of function; when associated with 571-A-A-572.|||Loss of function; when associated with 571-N-N-572.|||Loss of function; when associated with A-1049.|||Loss of function; when associated with N-1049.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein dispatched homolog 1|||SSD ^@ http://purl.uniprot.org/annotation/PRO_0000310694|||http://purl.uniprot.org/annotation/VSP_029322|||http://purl.uniprot.org/annotation/VSP_029323 http://togogenome.org/gene/10090:Rcan1 ^@ http://purl.uniprot.org/uniprot/Q542V6|||http://purl.uniprot.org/uniprot/Q9JHG6 ^@ 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|||Calcipressin-1|||Disordered|||In isoform B.|||In isoform C.|||In isoform E.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000211415|||http://purl.uniprot.org/annotation/VSP_001317|||http://purl.uniprot.org/annotation/VSP_001318|||http://purl.uniprot.org/annotation/VSP_059568 http://togogenome.org/gene/10090:Kcna5 ^@ http://purl.uniprot.org/uniprot/Q61762 ^@ Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Crosslink|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||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 isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine; by CK2 and PKA|||Phosphoserine; by PKA|||Potassium voltage-gated channel subfamily A member 5|||S-palmitoyl cysteine|||S4-S5 linker|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000053986|||http://purl.uniprot.org/annotation/VSP_000961|||http://purl.uniprot.org/annotation/VSP_000962 http://togogenome.org/gene/10090:Ncoa7 ^@ http://purl.uniprot.org/uniprot/A9Q6S9|||http://purl.uniprot.org/uniprot/Q6DFV7 ^@ 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.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||LysM|||N-acetylmethionine|||Nuclear receptor coactivator 7|||Phosphoserine|||Phosphothreonine|||Polar residues|||TLDc ^@ http://purl.uniprot.org/annotation/PRO_0000245230|||http://purl.uniprot.org/annotation/VSP_019640|||http://purl.uniprot.org/annotation/VSP_019641|||http://purl.uniprot.org/annotation/VSP_019642|||http://purl.uniprot.org/annotation/VSP_019643|||http://purl.uniprot.org/annotation/VSP_019644|||http://purl.uniprot.org/annotation/VSP_019645|||http://purl.uniprot.org/annotation/VSP_019646|||http://purl.uniprot.org/annotation/VSP_019647|||http://purl.uniprot.org/annotation/VSP_019648 http://togogenome.org/gene/10090:Mageb2 ^@ http://purl.uniprot.org/uniprot/Q4U221 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic residues|||Disordered|||MAGE|||Polar residues ^@ http://togogenome.org/gene/10090:Anapc13 ^@ http://purl.uniprot.org/uniprot/Q8R034 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Anaphase-promoting complex subunit 13|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000253981 http://togogenome.org/gene/10090:Vmn1r30 ^@ http://purl.uniprot.org/uniprot/Q8R2D2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Foxn4 ^@ http://purl.uniprot.org/uniprot/Q8K3Q3 ^@ 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 N4|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000091871 http://togogenome.org/gene/10090:Sp9 ^@ http://purl.uniprot.org/uniprot/Q64HY3 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ 9aaTAD; inactive|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In isoform 2.|||Phosphoserine|||Transcription factor Sp9 ^@ http://purl.uniprot.org/annotation/PRO_0000395451|||http://purl.uniprot.org/annotation/VSP_039467 http://togogenome.org/gene/10090:Il16 ^@ http://purl.uniprot.org/uniprot/O54824 ^@ 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.|||Interaction with GRIN2A|||Interaction with PPP1R12A, PPP1R12B and PPP1R12C|||Interleukin-16|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphoserine|||Polar residues|||Pro-interleukin-16 ^@ http://purl.uniprot.org/annotation/PRO_0000015418|||http://purl.uniprot.org/annotation/PRO_0000377546|||http://purl.uniprot.org/annotation/VSP_037460 http://togogenome.org/gene/10090:Polk ^@ http://purl.uniprot.org/uniprot/A0A1Y7VIV8|||http://purl.uniprot.org/uniprot/Q3UUL1|||http://purl.uniprot.org/uniprot/Q5Q9H0|||http://purl.uniprot.org/uniprot/Q5Q9H6|||http://purl.uniprot.org/uniprot/Q5Q9H7|||http://purl.uniprot.org/uniprot/Q9CRV6|||http://purl.uniprot.org/uniprot/Q9QUG2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||DNA polymerase kappa|||Disordered|||In isoform 2.|||In strain: C3H/He.|||UBZ4-type|||UBZ4-type 1|||UBZ4-type 2|||UmuC ^@ http://purl.uniprot.org/annotation/PRO_0000173991|||http://purl.uniprot.org/annotation/VSP_012807|||http://purl.uniprot.org/annotation/VSP_012808 http://togogenome.org/gene/10090:Prss58 ^@ http://purl.uniprot.org/uniprot/Q8BW11 ^@ 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|||Putative inactive serine protease 58 ^@ http://purl.uniprot.org/annotation/PRO_0000317764 http://togogenome.org/gene/10090:Chka ^@ http://purl.uniprot.org/uniprot/O54804 ^@ 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 kinase alpha|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000206220|||http://purl.uniprot.org/annotation/VSP_009684 http://togogenome.org/gene/10090:Mdp1 ^@ http://purl.uniprot.org/uniprot/Q9D967 ^@ 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 ^@ 50% decrease in enzymatic activity.|||92% loss of enzymatic activity.|||Abolishes enzymatic activity.|||Magnesium-dependent phosphatase 1|||No effect on enzymatic activity.|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000068828 http://togogenome.org/gene/10090:Sema3b ^@ http://purl.uniprot.org/uniprot/M9MMK0|||http://purl.uniprot.org/uniprot/Q0VGP2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Ig-like|||Sema ^@ http://purl.uniprot.org/annotation/PRO_5004178659|||http://purl.uniprot.org/annotation/PRO_5015096666 http://togogenome.org/gene/10090:Or5d37 ^@ http://purl.uniprot.org/uniprot/A2AVT5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp629 ^@ http://purl.uniprot.org/uniprot/Q6A085 ^@ 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 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_0000280427 http://togogenome.org/gene/10090:H2ac10 ^@ http://purl.uniprot.org/uniprot/Q8CGP5 ^@ Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region ^@ Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A type 1-F|||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|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000227502 http://togogenome.org/gene/10090:Ensa ^@ http://purl.uniprot.org/uniprot/P60840 ^@ 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 ^@ Alpha-endosulfine|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by GWL|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000146759|||http://purl.uniprot.org/annotation/VSP_001444|||http://purl.uniprot.org/annotation/VSP_037068|||http://purl.uniprot.org/annotation/VSP_037069 http://togogenome.org/gene/10090:Cc2d1a ^@ http://purl.uniprot.org/uniprot/Q8K1A6 ^@ 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|||C2|||Coiled-coil and C2 domain-containing protein 1A|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000239610 http://togogenome.org/gene/10090:Mcidas ^@ http://purl.uniprot.org/uniprot/Q3UZ45 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||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_0000411077 http://togogenome.org/gene/10090:Ppp4r4 ^@ http://purl.uniprot.org/uniprot/Q8C0Y0 ^@ 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 ^@ Basic and acidic residues|||Disordered|||HEAT 1|||HEAT 2|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Serine/threonine-protein phosphatase 4 regulatory subunit 4 ^@ http://purl.uniprot.org/annotation/PRO_0000311851|||http://purl.uniprot.org/annotation/VSP_029618|||http://purl.uniprot.org/annotation/VSP_029619|||http://purl.uniprot.org/annotation/VSP_029620 http://togogenome.org/gene/10090:Dbf4 ^@ http://purl.uniprot.org/uniprot/B2RS44|||http://purl.uniprot.org/uniprot/Q9QZ41 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant|||Zinc Finger ^@ BRCT 1|||BRCT 2|||DBF4-type|||Disordered|||In isoform 2.|||In isoform 3.|||Integrase domain-binding motif 1 (IBM1)|||Integrase domain-binding motif 2 (IBM2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein DBF4 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000234062|||http://purl.uniprot.org/annotation/VSP_018205|||http://purl.uniprot.org/annotation/VSP_018206|||http://purl.uniprot.org/annotation/VSP_018207 http://togogenome.org/gene/10090:Cabs1 ^@ http://purl.uniprot.org/uniprot/Q8C633 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ Calcium-binding and spermatid-specific protein 1|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000339180 http://togogenome.org/gene/10090:Il27 ^@ http://purl.uniprot.org/uniprot/Q8K3I6 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide ^@ Disordered|||Interleukin-27 subunit alpha|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000320140 http://togogenome.org/gene/10090:Tmem217 ^@ http://purl.uniprot.org/uniprot/A0A3Q4EHH0|||http://purl.uniprot.org/uniprot/Q14AF1 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Rcn3 ^@ http://purl.uniprot.org/uniprot/Q8BH97 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||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_0000004152 http://togogenome.org/gene/10090:Ndrg2 ^@ http://purl.uniprot.org/uniprot/Q9QYG0 ^@ Chain|||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|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by PKC/PRKCQ or SGK1|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1 or SGK1|||Phosphothreonine; by SGK1|||Polar residues|||Protein NDRG2|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000441168|||http://purl.uniprot.org/annotation/VSP_019009 http://togogenome.org/gene/10090:Dazap2 ^@ http://purl.uniprot.org/uniprot/Q9DCP9 ^@ 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 ^@ DAZ-associated protein 2|||Disordered|||PPAY|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000079789 http://togogenome.org/gene/10090:Vmn1r6 ^@ http://purl.uniprot.org/uniprot/Q8R2D4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pogz ^@ http://purl.uniprot.org/uniprot/B9EIG6|||http://purl.uniprot.org/uniprot/D3YUX1|||http://purl.uniprot.org/uniprot/Q0VGT3|||http://purl.uniprot.org/uniprot/Q8BZH4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ 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|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||DDE-1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HTH CENPB-type|||Integrase domain-binding motif (IBM)|||Phosphoserine|||Phosphothreonine|||Pogo transposable element with ZNF domain|||Polar residues|||Pro residues|||Required for interaction with CBX5 ^@ http://purl.uniprot.org/annotation/PRO_0000047225 http://togogenome.org/gene/10090:Tnks1bp1 ^@ http://purl.uniprot.org/uniprot/P58871 ^@ 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 ^@ 182 kDa tankyrase-1-binding protein|||Acidic|||Basic and acidic residues|||Disordered|||N6-methyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Tankyrase-binding ^@ http://purl.uniprot.org/annotation/PRO_0000072438 http://togogenome.org/gene/10090:Chpt1 ^@ http://purl.uniprot.org/uniprot/D3YU39|||http://purl.uniprot.org/uniprot/Q8C025 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cholinephosphotransferase 1|||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 isoform 2.|||In isoform 3.|||Increases basicity of active site His|||Lumenal|||N-acetylalanine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000289253|||http://purl.uniprot.org/annotation/VSP_025991|||http://purl.uniprot.org/annotation/VSP_025992|||http://purl.uniprot.org/annotation/VSP_025993|||http://purl.uniprot.org/annotation/VSP_025994 http://togogenome.org/gene/10090:Usf3 ^@ http://purl.uniprot.org/uniprot/B2RUQ2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Basic and acidic residues|||Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or5aq6 ^@ http://purl.uniprot.org/uniprot/A2AT96 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:1700030J22Rik ^@ http://purl.uniprot.org/uniprot/B9EHE0|||http://purl.uniprot.org/uniprot/Q8BHB7 ^@ 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|||Uncharacterized protein C16orf46 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000279431|||http://purl.uniprot.org/annotation/VSP_023436|||http://purl.uniprot.org/annotation/VSP_023437 http://togogenome.org/gene/10090:Ap1m1 ^@ http://purl.uniprot.org/uniprot/P35585|||http://purl.uniprot.org/uniprot/Q3UG16 ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn ^@ AP-1 complex subunit mu-1|||MHD|||N-acetylserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000193771 http://togogenome.org/gene/10090:Spata17 ^@ http://purl.uniprot.org/uniprot/Q9D552 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ IQ 1|||IQ 2|||IQ 3|||In isoform 2.|||In isoform 3.|||Spermatogenesis-associated protein 17 ^@ http://purl.uniprot.org/annotation/PRO_0000265935|||http://purl.uniprot.org/annotation/VSP_021906|||http://purl.uniprot.org/annotation/VSP_021907|||http://purl.uniprot.org/annotation/VSP_021908|||http://purl.uniprot.org/annotation/VSP_021909 http://togogenome.org/gene/10090:Kcnb1 ^@ http://purl.uniprot.org/uniprot/Q03717 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphoserine; by CDK5; in vitro|||Phosphothreonine|||Phosphotyrosine; by Src|||Polar residues|||Potassium voltage-gated channel subfamily B member 1|||Selectivity filter|||Self-association ^@ http://purl.uniprot.org/annotation/PRO_0000054043 http://togogenome.org/gene/10090:Ltb4r1 ^@ http://purl.uniprot.org/uniprot/A7VJD3|||http://purl.uniprot.org/uniprot/O88855 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||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 1|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069709 http://togogenome.org/gene/10090:Btbd35f18 ^@ http://purl.uniprot.org/uniprot/L7MU83 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:Slc10a3 ^@ http://purl.uniprot.org/uniprot/A0A158SIT6|||http://purl.uniprot.org/uniprot/P21129 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||P3 protein ^@ http://purl.uniprot.org/annotation/PRO_0000052344 http://togogenome.org/gene/10090:Pcsk6 ^@ http://purl.uniprot.org/uniprot/E9Q4D0|||http://purl.uniprot.org/uniprot/F6XJP7 ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Charge relay system|||Disordered|||P/Homo B|||PLAC|||Pro residues ^@ http://togogenome.org/gene/10090:Mal2 ^@ http://purl.uniprot.org/uniprot/Q2KHK7|||http://purl.uniprot.org/uniprot/Q8BI08 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||MARVEL|||N-linked (GlcNAc...) asparagine|||Protein MAL2 ^@ http://purl.uniprot.org/annotation/PRO_0000156809 http://togogenome.org/gene/10090:Or12e8 ^@ http://purl.uniprot.org/uniprot/Q8VGT7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tcf21 ^@ http://purl.uniprot.org/uniprot/O35437 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Transcription factor 21|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127465 http://togogenome.org/gene/10090:Zfp846 ^@ http://purl.uniprot.org/uniprot/G3X996|||http://purl.uniprot.org/uniprot/Q8BIQ2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dmrtc1b ^@ http://purl.uniprot.org/uniprot/A2AI93|||http://purl.uniprot.org/uniprot/Q2PMX6|||http://purl.uniprot.org/uniprot/Q2PMX7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Doublesex- and mab-3-related transcription factor C1/C2 C-terminal|||Polar residues ^@ http://togogenome.org/gene/10090:Aoc1 ^@ http://purl.uniprot.org/uniprot/E9PYN9|||http://purl.uniprot.org/uniprot/Q3UKB9 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Signal Peptide ^@ 2',4',5'-topaquinone|||Amine oxidase|||Copper amine oxidase N2-terminal|||Copper amine oxidase N3-terminal|||Copper amine oxidase catalytic|||Proton acceptor|||Schiff-base intermediate with substrate; via topaquinone ^@ http://purl.uniprot.org/annotation/PRO_5004230158|||http://purl.uniprot.org/annotation/PRO_5015090354 http://togogenome.org/gene/10090:Stac3 ^@ http://purl.uniprot.org/uniprot/Q8BZ71 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Loss of co-localization with CACNA1S and strongly decreased co-localization with CACNA1C; when associated with E-133.|||Loss of co-localization with CACNA1S and strongly decreased co-localization with CACNA1C; when associated with L-104.|||Loss of normal excitation-contraction coupling. Loss of function in enhancing calcium channel activity.|||Phorbol-ester/DAG-type|||SH3 1|||SH3 2|||SH3 and cysteine-rich domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000232583 http://togogenome.org/gene/10090:Prkn ^@ http://purl.uniprot.org/uniprot/A0A3B2W489|||http://purl.uniprot.org/uniprot/Q9WVS6 ^@ Active Site|||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|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase parkin|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||IBR-type|||In isoform 2.|||In isoform 3.|||Necessary for PINK1-dependent localization to mitochondria|||Phosphoserine; by PINK1|||Phosphothreonine|||Phosphothreonine; by PINK1|||REP|||RING-type|||RING-type 0; atypical|||RING-type 1|||RING-type 2; atypical|||SYT11 binding 1|||SYT11 binding 2|||TRIAD supradomain|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000058577|||http://purl.uniprot.org/annotation/VSP_011713|||http://purl.uniprot.org/annotation/VSP_011714|||http://purl.uniprot.org/annotation/VSP_011715|||http://purl.uniprot.org/annotation/VSP_011716 http://togogenome.org/gene/10090:Lipn ^@ http://purl.uniprot.org/uniprot/Q3U4B4 ^@ 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 ^@ AB hydrolase-1|||Charge relay system|||Lipase member N|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000286832 http://togogenome.org/gene/10090:Slc38a7 ^@ http://purl.uniprot.org/uniprot/Q8BWH0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Sequence Conflict|||Transmembrane ^@ Helical|||Phosphoserine|||Sodium-coupled neutral amino acid transporter 7 ^@ http://purl.uniprot.org/annotation/PRO_0000319598 http://togogenome.org/gene/10090:1700019A02Rik ^@ http://purl.uniprot.org/uniprot/Q9DA74 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Gstm4 ^@ http://purl.uniprot.org/uniprot/A2AE91|||http://purl.uniprot.org/uniprot/Q8R5I6 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 4 ^@ http://purl.uniprot.org/annotation/PRO_0000449827 http://togogenome.org/gene/10090:Or8b9 ^@ http://purl.uniprot.org/uniprot/Q8VF62 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fam166b ^@ http://purl.uniprot.org/uniprot/A2AIP0|||http://purl.uniprot.org/uniprot/E9Q4G6 ^@ 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|||Ciliary microtubule inner protein 2B|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5. ^@ http://purl.uniprot.org/annotation/PRO_0000342384|||http://purl.uniprot.org/annotation/VSP_034440|||http://purl.uniprot.org/annotation/VSP_034441|||http://purl.uniprot.org/annotation/VSP_034442|||http://purl.uniprot.org/annotation/VSP_034443 http://togogenome.org/gene/10090:Pinx1 ^@ http://purl.uniprot.org/uniprot/Q9CZX5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||G-patch|||PIN2/TERF1-interacting telomerase inhibitor 1|||Phosphoserine|||TBM|||Telomerase inhibitory domain (TID) ^@ http://purl.uniprot.org/annotation/PRO_0000058444 http://togogenome.org/gene/10090:Or8g53 ^@ http://purl.uniprot.org/uniprot/Q8VFN4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H2-T23 ^@ http://purl.uniprot.org/uniprot/P06339|||http://purl.uniprot.org/uniprot/Q3V014 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane ^@ Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Extracellular|||H-2 class I histocompatibility antigen, D-37 alpha chain|||Helical|||Ig-like|||Ig-like C1-type|||Ig-like domain-containing protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000018927|||http://purl.uniprot.org/annotation/PRO_5009970845 http://togogenome.org/gene/10090:Mtnr1a ^@ http://purl.uniprot.org/uniprot/Q14AC3|||http://purl.uniprot.org/uniprot/Q61184 ^@ 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|||Melatonin receptor type 1A|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069863 http://togogenome.org/gene/10090:Nxpe4 ^@ http://purl.uniprot.org/uniprot/Q52KP5 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||N-linked (GlcNAc...) asparagine|||NXPE family member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000019554|||http://purl.uniprot.org/annotation/VSP_014702 http://togogenome.org/gene/10090:Rnf181 ^@ http://purl.uniprot.org/uniprot/D3YUJ1|||http://purl.uniprot.org/uniprot/Q9CY62 ^@ 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 ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF181|||In isoform 2.|||In isoform 3.|||Phosphothreonine|||RING-type|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000295175|||http://purl.uniprot.org/annotation/VSP_027006|||http://purl.uniprot.org/annotation/VSP_027007 http://togogenome.org/gene/10090:Npffr2 ^@ http://purl.uniprot.org/uniprot/Q924H0 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||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 2 ^@ http://purl.uniprot.org/annotation/PRO_0000069916 http://togogenome.org/gene/10090:Wars1 ^@ http://purl.uniprot.org/uniprot/P32921|||http://purl.uniprot.org/uniprot/Q3U6U7 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant ^@ 'HIGH' region|||'KMSKS' region|||In isoform 2.|||N6-succinyllysine|||Phosphoserine|||T1-TrpRS|||T2-TrpRS|||Tryptophan--tRNA ligase, cytoplasmic|||WHEP-TRS ^@ http://purl.uniprot.org/annotation/PRO_0000136739|||http://purl.uniprot.org/annotation/PRO_0000386463|||http://purl.uniprot.org/annotation/PRO_0000386464|||http://purl.uniprot.org/annotation/VSP_006313 http://togogenome.org/gene/10090:Abcb9 ^@ http://purl.uniprot.org/uniprot/Q9JJ59 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ ABC transmembrane type-1|||ABC transporter|||ABC-type oligopeptide transporter ABCB9|||Helical|||Important for the second trafficking step from the Golgi to the endosomal and lysosomal compartments|||In isoform 2.|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000000253|||http://purl.uniprot.org/annotation/VSP_000032|||http://purl.uniprot.org/annotation/VSP_000033 http://togogenome.org/gene/10090:Odf1 ^@ http://purl.uniprot.org/uniprot/A6H656 ^@ Domain Extent|||Region ^@ Domain Extent ^@ SHSP ^@ http://togogenome.org/gene/10090:Slc22a1 ^@ http://purl.uniprot.org/uniprot/O08966 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreased fenoterol uptake. Decreased fenoterol affinity. No change in trospium uptake. No change in terbutaline affinity.|||Extracellular|||Helical|||Increased trospium uptake. Increased trospium affinity. No change in fenoterol uptake.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Proline-rich sequence|||Solute carrier family 22 member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000333876 http://togogenome.org/gene/10090:Coch ^@ http://purl.uniprot.org/uniprot/Q62507 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide ^@ Cochlin|||Disordered|||LCCL|||N-linked (GlcNAc...) asparagine|||VWFA 1|||VWFA 2 ^@ http://purl.uniprot.org/annotation/PRO_0000020969 http://togogenome.org/gene/10090:Arl5c ^@ http://purl.uniprot.org/uniprot/Q6P068 ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Lipid Binding ^@ ADP-ribosylation factor-like protein 5C|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000332304 http://togogenome.org/gene/10090:Abi1 ^@ http://purl.uniprot.org/uniprot/B7ZCU0|||http://purl.uniprot.org/uniprot/B7ZCU3|||http://purl.uniprot.org/uniprot/B7ZCU4|||http://purl.uniprot.org/uniprot/Q3TJ64|||http://purl.uniprot.org/uniprot/Q3TJR5|||http://purl.uniprot.org/uniprot/Q3TPY5|||http://purl.uniprot.org/uniprot/Q8CBW3 ^@ 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 ^@ Abl interactor 1|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 5.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||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_0000191788|||http://purl.uniprot.org/annotation/VSP_010756|||http://purl.uniprot.org/annotation/VSP_010757|||http://purl.uniprot.org/annotation/VSP_010758|||http://purl.uniprot.org/annotation/VSP_022636 http://togogenome.org/gene/10090:Hmbox1 ^@ http://purl.uniprot.org/uniprot/H3BKM3|||http://purl.uniprot.org/uniprot/Q8BJA3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Site|||Splice Variant ^@ 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|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||POU-specific atypical|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000233288|||http://purl.uniprot.org/annotation/VSP_018114|||http://purl.uniprot.org/annotation/VSP_018115|||http://purl.uniprot.org/annotation/VSP_018116 http://togogenome.org/gene/10090:Ubtfl1 ^@ http://purl.uniprot.org/uniprot/Q3USZ2 ^@ 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|||HMG box 1|||HMG box 2|||Polar residues|||Upstream-binding factor 1-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000386641 http://togogenome.org/gene/10090:Ass1 ^@ http://purl.uniprot.org/uniprot/P16460 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Modified Residue ^@ Argininosuccinate synthase|||N6-acetyllysine|||N6-acetyllysine; by CLOCK|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000148555 http://togogenome.org/gene/10090:Sh3gl1 ^@ http://purl.uniprot.org/uniprot/A0A3B2W7K0|||http://purl.uniprot.org/uniprot/Q3TRJ7|||http://purl.uniprot.org/uniprot/Q62419 ^@ 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 ^@ BAR|||Basic and acidic residues|||Disordered|||Endophilin-A2|||Interaction with ARC|||Membrane-binding amphipathic helix|||Phosphoserine|||Phosphotyrosine|||Required for dimerization upon membrane association|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000146745 http://togogenome.org/gene/10090:Clec2d ^@ http://purl.uniprot.org/uniprot/F5BFH0|||http://purl.uniprot.org/uniprot/Q91V08 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||C-type lectin domain family 2 member D|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000315286 http://togogenome.org/gene/10090:Cbx2 ^@ http://purl.uniprot.org/uniprot/P30658|||http://purl.uniprot.org/uniprot/Q3URA3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ A.T hook|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Basic residues|||Chromo|||Chromobox protein homolog 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nuclear localization signal|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000080202 http://togogenome.org/gene/10090:Rbm31y ^@ http://purl.uniprot.org/uniprot/Q9D3U4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ RRM ^@ http://togogenome.org/gene/10090:Fscn1 ^@ http://purl.uniprot.org/uniprot/Q61553 ^@ Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ Fascin|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylthreonine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000219380 http://togogenome.org/gene/10090:Asap2 ^@ http://purl.uniprot.org/uniprot/D3YX85|||http://purl.uniprot.org/uniprot/E9PX52|||http://purl.uniprot.org/uniprot/Q3UH27|||http://purl.uniprot.org/uniprot/Q7SIG6 ^@ Chain|||Coiled-Coil|||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|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Strand|||Turn ^@ ANK|||ANK 1|||ANK 2|||Abolishes Arf-GAP mediated stimulation of GTP hydrolysis.|||Arf-GAP|||Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2|||Disordered|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduces Arf-GAP mediated stimulation of GTP hydrolysis 100-fold and abolishes Arf-GAP mediated stimulation of GTP hydrolysis; when associated with A-285.|||Reduces Arf-GAP mediated stimulation of GTP hydrolysis 100-fold and abolishes Arf-GAP mediated stimulation of GTP hydrolysis; when associated with A-306.|||Reduces Arf-GAP mediated stimulation of GTP hydrolysis 1000-fold.|||Reduces Arf-GAP mediated stimulation of GTP hydrolysis more than 10000-fold.|||SH3|||Strongly reduces Arf-GAP mediated stimulation of GTP hydrolysis. ^@ http://purl.uniprot.org/annotation/PRO_0000074199|||http://purl.uniprot.org/annotation/VSP_014776|||http://purl.uniprot.org/annotation/VSP_014777 http://togogenome.org/gene/10090:Fzd6 ^@ http://purl.uniprot.org/uniprot/Q3UTZ0|||http://purl.uniprot.org/uniprot/Q542J1|||http://purl.uniprot.org/uniprot/Q61089 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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|||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_0000012995|||http://purl.uniprot.org/annotation/PRO_5009971085 http://togogenome.org/gene/10090:Srebf2 ^@ http://purl.uniprot.org/uniprot/Q3U1N2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 L1.2.3A mutant; reduced affinity for importin-beta.|||In isoform 2.|||Interaction with LMNA|||Leucine-zipper|||Lumenal|||Phosphoserine|||Polar residues|||Pro residues|||Processed sterol regulatory element-binding protein 2|||Sterol regulatory element-binding protein 2|||Transcriptional activation (acidic)|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000317059|||http://purl.uniprot.org/annotation/PRO_0000317060|||http://purl.uniprot.org/annotation/VSP_052658|||http://purl.uniprot.org/annotation/VSP_052659 http://togogenome.org/gene/10090:Lrriq3 ^@ http://purl.uniprot.org/uniprot/Q14DL3 ^@ 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|||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_0000311195|||http://purl.uniprot.org/annotation/VSP_029412|||http://purl.uniprot.org/annotation/VSP_029413|||http://purl.uniprot.org/annotation/VSP_029414|||http://purl.uniprot.org/annotation/VSP_029415 http://togogenome.org/gene/10090:Or6k4 ^@ http://purl.uniprot.org/uniprot/E9Q0Q2|||http://purl.uniprot.org/uniprot/Q8VFZ1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Evi5 ^@ http://purl.uniprot.org/uniprot/F8VPT6|||http://purl.uniprot.org/uniprot/Q3UYX4 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||Polar residues|||Rab-GAP TBC ^@ http://togogenome.org/gene/10090:Pde3b ^@ http://purl.uniprot.org/uniprot/E9QLQ3|||http://purl.uniprot.org/uniprot/Q3UQ25|||http://purl.uniprot.org/uniprot/Q61409 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Interaction with PIK3R6|||Interaction with RAPGEF3|||Loss of insulin-induced phosphorylation.|||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_0000198803 http://togogenome.org/gene/10090:Tle5 ^@ http://purl.uniprot.org/uniprot/B7ZNK7|||http://purl.uniprot.org/uniprot/P63002|||http://purl.uniprot.org/uniprot/Q3TYD9 ^@ 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|||CCN domain|||Disordered|||Groucho/TLE N-terminal Q-rich|||In isoform 2.|||Phosphoserine|||TLE family member 5 ^@ http://purl.uniprot.org/annotation/PRO_0000050835|||http://purl.uniprot.org/annotation/VSP_006771 http://togogenome.org/gene/10090:Capn12 ^@ http://purl.uniprot.org/uniprot/E9QL26 ^@ Active Site|||Domain Extent|||Region|||Site ^@ Active Site|||Domain Extent|||Region ^@ Calpain catalytic|||Disordered|||EF-hand ^@ http://togogenome.org/gene/10090:Rhobtb3 ^@ http://purl.uniprot.org/uniprot/Q9CTN4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ BTB 1|||BTB 2|||Interaction with Rab9|||Rho-like|||Rho-related BTB domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000198965 http://togogenome.org/gene/10090:Zfp260 ^@ http://purl.uniprot.org/uniprot/Q62513 ^@ 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 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|||Disordered|||Polar residues|||Zinc finger protein 260 ^@ http://purl.uniprot.org/annotation/PRO_0000047321 http://togogenome.org/gene/10090:Plxnc1 ^@ http://purl.uniprot.org/uniprot/Q9CRY9|||http://purl.uniprot.org/uniprot/Q9QZC2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Plexin cytoplasmic RasGAP|||Plexin-C1|||Sema ^@ http://purl.uniprot.org/annotation/PRO_0000232750 http://togogenome.org/gene/10090:B3gat3 ^@ http://purl.uniprot.org/uniprot/P58158 ^@ 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|||Region|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3|||Helical; Signal-anchor for type II membrane protein|||Interaction with galactose moiety of substrate glycoprotein|||Interchain|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000195177 http://togogenome.org/gene/10090:Clec2i ^@ http://purl.uniprot.org/uniprot/B2RTA4|||http://purl.uniprot.org/uniprot/B7ZP15|||http://purl.uniprot.org/uniprot/E0CX52|||http://purl.uniprot.org/uniprot/Q9WVF9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||C-type lectin domain family 2 member I|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000315291|||http://purl.uniprot.org/annotation/VSP_030530|||http://purl.uniprot.org/annotation/VSP_030531|||http://purl.uniprot.org/annotation/VSP_030532 http://togogenome.org/gene/10090:Naaladl1 ^@ http://purl.uniprot.org/uniprot/Q7M758 ^@ 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 ^@ Aminopeptidase NAALADL1|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000174124 http://togogenome.org/gene/10090:Bhmt2 ^@ http://purl.uniprot.org/uniprot/Q91WS4 ^@ 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 ^@ Hcy-binding|||Phosphoserine|||S-methylmethionine--homocysteine S-methyltransferase BHMT2 ^@ http://purl.uniprot.org/annotation/PRO_0000273225 http://togogenome.org/gene/10090:Or6b13 ^@ http://purl.uniprot.org/uniprot/Q7TRU0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp648 ^@ http://purl.uniprot.org/uniprot/D3Z0W3 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Svil ^@ http://purl.uniprot.org/uniprot/Q3TTX5|||http://purl.uniprot.org/uniprot/Q8K4L3 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Basic and acidic residues|||Disordered|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||HP|||In isoform 2.|||Interaction with MYLK|||Interaction with NEB|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Supervillin ^@ http://purl.uniprot.org/annotation/PRO_0000218741|||http://purl.uniprot.org/annotation/VSP_058333|||http://purl.uniprot.org/annotation/VSP_058334 http://togogenome.org/gene/10090:Clpsl2 ^@ http://purl.uniprot.org/uniprot/Q3UW21 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Colipase-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000352880 http://togogenome.org/gene/10090:Vmn1r151 ^@ http://purl.uniprot.org/uniprot/L7N288 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cdk18 ^@ http://purl.uniprot.org/uniprot/Q04899|||http://purl.uniprot.org/uniprot/Q0VDL6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Cyclin-dependent kinase 18|||Phosphoserine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086491 http://togogenome.org/gene/10090:AAdacl4fm3 ^@ http://purl.uniprot.org/uniprot/B1AVU7 ^@ Active Site|||Domain Extent|||Region|||Site|||Transmembrane ^@ Active Site|||Domain Extent|||Transmembrane ^@ Alpha/beta hydrolase fold-3|||Helical ^@ http://togogenome.org/gene/10090:Zfp976 ^@ http://purl.uniprot.org/uniprot/E9Q981 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Eppin ^@ http://purl.uniprot.org/uniprot/Q9DA01 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide ^@ BPTI/Kunitz inhibitor|||Eppin|||Interaction with LTF|||Interaction with SEMG1|||WAP ^@ http://purl.uniprot.org/annotation/PRO_0000041380 http://togogenome.org/gene/10090:Itpkb ^@ http://purl.uniprot.org/uniprot/B2RXC2 ^@ Binding Site|||Compositionally Biased Region|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Jag1 ^@ http://purl.uniprot.org/uniprot/Q3UVN4|||http://purl.uniprot.org/uniprot/Q9QXX0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DSL|||Delta-like protein|||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|||Helical|||Heterozygous mutant mice exhibit mild peripheral neuropathy. Homozygous expression results in embryonic lethality by midgestation.|||Important for interaction with NOTCH1|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein jagged-1 ^@ http://purl.uniprot.org/annotation/PRO_0000007626|||http://purl.uniprot.org/annotation/PRO_5014309232 http://togogenome.org/gene/10090:Grk3 ^@ http://purl.uniprot.org/uniprot/Q3UYH7|||http://purl.uniprot.org/uniprot/Q8BVT9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ AGC-kinase C-terminal|||Beta-adrenergic receptor kinase 2|||N-terminal|||PH|||Protein kinase|||Proton acceptor|||RGS ^@ http://purl.uniprot.org/annotation/PRO_0000260828 http://togogenome.org/gene/10090:Selenon ^@ http://purl.uniprot.org/uniprot/D3Z2R5 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Non standard residue|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Non standard residue|||Region|||Signal Peptide ^@ Disordered|||EF-hand|||N-linked (GlcNAc...) asparagine|||Selenocysteine|||Selenoprotein N ^@ http://purl.uniprot.org/annotation/PRO_0000436040 http://togogenome.org/gene/10090:Degs1l ^@ http://purl.uniprot.org/uniprot/Q3TS87 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Sphingolipid delta4-desaturase N-terminal ^@ http://togogenome.org/gene/10090:Klhl2 ^@ http://purl.uniprot.org/uniprot/A0A1B0GQV2|||http://purl.uniprot.org/uniprot/Q8JZP3 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Region|||Repeat ^@ BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000119102 http://togogenome.org/gene/10090:Kcnt2 ^@ http://purl.uniprot.org/uniprot/D3YTU6|||http://purl.uniprot.org/uniprot/D3Z592|||http://purl.uniprot.org/uniprot/D3Z649 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Calcium-activated potassium channel BK alpha subunit|||Disordered|||Helical|||Polar residues|||Potassium channel ^@ http://togogenome.org/gene/10090:Arhgap21 ^@ http://purl.uniprot.org/uniprot/B7ZCJ0|||http://purl.uniprot.org/uniprot/B7ZCJ1|||http://purl.uniprot.org/uniprot/Q6DFV3 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Interaction with ARF1 and ARF6|||Interaction with CTNNA1|||Omega-N-methylarginine|||PDZ|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Rho GTPase-activating protein 21|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000305246 http://togogenome.org/gene/10090:Tnrc18 ^@ http://purl.uniprot.org/uniprot/D3YV17|||http://purl.uniprot.org/uniprot/Q52KG0|||http://purl.uniprot.org/uniprot/Q80WC3 ^@ 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 ^@ Acidic residues|||BAH|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Trinucleotide repeat-containing gene 18 protein ^@ http://purl.uniprot.org/annotation/PRO_0000330826|||http://purl.uniprot.org/annotation/VSP_033130|||http://purl.uniprot.org/annotation/VSP_033131|||http://purl.uniprot.org/annotation/VSP_033132|||http://purl.uniprot.org/annotation/VSP_033133|||http://purl.uniprot.org/annotation/VSP_033134 http://togogenome.org/gene/10090:Rsph6a ^@ http://purl.uniprot.org/uniprot/B2RQM5|||http://purl.uniprot.org/uniprot/Q8CDR2 ^@ 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|||Disordered|||In isoform 2.|||Polar residues|||Radial spoke head protein 6 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000312761|||http://purl.uniprot.org/annotation/VSP_060558 http://togogenome.org/gene/10090:Chmp1b ^@ http://purl.uniprot.org/uniprot/Q99LU0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Charged multivesicular body protein 1B1|||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_0000211455 http://togogenome.org/gene/10090:Susd3 ^@ http://purl.uniprot.org/uniprot/Q9D176 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Sushi|||Sushi domain-containing protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000251974|||http://purl.uniprot.org/annotation/VSP_020835|||http://purl.uniprot.org/annotation/VSP_020836|||http://purl.uniprot.org/annotation/VSP_020837 http://togogenome.org/gene/10090:Fadd ^@ http://purl.uniprot.org/uniprot/Q61160 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict ^@ DED|||Death|||Disordered|||FAS-associated death domain protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000191280 http://togogenome.org/gene/10090:Sec16a ^@ http://purl.uniprot.org/uniprot/E9QAT4|||http://purl.uniprot.org/uniprot/Q3TRA8|||http://purl.uniprot.org/uniprot/Q8K000 ^@ 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 ^@ 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.|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000445696|||http://purl.uniprot.org/annotation/VSP_059936 http://togogenome.org/gene/10090:Gm17660 ^@ http://purl.uniprot.org/uniprot/B9UIU9 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Secretory calcium-binding phosphoprotein proline-glutamine-rich 1 ^@ http://purl.uniprot.org/annotation/PRO_5015087622 http://togogenome.org/gene/10090:Crtc2 ^@ http://purl.uniprot.org/uniprot/Q3U182 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Asymmetric dimethylarginine; by PRMT6|||CREB-regulated transcription coactivator 2|||Disordered|||Does not affect interaction with 14-3-3 proteins.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||No effect on COP1-mediated degradation of TORC1 under forksolin stimulation.|||No interaction with COP1. Inhibition of degradation under exposure to FSK/INS.|||Nuclear export signal|||Phosphoserine|||Phosphoserine; by AMPK, MARK2, SIK1 and SIK2|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Required for interaction with COP1|||Required for ubiquitination and degradation|||Translocates to the nucleus and no COP1-mediated degradation.|||Up-regulates CREB transcription factor activity. Reduces interaction with 14-3-3 proteins.|||Up-regulates CREB-mediated gluconeogenic gene expression. No degradation of CRTC2. Loss of SIK2-mediated phosphorylation. ^@ http://purl.uniprot.org/annotation/PRO_0000318529 http://togogenome.org/gene/10090:Vmn1r166 ^@ http://purl.uniprot.org/uniprot/D3YTY2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc30a10 ^@ http://purl.uniprot.org/uniprot/Q3UVU3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Calcium/manganese antiporter SLC30A10|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Important for coupling of manganese to calcium transport|||In isoform 2.|||Polar residues|||Required for plasma membrane localization ^@ http://purl.uniprot.org/annotation/PRO_0000312581|||http://purl.uniprot.org/annotation/VSP_029867 http://togogenome.org/gene/10090:Tmeff2 ^@ http://purl.uniprot.org/uniprot/Q9QYM9 ^@ 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|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||Kazal-like 1|||Kazal-like 2|||N-linked (GlcNAc...) asparagine|||Polar residues|||Required for shedding|||Tomoregulin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000016588|||http://purl.uniprot.org/annotation/VSP_014314 http://togogenome.org/gene/10090:Prdm16 ^@ http://purl.uniprot.org/uniprot/A2A931|||http://purl.uniprot.org/uniprot/A2A933|||http://purl.uniprot.org/uniprot/A2A934|||http://purl.uniprot.org/uniprot/A2A935|||http://purl.uniprot.org/uniprot/Q8BNF5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||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; atypical|||C2H2-type 8|||C2H2-type 9|||Disordered|||Histone-lysine N-methyltransferase PRDM16|||In isoform 2 and isoform 3.|||In isoform 2.|||Interaction with CTBP1, CTBP2 and ZNF516|||Loss of DNA-binding activity but no effect on PRDM16-mediated BAT gene transcription activation.|||Loss of interaction with CTBP1 and CTBP2 and loss of repression of WAT-specific genes.|||Mediates interaction with SKI and regulation of TGF-beta signaling|||Polar residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000384377|||http://purl.uniprot.org/annotation/VSP_038066|||http://purl.uniprot.org/annotation/VSP_038067|||http://purl.uniprot.org/annotation/VSP_038068|||http://purl.uniprot.org/annotation/VSP_038069 http://togogenome.org/gene/10090:Fbxo33 ^@ http://purl.uniprot.org/uniprot/Q8VE08 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||F-box|||F-box only protein 33 ^@ http://purl.uniprot.org/annotation/PRO_0000314464 http://togogenome.org/gene/10090:Gng3 ^@ http://purl.uniprot.org/uniprot/P63216 ^@ 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_0000012619|||http://purl.uniprot.org/annotation/PRO_0000012620 http://togogenome.org/gene/10090:Mgrn1 ^@ http://purl.uniprot.org/uniprot/Q9D074 ^@ 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.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||Loss of TSG101-binding.|||Loss of ubiquitin-protein ligase activity. Increase in TSG101-binding.|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RING-type|||Removed|||Required for TSG101-binding ^@ http://purl.uniprot.org/annotation/PRO_0000246688|||http://purl.uniprot.org/annotation/VSP_019854|||http://purl.uniprot.org/annotation/VSP_019855|||http://purl.uniprot.org/annotation/VSP_019856 http://togogenome.org/gene/10090:Or7g21 ^@ http://purl.uniprot.org/uniprot/Q8VFJ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rassf8 ^@ http://purl.uniprot.org/uniprot/Q8CJ96 ^@ 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|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ras association domain-containing protein 8|||Ras-associating ^@ http://purl.uniprot.org/annotation/PRO_0000089841 http://togogenome.org/gene/10090:Aoc1l3 ^@ http://purl.uniprot.org/uniprot/Q6WIZ7|||http://purl.uniprot.org/uniprot/Q8BZI2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Copper amine oxidase N2-terminal|||Copper amine oxidase N3-terminal|||Copper amine oxidase catalytic ^@ http://togogenome.org/gene/10090:Ric1 ^@ http://purl.uniprot.org/uniprot/E9QPA1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Ribosome control protein 1 ^@ http://togogenome.org/gene/10090:Nkiras1 ^@ http://purl.uniprot.org/uniprot/Q8CEC5 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Effector region|||Interactions with NFKBIA and NFKBIB|||NF-kappa-B inhibitor-interacting Ras-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000225677 http://togogenome.org/gene/10090:Ccdc73 ^@ http://purl.uniprot.org/uniprot/Q8CDM4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Coiled-coil domain-containing protein 73|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000285295 http://togogenome.org/gene/10090:Dtd2 ^@ http://purl.uniprot.org/uniprot/Q8BHA3 ^@ Chain|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Helix|||Motif|||Splice Variant|||Strand|||Turn ^@ D-aminoacyl-tRNA deacylase 2|||Gly-transPro motif, allows the protein to recognize chirality of D-amino acids|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000254050|||http://purl.uniprot.org/annotation/VSP_021174 http://togogenome.org/gene/10090:Zpld1 ^@ http://purl.uniprot.org/uniprot/Q8BGZ8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Cleavage|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||ZP|||Zona pellucida-like domain-containing protein 1|||Zona pellucida-like domain-containing protein 1, secreted form ^@ http://purl.uniprot.org/annotation/PRO_0000307286|||http://purl.uniprot.org/annotation/PRO_0000441816 http://togogenome.org/gene/10090:Aurka ^@ http://purl.uniprot.org/uniprot/P97477|||http://purl.uniprot.org/uniprot/Q3TEY6 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Activation segment|||Aurora kinase A|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphoserine; by PKA and PAK|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086693|||http://purl.uniprot.org/annotation/VSP_004871 http://togogenome.org/gene/10090:Tcp10c ^@ http://purl.uniprot.org/uniprot/E9Q046|||http://purl.uniprot.org/uniprot/Q8C641 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Centromere protein J C-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:H2ac24 ^@ http://purl.uniprot.org/uniprot/B2RVF0|||http://purl.uniprot.org/uniprot/C0HKE1|||http://purl.uniprot.org/uniprot/C0HKE2|||http://purl.uniprot.org/uniprot/C0HKE3|||http://purl.uniprot.org/uniprot/C0HKE4|||http://purl.uniprot.org/uniprot/C0HKE5|||http://purl.uniprot.org/uniprot/C0HKE6|||http://purl.uniprot.org/uniprot/C0HKE7|||http://purl.uniprot.org/uniprot/C0HKE8|||http://purl.uniprot.org/uniprot/C0HKE9 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Histone H2A type 1-C|||Histone H2A type 1-D|||Histone H2A type 1-E|||Histone H2A type 1-G|||Histone H2A type 1-I|||Histone H2A type 1-N|||Histone H2A type 1-O|||Histone H2A type 1-P|||Histone H2A/H2B/H3|||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_0000439715|||http://purl.uniprot.org/annotation/PRO_0000439716|||http://purl.uniprot.org/annotation/PRO_0000439717|||http://purl.uniprot.org/annotation/PRO_0000439718|||http://purl.uniprot.org/annotation/PRO_0000439719|||http://purl.uniprot.org/annotation/PRO_0000439720|||http://purl.uniprot.org/annotation/PRO_0000439721|||http://purl.uniprot.org/annotation/PRO_0000439722|||http://purl.uniprot.org/annotation/PRO_0000439723 http://togogenome.org/gene/10090:Surf4 ^@ http://purl.uniprot.org/uniprot/Q545Q2|||http://purl.uniprot.org/uniprot/Q64310 ^@ Chain|||Molecule Processing|||Motif|||Region|||Transmembrane ^@ Chain|||Motif|||Transmembrane ^@ Di-lysine motif|||Helical|||Surfeit locus protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000127665 http://togogenome.org/gene/10090:Nmi ^@ http://purl.uniprot.org/uniprot/O35309|||http://purl.uniprot.org/uniprot/Q3UJ82 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-myc-interactor|||NID|||NID 1|||NID 2|||Nmi/IFP 35|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000159703 http://togogenome.org/gene/10090:Crmp1 ^@ http://purl.uniprot.org/uniprot/P97427|||http://purl.uniprot.org/uniprot/Q6P1J1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn ^@ 3'-nitrotyrosine|||Amidohydrolase-related|||Dihydropyrimidinase-related protein 1|||Disordered|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by AURKA|||Phosphotyrosine|||Polar residues|||Required for interaction with FLNA ^@ http://purl.uniprot.org/annotation/PRO_0000165910 http://togogenome.org/gene/10090:Mterf3 ^@ http://purl.uniprot.org/uniprot/Q8R3J4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||Transcription termination factor 3, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000255458 http://togogenome.org/gene/10090:Kirrel ^@ http://purl.uniprot.org/uniprot/Q80W68 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cell attachment site|||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 isoform 2.|||Inhibits interaction with NPHS2.|||Kin of IRRE-like protein 1|||N-linked (GlcNAc...) asparagine|||No effect on interaction with NPHS2.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by FYN ^@ http://purl.uniprot.org/annotation/PRO_0000015094|||http://purl.uniprot.org/annotation/VSP_011736|||http://purl.uniprot.org/annotation/VSP_011737 http://togogenome.org/gene/10090:Fbxo48 ^@ http://purl.uniprot.org/uniprot/Q8CAT8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Disordered|||F-box|||F-box only protein 48 ^@ http://purl.uniprot.org/annotation/PRO_0000335678 http://togogenome.org/gene/10090:Cct2 ^@ http://purl.uniprot.org/uniprot/P80314 ^@ 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)|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||T-complex protein 1 subunit beta ^@ http://purl.uniprot.org/annotation/PRO_0000128317 http://togogenome.org/gene/10090:Aak1 ^@ http://purl.uniprot.org/uniprot/Q3UHJ0 ^@ 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 ^@ AP2-associated protein kinase 1|||Clathrin-binding domain (CBD)|||Disordered|||In isoform 2.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000250579|||http://purl.uniprot.org/annotation/VSP_020670 http://togogenome.org/gene/10090:Parg ^@ http://purl.uniprot.org/uniprot/G3X8U8 ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Poly (ADP-ribose) glycohydrolase (PARG) catalytic ^@ http://togogenome.org/gene/10090:Oas1a ^@ http://purl.uniprot.org/uniprot/P11928 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Region|||Sequence Conflict ^@ 2'-5'-oligoadenylate synthase 1A|||Interaction with dsRNA|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000160260 http://togogenome.org/gene/10090:Tsc22d2 ^@ http://purl.uniprot.org/uniprot/E9Q7M2|||http://purl.uniprot.org/uniprot/Q9CVK3 ^@ 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|||In isoform TSC22D2-1.|||In isoform TSC22D2-4.|||Polar residues|||TSC22 domain family protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000458071|||http://purl.uniprot.org/annotation/VSP_061912|||http://purl.uniprot.org/annotation/VSP_061913 http://togogenome.org/gene/10090:Matr3 ^@ http://purl.uniprot.org/uniprot/Q5BL18|||http://purl.uniprot.org/uniprot/Q8K310 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Strand|||Turn|||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|||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_0000081623 http://togogenome.org/gene/10090:Scyl2 ^@ http://purl.uniprot.org/uniprot/G5E8J9|||http://purl.uniprot.org/uniprot/Q8CFE4 ^@ 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|||HEAT|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Protein kinase|||SCY1-like protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000252447|||http://purl.uniprot.org/annotation/VSP_020980|||http://purl.uniprot.org/annotation/VSP_020981|||http://purl.uniprot.org/annotation/VSP_020982 http://togogenome.org/gene/10090:Ptges3 ^@ http://purl.uniprot.org/uniprot/Q9R0Q7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Strand|||Turn ^@ Acidic residues|||Basic and acidic residues|||CS|||Cleavage; by caspase-7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||PXLE motif|||Phosphoserine|||Prostaglandin E synthase 3 ^@ http://purl.uniprot.org/annotation/PRO_0000218953 http://togogenome.org/gene/10090:Arhgef18 ^@ http://purl.uniprot.org/uniprot/Q6P9R4 ^@ 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|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ Basic and acidic residues|||C2H2-type; degenerate|||DH|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho guanine nucleotide exchange factor 18 ^@ http://purl.uniprot.org/annotation/PRO_0000341416|||http://purl.uniprot.org/annotation/VSP_059878|||http://purl.uniprot.org/annotation/VSP_059879|||http://purl.uniprot.org/annotation/VSP_059880 http://togogenome.org/gene/10090:Gstm2 ^@ http://purl.uniprot.org/uniprot/P15626 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 2|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000185827 http://togogenome.org/gene/10090:Teddm1a ^@ http://purl.uniprot.org/uniprot/E9QLK8|||http://purl.uniprot.org/uniprot/Q810U2 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane epididymal protein 1A ^@ http://purl.uniprot.org/annotation/PRO_0000307130 http://togogenome.org/gene/10090:Cysltr1 ^@ http://purl.uniprot.org/uniprot/Q99JA4 ^@ 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 ^@ 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|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069300|||http://purl.uniprot.org/annotation/VSP_001921 http://togogenome.org/gene/10090:Vps51 ^@ http://purl.uniprot.org/uniprot/Q3UVL4 ^@ 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|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Removed|||Vacuolar protein sorting-associated protein 51 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000358913|||http://purl.uniprot.org/annotation/VSP_036126|||http://purl.uniprot.org/annotation/VSP_036127|||http://purl.uniprot.org/annotation/VSP_036128|||http://purl.uniprot.org/annotation/VSP_036129 http://togogenome.org/gene/10090:Oas1h ^@ http://purl.uniprot.org/uniprot/E9Q326|||http://purl.uniprot.org/uniprot/Q8VI97 ^@ Domain Extent|||Region ^@ Domain Extent ^@ 2'-5'-oligoadenylate synthetase 1|||Polymerase nucleotidyl transferase ^@ http://togogenome.org/gene/10090:Adcy9 ^@ http://purl.uniprot.org/uniprot/E9Q706|||http://purl.uniprot.org/uniprot/P51830 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Adenylate cyclase type 9|||Cytoplasmic|||Disordered|||Extracellular|||Guanylate cyclase|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000195709 http://togogenome.org/gene/10090:Uqcrfs1 ^@ http://purl.uniprot.org/uniprot/Q9CR68 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Topological Domain|||Transmembrane ^@ Cytochrome b-c1 complex subunit 9|||Cytochrome b-c1 complex subunit Rieske, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Rieske ^@ http://purl.uniprot.org/annotation/PRO_0000030667|||http://purl.uniprot.org/annotation/PRO_0000307244 http://togogenome.org/gene/10090:Atxn7 ^@ http://purl.uniprot.org/uniprot/A0A286YDW9|||http://purl.uniprot.org/uniprot/Q8R4I1 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ 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|||N6-acetyllysine|||Polar residues|||Pro residues|||SCA7 ^@ http://purl.uniprot.org/annotation/PRO_0000064760 http://togogenome.org/gene/10090:Ints1 ^@ http://purl.uniprot.org/uniprot/A0A0G2JH17|||http://purl.uniprot.org/uniprot/Q3U1N8|||http://purl.uniprot.org/uniprot/Q6P4S8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ DUF3677|||Disordered|||Helical|||Integrator complex subunit 1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000236045 http://togogenome.org/gene/10090:Colec10 ^@ http://purl.uniprot.org/uniprot/Q8CF98 ^@ 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 ^@ Basic and acidic residues|||C-type lectin|||Collagen-like|||Collectin-10|||Disordered|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000314234 http://togogenome.org/gene/10090:Slc38a3 ^@ http://purl.uniprot.org/uniprot/Q9DCP2 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Disordered|||Helical|||Homozygous mice are lethal. Mice die between 18 and 20 days after birth. Mice are small, lethargic and ataxic.|||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_0000093829 http://togogenome.org/gene/10090:Hexdc ^@ http://purl.uniprot.org/uniprot/Q3U4H6 ^@ Active Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Chain|||Region|||Splice Variant ^@ Disordered|||Hexosaminidase D|||In isoform 2.|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000316791|||http://purl.uniprot.org/annotation/VSP_030778 http://togogenome.org/gene/10090:Phc3 ^@ http://purl.uniprot.org/uniprot/B7ZNA5|||http://purl.uniprot.org/uniprot/D3YY34|||http://purl.uniprot.org/uniprot/Q8CHP6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||FCS-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HD1|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Polyhomeotic-like protein 3|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000076291|||http://purl.uniprot.org/annotation/VSP_016772|||http://purl.uniprot.org/annotation/VSP_016773|||http://purl.uniprot.org/annotation/VSP_016774|||http://purl.uniprot.org/annotation/VSP_016775 http://togogenome.org/gene/10090:G6pd2 ^@ http://purl.uniprot.org/uniprot/G3UWD6|||http://purl.uniprot.org/uniprot/P97324 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Glucose-6-phosphate 1-dehydrogenase 2|||Glucose-6-phosphate dehydrogenase C-terminal|||Glucose-6-phosphate dehydrogenase NAD-binding|||N-acetylalanine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000068086 http://togogenome.org/gene/10090:Nox1 ^@ http://purl.uniprot.org/uniprot/Q8CIZ9 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||FAD-binding FR-type|||Ferric oxidoreductase|||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.|||Interaction with NOXO1|||N-linked (GlcNAc...) asparagine|||NADPH oxidase 1|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000322982|||http://purl.uniprot.org/annotation/VSP_038574|||http://purl.uniprot.org/annotation/VSP_038575 http://togogenome.org/gene/10090:Rsbn1l ^@ http://purl.uniprot.org/uniprot/D3Z0K6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or2t1 ^@ http://purl.uniprot.org/uniprot/E9Q3K2|||http://purl.uniprot.org/uniprot/Q62342 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Domain Extent|||Non-terminal Residue|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Elmo2 ^@ http://purl.uniprot.org/uniprot/Q8BHL5 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ ELMO|||Engulfment and cell motility protein 2|||In isoform 2 and isoform 3.|||In isoform 3.|||PH|||Phosphoserine|||Phosphotyrosine|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000153715|||http://purl.uniprot.org/annotation/VSP_007488|||http://purl.uniprot.org/annotation/VSP_007489 http://togogenome.org/gene/10090:Inhba ^@ http://purl.uniprot.org/uniprot/Q04998|||http://purl.uniprot.org/uniprot/Q3UY39 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Inhibin beta A chain|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033710|||http://purl.uniprot.org/annotation/PRO_0000033711|||http://purl.uniprot.org/annotation/PRO_5014309177 http://togogenome.org/gene/10090:Lrrc43 ^@ http://purl.uniprot.org/uniprot/A0A0G2JGK7|||http://purl.uniprot.org/uniprot/Q3V0L5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Leucine-rich repeat-containing protein 43 ^@ http://purl.uniprot.org/annotation/PRO_0000311910|||http://purl.uniprot.org/annotation/VSP_029638 http://togogenome.org/gene/10090:Brat1 ^@ http://purl.uniprot.org/uniprot/Q8C3R1 ^@ 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 ^@ BRCA1-associated ATM activator 1|||HEAT 1|||HEAT 2|||In isoform 2.|||Phosphoserine|||Required for interaction with NDFIP1 ^@ http://purl.uniprot.org/annotation/PRO_0000395837|||http://purl.uniprot.org/annotation/VSP_039548|||http://purl.uniprot.org/annotation/VSP_039549 http://togogenome.org/gene/10090:Ooep ^@ http://purl.uniprot.org/uniprot/Q9CWE6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ KH; atypical|||Oocyte-expressed protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000328803 http://togogenome.org/gene/10090:Acot13 ^@ http://purl.uniprot.org/uniprot/Q4VA32|||http://purl.uniprot.org/uniprot/Q9CQR4 ^@ 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 ^@ Acyl-coenzyme A thioesterase 13|||N-acetylmethionine|||N6-acetyllysine|||Thioesterase ^@ http://purl.uniprot.org/annotation/PRO_0000156698 http://togogenome.org/gene/10090:Fstl5 ^@ http://purl.uniprot.org/uniprot/Q8BFR2 ^@ 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 ^@ EF-hand 1|||EF-hand 2|||Follistatin-related protein 5|||Ig-like 1|||Ig-like 2|||Kazal-like|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000010119 http://togogenome.org/gene/10090:Ptpn12 ^@ http://purl.uniprot.org/uniprot/P35831 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Interaction with TGFB1I1|||N-acetylmethionine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 12 ^@ http://purl.uniprot.org/annotation/PRO_0000094772 http://togogenome.org/gene/10090:Msh3 ^@ http://purl.uniprot.org/uniprot/A0A087WQ16|||http://purl.uniprot.org/uniprot/E9QPY6|||http://purl.uniprot.org/uniprot/P13705 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||DNA mismatch repair protein Msh3|||DNA mismatch repair proteins mutS family|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000115193 http://togogenome.org/gene/10090:Ranbp10 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0G4|||http://purl.uniprot.org/uniprot/A9UGK3|||http://purl.uniprot.org/uniprot/Q6VN19 ^@ 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 ^@ B30.2/SPRY|||CTLH|||Complete loss RAN-GEF activity. Partial loss of RAN-binding.|||Disordered|||LisH|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Ran-binding protein 10|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000305238 http://togogenome.org/gene/10090:Or2l5 ^@ http://purl.uniprot.org/uniprot/Q8VGJ5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trim21 ^@ http://purl.uniprot.org/uniprot/Q3U7K7|||http://purl.uniprot.org/uniprot/Q3UCL2 ^@ Coiled-Coil|||Domain Extent|||Region ^@ Coiled-Coil|||Domain Extent ^@ B box-type|||B30.2/SPRY|||RING-type ^@ http://togogenome.org/gene/10090:Cd34 ^@ http://purl.uniprot.org/uniprot/Q543B6|||http://purl.uniprot.org/uniprot/Q543Y2|||http://purl.uniprot.org/uniprot/Q64314 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hematopoietic progenitor cell antigen CD34|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000020901|||http://purl.uniprot.org/annotation/PRO_5004249209|||http://purl.uniprot.org/annotation/PRO_5014309605|||http://purl.uniprot.org/annotation/VSP_004161|||http://purl.uniprot.org/annotation/VSP_004162 http://togogenome.org/gene/10090:Psg19 ^@ http://purl.uniprot.org/uniprot/Q4KL31 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Rrp15 ^@ http://purl.uniprot.org/uniprot/Q9CYX7 ^@ 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 ^@ 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_0000273214 http://togogenome.org/gene/10090:Ccdc82 ^@ http://purl.uniprot.org/uniprot/Q6PG04 ^@ 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 82|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000234289 http://togogenome.org/gene/10090:Map2k2 ^@ http://purl.uniprot.org/uniprot/Q63932|||http://purl.uniprot.org/uniprot/Q8CB46|||http://purl.uniprot.org/uniprot/Q91YS7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Cleavage; by anthrax lethal factor|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 2|||Inactivation.|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by RAF|||Phosphothreonine|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086373 http://togogenome.org/gene/10090:Rph3al ^@ http://purl.uniprot.org/uniprot/Q768S4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger ^@ Disordered|||FYVE-type|||In isoform 2.|||Loss of binding to RAB27A, remaining cytoplasmic.|||Phosphoserine|||Polar residues|||Rab effector Noc2|||RabBD ^@ http://purl.uniprot.org/annotation/PRO_0000278264|||http://purl.uniprot.org/annotation/VSP_023245|||http://purl.uniprot.org/annotation/VSP_023246 http://togogenome.org/gene/10090:Wdr1 ^@ http://purl.uniprot.org/uniprot/O88342|||http://purl.uniprot.org/uniprot/Q3TJY2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ 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_0000051342 http://togogenome.org/gene/10090:Iqsec3 ^@ http://purl.uniprot.org/uniprot/Q3TES0 ^@ 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 ^@ Disordered|||IQ|||IQ motif and SEC7 domain-containing protein 3|||PH|||Phosphoserine|||Polar residues|||Pro residues|||SEC7 ^@ http://purl.uniprot.org/annotation/PRO_0000245611 http://togogenome.org/gene/10090:Trim42 ^@ http://purl.uniprot.org/uniprot/Q9D2H5 ^@ 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 1|||B box-type 2|||COS|||Fibronectin type-III|||RING-type|||Tripartite motif-containing protein 42 ^@ http://purl.uniprot.org/annotation/PRO_0000056264 http://togogenome.org/gene/10090:Ccl21a ^@ http://purl.uniprot.org/uniprot/P84444 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Region|||Signal Peptide ^@ C-C motif chemokine 21a|||C-terminal basic extension|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000005223 http://togogenome.org/gene/10090:Snf8 ^@ http://purl.uniprot.org/uniprot/Q9CZ28 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue ^@ Omega-N-methylarginine|||Vacuolar-sorting protein SNF8 ^@ http://purl.uniprot.org/annotation/PRO_0000215210 http://togogenome.org/gene/10090:Tac4 ^@ http://purl.uniprot.org/uniprot/Q99N14 ^@ Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Disordered|||Hemokinin|||Methionine amide ^@ http://purl.uniprot.org/annotation/PRO_0000320014|||http://purl.uniprot.org/annotation/PRO_0000320015|||http://purl.uniprot.org/annotation/PRO_0000320016 http://togogenome.org/gene/10090:Ado ^@ http://purl.uniprot.org/uniprot/Q6PDY2 ^@ Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand ^@ Binding Site|||Chain|||Helix|||Mutagenesis Site|||Strand ^@ 2-aminoethanethiol dioxygenase|||Loss of enzyme activity and iron incorporation. ^@ http://purl.uniprot.org/annotation/PRO_0000089785 http://togogenome.org/gene/10090:Tspan31 ^@ http://purl.uniprot.org/uniprot/Q9CQ88 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-31 ^@ http://purl.uniprot.org/annotation/PRO_0000219271 http://togogenome.org/gene/10090:Plppr3 ^@ http://purl.uniprot.org/uniprot/A0A0R3P9D0|||http://purl.uniprot.org/uniprot/E9QAX3|||http://purl.uniprot.org/uniprot/Q7TPB0 ^@ 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 ^@ Acidic residues|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphatidic acid phosphatase type 2/haloperoxidase|||Phospholipid phosphatase-related protein type 3|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000317530|||http://purl.uniprot.org/annotation/VSP_031007|||http://purl.uniprot.org/annotation/VSP_031008 http://togogenome.org/gene/10090:Plxna4 ^@ http://purl.uniprot.org/uniprot/Q80UG2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||PSI 1|||PSI 2|||PSI 3|||Plexin-A4|||Sema ^@ http://purl.uniprot.org/annotation/PRO_0000240284 http://togogenome.org/gene/10090:Hspb3 ^@ http://purl.uniprot.org/uniprot/Q9QZ57 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||Heat shock protein beta-3|||sHSP ^@ http://purl.uniprot.org/annotation/PRO_0000125937 http://togogenome.org/gene/10090:Nek8 ^@ http://purl.uniprot.org/uniprot/Q91ZR4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant ^@ Disordered|||In ARJPKD.|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||Results in enlarged multinucleated cells.|||Serine/threonine-protein kinase Nek8|||Shows a defect in ciliary localization with no apparent effect on ciliation, mitosis or centriole number. ^@ http://purl.uniprot.org/annotation/PRO_0000086433 http://togogenome.org/gene/10090:Mrpl54 ^@ http://purl.uniprot.org/uniprot/Q9CPW3 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Large ribosomal subunit protein mL54|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000278281 http://togogenome.org/gene/10090:Or52i2 ^@ http://purl.uniprot.org/uniprot/E9Q549 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:H60c ^@ http://purl.uniprot.org/uniprot/B1B213 ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide ^@ Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide ^@ GPI-anchor amidated serine|||Histocompatibility antigen 60c|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000436149|||http://purl.uniprot.org/annotation/PRO_5006716406 http://togogenome.org/gene/10090:Ecpas ^@ http://purl.uniprot.org/uniprot/Q6PDI5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||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 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proteasome adapter and scaffold protein ECM29 ^@ http://purl.uniprot.org/annotation/PRO_0000212560|||http://purl.uniprot.org/annotation/VSP_013178 http://togogenome.org/gene/10090:Pdyn ^@ http://purl.uniprot.org/uniprot/O35852|||http://purl.uniprot.org/uniprot/Q3UZW2 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Signal Peptide ^@ Chain|||Non-terminal Residue|||Signal Peptide ^@ Proenkephalin-B ^@ http://purl.uniprot.org/annotation/PRO_5004230427|||http://purl.uniprot.org/annotation/PRO_5015096768 http://togogenome.org/gene/10090:Or6c76b ^@ http://purl.uniprot.org/uniprot/Q7TRH5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nes ^@ http://purl.uniprot.org/uniprot/Q6P5H2 ^@ 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 ^@ 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-acetylmethionine|||Nestin|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000285856|||http://purl.uniprot.org/annotation/VSP_024923 http://togogenome.org/gene/10090:Or1j10 ^@ http://purl.uniprot.org/uniprot/Q8VGK6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Iws1 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLV0|||http://purl.uniprot.org/uniprot/Q8C1D8 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Integrase domain-binding motif (IBM)|||Interaction with SUPT6H and ALYREF|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein IWS1 homolog|||TFIIS N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000083347|||http://purl.uniprot.org/annotation/VSP_016994|||http://purl.uniprot.org/annotation/VSP_016995 http://togogenome.org/gene/10090:2310079G19Rik ^@ http://purl.uniprot.org/uniprot/Q9D6L6 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Vmn1r192 ^@ http://purl.uniprot.org/uniprot/Q8K4C9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Xlr ^@ http://purl.uniprot.org/uniprot/P05531|||http://purl.uniprot.org/uniprot/Q544L6|||http://purl.uniprot.org/uniprot/Q8BS74 ^@ 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|||X-linked lymphocyte-regulated protein PM1|||XLR/SYCP3/FAM9 ^@ http://purl.uniprot.org/annotation/PRO_0000223040 http://togogenome.org/gene/10090:Cfap107 ^@ http://purl.uniprot.org/uniprot/Q4KKZ1 ^@ Chain|||Molecule Processing ^@ Chain ^@ Cilia- and flagella-associated protein 107 ^@ http://purl.uniprot.org/annotation/PRO_0000247261 http://togogenome.org/gene/10090:Lipg ^@ http://purl.uniprot.org/uniprot/C0LQ91|||http://purl.uniprot.org/uniprot/Q3U5K0|||http://purl.uniprot.org/uniprot/Q3U713|||http://purl.uniprot.org/uniprot/Q3U807|||http://purl.uniprot.org/uniprot/Q3UDI6|||http://purl.uniprot.org/uniprot/Q9WVG5 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide ^@ Charge relay system|||Endothelial lipase|||Lipase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PLAT|||Phospholipase A1|||phospholipase A1 ^@ http://purl.uniprot.org/annotation/PRO_0000017798|||http://purl.uniprot.org/annotation/PRO_5011946466|||http://purl.uniprot.org/annotation/PRO_5012474983|||http://purl.uniprot.org/annotation/PRO_5012655429|||http://purl.uniprot.org/annotation/PRO_5015087647 http://togogenome.org/gene/10090:Zfy1 ^@ http://purl.uniprot.org/uniprot/P10925 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||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|||Disordered|||Nuclear localization signal|||Polar residues|||Zinc finger Y-chromosomal protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000047263 http://togogenome.org/gene/10090:Cdkn2aip ^@ http://purl.uniprot.org/uniprot/Q8BI72 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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_0000324340 http://togogenome.org/gene/10090:Mr1 ^@ http://purl.uniprot.org/uniprot/Q8HWB0 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Activated.|||Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C1-type|||Impair expression of folded protein.|||In isoform 2.|||Loss of MAIT cell activation.|||Major histocompatibility complex class I-related gene protein|||N-linked (GlcNAc...) asparagine|||No effect on cell surface expression.|||Reduced MAIT cell activation.|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000344442|||http://purl.uniprot.org/annotation/VSP_034759 http://togogenome.org/gene/10090:Cfap68 ^@ http://purl.uniprot.org/uniprot/Q9D131 ^@ 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 68|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000089830|||http://purl.uniprot.org/annotation/VSP_027584 http://togogenome.org/gene/10090:Copg1 ^@ http://purl.uniprot.org/uniprot/Q7TNQ1|||http://purl.uniprot.org/uniprot/Q9QZE5 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Clathrin/coatomer adaptor adaptin-like N-terminal|||Coatomer subunit gamma-1|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||Interaction with ZNF289/ARFGAP2|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000304939 http://togogenome.org/gene/10090:Trim66 ^@ http://purl.uniprot.org/uniprot/E9PZP2|||http://purl.uniprot.org/uniprot/Q3UH62|||http://purl.uniprot.org/uniprot/Q924W6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ B box-type|||B box-type 1; atypical|||B box-type 2|||Basic and acidic residues|||Bromo|||Disordered|||Drastic decrease of CBX5, CBX1 and CBX3 binding; When associated with A-991.|||Drastic decrease of CBX5, CBX1 and CBX3 binding; When associated with A-993.|||In isoform 2 and isoform 3.|||In isoform 2.|||PHD-type|||Polar residues|||Pro residues|||PxVxL motif|||RING-type|||Tripartite motif-containing protein 66 ^@ http://purl.uniprot.org/annotation/PRO_0000220376|||http://purl.uniprot.org/annotation/VSP_061682|||http://purl.uniprot.org/annotation/VSP_061683|||http://purl.uniprot.org/annotation/VSP_061684 http://togogenome.org/gene/10090:Scaper ^@ http://purl.uniprot.org/uniprot/F8VQ70 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||U1-type ^@ http://togogenome.org/gene/10090:Nrxn2 ^@ http://purl.uniprot.org/uniprot/A0A494B8Y4|||http://purl.uniprot.org/uniprot/E9PUM9|||http://purl.uniprot.org/uniprot/E9Q5N7 ^@ 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|||EGF-like|||Helical|||Laminin G|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003244243|||http://purl.uniprot.org/annotation/PRO_5019745799|||http://purl.uniprot.org/annotation/PRO_5040054245 http://togogenome.org/gene/10090:Nars2 ^@ http://purl.uniprot.org/uniprot/Q8BGV0|||http://purl.uniprot.org/uniprot/Q8BXJ6 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Aminoacyl-transfer RNA synthetases class-II family profile|||Mitochondrion|||N6-acetyllysine|||Probable asparagine--tRNA ligase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000250723 http://togogenome.org/gene/10090:Pi16 ^@ http://purl.uniprot.org/uniprot/Q9ET66 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase inhibitor 16|||Polar residues|||SCP ^@ http://purl.uniprot.org/annotation/PRO_0000287634|||http://purl.uniprot.org/annotation/VSP_025575 http://togogenome.org/gene/10090:Vmn2r47 ^@ http://purl.uniprot.org/uniprot/K7N709 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5030173240 http://togogenome.org/gene/10090:Cox6b2 ^@ http://purl.uniprot.org/uniprot/Q059Q8|||http://purl.uniprot.org/uniprot/Q80ZN9|||http://purl.uniprot.org/uniprot/S4R2Q6|||http://purl.uniprot.org/uniprot/V9GXN3 ^@ 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_0000194922 http://togogenome.org/gene/10090:Ctr9 ^@ http://purl.uniprot.org/uniprot/Q05CJ7|||http://purl.uniprot.org/uniprot/Q62018 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA polymerase-associated protein CTR9 homolog|||TPR|||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_0000231589|||http://purl.uniprot.org/annotation/VSP_017846|||http://purl.uniprot.org/annotation/VSP_017847|||http://purl.uniprot.org/annotation/VSP_017848|||http://purl.uniprot.org/annotation/VSP_017849 http://togogenome.org/gene/10090:Slfn8 ^@ http://purl.uniprot.org/uniprot/B1ARD8|||http://purl.uniprot.org/uniprot/E9Q0R4 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ N'-domain region|||Schlafen AlbA-2|||Schlafen family member 8 ^@ http://purl.uniprot.org/annotation/PRO_0000444607 http://togogenome.org/gene/10090:Acsl4 ^@ http://purl.uniprot.org/uniprot/Q8BW44|||http://purl.uniprot.org/uniprot/Q91YN3|||http://purl.uniprot.org/uniprot/Q9QUJ7 ^@ 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 ^@ AMP-dependent synthetase/ligase|||Cytoplasmic|||Helical; Signal-anchor for type III membrane protein|||In isoform Short.|||Long-chain-fatty-acid--CoA ligase 4|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000193110|||http://purl.uniprot.org/annotation/VSP_000239 http://togogenome.org/gene/10090:Zfp623 ^@ http://purl.uniprot.org/uniprot/Q9CY99 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered ^@ http://togogenome.org/gene/10090:Kynu ^@ http://purl.uniprot.org/uniprot/A2ARD6|||http://purl.uniprot.org/uniprot/Q6NSV5|||http://purl.uniprot.org/uniprot/Q9CXF0 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Aminotransferase class V|||Kynureninase|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine ^@ http://purl.uniprot.org/annotation/PRO_0000218658 http://togogenome.org/gene/10090:Gemin8 ^@ http://purl.uniprot.org/uniprot/B1AVP5|||http://purl.uniprot.org/uniprot/Q8BHE1 ^@ 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|||Gem-associated protein 8|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000087156 http://togogenome.org/gene/10090:Pcdhb1 ^@ http://purl.uniprot.org/uniprot/Q91Y08 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_5015099505 http://togogenome.org/gene/10090:Smc2 ^@ http://purl.uniprot.org/uniprot/Q3ULS2|||http://purl.uniprot.org/uniprot/Q8CG48 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn ^@ N6-acetyllysine|||SMC hinge|||Structural maintenance of chromosomes protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000118996 http://togogenome.org/gene/10090:Smu1 ^@ http://purl.uniprot.org/uniprot/Q3UKJ7 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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|||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_0000237591|||http://purl.uniprot.org/annotation/PRO_0000424521|||http://purl.uniprot.org/annotation/VSP_018593 http://togogenome.org/gene/10090:Pla2g1b ^@ http://purl.uniprot.org/uniprot/Q9Z0Y2 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Phospholipase A2 ^@ http://purl.uniprot.org/annotation/PRO_0000022741|||http://purl.uniprot.org/annotation/PRO_0000022742 http://togogenome.org/gene/10090:Psrc1 ^@ http://purl.uniprot.org/uniprot/Q9D0P7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||4|||5|||5 X 4 AA repeats of P-X-X-P|||Disordered|||Phosphoserine|||Polar residues|||Proline/serine-rich coiled-coil protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000273729 http://togogenome.org/gene/10090:Or4n5 ^@ http://purl.uniprot.org/uniprot/Q8VFC8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tfb1m ^@ http://purl.uniprot.org/uniprot/Q8JZM0 ^@ Binding Site|||Chain|||Helix|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn ^@ Binding Site|||Chain|||Helix|||Strand|||Transit Peptide|||Turn ^@ Dimethyladenosine transferase 1, mitochondrial|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000273173 http://togogenome.org/gene/10090:Ppp1r42 ^@ http://purl.uniprot.org/uniprot/Q8R1Z4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||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_0000326177|||http://purl.uniprot.org/annotation/VSP_032589|||http://purl.uniprot.org/annotation/VSP_032590|||http://purl.uniprot.org/annotation/VSP_032591 http://togogenome.org/gene/10090:Efna3 ^@ http://purl.uniprot.org/uniprot/O08545 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Ephrin RBD|||Ephrin-A3|||GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000008371|||http://purl.uniprot.org/annotation/PRO_0000008372 http://togogenome.org/gene/10090:Eef1e1 ^@ http://purl.uniprot.org/uniprot/Q9D1M4 ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ C-terminal|||Eukaryotic translation elongation factor 1 epsilon-1|||GST C-terminal|||Linker|||N-acetylalanine|||N-terminal|||N6-acetyllysine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000221133 http://togogenome.org/gene/10090:Tbata ^@ http://purl.uniprot.org/uniprot/Q7TSD4|||http://purl.uniprot.org/uniprot/Q91YF1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2, isoform 3, isoform 5 and isoform 7.|||In isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 3, isoform 4, isoform 6, isoform 7 and isoform 8.|||In isoform 3.|||In isoform 4.|||In isoform 8.|||Polar residues|||Protein TBATA ^@ http://purl.uniprot.org/annotation/PRO_0000351147|||http://purl.uniprot.org/annotation/VSP_052935|||http://purl.uniprot.org/annotation/VSP_052936|||http://purl.uniprot.org/annotation/VSP_052937|||http://purl.uniprot.org/annotation/VSP_052938|||http://purl.uniprot.org/annotation/VSP_052939|||http://purl.uniprot.org/annotation/VSP_052940|||http://purl.uniprot.org/annotation/VSP_052941|||http://purl.uniprot.org/annotation/VSP_052942 http://togogenome.org/gene/10090:Atg4a ^@ http://purl.uniprot.org/uniprot/Q5EBK1|||http://purl.uniprot.org/uniprot/Q8C9S8 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict ^@ Cysteine protease ATG4A|||LIR|||Nucleophile|||Peptidase C54 catalytic ^@ http://purl.uniprot.org/annotation/PRO_0000215839 http://togogenome.org/gene/10090:Rab3a ^@ http://purl.uniprot.org/uniprot/P63011|||http://purl.uniprot.org/uniprot/Q0PD63 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region ^@ Cysteine methyl ester|||Disordered|||Effector region|||No effect on neurite transport. Reduced axonal transport in a Madd RNAi-mediated knockdown or a Kif1b knockout background.|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-3A|||Reduced axon localization and aggregation in neuronal cell bodies.|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121078 http://togogenome.org/gene/10090:Stat6 ^@ http://purl.uniprot.org/uniprot/P52633 ^@ 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 ^@ Disordered|||LXXLL motif|||N-acetylserine|||Phosphotyrosine; by JAK|||Polar residues|||Removed|||SH2|||Signal transducer and transcription activator 6 ^@ http://purl.uniprot.org/annotation/PRO_0000182434 http://togogenome.org/gene/10090:Noc3l ^@ http://purl.uniprot.org/uniprot/Q8VI84 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nucleolar complex protein 3 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000173475 http://togogenome.org/gene/10090:Spsb4 ^@ http://purl.uniprot.org/uniprot/Q8R5B6 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Splice Variant ^@ B30.2/SPRY|||In isoform 2.|||SOCS box|||SPRY domain-containing SOCS box protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000238478|||http://purl.uniprot.org/annotation/VSP_018614 http://togogenome.org/gene/10090:Ddx6 ^@ http://purl.uniprot.org/uniprot/P54823 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ DEAD box|||Disordered|||Gyf binding|||Helicase ATP-binding|||Helicase C-terminal|||Phosphothreonine|||Polar residues|||Probable ATP-dependent RNA helicase DDX6|||Q motif|||RecA-like domain 2 ^@ http://purl.uniprot.org/annotation/PRO_0000054984 http://togogenome.org/gene/10090:Fmnl2 ^@ http://purl.uniprot.org/uniprot/A2APV2|||http://purl.uniprot.org/uniprot/A2AQW2|||http://purl.uniprot.org/uniprot/F8VPR2|||http://purl.uniprot.org/uniprot/Q8BI52 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||DAD|||Disordered|||FH2|||Formin-like protein 2|||GBD/FH3|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||Phosphoserine|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000289094|||http://purl.uniprot.org/annotation/VSP_025888|||http://purl.uniprot.org/annotation/VSP_025889|||http://purl.uniprot.org/annotation/VSP_025890|||http://purl.uniprot.org/annotation/VSP_025891 http://togogenome.org/gene/10090:Kxd1 ^@ http://purl.uniprot.org/uniprot/Q80XH1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||KxDL motif-containing protein 1|||N-acetylmethionine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295260 http://togogenome.org/gene/10090:Myl3 ^@ http://purl.uniprot.org/uniprot/P09542 ^@ 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 ^@ Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Myosin light chain 3|||N,N,N-trimethylalanine; by NTM1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000198697 http://togogenome.org/gene/10090:Nup107 ^@ http://purl.uniprot.org/uniprot/Q8BH74 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Asymmetric dimethylarginine; alternate|||N-acetylmethionine|||Nuclear pore complex protein Nup107|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000204832 http://togogenome.org/gene/10090:Yipf3 ^@ http://purl.uniprot.org/uniprot/Q3UDR8 ^@ 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|||Helical|||Lumenal|||N-acetylalanine; in Protein YIPF3, N-terminally processed|||N-linked (GlcNAc...) asparagine|||Protein YIPF3|||Protein YIPF3, N-terminally processed|||Removed; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000244447|||http://purl.uniprot.org/annotation/PRO_0000424523 http://togogenome.org/gene/10090:Spink2 ^@ http://purl.uniprot.org/uniprot/D3YTY0|||http://purl.uniprot.org/uniprot/Q8BMY7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Site|||Splice Variant ^@ In isoform 2.|||Kazal-like|||Reactive bond|||Serine protease inhibitor Kazal-type 2 ^@ http://purl.uniprot.org/annotation/PRO_0000016563|||http://purl.uniprot.org/annotation/PRO_5003052332|||http://purl.uniprot.org/annotation/VSP_060766 http://togogenome.org/gene/10090:Pla2g6 ^@ http://purl.uniprot.org/uniprot/P97819|||http://purl.uniprot.org/uniprot/Q3U613|||http://purl.uniprot.org/uniprot/Q3UN31 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Splice Variant|||Transmembrane ^@ 85/88 kDa calcium-independent phospholipase A2|||ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 9|||Calmodulin-binding (1-9-14 motif)|||Calmodulin-binding (IQ motif)|||DGA/G|||GXGXXG|||GXSXG|||Helical|||In isoform Short.|||Nucleophile|||PNPLA|||Phosphoserine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000067038|||http://purl.uniprot.org/annotation/VSP_044364 http://togogenome.org/gene/10090:Podxl ^@ http://purl.uniprot.org/uniprot/Q791G4|||http://purl.uniprot.org/uniprot/Q9R0M4 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Podocalyxin ^@ http://purl.uniprot.org/annotation/PRO_0000024755|||http://purl.uniprot.org/annotation/PRO_5014310811 http://togogenome.org/gene/10090:Uba2 ^@ http://purl.uniprot.org/uniprot/Q9Z1F9 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||SUMO-activating enzyme subunit 2 ^@ http://purl.uniprot.org/annotation/PRO_0000194969 http://togogenome.org/gene/10090:Celsr2 ^@ http://purl.uniprot.org/uniprot/Q9R0M0 ^@ 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 ^@ (3R)-3-hydroxyasparagine|||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 2|||Cytoplasmic|||Disordered|||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|||EGF-like 7; 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.|||Laminin EGF-like|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000012917|||http://purl.uniprot.org/annotation/VSP_025765 http://togogenome.org/gene/10090:Aldh16a1 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSU0|||http://purl.uniprot.org/uniprot/Q571I9 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ Aldehyde dehydrogenase|||Aldehyde dehydrogenase family 16 member A1 ^@ http://purl.uniprot.org/annotation/PRO_0000312987 http://togogenome.org/gene/10090:Or13a24 ^@ http://purl.uniprot.org/uniprot/Q7TRT5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp189 ^@ http://purl.uniprot.org/uniprot/Q8BKP2|||http://purl.uniprot.org/uniprot/Q8BKW8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Grcc10 ^@ http://purl.uniprot.org/uniprot/O35127 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||Protein C10|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000065035 http://togogenome.org/gene/10090:Crtap ^@ http://purl.uniprot.org/uniprot/Q9CYD3 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Cartilage-associated protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000006320 http://togogenome.org/gene/10090:Bex3 ^@ http://purl.uniprot.org/uniprot/Q9WTZ9 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolished zinc-binding and association with FEM1B.|||Abolishes localization with replicating mitochondria.|||Abolishes nuclear export and interactions with itself and p75NTR/NGFR; when associated with A-94 and A-97.|||Abolishes nuclear export and interactions with itself and p75NTR/NGFR; when associated with A-97 and A-99.|||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_0000229781|||http://purl.uniprot.org/annotation/VSP_017744 http://togogenome.org/gene/10090:Thumpd3 ^@ http://purl.uniprot.org/uniprot/P97770 ^@ 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.|||THUMP|||tRNA (guanine(6)-N2)-methyltransferase THUMP3 ^@ http://purl.uniprot.org/annotation/PRO_0000259770|||http://purl.uniprot.org/annotation/VSP_021537|||http://purl.uniprot.org/annotation/VSP_021538 http://togogenome.org/gene/10090:Ctu1 ^@ http://purl.uniprot.org/uniprot/Q99J10 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Cytoplasmic tRNA 2-thiolation protein 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000282392 http://togogenome.org/gene/10090:Pygo1 ^@ http://purl.uniprot.org/uniprot/Q1JPR5|||http://purl.uniprot.org/uniprot/Q9D0P5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Strand|||Turn|||Zinc Finger ^@ Disordered|||Interaction with BCL9|||Interaction with H3K4me2|||Nuclear localization signal|||PHD-type|||Polar residues|||Pygopus homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000097122 http://togogenome.org/gene/10090:Cyb561a3 ^@ http://purl.uniprot.org/uniprot/Q6P1H1 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytochrome b561|||Cytoplasmic|||Decreased transmembrane ascorbate ferrireductase activity.|||Decreased transmembrane ascorbate ferrireductase activity. Approximately 45% reduction in enzyme activity.|||Decreased transmembrane ascorbate ferrireductase activity. Approximately 50% reduction in enzyme activity.|||Decreased transmembrane ascorbate ferrireductase activity. Approximately 55% reduction in enzyme activity.|||Decreased transmembrane ascorbate ferrireductase activity. Approximately 75% reduction in enzyme activity.|||Decreased transmembrane ascorbate ferrireductase activity. Approximately 80% reduction in enzyme activity.|||Helical|||In isoform 2.|||In isoform 3.|||Loss of transmembrane ascorbate ferrireductase activity.|||Lumenal|||Lysosomal membrane ascorbate-dependent ferrireductase CYB561A3|||No effect on transmembrane ascorbate ferrireductase activity.|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000314839|||http://purl.uniprot.org/annotation/VSP_030398|||http://purl.uniprot.org/annotation/VSP_030399 http://togogenome.org/gene/10090:Akr1cl ^@ http://purl.uniprot.org/uniprot/G3XA14|||http://purl.uniprot.org/uniprot/Q3UXL1|||http://purl.uniprot.org/uniprot/Q9D5U2 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Site ^@ Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor ^@ http://togogenome.org/gene/10090:Ilvbl ^@ http://purl.uniprot.org/uniprot/Q8BU33 ^@ Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Modified Residue|||Region|||Splice Variant|||Transmembrane ^@ 2-hydroxyacyl-CoA lyase 2|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Thiamine pyrophosphate binding ^@ http://purl.uniprot.org/annotation/PRO_0000314826|||http://purl.uniprot.org/annotation/VSP_030392|||http://purl.uniprot.org/annotation/VSP_030393|||http://purl.uniprot.org/annotation/VSP_030394|||http://purl.uniprot.org/annotation/VSP_030395 http://togogenome.org/gene/10090:Lrfn1 ^@ http://purl.uniprot.org/uniprot/Q2WF71 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Decreased promotion of neurite outgrowth. No effect on homomeric interactions.|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Ig-like|||In isoform 2.|||In isoform 3.|||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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000334146|||http://purl.uniprot.org/annotation/VSP_033617|||http://purl.uniprot.org/annotation/VSP_033618|||http://purl.uniprot.org/annotation/VSP_033619 http://togogenome.org/gene/10090:Tk1 ^@ http://purl.uniprot.org/uniprot/P04184 ^@ 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-acetylserine|||Phosphoserine|||Proton acceptor|||Removed|||Thymidine kinase, cytosolic ^@ http://purl.uniprot.org/annotation/PRO_0000174949|||http://purl.uniprot.org/annotation/VSP_061491 http://togogenome.org/gene/10090:Rgs6 ^@ http://purl.uniprot.org/uniprot/A0A087WNZ9|||http://purl.uniprot.org/uniprot/Q3UTM5|||http://purl.uniprot.org/uniprot/Q9Z2H2 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ DEP|||G protein gamma|||RGS|||Regulator of G-protein signaling 6 ^@ http://purl.uniprot.org/annotation/PRO_0000204193 http://togogenome.org/gene/10090:Clu ^@ http://purl.uniprot.org/uniprot/Q06890|||http://purl.uniprot.org/uniprot/Q549A5 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide ^@ Abolishes interaction with XRCC6.|||Clusterin|||Clusterin C-terminal|||Clusterin N-terminal|||Clusterin alpha chain|||Clusterin beta chain|||Interchain (between beta and alpha chains)|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||Phosphoserine|||Reduced nuclear location.|||Strongly reduced interaction with XRCC6.|||Strongly reduced nuclear location. ^@ http://purl.uniprot.org/annotation/PRO_0000005535|||http://purl.uniprot.org/annotation/PRO_0000005536|||http://purl.uniprot.org/annotation/PRO_0000005537|||http://purl.uniprot.org/annotation/PRO_5014212507 http://togogenome.org/gene/10090:Alkbh1 ^@ http://purl.uniprot.org/uniprot/P0CB42 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Fe2OG dioxygenase|||Interaction with DNAJB6|||Loss of activity.|||Nucleic acid dioxygenase ALKBH1|||tRNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000386453 http://togogenome.org/gene/10090:Osbpl10 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0F9|||http://purl.uniprot.org/uniprot/S4R1M9|||http://purl.uniprot.org/uniprot/S4R296 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Acidic residues|||Disordered|||Omega-N-methylarginine|||Oxysterol-binding protein-related protein 10|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000434122 http://togogenome.org/gene/10090:Ghrl ^@ http://purl.uniprot.org/uniprot/A2RSS9|||http://purl.uniprot.org/uniprot/Q7TSD1|||http://purl.uniprot.org/uniprot/Q811T4|||http://purl.uniprot.org/uniprot/Q9EQX0 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Mass|||Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Strand ^@ Appetite-regulating hormone|||Basic and acidic residues|||Disordered|||Ghrelin|||Ghrelin, O-octanoylated form.|||In isoform 2.|||Leucine amide|||Motilin/ghrelin|||Motilin/ghrelin-associated peptide|||O-decanoyl serine; alternate|||O-hexanoyl serine; alternate|||O-octanoyl serine; alternate|||Obestatin|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000019205|||http://purl.uniprot.org/annotation/PRO_0000019206|||http://purl.uniprot.org/annotation/PRO_0000045142|||http://purl.uniprot.org/annotation/PRO_0000045143|||http://purl.uniprot.org/annotation/PRO_5014296833|||http://purl.uniprot.org/annotation/PRO_5015098868|||http://purl.uniprot.org/annotation/PRO_5015098954|||http://purl.uniprot.org/annotation/VSP_003246 http://togogenome.org/gene/10090:Ubb ^@ http://purl.uniprot.org/uniprot/P0CG49|||http://purl.uniprot.org/uniprot/Q78XY9 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Propeptide|||Sequence Conflict|||Site ^@ ADP-ribosylglycine|||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|||Phosphoserine|||Phosphoserine; by PINK1|||Ubiquitin|||Ubiquitin-like|||Ubiquitin-like 1|||Ubiquitin-like 2|||Ubiquitin-like 3|||Ubiquitin-like 4 ^@ http://purl.uniprot.org/annotation/PRO_0000114801|||http://purl.uniprot.org/annotation/PRO_0000396188|||http://purl.uniprot.org/annotation/PRO_0000396189|||http://purl.uniprot.org/annotation/PRO_0000396190|||http://purl.uniprot.org/annotation/PRO_0000396191 http://togogenome.org/gene/10090:Sez6l ^@ http://purl.uniprot.org/uniprot/A0A0G2JG23|||http://purl.uniprot.org/uniprot/A0A0R4J0Y4|||http://purl.uniprot.org/uniprot/Q6P1D5 ^@ 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 ^@ CUB|||CUB 1|||CUB 2|||CUB 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Seizure 6-like protein|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5 ^@ http://purl.uniprot.org/annotation/PRO_0000333886|||http://purl.uniprot.org/annotation/PRO_5002546567|||http://purl.uniprot.org/annotation/PRO_5015044293|||http://purl.uniprot.org/annotation/VSP_033594 http://togogenome.org/gene/10090:Slc1a1 ^@ http://purl.uniprot.org/uniprot/P51906 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000202066 http://togogenome.org/gene/10090:Sorcs3 ^@ http://purl.uniprot.org/uniprot/Q1HL22|||http://purl.uniprot.org/uniprot/Q8VI51 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||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_0000033175|||http://purl.uniprot.org/annotation/PRO_5009970135 http://togogenome.org/gene/10090:Hsd3b6 ^@ http://purl.uniprot.org/uniprot/O35469|||http://purl.uniprot.org/uniprot/Q7TPU0 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6|||3-beta hydroxysteroid dehydrogenase/isomerase|||Helical|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000087785 http://togogenome.org/gene/10090:Becn1 ^@ http://purl.uniprot.org/uniprot/O88597 ^@ Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ BH3|||Beclin-1|||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-94.|||Disordered|||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|||Partial loss of phosphorylation. Complete loss of phosphorylation and defective autophagic function; when associated with Ala-91.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine; by DAPK1|||Required for membrane-association ^@ http://purl.uniprot.org/annotation/PRO_0000218556|||http://purl.uniprot.org/annotation/PRO_0000435038|||http://purl.uniprot.org/annotation/PRO_0000435039 http://togogenome.org/gene/10090:B3galt6 ^@ http://purl.uniprot.org/uniprot/Q91Z92 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Beta-1,3-galactosyltransferase 6|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000219169 http://togogenome.org/gene/10090:Gm6619 ^@ http://purl.uniprot.org/uniprot/F6URP1 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5005912884 http://togogenome.org/gene/10090:Pabpc6 ^@ http://purl.uniprot.org/uniprot/Q9D4E6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||PABC|||RRM ^@ http://togogenome.org/gene/10090:Rad23a ^@ http://purl.uniprot.org/uniprot/P54726|||http://purl.uniprot.org/uniprot/Q3TN85|||http://purl.uniprot.org/uniprot/Q8CAP3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Polar residues|||Pro residues|||UBA|||UBA 1|||UBA 2|||UV excision repair protein RAD23 homolog A|||Ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000114905 http://togogenome.org/gene/10090:Mrgprf ^@ http://purl.uniprot.org/uniprot/Q3TZA7|||http://purl.uniprot.org/uniprot/Q8VCJ6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||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|||Mas-related G-protein coupled receptor member F|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069765 http://togogenome.org/gene/10090:Utp20 ^@ http://purl.uniprot.org/uniprot/E9QK83 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||U3 small nucleolar RNA-associated protein 20 C-terminal|||U3 small nucleolar RNA-associated protein 20 N-terminal ^@ http://togogenome.org/gene/10090:1810030O07Rik ^@ http://purl.uniprot.org/uniprot/A2BDN9|||http://purl.uniprot.org/uniprot/Q8C5K5 ^@ 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.|||Omega-N-methylarginine|||Phosphothreonine|||Uncharacterized protein CXorf38 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000079733|||http://purl.uniprot.org/annotation/VSP_014623 http://togogenome.org/gene/10090:Tmem119 ^@ http://purl.uniprot.org/uniprot/Q8R138 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Loss of glycosylation. No effect on osteoblast mineralization. Loss of glycosylation; when associated with A-43; A-54; A-60 and A-67.|||No loss of glycosylation. Loss of glycosylation; when associated with A-36; A-43; A-54 and A-60.|||No loss of glycosylation. Loss of glycosylation; when associated with A-36; A-43; A-54 and A-67.|||No loss of glycosylation. Loss of glycosylation; when associated with A-36; A-43; A-60 and A-67.|||No loss of glycosylation. Loss of glycosylation; when associated with A-36; A-54; A-60 and A-67.|||O-linked (GalNAc...) serine|||Phosphoserine|||Polar residues|||Pro residues|||Transmembrane protein 119 ^@ http://purl.uniprot.org/annotation/PRO_0000251221 http://togogenome.org/gene/10090:Zfp46 ^@ http://purl.uniprot.org/uniprot/Q8BPP0 ^@ 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 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)|||KRAB|||Zinc finger protein 436 ^@ http://purl.uniprot.org/annotation/PRO_0000047585 http://togogenome.org/gene/10090:Defb26 ^@ http://purl.uniprot.org/uniprot/Q30KN7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Beta-defensin|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015097371 http://togogenome.org/gene/10090:Eeig1 ^@ http://purl.uniprot.org/uniprot/A0A158RFU0|||http://purl.uniprot.org/uniprot/Q78T81 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2 NT-type|||Disordered|||Early estrogen-induced gene 1 protein|||Polar residues|||Required for interaction with TNFRSF11A/RANK ^@ http://purl.uniprot.org/annotation/PRO_0000261635 http://togogenome.org/gene/10090:Stxbp2 ^@ http://purl.uniprot.org/uniprot/Q64324 ^@ Chain|||Molecule Processing ^@ Chain ^@ Syntaxin-binding protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000206282 http://togogenome.org/gene/10090:Arfgap1 ^@ http://purl.uniprot.org/uniprot/Q3TGS9|||http://purl.uniprot.org/uniprot/Q6PB94|||http://purl.uniprot.org/uniprot/Q9EPJ9|||http://purl.uniprot.org/uniprot/V9GXM1 ^@ 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 ^@ ADP-ribosylation factor GTPase-activating protein 1|||Arf-GAP|||C4-type|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000074191|||http://purl.uniprot.org/annotation/VSP_011303 http://togogenome.org/gene/10090:Ppp1r16b ^@ http://purl.uniprot.org/uniprot/Q544H9|||http://purl.uniprot.org/uniprot/Q8VHQ3 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Repeat ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||Phosphoserine|||Protein phosphatase 1 regulatory inhibitor subunit 16B|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000067044|||http://purl.uniprot.org/annotation/PRO_0000396711|||http://purl.uniprot.org/annotation/PRO_5036526222 http://togogenome.org/gene/10090:Lcn9 ^@ http://purl.uniprot.org/uniprot/Q9D267 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ Epididymal-specific lipocalin-9|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017919 http://togogenome.org/gene/10090:Rpl27a ^@ http://purl.uniprot.org/uniprot/P14115 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ (3S)-3-hydroxyhistidine|||Basic residues|||Disordered|||Large ribosomal subunit protein uL15|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000104880 http://togogenome.org/gene/10090:Or6ae1 ^@ http://purl.uniprot.org/uniprot/Q8VGL1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dmwd ^@ http://purl.uniprot.org/uniprot/Q08274|||http://purl.uniprot.org/uniprot/Q5HZG7 ^@ 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_0000050957 http://togogenome.org/gene/10090:Errfi1 ^@ http://purl.uniprot.org/uniprot/Q3TK48|||http://purl.uniprot.org/uniprot/Q99JZ7 ^@ 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 ^@ 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_0000096488 http://togogenome.org/gene/10090:Cacnb2 ^@ http://purl.uniprot.org/uniprot/C7IVS7|||http://purl.uniprot.org/uniprot/Q32MF3|||http://purl.uniprot.org/uniprot/Q8CC27 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces binding to RRAD.|||Required for CaMK2D-binding|||SH3|||Voltage-dependent L-type calcium channel subunit beta-2 ^@ http://purl.uniprot.org/annotation/PRO_0000144052|||http://purl.uniprot.org/annotation/VSP_010730|||http://purl.uniprot.org/annotation/VSP_010731|||http://purl.uniprot.org/annotation/VSP_010732 http://togogenome.org/gene/10090:Or2f2 ^@ http://purl.uniprot.org/uniprot/Q7TRV8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Camkk2 ^@ http://purl.uniprot.org/uniprot/Q8C078 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ Autoinhibitory domain|||Basic and acidic residues|||Calcium/calmodulin-dependent protein kinase kinase 2|||Calmodulin-binding|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||RP domain|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000086145|||http://purl.uniprot.org/annotation/VSP_012150|||http://purl.uniprot.org/annotation/VSP_012151|||http://purl.uniprot.org/annotation/VSP_012152|||http://purl.uniprot.org/annotation/VSP_012153|||http://purl.uniprot.org/annotation/VSP_012154|||http://purl.uniprot.org/annotation/VSP_012155|||http://purl.uniprot.org/annotation/VSP_012156 http://togogenome.org/gene/10090:Lrpap1 ^@ http://purl.uniprot.org/uniprot/P55302|||http://purl.uniprot.org/uniprot/Q52KI7 ^@ Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Signal Peptide ^@ Alpha-2-macroglobulin RAP C-terminal|||Alpha-2-macroglobulin receptor-associated protein|||LDL receptor binding|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000020725|||http://purl.uniprot.org/annotation/PRO_5014309490 http://togogenome.org/gene/10090:Dohh ^@ http://purl.uniprot.org/uniprot/Q99LN9 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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 isoform 2.|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000248576|||http://purl.uniprot.org/annotation/VSP_020315|||http://purl.uniprot.org/annotation/VSP_020316 http://togogenome.org/gene/10090:Eif4ebp2 ^@ http://purl.uniprot.org/uniprot/P70445 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Modified Residue|||Motif|||Mutagenesis Site ^@ Abolishes deamidation and impaired interaction with RPTOR.|||Abolishes interaction with RPTOR.|||Deamidated asparagine|||Does not greatlay affect hyperphosphorylation.|||Eukaryotic translation initiation factor 4E-binding protein 2|||Impaired hyperphosphorylation.|||Increased interaction with RPTOR.|||Phosphoserine|||Phosphoserine; by MTOR|||Phosphothreonine; by MTOR|||TOS motif|||YXXXXLphi motif ^@ http://purl.uniprot.org/annotation/PRO_0000190517 http://togogenome.org/gene/10090:Atp6v1g1 ^@ http://purl.uniprot.org/uniprot/Q5HZY7|||http://purl.uniprot.org/uniprot/Q9CR51 ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||Removed|||V-type proton ATPase subunit G 1 ^@ http://purl.uniprot.org/annotation/PRO_0000192898 http://togogenome.org/gene/10090:Mucl2 ^@ http://purl.uniprot.org/uniprot/P02815 ^@ 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|||Mucin-like protein 2|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5004324585 http://togogenome.org/gene/10090:Cldn34c4 ^@ http://purl.uniprot.org/uniprot/A2ANA3 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Vinac1 ^@ http://purl.uniprot.org/uniprot/A2AP89 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Stx1b ^@ http://purl.uniprot.org/uniprot/P61264 ^@ 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|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||Phosphoserine|||Syntaxin-1B|||t-SNARE coiled-coil homology ^@ http://purl.uniprot.org/annotation/PRO_0000210193 http://togogenome.org/gene/10090:Sprn ^@ http://purl.uniprot.org/uniprot/Q8BWU1 ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||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_0000320167|||http://purl.uniprot.org/annotation/PRO_0000320168 http://togogenome.org/gene/10090:Aco1 ^@ http://purl.uniprot.org/uniprot/P28271 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Cytoplasmic aconitate hydratase ^@ http://purl.uniprot.org/annotation/PRO_0000076681 http://togogenome.org/gene/10090:Sh2b3 ^@ http://purl.uniprot.org/uniprot/D3Z3Y5|||http://purl.uniprot.org/uniprot/O09039 ^@ 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 ^@ Disordered|||PH|||Phosphoserine|||Polar residues|||SH2|||SH2B adapter protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000084455 http://togogenome.org/gene/10090:Senp1 ^@ http://purl.uniprot.org/uniprot/M0QWX4|||http://purl.uniprot.org/uniprot/P59110 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Disordered|||Interaction with CCAR2|||Nuclear export signal|||Nuclear localization signal|||Nucleophile|||Phosphoserine|||Polar residues|||Protease|||Sentrin-specific protease 1|||Ubiquitin-like protease family profile ^@ http://purl.uniprot.org/annotation/PRO_0000101717 http://togogenome.org/gene/10090:Gprasp1 ^@ http://purl.uniprot.org/uniprot/Q5U4C1|||http://purl.uniprot.org/uniprot/Q6PD32 ^@ 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|||G-protein coupled receptor-associated sorting protein 1|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000239051|||http://purl.uniprot.org/annotation/VSP_019080 http://togogenome.org/gene/10090:Iqcb1 ^@ http://purl.uniprot.org/uniprot/Q8BP00 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ calmodulin-binding motif-containing protein 1|||In isoform 2.|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000084226|||http://purl.uniprot.org/annotation/VSP_010246 http://togogenome.org/gene/10090:Dmac1 ^@ http://purl.uniprot.org/uniprot/Q9CQ00 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Distal membrane-arm assembly complex protein 1|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089730 http://togogenome.org/gene/10090:Dcaf15 ^@ http://purl.uniprot.org/uniprot/Q6PFH3 ^@ 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 ^@ DDB1- and CUL4-associated factor 15|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000314486|||http://purl.uniprot.org/annotation/VSP_030290 http://togogenome.org/gene/10090:Zfand1 ^@ http://purl.uniprot.org/uniprot/D3Z7G5|||http://purl.uniprot.org/uniprot/Q8BFR6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ AN1-type|||AN1-type 1|||AN1-type 2|||AN1-type zinc finger protein 1|||Disordered|||ubiquitin-like ^@ http://purl.uniprot.org/annotation/PRO_0000066581 http://togogenome.org/gene/10090:Emp2 ^@ http://purl.uniprot.org/uniprot/O88662|||http://purl.uniprot.org/uniprot/Q548I4|||http://purl.uniprot.org/uniprot/Q8BPC2 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Glycosylation Site|||Transmembrane ^@ Epithelial membrane protein 2|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000164659 http://togogenome.org/gene/10090:Wnt8b ^@ http://purl.uniprot.org/uniprot/Q3TER4|||http://purl.uniprot.org/uniprot/Q8BQD1|||http://purl.uniprot.org/uniprot/Q9WUD6 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Non-terminal Residue|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Non-terminal Residue|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine|||Protein Wnt|||Protein Wnt-8b ^@ http://purl.uniprot.org/annotation/PRO_0000041451|||http://purl.uniprot.org/annotation/PRO_5015099062 http://togogenome.org/gene/10090:Kctd5 ^@ http://purl.uniprot.org/uniprot/A0A0R4J000|||http://purl.uniprot.org/uniprot/Q8VC57 ^@ 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 ^@ BTB|||BTB/POZ domain-containing protein KCTD5|||Disordered|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000191292 http://togogenome.org/gene/10090:Defb12 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0S5|||http://purl.uniprot.org/uniprot/Q8K4N3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ Beta-defensin|||Beta-defensin 12 ^@ http://purl.uniprot.org/annotation/PRO_0000006940 http://togogenome.org/gene/10090:Fank1 ^@ http://purl.uniprot.org/uniprot/Q9DAM9 ^@ 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 ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Fibronectin type 3 and ankyrin repeat domains 1 protein|||Fibronectin type-III ^@ http://purl.uniprot.org/annotation/PRO_0000066991 http://togogenome.org/gene/10090:Ppp4r3b ^@ http://purl.uniprot.org/uniprot/Q922R5 ^@ 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.|||Phosphoserine|||Polar residues|||Serine/threonine-protein phosphatase 4 regulatory subunit 3B|||WH1 ^@ http://purl.uniprot.org/annotation/PRO_0000254604|||http://purl.uniprot.org/annotation/VSP_021264|||http://purl.uniprot.org/annotation/VSP_021265 http://togogenome.org/gene/10090:Mettl15 ^@ http://purl.uniprot.org/uniprot/Q9DCL4 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ 12S rRNA N4-methylcytidine methyltransferase|||Mitochondrion|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000308333 http://togogenome.org/gene/10090:Or6c68 ^@ http://purl.uniprot.org/uniprot/Q8VEU0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:3110082I17Rik ^@ http://purl.uniprot.org/uniprot/Q9CXL3 ^@ 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|||Uncharacterized protein C7orf50 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000309511 http://togogenome.org/gene/10090:Entpd5 ^@ http://purl.uniprot.org/uniprot/Q3TQC7|||http://purl.uniprot.org/uniprot/Q9WUZ9 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Ectonucleoside triphosphate diphosphohydrolase 5|||Helical|||Loss of nucleoside-diphosphatase activity.|||N-linked (GlcNAc...) asparagine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000019910 http://togogenome.org/gene/10090:Nkx3-2 ^@ http://purl.uniprot.org/uniprot/P97503 ^@ 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-3.2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048948 http://togogenome.org/gene/10090:Tmem176b ^@ http://purl.uniprot.org/uniprot/Q9R1Q6 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Transmembrane protein 176B ^@ http://purl.uniprot.org/annotation/PRO_0000279876 http://togogenome.org/gene/10090:Btbd7 ^@ http://purl.uniprot.org/uniprot/Q8CFE5 ^@ 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 ^@ BACK|||BTB 1|||BTB 2|||BTB/POZ domain-containing protein 7|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000186216|||http://purl.uniprot.org/annotation/VSP_013828|||http://purl.uniprot.org/annotation/VSP_013829|||http://purl.uniprot.org/annotation/VSP_013830|||http://purl.uniprot.org/annotation/VSP_013831 http://togogenome.org/gene/10090:Paxbp1 ^@ http://purl.uniprot.org/uniprot/P58501 ^@ 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 SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Necessary and sufficient for interaction with PAX7|||PAX3- and PAX7-binding protein 1|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000087440|||http://purl.uniprot.org/annotation/VSP_004268|||http://purl.uniprot.org/annotation/VSP_004269 http://togogenome.org/gene/10090:Alg5 ^@ http://purl.uniprot.org/uniprot/Q9DB25 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dolichyl-phosphate beta-glucosyltransferase|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000059099 http://togogenome.org/gene/10090:Pdia3 ^@ http://purl.uniprot.org/uniprot/P27773 ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Basic and acidic residues|||Contributes to redox potential value|||Disordered|||Interchain (with 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|||Nucleophile|||Phosphothreonine|||Prevents secretion from ER|||Protein disulfide-isomerase A3|||Redox-active|||Redox-active; reversible|||Thioredoxin 1|||Thioredoxin 2 ^@ http://purl.uniprot.org/annotation/PRO_0000034226 http://togogenome.org/gene/10090:Lin54 ^@ http://purl.uniprot.org/uniprot/Q571G4 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Site|||Splice Variant ^@ CRC|||Critical for interaction with target DNA|||DNA-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with DNA|||Linker|||N6-acetyllysine|||Phosphoserine|||Protein lin-54 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000341390|||http://purl.uniprot.org/annotation/VSP_034277|||http://purl.uniprot.org/annotation/VSP_034278|||http://purl.uniprot.org/annotation/VSP_034279 http://togogenome.org/gene/10090:Sprr2f ^@ http://purl.uniprot.org/uniprot/O70557 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1|||2|||3|||3 X 9 AA approximate tandem repeats|||Disordered|||Small proline-rich protein 2F ^@ http://purl.uniprot.org/annotation/PRO_0000150018 http://togogenome.org/gene/10090:Cpne5 ^@ http://purl.uniprot.org/uniprot/Q8JZW4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ C2 1|||C2 2|||Copine-5|||Disordered|||Phosphoserine|||Pro residues|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000144844 http://togogenome.org/gene/10090:Or14c44 ^@ http://purl.uniprot.org/uniprot/Q7TS04 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Stard7 ^@ http://purl.uniprot.org/uniprot/Q8R1R3 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Site|||Transit Peptide ^@ Cleavage; by PARL|||Disordered|||Mitochondrion|||START|||StAR-related lipid transfer protein 7, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000220675 http://togogenome.org/gene/10090:Ube2z ^@ http://purl.uniprot.org/uniprot/Q3UE37 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl thioester intermediate|||Phosphoserine|||UBC core|||Ubiquitin-conjugating enzyme E2 Z ^@ http://purl.uniprot.org/annotation/PRO_0000280516 http://togogenome.org/gene/10090:Ttll3 ^@ http://purl.uniprot.org/uniprot/A4Q9E5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Essential for specifying initiation versus elongation step of the polyglycylase activity|||In isoform 2.|||In isoform 3.|||Loss of tubulin monoglycylation activity.|||Polar residues|||TTL|||Tubulin monoglycylase TTLL3 ^@ http://purl.uniprot.org/annotation/PRO_0000326159|||http://purl.uniprot.org/annotation/VSP_052722|||http://purl.uniprot.org/annotation/VSP_052723|||http://purl.uniprot.org/annotation/VSP_052724|||http://purl.uniprot.org/annotation/VSP_052725|||http://purl.uniprot.org/annotation/VSP_052726 http://togogenome.org/gene/10090:Morn3 ^@ http://purl.uniprot.org/uniprot/Q8C5T4 ^@ 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_0000247461|||http://purl.uniprot.org/annotation/VSP_019998|||http://purl.uniprot.org/annotation/VSP_019999 http://togogenome.org/gene/10090:Btg2 ^@ http://purl.uniprot.org/uniprot/Q04211|||http://purl.uniprot.org/uniprot/Q3TF68 ^@ Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Strand|||Turn ^@ Anti-proliferative protein|||Phosphoserine; by MAPK1 and MAPK3|||Phosphoserine; by MAPK14|||Protein BTG2 ^@ http://purl.uniprot.org/annotation/PRO_0000143805 http://togogenome.org/gene/10090:Skap1 ^@ http://purl.uniprot.org/uniprot/B2RWZ1|||http://purl.uniprot.org/uniprot/Q3UUV5|||http://purl.uniprot.org/uniprot/Q3V3I1 ^@ 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 ^@ Acidic residues|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||Interaction with FYB1|||PH|||Phosphotyrosine|||Phosphotyrosine; by FYN|||SH3|||Src kinase-associated phosphoprotein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000270174|||http://purl.uniprot.org/annotation/VSP_022180|||http://purl.uniprot.org/annotation/VSP_022181|||http://purl.uniprot.org/annotation/VSP_022182|||http://purl.uniprot.org/annotation/VSP_022183 http://togogenome.org/gene/10090:Syt9 ^@ http://purl.uniprot.org/uniprot/Q9R0N9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ C2 1|||C2 2|||Cysteine motif|||Cytoplasmic|||Disordered|||Helical|||Phosphoserine|||Polar residues|||Synaptotagmin-9|||Vesicular ^@ http://purl.uniprot.org/annotation/PRO_0000183963 http://togogenome.org/gene/10090:Fbxo32 ^@ http://purl.uniprot.org/uniprot/Q9CPU7 ^@ Chain|||Domain Extent|||Molecule Processing|||Motif|||Region ^@ Chain|||Domain Extent|||Motif ^@ Bipartite nuclear localization signal|||F-box|||F-box only protein 32|||Nuclear export signal|||Nuclear localization signal ^@ http://purl.uniprot.org/annotation/PRO_0000119923 http://togogenome.org/gene/10090:Golga7 ^@ http://purl.uniprot.org/uniprot/Q91W53 ^@ Chain|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Lipid Binding|||Splice Variant ^@ Golgin subfamily A member 7|||In isoform 2.|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000213978|||http://purl.uniprot.org/annotation/VSP_016281 http://togogenome.org/gene/10090:Prl2b1 ^@ http://purl.uniprot.org/uniprot/B9EHM9|||http://purl.uniprot.org/uniprot/Q9DAZ2 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Prolactin-2B1 ^@ http://purl.uniprot.org/annotation/PRO_0000045169|||http://purl.uniprot.org/annotation/PRO_5015087497 http://togogenome.org/gene/10090:Orc2 ^@ http://purl.uniprot.org/uniprot/Q543F8|||http://purl.uniprot.org/uniprot/Q59IX1|||http://purl.uniprot.org/uniprot/Q60862 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Involved in LRWD1-binding|||Origin recognition complex subunit 2|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000127076 http://togogenome.org/gene/10090:Dlc1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J171|||http://purl.uniprot.org/uniprot/D5M8I5|||http://purl.uniprot.org/uniprot/E9PXD2|||http://purl.uniprot.org/uniprot/E9QKB1|||http://purl.uniprot.org/uniprot/Q9R0Z9 ^@ 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|||Focal adhesion-targeting (FAT)|||In isoform 2.|||Phosphoserine|||Polar residues|||Polybasic cluster (PBR)|||Rho GTPase-activating protein 7|||Rho-GAP|||SAM|||START ^@ http://purl.uniprot.org/annotation/PRO_0000056708|||http://purl.uniprot.org/annotation/VSP_026144 http://togogenome.org/gene/10090:Gna11 ^@ http://purl.uniprot.org/uniprot/P21278 ^@ 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 ^@ G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein subunit alpha-11|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000203747 http://togogenome.org/gene/10090:Kdm5a ^@ http://purl.uniprot.org/uniprot/Q3UXZ9 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ ARID|||C5HC2|||Disordered|||GSGFP motif|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with LMO2|||JmjC|||JmjN|||Lysine-specific demethylase 5A|||PHD-type 1|||PHD-type 2|||PHD-type 3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000292411 http://togogenome.org/gene/10090:Btbd35f19 ^@ http://purl.uniprot.org/uniprot/A2CG71 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BTB ^@ http://togogenome.org/gene/10090:P3h2 ^@ http://purl.uniprot.org/uniprot/Q8CG71 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Disordered|||Fe2OG dioxygenase|||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_0000240357 http://togogenome.org/gene/10090:Mak16 ^@ http://purl.uniprot.org/uniprot/Q8BGS0 ^@ 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 SUMO2)|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Protein MAK16 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000203795|||http://purl.uniprot.org/annotation/VSP_014840 http://togogenome.org/gene/10090:Frem2 ^@ http://purl.uniprot.org/uniprot/Q6NVD0 ^@ Chain|||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|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||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 isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000010125|||http://purl.uniprot.org/annotation/VSP_015037|||http://purl.uniprot.org/annotation/VSP_015038|||http://purl.uniprot.org/annotation/VSP_015039 http://togogenome.org/gene/10090:Spaca5 ^@ http://purl.uniprot.org/uniprot/A0A077S1H9|||http://purl.uniprot.org/uniprot/A2AE20 ^@ 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|||Sperm acrosome-associated protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000284471|||http://purl.uniprot.org/annotation/PRO_5015028437 http://togogenome.org/gene/10090:Il18r1 ^@ http://purl.uniprot.org/uniprot/Q61098|||http://purl.uniprot.org/uniprot/Q8C257 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like|||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_0000015449|||http://purl.uniprot.org/annotation/PRO_5015099083 http://togogenome.org/gene/10090:Polr1h ^@ http://purl.uniprot.org/uniprot/Q791N7 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Zinc Finger ^@ C4-type|||DNA-directed RNA polymerase I subunit RPA12|||TFIIS-type ^@ http://purl.uniprot.org/annotation/PRO_0000121462 http://togogenome.org/gene/10090:Pskh1 ^@ http://purl.uniprot.org/uniprot/Q91YA2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||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_0000086168 http://togogenome.org/gene/10090:Or5d46 ^@ http://purl.uniprot.org/uniprot/Q8VG40 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r113 ^@ http://purl.uniprot.org/uniprot/E9PZA6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003243038 http://togogenome.org/gene/10090:Col26a1 ^@ http://purl.uniprot.org/uniprot/Q91VF6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||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_0000007826|||http://purl.uniprot.org/annotation/VSP_008448 http://togogenome.org/gene/10090:Asb17 ^@ http://purl.uniprot.org/uniprot/Q8VHP9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ ANK|||Ankyrin repeat and SOCS box protein 17|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066961 http://togogenome.org/gene/10090:Fam169b ^@ http://purl.uniprot.org/uniprot/Q8CHT6 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM169B ^@ http://purl.uniprot.org/annotation/PRO_0000342880 http://togogenome.org/gene/10090:Fgd3 ^@ http://purl.uniprot.org/uniprot/Q3TNB8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||DH|||Disordered|||FYVE-type|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Mcm8 ^@ http://purl.uniprot.org/uniprot/Q9CWV1 ^@ 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 ^@ DNA helicase MCM8|||In isoform 2.|||MCM|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000194126|||http://purl.uniprot.org/annotation/VSP_015786 http://togogenome.org/gene/10090:Ccdc106 ^@ http://purl.uniprot.org/uniprot/E9QPN6|||http://purl.uniprot.org/uniprot/Q3ULM0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Basic residues|||Bipartite nuclear localization signal|||Coiled-coil domain-containing protein 106|||Disordered|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000274344|||http://purl.uniprot.org/annotation/VSP_022717|||http://purl.uniprot.org/annotation/VSP_022718 http://togogenome.org/gene/10090:Mmp3 ^@ http://purl.uniprot.org/uniprot/P28862|||http://purl.uniprot.org/uniprot/Q3UFJ0|||http://purl.uniprot.org/uniprot/Q922W6 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Propeptide|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Activation peptide|||Cysteine switch|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Peptidase metallopeptidase|||Peptidase metallopeptidase domain-containing protein|||Phosphotyrosine; by PKDCC|||Stromelysin-1|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000028730|||http://purl.uniprot.org/annotation/PRO_0000028731|||http://purl.uniprot.org/annotation/PRO_5004230117|||http://purl.uniprot.org/annotation/PRO_5015020136 http://togogenome.org/gene/10090:Mymk ^@ http://purl.uniprot.org/uniprot/E9QA72|||http://purl.uniprot.org/uniprot/Q9D1N4 ^@ Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Lipid Binding|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Abolished localization to the Golgi apparatus.|||Cytoplasmic|||Does not affect subcellular localization.|||Extracellular|||Helical|||Protein myomaker|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000319063 http://togogenome.org/gene/10090:4930474N05Rik ^@ http://purl.uniprot.org/uniprot/Q8BVR5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||N-terminal Ras-GEF ^@ http://togogenome.org/gene/10090:Cage1 ^@ http://purl.uniprot.org/uniprot/Q5IR70 ^@ 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|||Cancer-associated gene 1 protein homolog|||Disordered|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000280752|||http://purl.uniprot.org/annotation/VSP_023906|||http://purl.uniprot.org/annotation/VSP_023907|||http://purl.uniprot.org/annotation/VSP_023908 http://togogenome.org/gene/10090:Zfp784 ^@ http://purl.uniprot.org/uniprot/B2RVK6|||http://purl.uniprot.org/uniprot/Q8BI69 ^@ 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 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger protein 784 ^@ http://purl.uniprot.org/annotation/PRO_0000270997 http://togogenome.org/gene/10090:Tmem225 ^@ http://purl.uniprot.org/uniprot/Q9D9S2 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Motif|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Abolishes interaction with PPP1CC.|||Cytoplasmic|||Extracellular|||Helical|||RVxF|||Transmembrane protein 225 ^@ http://purl.uniprot.org/annotation/PRO_0000339351 http://togogenome.org/gene/10090:Rd3l ^@ http://purl.uniprot.org/uniprot/B2RV38 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Ndufa12 ^@ http://purl.uniprot.org/uniprot/Q7TMF3 ^@ Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn ^@ Chain|||Helix|||Modified Residue|||Strand|||Turn ^@ N-acetylmethionine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 ^@ http://purl.uniprot.org/annotation/PRO_0000118846 http://togogenome.org/gene/10090:Vmn1r71 ^@ http://purl.uniprot.org/uniprot/Q8VIC0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Taf1 ^@ http://purl.uniprot.org/uniprot/B1Q2W7|||http://purl.uniprot.org/uniprot/Q80UV9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Basic and acidic residues|||Bromo|||Bromo 1|||Bromo 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HMG box|||Histone acetyltransferase (HAT)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ASF1A and ASF1B|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by autocatalysis|||Polar residues|||Protein kinase 1|||Protein kinase 2|||Transcription initiation factor TFIID subunit 1 ^@ http://purl.uniprot.org/annotation/PRO_0000278524|||http://purl.uniprot.org/annotation/VSP_023320|||http://purl.uniprot.org/annotation/VSP_023321|||http://purl.uniprot.org/annotation/VSP_062001 http://togogenome.org/gene/10090:Ndufb4 ^@ http://purl.uniprot.org/uniprot/Q9CQC7 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane|||Turn ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Transmembrane|||Turn ^@ Helical|||N-acetylserine|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000118801 http://togogenome.org/gene/10090:Usp11 ^@ http://purl.uniprot.org/uniprot/Q3TFK2|||http://purl.uniprot.org/uniprot/Q8BX45|||http://purl.uniprot.org/uniprot/Q8C0C2|||http://purl.uniprot.org/uniprot/Q99K46 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Acidic residues|||DUSP|||Disordered|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 11 ^@ http://purl.uniprot.org/annotation/PRO_0000080633 http://togogenome.org/gene/10090:Chrm2 ^@ http://purl.uniprot.org/uniprot/Q9ERZ4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||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|||Important for signaling|||Muscarinic acetylcholine receptor M2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000069022 http://togogenome.org/gene/10090:Slc25a4 ^@ http://purl.uniprot.org/uniprot/P48962 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ADP/ATP translocase 1|||Abolished ADP:ATP antiporter activity without affecting ability to regulate mitophagy; when associated with E-244.|||Abolished ADP:ATP antiporter activity without affecting ability to regulate mitophagy; when associated with E-43.|||Abolished ability to regulate mitophagy.|||Abolished interaction with TIMM4, thereby abolishing ability to regulate mitophagy.|||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-acetylglycine|||N6,N6,N6-trimethyllysine|||N6-succinyllysine|||Nucleotide carrier signature motif|||Phosphoserine|||Removed|||S-nitrosocysteine|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090575 http://togogenome.org/gene/10090:Apcs ^@ http://purl.uniprot.org/uniprot/P12246|||http://purl.uniprot.org/uniprot/Q4JFI8 ^@ 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|||Pentraxin (PTX)|||Pentraxin family member|||Serum amyloid P-component ^@ http://purl.uniprot.org/annotation/PRO_0000023542|||http://purl.uniprot.org/annotation/PRO_5014205851 http://togogenome.org/gene/10090:Hmg20b ^@ http://purl.uniprot.org/uniprot/Q3U1L0|||http://purl.uniprot.org/uniprot/Q3U1Z7|||http://purl.uniprot.org/uniprot/Q9Z104 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HMG box|||Phosphoserine|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related ^@ http://purl.uniprot.org/annotation/PRO_0000048576 http://togogenome.org/gene/10090:1700065D16Rik ^@ http://purl.uniprot.org/uniprot/Q8BR99 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Kcng1 ^@ http://purl.uniprot.org/uniprot/A2BDX4|||http://purl.uniprot.org/uniprot/B2RVK9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Motif|||Region|||Topological Domain|||Transmembrane ^@ Acidic residues|||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|||Potassium voltage-gated channel subfamily G member 1|||Selectivity filter ^@ http://purl.uniprot.org/annotation/PRO_0000320106 http://togogenome.org/gene/10090:Fhl3 ^@ http://purl.uniprot.org/uniprot/Q9R059 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Zinc Finger ^@ C4-type|||Four and a half LIM domains protein 3|||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_0000075741 http://togogenome.org/gene/10090:Tpst1 ^@ http://purl.uniprot.org/uniprot/O70281 ^@ 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|||Region|||Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Interaction with peptide substrate|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein-tyrosine sulfotransferase 1|||Proton donor/acceptor|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000189827 http://togogenome.org/gene/10090:Slc12a3 ^@ http://purl.uniprot.org/uniprot/P59158|||http://purl.uniprot.org/uniprot/Q543E4 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Amino acid permease N-terminal|||Amino acid permease/ SLC12A|||Cytoplasmic|||Discontinuously helical|||Does not affect protein processing and glycosylation.|||Does not affect protein processing and glycosylation. Decreases localization at the plasma membrane and affinity for sodium and chloride ions.|||Does not affect protein processing and glycosylation. Decreases localization at the plasma membrane.|||Extracellular|||Helical|||Impairs protein processing and glycosylation.|||Knockin mice display typical Gitelman syndrome features, characterized by hypokalemia, hypomagnesemia and increased fractional excretion of K(+) and Mg(2+) with a normal blood pressure level; when associated with Q-156.|||Knockin mice display typical Gitelman syndrome features, characterized by hypokalemia, hypomagnesemia and increased fractional excretion of K(+) and Mg(2+) with a normal blood pressure level; when associated with S-210.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Reduced phosphorylation by OXSR1/OSR1 and STK39/SPAK; when associated with A-53 and A-58. No effect on MAPK1/3 (ERK1/2) phosphorylation in response to IL18, with or without IL12. Substantial reduction in MAPK1/3 (ERK1/2) phosphorylation in response to IL18, with or without IL12; when associated with A-53 and A-58.|||Reduced phosphorylation by OXSR1/OSR1 and STK39/SPAK; when associated with A-53 and A-71. No effect on MAPK1/3 (ERK1/2) phosphorylation in response to IL18, with or without IL12. Substantial reduction in MAPK1/3 (ERK1/2) phosphorylation in response to IL18, with or without IL12; when associated with A-53 and A-71.|||Reduced phosphorylation by OXSR1/OSR1 and STK39/SPAK; when associated with A-58 and A-71. Substantial reduction in MAPK1/3 (ERK1/2) phosphorylation in response to IL18, with or without IL12.|||SLC12A transporter C-terminal|||Solute carrier family 12 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000178027 http://togogenome.org/gene/10090:Rnft1 ^@ http://purl.uniprot.org/uniprot/Q9DCN7 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Chain|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNFT1|||Helical|||RING-type|||Required for ubiquitin ligase activity and for protection against ER stress-induced cell death ^@ http://purl.uniprot.org/annotation/PRO_0000320636 http://togogenome.org/gene/10090:Kitl ^@ http://purl.uniprot.org/uniprot/P20826 ^@ 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|||Helical|||In MGFSL-3NEU.|||In isoform 2.|||Kit ligand|||N-linked (GlcNAc...) asparagine|||Polar residues|||Soluble KIT ligand ^@ http://purl.uniprot.org/annotation/PRO_0000031914|||http://purl.uniprot.org/annotation/PRO_0000403392|||http://purl.uniprot.org/annotation/VSP_006023 http://togogenome.org/gene/10090:Rnf24 ^@ http://purl.uniprot.org/uniprot/Q4VA59|||http://purl.uniprot.org/uniprot/Q8BGI1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Transmembrane|||Zinc Finger ^@ Helical|||RING finger protein 24|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056064 http://togogenome.org/gene/10090:Macrod1 ^@ http://purl.uniprot.org/uniprot/Q922B1 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue ^@ ADP-ribose glycohydrolase MACROD1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Macro|||N6-acetyllysine|||N6-succinyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000084486 http://togogenome.org/gene/10090:Or12k8 ^@ http://purl.uniprot.org/uniprot/Q8VF16 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rnf217 ^@ http://purl.uniprot.org/uniprot/D3YYI7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Transmembrane|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNF217|||Helical|||IBR-type|||Loss of SLC40A1 degradation.|||Loss of SLC40A1 degradation; when associated with A-236.|||Loss of SLC40A1 degradation; when associated with A-239.|||Pro residues|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain ^@ http://purl.uniprot.org/annotation/PRO_0000415821 http://togogenome.org/gene/10090:Rps14 ^@ http://purl.uniprot.org/uniprot/P62264 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Modified Residue|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Small ribosomal subunit protein uS11 ^@ http://purl.uniprot.org/annotation/PRO_0000123338 http://togogenome.org/gene/10090:Ap1ar ^@ http://purl.uniprot.org/uniprot/A0A0G2JG85|||http://purl.uniprot.org/uniprot/E9PYF7 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Stambp ^@ http://purl.uniprot.org/uniprot/Q9CQ26 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Site ^@ Indirect zinc-binding|||Interaction with CHMP3|||Interaction with STAM|||JAMM motif|||MPN|||Phosphoserine|||STAM-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000194870 http://togogenome.org/gene/10090:Cog2 ^@ http://purl.uniprot.org/uniprot/Q921L5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Conserved oligomeric Golgi complex subunit 2|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000213496 http://togogenome.org/gene/10090:Prl3c1 ^@ http://purl.uniprot.org/uniprot/Q9QUN5 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prolactin-3C1 ^@ http://purl.uniprot.org/annotation/PRO_0000045276 http://togogenome.org/gene/10090:Slc51b ^@ http://purl.uniprot.org/uniprot/Q80WK2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not inhibit transport activity. Does not inhibit colocalization with SLC51A at the plasma membrane.|||Does not inhibit transport activity. Does not inhibit colocalization with SLC51A at the plasma membrane. Does not decrease glycosylation of SLC51A.|||Extracellular|||Helical|||Inhibits transport activity. Inhibits localization at the plasma membrane and membrane orientation. Decreases glycosylation of SLC51A.|||Inhibits transport activity. Inhibits weakly colocalization with SLC51A at the plasma membrane. Decreases glycosylation of SLC51A.|||Organic solute transporter subunit beta|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000331555 http://togogenome.org/gene/10090:Gm21677 ^@ http://purl.uniprot.org/uniprot/O35698 ^@ 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|||RNA-binding motif protein, Y chromosome, family 1 member A1|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000341540 http://togogenome.org/gene/10090:Or8c20 ^@ http://purl.uniprot.org/uniprot/L7N1Z5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ctnnb1 ^@ http://purl.uniprot.org/uniprot/Q02248 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||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|||Abolished HIPK2-mediated proteasomal degradation.|||Abolishes AMPK-mediated phosphorylation.|||Catenin beta-1|||Disordered|||Interaction with BCL9|||Interaction with SCRIB|||Interaction with VCL|||Loss of interaction with VCL.|||N-acetylalanine|||N6-acetyllysine|||O-linked (GlcNAc) serine; alternate|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by CDK5|||Phosphoserine; by GSK3-beta|||Phosphoserine; by GSK3-beta and HIPK2|||Phosphoserine; by GSK3-beta; alternate|||Phosphothreonine|||Phosphothreonine; by GSK3-beta|||Phosphotyrosine|||Phosphotyrosine; by FYN and PTK6|||Phosphotyrosine; by PTK6|||Polar residues|||Removed|||S-nitrosocysteine ^@ http://purl.uniprot.org/annotation/PRO_0000064272 http://togogenome.org/gene/10090:Traf3ip1 ^@ http://purl.uniprot.org/uniprot/A0A087WQD8|||http://purl.uniprot.org/uniprot/Q149C2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Turn ^@ Abolishes microtubules binding when missing|||Basic and acidic residues|||DISC1-interaction domain|||Decreased interaction with MAP4. No effect on interaction with IFT20.|||Disordered|||Phosphoserine|||Polar residues|||TRAF3-interacting protein 1|||TRAF3-interacting protein 1 C-terminal|||TRAF3-interacting protein 1 N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000299545 http://togogenome.org/gene/10090:Hamp ^@ http://purl.uniprot.org/uniprot/Q9EQ21 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Propeptide|||Signal Peptide ^@ Hepcidin ^@ http://purl.uniprot.org/annotation/PRO_0000013381|||http://purl.uniprot.org/annotation/PRO_0000013382 http://togogenome.org/gene/10090:Nfe2l2 ^@ http://purl.uniprot.org/uniprot/Q60795 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Turn ^@ Abolished interaction with KEAP1.|||Abolished ubiquitination and degradation by the BCR(KEAP1) complex in the cytoplasm.|||Abolished ubiquitination and degradation by the BCR(KEAP1) complex in the cytoplasm; when associated with 19-A--A-23.|||Abolished ubiquitination and degradation by the BCR(KEAP1) complex in the cytoplasm; when associated with A-30.|||Basic motif|||DLG motif|||Disordered|||Does not affect ubiquitination and degradation by the BCR(KEAP1) complex in the cytoplasm.|||ETGE motif|||Leucine-zipper|||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_0000076450 http://togogenome.org/gene/10090:Vmn2r30 ^@ http://purl.uniprot.org/uniprot/K7N5W1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003908924 http://togogenome.org/gene/10090:Bpifc ^@ http://purl.uniprot.org/uniprot/Q3V1D7|||http://purl.uniprot.org/uniprot/Q8C186 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ BPI fold-containing family C protein|||Bactericidal permeability-increasing protein|||Lipid-binding serum glycoprotein C-terminal|||Lipid-binding serum glycoprotein N-terminal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000017167|||http://purl.uniprot.org/annotation/PRO_5015097524 http://togogenome.org/gene/10090:H2-Eb2 ^@ http://purl.uniprot.org/uniprot/Q3UUV9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Ig-like ^@ http://togogenome.org/gene/10090:Dynlt1a ^@ http://purl.uniprot.org/uniprot/P51807 ^@ 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 ^@ Dynein light chain Tctex-type 1|||Interaction with GNB1|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000195153 http://togogenome.org/gene/10090:Pdcd6ip ^@ http://purl.uniprot.org/uniprot/Q80Y09|||http://purl.uniprot.org/uniprot/Q9WU78 ^@ 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 ^@ BRO1|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with CEP55|||Interaction with CHMP4A, CHMP4B and CHMP4C|||Interaction with SDCBP|||Interaction with TSG101|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Programmed cell death 6-interacting protein|||Removed|||Self-association ^@ http://purl.uniprot.org/annotation/PRO_0000218892|||http://purl.uniprot.org/annotation/VSP_007501|||http://purl.uniprot.org/annotation/VSP_007502 http://togogenome.org/gene/10090:Rnf2 ^@ http://purl.uniprot.org/uniprot/Q9CQJ4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||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|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ 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)|||Interaction with HIP2|||Interaction with nucleosomes via an acidic patch on histone H2A and histone H2B|||Loss of ubiquitin ligase activity.|||N-acetylserine|||Phosphoserine|||Polar residues|||RING-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056039 http://togogenome.org/gene/10090:Or13a26 ^@ http://purl.uniprot.org/uniprot/Q8VGM0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Washc1 ^@ http://purl.uniprot.org/uniprot/Q8VDD8 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Polar residues|||Pro residues|||Required for WASH complex assembly|||VCA|||WASH complex subunit 1|||WH2|||WHD1 ^@ http://purl.uniprot.org/annotation/PRO_0000390963 http://togogenome.org/gene/10090:Npm2 ^@ http://purl.uniprot.org/uniprot/Q80W85 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Site ^@ Acidic residues|||Acidic tract A2|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Interaction between pentamers|||Nucleoplasmin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000219488 http://togogenome.org/gene/10090:Zfp90 ^@ http://purl.uniprot.org/uniprot/Q61967 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Region|||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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 90 ^@ http://purl.uniprot.org/annotation/PRO_0000047311 http://togogenome.org/gene/10090:Hmx3 ^@ http://purl.uniprot.org/uniprot/P42581 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes DNA-binding.|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein HMX3|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000048949 http://togogenome.org/gene/10090:Idi2 ^@ http://purl.uniprot.org/uniprot/Q8BFZ6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict ^@ Isopentenyl-diphosphate delta-isomerase 2|||Microbody targeting signal|||Nudix hydrolase ^@ http://purl.uniprot.org/annotation/PRO_0000420867 http://togogenome.org/gene/10090:Ascc2 ^@ http://purl.uniprot.org/uniprot/Q91WR3 ^@ 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 ^@ Activating signal cointegrator 1 complex subunit 2|||Basic and acidic residues|||CUE|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000064690|||http://purl.uniprot.org/annotation/VSP_011012|||http://purl.uniprot.org/annotation/VSP_011013 http://togogenome.org/gene/10090:Ddx59 ^@ http://purl.uniprot.org/uniprot/Q9DBN9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||DEAD box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HIT-type|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Phosphoserine|||Polar residues|||Probable ATP-dependent RNA helicase DDX59|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000282714|||http://purl.uniprot.org/annotation/VSP_026429|||http://purl.uniprot.org/annotation/VSP_026430 http://togogenome.org/gene/10090:Ccdc87 ^@ http://purl.uniprot.org/uniprot/Q8CDL9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Coiled-coil domain-containing protein 87|||Disordered|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000295146 http://togogenome.org/gene/10090:Col11a2 ^@ http://purl.uniprot.org/uniprot/I7HJS8|||http://purl.uniprot.org/uniprot/Q64739 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||C-terminal propeptide|||Collagen alpha-2(XI) 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|||Fibrillar collagen NC1|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3, isoform 5, isoform 6 and isoform 7.|||In isoform 4, isoform 6 and isoform 7.|||Interchain|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nonhelical region|||Pro residues|||Triple-helical region ^@ http://purl.uniprot.org/annotation/PRO_0000005842|||http://purl.uniprot.org/annotation/PRO_0000005843|||http://purl.uniprot.org/annotation/PRO_5003709868|||http://purl.uniprot.org/annotation/VSP_007345|||http://purl.uniprot.org/annotation/VSP_007346|||http://purl.uniprot.org/annotation/VSP_007347 http://togogenome.org/gene/10090:1700001P01Rik ^@ http://purl.uniprot.org/uniprot/Q9DAQ5 ^@ Chain|||Molecule Processing ^@ Chain ^@ Sperm microtubule associated protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000340711 http://togogenome.org/gene/10090:Abl1 ^@ http://purl.uniprot.org/uniprot/P00520|||http://purl.uniprot.org/uniprot/Q3SYK5 ^@ 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|||Site|||Splice Variant|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Basic and acidic residues|||CAP|||DNA-binding|||Disordered|||F-actin-binding|||In isoform II.|||In isoform III.|||In isoform IV.|||Kinase activation loop|||Loss of inhibition by GNF-2.|||Loss of inhibition by imatinib. Loss of inhibition by GNF-2.|||Loss of kinase activity.|||Loss of nuclear export.|||Minimal reduction in ability to autophosphorylate.|||N-myristoyl glycine|||N6-acetyllysine; by EP300|||No effect on basal activity, but abolishes ionizing radiation-induced activation.|||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|||Pro residues|||Protein kinase|||Proton acceptor|||Removed|||SH2|||SH3|||Strongly reduced inhibition by GNF-2.|||Tyrosine-protein kinase ABL1 ^@ http://purl.uniprot.org/annotation/PRO_0000088051|||http://purl.uniprot.org/annotation/VSP_004958|||http://purl.uniprot.org/annotation/VSP_004959|||http://purl.uniprot.org/annotation/VSP_004960 http://togogenome.org/gene/10090:Kmt5c ^@ http://purl.uniprot.org/uniprot/Q6Q783 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Site|||Strand|||Turn ^@ Does not affect affinity for S-adenosyl-L-methionine.|||Does not methylate either an unmodified or monomethylated H4K20 substrate. Methylates a di-methylated H4K20 peptide.|||Histone H4 binding|||Histone H4 binding; via carbonyl oxygen|||Histone-lysine N-methyltransferase KMT5C|||Required for heterochromatin localization|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000281794 http://togogenome.org/gene/10090:Tars2 ^@ http://purl.uniprot.org/uniprot/E9Q7H6|||http://purl.uniprot.org/uniprot/Q3TP97|||http://purl.uniprot.org/uniprot/Q3UQ84|||http://purl.uniprot.org/uniprot/Q922A3 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Aminoacyl-transfer RNA synthetases class-II family profile|||Mitochondrion|||Phosphoserine|||TGS|||Threonine--tRNA ligase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000254587 http://togogenome.org/gene/10090:Rab11fip3 ^@ http://purl.uniprot.org/uniprot/Q8CHD8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ ARF-binding domain (ABD)|||Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||FIP-RBD|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Rab11 family-interacting protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000390970|||http://purl.uniprot.org/annotation/VSP_038667|||http://purl.uniprot.org/annotation/VSP_038668 http://togogenome.org/gene/10090:Ttc27 ^@ http://purl.uniprot.org/uniprot/Q8CD92 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||Tetratricopeptide repeat protein 27 ^@ http://purl.uniprot.org/annotation/PRO_0000295097|||http://purl.uniprot.org/annotation/VSP_026720 http://togogenome.org/gene/10090:Mocs2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J206|||http://purl.uniprot.org/uniprot/E9PVP5|||http://purl.uniprot.org/uniprot/F6ZGI7|||http://purl.uniprot.org/uniprot/Q9Z223 ^@ 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 ^@ 1-thioglycine; alternate|||Disordered|||Glycyl adenylate; alternate|||In isoform 2.|||In isoform 3.|||Molybdopterin synthase catalytic subunit|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000163112|||http://purl.uniprot.org/annotation/VSP_010081|||http://purl.uniprot.org/annotation/VSP_010082|||http://purl.uniprot.org/annotation/VSP_036808 http://togogenome.org/gene/10090:Atox1 ^@ http://purl.uniprot.org/uniprot/O08997 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ Copper transport protein ATOX1|||HMA|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000212538 http://togogenome.org/gene/10090:Cox4i2 ^@ http://purl.uniprot.org/uniprot/Q91W29 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Cytochrome c oxidase subunit 4 isoform 2, mitochondrial|||Disordered|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000006090 http://togogenome.org/gene/10090:Smpdl3b ^@ http://purl.uniprot.org/uniprot/P58242|||http://purl.uniprot.org/uniprot/Q3TLX9 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Turn ^@ Acid sphingomyelinase-like phosphodiesterase|||Acid sphingomyelinase-like phosphodiesterase 3b|||Calcineurin-like phosphoesterase|||Increased phosphodiesterase activity (in vitro).|||N-linked (GlcNAc...) asparagine|||No effect on enzyme activity and innate immune responses.|||Reduced phosphodiesterase activity. Decreases inhibition of innate immune responses.|||Sphingomyelin phosphodiesterase C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000002332|||http://purl.uniprot.org/annotation/PRO_5014212502 http://togogenome.org/gene/10090:Treh ^@ http://purl.uniprot.org/uniprot/E9PYP7|||http://purl.uniprot.org/uniprot/Q9JLT2 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor|||Removed in mature form|||Trehalase ^@ http://purl.uniprot.org/annotation/PRO_0000012053|||http://purl.uniprot.org/annotation/PRO_0000012054|||http://purl.uniprot.org/annotation/PRO_5003244326 http://togogenome.org/gene/10090:Samt1c ^@ http://purl.uniprot.org/uniprot/A2BED8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Rbp3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0H3|||http://purl.uniprot.org/uniprot/P49194 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide ^@ 1|||2|||3|||4|||4 X approximate tandem repeats|||Disordered|||N-linked (GlcNAc...) asparagine|||Retinol-binding protein 3|||Tail specific protease ^@ http://purl.uniprot.org/annotation/PRO_0000021524|||http://purl.uniprot.org/annotation/PRO_5006451955 http://togogenome.org/gene/10090:Fto ^@ http://purl.uniprot.org/uniprot/Q8BGW1 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Alpha-ketoglutarate-dependent dioxygenase FTO|||Alters protein structure and causes an increase in whole body metabolism, leading to a lean phenotype in adult males, but not in females.|||Fe2OG dioxygenase domain|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loop L1; predicted to block binding of double-stranded DNA or RNA|||Loss of enzyme activity.|||N6-acetyllysine|||Reduced enzyme activity.|||Reduces enzyme activity by about 60%. ^@ http://purl.uniprot.org/annotation/PRO_0000286164|||http://purl.uniprot.org/annotation/VSP_025007|||http://purl.uniprot.org/annotation/VSP_025008|||http://purl.uniprot.org/annotation/VSP_025009|||http://purl.uniprot.org/annotation/VSP_025010|||http://purl.uniprot.org/annotation/VSP_025011 http://togogenome.org/gene/10090:Asb12 ^@ http://purl.uniprot.org/uniprot/Q3KNI9|||http://purl.uniprot.org/uniprot/Q9D738 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Repeat ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat and SOCS box protein 12|||SOCS box ^@ http://purl.uniprot.org/annotation/PRO_0000066948 http://togogenome.org/gene/10090:Gm5414 ^@ http://purl.uniprot.org/uniprot/Q6IFZ8 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||IF rod|||Polar residues ^@ http://togogenome.org/gene/10090:Timmdc1 ^@ http://purl.uniprot.org/uniprot/Q8BUY5 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ Complex I assembly factor TIMMDC1, mitochondrial|||Disordered|||Helical|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000252479 http://togogenome.org/gene/10090:Cog8 ^@ http://purl.uniprot.org/uniprot/Q9JJA2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Conserved oligomeric Golgi complex subunit 8|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000213522 http://togogenome.org/gene/10090:Rbm46 ^@ http://purl.uniprot.org/uniprot/P86049|||http://purl.uniprot.org/uniprot/S4R1Y9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Probable RNA-binding protein 46|||RRM|||RRM 1|||RRM 2|||RRM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000355073 http://togogenome.org/gene/10090:Zfp526 ^@ http://purl.uniprot.org/uniprot/Q8BI66 ^@ 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 ^@ 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.|||Polar residues|||Pro residues|||Zinc finger protein 526 ^@ http://purl.uniprot.org/annotation/PRO_0000306876|||http://purl.uniprot.org/annotation/VSP_028554|||http://purl.uniprot.org/annotation/VSP_028555 http://togogenome.org/gene/10090:Cutc ^@ http://purl.uniprot.org/uniprot/Q9D8X1 ^@ Chain|||Molecule Processing ^@ Chain ^@ Copper homeostasis protein cutC homolog ^@ http://purl.uniprot.org/annotation/PRO_0000215089 http://togogenome.org/gene/10090:Aida ^@ http://purl.uniprot.org/uniprot/Q8C4Q6 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Axin interactor, dorsalization-associated protein|||Axin-binding|||C2 Aida-type|||Disordered|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000305279|||http://purl.uniprot.org/annotation/VSP_028323 http://togogenome.org/gene/10090:Slc9a8 ^@ http://purl.uniprot.org/uniprot/A2A464|||http://purl.uniprot.org/uniprot/Q8R4D1 ^@ 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 ^@ Cation/H+ exchanger|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Sodium/hydrogen exchanger 8 ^@ http://purl.uniprot.org/annotation/PRO_0000052366|||http://purl.uniprot.org/annotation/VSP_009500|||http://purl.uniprot.org/annotation/VSP_009503|||http://purl.uniprot.org/annotation/VSP_009504 http://togogenome.org/gene/10090:Ear6 ^@ http://purl.uniprot.org/uniprot/Q923L7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ribonuclease A-domain ^@ http://purl.uniprot.org/annotation/PRO_5015020139 http://togogenome.org/gene/10090:Pin1rt1 ^@ http://purl.uniprot.org/uniprot/Q3ULQ2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ PpiC|||WW ^@ http://togogenome.org/gene/10090:Gorasp2 ^@ http://purl.uniprot.org/uniprot/Q99JX3 ^@ 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 ^@ Dimethylated arginine|||Disordered|||GRASP|||Golgi reassembly-stacking protein 2|||Important for membrane binding|||In isoform 2.|||N-myristoyl glycine|||No significant effect on interaction with BLZF1.|||PDZ GRASP-type 1|||PDZ GRASP-type 2|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK|||Polar residues|||Reduced interaction with BLZF1.|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000087546|||http://purl.uniprot.org/annotation/VSP_011301 http://togogenome.org/gene/10090:Or4c127 ^@ http://purl.uniprot.org/uniprot/Q8VGN2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp36 ^@ http://purl.uniprot.org/uniprot/P22893|||http://purl.uniprot.org/uniprot/Q3U3D2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Strand|||Turn|||Zinc Finger ^@ Abolished interaction with GIGYF2 and impaired TTP-mediated mRNA repression; when associated with 191-S--S-193.|||Abolished interaction with GIGYF2 and impaired TTP-mediated mRNA repression; when associated with 64-S--S-66.|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||Disordered|||Does not affect interaction with GIGYF2.|||Impairs phosphorylation by MAPKAPK2, decreases its stability and cytoplasmic localization, increases interaction with PPP2CA, inhibits binding to 14-3-3 proteins, but does not impair binding to ARE-containing transcripts, recruitment of mRNA decay factors and ZFP36-mediated deadenylation and decay of ARE-containing transcripts; when associated with A-178.|||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|||Pro residues|||Reduces both interaction with 14-3-3 proteins and YWHAB-induced cytoplasmic localization. Impairs phosphorylation by MAPKAPK2, decreases its stability and cytoplasmic localization, increases interaction with PPP2CA, inhibits binding to 14-3-3 proteins, but does not impair binding to ARE-containing transcripts, recruitment of mRNA decay factors and ZFP36-mediated deadenylation and decay of ARE-containing transcripts; when associated with A-52.|||Stimulates interaction with SH3KBP1.|||mRNA decay activator protein ZFP36 ^@ http://purl.uniprot.org/annotation/PRO_0000089164 http://togogenome.org/gene/10090:Eapp ^@ http://purl.uniprot.org/uniprot/Q5BU09 ^@ 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|||E2F-associated phosphoprotein|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000086905|||http://purl.uniprot.org/annotation/VSP_015331 http://togogenome.org/gene/10090:Baz2b ^@ http://purl.uniprot.org/uniprot/A2AUY4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||Bromo|||Bromodomain adjacent to zinc finger domain protein 2B|||DDT|||Disordered|||In isoform 2.|||MBD|||PHD-type|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000452177|||http://purl.uniprot.org/annotation/VSP_060916|||http://purl.uniprot.org/annotation/VSP_060917|||http://purl.uniprot.org/annotation/VSP_060918 http://togogenome.org/gene/10090:Mrps18c ^@ http://purl.uniprot.org/uniprot/Q8R2L5 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||Small ribosomal subunit protein bS18m ^@ http://purl.uniprot.org/annotation/PRO_0000030630 http://togogenome.org/gene/10090:Or6c66b ^@ http://purl.uniprot.org/uniprot/Q7TRH9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp655 ^@ http://purl.uniprot.org/uniprot/A0A0G2JEM1|||http://purl.uniprot.org/uniprot/Q6P8W7|||http://purl.uniprot.org/uniprot/Q9CZP3 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Hoxd9 ^@ http://purl.uniprot.org/uniprot/P28357 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Disordered|||Homeobox|||Homeobox protein Hox-D9|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000200221 http://togogenome.org/gene/10090:Swi5 ^@ http://purl.uniprot.org/uniprot/E3WH32|||http://purl.uniprot.org/uniprot/Q8K3D3 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Non-terminal Residue|||Splice Variant ^@ DNA repair protein SWI5 homolog|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000324585|||http://purl.uniprot.org/annotation/VSP_040899 http://togogenome.org/gene/10090:Hoxb2 ^@ http://purl.uniprot.org/uniprot/P0C1T1 ^@ 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-B2|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000248841 http://togogenome.org/gene/10090:Mup13 ^@ http://purl.uniprot.org/uniprot/A2CEK6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5015086053 http://togogenome.org/gene/10090:Cand1 ^@ http://purl.uniprot.org/uniprot/Q6ZQ38 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat ^@ 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|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000089294 http://togogenome.org/gene/10090:Junb ^@ http://purl.uniprot.org/uniprot/P09450|||http://purl.uniprot.org/uniprot/Q569U6 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ 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_0000076439 http://togogenome.org/gene/10090:Anks1 ^@ http://purl.uniprot.org/uniprot/A0A3B2W7H4|||http://purl.uniprot.org/uniprot/P59672|||http://purl.uniprot.org/uniprot/Q3UHP6 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Splice Variant|||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|||SAM 1|||SAM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000066922|||http://purl.uniprot.org/annotation/VSP_012704|||http://purl.uniprot.org/annotation/VSP_012705|||http://purl.uniprot.org/annotation/VSP_012706 http://togogenome.org/gene/10090:Utp3 ^@ http://purl.uniprot.org/uniprot/Q9JI13 ^@ 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 residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Something about silencing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000114327|||http://purl.uniprot.org/annotation/VSP_051655|||http://purl.uniprot.org/annotation/VSP_051656 http://togogenome.org/gene/10090:Phb ^@ http://purl.uniprot.org/uniprot/P67778 ^@ 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|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphothreonine|||Phosphotyrosine|||Prohibitin 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213879 http://togogenome.org/gene/10090:Cdk16 ^@ http://purl.uniprot.org/uniprot/Q04735|||http://purl.uniprot.org/uniprot/Q3TM24|||http://purl.uniprot.org/uniprot/Q543G3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes phosphorylation by CDK5. Impairs normal denrite development.|||Cyclin-dependent kinase 16|||Disordered|||In isoform Short.|||Phosphoserine|||Phosphoserine; by BRSK2|||Phosphoserine; by CDK5|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086485|||http://purl.uniprot.org/annotation/VSP_004801|||http://purl.uniprot.org/annotation/VSP_004802 http://togogenome.org/gene/10090:Septin14 ^@ http://purl.uniprot.org/uniprot/Q9DA97|||http://purl.uniprot.org/uniprot/S4R2P6 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict ^@ 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_0000294426 http://togogenome.org/gene/10090:Mb ^@ http://purl.uniprot.org/uniprot/P04247|||http://purl.uniprot.org/uniprot/Q3UVB1 ^@ 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 ^@ Globin family profile|||Myoglobin|||Phosphoserine|||Phosphothreonine|||Removed|||distal binding residue|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000053319 http://togogenome.org/gene/10090:Toe1 ^@ http://purl.uniprot.org/uniprot/Q9D2E2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||C3H1-type|||Disordered|||In isoform 2.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Removed|||Target of EGR1 protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000270834|||http://purl.uniprot.org/annotation/VSP_022242|||http://purl.uniprot.org/annotation/VSP_022243 http://togogenome.org/gene/10090:Rsrc2 ^@ http://purl.uniprot.org/uniprot/A2RTL5|||http://purl.uniprot.org/uniprot/B7ZNU2|||http://purl.uniprot.org/uniprot/S4R265|||http://purl.uniprot.org/uniprot/S4R2L4 ^@ 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 ^@ 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|||Phosphoserine|||Small acidic protein-like ^@ http://purl.uniprot.org/annotation/PRO_0000314938 http://togogenome.org/gene/10090:Or52b1 ^@ http://purl.uniprot.org/uniprot/Q8VH18 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r172 ^@ http://purl.uniprot.org/uniprot/Q9EPS4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cryba1 ^@ http://purl.uniprot.org/uniprot/Q9QXC6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Beta/gamma crystallin 'Greek key' ^@ http://togogenome.org/gene/10090:Cel ^@ http://purl.uniprot.org/uniprot/Q3V2H7|||http://purl.uniprot.org/uniprot/Q64285 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide ^@ 1|||2|||3|||4 X 11 AA tandem repeats, O-glycosylated region|||Acyl-ester intermediate|||Bile salt-activated lipase|||Carboxylesterase type B|||Carboxylic ester hydrolase|||Charge relay system|||Disordered|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000008632|||http://purl.uniprot.org/annotation/PRO_5010754681 http://togogenome.org/gene/10090:Slc30a9 ^@ http://purl.uniprot.org/uniprot/F8WHL1|||http://purl.uniprot.org/uniprot/Q5IRJ6 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Motif|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||LXXLL motif|||Proton-coupled zinc antiporter SLC30A9, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000295806|||http://purl.uniprot.org/annotation/VSP_027088 http://togogenome.org/gene/10090:Tmem114 ^@ http://purl.uniprot.org/uniprot/Q9D563 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Mutagenesis Site|||Region|||Transmembrane ^@ Complete loss of glycosylation; when associated with K-54.|||Complete loss of glycosylation; when associated with K-88.|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 114 ^@ http://purl.uniprot.org/annotation/PRO_0000352760 http://togogenome.org/gene/10090:Iqcf5 ^@ http://purl.uniprot.org/uniprot/Q9DAL7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ IQ 1|||IQ 2|||IQ domain-containing protein F5 ^@ http://purl.uniprot.org/annotation/PRO_0000345957 http://togogenome.org/gene/10090:Ap5z1 ^@ http://purl.uniprot.org/uniprot/Q3U829 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ AP-5 complex subunit zeta-1 ^@ http://purl.uniprot.org/annotation/PRO_0000261358 http://togogenome.org/gene/10090:Gsap ^@ http://purl.uniprot.org/uniprot/Q3TCV3 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ Gamma-secretase-activating protein|||Gamma-secretase-activating protein 16 kDa C-terminal form|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000335810|||http://purl.uniprot.org/annotation/PRO_0000403729|||http://purl.uniprot.org/annotation/VSP_033775|||http://purl.uniprot.org/annotation/VSP_033776|||http://purl.uniprot.org/annotation/VSP_033777|||http://purl.uniprot.org/annotation/VSP_033778 http://togogenome.org/gene/10090:Sesn3 ^@ http://purl.uniprot.org/uniprot/A2RSF4|||http://purl.uniprot.org/uniprot/Q9CYP7 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Region ^@ C-terminal domain; mediates TORC1 regulation|||Cysteine sulfenic acid (-SOH) intermediate|||N-terminal domain; may mediate the alkylhydroperoxide reductase activity|||Sestrin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000221184 http://togogenome.org/gene/10090:Phf11b ^@ http://purl.uniprot.org/uniprot/B4XVQ1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ PHD-type ^@ http://togogenome.org/gene/10090:Dpy19l1 ^@ http://purl.uniprot.org/uniprot/A6X919 ^@ 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.|||In isoform 3.|||Phosphoserine|||Probable C-mannosyltransferase DPY19L1 ^@ http://purl.uniprot.org/annotation/PRO_0000311878|||http://purl.uniprot.org/annotation/VSP_029629|||http://purl.uniprot.org/annotation/VSP_029630|||http://purl.uniprot.org/annotation/VSP_029631 http://togogenome.org/gene/10090:Prl8a6 ^@ http://purl.uniprot.org/uniprot/A0A0M6L0X0|||http://purl.uniprot.org/uniprot/Q9DAY2 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Prolactin-8A6 ^@ http://purl.uniprot.org/annotation/PRO_0000045396|||http://purl.uniprot.org/annotation/PRO_5015043312|||http://purl.uniprot.org/annotation/VSP_016903|||http://purl.uniprot.org/annotation/VSP_016904 http://togogenome.org/gene/10090:Or2t6 ^@ http://purl.uniprot.org/uniprot/Q8VF37 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tspan14 ^@ http://purl.uniprot.org/uniprot/Q8QZY6 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Necessary and sufficient for interaction with ADAM10|||Tetraspanin-14 ^@ http://purl.uniprot.org/annotation/PRO_0000219262 http://togogenome.org/gene/10090:Mlst8 ^@ http://purl.uniprot.org/uniprot/A0A3Q4EC26|||http://purl.uniprot.org/uniprot/Q9DCJ1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Repeat|||Sequence Conflict ^@ N-acetylmethionine|||Phosphothreonine|||Target of rapamycin complex subunit LST8|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000326500 http://togogenome.org/gene/10090:Dtwd1 ^@ http://purl.uniprot.org/uniprot/Q9D8U7 ^@ Chain|||Molecule Processing|||Motif|||Region ^@ Chain|||Motif|||Region ^@ DXTW|||Disordered|||tRNA-uridine aminocarboxypropyltransferase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000308213 http://togogenome.org/gene/10090:Zscan10 ^@ http://purl.uniprot.org/uniprot/Q3URR7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||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|||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|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000394248|||http://purl.uniprot.org/annotation/VSP_039227|||http://purl.uniprot.org/annotation/VSP_039228 http://togogenome.org/gene/10090:H2ac8 ^@ http://purl.uniprot.org/uniprot/B2RVF0|||http://purl.uniprot.org/uniprot/C0HKE1|||http://purl.uniprot.org/uniprot/C0HKE2|||http://purl.uniprot.org/uniprot/C0HKE3|||http://purl.uniprot.org/uniprot/C0HKE4|||http://purl.uniprot.org/uniprot/C0HKE5|||http://purl.uniprot.org/uniprot/C0HKE6|||http://purl.uniprot.org/uniprot/C0HKE7|||http://purl.uniprot.org/uniprot/C0HKE8|||http://purl.uniprot.org/uniprot/C0HKE9 ^@ 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|||Region|||Sequence Conflict|||Strand|||Turn ^@ 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|||Histone H2A type 1-C|||Histone H2A type 1-D|||Histone H2A type 1-E|||Histone H2A type 1-G|||Histone H2A type 1-I|||Histone H2A type 1-N|||Histone H2A type 1-O|||Histone H2A type 1-P|||Histone H2A/H2B/H3|||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_0000439715|||http://purl.uniprot.org/annotation/PRO_0000439716|||http://purl.uniprot.org/annotation/PRO_0000439717|||http://purl.uniprot.org/annotation/PRO_0000439718|||http://purl.uniprot.org/annotation/PRO_0000439719|||http://purl.uniprot.org/annotation/PRO_0000439720|||http://purl.uniprot.org/annotation/PRO_0000439721|||http://purl.uniprot.org/annotation/PRO_0000439722|||http://purl.uniprot.org/annotation/PRO_0000439723 http://togogenome.org/gene/10090:Tdg ^@ http://purl.uniprot.org/uniprot/P56581 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ 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|||In isoform 2.|||Loss of DNA glycosylase activity. ^@ http://purl.uniprot.org/annotation/PRO_0000185778|||http://purl.uniprot.org/annotation/VSP_046491 http://togogenome.org/gene/10090:Avpr2 ^@ http://purl.uniprot.org/uniprot/O88721|||http://purl.uniprot.org/uniprot/Q3KNZ4|||http://purl.uniprot.org/uniprot/Q3SWS1|||http://purl.uniprot.org/uniprot/Q3SWS4 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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|||N-linked (GlcNAc...) asparagine|||Polar residues|||S-palmitoyl cysteine|||Vasopressin V2 receptor ^@ http://purl.uniprot.org/annotation/PRO_0000070209 http://togogenome.org/gene/10090:Krt86 ^@ http://purl.uniprot.org/uniprot/B2RTB6|||http://purl.uniprot.org/uniprot/P97861 ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Region ^@ Coil 1A|||Coil 1B|||Coil 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Head|||IF rod|||Keratin, type II cuticular Hb6|||Linker 1|||Linker 12|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063705 http://togogenome.org/gene/10090:Ptbp2 ^@ http://purl.uniprot.org/uniprot/Q91Z31 ^@ 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 ^@ In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polypyrimidine tract-binding protein 2|||RRM 1|||RRM 2|||RRM 3|||RRM 4 ^@ http://purl.uniprot.org/annotation/PRO_0000232929|||http://purl.uniprot.org/annotation/VSP_018019 http://togogenome.org/gene/10090:Ccdc126 ^@ http://purl.uniprot.org/uniprot/Q8BIS8 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant ^@ Coiled-coil domain-containing protein 126|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000288817|||http://purl.uniprot.org/annotation/VSP_025785 http://togogenome.org/gene/10090:Mto1 ^@ http://purl.uniprot.org/uniprot/G5E889|||http://purl.uniprot.org/uniprot/Q923Z3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||N6-methyllysine|||Protein MTO1 homolog, mitochondrial|||tRNA uridine 5-carboxymethylaminomethyl modification enzyme C-terminal subdomain ^@ http://purl.uniprot.org/annotation/PRO_0000042690 http://togogenome.org/gene/10090:Prmt3 ^@ http://purl.uniprot.org/uniprot/Q922H1 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Zinc Finger ^@ C2H2-type|||Disordered|||Mediates interaction with ALDH1A1|||N-acetylcysteine|||Phosphoserine|||Protein arginine N-methyltransferase 3|||Removed|||SAM-dependent MTase PRMT-type ^@ http://purl.uniprot.org/annotation/PRO_0000212327 http://togogenome.org/gene/10090:Fbxw10 ^@ http://purl.uniprot.org/uniprot/B7ZC91|||http://purl.uniprot.org/uniprot/H3BLP9 ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Polar residues|||WD ^@ http://togogenome.org/gene/10090:Cd151 ^@ http://purl.uniprot.org/uniprot/O35566 ^@ Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ CD151 antigen|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000219232 http://togogenome.org/gene/10090:Rbm6 ^@ http://purl.uniprot.org/uniprot/Q3ULB0|||http://purl.uniprot.org/uniprot/S4R1W5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||G-patch|||Polar residues|||RRM ^@ http://togogenome.org/gene/10090:Npy1r ^@ http://purl.uniprot.org/uniprot/Q04573|||http://purl.uniprot.org/uniprot/Q3V1K5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||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 isoform NPY1-R beta.|||N-linked (GlcNAc...) asparagine|||Neuropeptide Y receptor type 1|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069921|||http://purl.uniprot.org/annotation/VSP_001912|||http://purl.uniprot.org/annotation/VSP_001913 http://togogenome.org/gene/10090:Iftap ^@ http://purl.uniprot.org/uniprot/Q9CQI4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Intraflagellar transport-associated protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000288855 http://togogenome.org/gene/10090:Snx11 ^@ http://purl.uniprot.org/uniprot/Q91WL6 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Important for membrane trafficking|||PX|||Polar residues|||Sorting nexin-11 ^@ http://purl.uniprot.org/annotation/PRO_0000213857 http://togogenome.org/gene/10090:Or2w1 ^@ http://purl.uniprot.org/uniprot/Q7TQT8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tsga10 ^@ http://purl.uniprot.org/uniprot/Q6NY15 ^@ 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 and isoform 3.|||In isoform 3.|||Interaction with HIF1A|||Phosphoserine|||Testis-specific gene 10 protein ^@ http://purl.uniprot.org/annotation/PRO_0000307128|||http://purl.uniprot.org/annotation/VSP_028579|||http://purl.uniprot.org/annotation/VSP_028580 http://togogenome.org/gene/10090:Sdf4 ^@ http://purl.uniprot.org/uniprot/Q61112 ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant ^@ 45 kDa calcium-binding protein|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||In CAB45A.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Necessary for intracellular retention in Golgi apparatus lumen|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000004157|||http://purl.uniprot.org/annotation/VSP_037450|||http://purl.uniprot.org/annotation/VSP_037451 http://togogenome.org/gene/10090:Chmp5 ^@ http://purl.uniprot.org/uniprot/Q9D7S9 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Region ^@ Charged multivesicular body protein 5|||Disordered|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000211501 http://togogenome.org/gene/10090:Abtb3 ^@ http://purl.uniprot.org/uniprot/B2RUH2|||http://purl.uniprot.org/uniprot/E9QJW1|||http://purl.uniprot.org/uniprot/Q6GQW0|||http://purl.uniprot.org/uniprot/Q8BRL1 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Chain|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||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. ^@ http://purl.uniprot.org/annotation/PRO_0000328828|||http://purl.uniprot.org/annotation/PRO_5002781881|||http://purl.uniprot.org/annotation/VSP_032804|||http://purl.uniprot.org/annotation/VSP_032805|||http://purl.uniprot.org/annotation/VSP_032806|||http://purl.uniprot.org/annotation/VSP_032807|||http://purl.uniprot.org/annotation/VSP_032808 http://togogenome.org/gene/10090:Emc1 ^@ http://purl.uniprot.org/uniprot/Q8C7X2 ^@ 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|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||ER membrane protein complex subunit 1|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000248598|||http://purl.uniprot.org/annotation/VSP_020330|||http://purl.uniprot.org/annotation/VSP_020331 http://togogenome.org/gene/10090:Zscan4b ^@ http://purl.uniprot.org/uniprot/E9Q3G0 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||SCAN box ^@ http://togogenome.org/gene/10090:Tdrd5 ^@ http://purl.uniprot.org/uniprot/J3QPB7|||http://purl.uniprot.org/uniprot/Q5VCS6 ^@ 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|||HTH OST-type|||HTH OST-type 1|||HTH OST-type 2|||HTH OST-type 3|||In isoform 2.|||Phosphoserine|||Polar residues|||Tudor|||Tudor domain-containing protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000281122|||http://purl.uniprot.org/annotation/VSP_041054 http://togogenome.org/gene/10090:Polr3c ^@ http://purl.uniprot.org/uniprot/B2RX77|||http://purl.uniprot.org/uniprot/Q9D483 ^@ 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|||DNA-directed RNA polymerase III subunit RPC3|||Disordered|||In isoform 2.|||Phosphoserine|||RNA polymerase III Rpc82 C -terminal|||RNA polymerase III subunit RPC82-related helix-turn-helix ^@ http://purl.uniprot.org/annotation/PRO_0000073964|||http://purl.uniprot.org/annotation/VSP_010678|||http://purl.uniprot.org/annotation/VSP_010679 http://togogenome.org/gene/10090:Vps9d1 ^@ http://purl.uniprot.org/uniprot/Q3U280|||http://purl.uniprot.org/uniprot/Q8C190 ^@ 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.|||Phosphoserine|||Pro residues|||VPS9|||VPS9 domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000079280|||http://purl.uniprot.org/annotation/VSP_014703|||http://purl.uniprot.org/annotation/VSP_014704 http://togogenome.org/gene/10090:Cyth3 ^@ http://purl.uniprot.org/uniprot/G5E8Q4|||http://purl.uniprot.org/uniprot/O08967|||http://purl.uniprot.org/uniprot/Q3TXK1 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn ^@ Abolishes phosphatidylinositol 3,4,5-trisphosphate binding.|||C-terminal autoinhibitory region|||Cytohesin-3|||Disordered|||Impairs autoinhibition; when associated with A-388.|||Impairs autoinhibition; when associated with A-392.|||Impairs epithelium polarization.|||PH|||Reduces phosphatidylinositol 3,4,5-trisphosphate binding.|||SEC7|||Slightly reduces phosphatidylinositol 3,4,5-trisphosphate binding. ^@ http://purl.uniprot.org/annotation/PRO_0000120201 http://togogenome.org/gene/10090:Dnajb3 ^@ http://purl.uniprot.org/uniprot/O35723|||http://purl.uniprot.org/uniprot/Q5RL26 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Sequence Conflict ^@ DnaJ homolog subfamily B member 3|||J ^@ http://purl.uniprot.org/annotation/PRO_0000071020 http://togogenome.org/gene/10090:Add3 ^@ http://purl.uniprot.org/uniprot/Q3UNK1|||http://purl.uniprot.org/uniprot/Q8BM29|||http://purl.uniprot.org/uniprot/Q9QYB5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||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 isoform 1.|||Interaction with calmodulin|||Loss of cleavage by asparagine endopeptidase (AEP).|||N-acetylserine|||No effect on cleavage by asparagine endopeptidase (AEP).|||Phosphoserine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000218537|||http://purl.uniprot.org/annotation/VSP_000189 http://togogenome.org/gene/10090:Usp16 ^@ http://purl.uniprot.org/uniprot/Q99LG0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nucleophile|||Phosphoserine|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 16 ^@ http://purl.uniprot.org/annotation/PRO_0000367503 http://togogenome.org/gene/10090:Mblac1 ^@ http://purl.uniprot.org/uniprot/Q8BWY4 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Metallo-beta-lactamase domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000337028 http://togogenome.org/gene/10090:Fus ^@ http://purl.uniprot.org/uniprot/P56959|||http://purl.uniprot.org/uniprot/Q3USY4|||http://purl.uniprot.org/uniprot/Q564D0|||http://purl.uniprot.org/uniprot/Q8CFQ9 ^@ 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 ^@ Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA-binding protein FUS|||RRM|||RanBP2-type ^@ http://purl.uniprot.org/annotation/PRO_0000081592 http://togogenome.org/gene/10090:Rbm17 ^@ http://purl.uniprot.org/uniprot/Q8JZX4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||RRM|||Removed|||Splicing factor 45 ^@ http://purl.uniprot.org/annotation/PRO_0000081904 http://togogenome.org/gene/10090:Coq6 ^@ http://purl.uniprot.org/uniprot/Q8R1S0 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Mitochondrion|||N6-succinyllysine|||Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000207584 http://togogenome.org/gene/10090:Slc39a10 ^@ http://purl.uniprot.org/uniprot/Q6P5F6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Zinc transporter ZIP10 ^@ http://purl.uniprot.org/annotation/PRO_0000297633 http://togogenome.org/gene/10090:Hgh1 ^@ http://purl.uniprot.org/uniprot/Q8C3I8 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Protein HGH1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000273319 http://togogenome.org/gene/10090:Vmn1r210 ^@ http://purl.uniprot.org/uniprot/Q8R274 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Srcin1 ^@ http://purl.uniprot.org/uniprot/B1AQX7|||http://purl.uniprot.org/uniprot/B1AQX9|||http://purl.uniprot.org/uniprot/Q9QWI6 ^@ 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 interacting protein 3-like C-terminal|||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_0000072012|||http://purl.uniprot.org/annotation/VSP_050631|||http://purl.uniprot.org/annotation/VSP_050632 http://togogenome.org/gene/10090:Nr2e1 ^@ http://purl.uniprot.org/uniprot/Q64104|||http://purl.uniprot.org/uniprot/Q78ZM1 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||DNA Binding|||Domain Extent|||Region|||Zinc Finger ^@ 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_0000053593 http://togogenome.org/gene/10090:Or52n2b ^@ http://purl.uniprot.org/uniprot/Q7TRP4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Unc119 ^@ http://purl.uniprot.org/uniprot/B1AQD7|||http://purl.uniprot.org/uniprot/B1AQD9|||http://purl.uniprot.org/uniprot/Q3V299|||http://purl.uniprot.org/uniprot/Q9Z2R6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||GMP phosphodiesterase delta subunit|||Phosphoserine; by CK2|||Protein unc-119 homolog A|||Up-regulation of KLH18-mediated degradation; when associated with A-37 and A-39.|||Up-regulation of KLH18-mediated degradation; when associated with A-37 and A-41.|||Up-regulation of KLH18-mediated degradation; when associated with A-39 and A-41. ^@ http://purl.uniprot.org/annotation/PRO_0000221213 http://togogenome.org/gene/10090:Slco4c1 ^@ http://purl.uniprot.org/uniprot/Q8BGD4 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||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|||Phosphothreonine|||Polar residues|||Solute carrier organic anion transporter family member 4C1 ^@ http://purl.uniprot.org/annotation/PRO_0000337152 http://togogenome.org/gene/10090:Sec11a ^@ http://purl.uniprot.org/uniprot/Q9R0P6 ^@ Active Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Region|||Topological Domain|||Transmembrane ^@ C-terminal short (CTS) helix|||Charge relay system|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Signal peptidase complex catalytic subunit SEC11A ^@ http://purl.uniprot.org/annotation/PRO_0000109544 http://togogenome.org/gene/10090:Eloc ^@ http://purl.uniprot.org/uniprot/A0A087WNT1|||http://purl.uniprot.org/uniprot/P83940 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Elongin-C|||SKP1 component POZ ^@ http://purl.uniprot.org/annotation/PRO_0000187259 http://togogenome.org/gene/10090:Inpp1 ^@ http://purl.uniprot.org/uniprot/P49442 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ Inositol polyphosphate 1-phosphatase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000142511 http://togogenome.org/gene/10090:Ddit4 ^@ http://purl.uniprot.org/uniprot/B7ZNP9|||http://purl.uniprot.org/uniprot/Q9D3F7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ DNA damage-inducible transcript 4 protein|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000307198 http://togogenome.org/gene/10090:Brd3 ^@ http://purl.uniprot.org/uniprot/Q3TUI3|||http://purl.uniprot.org/uniprot/Q5CCJ9|||http://purl.uniprot.org/uniprot/Q8K2F0 ^@ 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 ^@ Acetylated histone H3 binding|||Basic and acidic residues|||Bromo|||Bromo 1|||Bromo 2|||Bromodomain-containing protein 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||NET|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000211182|||http://purl.uniprot.org/annotation/VSP_010249 http://togogenome.org/gene/10090:D3Ertd751e ^@ http://purl.uniprot.org/uniprot/Q8BGN2 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||UPF0462 protein C4orf33 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000295715|||http://purl.uniprot.org/annotation/VSP_027013 http://togogenome.org/gene/10090:Zbtb49 ^@ http://purl.uniprot.org/uniprot/Q8BXX2 ^@ 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 ^@ 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|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Zinc finger and BTB domain-containing protein 49 ^@ http://purl.uniprot.org/annotation/PRO_0000047627|||http://purl.uniprot.org/annotation/VSP_016344|||http://purl.uniprot.org/annotation/VSP_016345|||http://purl.uniprot.org/annotation/VSP_016346 http://togogenome.org/gene/10090:Fthl17d ^@ http://purl.uniprot.org/uniprot/Q3SXD1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ferritin-like diiron ^@ http://togogenome.org/gene/10090:Ptpn3 ^@ http://purl.uniprot.org/uniprot/A2ALK8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Disordered|||FERM|||PDZ|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 3 ^@ http://purl.uniprot.org/annotation/PRO_0000320074 http://togogenome.org/gene/10090:Msl1 ^@ http://purl.uniprot.org/uniprot/Q6PDM1 ^@ 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|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolishes interaction with KAT8.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 6.|||Interaction with KAT8|||Interaction with MSL2|||Interaction with MSL3 MRG domain|||Male-specific lethal 1 homolog|||N6-acetyllysine|||No effect on interaction with MSL3. Reduces interaction; when associated with E-589. Strongly reduces interaction with MSL3; when associated with E-556 and E-589.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Pro residues|||Strongly reduces interaction with MSL3; when associated with E-556 and E-576 or E-556 and E-577.|||Strongly reduces interaction with MSL3; when associated with E-576 and E-589 or E-577 and E-589. ^@ http://purl.uniprot.org/annotation/PRO_0000349237|||http://purl.uniprot.org/annotation/VSP_035238|||http://purl.uniprot.org/annotation/VSP_035239|||http://purl.uniprot.org/annotation/VSP_035240|||http://purl.uniprot.org/annotation/VSP_035241|||http://purl.uniprot.org/annotation/VSP_035242|||http://purl.uniprot.org/annotation/VSP_035243 http://togogenome.org/gene/10090:Rbm28 ^@ http://purl.uniprot.org/uniprot/Q8CGC6 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Phosphoserine|||Polar residues|||RNA-binding protein 28|||RRM 1|||RRM 2|||RRM 3|||RRM 4|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000081786 http://togogenome.org/gene/10090:Zdhhc17 ^@ http://purl.uniprot.org/uniprot/Q80TN5|||http://purl.uniprot.org/uniprot/Q8BIT5 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||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.|||Loss of palmitoyltransferase activity toward DNAJC5 and SNAP25.|||Lumenal|||Necessary and sufficient for interaction with DNAJC5 and SNAP25|||No effect on interaction with DNAJC5 and SNAP25.|||Palmitoyltransferase ZDHHC17|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212901|||http://purl.uniprot.org/annotation/VSP_010026|||http://purl.uniprot.org/annotation/VSP_010027 http://togogenome.org/gene/10090:Cpne2 ^@ http://purl.uniprot.org/uniprot/P59108 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict ^@ C2 1|||C2 2|||Copine-2|||Does not inhibit calcium-dependent translocation to the cell membrane. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-170; N-232 and N-234.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-37; N-39 and N-97.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-37; N-39 and N-99.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-37; N-97 and N-99.|||Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-39; N-97 and N-99.|||Leads to a reduction in the amount of calcium-dependent translocation to the cell membrane. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-170; N-176 and N-232.|||Leads to a reduction in the amount of calcium-dependent translocation to the cell membrane. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-170; N-176 and N-234.|||Leads to a reduction in the amount of calcium-dependent translocation to the cell membrane. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-176; N-232 and N-234.|||Linker region|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000144837 http://togogenome.org/gene/10090:Ssbp1 ^@ http://purl.uniprot.org/uniprot/Q9CYR0 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||SSB|||Single-stranded DNA-binding protein, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000033264 http://togogenome.org/gene/10090:Ankrd45 ^@ http://purl.uniprot.org/uniprot/G3X9E0|||http://purl.uniprot.org/uniprot/Q810N6 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ ANK|||ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein 45|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000244575 http://togogenome.org/gene/10090:Cxcl5 ^@ http://purl.uniprot.org/uniprot/P50228 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ C-X-C motif chemokine 5|||GCP-2(1-78)|||GCP-2(9-78) ^@ http://purl.uniprot.org/annotation/PRO_0000005078|||http://purl.uniprot.org/annotation/PRO_0000005079|||http://purl.uniprot.org/annotation/PRO_0000005080 http://togogenome.org/gene/10090:Cd48 ^@ http://purl.uniprot.org/uniprot/P18181 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Signal Peptide|||Strand|||Turn ^@ CD48 antigen|||GPI-anchor amidated serine|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000014883|||http://purl.uniprot.org/annotation/PRO_0000014884 http://togogenome.org/gene/10090:Psmb10 ^@ http://purl.uniprot.org/uniprot/O35955 ^@ Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Site|||Strand|||Turn ^@ Cleavage; by autolysis|||N-acetylmethionine|||Nucleophile|||Prevents the correct removal of the propeptide.|||Proteasome subunit beta type-10|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000026653|||http://purl.uniprot.org/annotation/PRO_0000026654 http://togogenome.org/gene/10090:Il11 ^@ http://purl.uniprot.org/uniprot/A3KPB8|||http://purl.uniprot.org/uniprot/P47873|||http://purl.uniprot.org/uniprot/Q3V0U3 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Site ^@ Chain|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Site ^@ Impairs IL11RA binding and mildly reduces stimulation of cell proliferation.|||Important for interaction with IL11RA and for the stimulation of cell proliferation|||Important for interaction with IL6ST and for the stimulation of cell proliferation|||Interleukin-11|||No effect on IL11RA binding. Decreases stimulation of cell proliferation.|||Slightly increases IL11RA binding. Abolishes interaction with IL6ST. Abolishes stimulation of cell proliferation.|||Srongly reduces IL11RA binding and stimulation of cell proliferation. ^@ http://purl.uniprot.org/annotation/PRO_0000015620|||http://purl.uniprot.org/annotation/PRO_5014296857 http://togogenome.org/gene/10090:F11 ^@ http://purl.uniprot.org/uniprot/Q91Y47 ^@ 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|||Sequence Conflict|||Signal Peptide ^@ Apple 1|||Apple 2|||Apple 3|||Apple 4|||Charge relay system|||Coagulation factor XIa heavy chain|||Coagulation factor XIa light chain|||Interchain|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_0000027827|||http://purl.uniprot.org/annotation/PRO_0000027828 http://togogenome.org/gene/10090:Bri3bp ^@ http://purl.uniprot.org/uniprot/Q8BXV2 ^@ 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|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000229748 http://togogenome.org/gene/10090:Tmco5 ^@ http://purl.uniprot.org/uniprot/Q9D9D5 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Splice Variant|||Transmembrane ^@ Helical|||In isoform 2.|||Transmembrane and coiled-coil domain-containing protein 5A ^@ http://purl.uniprot.org/annotation/PRO_0000305154|||http://purl.uniprot.org/annotation/VSP_028248 http://togogenome.org/gene/10090:Wnt10b ^@ http://purl.uniprot.org/uniprot/P48614|||http://purl.uniprot.org/uniprot/Q1RME7 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Signal Peptide|||Splice Variant ^@ In isoform Short.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Phosphothreonine|||Protein Wnt|||Protein Wnt-10b ^@ http://purl.uniprot.org/annotation/PRO_0000041464|||http://purl.uniprot.org/annotation/PRO_5015097177|||http://purl.uniprot.org/annotation/VSP_006796 http://togogenome.org/gene/10090:Oaz2 ^@ http://purl.uniprot.org/uniprot/O08608 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Ornithine decarboxylase antizyme 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000220858 http://togogenome.org/gene/10090:Irak3 ^@ http://purl.uniprot.org/uniprot/Q0VB14|||http://purl.uniprot.org/uniprot/Q8K4B2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site ^@ Cis/trans isomerization of proline peptide bond; by PIN1; dependent on Thr-110 phosphorylation|||Death|||Interleukin-1 receptor-associated kinase 3|||Phosphoserine|||Phosphothreonine|||Protein kinase ^@ http://purl.uniprot.org/annotation/PRO_0000086034|||http://purl.uniprot.org/annotation/PRO_5014306829 http://togogenome.org/gene/10090:Bag2 ^@ http://purl.uniprot.org/uniprot/Q91YN9 ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue ^@ BAG|||BAG family molecular chaperone regulator 2|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000088867 http://togogenome.org/gene/10090:Lemd3 ^@ http://purl.uniprot.org/uniprot/E9QP59|||http://purl.uniprot.org/uniprot/Q9WU40 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Inner nuclear membrane protein Man1|||Interaction with SMAD1, SMAD2, SMAD3 and SMAD5|||LEM|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000206150|||http://purl.uniprot.org/annotation/VSP_026782 http://togogenome.org/gene/10090:Or4z4 ^@ http://purl.uniprot.org/uniprot/Q8VFU9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Glrx3 ^@ http://purl.uniprot.org/uniprot/Q9CQM9 ^@ 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 ^@ Glutaredoxin 1|||Glutaredoxin 2|||Glutaredoxin-3|||N-acetylalanine|||Phosphoserine|||Removed|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000120020 http://togogenome.org/gene/10090:Rmdn3 ^@ http://purl.uniprot.org/uniprot/Q3UJU9 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||FFAT|||Helical|||Mitochondrial intermembrane|||Phosphoserine|||Phosphothreonine|||Regulator of microtubule dynamics protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000287511 http://togogenome.org/gene/10090:Ccl5 ^@ http://purl.uniprot.org/uniprot/P30882|||http://purl.uniprot.org/uniprot/Q5XZF2 ^@ 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 ^@ C-C motif chemokine|||C-C motif chemokine 5|||Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_0000005179|||http://purl.uniprot.org/annotation/PRO_5014205910 http://togogenome.org/gene/10090:Snrpa ^@ http://purl.uniprot.org/uniprot/Q62189 ^@ 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|||N6-acetyllysine|||Omega-N-methylarginine|||RRM 1|||RRM 2|||U1 small nuclear ribonucleoprotein A ^@ http://purl.uniprot.org/annotation/PRO_0000081888 http://togogenome.org/gene/10090:Tmem121b ^@ http://purl.uniprot.org/uniprot/B2RQD1|||http://purl.uniprot.org/uniprot/Q99MX7 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Polar residues|||Pro residues|||Transmembrane protein 121B ^@ http://purl.uniprot.org/annotation/PRO_0000089467 http://togogenome.org/gene/10090:Adra1a ^@ http://purl.uniprot.org/uniprot/P97718|||http://purl.uniprot.org/uniprot/Q8BUE5|||http://purl.uniprot.org/uniprot/Q8BXZ4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Alpha-1A 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|||Nuclear localization signal|||Phosphoserine; by PKA|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069064 http://togogenome.org/gene/10090:Serpine1 ^@ http://purl.uniprot.org/uniprot/G5E899 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Serpin ^@ http://purl.uniprot.org/annotation/PRO_5015091903 http://togogenome.org/gene/10090:Cnga4 ^@ http://purl.uniprot.org/uniprot/Q3UW12 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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. ^@ http://purl.uniprot.org/annotation/PRO_0000317108|||http://purl.uniprot.org/annotation/VSP_030873 http://togogenome.org/gene/10090:Tprn ^@ http://purl.uniprot.org/uniprot/A2AI08 ^@ 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|||Polar residues|||Pro residues|||Taperin ^@ http://purl.uniprot.org/annotation/PRO_0000330310 http://togogenome.org/gene/10090:Pask ^@ http://purl.uniprot.org/uniprot/Q8CEE6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylmethionine|||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_0000086481 http://togogenome.org/gene/10090:Stk19 ^@ http://purl.uniprot.org/uniprot/Q9JHN8 ^@ Chain|||Molecule Processing ^@ Chain ^@ Inactive serine/threonine-protein kinase 19 ^@ http://purl.uniprot.org/annotation/PRO_0000072276 http://togogenome.org/gene/10090:Dgcr2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1M6|||http://purl.uniprot.org/uniprot/P98154|||http://purl.uniprot.org/uniprot/Q6P5A9 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ C-type lectin|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Integral membrane protein DGCR2/IDD|||LDL-receptor class A|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues|||VWFC ^@ http://purl.uniprot.org/annotation/PRO_0000021485|||http://purl.uniprot.org/annotation/PRO_5015044318|||http://purl.uniprot.org/annotation/PRO_5015098415 http://togogenome.org/gene/10090:Or5p5 ^@ http://purl.uniprot.org/uniprot/Q7TRV2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hdac11 ^@ http://purl.uniprot.org/uniprot/Q543U1|||http://purl.uniprot.org/uniprot/Q91WA3 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Region ^@ Histone deacetylase|||Histone deacetylase 11 ^@ http://purl.uniprot.org/annotation/PRO_0000114717 http://togogenome.org/gene/10090:Xlr5a ^@ http://purl.uniprot.org/uniprot/A2BI45|||http://purl.uniprot.org/uniprot/A2BI46 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Fbxl7 ^@ http://purl.uniprot.org/uniprot/Q5BJ29 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Disordered|||F-box|||F-box/LRR-repeat protein 7|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000307720 http://togogenome.org/gene/10090:Cfap276 ^@ http://purl.uniprot.org/uniprot/Q9DAD0 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region ^@ Cilia- and flagella-associated protein 276|||Disordered|||Knockin mice develop peripheral neuropathy that mimic the phenotype of intermediate forms of Charcot-Marie-Tooth disease. Knockin mice shown impairments in motor and neuromuscular functions, and aberrant myelination and axonal phenotypes.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000303066 http://togogenome.org/gene/10090:Fgr ^@ http://purl.uniprot.org/uniprot/P14234 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes localization at the cell membrane.|||Interaction with CLNK|||Loss of CLNK binding.|||Loss of kinase activity.|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Protein kinase|||Proton acceptor|||Removed|||S-palmitoyl cysteine|||SH2|||SH3|||Tyrosine-protein kinase Fgr ^@ http://purl.uniprot.org/annotation/PRO_0000088092 http://togogenome.org/gene/10090:Icos ^@ http://purl.uniprot.org/uniprot/Q3V3X2|||http://purl.uniprot.org/uniprot/Q5SUZ7|||http://purl.uniprot.org/uniprot/Q9WVS0 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||Immunoglobulin V-set|||Inducible T-cell costimulator|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000014807|||http://purl.uniprot.org/annotation/PRO_5004230408|||http://purl.uniprot.org/annotation/PRO_5014309972 http://togogenome.org/gene/10090:Nlrp3 ^@ http://purl.uniprot.org/uniprot/Q8R4B8 ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Abolished phosphorylation by JNK1 leading to decreased activation of the NLRP3 inflammasome.|||Abolished phosphorylation by PKD/PRKD1, leading to prevent NLRP3 inflammasome activation.|||FISNA|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In 4KA mutant; abolished binding to phosphatidylinositol 4-phosphate (PtdIns4P) and recruitment to dispersed trans-Golgi network (dTGN) vesicle membranes.|||In LRR6 mutant; does not affect ability to form homooligomeric double-ring cages that hide pyrin domains to avoid premature activation; when associated with E-970 and A-1029.|||In LRR6 mutant; does not affect ability to form homooligomeric double-ring cages that hide pyrin domains to avoid premature activation; when associated with E-970 and R-1001.|||In LRR6 mutant; does not affect ability to form homooligomeric double-ring cages that hide pyrin domains to avoid premature activation; when associated with R-1001 and A-1029.|||In LRRm1 mutant; abolished ability to form homooligomeric double-ring cages that hide pyrin domains to avoid premature activation; when associated with A-830.|||In LRRm1 mutant; abolished ability to form homooligomeric double-ring cages that hide pyrin domains to avoid premature activation; when associated with C-858.|||In LRRm2 mutant; abolished ability to form homooligomeric double-ring cages that hide pyrin domains to avoid premature activation.|||In LRRm3 mutant; abolished ability to form homooligomeric double-ring cages that hide pyrin domains to avoid premature activation.|||In LRRm4 mutant; abolished ability to form homooligomeric double-ring cages that hide pyrin domains to avoid premature activation.|||In LRRm5 mutant; abolished ability to form homooligomeric double-ring cages that hide pyrin domains to avoid premature activation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In linker-mutant; strongly reduced binding to phosphorylated phosphatidylinositides. Abolished ability to form homooligomeric double-ring cages that hide pyrin domains to avoid premature activation.|||Increases interaction with NEK7.|||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|||Mimics phosphorylation state; despite this, does not promote activation of the NLRP3 inflammasome.|||Mimics phosphorylation state; impaired ability to recruit NEK7, leding to decreased activation of the NLRP3 inflammasome.|||NACHT|||NACHT, LRR and PYD domains-containing protein 3|||Phosphoserine|||Phosphoserine; by CSNK1A1|||Phosphoserine; by MAPK8|||Phosphoserine; by PKD/PRKD1|||Phosphotyrosine|||Phosphotyrosine; by BTK|||Pyrin|||Redox-active|||Required for binding to phosphatidylinositol 4-phosphate (PtdIns4P)|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000080887|||http://purl.uniprot.org/annotation/VSP_014925|||http://purl.uniprot.org/annotation/VSP_014926|||http://purl.uniprot.org/annotation/VSP_014927 http://togogenome.org/gene/10090:Cdh22 ^@ http://purl.uniprot.org/uniprot/I6L9J1|||http://purl.uniprot.org/uniprot/Q9WTP5 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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_0000003822|||http://purl.uniprot.org/annotation/PRO_5015094005 http://togogenome.org/gene/10090:Hspb2 ^@ http://purl.uniprot.org/uniprot/Q6P3C8|||http://purl.uniprot.org/uniprot/Q99PR8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ Heat shock protein beta-2|||In isoform 2.|||SHSP|||sHSP ^@ http://purl.uniprot.org/annotation/PRO_0000125934|||http://purl.uniprot.org/annotation/VSP_010160 http://togogenome.org/gene/10090:Mapre1 ^@ http://purl.uniprot.org/uniprot/Q3U4H0|||http://purl.uniprot.org/uniprot/Q61166 ^@ 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|||Region|||Strand|||Turn ^@ APC-binding|||Calponin-homology (CH)|||DCTN1-binding|||Disordered|||EB1 C-terminal|||Interaction with APC|||Interaction with MTUS2/TIP150|||Loss of interaction with APC and DCTN1.|||Microtubule-associated protein RP/EB family member 1|||N-acetylalanine|||N6-acetyllysine|||N6-crotonyllysine|||Partial loss of interaction with APC.|||Phosphoserine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000213417 http://togogenome.org/gene/10090:Mast2 ^@ http://purl.uniprot.org/uniprot/Q60592 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ AGC-kinase C-terminal|||Abolishes LPS-stimulated IL12B synthesis.|||Basic and acidic residues|||Disordered|||Microtubule-associated serine/threonine-protein kinase 2|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086313 http://togogenome.org/gene/10090:Cars2 ^@ http://purl.uniprot.org/uniprot/G3X975|||http://purl.uniprot.org/uniprot/Q8BYM8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict|||Transit Peptide ^@ 'HIGH' region|||'KMSKS' region|||Mitochondrion|||Probable cysteine--tRNA ligase, mitochondrial|||tRNA synthetases class I catalytic ^@ http://purl.uniprot.org/annotation/PRO_0000250739 http://togogenome.org/gene/10090:Tiam2 ^@ http://purl.uniprot.org/uniprot/Q6ZPF3 ^@ 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|||Splice Variant|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-myristoyl glycine|||No change of phosphorylation by Rho-kinase.|||PDZ|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||RBD|||Removed|||Rho guanine nucleotide exchange factor TIAM2|||Slight decrease phosphorylation by Rho-kinase. No change in promoting neurite growth; when associated with A-1662 and A-1668.|||Slight decrease phosphorylation by Rho-kinase. No change in promoting neurite growth; when associated with A-1662 and A-1672.|||Strongly decrease phosphorylation by Rho-kinase. No change in promoting neurite growth; when associated with A-1668 and A-1672. ^@ http://purl.uniprot.org/annotation/PRO_0000317468|||http://purl.uniprot.org/annotation/VSP_030976|||http://purl.uniprot.org/annotation/VSP_030977|||http://purl.uniprot.org/annotation/VSP_030978|||http://purl.uniprot.org/annotation/VSP_030979 http://togogenome.org/gene/10090:Tmem150c ^@ http://purl.uniprot.org/uniprot/Q8C8S3 ^@ Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Affects ion selectivity.|||Cytoplasmic|||Does not affect ion selectivity.|||Extracellular|||Helical|||In isoform 2.|||Transmembrane protein 150C ^@ http://purl.uniprot.org/annotation/PRO_0000395033|||http://purl.uniprot.org/annotation/VSP_039351 http://togogenome.org/gene/10090:Pierce1 ^@ http://purl.uniprot.org/uniprot/Q5BN45 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Piercer of microtubule wall 1 protein ^@ http://purl.uniprot.org/annotation/PRO_0000359780 http://togogenome.org/gene/10090:Ctsk ^@ http://purl.uniprot.org/uniprot/P55097|||http://purl.uniprot.org/uniprot/Q545T0 ^@ 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 K|||Cathepsin propeptide inhibitor|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000026301|||http://purl.uniprot.org/annotation/PRO_0000026302|||http://purl.uniprot.org/annotation/PRO_5014309644 http://togogenome.org/gene/10090:L3mbtl3 ^@ http://purl.uniprot.org/uniprot/Q8BLB7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||CCHHC-type; degenerate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with RBPJ. Required for transcription repressor activity on Notch target genes|||Lethal(3)malignant brain tumor-like protein 3|||MBT 1|||MBT 2|||MBT 3|||Polar residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000084451|||http://purl.uniprot.org/annotation/VSP_013509|||http://purl.uniprot.org/annotation/VSP_013510|||http://purl.uniprot.org/annotation/VSP_013511 http://togogenome.org/gene/10090:Gfi1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J292|||http://purl.uniprot.org/uniprot/H3BJM0|||http://purl.uniprot.org/uniprot/P70338 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Abolishes most of the nuclear localization and reduces transcriptional repressor activity; when associated with A-10.|||Abolishes most of the nuclear localization and reduces transcriptional repressor activity; when associated with A-11.|||Abrogates transcriptional repression. No change in nuclear location.|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Partial loss of transcription repression. No change in nuclear location.|||Phosphoserine|||Required for interaction with RELA|||SNAG domain|||Zinc finger protein Gfi-1 ^@ http://purl.uniprot.org/annotation/PRO_0000047194 http://togogenome.org/gene/10090:Tyk2 ^@ http://purl.uniprot.org/uniprot/E9QJS1|||http://purl.uniprot.org/uniprot/Q9R117 ^@ Active Site|||Binding 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|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Disordered|||FERM|||Non-receptor tyrosine-protein kinase TYK2|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||SH2; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000088178 http://togogenome.org/gene/10090:Akap3 ^@ http://purl.uniprot.org/uniprot/O88987 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict ^@ A-kinase anchor protein 3|||Basic and acidic residues|||Disordered|||PKA-RII subunit binding domain|||Phosphoserine|||Phosphotyrosine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064527 http://togogenome.org/gene/10090:Snd1 ^@ http://purl.uniprot.org/uniprot/Q3TJ56|||http://purl.uniprot.org/uniprot/Q78PY7 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict ^@ 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_0000183181 http://togogenome.org/gene/10090:Them6 ^@ http://purl.uniprot.org/uniprot/Q80ZW2 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Signal Peptide ^@ Chain|||Glycosylation Site|||Modified Residue|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein THEM6 ^@ http://purl.uniprot.org/annotation/PRO_0000285637 http://togogenome.org/gene/10090:Scgb1b20 ^@ http://purl.uniprot.org/uniprot/E9PWZ2 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015090353 http://togogenome.org/gene/10090:Sp5 ^@ http://purl.uniprot.org/uniprot/Q9JHX2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Zinc Finger ^@ 9aaTAD|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Polar residues|||Pro residues|||Transcription factor Sp5 ^@ http://purl.uniprot.org/annotation/PRO_0000047147 http://togogenome.org/gene/10090:Efcab11 ^@ http://purl.uniprot.org/uniprot/Q9D0E5 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand calcium-binding domain-containing protein 11|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000286581|||http://purl.uniprot.org/annotation/VSP_025103 http://togogenome.org/gene/10090:Strap ^@ http://purl.uniprot.org/uniprot/B2RUC7|||http://purl.uniprot.org/uniprot/Q9Z1Z2 ^@ 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|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Serine-threonine kinase receptor-associated protein|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000051231 http://togogenome.org/gene/10090:Irx4 ^@ http://purl.uniprot.org/uniprot/Q9QY61 ^@ 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; TALE-type|||Iroquois-class homeodomain protein IRX-4|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000049158 http://togogenome.org/gene/10090:Or10ak7 ^@ http://purl.uniprot.org/uniprot/B1ARV2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Def8 ^@ http://purl.uniprot.org/uniprot/A0A0R4IZW6|||http://purl.uniprot.org/uniprot/G3X9U5|||http://purl.uniprot.org/uniprot/Q99J78 ^@ 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|||Differentially expressed in FDCP 8|||Disordered|||In isoform 2.|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000321914|||http://purl.uniprot.org/annotation/VSP_031825 http://togogenome.org/gene/10090:Zkscan1 ^@ http://purl.uniprot.org/uniprot/Q8BGS3 ^@ 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 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|||Polar residues|||SCAN box|||Zinc finger protein with KRAB and SCAN domains 1 ^@ http://purl.uniprot.org/annotation/PRO_0000047754|||http://purl.uniprot.org/annotation/VSP_016958 http://togogenome.org/gene/10090:Lamtor1 ^@ http://purl.uniprot.org/uniprot/Q9CQ22 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolished N-myristoylation and subsequent localization to lysosomes.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with LAMTOR2 and LAMTOR3|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Ragulator complex protein LAMTOR1|||Reduces ubiquitination by UBE3A.|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000274293 http://togogenome.org/gene/10090:Nxpe2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0E5|||http://purl.uniprot.org/uniprot/Q3U095 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||NXPE family member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000403788 http://togogenome.org/gene/10090:Ypel2 ^@ http://purl.uniprot.org/uniprot/Q0VA86|||http://purl.uniprot.org/uniprot/Q65Z95 ^@ 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_0000212386 http://togogenome.org/gene/10090:Nup54 ^@ http://purl.uniprot.org/uniprot/Q8BTS4 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ 1|||2|||3|||4|||5|||6|||7|||8|||8 X 2 AA repeats of F-G|||Nuclear pore complex protein Nup54 ^@ http://purl.uniprot.org/annotation/PRO_0000204875 http://togogenome.org/gene/10090:Foxs1 ^@ http://purl.uniprot.org/uniprot/Q4VA05|||http://purl.uniprot.org/uniprot/Q61574 ^@ Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Fork-head|||Forkhead box protein S1 ^@ http://purl.uniprot.org/annotation/PRO_0000091894 http://togogenome.org/gene/10090:Eif5 ^@ http://purl.uniprot.org/uniprot/P59325|||http://purl.uniprot.org/uniprot/Q3TQR3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Site ^@ Arginine finger|||Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||W2 ^@ http://purl.uniprot.org/annotation/PRO_0000212517 http://togogenome.org/gene/10090:Ercc6l2 ^@ http://purl.uniprot.org/uniprot/Q9JIM3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||DEAH box|||DNA excision repair protein ERCC-6-like 2|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000326087|||http://purl.uniprot.org/annotation/VSP_054670|||http://purl.uniprot.org/annotation/VSP_054671|||http://purl.uniprot.org/annotation/VSP_054672|||http://purl.uniprot.org/annotation/VSP_054673|||http://purl.uniprot.org/annotation/VSP_054674|||http://purl.uniprot.org/annotation/VSP_054675|||http://purl.uniprot.org/annotation/VSP_054676 http://togogenome.org/gene/10090:Plac8 ^@ http://purl.uniprot.org/uniprot/Q9JI48 ^@ Chain|||Molecule Processing ^@ Chain ^@ Placenta-specific gene 8 protein ^@ http://purl.uniprot.org/annotation/PRO_0000186093 http://togogenome.org/gene/10090:Alox12e ^@ http://purl.uniprot.org/uniprot/P55249|||http://purl.uniprot.org/uniprot/Q5F2E4 ^@ 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|||Site ^@ Essential for stabilizing binding to COTL1|||In strain:FVB/N.|||Lipoxygenase|||PLAT|||Polyunsaturated fatty acid (12S)/(13S)-lipoxygenase, epidermal-type ^@ http://purl.uniprot.org/annotation/PRO_0000220688 http://togogenome.org/gene/10090:Or51a5 ^@ http://purl.uniprot.org/uniprot/Q8VH13 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn1r107 ^@ http://purl.uniprot.org/uniprot/D3YTY1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Actn3 ^@ http://purl.uniprot.org/uniprot/O88990 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ Actin-binding|||Alpha-actinin-3|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||EF-hand 1|||EF-hand 2|||N-acetylmethionine|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4 ^@ http://purl.uniprot.org/annotation/PRO_0000073439 http://togogenome.org/gene/10090:Thap11 ^@ http://purl.uniprot.org/uniprot/Q9JJD0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Zinc Finger ^@ Disordered|||HCFC1-binding motif (HBM)|||Polar residues|||THAP domain-containing protein 11|||THAP-type ^@ http://purl.uniprot.org/annotation/PRO_0000068654 http://togogenome.org/gene/10090:Mgp ^@ http://purl.uniprot.org/uniprot/P19788 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ 4-carboxyglutamate|||Gla|||Matrix Gla protein|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000011111 http://togogenome.org/gene/10090:Nceh1 ^@ http://purl.uniprot.org/uniprot/Q8BLF1 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Motif|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||Neutral cholesterol ester hydrolase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000265940 http://togogenome.org/gene/10090:Bfsp2 ^@ http://purl.uniprot.org/uniprot/Q6NVD9 ^@ 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 ^@ Disordered|||Head|||IF rod|||In isoform 2.|||N-acetylserine|||Phakinin|||Phosphoserine|||Polar residues|||Removed|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063852|||http://purl.uniprot.org/annotation/VSP_011111 http://togogenome.org/gene/10090:Ces3b ^@ http://purl.uniprot.org/uniprot/Q8VCU1 ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Signal Peptide|||Splice Variant ^@ Acyl-ester intermediate|||Carboxylesterase 3B|||Charge relay system|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000305195|||http://purl.uniprot.org/annotation/VSP_028269 http://togogenome.org/gene/10090:Msrb3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J139|||http://purl.uniprot.org/uniprot/Q8BU85 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Signal Peptide ^@ Disordered|||Endoplasmic reticulum retention signal|||Methionine-R-sulfoxide reductase B3, mitochondrial|||MsrB|||N6-acetyllysine|||Nucleophile|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000327241 http://togogenome.org/gene/10090:Gramd1b ^@ http://purl.uniprot.org/uniprot/Q80TI0 ^@ 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 ^@ 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_0000287450|||http://purl.uniprot.org/annotation/VSP_025473|||http://purl.uniprot.org/annotation/VSP_025474|||http://purl.uniprot.org/annotation/VSP_025475|||http://purl.uniprot.org/annotation/VSP_025476 http://togogenome.org/gene/10090:Cyp2c40 ^@ http://purl.uniprot.org/uniprot/E9Q7C8|||http://purl.uniprot.org/uniprot/P56657 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Signal Peptide|||Transmembrane ^@ Cytochrome P450 2C40|||Helical|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051723 http://togogenome.org/gene/10090:Tlcd3a ^@ http://purl.uniprot.org/uniprot/Q3TVE0|||http://purl.uniprot.org/uniprot/Q5ND56 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Transmembrane ^@ Helical|||TLC|||TLC domain-containing protein 3A ^@ http://purl.uniprot.org/annotation/PRO_0000185541 http://togogenome.org/gene/10090:Lrig2 ^@ http://purl.uniprot.org/uniprot/B2RRI5|||http://purl.uniprot.org/uniprot/Q52KR2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Repeat|||Signal Peptide|||Splice Variant|||Transmembrane ^@ 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 2|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000014830|||http://purl.uniprot.org/annotation/PRO_5015087158|||http://purl.uniprot.org/annotation/VSP_014993|||http://purl.uniprot.org/annotation/VSP_057113 http://togogenome.org/gene/10090:Rhbdd1 ^@ http://purl.uniprot.org/uniprot/Q8BHC7 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Enzyme inactivation. Reduces the cleavage of PTCRA and TRAC. Does not inhibit interaction with PTCRA. Stimulates interaction with ubiquitinated proteins.|||Helical|||Inhibits interaction with ubiquitin and ubiquitinated proteins; when associated with A-274. Reduces the cleavage of PTCRA; when associated with A-274.|||Inhibits interaction with ubiquitin and ubiquitinated proteins; when associated with A-278. Reduces the cleavage of PTCRA; when associated with A-278.|||Lumenal|||Nucleophile|||Rhomboid-related protein 4|||Ubiquitin-binding domain (UBD)|||VCP/p97-interacting motif (VIM) ^@ http://purl.uniprot.org/annotation/PRO_0000254190 http://togogenome.org/gene/10090:Gpr26 ^@ http://purl.uniprot.org/uniprot/Q0VBG4|||http://purl.uniprot.org/uniprot/Q8BZA7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||G-protein coupled receptor 26|||G-protein coupled receptors family 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_0000069546 http://togogenome.org/gene/10090:Gimap8 ^@ http://purl.uniprot.org/uniprot/A0A0R3P9C7|||http://purl.uniprot.org/uniprot/Q75N62 ^@ 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 ^@ AIG1-type G|||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_0000341971 http://togogenome.org/gene/10090:Mrpl37 ^@ http://purl.uniprot.org/uniprot/Q921S7 ^@ Chain|||Molecule Processing|||Transit Peptide ^@ Chain|||Transit Peptide ^@ Large ribosomal subunit protein mL37|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000045906 http://togogenome.org/gene/10090:Ube2d3 ^@ http://purl.uniprot.org/uniprot/P61079|||http://purl.uniprot.org/uniprot/Q4QQL2 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent ^@ Glycyl thioester intermediate|||UBC core|||Ubiquitin-conjugating enzyme E2 D3 ^@ http://purl.uniprot.org/annotation/PRO_0000082467 http://togogenome.org/gene/10090:Angptl3 ^@ http://purl.uniprot.org/uniprot/Q3UEF5|||http://purl.uniprot.org/uniprot/Q9R182 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide ^@ ANGPTL3(17-224)|||Abolishes proteolytical cleavage.|||Angiopoietin-related protein 3|||Disordered|||Fibrinogen C-terminal|||Fibrinogen C-terminal domain-containing protein|||N-linked (GlcNAc...) asparagine|||O-linked (GlcNAc) threonine|||Polar residues|||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_0000009123|||http://purl.uniprot.org/annotation/PRO_0000435905|||http://purl.uniprot.org/annotation/PRO_5014309219 http://togogenome.org/gene/10090:Sfmbt1 ^@ http://purl.uniprot.org/uniprot/Q3TUT9|||http://purl.uniprot.org/uniprot/Q9JMD1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat ^@ Acidic residues|||Basic residues|||Disordered|||MBT|||MBT 1|||MBT 2|||MBT 3|||MBT 4|||Phosphoserine|||Polar residues|||SAM|||SLED|||Scm-like with four MBT domains protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000071967 http://togogenome.org/gene/10090:Fbf1 ^@ http://purl.uniprot.org/uniprot/A2A870|||http://purl.uniprot.org/uniprot/B7ZN01 ^@ 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|||Fas-binding factor 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000297647|||http://purl.uniprot.org/annotation/VSP_027324 http://togogenome.org/gene/10090:Pkd2l1 ^@ http://purl.uniprot.org/uniprot/A2A259 ^@ 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|||Region|||Secondary Structure|||Sequence Conflict|||Site|||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|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||EF-hand|||Extracellular|||Helical|||Impaired calcium channel activity.|||Increases localization at the cell surface when expressed in absence of PKD1.|||Induces localization to the endoplasmic reticulum when expressed in absence of PKD1.|||Little or no effect on calcium channel activity.|||Loss of activation by low pH.|||Loss of channel activity.|||N-linked (GlcNAc...) asparagine|||No effect on activation by low pH.|||Polar residues|||Polycystin-2-like protein 1|||Pore-forming|||Required for homooligomerization|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000425551 http://togogenome.org/gene/10090:Sh2d4b ^@ http://purl.uniprot.org/uniprot/A6X942 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||SH2|||SH2 domain-containing protein 4B ^@ http://purl.uniprot.org/annotation/PRO_0000308601|||http://purl.uniprot.org/annotation/VSP_029013 http://togogenome.org/gene/10090:Rab25 ^@ http://purl.uniprot.org/uniprot/Q9WTL2 ^@ 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 Rab-25|||Removed in mature form|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121216|||http://purl.uniprot.org/annotation/PRO_0000370822 http://togogenome.org/gene/10090:Pacsin2 ^@ http://purl.uniprot.org/uniprot/Q3TDA7|||http://purl.uniprot.org/uniprot/Q8BNK9|||http://purl.uniprot.org/uniprot/Q9WVE8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Strand|||Turn ^@ Decreases affinity for membranes.|||Disordered|||F-BAR|||Loss of DNM1-, SYNJ1- and WASL-binding.|||N6-acetyllysine|||NPF1|||NPF2|||NPF3|||Nearly abolishes membrane tubulation activity.|||Phosphoserine|||Phosphoserine; by IKKB|||Phosphoserine; by PKC|||Polar residues|||Protein kinase C and casein kinase substrate in neurons protein 2|||Reduced membrane-binding affinity.|||SH3|||Slight decrease in affinity for membranes. Nearly abolishes membrane tubulation activity.|||Slight increase in affinity for membranes. Increases membrane tubulation activity. ^@ http://purl.uniprot.org/annotation/PRO_0000161796 http://togogenome.org/gene/10090:Pmepa1 ^@ http://purl.uniprot.org/uniprot/A2APF4 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Msto1 ^@ http://purl.uniprot.org/uniprot/E9PUB7|||http://purl.uniprot.org/uniprot/Q2YDW2 ^@ 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 ^@ DML1/Misato tubulin|||In isoform 2.|||Misato Segment II tubulin-like|||Phosphoserine|||Protein misato homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000304628|||http://purl.uniprot.org/annotation/VSP_028057 http://togogenome.org/gene/10090:Mapk7 ^@ http://purl.uniprot.org/uniprot/Q5NCN8|||http://purl.uniprot.org/uniprot/Q9WVS8 ^@ Active Site|||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 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||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_0000186261|||http://purl.uniprot.org/annotation/VSP_035201|||http://purl.uniprot.org/annotation/VSP_035202|||http://purl.uniprot.org/annotation/VSP_035203|||http://purl.uniprot.org/annotation/VSP_035204 http://togogenome.org/gene/10090:Ppm1e ^@ http://purl.uniprot.org/uniprot/B2KGP3|||http://purl.uniprot.org/uniprot/Q80TL0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 1|||2|||3|||4; approximate|||5|||6|||7|||7 X 2 AA tandem repeats of P-E|||Acidic residues|||Basic and acidic residues|||Disordered|||PPM-type phosphatase|||Phosphoserine|||Pro residues|||Protein phosphatase 1E ^@ http://purl.uniprot.org/annotation/PRO_0000286821 http://togogenome.org/gene/10090:Or52r1c ^@ http://purl.uniprot.org/uniprot/Q8VGW0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp488 ^@ http://purl.uniprot.org/uniprot/Q5HZG9 ^@ Chain|||Molecule Processing|||Motif|||Region|||Zinc Finger ^@ Chain|||Motif|||Region|||Zinc Finger ^@ C2H2-type 1|||C2H2-type 2|||Disordered|||Important for transcriptional repression activity|||Nuclear localization signal|||Zinc finger protein 488 ^@ http://purl.uniprot.org/annotation/PRO_0000353090 http://togogenome.org/gene/10090:Defb36 ^@ http://purl.uniprot.org/uniprot/Q8K3U4 ^@ Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Signal Peptide ^@ Disulfide Bond|||Peptide|||Signal Peptide ^@ Beta-defensin 36 ^@ http://purl.uniprot.org/annotation/PRO_0000006948 http://togogenome.org/gene/10090:Psg20 ^@ http://purl.uniprot.org/uniprot/E9Q9B4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ig-like ^@ http://togogenome.org/gene/10090:Arfgef3 ^@ http://purl.uniprot.org/uniprot/Q3UGY8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||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_0000286672 http://togogenome.org/gene/10090:Spint2 ^@ http://purl.uniprot.org/uniprot/Q9D8Q8|||http://purl.uniprot.org/uniprot/Q9WU03 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ BPTI/Kunitz inhibitor|||BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||BPTI/Kunitz inhibitor domain-containing protein|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Kunitz-type protease inhibitor 2|||N-linked (GlcNAc...) asparagine|||Reactive bond ^@ http://purl.uniprot.org/annotation/PRO_0000016886|||http://purl.uniprot.org/annotation/PRO_5004324576|||http://purl.uniprot.org/annotation/VSP_003034|||http://purl.uniprot.org/annotation/VSP_003035|||http://purl.uniprot.org/annotation/VSP_003036 http://togogenome.org/gene/10090:Ppp1r32 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0F3|||http://purl.uniprot.org/uniprot/Q148A4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||Stabilizer of axonemal microtubules 4 ^@ http://purl.uniprot.org/annotation/PRO_0000274378 http://togogenome.org/gene/10090:Leprotl1 ^@ http://purl.uniprot.org/uniprot/Q9CQ74 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Leptin receptor overlapping transcript-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000215198 http://togogenome.org/gene/10090:Rasef ^@ http://purl.uniprot.org/uniprot/A0A1D8RIR4|||http://purl.uniprot.org/uniprot/Q5RI75 ^@ Binding Site|||Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Phosphoserine|||Ras and EF-hand domain-containing protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000299578|||http://purl.uniprot.org/annotation/VSP_027768 http://togogenome.org/gene/10090:Ybey ^@ http://purl.uniprot.org/uniprot/Q8CAV0 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Endoribonuclease YbeY ^@ http://purl.uniprot.org/annotation/PRO_0000102579 http://togogenome.org/gene/10090:Vmn2r78 ^@ http://purl.uniprot.org/uniprot/K7N6U5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003910734 http://togogenome.org/gene/10090:Or6c1b ^@ http://purl.uniprot.org/uniprot/Q8VFH8 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Abraxas2 ^@ http://purl.uniprot.org/uniprot/Q3TCJ1|||http://purl.uniprot.org/uniprot/Z4YJY0 ^@ 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 ^@ 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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000050726 http://togogenome.org/gene/10090:Txndc12 ^@ http://purl.uniprot.org/uniprot/Q9CQU0 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Redox-active|||Thioredoxin domain-containing protein 12 ^@ http://purl.uniprot.org/annotation/PRO_0000034190 http://togogenome.org/gene/10090:Esp1 ^@ http://purl.uniprot.org/uniprot/Q3LHH8 ^@ Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Signal Peptide|||Site|||Strand ^@ Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Signal Peptide|||Site|||Strand ^@ Exocrine gland-secreted peptide 1|||No neuron activity in the VNO and marked reduction in the accessory olfactory bulb.|||No neuron activity in the VNO.|||Reduced neuron activity in the VNO.|||Required for activity ^@ http://purl.uniprot.org/annotation/PRO_0000424697 http://togogenome.org/gene/10090:Cad ^@ http://purl.uniprot.org/uniprot/B2RQC6|||http://purl.uniprot.org/uniprot/G3UWN2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant ^@ ATCase (Aspartate transcarbamylase)|||ATP-grasp|||ATP-grasp 1|||ATP-grasp 2|||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 isoform 2.|||Linker|||MGS-like|||N-acetylalanine|||N6-acetyllysine|||N6-carboxylysine|||Nucleophile|||Nucleophile; for GATase activity|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Removed|||via carbamate group ^@ http://purl.uniprot.org/annotation/PRO_0000425955|||http://purl.uniprot.org/annotation/VSP_053912 http://togogenome.org/gene/10090:Nat8f6 ^@ http://purl.uniprot.org/uniprot/Q9JIY8 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ Helical|||N-acetyltransferase|||N-acetyltransferase family 8 member 3 ^@ http://purl.uniprot.org/annotation/PRO_0000284690 http://togogenome.org/gene/10090:Hcrtr1 ^@ http://purl.uniprot.org/uniprot/P58307|||http://purl.uniprot.org/uniprot/Q0VDP6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||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|||Important for responses to orexin|||N-linked (GlcNAc...) asparagine|||Orexin/Hypocretin receptor type 1|||Required for response to orexin-A ^@ http://purl.uniprot.org/annotation/PRO_0000069985 http://togogenome.org/gene/10090:Slc28a2b ^@ http://purl.uniprot.org/uniprot/A2AWR5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Concentrative nucleoside transporter C-terminal|||Concentrative nucleoside transporter N-terminal|||Helical|||Nucleoside transporter/FeoB GTPase Gate ^@ http://togogenome.org/gene/10090:Ltb ^@ http://purl.uniprot.org/uniprot/A0A0U5JAA2|||http://purl.uniprot.org/uniprot/P41155 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lymphotoxin-beta|||N-linked (GlcNAc...) asparagine|||Polar residues|||TNF family profile ^@ http://purl.uniprot.org/annotation/PRO_0000185490 http://togogenome.org/gene/10090:Camsap3 ^@ http://purl.uniprot.org/uniprot/Q80VC9 ^@ 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 ^@ Basic and acidic residues|||CKK|||Calmodulin-regulated spectrin-associated protein 3|||Calponin-homology (CH)|||Disordered|||In isoform 10, isoform 11, isoform 12, isoform 13, isoform 14, isoform 15, isoform 16 and isoform 17.|||In isoform 2.|||In isoform 3, isoform 6, isoform 12 and isoform 15.|||In isoform 4, isoform 7, isoform 11 and isoform 16.|||In isoform 5, isoform 8, isoform 14 and isoform 17.|||In isoform 6, isoform 7, isoform 8, isoform 9, isoform 13, isoform 15, isoform 16 and isoform 17.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Retains the ability to interact with microtubules but abolishes the apical localization in epithelial cells. ^@ http://purl.uniprot.org/annotation/PRO_0000050800|||http://purl.uniprot.org/annotation/VSP_013705|||http://purl.uniprot.org/annotation/VSP_059237|||http://purl.uniprot.org/annotation/VSP_059238|||http://purl.uniprot.org/annotation/VSP_059239|||http://purl.uniprot.org/annotation/VSP_059240|||http://purl.uniprot.org/annotation/VSP_059241 http://togogenome.org/gene/10090:Tas2r114 ^@ http://purl.uniprot.org/uniprot/Q7M722 ^@ 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 114 ^@ http://purl.uniprot.org/annotation/PRO_0000248473 http://togogenome.org/gene/10090:Or52s1b ^@ http://purl.uniprot.org/uniprot/Q7TRR7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp524 ^@ http://purl.uniprot.org/uniprot/Q9D0B1 ^@ 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|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Polar residues|||Zinc finger protein 524 ^@ http://purl.uniprot.org/annotation/PRO_0000234580 http://togogenome.org/gene/10090:Sugp2 ^@ http://purl.uniprot.org/uniprot/Q8CH09 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant ^@ Acidic residues|||Disordered|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In strain: FVB/N.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||SURP and G-patch domain-containing protein 2|||SURP motif 1|||SURP motif 2 ^@ http://purl.uniprot.org/annotation/PRO_0000097709 http://togogenome.org/gene/10090:Fmo4 ^@ http://purl.uniprot.org/uniprot/Q8VHG0 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Transmembrane ^@ Dimethylaniline monooxygenase [N-oxide-forming] 4|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000147661 http://togogenome.org/gene/10090:Vkorc1l1 ^@ http://purl.uniprot.org/uniprot/A0A0M3HEP8|||http://purl.uniprot.org/uniprot/Q6TEK5 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Redox-active|||Vitamin K epoxide reductase|||Vitamin K epoxide reductase complex subunit 1-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000191672 http://togogenome.org/gene/10090:Cldnd2 ^@ http://purl.uniprot.org/uniprot/A1A539|||http://purl.uniprot.org/uniprot/Q9D9H2 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Claudin domain-containing protein 2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000271021 http://togogenome.org/gene/10090:Rps2 ^@ http://purl.uniprot.org/uniprot/P25444|||http://purl.uniprot.org/uniprot/Q58EU3 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ 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)|||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_0000131674 http://togogenome.org/gene/10090:Ankfn1 ^@ http://purl.uniprot.org/uniprot/Q8CDJ6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Irgm1 ^@ http://purl.uniprot.org/uniprot/J7NUP1|||http://purl.uniprot.org/uniprot/Q60766 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant ^@ Abolished lipid-binding and subsequent recruitment to phagosome membranes, leading to impaired innate immunity.|||Abolished palmitoylation and localization to membranes.|||Abolished ubiquitination by the DCX(WDR77) complex.|||Alpha-K amphipathic helix|||Decreased lipid-binding.|||Disrupts amphipathicity and abolishes Golgi localization; when associated with Glu-362.|||Disrupts amphipathicity and abolishes Golgi localization; when associated with Glu-367.|||Does not affect palmitoylation.|||Does not affect ubiquitination by the DCX(WDR77) complex.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||IRG-type G|||Immunity-related GTPase family M protein 1|||In isoform 2.|||Loss of targeting to plasma membrane and phagosomes.|||No effect on subcellular location.|||No effect on subcellular location. Abolishes Golgi and lysosomal localization; when associated with A-360 or A-367.|||No effect on subcellular location. Abolishes Golgi and lysosomal localization; when associated with A-364.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000325750|||http://purl.uniprot.org/annotation/VSP_032384 http://togogenome.org/gene/10090:Foxk2 ^@ http://purl.uniprot.org/uniprot/Q3UCQ1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ DNA-binding; major groove|||DNA-binding; minor groove|||Disordered|||FHA|||Fork-head|||Forkhead box protein K2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Required for interaction with DVL2 and SUDS3 ^@ http://purl.uniprot.org/annotation/PRO_0000261668|||http://purl.uniprot.org/annotation/VSP_052236 http://togogenome.org/gene/10090:Psmd5 ^@ http://purl.uniprot.org/uniprot/Q8BJY1 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ 26S proteasome non-ATPase regulatory subunit 5|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000173837 http://togogenome.org/gene/10090:Actg2 ^@ http://purl.uniprot.org/uniprot/P63268 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ Actin, gamma-enteric smooth muscle|||Actin, gamma-enteric smooth muscle, intermediate form|||Methionine (R)-sulfoxide|||N-acetylcysteine; in intermediate form|||Removed|||Tele-methylhistidine ^@ http://purl.uniprot.org/annotation/PRO_0000442951|||http://purl.uniprot.org/annotation/PRO_0000442952 http://togogenome.org/gene/10090:Gprin1 ^@ http://purl.uniprot.org/uniprot/Q3UNH4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolishes membrane targeting.|||Basic and acidic residues|||Disordered|||G protein-regulated inducer of neurite outgrowth 1|||Interaction with GNAO1|||Phosphoserine|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000235978 http://togogenome.org/gene/10090:Polr1g ^@ http://purl.uniprot.org/uniprot/Q76KJ5 ^@ 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|||DNA-directed RNA polymerase I subunit RPA34|||Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000228121 http://togogenome.org/gene/10090:Samsn1 ^@ http://purl.uniprot.org/uniprot/P57725 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Turn ^@ Basic and acidic residues|||Disordered|||Important for interaction with 14-3-3 proteins|||Loss of phosphorylation site. Strongly reduced interaction with YWHAG and YWHAB.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SAM|||SAM domain-containing protein SAMSN-1|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000097575 http://togogenome.org/gene/10090:Irag1 ^@ http://purl.uniprot.org/uniprot/Q3UR44|||http://purl.uniprot.org/uniprot/Q9WUX5 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Inositol 1,4,5-triphosphate receptor associated 1|||Interaction with ITPR1|||Interaction with PRKG1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000305293|||http://purl.uniprot.org/annotation/VSP_028343 http://togogenome.org/gene/10090:Skint10 ^@ http://purl.uniprot.org/uniprot/A7TZG1 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Selection and upkeep of intraepithelial T-cells protein 10 ^@ http://purl.uniprot.org/annotation/PRO_5000270116 http://togogenome.org/gene/10090:Tmprss6 ^@ http://purl.uniprot.org/uniprot/Q9DBI0 ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||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|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Protease-dead.|||SEA|||Transmembrane protease serine 6 ^@ http://purl.uniprot.org/annotation/PRO_0000088697|||http://purl.uniprot.org/annotation/VSP_035564|||http://purl.uniprot.org/annotation/VSP_035565|||http://purl.uniprot.org/annotation/VSP_035566|||http://purl.uniprot.org/annotation/VSP_035567 http://togogenome.org/gene/10090:Ccp110 ^@ http://purl.uniprot.org/uniprot/Q7TSH4 ^@ 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|||CEP97 binding|||Calmodulin-binding|||Centriolar coiled-coil protein of 110 kDa|||Disordered|||Interaction with CEP76|||Phosphoserine|||Polar residues|||Required for interaction with CEP290 ^@ http://purl.uniprot.org/annotation/PRO_0000089461 http://togogenome.org/gene/10090:Rps19 ^@ http://purl.uniprot.org/uniprot/Q9CZX8 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ N6-acetyllysine|||N6-succinyllysine|||Omega-N-methylarginine|||Small ribosomal subunit protein eS19 ^@ http://purl.uniprot.org/annotation/PRO_0000153811 http://togogenome.org/gene/10090:Cep41 ^@ http://purl.uniprot.org/uniprot/Q99NF3 ^@ 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 ^@ Centrosomal protein of 41 kDa|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rhodanese ^@ http://purl.uniprot.org/annotation/PRO_0000089490|||http://purl.uniprot.org/annotation/VSP_012249|||http://purl.uniprot.org/annotation/VSP_012250 http://togogenome.org/gene/10090:Endog ^@ http://purl.uniprot.org/uniprot/O08600|||http://purl.uniprot.org/uniprot/Q3UN47 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Transit Peptide|||Turn ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Strand|||Transit Peptide|||Turn ^@ Catalytically inactive.|||DNA/RNA non-specific endonuclease|||Endonuclease|||Endonuclease G, mitochondrial|||Essential for catalytic activity|||Essential for deoxyribonuclease activity|||Extracellular Endonuclease subunit A|||Interchain|||Loss of deoxyribonuclease activity.|||Loss of homodimerization and deoxyribonuclease activity. Shows a 1.3-fold higher rate for the cleavage of the 5hmC-modified DNA junction over unmodified junction, as compared to the 1.8-fold difference seen in the wild type enzyme.|||Mitochondrion|||Phosphothreonine|||Proton acceptor|||Shows a 2.1-fold higher rate for the cleavage of the 5hmC-modified DNA junction over unmodified junction, as compared to the 1.8-fold difference seen in the wild type enzyme. ^@ http://purl.uniprot.org/annotation/PRO_0000019919|||http://purl.uniprot.org/annotation/PRO_5014309171 http://togogenome.org/gene/10090:Gm14692 ^@ http://purl.uniprot.org/uniprot/A2BH01 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Usp17la ^@ http://purl.uniprot.org/uniprot/Q61068 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region ^@ Disordered|||Loss of activity.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein A ^@ http://purl.uniprot.org/annotation/PRO_0000080683 http://togogenome.org/gene/10090:Cr1l ^@ http://purl.uniprot.org/uniprot/Q64735 ^@ 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 ^@ Complement component receptor 1-like protein|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5 ^@ http://purl.uniprot.org/annotation/PRO_0000238978|||http://purl.uniprot.org/annotation/VSP_019050 http://togogenome.org/gene/10090:Fas ^@ http://purl.uniprot.org/uniprot/P25446 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Death|||Disordered|||Extracellular|||Helical|||In lpr.|||Interaction with CALM|||Interaction with HIPK3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 6 ^@ http://purl.uniprot.org/annotation/PRO_0000034567 http://togogenome.org/gene/10090:Or6c75 ^@ http://purl.uniprot.org/uniprot/Q8VGJ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Usp31 ^@ http://purl.uniprot.org/uniprot/E9Q6Y8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||USP ^@ http://togogenome.org/gene/10090:4921536K21Rik ^@ http://purl.uniprot.org/uniprot/Q9CR34 ^@ 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 C5orf52 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000341211|||http://purl.uniprot.org/annotation/VSP_034220 http://togogenome.org/gene/10090:Adat3 ^@ http://purl.uniprot.org/uniprot/Q6PAT0 ^@ 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 ^@ CMP/dCMP-type deaminase|||Disordered|||N-acetylmethionine|||Probable inactive tRNA-specific adenosine deaminase-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000287659 http://togogenome.org/gene/10090:Cacna2d3 ^@ http://purl.uniprot.org/uniprot/A0A411ACY3|||http://purl.uniprot.org/uniprot/Q9Z1L5 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cache|||Cytoplasmic|||Extracellular|||Helical|||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_0000304649|||http://purl.uniprot.org/annotation/PRO_0000304650|||http://purl.uniprot.org/annotation/PRO_0000304651|||http://purl.uniprot.org/annotation/PRO_5019179529 http://togogenome.org/gene/10090:Adgrb3 ^@ http://purl.uniprot.org/uniprot/Q6ZQ96|||http://purl.uniprot.org/uniprot/Q80ZF8|||http://purl.uniprot.org/uniprot/Q8BJ13|||http://purl.uniprot.org/uniprot/Q8K0A3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Adhesion G protein-coupled receptor B3|||CUB|||Cytoplasmic|||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|||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_0000012866 http://togogenome.org/gene/10090:Nodal ^@ http://purl.uniprot.org/uniprot/P43021 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Interchain|||N-linked (GlcNAc...) asparagine|||Nodal ^@ http://purl.uniprot.org/annotation/PRO_0000034000|||http://purl.uniprot.org/annotation/PRO_0000034001 http://togogenome.org/gene/10090:Herc4 ^@ http://purl.uniprot.org/uniprot/Q6PAV2 ^@ 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.|||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_0000278217|||http://purl.uniprot.org/annotation/VSP_023180|||http://purl.uniprot.org/annotation/VSP_023181|||http://purl.uniprot.org/annotation/VSP_023182 http://togogenome.org/gene/10090:Dph2 ^@ http://purl.uniprot.org/uniprot/Q9CR25 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict ^@ 2-(3-amino-3-carboxypropyl)histidine synthase subunit 2|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000307890 http://togogenome.org/gene/10090:Zfyve28 ^@ http://purl.uniprot.org/uniprot/Q6ZPK7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||FYVE-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Lateral signaling target protein 2 homolog|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAP2K|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000378953 http://togogenome.org/gene/10090:Gnpat ^@ http://purl.uniprot.org/uniprot/P98192|||http://purl.uniprot.org/uniprot/Q545P6|||http://purl.uniprot.org/uniprot/Q9CT84 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue ^@ Dihydroxyacetone phosphate acyltransferase|||GPAT/DHAPAT C-terminal|||HXXXXD motif|||Microbody targeting signal|||N6-acetyllysine|||Phospholipid/glycerol acyltransferase|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000195247 http://togogenome.org/gene/10090:Tbrg4 ^@ http://purl.uniprot.org/uniprot/Q91YM4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ FAST kinase domain-containing protein 4|||In isoform 2.|||Mitochondrion|||RAP ^@ http://purl.uniprot.org/annotation/PRO_0000273027|||http://purl.uniprot.org/annotation/VSP_022461 http://togogenome.org/gene/10090:Atp5d ^@ http://purl.uniprot.org/uniprot/D3Z7S4|||http://purl.uniprot.org/uniprot/Q4FK74|||http://purl.uniprot.org/uniprot/Q9D3D9 ^@ Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Transit Peptide ^@ ATP synthase F1 complex delta/epsilon subunit N-terminal|||ATP synthase subunit delta, mitochondrial|||Disordered|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000002662 http://togogenome.org/gene/10090:Spry4 ^@ http://purl.uniprot.org/uniprot/Q9WTP2 ^@ 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|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein sprouty homolog 4|||SPR ^@ http://purl.uniprot.org/annotation/PRO_0000076906 http://togogenome.org/gene/10090:Or2ak7 ^@ http://purl.uniprot.org/uniprot/Q7TRZ4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Kdsr ^@ http://purl.uniprot.org/uniprot/Q6GV12 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Signal Peptide|||Topological Domain|||Transmembrane ^@ 3-ketodihydrosphingosine reductase|||Cytoplasmic|||Helical|||Lumenal|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000031983 http://togogenome.org/gene/10090:Stat5b ^@ http://purl.uniprot.org/uniprot/P42232 ^@ 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 ^@ Fails to interact with INSR.|||In strain: NOD; reduces DNA-binding affinity.|||Phosphoserine|||Phosphotyrosine|||SH2|||Signal transducer and activator of transcription 5B ^@ http://purl.uniprot.org/annotation/PRO_0000182430 http://togogenome.org/gene/10090:Kat8 ^@ http://purl.uniprot.org/uniprot/Q9D1P2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ C2HC MYST-type|||Disordered|||Histone acetyltransferase KAT8|||In isoform 2.|||MYST-type HAT|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; by autocatalysis|||Phosphoserine|||Proton donor/acceptor|||Removed|||Sufficient for interaction with KANSL1|||Tudor-knot ^@ http://purl.uniprot.org/annotation/PRO_0000051567|||http://purl.uniprot.org/annotation/VSP_014580|||http://purl.uniprot.org/annotation/VSP_014581 http://togogenome.org/gene/10090:C1qbp ^@ http://purl.uniprot.org/uniprot/Q8R5L1 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Fam193b ^@ http://purl.uniprot.org/uniprot/Q3U2K0 ^@ 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 ^@ Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues|||Protein FAM193B ^@ http://purl.uniprot.org/annotation/PRO_0000344458|||http://purl.uniprot.org/annotation/VSP_034781|||http://purl.uniprot.org/annotation/VSP_034782 http://togogenome.org/gene/10090:Npbwr1 ^@ http://purl.uniprot.org/uniprot/P49681 ^@ 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|||Neuropeptides B/W receptor type 1 ^@ http://purl.uniprot.org/annotation/PRO_0000069519 http://togogenome.org/gene/10090:Trnt1 ^@ http://purl.uniprot.org/uniprot/Q8K1J6 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ CCA tRNA nucleotidyltransferase 1, mitochondrial|||In isoform 2.|||Involved in nucleotide selection|||May assist in discriminating ATP from CTP|||Mitochondrion|||N6-acetyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000004783|||http://purl.uniprot.org/annotation/VSP_018616|||http://purl.uniprot.org/annotation/VSP_018617 http://togogenome.org/gene/10090:Scgb2b21 ^@ http://purl.uniprot.org/uniprot/A0A087WQA9 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015029548 http://togogenome.org/gene/10090:Prl8a1 ^@ http://purl.uniprot.org/uniprot/Q9DAV8 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Gnal ^@ http://purl.uniprot.org/uniprot/Q3TY78|||http://purl.uniprot.org/uniprot/Q66L47|||http://purl.uniprot.org/uniprot/Q8BHK8|||http://purl.uniprot.org/uniprot/Q8CGK7 ^@ 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 ^@ Basic and acidic residues|||Disordered|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(olf) subunit alpha|||N-palmitoyl glycine|||Phosphothreonine|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000203733 http://togogenome.org/gene/10090:Tef ^@ http://purl.uniprot.org/uniprot/Q9JLC6 ^@ 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 motif|||Disordered|||In isoform 2.|||In isoform Beta.|||Leucine-zipper|||Phosphoserine|||Polar residues|||Thyrotroph embryonic factor|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076513|||http://purl.uniprot.org/annotation/VSP_011245|||http://purl.uniprot.org/annotation/VSP_011246 http://togogenome.org/gene/10090:Panx3 ^@ http://purl.uniprot.org/uniprot/Q6IMP0|||http://purl.uniprot.org/uniprot/Q8CEG0 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Impairs glycosylation.|||N-linked (GlcNAc...) asparagine|||Pannexin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000208492 http://togogenome.org/gene/10090:Gm3411 ^@ http://purl.uniprot.org/uniprot/Q8C7R2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disks large homolog 5 N-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cyp2c39 ^@ http://purl.uniprot.org/uniprot/P56656 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Sequence Conflict|||Signal Peptide ^@ Cytochrome P450 2C39|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051722 http://togogenome.org/gene/10090:Nudt5 ^@ http://purl.uniprot.org/uniprot/Q9JKX6 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict ^@ ADP-sugar pyrophosphatase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||N6-acetyllysine|||Nudix box|||Nudix hydrolase|||Phosphoserine|||Phosphothreonine|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000057049 http://togogenome.org/gene/10090:Adi1 ^@ http://purl.uniprot.org/uniprot/Q99JT9 ^@ Binding Site|||Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Helix|||Region|||Strand|||Turn ^@ Acireductone dioxygenase|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000162943 http://togogenome.org/gene/10090:Egln3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0H9|||http://purl.uniprot.org/uniprot/Q91UZ4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict ^@ Beta(2)beta(3) 'finger-like' loop|||Fe2OG dioxygenase|||Prolyl hydroxylase EGLN3|||Required for interaction with ADRB2 ^@ http://purl.uniprot.org/annotation/PRO_0000206667 http://togogenome.org/gene/10090:Vnn1 ^@ http://purl.uniprot.org/uniprot/Q9Z0K8 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ CN hydrolase|||GPI-anchor amidated asparagine|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Pantetheinase|||Proton acceptor|||Proton donor|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000019714|||http://purl.uniprot.org/annotation/PRO_0000019715 http://togogenome.org/gene/10090:Col6a2 ^@ http://purl.uniprot.org/uniprot/D3Z7D5|||http://purl.uniprot.org/uniprot/Q02788 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Cell attachment site|||Collagen alpha-2(VI) chain|||Disordered|||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_0000005833|||http://purl.uniprot.org/annotation/PRO_5003052862 http://togogenome.org/gene/10090:Cox6a1 ^@ http://purl.uniprot.org/uniprot/P43024|||http://purl.uniprot.org/uniprot/Q9DCW5 ^@ 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_0000006120 http://togogenome.org/gene/10090:Asf1b ^@ http://purl.uniprot.org/uniprot/Q9DAP7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Histone chaperone ASF1B|||Interaction with histone H3 and CHAF1B|||Phosphoserine; by TLK2 ^@ http://purl.uniprot.org/annotation/PRO_0000284016 http://togogenome.org/gene/10090:Fgfbp3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0R6|||http://purl.uniprot.org/uniprot/Q1HCM0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Signal Peptide ^@ Disordered|||Fibroblast growth factor-binding protein 3|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000322978|||http://purl.uniprot.org/annotation/PRO_5015044291 http://togogenome.org/gene/10090:Zfp799 ^@ http://purl.uniprot.org/uniprot/Q4VA42|||http://purl.uniprot.org/uniprot/Q6P5N6|||http://purl.uniprot.org/uniprot/Q8BHK4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Ifna1 ^@ http://purl.uniprot.org/uniprot/A0A7R8GV68|||http://purl.uniprot.org/uniprot/P01572 ^@ 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-1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000016375|||http://purl.uniprot.org/annotation/PRO_5030505205 http://togogenome.org/gene/10090:Megf8 ^@ http://purl.uniprot.org/uniprot/P60882 ^@ 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 ^@ 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|||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_0000055630 http://togogenome.org/gene/10090:Or1e31 ^@ http://purl.uniprot.org/uniprot/A0A0U1RNJ4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp932 ^@ http://purl.uniprot.org/uniprot/D3Z5Z2|||http://purl.uniprot.org/uniprot/E9QAG8 ^@ 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 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_0000425265 http://togogenome.org/gene/10090:Galnt13 ^@ http://purl.uniprot.org/uniprot/A2RRI8|||http://purl.uniprot.org/uniprot/Q8CF93 ^@ 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 13|||Ricin B lectin|||Ricin B-type lectin ^@ http://purl.uniprot.org/annotation/PRO_0000059131|||http://purl.uniprot.org/annotation/VSP_011220 http://togogenome.org/gene/10090:Taf2 ^@ http://purl.uniprot.org/uniprot/B9EJX5 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Asgr2 ^@ http://purl.uniprot.org/uniprot/P24721 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Asialoglycoprotein receptor 2|||Basic and acidic residues|||C-type lectin|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000046655 http://togogenome.org/gene/10090:Il2 ^@ http://purl.uniprot.org/uniprot/P04351 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand ^@ In strain: CAST/Ei.|||In strain: RF/J and CAST/Ei.|||In strain: RF/J.|||Interleukin-2|||O-linked (GalNAc...) threonine ^@ http://purl.uniprot.org/annotation/PRO_0000015493 http://togogenome.org/gene/10090:Ndufs3 ^@ http://purl.uniprot.org/uniprot/Q9DCT2 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Mitochondrion|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000019999 http://togogenome.org/gene/10090:Tmem59l ^@ http://purl.uniprot.org/uniprot/Q7TNI2 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Microbody targeting signal|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 59-like ^@ http://purl.uniprot.org/annotation/PRO_0000003001 http://togogenome.org/gene/10090:Atf6b ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ69|||http://purl.uniprot.org/uniprot/Q3UJ07 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ BZIP|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Kcnh4 ^@ http://purl.uniprot.org/uniprot/A2A5F7 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Cyclic nucleotide-binding|||Disordered|||Helical|||PAC|||PAS|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Fign ^@ http://purl.uniprot.org/uniprot/Q9ERZ6 ^@ 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|||Fidgetin|||In isoform 2.|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000250749|||http://purl.uniprot.org/annotation/VSP_020731 http://togogenome.org/gene/10090:Ppt1 ^@ http://purl.uniprot.org/uniprot/O88531|||http://purl.uniprot.org/uniprot/Q3TEL0|||http://purl.uniprot.org/uniprot/Q3U6J9|||http://purl.uniprot.org/uniprot/Q3U6W3 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Palmitoyl-protein thioesterase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000025552|||http://purl.uniprot.org/annotation/PRO_5004229465|||http://purl.uniprot.org/annotation/PRO_5010843377|||http://purl.uniprot.org/annotation/PRO_5010843389 http://togogenome.org/gene/10090:Trabd ^@ http://purl.uniprot.org/uniprot/Q99JY4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ N-acetylmethionine|||Phosphothreonine|||TraB domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000050826 http://togogenome.org/gene/10090:Ccdc141 ^@ http://purl.uniprot.org/uniprot/E9Q8Q6|||http://purl.uniprot.org/uniprot/Q8BLD3|||http://purl.uniprot.org/uniprot/Q8BUK9 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Splice Variant ^@ Coiled-coil domain-containing protein 141|||Does not affect ubiqutination. Abolishes ubiquitinatination; when associated with 123-A.|||Ig-like|||In isoform 2.|||Induced abnormal dilation formation. Delayed radial migration with decreases of migration distance and speed. More resistant to degradation during the G2/M phase. Abolishes ubiquitination. Abolishes ubiquitinatination; when associated with 660-A.|||Not resistant to CDC20-dependent degradation.|||Phosphothreonine|||Resistance to CDC20-dependent degradation. ^@ http://purl.uniprot.org/annotation/PRO_0000458902|||http://purl.uniprot.org/annotation/VSP_062009|||http://purl.uniprot.org/annotation/VSP_062010 http://togogenome.org/gene/10090:Rpe65 ^@ http://purl.uniprot.org/uniprot/Q91ZQ5 ^@ 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 ^@ Increased light damage susceptibility.|||Knockin mice exhibit mild age-dependent degeneration of retinal structure and function; Knockin mice exhibit adequate isomerization activity with an accumulation of retinyl esters and a delay in rhodopsin regeneration kinetics and diminished electroretinography responses. Retinae of knockin mice are more sensitive to light exposition and exhibit signs of degenerative features when sujected to light stress. May cause abnormal splicing mRNAs thereby decreasing protein levels.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Retinoid isomerohydrolase|||S-palmitoyl cysteine; in membrane form ^@ http://purl.uniprot.org/annotation/PRO_0000143944 http://togogenome.org/gene/10090:COX1 ^@ http://purl.uniprot.org/uniprot/P00397|||http://purl.uniprot.org/uniprot/Q9MD68 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 1'-histidyl-3'-tyrosine (His-Tyr)|||Cytochrome c oxidase subunit 1|||Cytochrome oxidase subunit I profile|||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|||Mitochondrial intermembrane|||Mitochondrial matrix|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000183363 http://togogenome.org/gene/10090:Rpl32 ^@ http://purl.uniprot.org/uniprot/P62911 ^@ Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Crosslink|||Modified Residue ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL32|||N6-succinyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000131115 http://togogenome.org/gene/10090:Mad2l2 ^@ http://purl.uniprot.org/uniprot/A2A7G7|||http://purl.uniprot.org/uniprot/Q9D752 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn ^@ HORMA|||Mediates interaction with REV1 and REV3L and homodimerization|||Mitotic spindle assembly checkpoint protein MAD2B ^@ http://purl.uniprot.org/annotation/PRO_0000126120 http://togogenome.org/gene/10090:Rnf25 ^@ http://purl.uniprot.org/uniprot/E9Q446|||http://purl.uniprot.org/uniprot/Q9CT51|||http://purl.uniprot.org/uniprot/Q9QZR0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF25|||No E2 binding. Loss of ubiquitination activity.|||Polar residues|||RING-type|||RWD ^@ http://purl.uniprot.org/annotation/PRO_0000056067 http://togogenome.org/gene/10090:Slc25a16 ^@ http://purl.uniprot.org/uniprot/Q8C0K5 ^@ 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.|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 16 ^@ http://purl.uniprot.org/annotation/PRO_0000090617|||http://purl.uniprot.org/annotation/VSP_016549|||http://purl.uniprot.org/annotation/VSP_016550 http://togogenome.org/gene/10090:Gdi1 ^@ http://purl.uniprot.org/uniprot/P50396 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Rab GDP dissociation inhibitor alpha ^@ http://purl.uniprot.org/annotation/PRO_0000056673 http://togogenome.org/gene/10090:Gm21708 ^@ http://purl.uniprot.org/uniprot/O35698 ^@ 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|||RNA-binding motif protein, Y chromosome, family 1 member A1|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000341540 http://togogenome.org/gene/10090:Tnfsf12 ^@ http://purl.uniprot.org/uniprot/O54907|||http://purl.uniprot.org/uniprot/Q5F2A0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||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_0000034522|||http://purl.uniprot.org/annotation/PRO_0000034523 http://togogenome.org/gene/10090:Ctps ^@ http://purl.uniprot.org/uniprot/P70698 ^@ 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 ^@ CTP synthase 1|||Disordered|||For GATase activity|||Glutamine amidotransferase type-1|||N6-acetyllysine|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000138276 http://togogenome.org/gene/10090:Trappc5 ^@ http://purl.uniprot.org/uniprot/Q9CQA1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Phosphoserine|||Trafficking protein particle complex subunit 5 ^@ http://purl.uniprot.org/annotation/PRO_0000211580 http://togogenome.org/gene/10090:Pak1 ^@ http://purl.uniprot.org/uniprot/G5E884 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||CRIB|||Disordered|||Polar residues|||Protein kinase ^@ http://togogenome.org/gene/10090:Dnm2 ^@ http://purl.uniprot.org/uniprot/P39054|||http://purl.uniprot.org/uniprot/Q3T9X3|||http://purl.uniprot.org/uniprot/Q3TCR7 ^@ 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 ^@ Apoptotic cell corpse-containing phagosomes fail to mature into acidic phagosomes. Loss of PIK3C3 and RAB5A recruitment to phagosomes.|||Disordered|||Dynamin-2|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||GED|||In isoform 2.|||N6-acetyllysine|||PH|||Phosphoserine; by CDK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000206571|||http://purl.uniprot.org/annotation/VSP_001326 http://togogenome.org/gene/10090:Haus7 ^@ http://purl.uniprot.org/uniprot/Q8BKT8 ^@ 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|||HAUS augmin-like complex subunit 7|||In isoform 2.|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000097553|||http://purl.uniprot.org/annotation/VSP_040922 http://togogenome.org/gene/10090:Myrip ^@ http://purl.uniprot.org/uniprot/Q8K3I4 ^@ 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 ^@ Actin-binding|||Basic and acidic residues|||Disordered|||FYVE-type|||Increased PRKAR2A-binding; when associated with P-245.|||Loss of PRKAR2A-binding; when associated with P-197.|||Loss of PRKAR2A-binding; when associated with P-206.|||Myosin-binding|||Negative regulation of PRKAR2A-binding|||PRKAR2A-binding|||Phosphoserine|||Polar residues|||Rab effector MyRIP|||RabBD ^@ http://purl.uniprot.org/annotation/PRO_0000190225 http://togogenome.org/gene/10090:Nfkb1 ^@ http://purl.uniprot.org/uniprot/P25799 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Chain|||Crosslink|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ (3S)-3-hydroxyasparagine; by HIF1AN|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Cleavage (when cotranslationally processed)|||Death|||Disordered|||Essential for interaction with HIF1AN|||GRR|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 7.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||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|||RHD|||S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate|||S-nitrosocysteine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000030312|||http://purl.uniprot.org/annotation/PRO_0000030313|||http://purl.uniprot.org/annotation/VSP_005583|||http://purl.uniprot.org/annotation/VSP_005584|||http://purl.uniprot.org/annotation/VSP_017236|||http://purl.uniprot.org/annotation/VSP_017237|||http://purl.uniprot.org/annotation/VSP_017238 http://togogenome.org/gene/10090:Mos ^@ http://purl.uniprot.org/uniprot/P00536 ^@ 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|||Proto-oncogene serine/threonine-protein kinase mos|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086345 http://togogenome.org/gene/10090:Bst2 ^@ http://purl.uniprot.org/uniprot/Q8R2Q8 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Topological Domain|||Transmembrane|||Turn ^@ Bone marrow stromal antigen 2|||Cytoplasmic|||Extracellular|||GPI-anchor amidated serine|||Helical; Signal-anchor for type II membrane protein|||Interchain|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000253553|||http://purl.uniprot.org/annotation/PRO_0000253554 http://togogenome.org/gene/10090:H2-M9 ^@ http://purl.uniprot.org/uniprot/O19442 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015096741 http://togogenome.org/gene/10090:Dynlt2b ^@ http://purl.uniprot.org/uniprot/Q9CQ66|||http://purl.uniprot.org/uniprot/Q9CQJ9 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Dynein light chain Tctex-type protein 2B ^@ http://purl.uniprot.org/annotation/PRO_0000316870 http://togogenome.org/gene/10090:Pde1b ^@ http://purl.uniprot.org/uniprot/A0A2I3BPC1|||http://purl.uniprot.org/uniprot/Q01065|||http://purl.uniprot.org/uniprot/Q6PDS5|||http://purl.uniprot.org/uniprot/Q9DBS6 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Calmodulin-binding|||Disordered|||Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B|||PDEase|||Phosphoserine|||Polar residues|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000198790 http://togogenome.org/gene/10090:Rtl1 ^@ http://purl.uniprot.org/uniprot/B4YB44|||http://purl.uniprot.org/uniprot/Q7M732 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ 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_0000339234 http://togogenome.org/gene/10090:Twnk ^@ http://purl.uniprot.org/uniprot/A0A494B8Y2|||http://purl.uniprot.org/uniprot/Q3V303|||http://purl.uniprot.org/uniprot/Q8CIW5 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Region|||Splice Variant|||Transit Peptide ^@ Contributes to single strand DNA binding activity|||Disordered|||In isoform 2.|||Maybe required for stable oligomeric structure|||Might negatively regulate ATPase activity|||Mitochondrion|||Required for hexamers formation and DNA helicase activity|||SF4 helicase|||Twinkle mtDNA helicase ^@ http://purl.uniprot.org/annotation/PRO_0000042641|||http://purl.uniprot.org/annotation/VSP_015962|||http://purl.uniprot.org/annotation/VSP_015963 http://togogenome.org/gene/10090:Or13d1 ^@ http://purl.uniprot.org/uniprot/Q8VFN0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Smco2 ^@ http://purl.uniprot.org/uniprot/Q9DA21 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Single-pass membrane and coiled-coil domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000340701 http://togogenome.org/gene/10090:Ifne ^@ http://purl.uniprot.org/uniprot/A0A7R8GUW5|||http://purl.uniprot.org/uniprot/Q80ZF2 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Interferon epsilon ^@ http://purl.uniprot.org/annotation/PRO_0000317632|||http://purl.uniprot.org/annotation/PRO_5031158773 http://togogenome.org/gene/10090:Bbs12 ^@ http://purl.uniprot.org/uniprot/Q5SUD9 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Bardet-Biedl syndrome 12 protein homolog ^@ http://purl.uniprot.org/annotation/PRO_0000301982 http://togogenome.org/gene/10090:Hoxa3 ^@ http://purl.uniprot.org/uniprot/P02831 ^@ 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-A3|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000200044 http://togogenome.org/gene/10090:Ccer2 ^@ http://purl.uniprot.org/uniprot/J3QPU5 ^@ 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_5003776681 http://togogenome.org/gene/10090:Mex3c ^@ http://purl.uniprot.org/uniprot/Q05A36 ^@ 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|||Disordered|||KH 1|||KH 2|||Phosphoserine|||Polar residues|||Pro residues|||RING-type|||RNA-binding E3 ubiquitin-protein ligase MEX3C ^@ http://purl.uniprot.org/annotation/PRO_0000278783 http://togogenome.org/gene/10090:Cttn ^@ http://purl.uniprot.org/uniprot/Q60598|||http://purl.uniprot.org/uniprot/Q8BNA5|||http://purl.uniprot.org/uniprot/Q921L6 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand ^@ Abolishes cortactin-mediated endocytosis of KCNA2.|||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|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on interaction with KCNA2, but decreases KCNA2 levels at the cell membrane.|||No effect on interaction with KCNA2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FAK1|||Phosphotyrosine; by SRC|||SH3|||Src substrate cortactin ^@ http://purl.uniprot.org/annotation/PRO_0000072190 http://togogenome.org/gene/10090:Wfdc3 ^@ http://purl.uniprot.org/uniprot/Q14AE4 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||WAP 1|||WAP 2|||WAP four-disulfide core domain protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000415846 http://togogenome.org/gene/10090:Cdc42ep2 ^@ http://purl.uniprot.org/uniprot/Q8JZX9 ^@ 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 ^@ CRIB|||Cdc42 effector protein 2|||Disordered|||N-acetylserine|||Phosphoserine|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000212649 http://togogenome.org/gene/10090:Knop1 ^@ http://purl.uniprot.org/uniprot/F6ZLH4|||http://purl.uniprot.org/uniprot/K4DI66|||http://purl.uniprot.org/uniprot/Q9Z2Q2 ^@ 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 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.|||Interaction with ZNF106|||Lysine-rich nucleolar protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Small acidic protein-like ^@ http://purl.uniprot.org/annotation/PRO_0000321939|||http://purl.uniprot.org/annotation/VSP_031834|||http://purl.uniprot.org/annotation/VSP_031835 http://togogenome.org/gene/10090:Zcchc10 ^@ http://purl.uniprot.org/uniprot/Q9CX48 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Zinc Finger ^@ CCHC-type|||Disordered|||Polar residues|||Zinc finger CCHC domain-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000150968 http://togogenome.org/gene/10090:Cdh11 ^@ http://purl.uniprot.org/uniprot/P55288|||http://purl.uniprot.org/uniprot/Q8C7Q6 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin domain-containing protein|||Cadherin-11|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000003787|||http://purl.uniprot.org/annotation/PRO_0000003788|||http://purl.uniprot.org/annotation/PRO_5004307342 http://togogenome.org/gene/10090:Morc2a ^@ http://purl.uniprot.org/uniprot/Q69ZX6|||http://purl.uniprot.org/uniprot/Q6PCN6 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Zinc Finger ^@ ATPase MORC2A|||Abolishes repression of germ cell-related genes and L1 retrotransposons.|||Basic and acidic residues|||CW-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000248243 http://togogenome.org/gene/10090:Soat2 ^@ http://purl.uniprot.org/uniprot/O88908 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cysteine sulfenic acid (-SOH); alternate|||Cytoplasmic|||Disordered|||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|||Lumenal|||Sterol O-acyltransferase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000207646 http://togogenome.org/gene/10090:Nfx1 ^@ http://purl.uniprot.org/uniprot/B1AY10 ^@ 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|||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|||Transcriptional repressor NF-X1 ^@ http://purl.uniprot.org/annotation/PRO_0000334614|||http://purl.uniprot.org/annotation/VSP_033693|||http://purl.uniprot.org/annotation/VSP_033694|||http://purl.uniprot.org/annotation/VSP_033695|||http://purl.uniprot.org/annotation/VSP_033696 http://togogenome.org/gene/10090:Dmtf1l ^@ http://purl.uniprot.org/uniprot/Q8C0S0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ HTH myb-type|||Myb-like ^@ http://togogenome.org/gene/10090:Hpca ^@ http://purl.uniprot.org/uniprot/P84075 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding ^@ EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||N-myristoyl glycine|||Neuron-specific calcium-binding protein hippocalcin|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000073769 http://togogenome.org/gene/10090:Treml4 ^@ http://purl.uniprot.org/uniprot/D3YY88|||http://purl.uniprot.org/uniprot/D3YYN5|||http://purl.uniprot.org/uniprot/Q3LRV9 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||Loss of TLR7 signaling.|||N-linked (GlcNAc...) asparagine|||Trem-like transcript 4 protein ^@ http://purl.uniprot.org/annotation/PRO_0000418835|||http://purl.uniprot.org/annotation/PRO_5003052980|||http://purl.uniprot.org/annotation/PRO_5003053117|||http://purl.uniprot.org/annotation/VSP_044083|||http://purl.uniprot.org/annotation/VSP_044084 http://togogenome.org/gene/10090:Sap130 ^@ http://purl.uniprot.org/uniprot/A0A0R4J060|||http://purl.uniprot.org/uniprot/Q8BIH0 ^@ 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)|||Histone deacetylase complex subunit SAP130|||Histone deacetylase complex subunit SAP130 C-terminal|||In isoform 2.|||In isoform 3.|||Interactions with SIN3A and HDAC1|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000283737|||http://purl.uniprot.org/annotation/VSP_024357|||http://purl.uniprot.org/annotation/VSP_024358|||http://purl.uniprot.org/annotation/VSP_024359 http://togogenome.org/gene/10090:Adam22 ^@ http://purl.uniprot.org/uniprot/D3YUP9|||http://purl.uniprot.org/uniprot/D6QSS8|||http://purl.uniprot.org/uniprot/Q9R1V6 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 22|||Disordered|||EGF-like|||Extracellular|||Fails to bind to LGI1.|||Helical|||In isoform 10, isoform 11, isoform 12 and isoform 13.|||In isoform 10.|||In isoform 11 and isoform 19.|||In isoform 12.|||In isoform 14.|||In isoform 15.|||In isoform 16.|||In isoform 17, isoform 18, isoform 19 and isoform 20.|||In isoform 2, isoform 5, isoform 8, isoform 15 and isoform 17.|||In isoform 21.|||In isoform 3, isoform 4 and isoform 18.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000029114|||http://purl.uniprot.org/annotation/PRO_0000029115|||http://purl.uniprot.org/annotation/PRO_5003052335|||http://purl.uniprot.org/annotation/PRO_5003087233|||http://purl.uniprot.org/annotation/VSP_018233|||http://purl.uniprot.org/annotation/VSP_018234|||http://purl.uniprot.org/annotation/VSP_018235|||http://purl.uniprot.org/annotation/VSP_018236|||http://purl.uniprot.org/annotation/VSP_018237|||http://purl.uniprot.org/annotation/VSP_018238|||http://purl.uniprot.org/annotation/VSP_018239|||http://purl.uniprot.org/annotation/VSP_018240|||http://purl.uniprot.org/annotation/VSP_018241|||http://purl.uniprot.org/annotation/VSP_018242|||http://purl.uniprot.org/annotation/VSP_018243|||http://purl.uniprot.org/annotation/VSP_018244|||http://purl.uniprot.org/annotation/VSP_018245|||http://purl.uniprot.org/annotation/VSP_018246|||http://purl.uniprot.org/annotation/VSP_018247|||http://purl.uniprot.org/annotation/VSP_018248 http://togogenome.org/gene/10090:Hsd3b8 ^@ http://purl.uniprot.org/uniprot/Q3UIU9|||http://purl.uniprot.org/uniprot/Q61767 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Transmembrane ^@ 3-beta hydroxysteroid dehydrogenase/isomerase|||Helical|||N6-acetyllysine|||NADPH-dependent 3-keto-steroid reductase Hsd3b4|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000087783 http://togogenome.org/gene/10090:Epor ^@ http://purl.uniprot.org/uniprot/P14753|||http://purl.uniprot.org/uniprot/Q3UTV9 ^@ 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|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn ^@ 100-fold less EPO binding.|||14-fold less EPO binding.|||2-fold less EPO binding.|||50-fold less EPO binding.|||Binds to PTPN6 and PTPN11 SH2 domains.|||Box 1 motif|||C-linked (Man) tryptophan|||Cytoplasmic|||Disordered|||Enhanced secretion and increased EPO binding.|||Erythropoietin receptor|||Extracellular|||Fibronectin type-III|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Greatly reduced EPO binding.|||Greatly reduced JAK2/STAT5 activation and some loss of mitogenic response.|||Helical|||ITIM motif|||In isoform EPOR-S.|||Interaction with APS and STAT5, and activation|||Interaction with PTPN6|||Little EPO binding.|||Loss of EPO binding.|||N-linked (GlcNAc...) asparagine|||No JAK2 binding nor JAK2/STAT5 activation. No EPO-induced phosphorylation. Complete loss of mitogenic response.|||No PTPN11 binding, reduced PTPN11 tyrosine phosphorylation and reduced cell proliferation.|||No PTPN6 binding, binds PTPN11.|||No STAT5 activation.|||No binding to PTPN6 SH2 domains. Enhanced JAK2 activation and cell proliferation.|||No change in EPO binding.|||No change in JAK2/STAT5 activation nor mitogenic response.|||No loss of EPO binding.|||No loss of PTPN11 binding.|||Not secreted and loss of EPO binding.|||Phosphotyrosine; by JAK2|||Polar residues|||Reduced EPO binding.|||Reduced JAK2/STAT5 activation and mitogenic response.|||Reduced JAK2/STAT5 activation.|||Required for CrkL binding|||Required for STAT1/STAT3 activation|||Required for STAT5/PTPN11/SOCS3 binding|||Required for ligand binding|||Slightly reduced JAK2/STAT5 activation and mitogenic response.|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010869|||http://purl.uniprot.org/annotation/PRO_5014309185|||http://purl.uniprot.org/annotation/VSP_009512|||http://purl.uniprot.org/annotation/VSP_009513 http://togogenome.org/gene/10090:Mrgprg ^@ http://purl.uniprot.org/uniprot/Q91ZB5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||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|||Mas-related G-protein coupled receptor member G ^@ http://purl.uniprot.org/annotation/PRO_0000069768 http://togogenome.org/gene/10090:Pdilt ^@ http://purl.uniprot.org/uniprot/Q9DAN1 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide ^@ Disordered|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Protein disulfide-isomerase-like protein of the testis|||Thioredoxin ^@ http://purl.uniprot.org/annotation/PRO_0000325851 http://togogenome.org/gene/10090:Cd9 ^@ http://purl.uniprot.org/uniprot/P40240 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ 4-fold reduction of sperm-egg fusion.|||CD9 antigen|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Sperm-egg fusion abolished. ^@ http://purl.uniprot.org/annotation/PRO_0000219206 http://togogenome.org/gene/10090:Pex2 ^@ http://purl.uniprot.org/uniprot/P55098|||http://purl.uniprot.org/uniprot/Q91YZ5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Cytoplasmic|||Helical; Name=TM1|||Helical; Name=TM2|||Helical; Name=TM3|||Helical; Name=TM4|||Helical; Name=TM5|||Peroxisomal matrix|||Peroxisome biogenesis factor 2|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056370 http://togogenome.org/gene/10090:ND4L ^@ http://purl.uniprot.org/uniprot/P03903|||http://purl.uniprot.org/uniprot/Q9MD77 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transmembrane ^@ Chain|||Helix|||Sequence Conflict|||Strand|||Transmembrane ^@ Helical|||NADH-ubiquinone oxidoreductase chain 4L ^@ http://purl.uniprot.org/annotation/PRO_0000118448 http://togogenome.org/gene/10090:Krt14 ^@ http://purl.uniprot.org/uniprot/Q61781 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Interaction with Type I keratins and keratin filaments|||Interchain|||Keratin, type I cytoskeletal 14|||Linker 1|||Linker 12|||Phosphoserine|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063654 http://togogenome.org/gene/10090:Garre1 ^@ http://purl.uniprot.org/uniprot/Q8C5X1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ DUF4745|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Or2a57 ^@ http://purl.uniprot.org/uniprot/Q8VF18 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Erc1 ^@ http://purl.uniprot.org/uniprot/F8VPM7|||http://purl.uniprot.org/uniprot/Q99MI1 ^@ 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|||ELKS/Rab6-interacting/CAST family member 1|||FIP-RBD|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000097177|||http://purl.uniprot.org/annotation/VSP_011456|||http://purl.uniprot.org/annotation/VSP_011457|||http://purl.uniprot.org/annotation/VSP_011458|||http://purl.uniprot.org/annotation/VSP_011459|||http://purl.uniprot.org/annotation/VSP_011460|||http://purl.uniprot.org/annotation/VSP_011462|||http://purl.uniprot.org/annotation/VSP_011463 http://togogenome.org/gene/10090:Slco1a6 ^@ http://purl.uniprot.org/uniprot/Q99J94 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||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|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Solute carrier organic anion transporter family member 1A6 ^@ http://purl.uniprot.org/annotation/PRO_0000191048 http://togogenome.org/gene/10090:Pip4p1 ^@ http://purl.uniprot.org/uniprot/E0CZ18|||http://purl.uniprot.org/uniprot/E0CZF6|||http://purl.uniprot.org/uniprot/F8WHW3|||http://purl.uniprot.org/uniprot/Q3TWL2 ^@ 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|||Pro residues|||Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000235234 http://togogenome.org/gene/10090:Prss53 ^@ http://purl.uniprot.org/uniprot/B2RX64|||http://purl.uniprot.org/uniprot/Q571E5 ^@ 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|||Peptidase S1 1|||Peptidase S1 2|||Serine protease 53 ^@ http://purl.uniprot.org/annotation/PRO_0000316764|||http://purl.uniprot.org/annotation/PRO_5014298317 http://togogenome.org/gene/10090:Mast1 ^@ http://purl.uniprot.org/uniprot/Q7TQ97|||http://purl.uniprot.org/uniprot/Q9R1L5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ AGC-kinase C-terminal|||Basic and acidic residues|||Disordered|||Microtubule-associated serine/threonine-protein kinase 1|||Mutant heterozygous mice have a thicker corpus callosum, hypoplastic cortex and cerebellum, increased neuronal apoptosis, and decreased protein levels.|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086310 http://togogenome.org/gene/10090:Usp51 ^@ http://purl.uniprot.org/uniprot/B1AY15 ^@ 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 R-615.|||Abolishes ability to deubiquitinate histone H2A; when associated with S-329.|||Disordered|||Nucleophile|||Pro residues|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 51 ^@ http://purl.uniprot.org/annotation/PRO_0000441892 http://togogenome.org/gene/10090:Cirbp ^@ http://purl.uniprot.org/uniprot/P60824 ^@ 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 ^@ Cold-inducible RNA-binding protein|||Disordered|||Inhibits stress granules localization and translational repression.|||Inhibits translational repression.|||Phosphoserine|||Polar residues|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081504 http://togogenome.org/gene/10090:Or4c52 ^@ http://purl.uniprot.org/uniprot/Q8VG63 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rem1 ^@ http://purl.uniprot.org/uniprot/O35929 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Calmodulin-binding|||Disordered|||GTP-binding protein REM 1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000122482 http://togogenome.org/gene/10090:Taf5 ^@ http://purl.uniprot.org/uniprot/F8VPY2|||http://purl.uniprot.org/uniprot/Q8C092 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict ^@ Disordered|||LisH|||Transcription initiation factor TFIID subunit 5|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000051258 http://togogenome.org/gene/10090:Otub1 ^@ http://purl.uniprot.org/uniprot/Q7TQI3 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Free ubiquitin binding|||Interacts with free ubiquitin|||N-acetylalanine|||Nucleophile|||OTU|||Phosphoserine|||Phosphotyrosine|||Removed|||Ubiquitin thioesterase OTUB1|||Ubiquitin-conjugating enzyme E2 binding ^@ http://purl.uniprot.org/annotation/PRO_0000221009 http://togogenome.org/gene/10090:Ebf4 ^@ http://purl.uniprot.org/uniprot/B2RQX3|||http://purl.uniprot.org/uniprot/Q8K4J2 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Site|||Splice Variant|||Zinc Finger ^@ C5-type|||Disordered|||IPT/TIG|||In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Interaction with DNA|||Transcription factor COE4 ^@ http://purl.uniprot.org/annotation/PRO_0000107836|||http://purl.uniprot.org/annotation/VSP_001119|||http://purl.uniprot.org/annotation/VSP_001120|||http://purl.uniprot.org/annotation/VSP_001121|||http://purl.uniprot.org/annotation/VSP_001122|||http://purl.uniprot.org/annotation/VSP_001123|||http://purl.uniprot.org/annotation/VSP_001124|||http://purl.uniprot.org/annotation/VSP_001125|||http://purl.uniprot.org/annotation/VSP_001126 http://togogenome.org/gene/10090:Drc3 ^@ http://purl.uniprot.org/uniprot/Q9D5E4 ^@ Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Domain Extent|||Repeat ^@ Dynein regulatory complex subunit 3|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT ^@ http://purl.uniprot.org/annotation/PRO_0000227776 http://togogenome.org/gene/10090:Mrpl41 ^@ http://purl.uniprot.org/uniprot/Q9CQN7 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Transit Peptide ^@ Chain|||Sequence Conflict|||Transit Peptide ^@ Large ribosomal subunit protein mL41|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000273229 http://togogenome.org/gene/10090:Gpm6a ^@ http://purl.uniprot.org/uniprot/P35802|||http://purl.uniprot.org/uniprot/Q542P2|||http://purl.uniprot.org/uniprot/Q8R1P3 ^@ 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|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Neuronal membrane glycoprotein M6-a|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000159019 http://togogenome.org/gene/10090:Setd1b ^@ http://purl.uniprot.org/uniprot/Q3URP1|||http://purl.uniprot.org/uniprot/Q8CFT2 ^@ 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|||Disordered|||Histone-lysine N-methyltransferase SETD1B|||In isoform 2.|||Phosphoserine|||Polar residues|||Post-SET|||Pro residues|||RRM|||SET|||WDR5 interaction motif (WIN) ^@ http://purl.uniprot.org/annotation/PRO_0000316994|||http://purl.uniprot.org/annotation/VSP_030851 http://togogenome.org/gene/10090:Dctn6 ^@ http://purl.uniprot.org/uniprot/Q9WUB4 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Dynactin subunit 6|||Phosphothreonine; by CDK1 ^@ http://purl.uniprot.org/annotation/PRO_0000079831 http://togogenome.org/gene/10090:Hs3st1 ^@ http://purl.uniprot.org/uniprot/O35310 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Turn ^@ Abolishes the enzymatic activity.|||Decreases the enzymatic activity.|||Heparan sulfate glucosamine 3-O-sulfotransferase 1|||N-linked (GlcNAc...) asparagine|||No effect.|||Strongly decrease the enzymatic activity.|||Strongly decreases the enzymatic activity.|||Weakly decrease the enzymatic activity. ^@ http://purl.uniprot.org/annotation/PRO_0000033452 http://togogenome.org/gene/10090:Ntm ^@ http://purl.uniprot.org/uniprot/Q8BG33 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015099047 http://togogenome.org/gene/10090:Xbp1 ^@ http://purl.uniprot.org/uniprot/O35426 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic motif|||Cleavage; by HM13/SPP|||Cytoplasmic|||Disordered|||Enhances stability and accumulates in the cytoplasm; when associated with R-231 (isoform 1).|||Enhances stability and accumulates in the cytoplasm; when associated with R-252 (isoform 1).|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Leucine-zipper|||Lumenal|||Necessary for the translational pausing of its own mRNA|||Nuclear localization signal (NLS); in isoforms 1 and isoform 2|||Phosphoserine|||Reduces degradation (isoform 1); when associated with 177-L-H-178.|||Reduces degradation (isoform 1); when associated with 238-L-H-239.|||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_0000076544|||http://purl.uniprot.org/annotation/PRO_0000431893|||http://purl.uniprot.org/annotation/PRO_0000431894|||http://purl.uniprot.org/annotation/VSP_012937 http://togogenome.org/gene/10090:Dusp1 ^@ http://purl.uniprot.org/uniprot/P28563|||http://purl.uniprot.org/uniprot/Q3U8K3 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site ^@ 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_0000094791 http://togogenome.org/gene/10090:Spata7 ^@ http://purl.uniprot.org/uniprot/Q3TTL3|||http://purl.uniprot.org/uniprot/Q3U5D0|||http://purl.uniprot.org/uniprot/Q80VP2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Spermatogenesis-associated protein 7 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000072105 http://togogenome.org/gene/10090:Capns2 ^@ http://purl.uniprot.org/uniprot/Q9D7J7 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent ^@ Calpain small subunit 2|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4 ^@ http://purl.uniprot.org/annotation/PRO_0000073719 http://togogenome.org/gene/10090:Vmn1r171 ^@ http://purl.uniprot.org/uniprot/Q9EPS6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Phlda2 ^@ http://purl.uniprot.org/uniprot/O08969 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site ^@ Impairs the ability to rescue growth in cdc25ts mutant yeasts.|||PH|||Phosphoserine|||Pleckstrin homology-like domain family A member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000053901 http://togogenome.org/gene/10090:Cdk8 ^@ http://purl.uniprot.org/uniprot/Q8R3L8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant ^@ Basic and acidic residues|||Cyclin-dependent kinase 8|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with CCNC|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000280443|||http://purl.uniprot.org/annotation/VSP_023673|||http://purl.uniprot.org/annotation/VSP_023674|||http://purl.uniprot.org/annotation/VSP_023675 http://togogenome.org/gene/10090:Kpna4 ^@ http://purl.uniprot.org/uniprot/O35343|||http://purl.uniprot.org/uniprot/Q4FJX1 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat ^@ ARM|||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_0000120727 http://togogenome.org/gene/10090:Pcdhga7 ^@ http://purl.uniprot.org/uniprot/Q6DD96 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015098184 http://togogenome.org/gene/10090:Skor1 ^@ http://purl.uniprot.org/uniprot/D3YX64|||http://purl.uniprot.org/uniprot/Q8BX46 ^@ 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.|||Polar residues|||Pro residues|||SKI family transcriptional corepressor 1|||c-SKI SMAD4-binding ^@ http://purl.uniprot.org/annotation/PRO_0000129391|||http://purl.uniprot.org/annotation/VSP_014179 http://togogenome.org/gene/10090:Lsm12 ^@ http://purl.uniprot.org/uniprot/Q9D0R8 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ AD|||N-acetylalanine|||Phosphothreonine|||Protein LSM12|||Removed|||Required for NAADP and TPCN2 binding|||Sm ^@ http://purl.uniprot.org/annotation/PRO_0000305127 http://togogenome.org/gene/10090:Thoc6 ^@ http://purl.uniprot.org/uniprot/Q5U4D9 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Repeat ^@ 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_0000233159 http://togogenome.org/gene/10090:Lmf2 ^@ http://purl.uniprot.org/uniprot/Q8C3X8 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Lipase maturation factor 2|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000324511 http://togogenome.org/gene/10090:Retreg1 ^@ http://purl.uniprot.org/uniprot/Q8VE91 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Abolishes interaction with ATG8 family proteins.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 1.|||In isoform 2.|||In isoform 3.|||LIR motif|||Lumenal|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CAMK2B|||Polar residues|||Reticulon homology domain|||Reticulophagy regulator 1 ^@ http://purl.uniprot.org/annotation/PRO_0000288467|||http://purl.uniprot.org/annotation/VSP_057836|||http://purl.uniprot.org/annotation/VSP_057837|||http://purl.uniprot.org/annotation/VSP_057838 http://togogenome.org/gene/10090:Osgin1 ^@ http://purl.uniprot.org/uniprot/Q8VC10 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Oxidative stress-induced growth inhibitor 1|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000447508 http://togogenome.org/gene/10090:Ces1c ^@ http://purl.uniprot.org/uniprot/P23953 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide ^@ Acyl-ester intermediate|||Carboxylesterase 1C|||Charge relay system|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Prevents secretion from ER ^@ http://purl.uniprot.org/annotation/PRO_0000008574 http://togogenome.org/gene/10090:Zcchc7 ^@ http://purl.uniprot.org/uniprot/B1AX39 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||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|||Polar residues|||Zinc finger CCHC domain-containing protein 7 ^@ http://purl.uniprot.org/annotation/PRO_0000370241|||http://purl.uniprot.org/annotation/VSP_036901|||http://purl.uniprot.org/annotation/VSP_036902 http://togogenome.org/gene/10090:Rpl36 ^@ http://purl.uniprot.org/uniprot/P47964 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Large ribosomal subunit protein eL36|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000195008 http://togogenome.org/gene/10090:Cmtm2b ^@ http://purl.uniprot.org/uniprot/Q9DAC0 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Transmembrane ^@ CKLF-like MARVEL transmembrane domain-containing protein 2B|||Helical|||MARVEL ^@ http://purl.uniprot.org/annotation/PRO_0000186100 http://togogenome.org/gene/10090:Fut8 ^@ http://purl.uniprot.org/uniprot/B2X2D7|||http://purl.uniprot.org/uniprot/B2X2D8|||http://purl.uniprot.org/uniprot/Q9WTS2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Alpha-(1,6)-fucosyltransferase|||Cytoplasmic|||GT23|||Helical; Signal-anchor for type II membrane protein|||Important for donor substrate binding|||Lumenal|||Phosphoserine|||SH3|||SH3-binding ^@ http://purl.uniprot.org/annotation/PRO_0000080527 http://togogenome.org/gene/10090:Gdap2 ^@ http://purl.uniprot.org/uniprot/Q9DBL2 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ CRAL-TRIO|||Disordered|||Ganglioside-induced differentiation-associated protein 2|||In isoform 2.|||Macro|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000331396|||http://purl.uniprot.org/annotation/VSP_033187 http://togogenome.org/gene/10090:Snai1 ^@ http://purl.uniprot.org/uniprot/Q02085|||http://purl.uniprot.org/uniprot/Q4FK48 ^@ Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger ^@ C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||Destruction motif|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||LATS2 binding|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine|||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|||Zinc finger protein SNAI1 ^@ http://purl.uniprot.org/annotation/PRO_0000047030 http://togogenome.org/gene/10090:Sf3b6 ^@ http://purl.uniprot.org/uniprot/P59708 ^@ Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ 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_0000081726 http://togogenome.org/gene/10090:Prmt1 ^@ http://purl.uniprot.org/uniprot/Q3UIG8|||http://purl.uniprot.org/uniprot/Q9JIF0 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Splice Variant ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired interaction with FBXL17, leading to decreased ubiquitination by the SCF(FBXL17) complex.|||In isoform 2.|||In isoform 3.|||Increased interaction with FBXL17, leading to increased ubiquitination by the SCF(FBXL17) complex.|||Increased stability of the protein caused by impaired ubiquitination by the SCF(FBXL17) complex.|||Increased stability of the protein.|||Methyltransferase|||Mimicks residue acetylation; impaired interaction with FBXL17, leading to decreased ubiquitination by the SCF(FBXL17) complex.|||Mimicks residue acetylation; increased interaction with FBXL17, leading to increased ubiquitination by the SCF(FBXL17) complex.|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Protein arginine N-methyltransferase 1|||SAM-dependent MTase PRMT-type|||Slightly reduced degradation, probably caused by reduced ubiquitination by the SCF(FBXL17) complex. ^@ http://purl.uniprot.org/annotation/PRO_0000212322|||http://purl.uniprot.org/annotation/VSP_005210|||http://purl.uniprot.org/annotation/VSP_005211 http://togogenome.org/gene/10090:Mmab ^@ http://purl.uniprot.org/uniprot/D3Z1G7|||http://purl.uniprot.org/uniprot/Q9D273 ^@ Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Transit Peptide ^@ Cobalamin adenosyltransferase-like|||Corrinoid adenosyltransferase MMAB|||Disordered|||In isoform 2.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000005569|||http://purl.uniprot.org/annotation/VSP_008847 http://togogenome.org/gene/10090:Tspan8 ^@ http://purl.uniprot.org/uniprot/Q8R3G9 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-8 ^@ http://purl.uniprot.org/annotation/PRO_0000415811 http://togogenome.org/gene/10090:Or8g23 ^@ http://purl.uniprot.org/uniprot/Q9EQB4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Otub2 ^@ http://purl.uniprot.org/uniprot/D3Z0Y8|||http://purl.uniprot.org/uniprot/Q9CQX0 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Site ^@ Nucleophile|||OTU|||Required to orient and stabilize the active site H-224|||Ubiquitin thioesterase OTUB2 ^@ http://purl.uniprot.org/annotation/PRO_0000221011 http://togogenome.org/gene/10090:Lrrc10 ^@ http://purl.uniprot.org/uniprot/Q3UQT4|||http://purl.uniprot.org/uniprot/Q8K3W2 ^@ 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|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||Leucine-rich repeat-containing protein 10 ^@ http://purl.uniprot.org/annotation/PRO_0000084471 http://togogenome.org/gene/10090:Hhatl ^@ http://purl.uniprot.org/uniprot/Q9D1G3 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Protein-cysteine N-palmitoyltransferase HHAT-like protein ^@ http://purl.uniprot.org/annotation/PRO_0000213131 http://togogenome.org/gene/10090:Ddx4 ^@ http://purl.uniprot.org/uniprot/Q3V086|||http://purl.uniprot.org/uniprot/Q61496 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ ATP-dependent RNA helicase DDX4|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In Mvh(KI); heterozygous and homozygous knockin male mice are infertile due to derepression of transposable elements. Defects in piRNA biogenesis. Pre-piRNAs fail to mature into piRNAs.|||Interaction with RANBP9|||Phosphoserine|||Polar residues|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000054979 http://togogenome.org/gene/10090:Vsx2 ^@ http://purl.uniprot.org/uniprot/Q61412|||http://purl.uniprot.org/uniprot/Q6PDC1|||http://purl.uniprot.org/uniprot/Q80WF9 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Mutagenesis Site|||Region ^@ Basic and acidic residues|||CVC|||Disordered|||Homeobox|||Loss of DNA binding activity; mice are microphthalmic but viable with defects in retinal morphology and pigmentation as a result of delayed retinal neurogenesis. Reduction in transcription repression activity.|||OAR|||Polar residues|||Reduction in DNA binding activity; mice are microphthalmic but viable with severe defects in retinal morphology and extensive pigmentation as a result of a lack of retinal neurogenesis.|||Visual system homeobox 2 ^@ http://purl.uniprot.org/annotation/PRO_0000049363 http://togogenome.org/gene/10090:Apmap ^@ http://purl.uniprot.org/uniprot/Q9D7N9 ^@ Chain|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Adipocyte plasma membrane-associated protein|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-acetylserine|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000205946 http://togogenome.org/gene/10090:Gbx2 ^@ http://purl.uniprot.org/uniprot/P48031 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein GBX-2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000048881 http://togogenome.org/gene/10090:Rcvrn ^@ http://purl.uniprot.org/uniprot/P34057|||http://purl.uniprot.org/uniprot/Q2TB46 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Site ^@ Cysteine sulfenic acid (-SOH)|||EF-hand|||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_0000073760 http://togogenome.org/gene/10090:Nr1h3 ^@ http://purl.uniprot.org/uniprot/Q91X41|||http://purl.uniprot.org/uniprot/Q9Z0Y9 ^@ Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Disordered|||NR C4-type|||NR LBD|||Nuclear receptor|||Oxysterols receptor LXR-alpha|||Phosphoserine|||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_0000053536 http://togogenome.org/gene/10090:Igf2bp1 ^@ http://purl.uniprot.org/uniprot/O88477 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Disordered|||Insulin-like growth factor 2 mRNA-binding protein 1|||KH 1|||KH 2|||KH 3|||KH 4|||Necessary for interaction with IGF2BP1 and binding to TAU mRNA|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2|||Sufficient for nuclear export ^@ http://purl.uniprot.org/annotation/PRO_0000282534 http://togogenome.org/gene/10090:Snx17 ^@ http://purl.uniprot.org/uniprot/Q8BVL3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||FERM-like|||PTB-like F3 module|||PX|||Phosphoserine|||Ras-associating|||Sorting nexin-17 ^@ http://purl.uniprot.org/annotation/PRO_0000236205 http://togogenome.org/gene/10090:Trim65 ^@ http://purl.uniprot.org/uniprot/Q8BFW4|||http://purl.uniprot.org/uniprot/Q8BJT1 ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Splice Variant|||Zinc Finger ^@ B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM65|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||RING-type|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000249192|||http://purl.uniprot.org/annotation/VSP_020368|||http://purl.uniprot.org/annotation/VSP_020369 http://togogenome.org/gene/10090:Acat3 ^@ http://purl.uniprot.org/uniprot/Q80X81 ^@ Active Site|||Domain Extent|||Region|||Site ^@ Active Site|||Domain Extent ^@ Acyl-thioester intermediate|||Proton acceptor|||Thiolase C-terminal|||Thiolase N-terminal ^@ http://togogenome.org/gene/10090:Pcgf5 ^@ http://purl.uniprot.org/uniprot/Q3UK78 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Region|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform 2.|||Polycomb group RING finger protein 5|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000277869|||http://purl.uniprot.org/annotation/VSP_023120 http://togogenome.org/gene/10090:Zswim5 ^@ http://purl.uniprot.org/uniprot/Q80TC6 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Region|||Zinc Finger ^@ Disordered|||SWIM-type|||Zinc finger SWIM domain-containing protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000223104 http://togogenome.org/gene/10090:Lama4 ^@ http://purl.uniprot.org/uniprot/P97927 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Cell attachment site|||Disordered|||Domain II and I|||Interchain|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4; truncated|||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_0000017061 http://togogenome.org/gene/10090:Tead1 ^@ http://purl.uniprot.org/uniprot/Q3UFP5|||http://purl.uniprot.org/uniprot/Q3USK5|||http://purl.uniprot.org/uniprot/Q6PAQ8|||http://purl.uniprot.org/uniprot/Q80W05 ^@ DNA Binding|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ DNA Binding|||Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||TEA ^@ http://togogenome.org/gene/10090:Pomp ^@ http://purl.uniprot.org/uniprot/Q9CQT5 ^@ Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict ^@ Chain|||Crosslink|||Sequence Conflict ^@ Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Proteasome maturation protein ^@ http://purl.uniprot.org/annotation/PRO_0000247185 http://togogenome.org/gene/10090:Dok3 ^@ http://purl.uniprot.org/uniprot/Q14AA1|||http://purl.uniprot.org/uniprot/Q9QZK7 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region ^@ Disordered|||Docking protein 3|||Enhanced reduction of BCR-induced IL2 secretion. No effect on interaction with INPP5DSH2 domain. Abolishes interaction with CSKSH2 domain. No effect on BCR-triggered tyrosine phosphorylation. Abolishes reduction of BCR-induced IL2 secretion, the interaction with INPP5DSH2 domain and BCR-triggered tyrosine phosphorylation; when associated with F-343.|||Greatly reduced ABL1-binding; reduced tyrosine phosphorylation.|||IRS-type PTB|||No effect on the reduction of BCR-induced IL2 secretion, nor on the interaction with the SH2 domain of INPP5D or CSK nor on BCR-triggered tyrosine phosphorylation; when associated with F-378.|||No effect on the reduction of BCR-induced IL2 secretion, nor on the interaction with the SH2 domain of INPP5D or CSK nor on BCR-triggered tyrosine phosphorylation; when associated with F-399.|||PH|||Phosphoserine|||Phosphotyrosine|||Some reduction of BCR-induced IL2 secretion. Some interaction with INPP5DSH2 domain. Some decrease in BCR-triggered tyrosine phosphorylation. Abolishes reduction of BCR-induced IL2 secretion, the interaction with INPP5DSH2 domain and BCR-triggered tyrosine phosphorylation; when associated with F-325. ^@ http://purl.uniprot.org/annotation/PRO_0000187273 http://togogenome.org/gene/10090:Gnai2 ^@ http://purl.uniprot.org/uniprot/P08752 ^@ 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 ^@ G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(i) subunit alpha-2|||N-myristoyl glycine|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000203681 http://togogenome.org/gene/10090:Slc43a3 ^@ http://purl.uniprot.org/uniprot/A2AVZ9 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Equilibrative nucleobase transporter 1|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000305037|||http://purl.uniprot.org/annotation/VSP_028193 http://togogenome.org/gene/10090:Me2 ^@ http://purl.uniprot.org/uniprot/Q99KE1 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Transit Peptide ^@ Mitochondrion|||N6-acetyllysine|||NAD-dependent malic enzyme, mitochondrial|||Proton acceptor|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000018538 http://togogenome.org/gene/10090:Klhdc7b ^@ http://purl.uniprot.org/uniprot/E9Q9M9 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Glyatl3 ^@ http://purl.uniprot.org/uniprot/E9Q5L8 ^@ Chain|||Molecule Processing ^@ Chain ^@ Glycine-N-acyltransferase-like protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000446855 http://togogenome.org/gene/10090:Rbm26 ^@ http://purl.uniprot.org/uniprot/E9PUF4|||http://purl.uniprot.org/uniprot/Q6NZN0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||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 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 5.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||RNA-binding protein 26|||RRM|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000273377|||http://purl.uniprot.org/annotation/VSP_022533|||http://purl.uniprot.org/annotation/VSP_022534|||http://purl.uniprot.org/annotation/VSP_022535 http://togogenome.org/gene/10090:Sars ^@ http://purl.uniprot.org/uniprot/P26638|||http://purl.uniprot.org/uniprot/Q8C483 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site ^@ Aminoacyl-transfer RNA synthetases class-II family profile|||Basic and acidic residues|||Disordered|||Important for serine binding|||Interaction with tRNA|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Serine--tRNA ligase, cytoplasmic ^@ http://purl.uniprot.org/annotation/PRO_0000122192 http://togogenome.org/gene/10090:Vmn1r215 ^@ http://purl.uniprot.org/uniprot/Q8R264 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Optn ^@ http://purl.uniprot.org/uniprot/Q8K3K8 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Zinc Finger ^@ Basic and acidic residues|||CCHC NOA-type|||Disordered|||Disrupts direct interaction with Rab8; accumulation in the retinal outer plexiform layer; loss of retinal ganglion cells and connecting synapses, degeneration of entire retina without elevation of intraocular pressure.|||Interaction with HD|||Interaction with MYO6|||Interaction with Rab8|||LIR|||Optineurin|||Phosphoserine|||UBAN ^@ http://purl.uniprot.org/annotation/PRO_0000058069 http://togogenome.org/gene/10090:Srp72 ^@ http://purl.uniprot.org/uniprot/F8VQC1|||http://purl.uniprot.org/uniprot/Q3UZL8|||http://purl.uniprot.org/uniprot/Q9CS54 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat ^@ Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||Signal recognition particle SRP72 subunit RNA-binding|||TPR ^@ http://togogenome.org/gene/10090:Fdxacb1 ^@ http://purl.uniprot.org/uniprot/Q3UY23 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Splice Variant ^@ FDX-ACB|||Ferredoxin-fold anticodon-binding domain-containing protein 1 homolog|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000325957|||http://purl.uniprot.org/annotation/VSP_032499|||http://purl.uniprot.org/annotation/VSP_032500|||http://purl.uniprot.org/annotation/VSP_032501 http://togogenome.org/gene/10090:Slitrk6 ^@ http://purl.uniprot.org/uniprot/A6H6M2|||http://purl.uniprot.org/uniprot/Q8C110 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||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|||LRRCT 1|||LRRCT 2|||LRRNT 1|||LRRNT 2|||SLIT and NTRK-like protein 6 ^@ http://purl.uniprot.org/annotation/PRO_0000032684|||http://purl.uniprot.org/annotation/PRO_5014297009 http://togogenome.org/gene/10090:Unc45b ^@ http://purl.uniprot.org/uniprot/Q8CGY6 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||Splice Variant ^@ ARM 1|||ARM 2|||ARM 3|||In isoform 2.|||Protein unc-45 homolog B|||TPR 1|||TPR 2|||TPR 3 ^@ http://purl.uniprot.org/annotation/PRO_0000249893|||http://purl.uniprot.org/annotation/VSP_020588 http://togogenome.org/gene/10090:Chd3 ^@ http://purl.uniprot.org/uniprot/B1AR17|||http://purl.uniprot.org/uniprot/E9Q614|||http://purl.uniprot.org/uniprot/Q8BR71|||http://purl.uniprot.org/uniprot/Q8K0T3 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Basic residues|||CHD C-terminal 2|||Chromo|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||PHD-type|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Cgn ^@ http://purl.uniprot.org/uniprot/A0A5F8MPT6 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Myosin tail|||Polar residues ^@ http://togogenome.org/gene/10090:Sec22a ^@ http://purl.uniprot.org/uniprot/B2RSR2|||http://purl.uniprot.org/uniprot/Q8BH47 ^@ Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Longin|||Lumenal|||N-acetylserine|||Phosphoserine|||Removed|||Vesicle-trafficking protein SEC22a ^@ http://purl.uniprot.org/annotation/PRO_0000253045 http://togogenome.org/gene/10090:Ddx20 ^@ http://purl.uniprot.org/uniprot/Q9JJY4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable ATP-dependent RNA helicase DDX20|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000055026 http://togogenome.org/gene/10090:Kmt2e ^@ http://purl.uniprot.org/uniprot/Q3UG20 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||Disordered|||HCFC1-binding motif (HBM)|||In isoform 2.|||Inactive histone-lysine N-methyltransferase 2E|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||PHD-type|||Phosphoserine|||Polar residues|||Pro residues|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000341420|||http://purl.uniprot.org/annotation/VSP_052813 http://togogenome.org/gene/10090:D630023F18Rik ^@ http://purl.uniprot.org/uniprot/B2RQD7|||http://purl.uniprot.org/uniprot/D3YUK5|||http://purl.uniprot.org/uniprot/Q8C3M9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues|||Uncharacterized protein C2orf80 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000326124 http://togogenome.org/gene/10090:Zbtb9 ^@ http://purl.uniprot.org/uniprot/Q8CDC7 ^@ 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 ^@ BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Zinc finger and BTB domain-containing protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000047724 http://togogenome.org/gene/10090:Pirb ^@ http://purl.uniprot.org/uniprot/P97484 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Abolishes interaction with PTPN6/SHP-1 and PTPN11/SHP-2; when associated with F-794.|||Abolishes interaction with PTPN6/SHP-1 and PTPN11/SHP-2; when associated with F-824.|||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|||Ig-like C2-type 5|||Ig-like C2-type 6|||Leukocyte immunoglobulin-like receptor subfamily B member 3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by LYN|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000414708 http://togogenome.org/gene/10090:Ly6g ^@ http://purl.uniprot.org/uniprot/P35461 ^@ 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|||Lymphocyte antigen 6G|||Removed in mature form|||UPAR/Ly6 ^@ http://purl.uniprot.org/annotation/PRO_0000036146|||http://purl.uniprot.org/annotation/PRO_0000036147 http://togogenome.org/gene/10090:Or4f53 ^@ http://purl.uniprot.org/uniprot/Q8VF40 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zdhhc23 ^@ http://purl.uniprot.org/uniprot/B7ZNY8|||http://purl.uniprot.org/uniprot/Q5Y5T3 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Helical|||Interaction with NOS1|||Lumenal|||Palmitoyltransferase DHHC|||Palmitoyltransferase ZDHHC23|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212913 http://togogenome.org/gene/10090:Crebl2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0D8|||http://purl.uniprot.org/uniprot/Q32M00 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ BZIP|||Basic motif|||Disordered|||Leucine-zipper|||Polar residues|||bZIP|||cAMP-responsive element-binding protein-like 2 ^@ http://purl.uniprot.org/annotation/PRO_0000318193 http://togogenome.org/gene/10090:Ssh1 ^@ http://purl.uniprot.org/uniprot/F8WHT2|||http://purl.uniprot.org/uniprot/Q76I79 ^@ 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|||In isoform 2.|||Interaction with YWHAG|||N-acetylalanine|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Protein phosphatase Slingshot homolog 1|||Removed|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094842|||http://purl.uniprot.org/annotation/VSP_016320 http://togogenome.org/gene/10090:Ankrd55 ^@ http://purl.uniprot.org/uniprot/A7MCU1|||http://purl.uniprot.org/uniprot/E9Q0E9|||http://purl.uniprot.org/uniprot/Q8BLD6|||http://purl.uniprot.org/uniprot/Q8BV14|||http://purl.uniprot.org/uniprot/Q8BYH9 ^@ 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|||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|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000274411 http://togogenome.org/gene/10090:Cyct ^@ http://purl.uniprot.org/uniprot/P00015 ^@ 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 ^@ Cytochrome c, testis-specific|||N-acetylglycine|||Removed|||axial binding residue|||covalent ^@ http://purl.uniprot.org/annotation/PRO_0000108226 http://togogenome.org/gene/10090:Bcar3 ^@ http://purl.uniprot.org/uniprot/Q9QZK2 ^@ 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 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Abolishes interaction with NEDD9.|||Breast cancer anti-estrogen resistance protein 3 homolog|||Disordered|||In isoform 2.|||Mediates the interaction with BCAR1/p130CAS|||N-acetylalanine|||N6-methyllysine|||No effect on interaction with NEDD9.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Ras-GEF|||Removed|||Required for interaction with NEDD9|||SH2 ^@ http://purl.uniprot.org/annotation/PRO_0000230286|||http://purl.uniprot.org/annotation/VSP_017815 http://togogenome.org/gene/10090:Tfr2 ^@ http://purl.uniprot.org/uniprot/Q9JKX3 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endocytosis signal|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) asparagine|||Transferrin receptor protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000174137|||http://purl.uniprot.org/annotation/VSP_005356|||http://purl.uniprot.org/annotation/VSP_005357|||http://purl.uniprot.org/annotation/VSP_005358 http://togogenome.org/gene/10090:Pyy ^@ http://purl.uniprot.org/uniprot/H3BK86|||http://purl.uniprot.org/uniprot/Q3V334|||http://purl.uniprot.org/uniprot/Q9EPS2 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Modified Residue|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ Cleavage; by FAP|||Peptide YY|||Peptide YY(3-36)|||Phosphoserine|||Tyrosine amide ^@ http://purl.uniprot.org/annotation/PRO_0000025387|||http://purl.uniprot.org/annotation/PRO_0000025388|||http://purl.uniprot.org/annotation/PRO_0000430664|||http://purl.uniprot.org/annotation/PRO_5014309194|||http://purl.uniprot.org/annotation/PRO_5015093548 http://togogenome.org/gene/10090:Zng1 ^@ http://purl.uniprot.org/uniprot/Q8VEH6 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Splice Variant ^@ CXCC motif|||CobW C-terminal|||In isoform 2.|||Zinc-regulated GTPase metalloprotein activator 1|||psi-PxLVp motif ^@ http://purl.uniprot.org/annotation/PRO_0000245524|||http://purl.uniprot.org/annotation/VSP_019735 http://togogenome.org/gene/10090:Unc93b1 ^@ http://purl.uniprot.org/uniprot/E9PYK0|||http://purl.uniprot.org/uniprot/Q8VCW4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Acidic residues|||Decreases interaction with TLR3.|||Disordered|||Helical|||In isoform 2.|||Increases interaction with TLR3.|||Increases the TLR7 response and decreases the TLR9 response.|||Increases the TLR7 response and decreases the TLR9 response. Enhances interaction with TLR7, TLR8 and TLR13 and TLR7 transport to endolysosomes in presence of single-stranded RNA. Decreases affinity for TLR9 and its transport to endolysosomes in presence of DNA.|||Loss of function in TLR signaling. Impaired in its own transport from endoplasmic reticulum to endosome, lysosome and phagosome. Loss of the interaction with TLR3, TLR7, TLR9 and TLR13 and of the ability to transport them to endolysosome.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with TLR3.|||Phosphoserine|||Protein unc-93 homolog B1|||Strongly decreases interaction with TLR3. ^@ http://purl.uniprot.org/annotation/PRO_0000190041|||http://purl.uniprot.org/annotation/VSP_014036 http://togogenome.org/gene/10090:Mttp ^@ http://purl.uniprot.org/uniprot/O08601 ^@ 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.|||Microsomal triglyceride transfer protein large subunit|||Vitellogenin ^@ http://purl.uniprot.org/annotation/PRO_0000041595|||http://purl.uniprot.org/annotation/VSP_038546 http://togogenome.org/gene/10090:1700030K09Rik ^@ http://purl.uniprot.org/uniprot/Q922C1 ^@ 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|||Uncharacterized protein C19orf44 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000291922 http://togogenome.org/gene/10090:Il12rb2 ^@ http://purl.uniprot.org/uniprot/D3Z6H5|||http://purl.uniprot.org/uniprot/P97378 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Box 1 motif|||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|||Interleukin-12 receptor subunit beta-2|||N-linked (GlcNAc...) asparagine|||No loss of IL12-induced STAT4 activation nor T-cell proliferation. No effect on IFN-gamma production.|||No loss of IL12-induced STAT4 activation. Greatly reduced IL12-induced T-cell proliferation and IFN-gamma production.|||Phosphotyrosine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010921 http://togogenome.org/gene/10090:Tmem43 ^@ http://purl.uniprot.org/uniprot/Q9DBS1 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Modified Residue|||Topological Domain|||Transmembrane ^@ Helical|||N-acetylalanine|||Nuclear|||Perinuclear space|||Removed|||Transmembrane protein 43 ^@ http://purl.uniprot.org/annotation/PRO_0000284499 http://togogenome.org/gene/10090:Emc9 ^@ http://purl.uniprot.org/uniprot/Q793L1|||http://purl.uniprot.org/uniprot/Q9DB76 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ ER membrane protein complex subunit 9|||MPN ^@ http://purl.uniprot.org/annotation/PRO_0000221190 http://togogenome.org/gene/10090:Ndn ^@ http://purl.uniprot.org/uniprot/P25233 ^@ Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant ^@ Chain|||Domain Extent|||Region|||Sequence Variant ^@ Disordered|||MAGE|||Necdin ^@ http://purl.uniprot.org/annotation/PRO_0000156741 http://togogenome.org/gene/10090:Tmeff1 ^@ http://purl.uniprot.org/uniprot/Q6PFE7 ^@ 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 and isoform 3.|||In isoform 3.|||Kazal-like 1|||Kazal-like 2|||N-linked (GlcNAc...) asparagine|||Polar residues|||Tomoregulin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000286057|||http://purl.uniprot.org/annotation/VSP_024960|||http://purl.uniprot.org/annotation/VSP_024961 http://togogenome.org/gene/10090:Brox ^@ http://purl.uniprot.org/uniprot/Q8K2Q7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Splice Variant ^@ BRO1|||BRO1 domain-containing protein BROX|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||In isoform 2.|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000304613|||http://purl.uniprot.org/annotation/PRO_0000396737|||http://purl.uniprot.org/annotation/VSP_028041|||http://purl.uniprot.org/annotation/VSP_028042 http://togogenome.org/gene/10090:Gtf2h2 ^@ http://purl.uniprot.org/uniprot/Q7TPV0|||http://purl.uniprot.org/uniprot/Q9JIB4 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||Zinc Finger ^@ C4-type|||General transcription factor IIH subunit 2|||Phosphotyrosine|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000119249 http://togogenome.org/gene/10090:Or5an11 ^@ http://purl.uniprot.org/uniprot/E9Q9Z6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Letm2 ^@ http://purl.uniprot.org/uniprot/Q7TNU7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Disordered|||Helical|||LETM1 domain-containing protein LETM2, mitochondrial|||Letm1 RBD|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000307138 http://togogenome.org/gene/10090:Krt39 ^@ http://purl.uniprot.org/uniprot/Q6IFX4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type I cytoskeletal 39|||Linker 1|||Linker 12|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000314854 http://togogenome.org/gene/10090:Serpina3a ^@ http://purl.uniprot.org/uniprot/H7BWY0|||http://purl.uniprot.org/uniprot/Q6P4P1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant ^@ In isoform 2.|||N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond|||Serine protease inhibitor A3A|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_0000032414|||http://purl.uniprot.org/annotation/PRO_5015093755|||http://purl.uniprot.org/annotation/VSP_014229|||http://purl.uniprot.org/annotation/VSP_014230 http://togogenome.org/gene/10090:Zfp748 ^@ http://purl.uniprot.org/uniprot/Q3V1X2|||http://purl.uniprot.org/uniprot/Q7TPL6 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:H4c8 ^@ http://purl.uniprot.org/uniprot/B2RTM0|||http://purl.uniprot.org/uniprot/P62806 ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand ^@ Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand ^@ Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||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|||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|||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_0000158329 http://togogenome.org/gene/10090:Sstr1 ^@ http://purl.uniprot.org/uniprot/P30873|||http://purl.uniprot.org/uniprot/Q543T0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||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|||N-linked (GlcNAc...) asparagine|||Polar residues|||S-palmitoyl cysteine|||Somatostatin receptor type 1 ^@ http://purl.uniprot.org/annotation/PRO_0000070117 http://togogenome.org/gene/10090:Itsn1 ^@ http://purl.uniprot.org/uniprot/E9Q0N0|||http://purl.uniprot.org/uniprot/Q6NZJ5|||http://purl.uniprot.org/uniprot/Q8C4B5|||http://purl.uniprot.org/uniprot/Q9Z0R4 ^@ 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|||Site|||Splice Variant|||Strand ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand ^@ Basic and acidic residues|||Bipartite nuclear localization signal; in isoform 2|||C2|||DH|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EH|||EH 1|||EH 2|||In isoform 2.|||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_0000080958|||http://purl.uniprot.org/annotation/VSP_004296 http://togogenome.org/gene/10090:Gm10439 ^@ http://purl.uniprot.org/uniprot/A2AJU2|||http://purl.uniprot.org/uniprot/Q32MH1 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered ^@ http://togogenome.org/gene/10090:Trappc11 ^@ http://purl.uniprot.org/uniprot/B2RXC1 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Modified Residue|||Splice Variant ^@ In isoform 2.|||N6-acetyllysine|||Trafficking protein particle complex subunit 11 ^@ http://purl.uniprot.org/annotation/PRO_0000348073|||http://purl.uniprot.org/annotation/VSP_035100|||http://purl.uniprot.org/annotation/VSP_035101|||http://purl.uniprot.org/annotation/VSP_035102 http://togogenome.org/gene/10090:Cnksr1 ^@ http://purl.uniprot.org/uniprot/A2A9K7 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ CRIC|||Disordered|||PDZ|||PH|||Polar residues|||SAM ^@ http://togogenome.org/gene/10090:Shroom2 ^@ http://purl.uniprot.org/uniprot/A2ALU4|||http://purl.uniprot.org/uniprot/A7TU71|||http://purl.uniprot.org/uniprot/Q8C7N5 ^@ 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 ^@ ASD1|||ASD2|||Basic and acidic residues|||Disordered|||In isoform 2.|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein Shroom2 ^@ http://purl.uniprot.org/annotation/PRO_0000286063|||http://purl.uniprot.org/annotation/VSP_024964 http://togogenome.org/gene/10090:Aim2 ^@ http://purl.uniprot.org/uniprot/Q91VJ1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand|||Turn ^@ Disordered|||HIN-200|||Interferon-inducible protein AIM2|||Polar residues|||Pyrin ^@ http://purl.uniprot.org/annotation/PRO_0000334528 http://togogenome.org/gene/10090:Gmeb1 ^@ http://purl.uniprot.org/uniprot/Q3UYV4|||http://purl.uniprot.org/uniprot/Q9JL60 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glucocorticoid modulatory element-binding protein 1|||N-acetylalanine|||Removed|||SAND ^@ http://purl.uniprot.org/annotation/PRO_0000074090 http://togogenome.org/gene/10090:Dgkg ^@ http://purl.uniprot.org/uniprot/Q570Z5|||http://purl.uniprot.org/uniprot/Q8C413|||http://purl.uniprot.org/uniprot/Q91WG7 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Zinc Finger ^@ DAGKc|||Diacylglycerol kinase gamma|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000218460 http://togogenome.org/gene/10090:Or5v1b ^@ http://purl.uniprot.org/uniprot/Q7TRK1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pou2af2 ^@ http://purl.uniprot.org/uniprot/Q9D8Q6 ^@ 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.|||OCA|||POU domain class 2-associating factor 2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000263612|||http://purl.uniprot.org/annotation/VSP_061593 http://togogenome.org/gene/10090:Or5b108 ^@ http://purl.uniprot.org/uniprot/Q8VFW3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tpm1 ^@ http://purl.uniprot.org/uniprot/A0A2R2Y2P8|||http://purl.uniprot.org/uniprot/B7ZNL3|||http://purl.uniprot.org/uniprot/E9Q448|||http://purl.uniprot.org/uniprot/E9Q450|||http://purl.uniprot.org/uniprot/E9Q452|||http://purl.uniprot.org/uniprot/E9Q453|||http://purl.uniprot.org/uniprot/E9Q454|||http://purl.uniprot.org/uniprot/E9Q455|||http://purl.uniprot.org/uniprot/G5E8R0|||http://purl.uniprot.org/uniprot/G5E8R1|||http://purl.uniprot.org/uniprot/G5E8R2|||http://purl.uniprot.org/uniprot/P58771|||http://purl.uniprot.org/uniprot/Q545Y3|||http://purl.uniprot.org/uniprot/Q564G1|||http://purl.uniprot.org/uniprot/Q8BP43 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine|||Tropomyosin alpha-1 chain ^@ http://purl.uniprot.org/annotation/PRO_0000205621|||http://purl.uniprot.org/annotation/VSP_006580 http://togogenome.org/gene/10090:Herc1 ^@ http://purl.uniprot.org/uniprot/E9PZP8 ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Site ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ B30.2/SPRY|||Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||HECT|||Polar residues|||RCC1|||WD ^@ http://togogenome.org/gene/10090:Or5p50 ^@ http://purl.uniprot.org/uniprot/Q8VF66 ^@ 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 5P50 ^@ http://purl.uniprot.org/annotation/PRO_0000150830 http://togogenome.org/gene/10090:Fbxw13 ^@ http://purl.uniprot.org/uniprot/Q8BI57 ^@ Domain Extent|||Region ^@ Domain Extent ^@ F-box ^@ http://togogenome.org/gene/10090:Fkbp3 ^@ http://purl.uniprot.org/uniprot/Q3UBU9|||http://purl.uniprot.org/uniprot/Q62446 ^@ 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_0000075308 http://togogenome.org/gene/10090:C2cd2l ^@ http://purl.uniprot.org/uniprot/Q3U590|||http://purl.uniprot.org/uniprot/Q80X80|||http://purl.uniprot.org/uniprot/Q9DBJ2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||C2|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Phospholipid transfer protein C2CD2L|||Phosphoserine|||Phosphothreonine|||Polar residues|||SMP-LBD ^@ http://purl.uniprot.org/annotation/PRO_0000072597 http://togogenome.org/gene/10090:Lztr1 ^@ http://purl.uniprot.org/uniprot/Q9CQ33 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ BTB 1|||BTB 2|||Disordered|||In isoform 2.|||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_0000119136|||http://purl.uniprot.org/annotation/VSP_007170 http://togogenome.org/gene/10090:Cnot6 ^@ http://purl.uniprot.org/uniprot/Q8K3P5 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ CCR4-NOT transcription complex subunit 6|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||Nuclease domain|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000218574|||http://purl.uniprot.org/annotation/VSP_009938|||http://purl.uniprot.org/annotation/VSP_009939 http://togogenome.org/gene/10090:Vmn1r255 ^@ http://purl.uniprot.org/uniprot/K9J7G9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Apex2 ^@ http://purl.uniprot.org/uniprot/A2AFM3|||http://purl.uniprot.org/uniprot/Q68G58 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Basic residues|||DNA-(apurinic or apyrimidinic site) endonuclease 2|||Disordered|||GRF-type|||Important for catalytic activity|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with DNA substrate|||Polar residues|||Proton acceptor|||Proton donor/acceptor|||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_0000200015|||http://purl.uniprot.org/annotation/VSP_015346|||http://purl.uniprot.org/annotation/VSP_015347|||http://purl.uniprot.org/annotation/VSP_015348|||http://purl.uniprot.org/annotation/VSP_015349|||http://purl.uniprot.org/annotation/VSP_015350|||http://purl.uniprot.org/annotation/VSP_015351|||http://purl.uniprot.org/annotation/VSP_015352 http://togogenome.org/gene/10090:F9 ^@ http://purl.uniprot.org/uniprot/P16294 ^@ Active Site|||Binding Site|||Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site ^@ (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|||Interchain (between light and heavy chains)|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; alternate|||O-linked (Glc...) serine|||Peptidase S1|||Phosphoserine|||Phosphothreonine; alternate|||Sulfotyrosine|||via 4-carboxyglutamate ^@ http://purl.uniprot.org/annotation/PRO_0000027760|||http://purl.uniprot.org/annotation/PRO_0000027761|||http://purl.uniprot.org/annotation/PRO_0000027762|||http://purl.uniprot.org/annotation/PRO_0000027763|||http://purl.uniprot.org/annotation/PRO_0000027764 http://togogenome.org/gene/10090:Matn1 ^@ http://purl.uniprot.org/uniprot/P51942 ^@ 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_0000007496 http://togogenome.org/gene/10090:Matcap2 ^@ http://purl.uniprot.org/uniprot/Q7TQE7 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Region|||Splice Variant ^@ Disordered|||In isoform 2.|||Nucleophile|||Polar residues|||Putative tyrosine carboxypeptidase MATCAP2 ^@ http://purl.uniprot.org/annotation/PRO_0000320618|||http://purl.uniprot.org/annotation/VSP_031688 http://togogenome.org/gene/10090:Casp2 ^@ http://purl.uniprot.org/uniprot/P29594 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict ^@ CARD|||Caspase-2 subunit p12|||Caspase-2 subunit p13|||Caspase-2 subunit p18|||Disordered|||Loss of function.|||N-acetylalanine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000004546|||http://purl.uniprot.org/annotation/PRO_0000004547|||http://purl.uniprot.org/annotation/PRO_0000004548|||http://purl.uniprot.org/annotation/PRO_0000004549 http://togogenome.org/gene/10090:Mup8 ^@ http://purl.uniprot.org/uniprot/A2AKN8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Lipocalin/cytosolic fatty-acid binding ^@ http://purl.uniprot.org/annotation/PRO_5015086026 http://togogenome.org/gene/10090:Slc4a8 ^@ http://purl.uniprot.org/uniprot/Q3UR07|||http://purl.uniprot.org/uniprot/Q8JZR6 ^@ 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 ^@ Basic and acidic residues|||Basic residues|||Cytoplasmic|||Disordered|||Electroneutral sodium bicarbonate exchanger 1|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000328923|||http://purl.uniprot.org/annotation/VSP_052769 http://togogenome.org/gene/10090:Mkrn3 ^@ http://purl.uniprot.org/uniprot/Q60764 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger ^@ Chain|||Region|||Sequence Conflict|||Zinc Finger ^@ C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||Makorin-type Cys-His|||Probable E3 ubiquitin-protein ligase makorin-3|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000055960 http://togogenome.org/gene/10090:3830406C13Rik ^@ http://purl.uniprot.org/uniprot/Q8BGD0 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ Centrosomal protein 15 kDa|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000089389|||http://purl.uniprot.org/annotation/VSP_014596 http://togogenome.org/gene/10090:Gyg ^@ http://purl.uniprot.org/uniprot/Q9R062 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Binding Site|||Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Site ^@ Disordered|||Glycogenin-1|||Important for catalytic activity|||Interaction with GYS1|||N-acetylthreonine|||No loss of interaction with GYS2.|||O-linked (Glc...) tyrosine|||Phosphoserine|||Removed|||Severe loss of interaction with GYS2. ^@ http://purl.uniprot.org/annotation/PRO_0000215177 http://togogenome.org/gene/10090:Dydc2 ^@ http://purl.uniprot.org/uniprot/Q9D3X8 ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Synrg ^@ http://purl.uniprot.org/uniprot/Q5SV85 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant ^@ DFXDF motif 1|||DFXDF motif 2|||DFXDF motif 3|||Disordered|||EH|||In isoform 2.|||Interaction with AP1G1|||Interaction with AP1G1, AP1G2 and GGA1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Synergin gamma ^@ http://purl.uniprot.org/annotation/PRO_0000072388|||http://purl.uniprot.org/annotation/VSP_013251|||http://purl.uniprot.org/annotation/VSP_013252|||http://purl.uniprot.org/annotation/VSP_013253|||http://purl.uniprot.org/annotation/VSP_013254 http://togogenome.org/gene/10090:Sf3a2 ^@ http://purl.uniprot.org/uniprot/G3UVU2|||http://purl.uniprot.org/uniprot/Q7TN25 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||Matrin-type ^@ http://togogenome.org/gene/10090:Akr1c12 ^@ http://purl.uniprot.org/uniprot/Q9JLI0 ^@ Active Site|||Binding Site|||Domain Extent|||Region|||Site ^@ Active Site|||Binding Site|||Domain Extent|||Site ^@ Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor ^@ http://togogenome.org/gene/10090:Kank1 ^@ http://purl.uniprot.org/uniprot/E9Q238|||http://purl.uniprot.org/uniprot/Q6AXG6|||http://purl.uniprot.org/uniprot/Q8BRZ8 ^@ Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat ^@ ANK|||Acidic residues|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Fdft1 ^@ http://purl.uniprot.org/uniprot/P53798 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane ^@ Binding Site|||Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Squalene synthase ^@ http://purl.uniprot.org/annotation/PRO_0000067444 http://togogenome.org/gene/10090:Smyd1 ^@ http://purl.uniprot.org/uniprot/P97443|||http://purl.uniprot.org/uniprot/Q3UQT9 ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Histone-lysine N-methyltransferase Smyd1|||In isoform 2.|||In isoform 3.|||In strain: C57BL/6.|||MYND-type|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000218308|||http://purl.uniprot.org/annotation/VSP_050402|||http://purl.uniprot.org/annotation/VSP_050403|||http://purl.uniprot.org/annotation/VSP_050404 http://togogenome.org/gene/10090:Rbfa ^@ http://purl.uniprot.org/uniprot/Q3UKZ0|||http://purl.uniprot.org/uniprot/Q6P3B9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Transit Peptide ^@ Basic and acidic residues|||Disordered|||Mitochondrion|||Putative ribosome-binding factor A, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000030227 http://togogenome.org/gene/10090:Isl1 ^@ http://purl.uniprot.org/uniprot/A2RSV5|||http://purl.uniprot.org/uniprot/P61372|||http://purl.uniprot.org/uniprot/Q8BTH7 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand|||Turn ^@ Disordered|||Homeobox|||In isoform 2.|||Insulin gene enhancer protein ISL-1|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM-binding domain (LID)|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000075748|||http://purl.uniprot.org/annotation/VSP_010338 http://togogenome.org/gene/10090:Padi3 ^@ http://purl.uniprot.org/uniprot/Q5DTJ8|||http://purl.uniprot.org/uniprot/Q9Z184 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict ^@ Protein-arginine deiminase (PAD) N-terminal|||Protein-arginine deiminase (PAD) central|||Protein-arginine deiminase C-terminal|||Protein-arginine deiminase type-3 ^@ http://purl.uniprot.org/annotation/PRO_0000220030 http://togogenome.org/gene/10090:Phip ^@ http://purl.uniprot.org/uniprot/F8VQ93 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Basic and acidic residues|||Bromo|||Disordered|||Polar residues|||WD ^@ http://togogenome.org/gene/10090:Esco2 ^@ http://purl.uniprot.org/uniprot/Q8CIB9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||CCHH-type|||Disordered|||N-acetyltransferase ESCO2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000074543 http://togogenome.org/gene/10090:Tff2 ^@ http://purl.uniprot.org/uniprot/Q9QX97 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide ^@ P-type ^@ http://purl.uniprot.org/annotation/PRO_5015099943 http://togogenome.org/gene/10090:Csnk2b ^@ http://purl.uniprot.org/uniprot/P67871 ^@ Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Casein kinase II subunit beta|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Interaction with alpha subunit|||KSSR motif|||N-acetylserine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000068237 http://togogenome.org/gene/10090:Obp1a ^@ http://purl.uniprot.org/uniprot/Q9D3H2 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Odorant-binding protein 1a ^@ http://purl.uniprot.org/annotation/PRO_5006751578 http://togogenome.org/gene/10090:Tlx2 ^@ http://purl.uniprot.org/uniprot/Q61663 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Region ^@ Disordered|||Homeobox|||Pro residues|||T-cell leukemia homeobox protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000049337 http://togogenome.org/gene/10090:Vmn1r115 ^@ http://purl.uniprot.org/uniprot/K7N6Y3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Nek1 ^@ http://purl.uniprot.org/uniprot/B2RXQ4|||http://purl.uniprot.org/uniprot/B2RXX0|||http://purl.uniprot.org/uniprot/B7ZWK0|||http://purl.uniprot.org/uniprot/P51954|||http://purl.uniprot.org/uniprot/Q3UXI0 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Loss of 14-3-3 protein-binding.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek1 ^@ http://purl.uniprot.org/annotation/PRO_0000086419 http://togogenome.org/gene/10090:Actrt3 ^@ http://purl.uniprot.org/uniprot/Q8BXF8 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Actin-related protein T3 ^@ http://purl.uniprot.org/annotation/PRO_0000089143 http://togogenome.org/gene/10090:Cd38 ^@ http://purl.uniprot.org/uniprot/P56528|||http://purl.uniprot.org/uniprot/Q3UCS6|||http://purl.uniprot.org/uniprot/Q4FJL8 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000144068 http://togogenome.org/gene/10090:Atg14 ^@ http://purl.uniprot.org/uniprot/Q8CDJ3 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Modified Residue|||Region ^@ BATS|||Beclin 1-associated autophagy-related key regulator|||Disordered|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000050775 http://togogenome.org/gene/10090:Themis3 ^@ http://purl.uniprot.org/uniprot/Q9CU24 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ CABIT 1|||CABIT 2|||Protein THEMIS3 ^@ http://purl.uniprot.org/annotation/PRO_0000383152 http://togogenome.org/gene/10090:Cfap210 ^@ http://purl.uniprot.org/uniprot/A0JLY1 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Region ^@ Cilia- and flagella- associated protein 210|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000318847 http://togogenome.org/gene/10090:Mta3 ^@ http://purl.uniprot.org/uniprot/E9Q794|||http://purl.uniprot.org/uniprot/Q3U3A7|||http://purl.uniprot.org/uniprot/Q3UII8|||http://purl.uniprot.org/uniprot/Q924K8 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger ^@ BAH|||Disordered|||ELM2|||GATA-type; atypical|||In isoform 2.|||Metastasis-associated protein MTA3|||Phosphoserine|||Phosphothreonine|||SANT ^@ http://purl.uniprot.org/annotation/PRO_0000083499|||http://purl.uniprot.org/annotation/VSP_001605|||http://purl.uniprot.org/annotation/VSP_001606 http://togogenome.org/gene/10090:Grap2 ^@ http://purl.uniprot.org/uniprot/O89100|||http://purl.uniprot.org/uniprot/Q3U0E8 ^@ Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn ^@ Disordered|||GRB2-related adaptor protein 2|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||SH2|||SH3|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000088209 http://togogenome.org/gene/10090:Zfp438 ^@ http://purl.uniprot.org/uniprot/Q8BFX2|||http://purl.uniprot.org/uniprot/Q8BXJ4 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Cyp2e1 ^@ http://purl.uniprot.org/uniprot/Q05421 ^@ Binding Site|||Chain|||Molecule Processing|||Site ^@ Binding Site|||Chain ^@ Cytochrome P450 2E1|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051755 http://togogenome.org/gene/10090:Hapln1 ^@ http://purl.uniprot.org/uniprot/Q9QUP5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict ^@ Hyaluronan and proteoglycan link protein 1|||Ig-like V-type|||Link 1|||Link 2|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000013179|||http://purl.uniprot.org/annotation/PRO_0000013180 http://togogenome.org/gene/10090:Gprc5a ^@ http://purl.uniprot.org/uniprot/G5E8C3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Region|||Transmembrane ^@ Disordered|||G-protein coupled receptors family 3 profile|||Helical ^@ http://togogenome.org/gene/10090:Mrpl49 ^@ http://purl.uniprot.org/uniprot/Q9CQ40 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Large ribosomal subunit protein mL49 ^@ http://purl.uniprot.org/annotation/PRO_0000207666 http://togogenome.org/gene/10090:Anxa3 ^@ http://purl.uniprot.org/uniprot/O35639 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict ^@ Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A3|||N-acetylalanine|||N6-acetyllysine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067478 http://togogenome.org/gene/10090:Rin3 ^@ http://purl.uniprot.org/uniprot/P59729|||http://purl.uniprot.org/uniprot/Q3U332|||http://purl.uniprot.org/uniprot/Q6PDX1 ^@ 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|||Interaction with RAB5B|||Polar residues|||Pro residues|||Ras and Rab interactor 3|||Ras-associating|||SH2|||VPS9 ^@ http://purl.uniprot.org/annotation/PRO_0000191323 http://togogenome.org/gene/10090:Ppbp ^@ http://purl.uniprot.org/uniprot/Q9EQI5 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Chemokine interleukin-8-like ^@ http://purl.uniprot.org/annotation/PRO_5015099719 http://togogenome.org/gene/10090:Isg20 ^@ http://purl.uniprot.org/uniprot/Q3UW00|||http://purl.uniprot.org/uniprot/Q4FK39|||http://purl.uniprot.org/uniprot/Q9JL16 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Splice Variant ^@ Exonuclease|||In isoform 2.|||Interferon-stimulated gene 20 kDa protein ^@ http://purl.uniprot.org/annotation/PRO_0000084244|||http://purl.uniprot.org/annotation/VSP_012431|||http://purl.uniprot.org/annotation/VSP_012432 http://togogenome.org/gene/10090:Fbln1 ^@ http://purl.uniprot.org/uniprot/B2CQD6|||http://purl.uniprot.org/uniprot/Q08879|||http://purl.uniprot.org/uniprot/Q3TWK8 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Anaphylatoxin-like|||Anaphylatoxin-like 1|||Anaphylatoxin-like 2|||Anaphylatoxin-like 3|||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|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Fibulin-1|||In isoform C.|||N-linked (GlcNAc...) asparagine|||Self-association and FN1-binding ^@ http://purl.uniprot.org/annotation/PRO_0000007564|||http://purl.uniprot.org/annotation/PRO_5004229787|||http://purl.uniprot.org/annotation/PRO_5014298277|||http://purl.uniprot.org/annotation/VSP_001386 http://togogenome.org/gene/10090:Plaa ^@ http://purl.uniprot.org/uniprot/P27612 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict ^@ ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||Loss of protein abundance. Increased abundance of ubiquitinated synaptic proteins. Decreased ubiquitin-mediated trafficking of membrane proteins through the endolysosomal pathway. Decreased synaptic vesicle recycling. Decreased cerebellar Purkinje cell migration and dendrite extension.|||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_0000051131 http://togogenome.org/gene/10090:Pthlh ^@ http://purl.uniprot.org/uniprot/Q540C1|||http://purl.uniprot.org/uniprot/Q924X4 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Basic residues|||Disordered|||Parathyroid hormone-related protein|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5014309579|||http://purl.uniprot.org/annotation/PRO_5015099525 http://togogenome.org/gene/10090:Rab38 ^@ http://purl.uniprot.org/uniprot/Q8QZZ8 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant ^@ Disrupts interaction with ANKRD27; inhibits peripheral distribution of TYRP1 in melanocytes.|||Effector region|||In cht.|||Inhibits the proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes.|||Ras-related protein Rab-38|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121252 http://togogenome.org/gene/10090:Ssmem1 ^@ http://purl.uniprot.org/uniprot/Q78FQ7|||http://purl.uniprot.org/uniprot/Q9D9Y8|||http://purl.uniprot.org/uniprot/Q9DAA0 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Pmp2 ^@ http://purl.uniprot.org/uniprot/P24526 ^@ Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue ^@ Myelin P2 protein|||N-acetylserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067389 http://togogenome.org/gene/10090:Ppp1cb ^@ http://purl.uniprot.org/uniprot/P62141 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylalanine|||Phosphothreonine|||Proton donor|||Removed|||Serine/threonine-protein phosphatase PP1-beta catalytic subunit ^@ http://purl.uniprot.org/annotation/PRO_0000058780 http://togogenome.org/gene/10090:Lrrc18 ^@ http://purl.uniprot.org/uniprot/Q9CQ07 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Repeat|||Sequence Conflict|||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_0000084473|||http://purl.uniprot.org/annotation/VSP_015741 http://togogenome.org/gene/10090:Gm14151 ^@ http://purl.uniprot.org/uniprot/A2AQX6 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||Protein kinase ^@ http://togogenome.org/gene/10090:Or52x1 ^@ http://purl.uniprot.org/uniprot/Q8VGX3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Recql5 ^@ http://purl.uniprot.org/uniprot/Q8VID5 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict ^@ ATP-dependent DNA helicase Q5|||Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Interaction with POLR2A|||Interaction with RAD51|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000423434 http://togogenome.org/gene/10090:Cers4 ^@ http://purl.uniprot.org/uniprot/Q9D6J1 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Ceramide synthase 4|||Cytoplasmic|||Disordered|||Helical|||Homeobox-like|||Last loop motif|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TLC ^@ http://purl.uniprot.org/annotation/PRO_0000185513 http://togogenome.org/gene/10090:Pate10 ^@ http://purl.uniprot.org/uniprot/B3GLJ5 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015087268 http://togogenome.org/gene/10090:Zkscan7 ^@ http://purl.uniprot.org/uniprot/E9PVW1 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues|||SCAN box ^@ http://togogenome.org/gene/10090:Fam184b ^@ http://purl.uniprot.org/uniprot/Q0KK56 ^@ 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|||Disordered|||In isoform 2.|||Polar residues|||Protein FAM184B ^@ http://purl.uniprot.org/annotation/PRO_0000320552|||http://purl.uniprot.org/annotation/VSP_031654|||http://purl.uniprot.org/annotation/VSP_031655 http://togogenome.org/gene/10090:Rasgrp3 ^@ http://purl.uniprot.org/uniprot/Q6NZH9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||EF-hand|||N-terminal Ras-GEF|||Phorbol-ester/DAG-type|||Ras-GEF ^@ http://togogenome.org/gene/10090:Oosp1 ^@ http://purl.uniprot.org/uniprot/Q925U0 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||Oocyte-secreted protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000343689|||http://purl.uniprot.org/annotation/VSP_034664|||http://purl.uniprot.org/annotation/VSP_034665 http://togogenome.org/gene/10090:Vmn2r83 ^@ http://purl.uniprot.org/uniprot/E9Q0G7 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003245775 http://togogenome.org/gene/10090:Zbed4 ^@ http://purl.uniprot.org/uniprot/Q80WQ9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ BED-type 1|||BED-type 2|||BED-type 3|||BED-type 4|||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_0000391794 http://togogenome.org/gene/10090:Acad9 ^@ http://purl.uniprot.org/uniprot/Q8JZN5 ^@ Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Complex I assembly factor ACAD9, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphothreonine|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000000525 http://togogenome.org/gene/10090:Vash2 ^@ http://purl.uniprot.org/uniprot/Q8C5G2 ^@ Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn ^@ Abolished tyrosine carboxypeptidase activity.|||Disordered|||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_0000189983 http://togogenome.org/gene/10090:Dhps ^@ http://purl.uniprot.org/uniprot/Q3TXU5 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict ^@ Deoxyhypusine synthase|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000314944 http://togogenome.org/gene/10090:Arhgef7 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0X8|||http://purl.uniprot.org/uniprot/Q9ES28 ^@ 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 ^@ Calponin-homology (CH)|||DH|||Disordered|||In isoform A and isoform D.|||In isoform C.|||In isoform D, isoform F and isoform G.|||In isoform E.|||In isoform F.|||In isoform H.|||PH|||Phosphoserine|||Polar residues|||Rho guanine nucleotide exchange factor 7|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000080922|||http://purl.uniprot.org/annotation/VSP_001816|||http://purl.uniprot.org/annotation/VSP_001817|||http://purl.uniprot.org/annotation/VSP_023051|||http://purl.uniprot.org/annotation/VSP_023052|||http://purl.uniprot.org/annotation/VSP_023053|||http://purl.uniprot.org/annotation/VSP_023054|||http://purl.uniprot.org/annotation/VSP_023055|||http://purl.uniprot.org/annotation/VSP_023056|||http://purl.uniprot.org/annotation/VSP_023057 http://togogenome.org/gene/10090:Kif18a ^@ http://purl.uniprot.org/uniprot/Q91WD7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ 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_0000125459 http://togogenome.org/gene/10090:Gga2 ^@ http://purl.uniprot.org/uniprot/Q6P5E6 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ ADP-ribosylation factor-binding protein GGA2|||Disordered|||GAE|||GAT|||In isoform 2.|||Unstructured hinge|||VHS ^@ http://purl.uniprot.org/annotation/PRO_0000212683|||http://purl.uniprot.org/annotation/VSP_013255 http://togogenome.org/gene/10090:Lxn ^@ http://purl.uniprot.org/uniprot/P70202 ^@ 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 ^@ Alpha-helical linker|||Cystatin LXN-type 1|||Cystatin LXN-type 2|||Latexin|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000191344 http://togogenome.org/gene/10090:Nav3 ^@ http://purl.uniprot.org/uniprot/A0A668KM70|||http://purl.uniprot.org/uniprot/E9QMF5 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Hdac7 ^@ http://purl.uniprot.org/uniprot/E9PX62|||http://purl.uniprot.org/uniprot/E9PXW1|||http://purl.uniprot.org/uniprot/E9PXW8|||http://purl.uniprot.org/uniprot/Q8C2B3 ^@ 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|||Site|||Splice Variant ^@ Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3.|||Contributes to catalysis|||Disordered|||Disrupts the dot-like nuclear pattern.|||Disrupts the dot-like nuclear pattern. Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3.|||Histone deacetylase|||Histone deacetylase 7|||In isoform 2 and isoform 4.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 4 and isoform 6.|||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|||Polar residues|||Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE.|||Transcription repression 1|||Transcription repression 2 ^@ http://purl.uniprot.org/annotation/PRO_0000114706|||http://purl.uniprot.org/annotation/VSP_007432|||http://purl.uniprot.org/annotation/VSP_007433|||http://purl.uniprot.org/annotation/VSP_007434|||http://purl.uniprot.org/annotation/VSP_007435 http://togogenome.org/gene/10090:Slc2a6 ^@ http://purl.uniprot.org/uniprot/Q3UDF0 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Glycosylation Site|||Motif|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 isoform 2.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 2, facilitated glucose transporter member 6 ^@ http://purl.uniprot.org/annotation/PRO_0000447625|||http://purl.uniprot.org/annotation/VSP_060214 http://togogenome.org/gene/10090:Slc22a26 ^@ http://purl.uniprot.org/uniprot/Q91WJ2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ Helical|||Major facilitator superfamily (MFS) profile ^@ http://togogenome.org/gene/10090:Tas2r121 ^@ http://purl.uniprot.org/uniprot/Q7M720 ^@ 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 13 ^@ http://purl.uniprot.org/annotation/PRO_0000082252 http://togogenome.org/gene/10090:Or56b34 ^@ http://purl.uniprot.org/uniprot/Q6W049 ^@ 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 56B34 ^@ http://purl.uniprot.org/annotation/PRO_0000409662 http://togogenome.org/gene/10090:Zfp541 ^@ http://purl.uniprot.org/uniprot/Q0GGX2 ^@ 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|||C2H2-type 4|||C2H2-type 5|||Disordered|||ELM2|||In isoform 2.|||Polar residues|||SANT|||Zinc finger protein 541 ^@ http://purl.uniprot.org/annotation/PRO_0000361545|||http://purl.uniprot.org/annotation/VSP_036221 http://togogenome.org/gene/10090:Hira ^@ http://purl.uniprot.org/uniprot/Q61666 ^@ 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 3.|||In isoform 4.|||In isoform Short.|||Interaction with ASF1A|||Interaction with CCNA1|||Interaction with PAX3|||Interaction with histone H2B|||Interaction with histone H4|||Phosphoserine|||Phosphothreonine|||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_0000051020|||http://purl.uniprot.org/annotation/VSP_006773|||http://purl.uniprot.org/annotation/VSP_006774|||http://purl.uniprot.org/annotation/VSP_025049|||http://purl.uniprot.org/annotation/VSP_025050|||http://purl.uniprot.org/annotation/VSP_025051|||http://purl.uniprot.org/annotation/VSP_025052 http://togogenome.org/gene/10090:Sult2a1 ^@ http://purl.uniprot.org/uniprot/P52843 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Proton acceptor|||Sulfotransferase 2A1 ^@ http://purl.uniprot.org/annotation/PRO_0000085147 http://togogenome.org/gene/10090:Gask1b ^@ http://purl.uniprot.org/uniprot/Q3UPI1 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Golgi-associated kinase 1B|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000288903 http://togogenome.org/gene/10090:Rhoj ^@ http://purl.uniprot.org/uniprot/Q9ER71 ^@ 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.|||Removed in mature form|||Rho-related GTP-binding protein RhoJ|||S-farnesyl cysteine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000198870|||http://purl.uniprot.org/annotation/PRO_0000281221|||http://purl.uniprot.org/annotation/VSP_005709 http://togogenome.org/gene/10090:Bpifa5 ^@ http://purl.uniprot.org/uniprot/Q9CQX3 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ BPI fold-containing family A member 5 ^@ http://purl.uniprot.org/annotation/PRO_0000017189 http://togogenome.org/gene/10090:Khdrbs3 ^@ http://purl.uniprot.org/uniprot/Q9R226 ^@ 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 splicing regulation.|||Confers SIAH1-mediated degradation and strong SIAH1 binding.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Involved in homodimerization|||KH|||KH domain-containing, RNA-binding, signal transduction-associated protein 3|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000232523 http://togogenome.org/gene/10090:Ankmy1 ^@ http://purl.uniprot.org/uniprot/E0CYY3|||http://purl.uniprot.org/uniprot/E9PUG3|||http://purl.uniprot.org/uniprot/Q8C0W1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||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|||MORN 1|||MORN 2|||MORN 3|||MYND-type|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000320065 http://togogenome.org/gene/10090:Ube2q1 ^@ http://purl.uniprot.org/uniprot/Q7TSS2 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||In isoform 2.|||Loss of ubiquitin binding. Normal dimer formation.|||N-acetylmethionine|||Polar residues|||UBC core|||Ubiquitin-conjugating enzyme E2 Q1 ^@ http://purl.uniprot.org/annotation/PRO_0000223877|||http://purl.uniprot.org/annotation/VSP_017297 http://togogenome.org/gene/10090:Psmg2 ^@ http://purl.uniprot.org/uniprot/Q9EST4 ^@ 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.|||Phosphothreonine|||Proteasome assembly chaperone 2 ^@ http://purl.uniprot.org/annotation/PRO_0000322553|||http://purl.uniprot.org/annotation/VSP_052691|||http://purl.uniprot.org/annotation/VSP_052692|||http://purl.uniprot.org/annotation/VSP_052693 http://togogenome.org/gene/10090:Foxp1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1H9|||http://purl.uniprot.org/uniprot/A0A0R4J282|||http://purl.uniprot.org/uniprot/D3Z6Q3|||http://purl.uniprot.org/uniprot/E2S038|||http://purl.uniprot.org/uniprot/H3BJ24|||http://purl.uniprot.org/uniprot/H3BLF2|||http://purl.uniprot.org/uniprot/P58462 ^@ 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|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ C2H2-type|||CTBP1-binding|||Disordered|||Fork-head|||Forkhead box protein P1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Leucine-zipper|||Loss of dimerization. Almost complete loss of DNA-binding. Reduced transcriptional repression activity.|||No significant effect on transcriptional repression activity.|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000009336|||http://purl.uniprot.org/annotation/VSP_001557|||http://purl.uniprot.org/annotation/VSP_018732|||http://purl.uniprot.org/annotation/VSP_026670|||http://purl.uniprot.org/annotation/VSP_057342 http://togogenome.org/gene/10090:Rnf103 ^@ http://purl.uniprot.org/uniprot/Q3TGP6|||http://purl.uniprot.org/uniprot/Q9R1W3 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase RNF103|||Helical|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056085 http://togogenome.org/gene/10090:Ppan ^@ http://purl.uniprot.org/uniprot/Q91YU8 ^@ 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|||Brix|||Disordered|||N6-acetyllysine|||Phosphoserine|||Suppressor of SWI4 1 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000120258 http://togogenome.org/gene/10090:Ncapd3 ^@ http://purl.uniprot.org/uniprot/K4DI67|||http://purl.uniprot.org/uniprot/Q3UTU7|||http://purl.uniprot.org/uniprot/Q6ZQK0|||http://purl.uniprot.org/uniprot/Q80W41 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ Basic and acidic residues|||Condensin complex subunit 1 C-terminal|||Condensin-2 complex subunit D3|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000050717 http://togogenome.org/gene/10090:Sapcd1 ^@ http://purl.uniprot.org/uniprot/Q9CY86 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Suppressor APC domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000244083 http://togogenome.org/gene/10090:Ckap4 ^@ http://purl.uniprot.org/uniprot/Q8BMK4 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Cytoskeleton-associated protein 4|||Disordered|||Extracellular|||Helical|||N6-acetyllysine|||Phosphoserine|||Pro residues|||S-palmitoyl cysteine; by ZDHHC2 ^@ http://purl.uniprot.org/annotation/PRO_0000252418 http://togogenome.org/gene/10090:Hdx ^@ http://purl.uniprot.org/uniprot/Q14B70 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Region|||Splice Variant ^@ 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_0000299488|||http://purl.uniprot.org/annotation/VSP_027709 http://togogenome.org/gene/10090:Ccrl2 ^@ http://purl.uniprot.org/uniprot/O35457 ^@ 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 ^@ C-C chemokine receptor-like 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_0000236800 http://togogenome.org/gene/10090:Tmtc1 ^@ http://purl.uniprot.org/uniprot/Q3UV71 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Polar residues|||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_0000280289|||http://purl.uniprot.org/annotation/VSP_023618 http://togogenome.org/gene/10090:Mapkap1 ^@ http://purl.uniprot.org/uniprot/Q8BKH7 ^@ 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.|||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_0000328033|||http://purl.uniprot.org/annotation/VSP_033208|||http://purl.uniprot.org/annotation/VSP_033209 http://togogenome.org/gene/10090:Slc16a12 ^@ http://purl.uniprot.org/uniprot/Q8BGC3 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Monocarboxylate transporter 12 ^@ http://purl.uniprot.org/annotation/PRO_0000286676 http://togogenome.org/gene/10090:Rps27l ^@ http://purl.uniprot.org/uniprot/Q6ZWY3 ^@ Chain|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Region|||Zinc Finger ^@ C4-type|||Disordered|||Small ribosomal subunit protein eS27-like ^@ http://purl.uniprot.org/annotation/PRO_0000149055 http://togogenome.org/gene/10090:Siglec15 ^@ http://purl.uniprot.org/uniprot/A7E1W8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Ig-like|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5015086551 http://togogenome.org/gene/10090:Grpr ^@ http://purl.uniprot.org/uniprot/P21729 ^@ 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|||Gastrin-releasing peptide receptor|||Helical; 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_0000069663 http://togogenome.org/gene/10090:L3mbtl4 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQK6|||http://purl.uniprot.org/uniprot/B1B1A0 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||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_0000337078|||http://purl.uniprot.org/annotation/VSP_033865|||http://purl.uniprot.org/annotation/VSP_033866 http://togogenome.org/gene/10090:Utf1 ^@ http://purl.uniprot.org/uniprot/B2RSF1|||http://purl.uniprot.org/uniprot/Q6J1H4 ^@ 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.|||Leucine-zipper|||Myb/SANT-like DNA-binding|||Phosphoserine|||Polar residues|||Undifferentiated embryonic cell transcription factor 1 ^@ http://purl.uniprot.org/annotation/PRO_0000274552|||http://purl.uniprot.org/annotation/VSP_052292 http://togogenome.org/gene/10090:Cracr2a ^@ http://purl.uniprot.org/uniprot/Q3UP38 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||EF-hand|||EF-hand calcium-binding domain-containing protein 4B|||In isoform 1.|||Polar residues|||Proline-rich domain (PRD) which mediates interaction with VAV1|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000283047|||http://purl.uniprot.org/annotation/VSP_060979|||http://purl.uniprot.org/annotation/VSP_060980 http://togogenome.org/gene/10090:Nudt9 ^@ http://purl.uniprot.org/uniprot/Q8BVU5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Transit Peptide ^@ ADP-ribose pyrophosphatase, mitochondrial|||Basic and acidic residues|||Disordered|||Mitochondrion|||Nudix box|||Nudix hydrolase|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000019951 http://togogenome.org/gene/10090:Pcdh15 ^@ http://purl.uniprot.org/uniprot/Q99PJ1 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ 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|||Impaired interaction with CDH23.|||In isoform 10 and isoform 12.|||In isoform 10.|||In isoform 11 and isoform 12.|||In isoform 12.|||In isoform 13.|||In isoform 14.|||In isoform 15.|||In isoform 16.|||In isoform 17.|||In isoform 18 and isoform 19.|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7, isoform 11, isoform 13, isoform 14, isoform 15, isoform 16, isoform 17, isoform 19, isoform 22 and isoform 23.|||In isoform 20.|||In isoform 21, isoform 22 and isoform 23.|||In isoform 23.|||In isoform 24.|||In isoform 25.|||In isoform 26.|||In isoform 3.|||In isoform 4, isoform 6 and isoform 7.|||In isoform 5.|||In isoform 6, isoform 7, isoform 9 and isoform 26.|||In isoform 7.|||In isoform 8 and isoform 9.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Protocadherin-15|||Strongly reduced interaction with CDH23. ^@ http://purl.uniprot.org/annotation/PRO_0000003999|||http://purl.uniprot.org/annotation/VSP_046576|||http://purl.uniprot.org/annotation/VSP_046577|||http://purl.uniprot.org/annotation/VSP_046578|||http://purl.uniprot.org/annotation/VSP_046579|||http://purl.uniprot.org/annotation/VSP_046580|||http://purl.uniprot.org/annotation/VSP_046581|||http://purl.uniprot.org/annotation/VSP_046582|||http://purl.uniprot.org/annotation/VSP_046583|||http://purl.uniprot.org/annotation/VSP_046584|||http://purl.uniprot.org/annotation/VSP_046585|||http://purl.uniprot.org/annotation/VSP_046587|||http://purl.uniprot.org/annotation/VSP_046588|||http://purl.uniprot.org/annotation/VSP_046589|||http://purl.uniprot.org/annotation/VSP_046590|||http://purl.uniprot.org/annotation/VSP_046591|||http://purl.uniprot.org/annotation/VSP_046592|||http://purl.uniprot.org/annotation/VSP_046593|||http://purl.uniprot.org/annotation/VSP_046594|||http://purl.uniprot.org/annotation/VSP_046595|||http://purl.uniprot.org/annotation/VSP_046596|||http://purl.uniprot.org/annotation/VSP_046597|||http://purl.uniprot.org/annotation/VSP_046598|||http://purl.uniprot.org/annotation/VSP_046599|||http://purl.uniprot.org/annotation/VSP_046600|||http://purl.uniprot.org/annotation/VSP_046601|||http://purl.uniprot.org/annotation/VSP_046602|||http://purl.uniprot.org/annotation/VSP_046603|||http://purl.uniprot.org/annotation/VSP_046604|||http://purl.uniprot.org/annotation/VSP_046605|||http://purl.uniprot.org/annotation/VSP_046606|||http://purl.uniprot.org/annotation/VSP_046607|||http://purl.uniprot.org/annotation/VSP_046608|||http://purl.uniprot.org/annotation/VSP_046609|||http://purl.uniprot.org/annotation/VSP_046610|||http://purl.uniprot.org/annotation/VSP_046611 http://togogenome.org/gene/10090:Ahsp ^@ http://purl.uniprot.org/uniprot/Q9CY02 ^@ Chain|||Molecule Processing ^@ Chain ^@ Alpha-hemoglobin-stabilizing protein ^@ http://purl.uniprot.org/annotation/PRO_0000064510 http://togogenome.org/gene/10090:Layn ^@ http://purl.uniprot.org/uniprot/Q8C351 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Strand|||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|||Extracellular|||Helical|||In isoform 2.|||Interaction with NF2|||Interaction with TLN1|||Layilin|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000262509|||http://purl.uniprot.org/annotation/VSP_021782|||http://purl.uniprot.org/annotation/VSP_021783 http://togogenome.org/gene/10090:Or10g9b ^@ http://purl.uniprot.org/uniprot/Q8VH08 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Adnp2 ^@ http://purl.uniprot.org/uniprot/Q8CHC8 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modification|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Region|||Zinc Finger ^@ Activity-dependent neuroprotector homeobox protein 2|||Basic and acidic residues|||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; degenerate|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox ^@ http://purl.uniprot.org/annotation/PRO_0000280417 http://togogenome.org/gene/10090:Calm3 ^@ http://purl.uniprot.org/uniprot/P0DP26|||http://purl.uniprot.org/uniprot/P0DP27|||http://purl.uniprot.org/uniprot/P0DP28 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand ^@ Calmodulin-1|||Calmodulin-2|||Calmodulin-3|||Decreases interaction with SCN8A in the absence of calcium.|||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|||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_0000439935|||http://purl.uniprot.org/annotation/PRO_0000439936|||http://purl.uniprot.org/annotation/PRO_0000439937 http://togogenome.org/gene/10090:Pex7 ^@ http://purl.uniprot.org/uniprot/B7ZNK8|||http://purl.uniprot.org/uniprot/P97865 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Repeat ^@ Peroxisomal targeting signal 2 receptor|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6 ^@ http://purl.uniprot.org/annotation/PRO_0000051117 http://togogenome.org/gene/10090:Armcx6 ^@ http://purl.uniprot.org/uniprot/Q8K3A6 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical; Signal-anchor|||Mitochondrial intermembrane|||Mitochondrion outer membrane (MOM)-targeting sequence|||Protein ARMCX6 ^@ http://purl.uniprot.org/annotation/PRO_0000191375 http://togogenome.org/gene/10090:Prickle1 ^@ http://purl.uniprot.org/uniprot/Q3U5C7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region ^@ Basic residues|||Cysteine methyl ester|||Disordered|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||PET|||Phosphoserine|||Polar residues|||Prickle-like protein 1|||Removed in mature form|||S-farnesyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000283027|||http://purl.uniprot.org/annotation/PRO_0000396713 http://togogenome.org/gene/10090:Or2ag12 ^@ http://purl.uniprot.org/uniprot/Q8VF89 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trpc1 ^@ http://purl.uniprot.org/uniprot/B2RPS7|||http://purl.uniprot.org/uniprot/B7ZMP6|||http://purl.uniprot.org/uniprot/Q61056 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform Beta.|||Polar residues|||Short transient receptor potential channel 1|||Transient receptor ion channel ^@ http://purl.uniprot.org/annotation/PRO_0000215304|||http://purl.uniprot.org/annotation/VSP_006561 http://togogenome.org/gene/10090:Mid2 ^@ http://purl.uniprot.org/uniprot/B1AVF4|||http://purl.uniprot.org/uniprot/Q9QUS6 ^@ 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|||B box-type 1; degenerate|||B box-type 2|||B30.2/SPRY|||COS|||Fibronectin type-III|||Probable E3 ubiquitin-protein ligase MID2|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056194 http://togogenome.org/gene/10090:Tmem203 ^@ http://purl.uniprot.org/uniprot/Q8R235 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Transmembrane protein 203 ^@ http://purl.uniprot.org/annotation/PRO_0000317204 http://togogenome.org/gene/10090:Or8b12b ^@ http://purl.uniprot.org/uniprot/Q7TRE5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zic1 ^@ http://purl.uniprot.org/uniprot/P46684 ^@ 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; atypical|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Polar residues|||Zinc finger protein ZIC 1 ^@ http://purl.uniprot.org/annotation/PRO_0000047245 http://togogenome.org/gene/10090:Dpp10 ^@ http://purl.uniprot.org/uniprot/E9QN98|||http://purl.uniprot.org/uniprot/Q6NXK7 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Dipeptidylpeptidase IV N-terminal|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Inactive dipeptidyl peptidase 10|||N-linked (GlcNAc...) asparagine|||Peptidase S9 prolyl oligopeptidase catalytic|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000122418 http://togogenome.org/gene/10090:Gpaa1 ^@ http://purl.uniprot.org/uniprot/Q9WTK3 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Glycosylphosphatidylinositol anchor attachment 1 protein|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000087555 http://togogenome.org/gene/10090:Tbx22 ^@ http://purl.uniprot.org/uniprot/E9Q5R8|||http://purl.uniprot.org/uniprot/Q8BKE4|||http://purl.uniprot.org/uniprot/Q8K402 ^@ 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|||Polar residues|||T-box|||T-box transcription factor TBX22 ^@ http://purl.uniprot.org/annotation/PRO_0000184456 http://togogenome.org/gene/10090:Atp5mpl ^@ http://purl.uniprot.org/uniprot/P56379 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ ATP synthase subunit ATP5MPL, mitochondrial|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000064394 http://togogenome.org/gene/10090:Casz1 ^@ http://purl.uniprot.org/uniprot/B1AS46|||http://purl.uniprot.org/uniprot/Q9CWL2 ^@ 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 ^@ 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|||Zinc finger protein castor homolog 1 ^@ http://purl.uniprot.org/annotation/PRO_0000046913|||http://purl.uniprot.org/annotation/VSP_027095|||http://purl.uniprot.org/annotation/VSP_027096 http://togogenome.org/gene/10090:Mlf2 ^@ http://purl.uniprot.org/uniprot/Q3UNV7|||http://purl.uniprot.org/uniprot/Q99KX1 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Myeloid leukemia factor 2|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000220755 http://togogenome.org/gene/10090:Rxrb ^@ http://purl.uniprot.org/uniprot/P28704|||http://purl.uniprot.org/uniprot/Q3TWJ1|||http://purl.uniprot.org/uniprot/Q8VCR0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||Hinge|||In isoform Short.|||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_0000053573|||http://purl.uniprot.org/annotation/VSP_003678 http://togogenome.org/gene/10090:Nol11 ^@ http://purl.uniprot.org/uniprot/Q8BJW5 ^@ 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.|||N6-methyllysine|||Nucleolar protein 11 ^@ http://purl.uniprot.org/annotation/PRO_0000096932|||http://purl.uniprot.org/annotation/VSP_015459 http://togogenome.org/gene/10090:Exph5 ^@ http://purl.uniprot.org/uniprot/Q0VAV2 ^@ 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|||Exophilin-5|||Phosphoserine|||Polar residues|||RabBD ^@ http://purl.uniprot.org/annotation/PRO_0000355582 http://togogenome.org/gene/10090:Smok2b ^@ http://purl.uniprot.org/uniprot/Q9QYZ3 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Protein kinase|||Proton acceptor|||Sperm motility kinase 2B|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000307868 http://togogenome.org/gene/10090:Id1 ^@ http://purl.uniprot.org/uniprot/Q6GTZ3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ BHLH ^@ http://togogenome.org/gene/10090:Nppc ^@ http://purl.uniprot.org/uniprot/Q544K5|||http://purl.uniprot.org/uniprot/Q61839 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Peptide|||Propeptide|||Region|||Signal Peptide ^@ C-type natriuretic peptide|||CNP-22|||CNP-29|||CNP-53|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000001557|||http://purl.uniprot.org/annotation/PRO_0000001558|||http://purl.uniprot.org/annotation/PRO_0000001559|||http://purl.uniprot.org/annotation/PRO_0000001560|||http://purl.uniprot.org/annotation/PRO_5014309625 http://togogenome.org/gene/10090:Abca7 ^@ http://purl.uniprot.org/uniprot/E9Q6G4|||http://purl.uniprot.org/uniprot/Q91V24 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ ABC transporter|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family A member 7|||Basic and acidic residues|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000250675 http://togogenome.org/gene/10090:Terb2 ^@ http://purl.uniprot.org/uniprot/A0A0P0YTB2|||http://purl.uniprot.org/uniprot/Q9D494 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Telomere repeats-binding bouquet formation protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000263718 http://togogenome.org/gene/10090:Eif4a2 ^@ http://purl.uniprot.org/uniprot/E9Q561|||http://purl.uniprot.org/uniprot/P10630|||http://purl.uniprot.org/uniprot/Q52KC1|||http://purl.uniprot.org/uniprot/Q8BTU6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Eukaryotic initiation factor 4A-II|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Phosphothreonine|||Q motif ^@ http://purl.uniprot.org/annotation/PRO_0000054940|||http://purl.uniprot.org/annotation/VSP_009630 http://togogenome.org/gene/10090:Cyp2c69 ^@ http://purl.uniprot.org/uniprot/E9PXC3 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5003244291 http://togogenome.org/gene/10090:Lrrc25 ^@ http://purl.uniprot.org/uniprot/B9EHD0|||http://purl.uniprot.org/uniprot/Q8K1T1 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 2|||Leucine-rich repeat-containing protein 25|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000021614|||http://purl.uniprot.org/annotation/PRO_5014300273 http://togogenome.org/gene/10090:Rara ^@ http://purl.uniprot.org/uniprot/P11416|||http://purl.uniprot.org/uniprot/Q3U3R3|||http://purl.uniprot.org/uniprot/Q3U5E7 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||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|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger ^@ 9aaTAD|||Abolishes phosphorylation and prevents phosphorylation of S-77.|||Decreases phosphorylation and no effect on interaction with CDK7. Strongly reduces transcriptional activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Greatly reduced interaction with RXRA and NCOR1 and transcriptional activation.|||Hinge|||In embryonal carcinoma cell line RAC65.|||In isoform Alpha-2.|||Modulating|||N6,N6,N6-trimethyllysine|||NR C4-type|||NR LBD|||No change in phosphorylation levels and no effect on transcriptional activity.|||No effect on phosphorylation, no effect on transcriptional activity.|||Nuclear receptor|||Phosphoserine; by CDK7|||Phosphoserine; by PKA|||Phosphoserine; by PKA and RPS6KA5|||Phosphoserine; by PKB/AKT1|||Polar residues|||Reduced methylation levels. Little effect on interaction with RXRA or NCOR1. Small loss in transcriptional activation.|||Required for binding corepressor NCOR1|||Retinoic acid receptor alpha ^@ http://purl.uniprot.org/annotation/PRO_0000053462|||http://purl.uniprot.org/annotation/VSP_003630 http://togogenome.org/gene/10090:Or4a72 ^@ http://purl.uniprot.org/uniprot/A0A1L1SQJ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vps72 ^@ http://purl.uniprot.org/uniprot/Q62481 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Pro residues|||Vacuolar protein sorting-associated protein 72 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000066284 http://togogenome.org/gene/10090:Cpa3 ^@ http://purl.uniprot.org/uniprot/P15089|||http://purl.uniprot.org/uniprot/Q542E3 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Signal Peptide ^@ Activation peptide|||Mast cell carboxypeptidase A|||Peptidase M14 carboxypeptidase A|||Peptidase M14 carboxypeptidase A domain-containing protein|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000004397|||http://purl.uniprot.org/annotation/PRO_0000004398|||http://purl.uniprot.org/annotation/PRO_5011946779 http://togogenome.org/gene/10090:Ube2s ^@ http://purl.uniprot.org/uniprot/Q921J4 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Glycyl thioester intermediate|||N-acetylmethionine|||Phosphoserine|||UBC core|||Ubiquitin-conjugating enzyme E2 S ^@ http://purl.uniprot.org/annotation/PRO_0000082508 http://togogenome.org/gene/10090:B4galt4 ^@ http://purl.uniprot.org/uniprot/Q9JJ04 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Beta-1,4-galactosyltransferase 4|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000080543 http://togogenome.org/gene/10090:Mpi ^@ http://purl.uniprot.org/uniprot/Q3V100|||http://purl.uniprot.org/uniprot/Q924M7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ 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_0000194237 http://togogenome.org/gene/10090:Ubp1 ^@ http://purl.uniprot.org/uniprot/Q811S7 ^@ 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|||Erythroid-specific transcriptional activation|||Grh/CP2 DB|||In isoform 2.|||Phosphoserine|||Polar residues|||Transcriptional activation|||Upstream-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000229027|||http://purl.uniprot.org/annotation/VSP_017731 http://togogenome.org/gene/10090:Ces1a ^@ http://purl.uniprot.org/uniprot/E9PYP1|||http://purl.uniprot.org/uniprot/Q5FWH4 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Carboxylesterase type B|||Carboxylic ester hydrolase ^@ http://purl.uniprot.org/annotation/PRO_5005128625|||http://purl.uniprot.org/annotation/PRO_5005143651 http://togogenome.org/gene/10090:Prkci ^@ http://purl.uniprot.org/uniprot/Q5DTK3|||http://purl.uniprot.org/uniprot/Q62074 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Strand|||Turn|||Zinc Finger ^@ AGC-kinase C-terminal|||Basic and acidic residues|||Disordered|||Interaction with PARD6A|||Loss of interaction with SQSTM1.|||N-acetylproline|||No effect on interaction with SQSTM1.|||No effect on interaction with SQSTM1; when associated with A-118.|||No effect on interaction with SQSTM1; when associated with A-29.|||PB1|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by SRC|||Protein kinase|||Protein kinase C iota type|||Proton acceptor|||Pseudosubstrate|||Regulatory domain|||Removed|||Required for interaction with RAB2 ^@ http://purl.uniprot.org/annotation/PRO_0000055711 http://togogenome.org/gene/10090:Ifna7 ^@ http://purl.uniprot.org/uniprot/Q810G6 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015098944 http://togogenome.org/gene/10090:Ppp2r3a ^@ http://purl.uniprot.org/uniprot/B2RXC8|||http://purl.uniprot.org/uniprot/G3X9E8|||http://purl.uniprot.org/uniprot/Q3V1Y6|||http://purl.uniprot.org/uniprot/Q8BXX8 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue|||Region ^@ Disordered|||EF-hand ^@ http://togogenome.org/gene/10090:Meiosin ^@ http://purl.uniprot.org/uniprot/A0A5K7RLP0 ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Splice Variant ^@ Basic and acidic residues|||Basic motif|||Disordered|||HMG box|||Helix-loop-helix motif|||In isoform 2.|||Meiosis initiator protein|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000451166|||http://purl.uniprot.org/annotation/VSP_060768 http://togogenome.org/gene/10090:Il5 ^@ http://purl.uniprot.org/uniprot/P04401|||http://purl.uniprot.org/uniprot/Q5SV01 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Signal Peptide|||Strand|||Turn ^@ Interchain (with C-104)|||Interchain (with C-62)|||Interleukin-5|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000015564|||http://purl.uniprot.org/annotation/PRO_5014205901 http://togogenome.org/gene/10090:Calm2 ^@ http://purl.uniprot.org/uniprot/P0DP26|||http://purl.uniprot.org/uniprot/P0DP27|||http://purl.uniprot.org/uniprot/P0DP28 ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand ^@ Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand ^@ Calmodulin-1|||Calmodulin-2|||Calmodulin-3|||Decreases interaction with SCN8A in the absence of calcium.|||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|||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_0000439935|||http://purl.uniprot.org/annotation/PRO_0000439936|||http://purl.uniprot.org/annotation/PRO_0000439937 http://togogenome.org/gene/10090:Tmem74b ^@ http://purl.uniprot.org/uniprot/A2AU34 ^@ Region|||Transmembrane ^@ Region|||Transmembrane ^@ Disordered|||Helical ^@ http://togogenome.org/gene/10090:Zbtb37 ^@ http://purl.uniprot.org/uniprot/Q8C3U9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ BTB|||Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Crcp ^@ http://purl.uniprot.org/uniprot/O35427 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ DNA-directed RNA polymerase III subunit RPC9|||Disordered ^@ http://purl.uniprot.org/annotation/PRO_0000079336 http://togogenome.org/gene/10090:Atp2c2 ^@ http://purl.uniprot.org/uniprot/A7L9Z8 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Calcium-transporting ATPase type 2C member 2|||Cytoplasmic|||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|||Interaction with ORAI1|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000356156 http://togogenome.org/gene/10090:Angel2 ^@ http://purl.uniprot.org/uniprot/Q8K1C0 ^@ Chain|||Molecule Processing|||Natural Variation|||Splice Variant ^@ Chain|||Splice Variant ^@ In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||Protein angel homolog 2 ^@ http://purl.uniprot.org/annotation/PRO_0000305081|||http://purl.uniprot.org/annotation/VSP_028217|||http://purl.uniprot.org/annotation/VSP_028218|||http://purl.uniprot.org/annotation/VSP_028219|||http://purl.uniprot.org/annotation/VSP_028220|||http://purl.uniprot.org/annotation/VSP_028221 http://togogenome.org/gene/10090:Zdhhc21 ^@ http://purl.uniprot.org/uniprot/Q9D270 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||DHHC|||Extracellular|||Helical|||In depilated (dep) mutant mice. Loss of protein-cysteine S-palmitoyltransferase activity. Relocalized to the endoplasmic reticulum.|||Loss of protein-cysteine S-palmitoyltransferase activity. Decreased localization to the cis-Golgi network. Relocalized to the endoplasmic reticulum.|||No effect on protein-cysteine S-palmitoyltransferase activity. No effect on localization to the cis-Golgi network.|||Palmitoyltransferase ZDHHC21|||S-palmitoyl cysteine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000212909 http://togogenome.org/gene/10090:Prep ^@ http://purl.uniprot.org/uniprot/Q543B9|||http://purl.uniprot.org/uniprot/Q9QUR6 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue ^@ Charge relay system|||N-acetylmethionine|||N6-acetyllysine|||Peptidase S9 prolyl oligopeptidase catalytic|||Peptidase S9A N-terminal|||Prolyl endopeptidase ^@ http://purl.uniprot.org/annotation/PRO_0000122402 http://togogenome.org/gene/10090:Tdpoz5 ^@ http://purl.uniprot.org/uniprot/E0CYU8|||http://purl.uniprot.org/uniprot/Q2NL42 ^@ Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Domain Extent|||Non-terminal Residue ^@ BTB|||MATH ^@ http://togogenome.org/gene/10090:Npl ^@ http://purl.uniprot.org/uniprot/Q9DCJ9 ^@ Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Site ^@ Involved in proton transfer during cleavage|||N-acetylneuraminate lyase|||Phosphoserine|||Schiff-base intermediate with substrate ^@ http://purl.uniprot.org/annotation/PRO_0000273353 http://togogenome.org/gene/10090:Dock2 ^@ http://purl.uniprot.org/uniprot/Q6A0A3|||http://purl.uniprot.org/uniprot/Q8C3J5 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 2|||Disordered|||N6-acetyllysine|||Phosphoserine|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000189987 http://togogenome.org/gene/10090:Ift122 ^@ http://purl.uniprot.org/uniprot/E9Q9G8|||http://purl.uniprot.org/uniprot/Q6NWV3 ^@ 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 ^@ Acidic residues|||Disordered|||In isoform 2.|||Intraflagellar transport protein 122 homolog|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8 ^@ http://purl.uniprot.org/annotation/PRO_0000398816|||http://purl.uniprot.org/annotation/VSP_039810 http://togogenome.org/gene/10090:Etv3 ^@ http://purl.uniprot.org/uniprot/Q8R4Z4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict ^@ 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|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000204115 http://togogenome.org/gene/10090:Slc25a22 ^@ http://purl.uniprot.org/uniprot/Q80X52|||http://purl.uniprot.org/uniprot/Q9D6M3 ^@ Chain|||Molecule Processing|||Region|||Repeat|||Transmembrane ^@ Chain|||Repeat|||Transmembrane ^@ Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial glutamate carrier 1|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3 ^@ http://purl.uniprot.org/annotation/PRO_0000090620 http://togogenome.org/gene/10090:Map3k3 ^@ http://purl.uniprot.org/uniprot/Q61084 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Mitogen-activated protein kinase kinase kinase 3|||PB1|||Phosphoserine|||Phosphoserine; by SGK1|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086246 http://togogenome.org/gene/10090:Tanc1 ^@ http://purl.uniprot.org/uniprot/E9QAF9|||http://purl.uniprot.org/uniprot/Q0VGY8 ^@ 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 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_0000316960|||http://purl.uniprot.org/annotation/VSP_030829|||http://purl.uniprot.org/annotation/VSP_030830|||http://purl.uniprot.org/annotation/VSP_030831 http://togogenome.org/gene/10090:Mslnl ^@ http://purl.uniprot.org/uniprot/Q8C160 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Mesothelin-like protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000320649 http://togogenome.org/gene/10090:Scand1 ^@ http://purl.uniprot.org/uniprot/Q2M4I6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||SCAN box ^@ http://togogenome.org/gene/10090:Dnmt3b ^@ http://purl.uniprot.org/uniprot/O88509|||http://purl.uniprot.org/uniprot/Q3KR45|||http://purl.uniprot.org/uniprot/Q541E5 ^@ 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 ^@ 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 isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Interaction with DNMT1 and DNMT3A|||Interaction with the PRC2/EED-EZH2 complex|||Loss of activity.|||No effect on localization.|||PHD-type|||PHD-type; atypical|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues|||Prevents accumulation in pericentric heterochromatin.|||SAM-dependent MTase C5-type|||Significantly reduces activity. ^@ http://purl.uniprot.org/annotation/PRO_0000088046|||http://purl.uniprot.org/annotation/VSP_005642|||http://purl.uniprot.org/annotation/VSP_005643 http://togogenome.org/gene/10090:Cstdc1 ^@ http://purl.uniprot.org/uniprot/Q8VII3 ^@ Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ Cystatin-14 ^@ http://purl.uniprot.org/annotation/PRO_0000285793 http://togogenome.org/gene/10090:Scn11a ^@ http://purl.uniprot.org/uniprot/Q9R053 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||INTRAMEM|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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=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|||Increased voltage-gated sodium channel activity.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pore-forming|||Sodium channel protein type 11 subunit alpha ^@ http://purl.uniprot.org/annotation/PRO_0000048511 http://togogenome.org/gene/10090:Rps6kl1 ^@ http://purl.uniprot.org/uniprot/Q8R2S1 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||MIT|||Polar residues|||Protein kinase|||Proton acceptor|||Ribosomal protein S6 kinase-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000232642|||http://purl.uniprot.org/annotation/VSP_017935|||http://purl.uniprot.org/annotation/VSP_017936|||http://purl.uniprot.org/annotation/VSP_017937|||http://purl.uniprot.org/annotation/VSP_017938 http://togogenome.org/gene/10090:Nucb1 ^@ http://purl.uniprot.org/uniprot/A0A1C7CYU3|||http://purl.uniprot.org/uniprot/Q02819 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Binds to GNAI2 and GNAI3|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||GBA|||Nucleobindin-1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000004163|||http://purl.uniprot.org/annotation/PRO_5015063032 http://togogenome.org/gene/10090:Ttc9b ^@ http://purl.uniprot.org/uniprot/Q9D6E4 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat ^@ Disordered|||Phosphoserine|||Pro residues|||TPR 1|||TPR 2|||Tetratricopeptide repeat protein 9B ^@ http://purl.uniprot.org/annotation/PRO_0000294460 http://togogenome.org/gene/10090:Prss8 ^@ http://purl.uniprot.org/uniprot/Q99L44 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015099609 http://togogenome.org/gene/10090:Serpina3n ^@ http://purl.uniprot.org/uniprot/G3X8T9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Serpin ^@ http://purl.uniprot.org/annotation/PRO_5015091831 http://togogenome.org/gene/10090:Txndc2 ^@ http://purl.uniprot.org/uniprot/A0A3B2W416|||http://purl.uniprot.org/uniprot/H7BX21|||http://purl.uniprot.org/uniprot/Q6P902 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Repeat ^@ 1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||21 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|||Phosphoserine|||Polar residues|||Redox-active|||Thioredoxin|||Thioredoxin domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000120154 http://togogenome.org/gene/10090:Rtp3 ^@ http://purl.uniprot.org/uniprot/Q5QGU6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane|||Zinc Finger ^@ 3CxxC-type|||Cytoplasmic|||Disordered|||Helical|||Polar residues|||Receptor-transporting protein 3 ^@ http://purl.uniprot.org/annotation/PRO_0000181994 http://togogenome.org/gene/10090:Adrb3 ^@ http://purl.uniprot.org/uniprot/P25962|||http://purl.uniprot.org/uniprot/Q3UP63 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Beta-3 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 isoform B.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069146|||http://purl.uniprot.org/annotation/VSP_001864 http://togogenome.org/gene/10090:Pank3 ^@ http://purl.uniprot.org/uniprot/Q8R2W9 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Pantothenate kinase 3|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000161805 http://togogenome.org/gene/10090:Gkn1 ^@ http://purl.uniprot.org/uniprot/Q53YU8|||http://purl.uniprot.org/uniprot/Q9CR36 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ BRICHOS|||Gastrokine-1 ^@ http://purl.uniprot.org/annotation/PRO_0000021333|||http://purl.uniprot.org/annotation/PRO_5015097753 http://togogenome.org/gene/10090:Mfap5 ^@ http://purl.uniprot.org/uniprot/F8WJ99|||http://purl.uniprot.org/uniprot/Q9QZJ6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide ^@ Cell attachment site|||Disordered|||Microfibrillar-associated protein 5|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000018686|||http://purl.uniprot.org/annotation/PRO_5003379627 http://togogenome.org/gene/10090:Cckbr ^@ http://purl.uniprot.org/uniprot/P56481|||http://purl.uniprot.org/uniprot/Q3ZB46 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Region|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000069475 http://togogenome.org/gene/10090:Gm5797 ^@ http://purl.uniprot.org/uniprot/Q5BKP9 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Disks large homolog 5 N-terminal ^@ http://togogenome.org/gene/10090:Wfikkn1 ^@ http://purl.uniprot.org/uniprot/Q8R0S6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Site ^@ BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||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_0000307817 http://togogenome.org/gene/10090:F2rl3 ^@ http://purl.uniprot.org/uniprot/O88634 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane|||Turn ^@ Cleavage; by thrombin|||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|||Proteinase-activated receptor 4|||Removed for receptor activation ^@ http://purl.uniprot.org/annotation/PRO_0000012764|||http://purl.uniprot.org/annotation/PRO_0000012765 http://togogenome.org/gene/10090:Cdh13 ^@ http://purl.uniprot.org/uniprot/Q9WTR5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn ^@ Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-13|||Disordered|||GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Strongly inhibits dimerization. ^@ http://purl.uniprot.org/annotation/PRO_0000003796|||http://purl.uniprot.org/annotation/PRO_0000003797|||http://purl.uniprot.org/annotation/PRO_0000003798 http://togogenome.org/gene/10090:Ngef ^@ http://purl.uniprot.org/uniprot/E9QK62|||http://purl.uniprot.org/uniprot/Q8CHT1 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||DH|||Disordered|||Ephexin-1|||In isoform 2.|||Loss of ephrin-mediated growth cone collapse. No effect on interaction with EPHA4.|||PH|||Phosphotyrosine|||Polar residues|||Regulatory region; modulates activity toward RHOA, RAC1 and CDC42|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000248389|||http://purl.uniprot.org/annotation/VSP_020262|||http://purl.uniprot.org/annotation/VSP_020263 http://togogenome.org/gene/10090:Cachd1 ^@ http://purl.uniprot.org/uniprot/Q6PDJ1 ^@ 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 ^@ Basic and acidic residues|||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_0000304662|||http://purl.uniprot.org/annotation/VSP_028073 http://togogenome.org/gene/10090:Spc24 ^@ http://purl.uniprot.org/uniprot/Q9D083 ^@ Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||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_0000249560|||http://purl.uniprot.org/annotation/VSP_020515|||http://purl.uniprot.org/annotation/VSP_020516|||http://purl.uniprot.org/annotation/VSP_020517 http://togogenome.org/gene/10090:Hps1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J062|||http://purl.uniprot.org/uniprot/E9PYL0|||http://purl.uniprot.org/uniprot/O08983|||http://purl.uniprot.org/uniprot/Q3U309 ^@ 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 ^@ BLOC-3 complex member HPS1|||Disordered|||FUZ/MON1/HPS1 first Longin|||FUZ/MON1/HPS1 second Longin|||FUZ/MON1/HPS1 third Longin|||In strain: BALB/c.|||Polar residues|||[DE]-X(4)-L-L 1|||[DE]-X(4)-L-L 2|||[DE]-X(4)-L-L 3 ^@ http://purl.uniprot.org/annotation/PRO_0000084049 http://togogenome.org/gene/10090:Atp6v1c2 ^@ http://purl.uniprot.org/uniprot/Q99L60 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||In isoform 2.|||In isoform 3.|||V-type proton ATPase subunit C 2 ^@ http://purl.uniprot.org/annotation/PRO_0000285670|||http://purl.uniprot.org/annotation/VSP_024884|||http://purl.uniprot.org/annotation/VSP_024885 http://togogenome.org/gene/10090:Tceal1 ^@ http://purl.uniprot.org/uniprot/Q921P9 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Transcription elongation factor A protein-like 1 ^@ http://purl.uniprot.org/annotation/PRO_0000239204 http://togogenome.org/gene/10090:Rai1 ^@ http://purl.uniprot.org/uniprot/Q5QGZ6|||http://purl.uniprot.org/uniprot/Q61818|||http://purl.uniprot.org/uniprot/Q810L5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||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 isoform 2.|||Nuclear localization signal|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Retinoic acid-induced protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000097160|||http://purl.uniprot.org/annotation/VSP_011004|||http://purl.uniprot.org/annotation/VSP_011005 http://togogenome.org/gene/10090:Vps13a ^@ http://purl.uniprot.org/uniprot/Q5H8C4|||http://purl.uniprot.org/uniprot/Q6P6M9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Splice Variant ^@ Atg2/VPS13 C-terminal|||Chorein N-terminal|||Disordered|||FFAT|||In isoform 2.|||Intermembrane lipid transfer protein VPS13A|||Phosphoserine|||Phosphothreonine|||Required for lipid droplet localization|||Required for mitochondrial localization|||SHR-BD|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||Vacuolar protein sorting-associated protein 13 DH-like|||Vacuolar protein sorting-associated protein 13 VPS13 adaptor binding ^@ http://purl.uniprot.org/annotation/PRO_0000262948|||http://purl.uniprot.org/annotation/VSP_052241|||http://purl.uniprot.org/annotation/VSP_052242 http://togogenome.org/gene/10090:Bmpr2 ^@ http://purl.uniprot.org/uniprot/O35607|||http://purl.uniprot.org/uniprot/Q3UER5|||http://purl.uniprot.org/uniprot/Q3UG09|||http://purl.uniprot.org/uniprot/Q3UU71 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Bone morphogenetic protein receptor type-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||receptor protein serine/threonine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000024416|||http://purl.uniprot.org/annotation/PRO_5004230070 http://togogenome.org/gene/10090:Hsf3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J251|||http://purl.uniprot.org/uniprot/D0VYS2|||http://purl.uniprot.org/uniprot/E9QNK9|||http://purl.uniprot.org/uniprot/Q8BL67 ^@ 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|||HSF-type DNA-binding|||Heat shock factor protein 3|||In isoform 2.|||Required for nuclear translocation in heat-shocked cells ^@ http://purl.uniprot.org/annotation/PRO_0000392634|||http://purl.uniprot.org/annotation/VSP_053203|||http://purl.uniprot.org/annotation/VSP_053204|||http://purl.uniprot.org/annotation/VSP_053205 http://togogenome.org/gene/10090:Adam33 ^@ http://purl.uniprot.org/uniprot/A2AP51|||http://purl.uniprot.org/uniprot/Q923W9 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 33|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_0000029144|||http://purl.uniprot.org/annotation/PRO_0000029145|||http://purl.uniprot.org/annotation/PRO_5015086031|||http://purl.uniprot.org/annotation/VSP_005496 http://togogenome.org/gene/10090:Tnrc6a ^@ http://purl.uniprot.org/uniprot/Q3UHK8 ^@ 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|||Interaction with argonaute family proteins|||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_0000373980 http://togogenome.org/gene/10090:Eps8l1 ^@ http://purl.uniprot.org/uniprot/Q8R5F8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ Basic and acidic residues|||Disordered|||Epidermal growth factor receptor kinase substrate 8-like protein 1|||PTB|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000239083 http://togogenome.org/gene/10090:Tgfbr1 ^@ http://purl.uniprot.org/uniprot/Q4FJL1|||http://purl.uniprot.org/uniprot/Q64729|||http://purl.uniprot.org/uniprot/Q9D5H8 ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||FKBP1A-binding|||GS|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by TGFBR2|||Phosphothreonine; by TGFBR2|||Protein kinase|||Proton acceptor|||TGF-beta receptor type-1|||receptor protein serine/threonine kinase ^@ http://purl.uniprot.org/annotation/PRO_0000024424|||http://purl.uniprot.org/annotation/PRO_5015097605|||http://purl.uniprot.org/annotation/VSP_021593 http://togogenome.org/gene/10090:Frem1 ^@ http://purl.uniprot.org/uniprot/A2ADN1|||http://purl.uniprot.org/uniprot/Q684R7 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Splice Variant ^@ C-type lectin|||CSPG|||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|||Disordered|||FRAS1-related extracellular matrix protein 1|||Impairs cell adhesion ability in vitro.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000010123|||http://purl.uniprot.org/annotation/PRO_5002642459|||http://purl.uniprot.org/annotation/VSP_015032|||http://purl.uniprot.org/annotation/VSP_015033|||http://purl.uniprot.org/annotation/VSP_015034 http://togogenome.org/gene/10090:Pdzrn3 ^@ http://purl.uniprot.org/uniprot/Q3UPS8|||http://purl.uniprot.org/uniprot/Q69ZS0 ^@ 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|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase PDZRN3|||In isoform 2.|||In isoform 3.|||Loss of E3 ligase activity.|||PDZ|||PDZ 1|||PDZ 2|||Phosphoserine|||Polar residues|||RING-type; degenerate|||TRAF-type ^@ http://purl.uniprot.org/annotation/PRO_0000055918|||http://purl.uniprot.org/annotation/VSP_012610|||http://purl.uniprot.org/annotation/VSP_039769 http://togogenome.org/gene/10090:Trip4 ^@ http://purl.uniprot.org/uniprot/Q9QXN3 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ASCH|||Activating signal cointegrator 1|||C4-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)|||In isoform 2.|||Mediates interaction with DDRGK1|||Mediates interaction with UFL1|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000065632|||http://purl.uniprot.org/annotation/VSP_011109|||http://purl.uniprot.org/annotation/VSP_011110 http://togogenome.org/gene/10090:Nalcn ^@ http://purl.uniprot.org/uniprot/E9QLE4|||http://purl.uniprot.org/uniprot/Q8BXR5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||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=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 isoform 2.|||Ion transport|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pore-forming|||Sodium leak channel NALCN ^@ http://purl.uniprot.org/annotation/PRO_0000314011|||http://purl.uniprot.org/annotation/VSP_030192 http://togogenome.org/gene/10090:Krt32 ^@ http://purl.uniprot.org/uniprot/B1ATJ5|||http://purl.uniprot.org/uniprot/Q62168 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||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_0000063687 http://togogenome.org/gene/10090:Gas2l3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1A6|||http://purl.uniprot.org/uniprot/Q3TPC3|||http://purl.uniprot.org/uniprot/Q3UWW6 ^@ 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|||Calponin-homology (CH)|||Disordered|||GAR|||GAS2-like protein 3|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000322985 http://togogenome.org/gene/10090:Scn10a ^@ http://purl.uniprot.org/uniprot/K3W4P8|||http://purl.uniprot.org/uniprot/Q6QIY3 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||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=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 isoform 2.|||In isoform 3.|||Ion transport|||N-linked (GlcNAc...) asparagine|||No regulation by NEDD4L.|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues|||Pore-forming|||Sensitive to inhibition by some components of the venom of Centruroides sculpturatus.|||Sodium channel protein type 10 subunit alpha|||Sodium ion transport-associated ^@ http://purl.uniprot.org/annotation/PRO_0000048508|||http://purl.uniprot.org/annotation/VSP_012256|||http://purl.uniprot.org/annotation/VSP_012257 http://togogenome.org/gene/10090:Or4a67 ^@ http://purl.uniprot.org/uniprot/A2ATJ4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp385c ^@ http://purl.uniprot.org/uniprot/A2A5E6 ^@ 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 ^@ Disordered|||In isoform 2.|||Matrin-type 1|||Matrin-type 2|||Matrin-type 3|||Polar residues|||Pro residues|||Zinc finger protein 385C ^@ http://purl.uniprot.org/annotation/PRO_0000319942|||http://purl.uniprot.org/annotation/VSP_031547 http://togogenome.org/gene/10090:Cyb5r3 ^@ http://purl.uniprot.org/uniprot/Q9DCN2 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Splice Variant ^@ Decreased levels in mitochondrion and reduced activity of mitochondrial respiratory complex I.|||FAD-binding FR-type|||In isoform 2.|||N-myristoyl glycine|||N6-acetyllysine|||NADH-cytochrome b5 reductase 3|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000019398|||http://purl.uniprot.org/annotation/VSP_012952 http://togogenome.org/gene/10090:Dnd1 ^@ http://purl.uniprot.org/uniprot/Q6VY05 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Splice Variant ^@ Dead end protein homolog 1|||In isoform 2.|||Omega-N-methylarginine|||RRM 1|||RRM 2 ^@ http://purl.uniprot.org/annotation/PRO_0000081569|||http://purl.uniprot.org/annotation/VSP_012943 http://togogenome.org/gene/10090:Tagap ^@ http://purl.uniprot.org/uniprot/B2RWW0 ^@ 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|||Rho-GAP|||T-cell activation Rho GTPase-activating protein ^@ http://purl.uniprot.org/annotation/PRO_0000056720 http://togogenome.org/gene/10090:Eif3c ^@ http://purl.uniprot.org/uniprot/Q8R1B4 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 3 subunit C|||N6-acetyllysine|||PCI|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000259425 http://togogenome.org/gene/10090:Ciz1 ^@ http://purl.uniprot.org/uniprot/A2AN61|||http://purl.uniprot.org/uniprot/Q3TXU6|||http://purl.uniprot.org/uniprot/Q3UUV0|||http://purl.uniprot.org/uniprot/Q8VEH2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Matrin-type|||Polar residues ^@ http://togogenome.org/gene/10090:Rfx1 ^@ http://purl.uniprot.org/uniprot/P48377 ^@ 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|||Disordered|||MHC class II regulatory factor RFX1|||Phosphoserine|||Polar residues|||Pro residues|||RFX-type winged-helix ^@ http://purl.uniprot.org/annotation/PRO_0000215287 http://togogenome.org/gene/10090:Smoc2 ^@ http://purl.uniprot.org/uniprot/A0A3B2WCK7|||http://purl.uniprot.org/uniprot/Q8CD91 ^@ 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 ^@ Disordered|||EF-hand|||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|||Thyroglobulin type-1 1|||Thyroglobulin type-1 2 ^@ http://purl.uniprot.org/annotation/PRO_0000020319|||http://purl.uniprot.org/annotation/PRO_5017321016|||http://purl.uniprot.org/annotation/VSP_008723 http://togogenome.org/gene/10090:Cyp2j9 ^@ http://purl.uniprot.org/uniprot/Q924D1 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Dsp ^@ http://purl.uniprot.org/uniprot/E9PZW0|||http://purl.uniprot.org/uniprot/E9Q557 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Repeat ^@ 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|||Interaction with PKP1, JUP, PKP2|||Omega-N-methylarginine|||Omega-hydroxyceramide glutamate ester|||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_0000410831 http://togogenome.org/gene/10090:Smim14 ^@ http://purl.uniprot.org/uniprot/Q91VT8 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||Lumenal|||Small integral membrane protein 14 ^@ http://purl.uniprot.org/annotation/PRO_0000268817 http://togogenome.org/gene/10090:Ip6k2 ^@ http://purl.uniprot.org/uniprot/Q80V72 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Sequence Conflict ^@ Inositol hexakisphosphate kinase 2 ^@ http://purl.uniprot.org/annotation/PRO_0000066878 http://togogenome.org/gene/10090:Ambra1 ^@ http://purl.uniprot.org/uniprot/A2AH22 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Abolished ubiquitination by RNF2.|||Activating molecule in BECN1-regulated autophagy protein 1|||Asymmetric dimethylarginine|||Cleavage; by caspase-6, caspase-7 and caspase-8|||Disordered|||Does not affect ubiquitination by RNF2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2, isoform 5 and isoform 7.|||In isoform 3 and isoform 4.|||In isoform 4, isoform 5 and isoform 7.|||In isoform 5.|||In isoform 6.|||Interaction with DDB1|||LIR|||Phosphoserine|||Polar residues|||Pro residues|||PxP motif 1|||PxP motif 2|||TQT motif 1|||TQT motif 2|||WD 1|||WD 2|||WD 3 ^@ http://purl.uniprot.org/annotation/PRO_0000315704|||http://purl.uniprot.org/annotation/VSP_030658|||http://purl.uniprot.org/annotation/VSP_030659|||http://purl.uniprot.org/annotation/VSP_030660|||http://purl.uniprot.org/annotation/VSP_030661|||http://purl.uniprot.org/annotation/VSP_030662|||http://purl.uniprot.org/annotation/VSP_030663 http://togogenome.org/gene/10090:Ikbip ^@ http://purl.uniprot.org/uniprot/E9QMH7|||http://purl.uniprot.org/uniprot/Q9DBZ1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Inhibitor of nuclear factor kappa-B kinase-interacting protein|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000342262|||http://purl.uniprot.org/annotation/VSP_034411 http://togogenome.org/gene/10090:Mrpl9 ^@ http://purl.uniprot.org/uniprot/Q14B21|||http://purl.uniprot.org/uniprot/Q99N94 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Transit Peptide ^@ Chain|||Domain Extent|||Transit Peptide ^@ Large ribosomal subunit protein bL9m|||Mitochondrion|||Ribosomal protein L9 ^@ http://purl.uniprot.org/annotation/PRO_0000030551 http://togogenome.org/gene/10090:Gpr12 ^@ http://purl.uniprot.org/uniprot/P35412 ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||G-protein coupled receptor 12|||Helical; 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_0000069528 http://togogenome.org/gene/10090:Dcun1d5 ^@ http://purl.uniprot.org/uniprot/Q9CXV9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict ^@ Abolishes phosphoralation.|||DCN1-like protein 5|||DCUN1|||Does not affect phosphorylarion at Ser-41; when associated with A-195.|||Does not affect phosphorylarion at Ser-41; when associated with R-219.|||Phosphoserine; by IKKA ^@ http://purl.uniprot.org/annotation/PRO_0000254172 http://togogenome.org/gene/10090:Egr3 ^@ http://purl.uniprot.org/uniprot/P43300|||http://purl.uniprot.org/uniprot/Q3ZB14 ^@ 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|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Early growth response protein 3|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000047126 http://togogenome.org/gene/10090:Pfkm ^@ http://purl.uniprot.org/uniprot/P47857 ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant ^@ ATP-dependent 6-phosphofructokinase, muscle type|||C-terminal regulatory PFK domain 2|||In isoform 2.|||In isoform 3.|||Interdomain linker|||N-acetylthreonine|||N-terminal catalytic PFK domain 1|||N6-(2-hydroxyisobutyryl)lysine|||O-linked (GlcNAc) serine|||Phosphoserine|||Proton acceptor|||Removed|||in other chain ^@ http://purl.uniprot.org/annotation/PRO_0000112018|||http://purl.uniprot.org/annotation/VSP_057079|||http://purl.uniprot.org/annotation/VSP_057080 http://togogenome.org/gene/10090:Lnp1 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSK3 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Tmem44 ^@ http://purl.uniprot.org/uniprot/E9Q4M0|||http://purl.uniprot.org/uniprot/Q8C820 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Or2aj5 ^@ http://purl.uniprot.org/uniprot/Q8VGL6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Xkr5 ^@ http://purl.uniprot.org/uniprot/Q5GH66|||http://purl.uniprot.org/uniprot/Q8BG78 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues|||XK-related protein 5 ^@ http://purl.uniprot.org/annotation/PRO_0000190783 http://togogenome.org/gene/10090:Ntng2 ^@ http://purl.uniprot.org/uniprot/A2AKW8|||http://purl.uniprot.org/uniprot/Q8R4F1 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ EGF-like|||GPI-anchor amidated glycine|||In isoform 2A.|||In isoform 2C.|||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-G2|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000017097|||http://purl.uniprot.org/annotation/PRO_0000017098|||http://purl.uniprot.org/annotation/PRO_5015086025|||http://purl.uniprot.org/annotation/VSP_050562|||http://purl.uniprot.org/annotation/VSP_050563|||http://purl.uniprot.org/annotation/VSP_050564|||http://purl.uniprot.org/annotation/VSP_050565 http://togogenome.org/gene/10090:Dnai1 ^@ http://purl.uniprot.org/uniprot/A2ANP4|||http://purl.uniprot.org/uniprot/Q8C0M8 ^@ 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 ^@ Acidic residues|||Disordered|||Dynein axonemal intermediate chain 1|||Phosphoserine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000254655 http://togogenome.org/gene/10090:Dynlt2a1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J284|||http://purl.uniprot.org/uniprot/P11985 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant ^@ Disordered|||Dynein light chain Tctex-type protein 2|||In T-haplotype.|||In isoform 2.|||Requires 2 nucleotide substitutions; in T-haplotype. ^@ http://purl.uniprot.org/annotation/PRO_0000072471|||http://purl.uniprot.org/annotation/VSP_004449 http://togogenome.org/gene/10090:Bmp1 ^@ http://purl.uniprot.org/uniprot/P98063 ^@ 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 ^@ Bone morphogenetic protein 1|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000028891|||http://purl.uniprot.org/annotation/PRO_0000028892 http://togogenome.org/gene/10090:Gm13290 ^@ http://purl.uniprot.org/uniprot/Q8CD73 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5015099103 http://togogenome.org/gene/10090:Uvssa ^@ http://purl.uniprot.org/uniprot/Q9D479 ^@ 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|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Polar residues|||UV-stimulated scaffold protein A|||VHS-like ^@ http://purl.uniprot.org/annotation/PRO_0000317283 http://togogenome.org/gene/10090:Aacs ^@ http://purl.uniprot.org/uniprot/Q9D2R0 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Acetoacetyl-CoA synthetase ^@ http://purl.uniprot.org/annotation/PRO_0000315786 http://togogenome.org/gene/10090:Tctn2 ^@ http://purl.uniprot.org/uniprot/Q2MV57 ^@ 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|||Tectonic-2 ^@ http://purl.uniprot.org/annotation/PRO_0000229799|||http://purl.uniprot.org/annotation/VSP_017766 http://togogenome.org/gene/10090:Krt12 ^@ http://purl.uniprot.org/uniprot/Z4YJD9 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||IF rod|||Polar residues ^@ http://togogenome.org/gene/10090:Wnk4 ^@ http://purl.uniprot.org/uniprot/Q80UE6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolished serine/threonine-protein kinase activity without affecting ability to regulate localization of TRPV4 and SLC12A9.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Increased protein level, probably due to defects in ubiquitination. Knockin mice display higher blood pressure, hyperkalemia, hypercalciuria and marked hyperplasia of the distal convoluted tubule cells of kidney.|||Increased protein level, probably due to defects in ubiquitination. Knockin mice display higher blood pressure, hyperkalemia, hypercalciuria and marked hyperplasia of the distal convoluted tubule cells of kidney. Increased phosphorylation of OXSR1/OSR1 and STK39/SPAK is observed, leading to phosphorylation and activation of SLC12A3/NCC.|||Interaction with KLHL3|||Loss of serine/threonine-protein kinase activity. No effect on inhibition of KCNJ1, SCNN1A, SCNN1B or SCNN1D.|||No effect on inhibition of SLC12A3.|||No effect on inhibition of SLC4A4.|||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_0000086825 http://togogenome.org/gene/10090:Mrps23 ^@ http://purl.uniprot.org/uniprot/Q3TI14|||http://purl.uniprot.org/uniprot/Q8VE22 ^@ 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 ^@ Basic and acidic residues|||Disordered|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Removed|||Small ribosomal subunit protein mS23|||Small ribosomal subunit protein mS23 conserved ^@ http://purl.uniprot.org/annotation/PRO_0000087706 http://togogenome.org/gene/10090:Cenpu ^@ http://purl.uniprot.org/uniprot/Q8C4M7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||Centromere protein U|||Disordered|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PLK1|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247673|||http://purl.uniprot.org/annotation/VSP_020031|||http://purl.uniprot.org/annotation/VSP_020032 http://togogenome.org/gene/10090:Abca13 ^@ http://purl.uniprot.org/uniprot/Q5SSE9 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family A member 13|||Disordered|||Does not affect intracellular vesicle localization. Affects cholesterol internalization.|||Does not affect intracellular vesicle localization.Affects cholesterol internalization.|||Does not affect protein expression. Affects intracellular vesicles localization. Impairs intracellular cholesterol accumulation in the vesicle.|||Does not affect protein expression. Decreases intracellular cholesterol accumulation in the vesicle.|||Helical|||In isoform 2.|||In isoform 3. ^@ http://purl.uniprot.org/annotation/PRO_0000253574|||http://purl.uniprot.org/annotation/VSP_021071|||http://purl.uniprot.org/annotation/VSP_021072|||http://purl.uniprot.org/annotation/VSP_021073|||http://purl.uniprot.org/annotation/VSP_021074 http://togogenome.org/gene/10090:Gpr158 ^@ http://purl.uniprot.org/uniprot/Q8C419 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cache-like region|||Cytoplasmic|||Disordered|||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|||Metabotropic glycine receptor|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||VCPWE motif 1|||VCPWE motif 2|||VCPWE motif 3 ^@ http://purl.uniprot.org/annotation/PRO_0000012970 http://togogenome.org/gene/10090:Pcdhgb4 ^@ http://purl.uniprot.org/uniprot/Q91XX6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Cadherin|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099494 http://togogenome.org/gene/10090:Lmo1 ^@ http://purl.uniprot.org/uniprot/A0A140LHX4|||http://purl.uniprot.org/uniprot/A0A140LIB4|||http://purl.uniprot.org/uniprot/Q3UZX1|||http://purl.uniprot.org/uniprot/Q924W9 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent ^@ LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||Rhombotin-1 ^@ http://purl.uniprot.org/annotation/PRO_0000075895 http://togogenome.org/gene/10090:Thrb ^@ http://purl.uniprot.org/uniprot/P37242|||http://purl.uniprot.org/uniprot/Q3UZT5 ^@ Binding Site|||Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform Beta-2.|||Interaction with NR2F6|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Thyroid hormone receptor beta ^@ http://purl.uniprot.org/annotation/PRO_0000053448|||http://purl.uniprot.org/annotation/VSP_031078 http://togogenome.org/gene/10090:Rex2 ^@ http://purl.uniprot.org/uniprot/A2AWF2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Zfp418 ^@ http://purl.uniprot.org/uniprot/Q8BFS8 ^@ 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 418 ^@ http://purl.uniprot.org/annotation/PRO_0000458876 http://togogenome.org/gene/10090:Zfp966 ^@ http://purl.uniprot.org/uniprot/A2ART2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Dnal4 ^@ http://purl.uniprot.org/uniprot/Q9DCM4 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Dynein axonemal light chain 4 ^@ http://purl.uniprot.org/annotation/PRO_0000195137 http://togogenome.org/gene/10090:Rpl39l ^@ http://purl.uniprot.org/uniprot/Q9CQD0 ^@ Chain|||Molecule Processing ^@ Chain ^@ Large ribosomal subunit protein eL39-like ^@ http://purl.uniprot.org/annotation/PRO_0000457814 http://togogenome.org/gene/10090:Glt1d1 ^@ http://purl.uniprot.org/uniprot/A4FUP9 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Glycosyltransferase 1 domain-containing protein 1|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000312204|||http://purl.uniprot.org/annotation/VSP_029734|||http://purl.uniprot.org/annotation/VSP_029735 http://togogenome.org/gene/10090:Cmya5 ^@ http://purl.uniprot.org/uniprot/E9QLJ0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Acidic residues|||B30.2/SPRY|||Basic and acidic residues|||Basic residues|||Disordered|||Fibronectin type-III|||Polar residues ^@ http://togogenome.org/gene/10090:Gdpd2 ^@ http://purl.uniprot.org/uniprot/Q9ESM6 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||GP-PDE|||Glycerophosphoinositol inositolphosphodiesterase GDPD2|||Helical|||Loss of activity.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000251935 http://togogenome.org/gene/10090:Mmp1b ^@ http://purl.uniprot.org/uniprot/G5E8A9 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Motif|||Repeat|||Signal Peptide ^@ Cysteine switch|||Hemopexin|||Peptidase metallopeptidase|||in inhibited form ^@ http://purl.uniprot.org/annotation/PRO_5015019723 http://togogenome.org/gene/10090:Snrnp70 ^@ http://purl.uniprot.org/uniprot/A2RS68|||http://purl.uniprot.org/uniprot/Q62376 ^@ 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 ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||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_0000081881|||http://purl.uniprot.org/annotation/VSP_005851|||http://purl.uniprot.org/annotation/VSP_005852 http://togogenome.org/gene/10090:Or52a20 ^@ http://purl.uniprot.org/uniprot/E9PV96 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gpr156 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0P3|||http://purl.uniprot.org/uniprot/Q6PCP7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||N-linked (GlcNAc...) asparagine|||Polar residues|||Probable G-protein coupled receptor 156 ^@ http://purl.uniprot.org/annotation/PRO_0000206900 http://togogenome.org/gene/10090:Kcnn4 ^@ http://purl.uniprot.org/uniprot/O89109 ^@ Chain|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane ^@ 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|||Intermediate conductance calcium-activated potassium channel protein 4|||Phosphohistidine|||Pore-forming; Name=Segment H5 ^@ http://purl.uniprot.org/annotation/PRO_0000155018 http://togogenome.org/gene/10090:Fam53c ^@ http://purl.uniprot.org/uniprot/Q8BXQ8 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||Protein FAM53C ^@ http://purl.uniprot.org/annotation/PRO_0000189547 http://togogenome.org/gene/10090:Fanci ^@ http://purl.uniprot.org/uniprot/Q8K368 ^@ 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|||Fanconi anemia group I protein homolog|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000289977|||http://purl.uniprot.org/annotation/VSP_026072|||http://purl.uniprot.org/annotation/VSP_026073|||http://purl.uniprot.org/annotation/VSP_026074 http://togogenome.org/gene/10090:Prcc ^@ http://purl.uniprot.org/uniprot/Q9EQC8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Plekhg3 ^@ http://purl.uniprot.org/uniprot/Q4VAC9 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family G member 3|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000306864|||http://purl.uniprot.org/annotation/VSP_028535|||http://purl.uniprot.org/annotation/VSP_028536|||http://purl.uniprot.org/annotation/VSP_028537|||http://purl.uniprot.org/annotation/VSP_028538|||http://purl.uniprot.org/annotation/VSP_028539|||http://purl.uniprot.org/annotation/VSP_028540|||http://purl.uniprot.org/annotation/VSP_028541|||http://purl.uniprot.org/annotation/VSP_028542 http://togogenome.org/gene/10090:Lrrc59 ^@ http://purl.uniprot.org/uniprot/Q922Q8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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_0000235160|||http://purl.uniprot.org/annotation/PRO_0000441740 http://togogenome.org/gene/10090:Mamld1 ^@ http://purl.uniprot.org/uniprot/D3Z768|||http://purl.uniprot.org/uniprot/P0C6A2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Basic residues|||Disordered|||Mastermind-like domain-containing protein 1|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000317430 http://togogenome.org/gene/10090:Neu1 ^@ http://purl.uniprot.org/uniprot/O35657|||http://purl.uniprot.org/uniprot/Q3UL64 ^@ 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 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide ^@ BNR 1|||BNR 2|||BNR 3|||BNR 4|||FRIP motif|||Internalization signal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton acceptor|||Reduced activity.|||Sialidase|||Sialidase-1|||exo-alpha-sialidase ^@ http://purl.uniprot.org/annotation/PRO_0000012027|||http://purl.uniprot.org/annotation/PRO_5014309168 http://togogenome.org/gene/10090:Phospho1 ^@ http://purl.uniprot.org/uniprot/Q8R2H9 ^@ Active Site|||Binding Site|||Chain|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain ^@ Nucleophile|||Phosphoethanolamine/phosphocholine phosphatase|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000068830 http://togogenome.org/gene/10090:Hint3 ^@ http://purl.uniprot.org/uniprot/Q9CPS6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region ^@ Adenosine 5'-monophosphoramidase HINT3|||Disordered|||HIT|||Histidine triad motif|||N-acetylalanine|||Removed|||Tele-AMP-histidine intermediate ^@ http://purl.uniprot.org/annotation/PRO_0000324328 http://togogenome.org/gene/10090:Or51r1 ^@ http://purl.uniprot.org/uniprot/E9Q544 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ddx5 ^@ http://purl.uniprot.org/uniprot/Q8BTS0 ^@ Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Compositionally Biased Region|||Domain Extent|||Motif|||Region ^@ Basic and acidic residues|||DEAD-box RNA helicase Q|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Q motif ^@ http://togogenome.org/gene/10090:Defb6 ^@ http://purl.uniprot.org/uniprot/Q0VDZ1|||http://purl.uniprot.org/uniprot/Q91VD6 ^@ Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Modified Residue|||Signal Peptide ^@ Beta-defensin 6|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000006932|||http://purl.uniprot.org/annotation/PRO_5014306870 http://togogenome.org/gene/10090:Gclc ^@ http://purl.uniprot.org/uniprot/P97494 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Modified Residue|||Sequence Conflict ^@ Glutamate--cysteine ligase catalytic subunit|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000192564 http://togogenome.org/gene/10090:Sod3 ^@ http://purl.uniprot.org/uniprot/O09164|||http://purl.uniprot.org/uniprot/Q542X9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||Extracellular superoxide dismutase [Cu-Zn]|||N-linked (GlcNAc...) asparagine|||Superoxide dismutase [Cu-Zn]|||Superoxide dismutase copper/zinc binding ^@ http://purl.uniprot.org/annotation/PRO_0000032856|||http://purl.uniprot.org/annotation/PRO_0000032857|||http://purl.uniprot.org/annotation/PRO_5009971088 http://togogenome.org/gene/10090:Vmn2r35 ^@ http://purl.uniprot.org/uniprot/E9Q7U8 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003243124 http://togogenome.org/gene/10090:Trpm6 ^@ http://purl.uniprot.org/uniprot/A0A1W5LU38|||http://purl.uniprot.org/uniprot/Q8CIR4 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Alpha-type protein kinase|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphothreonine; by autocatalysis|||Polar residues|||Pore-forming|||Proton acceptor|||Transient receptor potential cation channel subfamily M member 6 ^@ http://purl.uniprot.org/annotation/PRO_0000215330 http://togogenome.org/gene/10090:Naa10 ^@ http://purl.uniprot.org/uniprot/B1AUY9|||http://purl.uniprot.org/uniprot/Q3V4D5|||http://purl.uniprot.org/uniprot/Q540H0|||http://purl.uniprot.org/uniprot/Q9QY36 ^@ 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|||Interaction with NAA15|||N-acetylmethionine|||N-acetyltransferase|||N-alpha-acetyltransferase 10|||N6-acetyllysine; by autocatalysis|||Phosphoserine|||Phosphoserine; by IKKB ^@ http://purl.uniprot.org/annotation/PRO_0000074533 http://togogenome.org/gene/10090:H2bc23 ^@ http://purl.uniprot.org/uniprot/P10853|||http://purl.uniprot.org/uniprot/Q8CBB6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||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 H2A/H2B/H3|||Histone H2B type 1-F/J/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-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_0000071839 http://togogenome.org/gene/10090:Slc23a2 ^@ http://purl.uniprot.org/uniprot/Q9EPR4 ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Solute carrier family 23 member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000165979|||http://purl.uniprot.org/annotation/VSP_007367|||http://purl.uniprot.org/annotation/VSP_007368 http://togogenome.org/gene/10090:Laptm4a ^@ http://purl.uniprot.org/uniprot/Q8BG66 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Zfp276 ^@ http://purl.uniprot.org/uniprot/Q8CE64 ^@ 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|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||Polar residues|||ZAD|||Zinc finger protein 276 ^@ http://purl.uniprot.org/annotation/PRO_0000047324|||http://purl.uniprot.org/annotation/VSP_026106|||http://purl.uniprot.org/annotation/VSP_026107 http://togogenome.org/gene/10090:Krt71 ^@ http://purl.uniprot.org/uniprot/Q9R0H5 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Site ^@ Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In Rco12; causes a wavy pelage and curly vibrissae.|||In Rco13; causes a wavy pelage and curly vibrissae.|||In caracul Rinshoken; causes a wavy hair phenotype.|||In caracul; causes a wavy hair phenotype.|||Keratin, type II cytoskeletal 71|||Linker 1|||Linker 12|||Polar residues|||Stutter|||Tail ^@ http://purl.uniprot.org/annotation/PRO_0000063738 http://togogenome.org/gene/10090:Gnb1 ^@ http://purl.uniprot.org/uniprot/P62874|||http://purl.uniprot.org/uniprot/Q3TQ70 ^@ Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Strand|||Turn ^@ Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1|||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_0000127688 http://togogenome.org/gene/10090:Slc48a1 ^@ http://purl.uniprot.org/uniprot/Q9D8M3 ^@ Chain|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Motif|||Sequence Conflict|||Transmembrane ^@ Di-leucine motif|||Helical|||Heme transporter HRG1 ^@ http://purl.uniprot.org/annotation/PRO_0000348576 http://togogenome.org/gene/10090:Sat2 ^@ http://purl.uniprot.org/uniprot/A0A158SIT0|||http://purl.uniprot.org/uniprot/Q6P8J2 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue ^@ N-acetyltransferase|||N6-acetyllysine|||Proton donor|||Thialysine N-epsilon-acetyltransferase ^@ http://purl.uniprot.org/annotation/PRO_0000074599 http://togogenome.org/gene/10090:Ffar1 ^@ http://purl.uniprot.org/uniprot/Q76JU9 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000227755 http://togogenome.org/gene/10090:Flot2 ^@ http://purl.uniprot.org/uniprot/Q3UEG9|||http://purl.uniprot.org/uniprot/Q60634 ^@ Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn ^@ Band 7|||Flotillin-2|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||Phosphoserine|||Removed|||S-palmitoyl cysteine|||S-palmitoyl cysteine; by ZDHHC5 ^@ http://purl.uniprot.org/annotation/PRO_0000094050|||http://purl.uniprot.org/annotation/VSP_000502|||http://purl.uniprot.org/annotation/VSP_037692 http://togogenome.org/gene/10090:Chrna2 ^@ http://purl.uniprot.org/uniprot/Q91X60 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Associated with receptor activation|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-2 ^@ http://purl.uniprot.org/annotation/PRO_0000000341 http://togogenome.org/gene/10090:Pex14 ^@ http://purl.uniprot.org/uniprot/Q9R0A0 ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||N-acetylalanine|||N6-acetyllysine|||Peroxisomal|||Peroxisomal membrane protein PEX14|||Phosphoserine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000058326 http://togogenome.org/gene/10090:Or9s14 ^@ http://purl.uniprot.org/uniprot/Q8VFC5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Plpp1 ^@ http://purl.uniprot.org/uniprot/Q61469 ^@ Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Decreased lipid phosphatase activity.|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Loss of N-glycosylation. No significant effect on lipid phosphatase activity.|||Loss of lipid phosphatase activity.|||N-linked (GlcNAc...) asparagine|||No effect on lipid phosphatase activity.|||No significant effect on lipid phosphatase activity.|||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|||Proton donors|||Stabilizes the active site histidine for nucleophilic attack ^@ http://purl.uniprot.org/annotation/PRO_0000220906|||http://purl.uniprot.org/annotation/VSP_009652 http://togogenome.org/gene/10090:Ccdc88c ^@ http://purl.uniprot.org/uniprot/Q6VGS5 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes binding to DVL1.|||Basic and acidic residues|||Calponin-homology (CH)|||DVL1-binding|||Disordered|||GBA|||In isoform 2.|||PDZ-binding|||Phosphoserine|||Polar residues|||Protein Daple ^@ http://purl.uniprot.org/annotation/PRO_0000284726|||http://purl.uniprot.org/annotation/VSP_052377 http://togogenome.org/gene/10090:Kremen2 ^@ http://purl.uniprot.org/uniprot/Q8K1S7 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ CUB|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Kremen protein 2|||Kringle|||N-linked (GlcNAc...) asparagine|||WSC ^@ http://purl.uniprot.org/annotation/PRO_0000021569 http://togogenome.org/gene/10090:Pitpnm3 ^@ http://purl.uniprot.org/uniprot/Q3UHE1 ^@ 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|||DDHD|||Disordered|||In isoform 2.|||Membrane-associated phosphatidylinositol transfer protein 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000232744|||http://purl.uniprot.org/annotation/VSP_017966 http://togogenome.org/gene/10090:Ly6g6f ^@ http://purl.uniprot.org/uniprot/B2RXM6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||Ig-like ^@ http://purl.uniprot.org/annotation/PRO_5015087169 http://togogenome.org/gene/10090:Tspo ^@ http://purl.uniprot.org/uniprot/P50637 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes cholesterol transport.|||Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Mitochondrial intermembrane|||No effect.|||Translocator protein ^@ http://purl.uniprot.org/annotation/PRO_0000190998 http://togogenome.org/gene/10090:Or4f6 ^@ http://purl.uniprot.org/uniprot/Q8VF85 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Bcat2 ^@ http://purl.uniprot.org/uniprot/O35855|||http://purl.uniprot.org/uniprot/O88374|||http://purl.uniprot.org/uniprot/Q3ULU3 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide ^@ Branched-chain-amino-acid aminotransferase, mitochondrial|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000001272 http://togogenome.org/gene/10090:Qrsl1 ^@ http://purl.uniprot.org/uniprot/Q9CZN8 ^@ Active Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Sequence Conflict ^@ Acyl-ester intermediate|||Charge relay system|||Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000316769 http://togogenome.org/gene/10090:Zswim9 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1C4|||http://purl.uniprot.org/uniprot/Q6DI92 ^@ 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.|||In isoform 3.|||In isoform 4.|||SWIM-type|||Uncharacterized protein ZSWIM9 ^@ http://purl.uniprot.org/annotation/PRO_0000322597|||http://purl.uniprot.org/annotation/VSP_031965|||http://purl.uniprot.org/annotation/VSP_031966|||http://purl.uniprot.org/annotation/VSP_031967|||http://purl.uniprot.org/annotation/VSP_031968|||http://purl.uniprot.org/annotation/VSP_031969|||http://purl.uniprot.org/annotation/VSP_031970 http://togogenome.org/gene/10090:Upf2 ^@ http://purl.uniprot.org/uniprot/A2AT37 ^@ 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|||Binds to UPF3B|||Disordered|||Interaction with UPF1|||MIF4G 1|||MIF4G 2|||MIF4G 3|||Necessary for interaction with UPF1|||Phosphothreonine|||Regulator of nonsense transcripts 2|||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_0000448685 http://togogenome.org/gene/10090:Mtx3 ^@ http://purl.uniprot.org/uniprot/D3YTP3 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Metaxin glutathione S-transferase|||Mitochondrial outer membrane transport complex Sam37/metaxin N-terminal ^@ http://togogenome.org/gene/10090:Bglap ^@ http://purl.uniprot.org/uniprot/P86546 ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Propeptide|||Signal Peptide ^@ 4-carboxyglutamate|||Gla|||Osteocalcin ^@ http://purl.uniprot.org/annotation/PRO_0000011088|||http://purl.uniprot.org/annotation/PRO_0000011089 http://togogenome.org/gene/10090:1700066M21Rik ^@ http://purl.uniprot.org/uniprot/Q9D9H8 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transit Peptide ^@ Disordered|||Mitochondrial protein C2orf69 homolog|||Mitochondrion|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000329089 http://togogenome.org/gene/10090:Tmem81 ^@ http://purl.uniprot.org/uniprot/Q9D5K1 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||Ig-like|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 81 ^@ http://purl.uniprot.org/annotation/PRO_0000287877 http://togogenome.org/gene/10090:Zfp251 ^@ http://purl.uniprot.org/uniprot/Q6PCX8 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB ^@ http://togogenome.org/gene/10090:Ndufs4 ^@ http://purl.uniprot.org/uniprot/Q9CXZ1 ^@ Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide|||Turn ^@ Mitochondrion|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000020039 http://togogenome.org/gene/10090:Mettl26 ^@ http://purl.uniprot.org/uniprot/Q9DCS2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Modified Residue ^@ Methyltransferase-like 26|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000337115 http://togogenome.org/gene/10090:Cdhr3 ^@ http://purl.uniprot.org/uniprot/Q8BL00 ^@ 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 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin-related family member 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000305904 http://togogenome.org/gene/10090:Gtf2ird2 ^@ http://purl.uniprot.org/uniprot/Q99NI3 ^@ Chain|||Molecule Processing|||Region|||Repeat ^@ Chain|||Region|||Repeat ^@ Disordered|||GTF2I-like 1|||GTF2I-like 2|||General transcription factor II-I repeat domain-containing protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000320122 http://togogenome.org/gene/10090:Ing4 ^@ http://purl.uniprot.org/uniprot/Q8C0D7 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger ^@ Basic and acidic residues|||Bipartite nuclear localization signal|||Citrulline|||Disordered|||Histone H3K4me3 binding|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Inhibitor of growth protein 4|||N6-acetyllysine|||PHD-type ^@ http://purl.uniprot.org/annotation/PRO_0000212669|||http://purl.uniprot.org/annotation/VSP_012520|||http://purl.uniprot.org/annotation/VSP_012521|||http://purl.uniprot.org/annotation/VSP_012522|||http://purl.uniprot.org/annotation/VSP_012523|||http://purl.uniprot.org/annotation/VSP_012524|||http://purl.uniprot.org/annotation/VSP_012525|||http://purl.uniprot.org/annotation/VSP_012526|||http://purl.uniprot.org/annotation/VSP_012527 http://togogenome.org/gene/10090:Specc1l ^@ http://purl.uniprot.org/uniprot/A0A0R4J0J8|||http://purl.uniprot.org/uniprot/Q2KN98|||http://purl.uniprot.org/uniprot/Q6GQV8|||http://purl.uniprot.org/uniprot/Q8C9Q9 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region ^@ Basic and acidic residues|||Calponin-homology (CH)|||Cytospin-A|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000231019 http://togogenome.org/gene/10090:Ppdpf ^@ http://purl.uniprot.org/uniprot/Q9CR37 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Modified Residue|||Region ^@ Disordered|||Pancreatic progenitor cell differentiation and proliferation factor|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000079469 http://togogenome.org/gene/10090:Rftn1 ^@ http://purl.uniprot.org/uniprot/Q6A0D4 ^@ 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|||Polar residues|||Raftlin|||Removed|||S-palmitoyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000251954 http://togogenome.org/gene/10090:Lpcat4 ^@ http://purl.uniprot.org/uniprot/Q6NVG1 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||HXXXXD motif|||Helical|||Lysophospholipid acyltransferase LPCAT4|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247055 http://togogenome.org/gene/10090:Serpina3m ^@ http://purl.uniprot.org/uniprot/Q03734 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond|||Serine protease inhibitor A3M ^@ http://purl.uniprot.org/annotation/PRO_0000032418 http://togogenome.org/gene/10090:Or5p67 ^@ http://purl.uniprot.org/uniprot/Q8VFD1 ^@ 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 5P67 ^@ http://purl.uniprot.org/annotation/PRO_0000150847 http://togogenome.org/gene/10090:Hapln3 ^@ http://purl.uniprot.org/uniprot/Q80WM5 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide ^@ Hyaluronan and proteoglycan link protein 3|||Ig-like V-type|||Link 1|||Link 2 ^@ http://purl.uniprot.org/annotation/PRO_0000013191 http://togogenome.org/gene/10090:Ssx2ip ^@ http://purl.uniprot.org/uniprot/A0A0R4J1A9|||http://purl.uniprot.org/uniprot/Q8VC66 ^@ 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 ^@ Afadin- and alpha-actinin-binding protein|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000064456 http://togogenome.org/gene/10090:Izumo2 ^@ http://purl.uniprot.org/uniprot/Q9DA16 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Izumo sperm-egg fusion protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000373774|||http://purl.uniprot.org/annotation/VSP_037224|||http://purl.uniprot.org/annotation/VSP_037225|||http://purl.uniprot.org/annotation/VSP_037226 http://togogenome.org/gene/10090:Psmg1 ^@ http://purl.uniprot.org/uniprot/Q9JK23 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Proteasome assembly chaperone 1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000322547 http://togogenome.org/gene/10090:Ajap1 ^@ http://purl.uniprot.org/uniprot/A2ALI5 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Adherens junction-associated protein 1|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues|||Targeting signals ^@ http://purl.uniprot.org/annotation/PRO_0000284802 http://togogenome.org/gene/10090:Ccdc28b ^@ http://purl.uniprot.org/uniprot/Q8CEG5 ^@ 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|||Coiled-coil domain-containing protein 28B|||Disordered|||N-acetylmethionine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000234095 http://togogenome.org/gene/10090:Fam110b ^@ http://purl.uniprot.org/uniprot/Q8C739 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Phosphoserine|||Protein FAM110B ^@ http://purl.uniprot.org/annotation/PRO_0000285652 http://togogenome.org/gene/10090:Gm12253 ^@ http://purl.uniprot.org/uniprot/Q5NC48 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ ^@ http://purl.uniprot.org/annotation/PRO_5004260397 http://togogenome.org/gene/10090:Rfpl4b ^@ http://purl.uniprot.org/uniprot/J3QPR6 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||RING-type ^@ http://togogenome.org/gene/10090:Neo1 ^@ http://purl.uniprot.org/uniprot/E9QK04|||http://purl.uniprot.org/uniprot/P97798|||http://purl.uniprot.org/uniprot/Q7TQG5 ^@ 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|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane ^@ 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.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Neogenin|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000015044|||http://purl.uniprot.org/annotation/PRO_5003246243|||http://purl.uniprot.org/annotation/PRO_5015098858|||http://purl.uniprot.org/annotation/VSP_002594|||http://purl.uniprot.org/annotation/VSP_002595|||http://purl.uniprot.org/annotation/VSP_002596|||http://purl.uniprot.org/annotation/VSP_002597 http://togogenome.org/gene/10090:Zfp87 ^@ http://purl.uniprot.org/uniprot/Q8K2A4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Pou6f1 ^@ http://purl.uniprot.org/uniprot/Q5U4D4 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||POU-specific|||Pro residues ^@ http://togogenome.org/gene/10090:Taf7l ^@ http://purl.uniprot.org/uniprot/B1AV36|||http://purl.uniprot.org/uniprot/Q9D3R9 ^@ 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 ^@ Acidic residues|||Disordered|||Does not affect interaction with TBP. Knockin mice are fertile.|||In isoform 2.|||Phosphoserine|||TAFII55 protein conserved region|||Transcription initiation factor TFIID subunit 7-like ^@ http://purl.uniprot.org/annotation/PRO_0000307862|||http://purl.uniprot.org/annotation/VSP_028849 http://togogenome.org/gene/10090:Or5b12 ^@ http://purl.uniprot.org/uniprot/Q8VFX1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Tppp2 ^@ http://purl.uniprot.org/uniprot/Q0P5Y3 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Tubulin polymerization-promoting protein family member 2 ^@ http://purl.uniprot.org/annotation/PRO_0000289004 http://togogenome.org/gene/10090:Or5p55 ^@ http://purl.uniprot.org/uniprot/Q8VGI4 ^@ 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 5P55 ^@ http://purl.uniprot.org/annotation/PRO_0000150835 http://togogenome.org/gene/10090:Clca4b ^@ http://purl.uniprot.org/uniprot/Q3UW98 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ Helical|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_5015097506 http://togogenome.org/gene/10090:Serpinb6c ^@ http://purl.uniprot.org/uniprot/Q6P6K7|||http://purl.uniprot.org/uniprot/W4VSP4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Serpin ^@ http://togogenome.org/gene/10090:Osbpl8 ^@ http://purl.uniprot.org/uniprot/A0A0R4J150|||http://purl.uniprot.org/uniprot/B9EJ86 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||Basic residues|||Disordered|||Helical|||N-acetylmethionine|||Oxysterol-binding protein-related protein 8|||PH|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000434121 http://togogenome.org/gene/10090:C2cd4d ^@ http://purl.uniprot.org/uniprot/P0CG09 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ C2|||C2 calcium-dependent domain-containing protein 4D|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000394961 http://togogenome.org/gene/10090:Macc1 ^@ http://purl.uniprot.org/uniprot/E9PXX8 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ Disordered|||SH3|||ZU5 ^@ http://togogenome.org/gene/10090:Dusp23 ^@ http://purl.uniprot.org/uniprot/Q6NT99 ^@ Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Domain Extent|||Sequence Conflict ^@ Dual specificity protein phosphatase 23|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000094836 http://togogenome.org/gene/10090:Ugt2b5 ^@ http://purl.uniprot.org/uniprot/Q3UWB9|||http://purl.uniprot.org/uniprot/Q8K169 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical|||UDP-glucuronosyltransferase ^@ http://purl.uniprot.org/annotation/PRO_5015020124 http://togogenome.org/gene/10090:Vmn1r260 ^@ http://purl.uniprot.org/uniprot/K9J7F4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cnppd1 ^@ http://purl.uniprot.org/uniprot/Q8K158 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Protein CNPPD1 ^@ http://purl.uniprot.org/annotation/PRO_0000089353 http://togogenome.org/gene/10090:Ar ^@ http://purl.uniprot.org/uniprot/P19091 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Site|||Strand|||Turn|||Zinc Finger ^@ Androgen receptor|||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 ubiquitin)|||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|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine|||Phosphoserine; by CDK9|||Phosphotyrosine; by CSK|||Phosphotyrosine; by CSK and TNK2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000053707 http://togogenome.org/gene/10090:Cldn11 ^@ http://purl.uniprot.org/uniprot/Q60771 ^@ 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_0000144762 http://togogenome.org/gene/10090:Klk13 ^@ http://purl.uniprot.org/uniprot/Q8CGR6 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015099072 http://togogenome.org/gene/10090:Mxd1 ^@ http://purl.uniprot.org/uniprot/Q8K1Z8 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ BHLH|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Apol6 ^@ http://purl.uniprot.org/uniprot/B7ZC54|||http://purl.uniprot.org/uniprot/B7ZC55|||http://purl.uniprot.org/uniprot/Q3UN08|||http://purl.uniprot.org/uniprot/Q9D6L7 ^@ Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region|||Transmembrane ^@ Compositionally Biased Region|||Non-terminal Residue|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Stox1 ^@ http://purl.uniprot.org/uniprot/B2RQL2 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic residues|||Disordered|||Polar residues|||Storkhead-box protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000433298 http://togogenome.org/gene/10090:Prps1l3 ^@ http://purl.uniprot.org/uniprot/G3UXL2|||http://purl.uniprot.org/uniprot/Q3UYQ0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ribose-phosphate pyrophosphokinase N-terminal ^@ http://togogenome.org/gene/10090:Spata33 ^@ http://purl.uniprot.org/uniprot/A0A1D5RLP4|||http://purl.uniprot.org/uniprot/A0A1D5RLV5|||http://purl.uniprot.org/uniprot/Q8C624 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region ^@ Basic and acidic residues|||Disordered|||Interaction with ATG16L1|||Interaction with VDAC2|||PQIIIT|||Phosphoserine|||Polar residues|||Spermatogenesis-associated protein 33 ^@ http://purl.uniprot.org/annotation/PRO_0000282410 http://togogenome.org/gene/10090:Mdga1 ^@ http://purl.uniprot.org/uniprot/D3Z499 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide ^@ Disordered|||Fibronectin type-III|||Ig-like|||MAM|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003053043 http://togogenome.org/gene/10090:Gzmn ^@ http://purl.uniprot.org/uniprot/Q76HN3|||http://purl.uniprot.org/uniprot/Q920S1 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Signal Peptide ^@ Peptidase S1 ^@ http://purl.uniprot.org/annotation/PRO_5015098638|||http://purl.uniprot.org/annotation/PRO_5015099547 http://togogenome.org/gene/10090:Or8k30 ^@ http://purl.uniprot.org/uniprot/A2AK60 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Zfp777 ^@ http://purl.uniprot.org/uniprot/B9EKF4|||http://purl.uniprot.org/uniprot/G5E8L5 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ C2H2-type|||Disordered|||KRAB|||KRAB-related|||Polar residues ^@ http://togogenome.org/gene/10090:Foxc2 ^@ http://purl.uniprot.org/uniprot/B9EI61|||http://purl.uniprot.org/uniprot/Q61850 ^@ 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 ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein C2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000091809 http://togogenome.org/gene/10090:Syt2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J2C2|||http://purl.uniprot.org/uniprot/P46097 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Acidic residues|||Basic and acidic residues|||C2|||C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||No binding to BoNT/B. No binding to BoNT/G.|||No binding to BoNT/B. Wild-type binding to BoNT/G.|||No binding to C.botulinum neurotoxin type B (BoNT/B, botB). Requires gangliosides to bind BoNT/B, wild-type binding to BoNT/G.|||Only binds to BoNT/B in presence of gangliosides.|||Phospholipid binding|||Phosphothreonine|||Phosphotyrosine|||Requires gangliosides to bind BoNT/B, no binding to BoNT/G with or without gangliosides.|||Synaptotagmin-2|||Vesicular|||Wild-type binding to BoNT/B.|||Wild-type binding to BoNT/B. Wild-type in binding to BoNT/G.|||Wild-type in binding to C.botulinum neurotoxin type G (BoNT/G, botG). ^@ http://purl.uniprot.org/annotation/PRO_0000183943 http://togogenome.org/gene/10090:Arnt2 ^@ http://purl.uniprot.org/uniprot/Q61324 ^@ 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 ^@ Aryl hydrocarbon receptor nuclear translocator 2|||Basic and acidic residues|||Compromises SIM1:ARNT2 heterodimer stability. Compromises NPAS4:ARNT2 heterodimer stability.|||Compromises SIM1:ARNT2 heterodimer stability. Does not compromise NPAS4:ARNT2 heterodimer stability.|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||PAC|||PAS 1|||PAS 2|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127123|||http://purl.uniprot.org/annotation/VSP_022689 http://togogenome.org/gene/10090:C8g ^@ http://purl.uniprot.org/uniprot/Q8VCG4|||http://purl.uniprot.org/uniprot/Q9DAC2 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide ^@ Complement component C8 gamma chain|||Interchain (with C-194 in C8-alpha chain)|||Lipocalin/cytosolic fatty-acid binding|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000017882 http://togogenome.org/gene/10090:Tmem245 ^@ http://purl.uniprot.org/uniprot/D3YWD3 ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Compositionally Biased Region|||Region|||Transmembrane ^@ Disordered|||Helical|||Polar residues ^@ http://togogenome.org/gene/10090:Pola1 ^@ http://purl.uniprot.org/uniprot/B9EHJ9|||http://purl.uniprot.org/uniprot/P33609 ^@ 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 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger ^@ Basic and acidic residues|||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|||Disordered|||In temperature-sensitive FT20 cell line; defective activity.|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Results in loss of primer extension catalytic activity but retains ability to bind to the primase complex.|||Zinc finger DNA-directed DNA polymerase family B alpha ^@ http://purl.uniprot.org/annotation/PRO_0000046429 http://togogenome.org/gene/10090:Kansl3 ^@ http://purl.uniprot.org/uniprot/A2RSY1 ^@ 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 3.|||In isoform 3.|||KAT8 regulatory NSL complex subunit 3|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000287138|||http://purl.uniprot.org/annotation/VSP_025334|||http://purl.uniprot.org/annotation/VSP_025335 http://togogenome.org/gene/10090:Fen1 ^@ http://purl.uniprot.org/uniprot/Q8C952|||http://purl.uniprot.org/uniprot/Q91Z50 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||XPG N-terminal|||XPG-I ^@ http://togogenome.org/gene/10090:Rpa1 ^@ http://purl.uniprot.org/uniprot/Q3U8B3|||http://purl.uniprot.org/uniprot/Q5SWN2|||http://purl.uniprot.org/uniprot/Q8VEE4 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Variant ^@ 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|||N-acetylmethionine|||N6-acetyllysine; alternate|||OB|||Phosphoserine|||Phosphothreonine|||Polar residues|||Replication factor A C-terminal|||Replication factor-A protein 1 N-terminal|||Replication protein A 70 kDa DNA-binding subunit|||Replication protein A OB ^@ http://purl.uniprot.org/annotation/PRO_0000097261 http://togogenome.org/gene/10090:Nrl ^@ http://purl.uniprot.org/uniprot/P54846|||http://purl.uniprot.org/uniprot/Q543Y0|||http://purl.uniprot.org/uniprot/Q8C8Y1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region ^@ BZIP|||Basic motif|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Leucine-zipper|||Minimal transactivation domain (MTD)|||Neural retina-specific leucine zipper protein|||Polar residues|||bZIP ^@ http://purl.uniprot.org/annotation/PRO_0000076634 http://togogenome.org/gene/10090:Wdtc1 ^@ http://purl.uniprot.org/uniprot/Q80ZK9 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Modified Residue|||Region|||Repeat ^@ Disordered|||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_0000051435 http://togogenome.org/gene/10090:B3gntl1 ^@ http://purl.uniprot.org/uniprot/Q3U129 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant ^@ Chain|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||In isoform 3.|||UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000289221|||http://purl.uniprot.org/annotation/VSP_025965|||http://purl.uniprot.org/annotation/VSP_025966|||http://purl.uniprot.org/annotation/VSP_025967 http://togogenome.org/gene/10090:Rccd1 ^@ http://purl.uniprot.org/uniprot/Q8BTU7 ^@ 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 ^@ (3R)-3-hydroxyarginine|||In isoform 2.|||Interaction with KDM8|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000337975|||http://purl.uniprot.org/annotation/VSP_034012 http://togogenome.org/gene/10090:Parp2 ^@ http://purl.uniprot.org/uniprot/O88554 ^@ 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|||Site|||Strand|||Turn ^@ Basic and acidic residues|||Cleavage; by caspase-8|||Decreased cleavages by caspase-8 (CASP8).|||Decreases levels of mono-ADP-ribosylation without loss of enzyme activity.|||Disordered|||For poly [ADP-ribose] polymerase activity|||N-terminal region (NTR)|||N6-(ADP-ribosyl)lysine; alternate|||N6-acetyllysine; alternate|||Nuclear localization signal|||PARP alpha-helical|||PARP catalytic|||Phosphoserine|||Poly [ADP-ribose] polymerase 2|||WGR ^@ http://purl.uniprot.org/annotation/PRO_0000211328 http://togogenome.org/gene/10090:Corin ^@ http://purl.uniprot.org/uniprot/Q9Z319 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Atrial natriuretic peptide-converting enzyme|||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|||Charge relay system|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||FZ 1|||FZ 2|||Helical; Signal-anchor for type II membrane protein|||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|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SRCR ^@ http://purl.uniprot.org/annotation/PRO_0000088674|||http://purl.uniprot.org/annotation/PRO_0000391767|||http://purl.uniprot.org/annotation/PRO_0000391768|||http://purl.uniprot.org/annotation/PRO_0000417987|||http://purl.uniprot.org/annotation/VSP_043953 http://togogenome.org/gene/10090:4930480E11Rik ^@ http://purl.uniprot.org/uniprot/Q0VG34|||http://purl.uniprot.org/uniprot/Q9D5A6 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered ^@ http://togogenome.org/gene/10090:Slc16a3 ^@ http://purl.uniprot.org/uniprot/P57787|||http://purl.uniprot.org/uniprot/Q3TMA0|||http://purl.uniprot.org/uniprot/Q3UDP9 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Basolateral sorting signal|||Cytoplasmic|||Extracellular|||Helical|||Major facilitator superfamily (MFS) profile|||Monocarboxylate transporter 4|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000211395 http://togogenome.org/gene/10090:Fut11 ^@ http://purl.uniprot.org/uniprot/B2RRR9|||http://purl.uniprot.org/uniprot/Q8BHC9 ^@ 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|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Alpha-(1,3)-fucosyltransferase|||Alpha-(1,3)-fucosyltransferase 11|||Cytoplasmic|||Fucosyltransferase N-terminal|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000299010|||http://purl.uniprot.org/annotation/PRO_5014298330 http://togogenome.org/gene/10090:Etfb ^@ http://purl.uniprot.org/uniprot/Q9DCW4 ^@ Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Electron transfer flavoprotein subunit beta|||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 ^@ http://purl.uniprot.org/annotation/PRO_0000167871 http://togogenome.org/gene/10090:Tgfbi ^@ http://purl.uniprot.org/uniprot/A1L353|||http://purl.uniprot.org/uniprot/P82198 ^@ Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Signal Peptide ^@ Cell attachment site|||EMI|||FAS1|||FAS1 1|||FAS1 2|||FAS1 3|||FAS1 4|||Phosphoserine|||S-cysteinyl cysteine|||Transforming growth factor-beta-induced protein ig-h3 ^@ http://purl.uniprot.org/annotation/PRO_0000041980|||http://purl.uniprot.org/annotation/PRO_5014296757 http://togogenome.org/gene/10090:Csrnp1 ^@ http://purl.uniprot.org/uniprot/P59054 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Cysteine/serine-rich nuclear protein 1|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000114787 http://togogenome.org/gene/10090:Dnah7b ^@ http://purl.uniprot.org/uniprot/A0A571BD48 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||EF-hand ^@ http://togogenome.org/gene/10090:Oxsm ^@ http://purl.uniprot.org/uniprot/Q9D404 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transit Peptide ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Transit Peptide ^@ 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial|||For beta-ketoacyl synthase activity|||Ketosynthase family 3 (KS3)|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000232661 http://togogenome.org/gene/10090:Limd1 ^@ http://purl.uniprot.org/uniprot/Q9QXD8 ^@ 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|||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_0000075802 http://togogenome.org/gene/10090:Tnfrsf11a ^@ http://purl.uniprot.org/uniprot/O35305 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||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_0000034586 http://togogenome.org/gene/10090:Nek6 ^@ http://purl.uniprot.org/uniprot/Q9ES70 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Autoinhibitory|||Disordered|||Interaction with APBB1|||Interaction with ARHGAP33, ANKRA2, CDC42, PRDX3, RAD26L, RBBP6, RPS7 and TRIP4|||Phosphoserine|||Phosphoserine; by NEK9|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek6 ^@ http://purl.uniprot.org/annotation/PRO_0000086428 http://togogenome.org/gene/10090:Map3k21 ^@ http://purl.uniprot.org/uniprot/Q8VDG6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||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_0000302761 http://togogenome.org/gene/10090:Atp10b ^@ http://purl.uniprot.org/uniprot/A0A571BEJ2|||http://purl.uniprot.org/uniprot/B1AWN4|||http://purl.uniprot.org/uniprot/Q5DU18 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane ^@ 4-aspartylphosphate intermediate|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Phospholipid-transporting ATPase VB|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000452096 http://togogenome.org/gene/10090:Cd40 ^@ http://purl.uniprot.org/uniprot/P27512 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform II.|||In isoform III.|||In isoform IV.|||In isoform V.|||N-linked (GlcNAc...) asparagine|||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_0000034560|||http://purl.uniprot.org/annotation/VSP_006474|||http://purl.uniprot.org/annotation/VSP_006475|||http://purl.uniprot.org/annotation/VSP_006476|||http://purl.uniprot.org/annotation/VSP_006477|||http://purl.uniprot.org/annotation/VSP_006478|||http://purl.uniprot.org/annotation/VSP_006479|||http://purl.uniprot.org/annotation/VSP_006480 http://togogenome.org/gene/10090:Gdf9 ^@ http://purl.uniprot.org/uniprot/Q07105|||http://purl.uniprot.org/uniprot/Q3UWR9|||http://purl.uniprot.org/uniprot/Q7TPZ4 ^@ 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|||Sequence Conflict|||Signal Peptide ^@ Growth/differentiation factor 9|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile ^@ http://purl.uniprot.org/annotation/PRO_0000033982|||http://purl.uniprot.org/annotation/PRO_0000033983|||http://purl.uniprot.org/annotation/PRO_5004291770|||http://purl.uniprot.org/annotation/PRO_5010843500 http://togogenome.org/gene/10090:Atf7ip ^@ http://purl.uniprot.org/uniprot/Q7TT18 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Acidic residues|||Activating transcription factor 7-interacting protein 1|||Basic and acidic residues|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||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_0000281781|||http://purl.uniprot.org/annotation/VSP_024040|||http://purl.uniprot.org/annotation/VSP_024041 http://togogenome.org/gene/10090:Garem1 ^@ http://purl.uniprot.org/uniprot/Q3UFT3 ^@ 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|||In isoform 2.|||Necessary for interaction with GRB2|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SAM ^@ http://purl.uniprot.org/annotation/PRO_0000277648|||http://purl.uniprot.org/annotation/VSP_023049|||http://purl.uniprot.org/annotation/VSP_023050 http://togogenome.org/gene/10090:Ttc8 ^@ http://purl.uniprot.org/uniprot/Q8VD72 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Splice Variant ^@ Disordered|||In isoform 2.|||Polar residues|||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_0000106389|||http://purl.uniprot.org/annotation/VSP_007825 http://togogenome.org/gene/10090:Hba-a1 ^@ http://purl.uniprot.org/uniprot/Q91VB8 ^@ Binding Site|||Domain Extent|||Region|||Site ^@ Binding Site|||Domain Extent ^@ Globin family profile|||distal binding residue|||proximal binding residue ^@ http://togogenome.org/gene/10090:Ccdc24 ^@ http://purl.uniprot.org/uniprot/Q3V0I8 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Mef2a ^@ http://purl.uniprot.org/uniprot/Q60929 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Beta domain|||Cleavage|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||In isoform 2 and isoform 3.|||In isoform 3.|||MADS-box|||Mef2-type|||Myocyte-specific enhancer factor 2A|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by MAPK7|||Phosphothreonine|||Phosphothreonine; by MAPK7|||Phosphothreonine; by NLK|||Polar residues|||Pro residues|||Required for interaction with MAPKs ^@ http://purl.uniprot.org/annotation/PRO_0000199429|||http://purl.uniprot.org/annotation/VSP_026031|||http://purl.uniprot.org/annotation/VSP_026060 http://togogenome.org/gene/10090:Tmem132b ^@ http://purl.uniprot.org/uniprot/F7BAB2 ^@ 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|||Transmembrane protein TMEM132 C-terminal|||Transmembrane protein TMEM132 N-terminal|||Transmembrane protein family 132 middle ^@ http://purl.uniprot.org/annotation/PRO_5003349212 http://togogenome.org/gene/10090:Ripk3 ^@ http://purl.uniprot.org/uniprot/E9PZP3|||http://purl.uniprot.org/uniprot/Q9QZL0 ^@ 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 ^@ Abolished protein kinase activity and ability to activate necroptosis. Knockin mice die during embryogenesis due to constitutive Ripk1- and Casp8-dependent apoptosis. Perinatal lethality observed in Ripk1 knockout mice is rescued in knockin mice carrying this mutation.|||Abolishes ability to mediate necroptosis.|||Abolishes ability to mediate necroptosis. Affects interaction with MLKL; when associated with A-230 and A-236.|||Abolishes kinase activity and ability to mediate necroptosis. No autophosphorylation.|||Complete loss of induced necrosis.|||Disordered|||In RIPK3(RHIM); abolished interaction with ZBP1 and subsequent necroptosis. Perinatal lethality observed in Ripk1 knockout mice is rescued in knockin mice carrying this mutation.|||No effect.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||RIP homotypic interaction motif (RHIM)|||Receptor-interacting serine/threonine-protein kinase 3|||Slightly affects interaction with MLKL; when associated with A-230. Affects interaction with MLKL; when associated with A-230 and A-232.|||Slightly affects interaction with MLKL; when associated with A-236. Affects interaction with MLKL; when associated with A-232 and A-236. ^@ http://purl.uniprot.org/annotation/PRO_0000086611 http://togogenome.org/gene/10090:Ppil4 ^@ http://purl.uniprot.org/uniprot/Q9CXG3 ^@ 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|||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_0000233053 http://togogenome.org/gene/10090:Dand5 ^@ http://purl.uniprot.org/uniprot/Q3UPN3|||http://purl.uniprot.org/uniprot/Q76LW6 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Signal Peptide ^@ CTCK|||DAN domain family member 5|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000311805 http://togogenome.org/gene/10090:Aggf1 ^@ http://purl.uniprot.org/uniprot/Q3V1B3|||http://purl.uniprot.org/uniprot/Q7TN31 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Angiogenic factor with G patch and FHA domains 1|||Basic and acidic residues|||Disordered|||FHA|||G-patch|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000064496 http://togogenome.org/gene/10090:Mrgprb8 ^@ http://purl.uniprot.org/uniprot/Q7TN51 ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||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|||Mas-related G-protein coupled receptor member B8|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000305303 http://togogenome.org/gene/10090:Mycbp ^@ http://purl.uniprot.org/uniprot/Q9EQS3 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ c-Myc-binding protein ^@ http://purl.uniprot.org/annotation/PRO_0000220981 http://togogenome.org/gene/10090:Atpif1 ^@ http://purl.uniprot.org/uniprot/O35143 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide ^@ Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Transit Peptide ^@ ATPase inhibitor, mitochondrial|||Antiparallel alpha-helical coiled coil region|||Disordered|||Mitochondrion|||N-terminal inhibitory region|||N6-succinyllysine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000002548 http://togogenome.org/gene/10090:Hoxa10 ^@ http://purl.uniprot.org/uniprot/P31310 ^@ 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_0000200091|||http://purl.uniprot.org/annotation/VSP_002386|||http://purl.uniprot.org/annotation/VSP_002387 http://togogenome.org/gene/10090:Acp2 ^@ http://purl.uniprot.org/uniprot/P24638|||http://purl.uniprot.org/uniprot/Q3UZN1 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Lysosomal acid phosphatase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000023961|||http://purl.uniprot.org/annotation/PRO_5004230413 http://togogenome.org/gene/10090:Ssu72 ^@ http://purl.uniprot.org/uniprot/Q9CY97 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant ^@ In isoform 2.|||RNA polymerase II subunit A C-terminal domain phosphatase SSU72 ^@ http://purl.uniprot.org/annotation/PRO_0000330013|||http://purl.uniprot.org/annotation/VSP_033006 http://togogenome.org/gene/10090:Enpp2 ^@ http://purl.uniprot.org/uniprot/G3UXY9|||http://purl.uniprot.org/uniprot/Q9R1E6 ^@ 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 Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn ^@ Basic residues|||Cell attachment site|||Complete inhibition of secretion.|||Disordered|||Ectonucleotide pyrophosphatase/phosphodiesterase family member 2|||Essential for catalytic activity|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||No catalytic activity.|||No effect on secretion nor lysophospholipase activity.|||No effect on secretion.|||No effect on secretion; greatly inhibits lysoPLD activity. Inhibits secretion. Almost complete loss of lysoPLD activity; when associated with N-53 del.|||No effect on secretion; slightly decreases lysophospholipase activity. Almost complete loss of lysophospholipase activity; when associated with N-410 del.|||No effect.|||Nuclease|||Nucleophile|||Phosphodiesterase|||Reduced lysophospholipase activity.|||Removed by furin|||Required for secretion|||SMB|||SMB 1|||SMB 2|||Strongly reduced catalytic activity. ^@ http://purl.uniprot.org/annotation/PRO_0000188568|||http://purl.uniprot.org/annotation/PRO_0000281650|||http://purl.uniprot.org/annotation/VSP_036396|||http://purl.uniprot.org/annotation/VSP_036397 http://togogenome.org/gene/10090:Pate2 ^@ http://purl.uniprot.org/uniprot/Q3UW31 ^@ 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_0000263608|||http://purl.uniprot.org/annotation/VSP_021874 http://togogenome.org/gene/10090:Zmiz2 ^@ http://purl.uniprot.org/uniprot/Q8CIE2 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Asymmetric dimethylarginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||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_0000218990|||http://purl.uniprot.org/annotation/VSP_012191|||http://purl.uniprot.org/annotation/VSP_024919 http://togogenome.org/gene/10090:Pdp2 ^@ http://purl.uniprot.org/uniprot/Q504M2 ^@ Domain Extent|||Region ^@ Domain Extent ^@ PPM-type phosphatase ^@ http://togogenome.org/gene/10090:Mogat2 ^@ http://purl.uniprot.org/uniprot/Q80W94 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ 2-acylglycerol O-acyltransferase 2|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000249063 http://togogenome.org/gene/10090:Fam216a ^@ http://purl.uniprot.org/uniprot/Q9DB54 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Protein FAM216A ^@ http://purl.uniprot.org/annotation/PRO_0000288862 http://togogenome.org/gene/10090:Klk7 ^@ http://purl.uniprot.org/uniprot/A0A0B6VPC4|||http://purl.uniprot.org/uniprot/Q91VE3 ^@ 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|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn ^@ Activation peptide|||Charge relay system|||Kallikrein-7|||Major binding site for inhibitory zinc or copper|||Peptidase S1|||Serine protease ^@ http://purl.uniprot.org/annotation/PRO_0000027944|||http://purl.uniprot.org/annotation/PRO_0000027945|||http://purl.uniprot.org/annotation/PRO_5014221783 http://togogenome.org/gene/10090:Or10a48 ^@ http://purl.uniprot.org/uniprot/Q8VFZ6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Or1e26 ^@ http://purl.uniprot.org/uniprot/Q8VGT1 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Arid3b ^@ http://purl.uniprot.org/uniprot/Q9Z1N7 ^@ 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 ^@ ARID|||AT-rich interactive domain-containing protein 3B|||Acidic residues|||Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with ARID3A|||Interaction with RB1|||N-acetylmethionine|||Phosphoserine|||Polar residues|||REKLES ^@ http://purl.uniprot.org/annotation/PRO_0000295163|||http://purl.uniprot.org/annotation/VSP_026775|||http://purl.uniprot.org/annotation/VSP_026776|||http://purl.uniprot.org/annotation/VSP_026777|||http://purl.uniprot.org/annotation/VSP_026778 http://togogenome.org/gene/10090:Kif20a ^@ http://purl.uniprot.org/uniprot/P97329 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region ^@ Disordered|||Globular|||Kinesin motor|||Kinesin-like protein KIF20A|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PLK1|||Phosphothreonine|||Polar residues|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000125461 http://togogenome.org/gene/10090:Rab19 ^@ http://purl.uniprot.org/uniprot/P35294 ^@ Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict ^@ Cysteine methyl ester|||Effector region|||Ras-related protein Rab-19|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000121201 http://togogenome.org/gene/10090:Lyg1 ^@ http://purl.uniprot.org/uniprot/Q0VE18|||http://purl.uniprot.org/uniprot/Q9D7Q0 ^@ Active Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Signal Peptide ^@ Lysozyme g-like protein|||Lysozyme g-like protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000012024|||http://purl.uniprot.org/annotation/PRO_5014306837 http://togogenome.org/gene/10090:Chn1 ^@ http://purl.uniprot.org/uniprot/A7VK12|||http://purl.uniprot.org/uniprot/A7VK13|||http://purl.uniprot.org/uniprot/A7VK14|||http://purl.uniprot.org/uniprot/Q91V57 ^@ Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N-chimaerin|||Phorbol-ester/DAG-type|||Phosphothreonine|||Removed|||Rho-GAP|||SH2 ^@ http://purl.uniprot.org/annotation/PRO_0000056695|||http://purl.uniprot.org/annotation/VSP_020145|||http://purl.uniprot.org/annotation/VSP_020146 http://togogenome.org/gene/10090:Slc25a24 ^@ http://purl.uniprot.org/uniprot/Q8BMD8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ 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|||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_0000317595 http://togogenome.org/gene/10090:Marchf7 ^@ http://purl.uniprot.org/uniprot/Q9WV66 ^@ 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 ^@ Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase MARCHF7|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-CH-type ^@ http://purl.uniprot.org/annotation/PRO_0000274416 http://togogenome.org/gene/10090:Vmn1r68 ^@ http://purl.uniprot.org/uniprot/E9Q0V3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Hmgcs2 ^@ http://purl.uniprot.org/uniprot/P54869 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Transit Peptide ^@ Abolishes enzymatic activity.|||Acyl-thioester intermediate|||Hydroxymethylglutaryl-CoA synthase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000013484 http://togogenome.org/gene/10090:Slc44a1 ^@ http://purl.uniprot.org/uniprot/A2AMH3|||http://purl.uniprot.org/uniprot/A2AMH4|||http://purl.uniprot.org/uniprot/Q6X893 ^@ Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Choline transporter-like protein 1|||Cytoplasmic|||Helical|||In isoform 2.|||Mitochondrial intermembrane|||N-myristoyl glycine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000191713|||http://purl.uniprot.org/annotation/VSP_015428 http://togogenome.org/gene/10090:Tmod4 ^@ http://purl.uniprot.org/uniprot/Q3UN19|||http://purl.uniprot.org/uniprot/Q9JLH8 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Tropomodulin-4 ^@ http://purl.uniprot.org/annotation/PRO_0000186137 http://togogenome.org/gene/10090:Rhpn2 ^@ http://purl.uniprot.org/uniprot/Q8BWR8 ^@ 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 ^@ BRO1|||Interaction with Rho|||PDZ|||Phosphothreonine|||REM-1|||Rhophilin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000218899 http://togogenome.org/gene/10090:Ddt ^@ http://purl.uniprot.org/uniprot/O35215 ^@ Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand ^@ Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand ^@ D-dopachrome decarboxylase|||N-acetylproline|||N6-acetyllysine|||Phosphoserine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000158071 http://togogenome.org/gene/10090:Brix1 ^@ http://purl.uniprot.org/uniprot/Q8CEX3|||http://purl.uniprot.org/uniprot/Q9DCA5 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic 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_0000120231 http://togogenome.org/gene/10090:Ubqln1 ^@ http://purl.uniprot.org/uniprot/Q3TN93|||http://purl.uniprot.org/uniprot/Q8R317 ^@ 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 ^@ Disordered|||In isoform 2.|||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_0000211009|||http://purl.uniprot.org/annotation/VSP_009788 http://togogenome.org/gene/10090:Rnf122 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0G8|||http://purl.uniprot.org/uniprot/Q8BP31 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Helical|||RING finger protein 122|||RING-type|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000247853 http://togogenome.org/gene/10090:Cmip ^@ http://purl.uniprot.org/uniprot/Q9D486 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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_0000317629|||http://purl.uniprot.org/annotation/VSP_031113|||http://purl.uniprot.org/annotation/VSP_031114 http://togogenome.org/gene/10090:Ncf1 ^@ http://purl.uniprot.org/uniprot/F8WH69|||http://purl.uniprot.org/uniprot/Q09014|||http://purl.uniprot.org/uniprot/Q3UBI5 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||Neutrophil cytosol factor 1|||PX|||Phosphoserine|||SH3|||SH3 1|||SH3 2 ^@ http://purl.uniprot.org/annotation/PRO_0000096763 http://togogenome.org/gene/10090:Clec2m ^@ http://purl.uniprot.org/uniprot/Q8C634 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Hectd1 ^@ http://purl.uniprot.org/uniprot/F8WIE5 ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Site ^@ Active Site|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ ANK|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||HECT|||MIB/HERC2|||Polar residues ^@ http://togogenome.org/gene/10090:Heg1 ^@ http://purl.uniprot.org/uniprot/A0A338P6D4|||http://purl.uniprot.org/uniprot/E9Q440|||http://purl.uniprot.org/uniprot/Q6DFX1 ^@ 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 ^@ Disordered|||EGF-like|||Helical|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003245674|||http://purl.uniprot.org/annotation/PRO_5016350034 http://togogenome.org/gene/10090:Ptprq ^@ http://purl.uniprot.org/uniprot/P0C5E4 ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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 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|||N-linked (GlcNAc...) asparagine|||Phosphatidylinositol phosphatase PTPRQ|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase ^@ http://purl.uniprot.org/annotation/PRO_0000302851 http://togogenome.org/gene/10090:Nbea ^@ http://purl.uniprot.org/uniprot/Q9EPN1 ^@ 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 ^@ BEACH|||BEACH-type PH|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Neurobeachin|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000051090|||http://purl.uniprot.org/annotation/VSP_050540|||http://purl.uniprot.org/annotation/VSP_050541|||http://purl.uniprot.org/annotation/VSP_050542 http://togogenome.org/gene/10090:1600014C10Rik ^@ http://purl.uniprot.org/uniprot/Q8WUR0 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Sequence Conflict|||Transmembrane ^@ Helical|||Protein C19orf12 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000296663 http://togogenome.org/gene/10090:Sigmar1 ^@ http://purl.uniprot.org/uniprot/A2AMS0|||http://purl.uniprot.org/uniprot/B7ZJH6|||http://purl.uniprot.org/uniprot/B7ZJH7|||http://purl.uniprot.org/uniprot/B7ZJH8|||http://purl.uniprot.org/uniprot/B7ZJH9|||http://purl.uniprot.org/uniprot/I4DCY6|||http://purl.uniprot.org/uniprot/O55242 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ C-terminal hydrophobic region|||Cytoplasmic|||Helical|||Important for ligand binding|||Important for ligand-binding|||In isoform 2.|||Lumenal|||Sigma non-opioid intracellular receptor 1|||Targeting to endoplasmic reticulum-associated lipid droplets ^@ http://purl.uniprot.org/annotation/PRO_0000268653|||http://purl.uniprot.org/annotation/VSP_021987 http://togogenome.org/gene/10090:Mrpl43 ^@ http://purl.uniprot.org/uniprot/Q5RL20 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Ribosomal protein/NADH dehydrogenase ^@ http://togogenome.org/gene/10090:Ripply3 ^@ http://purl.uniprot.org/uniprot/Q924S9 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Disordered|||Pro residues|||Protein ripply3|||Ripply homology domain|||WRPW motif ^@ http://purl.uniprot.org/annotation/PRO_0000307763 http://togogenome.org/gene/10090:Eif4enif1 ^@ http://purl.uniprot.org/uniprot/Q8BY82|||http://purl.uniprot.org/uniprot/Q9EST3 ^@ 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 ^@ Abolished interaction with EIF4E.|||Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 4E transporter|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||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|||YXXXXLphi motif ^@ http://purl.uniprot.org/annotation/PRO_0000064382|||http://purl.uniprot.org/annotation/VSP_003785 http://togogenome.org/gene/10090:Lcn10 ^@ http://purl.uniprot.org/uniprot/Q0VBF7|||http://purl.uniprot.org/uniprot/Q810Z1 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Signal Peptide ^@ Epididymal-specific lipocalin-10|||Lipocalin/cytosolic fatty-acid binding|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine ^@ http://purl.uniprot.org/annotation/PRO_0000017921|||http://purl.uniprot.org/annotation/PRO_5014306863 http://togogenome.org/gene/10090:Fez2 ^@ http://purl.uniprot.org/uniprot/A0A3Q4EGS7|||http://purl.uniprot.org/uniprot/D3Z6D5|||http://purl.uniprot.org/uniprot/Q3TN06|||http://purl.uniprot.org/uniprot/Q3U049|||http://purl.uniprot.org/uniprot/Q6TYB5 ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Disulfide Bond|||Modified Residue|||Region ^@ Disordered|||Fasciculation and elongation protein zeta-2|||Interchain|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000189529 http://togogenome.org/gene/10090:Nup50 ^@ http://purl.uniprot.org/uniprot/Q9JIH2 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Turn ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||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)|||N6-acetyllysine|||Nuclear pore complex protein Nup50|||Phosphoserine|||Phosphothreonine|||Polar residues|||RanBD1 ^@ http://purl.uniprot.org/annotation/PRO_0000204869 http://togogenome.org/gene/10090:Cd83 ^@ http://purl.uniprot.org/uniprot/O88324 ^@ 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 ^@ CD83 antigen|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000378451 http://togogenome.org/gene/10090:Riox1 ^@ http://purl.uniprot.org/uniprot/Q9JJF3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Abolished lysine demethylase activity; when associated with A-302.|||Abolished lysine demethylase activity; when associated with A-367.|||Basic and acidic residues|||Disordered|||JmjC|||N-acetylmethionine|||Phosphoserine|||Ribosomal oxygenase 1 ^@ http://purl.uniprot.org/annotation/PRO_0000264614 http://togogenome.org/gene/10090:Pcdh8 ^@ http://purl.uniprot.org/uniprot/Q7TSK3 ^@ 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 ^@ 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|||Phosphoserine|||Protocadherin-8 ^@ http://purl.uniprot.org/annotation/PRO_0000404296|||http://purl.uniprot.org/annotation/VSP_040562|||http://purl.uniprot.org/annotation/VSP_040563|||http://purl.uniprot.org/annotation/VSP_040564 http://togogenome.org/gene/10090:Chst7 ^@ http://purl.uniprot.org/uniprot/Q9EP78 ^@ 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_0000085199 http://togogenome.org/gene/10090:Lce1k ^@ http://purl.uniprot.org/uniprot/J3QP15 ^@ Region ^@ Region ^@ Disordered ^@ http://togogenome.org/gene/10090:Frmd4a ^@ http://purl.uniprot.org/uniprot/H3BIZ7|||http://purl.uniprot.org/uniprot/Q3TB04|||http://purl.uniprot.org/uniprot/Q8BIE6 ^@ 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|||Cytohesin Ubiquitin Protein Inducing|||Disordered|||FERM|||FERM domain-containing protein 4A|||In isoform 2.|||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_0000219445|||http://purl.uniprot.org/annotation/VSP_019592|||http://purl.uniprot.org/annotation/VSP_035378 http://togogenome.org/gene/10090:Or10k2 ^@ http://purl.uniprot.org/uniprot/E9Q848 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Slc16a1 ^@ http://purl.uniprot.org/uniprot/P53986|||http://purl.uniprot.org/uniprot/Q544N9 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Basic and acidic 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|||Major facilitator superfamily (MFS) profile|||Monocarboxylate transporter 1|||Phosphoserine|||Phosphothreonine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000211383 http://togogenome.org/gene/10090:Clptm1 ^@ http://purl.uniprot.org/uniprot/Q8VBZ3 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Putative lipid scramblase CLPTM1|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000245097 http://togogenome.org/gene/10090:Prkaa1 ^@ http://purl.uniprot.org/uniprot/Q3TUQ7|||http://purl.uniprot.org/uniprot/Q5EG47|||http://purl.uniprot.org/uniprot/Q8BUX6 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ 5'-AMP-activated protein kinase catalytic subunit alpha-1|||AIS|||AMPK C-terminal adenylate sensor|||Disordered|||Loss of kinase activity.|||Phosphoserine|||Phosphoserine; by ULK1|||Phosphothreonine|||Phosphothreonine; by LKB1 and CaMKK2|||Phosphothreonine; by ULK1|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000085590 http://togogenome.org/gene/10090:Prl3b1 ^@ http://purl.uniprot.org/uniprot/P09586|||http://purl.uniprot.org/uniprot/Q5SZY3 ^@ Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ Prolactin-3B1 ^@ http://purl.uniprot.org/annotation/PRO_0000032961|||http://purl.uniprot.org/annotation/PRO_5015098025 http://togogenome.org/gene/10090:Trpc5os ^@ http://purl.uniprot.org/uniprot/Q3UHV4 ^@ Chain|||Molecule Processing|||Region ^@ Chain|||Region ^@ Disordered|||Putative uncharacterized protein TRPC5OS homolog ^@ http://purl.uniprot.org/annotation/PRO_0000349179 http://togogenome.org/gene/10090:Mier1 ^@ http://purl.uniprot.org/uniprot/Q32P49|||http://purl.uniprot.org/uniprot/Q5UAK0|||http://purl.uniprot.org/uniprot/Q8C929 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||ELM2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Mesoderm induction early response protein 1|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SANT ^@ http://purl.uniprot.org/annotation/PRO_0000197142|||http://purl.uniprot.org/annotation/VSP_016174|||http://purl.uniprot.org/annotation/VSP_016175|||http://purl.uniprot.org/annotation/VSP_016177|||http://purl.uniprot.org/annotation/VSP_042454 http://togogenome.org/gene/10090:Tmem41b ^@ http://purl.uniprot.org/uniprot/Q8K1A5 ^@ 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.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Transmembrane protein 41B|||VTT domain; required for its function in autophagy ^@ http://purl.uniprot.org/annotation/PRO_0000291938|||http://purl.uniprot.org/annotation/VSP_026318|||http://purl.uniprot.org/annotation/VSP_026319 http://togogenome.org/gene/10090:Or8b3 ^@ http://purl.uniprot.org/uniprot/Q60886 ^@ 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|||Olfactory receptor 8B3 ^@ http://purl.uniprot.org/annotation/PRO_0000150824 http://togogenome.org/gene/10090:Wdr17 ^@ http://purl.uniprot.org/uniprot/G3UVU7|||http://purl.uniprot.org/uniprot/Q8C8Y2|||http://purl.uniprot.org/uniprot/Q8CFX0 ^@ Region|||Repeat ^@ Repeat ^@ WD ^@ http://togogenome.org/gene/10090:Cstdc5 ^@ http://purl.uniprot.org/uniprot/Q497J0 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Cystatin ^@ http://togogenome.org/gene/10090:Aga ^@ http://purl.uniprot.org/uniprot/A2RSS6|||http://purl.uniprot.org/uniprot/B7ZNK6|||http://purl.uniprot.org/uniprot/Q64191 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide|||Site ^@ Cleavage; by autolysis|||Glycosylasparaginase alpha chain|||Glycosylasparaginase beta chain|||N-linked (GlcNAc...) asparagine|||Nucleophile ^@ http://purl.uniprot.org/annotation/PRO_0000002335|||http://purl.uniprot.org/annotation/PRO_0000002336|||http://purl.uniprot.org/annotation/PRO_5014296835|||http://purl.uniprot.org/annotation/PRO_5015087443 http://togogenome.org/gene/10090:Wdr75 ^@ http://purl.uniprot.org/uniprot/Q3U821 ^@ 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|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphotyrosine|||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_0000435727 http://togogenome.org/gene/10090:Gtf2a1l ^@ http://purl.uniprot.org/uniprot/Q8R4I4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict ^@ Disordered|||Polar residues|||TFIIA-alpha and beta-like factor ^@ http://purl.uniprot.org/annotation/PRO_0000072496 http://togogenome.org/gene/10090:Mllt1 ^@ http://purl.uniprot.org/uniprot/Q9ERL0 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ AF-9 ANC1 homology|||Basic and acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Fpr2 ^@ http://purl.uniprot.org/uniprot/O88536 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Formyl peptide receptor 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|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000382022 http://togogenome.org/gene/10090:Slc6a19 ^@ http://purl.uniprot.org/uniprot/Q3KN89|||http://purl.uniprot.org/uniprot/Q9D687 ^@ Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Modified Residue|||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|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium-dependent neutral amino acid transporter B(0)AT1 ^@ http://purl.uniprot.org/annotation/PRO_0000214810 http://togogenome.org/gene/10090:Hmx2 ^@ http://purl.uniprot.org/uniprot/P43687 ^@ Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||DNA Binding|||Region|||Sequence Conflict ^@ Disordered|||Homeobox|||Homeobox protein HMX2 ^@ http://purl.uniprot.org/annotation/PRO_0000048950 http://togogenome.org/gene/10090:Or14j5 ^@ http://purl.uniprot.org/uniprot/Q8VGF0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Lcmt1 ^@ http://purl.uniprot.org/uniprot/A2RTH5 ^@ Binding Site|||Compositionally Biased Region|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:S100a13 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQ90|||http://purl.uniprot.org/uniprot/P97352|||http://purl.uniprot.org/uniprot/Q545H7 ^@ 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|||S100/CaBP-9k-type calcium binding subdomain ^@ http://purl.uniprot.org/annotation/PRO_0000144020 http://togogenome.org/gene/10090:Nol9 ^@ http://purl.uniprot.org/uniprot/Q3TZX8 ^@ 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 ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Polynucleotide 5'-hydroxyl-kinase NOL9|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000367432|||http://purl.uniprot.org/annotation/VSP_053056|||http://purl.uniprot.org/annotation/VSP_053057|||http://purl.uniprot.org/annotation/VSP_053058|||http://purl.uniprot.org/annotation/VSP_053059 http://togogenome.org/gene/10090:Ido1 ^@ http://purl.uniprot.org/uniprot/D3YXV1|||http://purl.uniprot.org/uniprot/P28776 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Indoleamine 2,3-dioxygenase 1|||Polar residues|||proximal binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000215205 http://togogenome.org/gene/10090:Smpd4 ^@ http://purl.uniprot.org/uniprot/Q6ZPR5 ^@ 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, isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Sphingomyelin phosphodiesterase 4 ^@ http://purl.uniprot.org/annotation/PRO_0000273164|||http://purl.uniprot.org/annotation/VSP_022484|||http://purl.uniprot.org/annotation/VSP_022485|||http://purl.uniprot.org/annotation/VSP_022486|||http://purl.uniprot.org/annotation/VSP_022487 http://togogenome.org/gene/10090:Syvn1 ^@ http://purl.uniprot.org/uniprot/A0A0R4J1R1|||http://purl.uniprot.org/uniprot/Q9DBY1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger ^@ 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.|||Interaction with SEL1L|||Interaction with p53/TP53|||Involved in FAM8A1 interaction|||Lumenal|||Phosphoserine|||Polar residues|||Pro residues|||RING-type|||RING-type; atypical ^@ http://purl.uniprot.org/annotation/PRO_0000280549|||http://purl.uniprot.org/annotation/VSP_023779|||http://purl.uniprot.org/annotation/VSP_023780|||http://purl.uniprot.org/annotation/VSP_023781|||http://purl.uniprot.org/annotation/VSP_023782|||http://purl.uniprot.org/annotation/VSP_023783 http://togogenome.org/gene/10090:Paqr4 ^@ http://purl.uniprot.org/uniprot/Q9JJE4 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Progestin and adipoQ receptor family member 4 ^@ http://purl.uniprot.org/annotation/PRO_0000218849 http://togogenome.org/gene/10090:Tmem74 ^@ http://purl.uniprot.org/uniprot/Q8BQU7 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Transmembrane protein 74 ^@ http://purl.uniprot.org/annotation/PRO_0000259601 http://togogenome.org/gene/10090:Akr1e1 ^@ http://purl.uniprot.org/uniprot/Q9DCT1 ^@ Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Sequence Conflict|||Site ^@ 1,5-anhydro-D-fructose reductase|||Lowers pKa of active site Tyr|||Proton donor ^@ http://purl.uniprot.org/annotation/PRO_0000124673 http://togogenome.org/gene/10090:Abcc3 ^@ http://purl.uniprot.org/uniprot/A0A0R4J015|||http://purl.uniprot.org/uniprot/B2RX12 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 3|||Cytoplasmic|||Disordered|||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.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000356238|||http://purl.uniprot.org/annotation/VSP_036011|||http://purl.uniprot.org/annotation/VSP_036012 http://togogenome.org/gene/10090:Gabrb3 ^@ http://purl.uniprot.org/uniprot/P63080|||http://purl.uniprot.org/uniprot/Q8C446 ^@ 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|||Gamma-aminobutyric acid receptor subunit beta-3|||Helical|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane ^@ http://purl.uniprot.org/annotation/PRO_0000000463|||http://purl.uniprot.org/annotation/PRO_5015099071 http://togogenome.org/gene/10090:Pxk ^@ http://purl.uniprot.org/uniprot/Q8BX57 ^@ 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.|||PX|||PX domain-containing protein kinase-like protein|||Polar residues|||Pro residues|||Protein kinase|||WH2 ^@ http://purl.uniprot.org/annotation/PRO_0000086593|||http://purl.uniprot.org/annotation/VSP_051914|||http://purl.uniprot.org/annotation/VSP_051915|||http://purl.uniprot.org/annotation/VSP_051916|||http://purl.uniprot.org/annotation/VSP_051917 http://togogenome.org/gene/10090:Mtmr4 ^@ http://purl.uniprot.org/uniprot/Q91XS1 ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger ^@ Disordered|||FYVE-type|||In isoform 2.|||Myotubularin phosphatase|||Myotubularin-related protein 4|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000304810|||http://purl.uniprot.org/annotation/VSP_028126 http://togogenome.org/gene/10090:Shkbp1 ^@ http://purl.uniprot.org/uniprot/Q6P7W2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ BTB|||Disordered|||In isoform 2.|||N-acetylalanine|||No loss of interaction with SH3KBP1, loss of translocation of SH3KBP1 to EGFR containing vesicles upon EGF stimulation, slight delay in the degradation of EGFR upon EGF activation and enhancement of EGFR signaling induced serum response element (SRE) transcriptional reporter activity. Loss of interaction with SH3KBP1, no loss of translocation of SH3KBP1 to EGFR containing vesicles upon EGF stimulation, no effect on the degradation of EGFR upon EGF activation and no effect on EGFR signaling induced serum response element (SRE) transcriptional reporter activity; when associated with A-623.|||No loss of interaction with SH3KBP1, loss of translocation of SH3KBP1 to EGFR containing vesicles upon EGF stimulation, strong delay in the degradation of EGFR upon EGF activation and enhancement of EGFR signaling induced serum response element (SRE) transcriptional reporter activity. Loss of interaction with SH3KBP1, no loss of translocation of SH3KBP1 to EGFR containing vesicles upon EGF stimulation, no effect on the degradation of EGFR upon EGF activation and no effect on EGFR signaling induced serum response element (SRE) transcriptional reporter activity; when associated with A-683.|||PXXXPR|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||SH3KBP1-binding protein 1|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5 ^@ http://purl.uniprot.org/annotation/PRO_0000307933|||http://purl.uniprot.org/annotation/VSP_028875|||http://purl.uniprot.org/annotation/VSP_028876 http://togogenome.org/gene/10090:Slc10a6 ^@ http://purl.uniprot.org/uniprot/Q9CXB2 ^@ 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|||Sodium-dependent organic anion transporter ^@ http://purl.uniprot.org/annotation/PRO_0000309216 http://togogenome.org/gene/10090:Lrrc58 ^@ http://purl.uniprot.org/uniprot/Q3UGP9 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000312018 http://togogenome.org/gene/10090:Gins1 ^@ http://purl.uniprot.org/uniprot/Q9CZ15 ^@ Chain|||Molecule Processing ^@ Chain ^@ DNA replication complex GINS protein PSF1 ^@ http://purl.uniprot.org/annotation/PRO_0000219036 http://togogenome.org/gene/10090:Rasa4 ^@ http://purl.uniprot.org/uniprot/Q6PFQ7 ^@ 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 ^@ Btk-type|||C2 1|||C2 2|||In isoform 2.|||PH|||Ras GTPase-activating protein 4|||Ras-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000323606|||http://purl.uniprot.org/annotation/VSP_032042 http://togogenome.org/gene/10090:Or4a80 ^@ http://purl.uniprot.org/uniprot/A2AUA2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:S100a7l2 ^@ http://purl.uniprot.org/uniprot/G3UWB8 ^@ Domain Extent|||Region ^@ Domain Extent ^@ S100/CaBP-9k-type calcium binding subdomain ^@ http://togogenome.org/gene/10090:Ufsp2 ^@ http://purl.uniprot.org/uniprot/Q99K23 ^@ Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Turn ^@ Active Site|||Chain|||Helix|||Mutagenesis Site|||Strand|||Turn ^@ Loss of enzyme activity.|||No effect on enzyme activity.|||Reduced enzyme activity.|||Ufm1-specific protease 2 ^@ http://purl.uniprot.org/annotation/PRO_0000280363 http://togogenome.org/gene/10090:Odad4 ^@ http://purl.uniprot.org/uniprot/Q9D4B2 ^@ 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|||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_0000284508 http://togogenome.org/gene/10090:Ramac ^@ http://purl.uniprot.org/uniprot/Q9CQY2 ^@ 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 ^@ Disordered|||Interaction with RNMT|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RNA guanine-N7 methyltransferase activating subunit|||RNA-binding|||RNMT-activating domain ^@ http://purl.uniprot.org/annotation/PRO_0000089984 http://togogenome.org/gene/10090:Ceacam20 ^@ http://purl.uniprot.org/uniprot/Q9D2Z1 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Abolishes tyrosine phosphorylation and interaction with SYK; when associated with F-559.|||Abolishes tyrosine phosphorylation and interaction with SYK; when associated with F-570.|||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|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5007716426 http://togogenome.org/gene/10090:Fam163b ^@ http://purl.uniprot.org/uniprot/B2RVN8|||http://purl.uniprot.org/uniprot/Q8BUM6 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Transmembrane ^@ Helical|||Phosphoserine|||Protein FAM163B ^@ http://purl.uniprot.org/annotation/PRO_0000280259 http://togogenome.org/gene/10090:Sdc1 ^@ http://purl.uniprot.org/uniprot/P18828|||http://purl.uniprot.org/uniprot/Q3V1F2 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neurexin/syndecan/glycophorin C|||O-linked (Xyl...) (chondroitin sulfate) serine|||O-linked (Xyl...) (heparan sulfate) serine|||Phosphoserine|||Polar residues|||Syndecan|||Syndecan-1 ^@ http://purl.uniprot.org/annotation/PRO_0000033501|||http://purl.uniprot.org/annotation/PRO_5014309254|||http://purl.uniprot.org/annotation/VSP_007542 http://togogenome.org/gene/10090:Ubr4 ^@ http://purl.uniprot.org/uniprot/A2AN08 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger ^@ Acidic residues|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase UBR4|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||UBR-type ^@ http://purl.uniprot.org/annotation/PRO_0000286862|||http://purl.uniprot.org/annotation/VSP_025210|||http://purl.uniprot.org/annotation/VSP_025211|||http://purl.uniprot.org/annotation/VSP_025212|||http://purl.uniprot.org/annotation/VSP_025213|||http://purl.uniprot.org/annotation/VSP_025214|||http://purl.uniprot.org/annotation/VSP_025215 http://togogenome.org/gene/10090:Ces2e ^@ http://purl.uniprot.org/uniprot/Q8BK48 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Acyl-ester intermediate|||Charge relay system|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pyrethroid hydrolase Ces2e|||Pyrrolidone carboxylic acid ^@ http://purl.uniprot.org/annotation/PRO_0000424211 http://togogenome.org/gene/10090:Cacng6 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQD3|||http://purl.uniprot.org/uniprot/Q14C42|||http://purl.uniprot.org/uniprot/Q8VHW3 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Voltage-dependent calcium channel gamma-6 subunit ^@ http://purl.uniprot.org/annotation/PRO_0000164685 http://togogenome.org/gene/10090:Zmat3 ^@ http://purl.uniprot.org/uniprot/B9EI21 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||U1-type ^@ http://togogenome.org/gene/10090:Oosp2 ^@ http://purl.uniprot.org/uniprot/Q4FZG8 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Oocyte-secreted protein 2 ^@ http://purl.uniprot.org/annotation/PRO_0000251151 http://togogenome.org/gene/10090:Dbnl ^@ http://purl.uniprot.org/uniprot/Q62418 ^@ 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 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ ADF-H|||Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||Drebrin-like protein|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Reduces phosphorylation. Abolishes phosphorylation; when associated with F-350.|||Reduces phosphorylation. Impairs podosome rosette formation. Abolishes phosphorylation; when associated with F-340.|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000079794|||http://purl.uniprot.org/annotation/VSP_050789|||http://purl.uniprot.org/annotation/VSP_050790 http://togogenome.org/gene/10090:Itih4 ^@ http://purl.uniprot.org/uniprot/A0A2K6EDJ7|||http://purl.uniprot.org/uniprot/A6X935|||http://purl.uniprot.org/uniprot/E9PVD2|||http://purl.uniprot.org/uniprot/E9Q5L2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||Inter alpha-trypsin inhibitor, heavy chain 4|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Pro residues|||VIT|||VWFA ^@ http://purl.uniprot.org/annotation/PRO_0000420864|||http://purl.uniprot.org/annotation/PRO_5003245390|||http://purl.uniprot.org/annotation/PRO_5003245752|||http://purl.uniprot.org/annotation/PRO_5014424557|||http://purl.uniprot.org/annotation/VSP_044763 http://togogenome.org/gene/10090:Cdk9 ^@ http://purl.uniprot.org/uniprot/Q99J95 ^@ 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 ^@ Cyclin-dependent kinase 9|||Disordered|||In isoform 2.|||In isoform 3.|||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; by CDK9|||Phosphothreonine; by CaMK1D|||Polar residues|||Protein kinase|||Proton acceptor|||T-loop ^@ http://purl.uniprot.org/annotation/PRO_0000085801|||http://purl.uniprot.org/annotation/VSP_016289|||http://purl.uniprot.org/annotation/VSP_016290 http://togogenome.org/gene/10090:Kcne1l ^@ http://purl.uniprot.org/uniprot/Q9QZ26 ^@ Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||N-linked (GlcNAc...) asparagine|||Potassium voltage-gated channel subfamily E regulatory beta subunit 5 ^@ http://purl.uniprot.org/annotation/PRO_0000144295 http://togogenome.org/gene/10090:Ahr ^@ http://purl.uniprot.org/uniprot/P30561|||http://purl.uniprot.org/uniprot/Q3U5D9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn ^@ Aryl hydrocarbon receptor|||BHLH|||Completely abolished the AHR induction activity, the ligand-induced nuclear translocation of AHR, and drastically reduced DRE-binding in vitro.|||DNA-binding|||Disordered|||Drastically reduces the AHR transcription activity induction. Increases constitutive AHR nuclear translocation in the absence of ligands. Reduces binding affinity for the DRE by more than 30-fold in vitro.|||Drastically reduces the binding affinity of AHR?ARNT to dioxin response element (DRE). Impairs ligand-induced nuclear translocation of AHR.|||Highly disrupts the dimerization ability of AHR.|||Highly disrupts the dimerization ability of AHR. Reduces the AHR transcription factor activity induction by 50%.|||Highly disrupts the dimerization ability of AHR. Reduces transcription activity. Decreases interaction with ARNT.|||Highly disrupts the dimerization ability of AHR. Reduces transcription activity. Impairs interaction with ARNT.|||In allele AHRB1 and allele AHRD.|||In allele AHRB1 and allele AHRD; no reduction in specific ligand binding.|||In allele AHRB1.|||In allele AHRB1; no increase in specific ligand binding.|||In allele AHRB3.|||In allele AHRD.|||In allele AHRD; reduced specific ligand binding.|||Nuclear export signal|||Nuclear localization signal 1|||Nuclear localization signal 2|||PAC|||PAS|||PAS 1|||PAS 2|||Polar residues|||Reduces the AHR induction activity by ~50%. Translocates to the nucleus at a high level.|||Reduces the AHR induction transcription activity by 50%. Increases ligand-induced nuclear translocation of AHR.|||Reduces the binding affinity of AHR?ARNT to the DRE by more than 10-fold.|||Reduces transcription activity. Decreases interaction with ARNT.|||Reduces transcription activity. Impairs interaction with ARNT.|||Required for maintaining the overall integrity of the AHR:ARNT heterodimer and its transcriptional activity|||Significantly reduces binding affinities of the AHR:ARNT heterodimer to DRE.|||Significantly reduces binding affinities of the AHR?ARNT heterodimer to DRE.|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000013452|||http://purl.uniprot.org/annotation/PRO_0000013453 http://togogenome.org/gene/10090:Sp4 ^@ http://purl.uniprot.org/uniprot/A0A1Y7VJR5|||http://purl.uniprot.org/uniprot/K4DI62|||http://purl.uniprot.org/uniprot/Q6DFV2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Pigf ^@ http://purl.uniprot.org/uniprot/O09101 ^@ Chain|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Transmembrane ^@ Helical|||Phosphatidylinositol-glycan biosynthesis class F protein ^@ http://purl.uniprot.org/annotation/PRO_0000191760 http://togogenome.org/gene/10090:Prss43 ^@ http://purl.uniprot.org/uniprot/Q76HL1 ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Basic and acidic residues|||Charge relay system|||Disordered|||Helical|||Peptidase S1|||Polar residues|||Serine protease 43 ^@ http://purl.uniprot.org/annotation/PRO_5015098640 http://togogenome.org/gene/10090:Lrrc9 ^@ http://purl.uniprot.org/uniprot/E9PUL2|||http://purl.uniprot.org/uniprot/Q8CDN9 ^@ Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 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 28|||LRR 29|||LRR 3|||LRR 30|||LRR 31|||LRR 32|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 9|||Phosphotyrosine|||U2A'/phosphoprotein 32 family A C-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000337677|||http://purl.uniprot.org/annotation/VSP_033992|||http://purl.uniprot.org/annotation/VSP_033993 http://togogenome.org/gene/10090:Or4c101 ^@ http://purl.uniprot.org/uniprot/A2AV10 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Crisp1 ^@ http://purl.uniprot.org/uniprot/Q03401|||http://purl.uniprot.org/uniprot/Q545H0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Cysteine-rich secretory protein 1|||N-linked (GlcNAc...) asparagine|||SCP|||ShKT|||ShKT domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000006262|||http://purl.uniprot.org/annotation/PRO_5010844029 http://togogenome.org/gene/10090:Ank2 ^@ http://purl.uniprot.org/uniprot/Q8C8R3|||http://purl.uniprot.org/uniprot/S4R2R5 ^@ 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 ^@ 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 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Acidic residues|||Ankyrin-2|||Basic and acidic residues|||Death|||Death 1|||Death 2|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 7.|||In isoform 8.|||Interaction with SPTBN1|||Loss of binding to phosphatidylinositol 3-phosphate (PI3P) lipids and loss of localization to PI3P-positive organelles. Expression of mutant protein does not rescue ITGB1 recycling deficit of ANK2 null mutant fibroblasts.|||Loss of interaction with RABGAP1L. Localizes on motile vesicles, but does not cotransport with RABGAP1L. Loss of polarized transport of PI3P-positive organelles to the leading edge of the migrating fibroblasts. Expression of mutant protein does not rescue ITGB1 recycling deficit of ANK2 null mutant fibroblasts nor the impaired haptotactic response of the fibroblasts.|||Loss of long-range transport of PI3P-positive organelles in embryonic fibroblasts. Expression of mutant protein in ANK2 null mutant fibroblasts partially rescues ITGB1 recycling to about 50% of the wild-type levels.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Significantly weaker interaction with RABGAP1L.|||UPA domain|||ZU5|||ZU5 1|||ZU5 2 ^@ http://purl.uniprot.org/annotation/PRO_0000364087|||http://purl.uniprot.org/annotation/VSP_053010|||http://purl.uniprot.org/annotation/VSP_053011|||http://purl.uniprot.org/annotation/VSP_053012|||http://purl.uniprot.org/annotation/VSP_053013|||http://purl.uniprot.org/annotation/VSP_053014|||http://purl.uniprot.org/annotation/VSP_053015|||http://purl.uniprot.org/annotation/VSP_053016|||http://purl.uniprot.org/annotation/VSP_053017|||http://purl.uniprot.org/annotation/VSP_053018|||http://purl.uniprot.org/annotation/VSP_053019|||http://purl.uniprot.org/annotation/VSP_053020|||http://purl.uniprot.org/annotation/VSP_053021|||http://purl.uniprot.org/annotation/VSP_053023|||http://purl.uniprot.org/annotation/VSP_053025|||http://purl.uniprot.org/annotation/VSP_053027|||http://purl.uniprot.org/annotation/VSP_053029 http://togogenome.org/gene/10090:Kcnk3 ^@ http://purl.uniprot.org/uniprot/O35111 ^@ Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Glycosylation Site|||INTRAMEM|||Sequence Conflict|||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 3 ^@ http://purl.uniprot.org/annotation/PRO_0000101745 http://togogenome.org/gene/10090:Tet1 ^@ http://purl.uniprot.org/uniprot/Q3URK3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||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|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||CXXC-type|||Decreased levels of ubiquitination in isoform 2; loss of isoform 2 localization to sites of ongoing DNA replication in heterochromatic regions; does not affect interaction with CRL4(VprBP) ubiquitin ligase complex.|||Decreased levels of ubiquitination in isoform 2; loss of isoform 2 localization to sites of ongoing DNA replication in heterochromatic regions; does not affect interaction with CRL4(VprBP) ubiquitin ligase complex. Loss of DNA-binding and of 5-methylcytosine demethylase activity in vivo. Does not affect nuclear localization.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Interaction with DNA|||Loss of catalytic activity; when associated with A-1654. Does not affect chromocenter clustering; when associated with A-1654. Does not affect interaction with DCAF1; when associated with A-1654. In isoform 2, does not affect localization to heterochromatin in late S-phase; when associated with A-1654.|||Loss of catalytic activity; when associated with Y-1652. Does not affect chromocenter clustering; when associated with A-1654; when associated with Y-1652. Does not affect interaction with DCAF1; when associated with Y-1652. In isoform 2, does not affect localization to heterochromatin in late S-phase; when associated with Y-1652.|||Methylcytosine dioxygenase TET1|||Phosphoserine|||Polar residues|||Strongly reduces ubiquitination, loss of DNA-binding and of 5-methylcytosine demethylase activity in vivo. Does not affect nuclear localization.|||Sufficient for binding to genomic CpG islands ^@ http://purl.uniprot.org/annotation/PRO_0000377549|||http://purl.uniprot.org/annotation/VSP_061830 http://togogenome.org/gene/10090:BC048562 ^@ http://purl.uniprot.org/uniprot/Q80ZQ7 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Domain of unknown function with conserved HDNR motif ^@ http://togogenome.org/gene/10090:Tlr12 ^@ http://purl.uniprot.org/uniprot/A2RRZ9|||http://purl.uniprot.org/uniprot/Q6QNU9 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Fails to activate NF-kappa-B.|||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|||TIR|||Toll-like receptor 12 ^@ http://purl.uniprot.org/annotation/PRO_0000042794|||http://purl.uniprot.org/annotation/PRO_5009946340 http://togogenome.org/gene/10090:Zfp341 ^@ http://purl.uniprot.org/uniprot/Q6PGC9 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||Polar residues|||Pro residues ^@ http://togogenome.org/gene/10090:Npvf ^@ http://purl.uniprot.org/uniprot/Q3UUP8|||http://purl.uniprot.org/uniprot/Q9ESQ8 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Neuropeptide NPSF|||Neuropeptide NPVF|||Neuropeptide RFRP-1|||Phenylalanine amide|||Pro-FMRFamide-related neuropeptide VF ^@ http://purl.uniprot.org/annotation/PRO_0000009927|||http://purl.uniprot.org/annotation/PRO_0000009928|||http://purl.uniprot.org/annotation/PRO_0000009929|||http://purl.uniprot.org/annotation/PRO_0000009930|||http://purl.uniprot.org/annotation/PRO_0000009931|||http://purl.uniprot.org/annotation/PRO_0000401485|||http://purl.uniprot.org/annotation/PRO_5014309190|||http://purl.uniprot.org/annotation/VSP_039963 http://togogenome.org/gene/10090:Ift70a2 ^@ http://purl.uniprot.org/uniprot/A2AKQ8 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Region|||Repeat ^@ Chain|||Coiled-Coil|||Repeat ^@ Intraflagellar transport protein 70A2|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8 ^@ http://purl.uniprot.org/annotation/PRO_0000333203 http://togogenome.org/gene/10090:Tas2r139 ^@ http://purl.uniprot.org/uniprot/Q7TQA5 ^@ 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 39 ^@ http://purl.uniprot.org/annotation/PRO_0000082286 http://togogenome.org/gene/10090:Grm3 ^@ http://purl.uniprot.org/uniprot/Q9QYS2 ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||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|||Metabotropic glutamate receptor 3|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000012928 http://togogenome.org/gene/10090:Vmn1r37 ^@ http://purl.uniprot.org/uniprot/Q8R2E4 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Sema4c ^@ http://purl.uniprot.org/uniprot/Q64151 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Cytoplasmic|||Disordered|||Dominant negative effect on myogenic differentiation|||Extracellular|||Helical|||Ig-like C2-type|||Loss of interaction with DLG4; when associated with A-832 and A-834.|||Loss of the effect on myogenic differentiation; when associated with A-832. Loss of interaction with DLG4; when associated with A-832 and A-833.|||Loss of the effect on myogenic differentiation; when associated with A-834. Loss of interaction with DLG4; when associated with A-833 and A-834.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||PSI|||Phosphoserine|||Pro residues|||Sema|||Semaphorin-4C ^@ http://purl.uniprot.org/annotation/PRO_0000032326 http://togogenome.org/gene/10090:Scgb1a1 ^@ http://purl.uniprot.org/uniprot/Q06318|||http://purl.uniprot.org/uniprot/Q3UKV9 ^@ Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Signal Peptide ^@ Interchain (with C-24)|||Interchain (with C-90)|||Uteroglobin ^@ http://purl.uniprot.org/annotation/PRO_0000036366|||http://purl.uniprot.org/annotation/PRO_5014309145 http://togogenome.org/gene/10090:Zfp641 ^@ http://purl.uniprot.org/uniprot/Q8BZ34 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger ^@ Chain|||Domain Extent|||Modified Residue|||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|||Phosphoserine|||Transactivation|||Zinc finger protein 641 ^@ http://purl.uniprot.org/annotation/PRO_0000285302|||http://purl.uniprot.org/annotation/VSP_024869 http://togogenome.org/gene/10090:H2ac19 ^@ http://purl.uniprot.org/uniprot/B2RWH3|||http://purl.uniprot.org/uniprot/Q6GSS7 ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region ^@ 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 2-A|||Histone H2A/H2B/H3|||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_0000055233 http://togogenome.org/gene/10090:Ctdnep1 ^@ http://purl.uniprot.org/uniprot/Q3TP92 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Domain Extent|||Sequence Conflict|||Transmembrane ^@ CTD nuclear envelope phosphatase 1|||FCP1 homology|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000297968 http://togogenome.org/gene/10090:Rragb ^@ http://purl.uniprot.org/uniprot/Q6NTA4 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region ^@ Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-acetylmethionine|||Ras-related GTP-binding protein B ^@ http://purl.uniprot.org/annotation/PRO_0000239949 http://togogenome.org/gene/10090:Nudcd3 ^@ http://purl.uniprot.org/uniprot/B0FTY3|||http://purl.uniprot.org/uniprot/Q8R1N4 ^@ 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|||CS|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||NudC domain-containing protein 3|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000057986|||http://purl.uniprot.org/annotation/VSP_013677|||http://purl.uniprot.org/annotation/VSP_013678|||http://purl.uniprot.org/annotation/VSP_013679|||http://purl.uniprot.org/annotation/VSP_013680 http://togogenome.org/gene/10090:Tub ^@ http://purl.uniprot.org/uniprot/P50586|||http://purl.uniprot.org/uniprot/Q4VA41 ^@ 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 ^@ Abolishes interaction with phosphatidylinositol 4,5-bisphosphate and reduces secretion by 40%; when associated with A-330.|||Abolishes interaction with phosphatidylinositol 4,5-bisphosphate and reduces secretion by 40%; when associated with A-332.|||Disordered|||In isoform Short.|||Polar residues|||Tubby C-terminal|||Tubby N-terminal|||Tubby protein ^@ http://purl.uniprot.org/annotation/PRO_0000186464|||http://purl.uniprot.org/annotation/VSP_006675 http://togogenome.org/gene/10090:Acaca ^@ http://purl.uniprot.org/uniprot/Q5SWU9 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant ^@ ATP-grasp|||Acetyl-CoA carboxylase 1|||Biotin carboxylation|||Biotinyl-binding|||Carboxyltransferase|||CoA carboxyltransferase C-terminal|||CoA carboxyltransferase N-terminal|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||N6-biotinyllysine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000258040|||http://purl.uniprot.org/annotation/VSP_026101 http://togogenome.org/gene/10090:Crim1 ^@ http://purl.uniprot.org/uniprot/Q9JLL0 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||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|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4|||VWFC 5|||VWFC 6 ^@ http://purl.uniprot.org/annotation/PRO_0000021002 http://togogenome.org/gene/10090:Abcg5 ^@ http://purl.uniprot.org/uniprot/Q99PE8 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane ^@ ABC transmembrane type-2|||ABC transporter|||ATP-binding cassette sub-family G member 5|||Abolishes palmitoylation. No effect on function and subcellular location.|||Cytoplasmic|||Decreases expression of both ABCG5 and ABCG8. Disrupts sterol transport activity.|||Disordered|||Disrupts sterol transport activity. Decreases expression of both ABCG5 and ABCG8.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In trac; strongly increased levels of sitosterol, brassicasterol and campesterol in blood plasma.|||Loss of one N-glycosylation site. Abolishes N-glycosylation; when associated with Q-585.|||Loss of one N-glycosylation site. Abolishes N-glycosylation; when associated with Q-592.|||N-linked (GlcNAc...) asparagine|||No effect on cholesterol and sitosterol transport activity. Mildly reduced expression of ABCG5 and ABCG8.|||No effect on cholesterol and sitosterol transport activity; when associated with G-196.|||No effect on cholesterol and sitosterol transport activity; when associated with V-194.|||S-palmitoyl cysteine|||Strongly decreases expression of both ABCG5 and ABCG8. Disrupts sterol transport activity.|||Strongly reduces cholesterol transport activity, but has little effect on biliary secretion of campesterol and sitosterol. No effect on ATP-binding and on expression of ABCG5 and ABCG8. ^@ http://purl.uniprot.org/annotation/PRO_0000093394 http://togogenome.org/gene/10090:Adamts3 ^@ http://purl.uniprot.org/uniprot/E9Q287|||http://purl.uniprot.org/uniprot/G3X9D2 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||PLAC|||Peptidase M12B|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_5003243064|||http://purl.uniprot.org/annotation/PRO_5015091854 http://togogenome.org/gene/10090:Pole4 ^@ http://purl.uniprot.org/uniprot/Q9CQ36 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Modified Residue|||Region ^@ DNA polymerase epsilon subunit 4|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000191747 http://togogenome.org/gene/10090:Gle1 ^@ http://purl.uniprot.org/uniprot/Q8R322 ^@ 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|||Interaction with NUP155|||Interaction with NUPL2|||Mediates the shuttling between the nucleus and the cytoplasm|||Phosphoserine|||Polar residues|||mRNA export factor GLE1 ^@ http://purl.uniprot.org/annotation/PRO_0000204823 http://togogenome.org/gene/10090:Or5c1 ^@ http://purl.uniprot.org/uniprot/Q8VF22 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Fabp2 ^@ http://purl.uniprot.org/uniprot/P55050|||http://purl.uniprot.org/uniprot/Q53YP5 ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue ^@ Cytosolic fatty-acid binding proteins|||Fatty acid-binding protein, intestinal|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000067329 http://togogenome.org/gene/10090:Spata9 ^@ http://purl.uniprot.org/uniprot/Q9D9R3 ^@ Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane ^@ Chain|||Region|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||Spermatogenesis-associated protein 9 ^@ http://purl.uniprot.org/annotation/PRO_0000278447|||http://purl.uniprot.org/annotation/VSP_023285|||http://purl.uniprot.org/annotation/VSP_023286 http://togogenome.org/gene/10090:Lonrf2 ^@ http://purl.uniprot.org/uniprot/B2RT44 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Lon N-terminal|||Polar residues|||RING-type ^@ http://togogenome.org/gene/10090:Ltn1 ^@ http://purl.uniprot.org/uniprot/Q6A009 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ Disordered|||E3 ubiquitin-protein ligase listerin|||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|||Polar residues|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000056305 http://togogenome.org/gene/10090:Atp7b ^@ http://purl.uniprot.org/uniprot/Q64446 ^@ 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 ^@ 4-aspartylphosphate intermediate|||Copper-transporting ATPase 2|||Cytoplasmic|||Disordered|||Extracellular|||HMA 1|||HMA 2|||HMA 3|||HMA 4|||HMA 5|||HMA 6|||Helical|||In tx mice.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000046315 http://togogenome.org/gene/10090:Tceanc ^@ http://purl.uniprot.org/uniprot/Q3US16 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||TFIIS N-terminal|||TFIIS central|||Transcription elongation factor A N-terminal and central domain-containing protein ^@ http://purl.uniprot.org/annotation/PRO_0000259661 http://togogenome.org/gene/10090:Ralgapa2 ^@ http://purl.uniprot.org/uniprot/A0A0A0MQD7|||http://purl.uniprot.org/uniprot/A3KGS3 ^@ 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.|||Phosphoserine|||Phosphoserine; by PKB|||Phosphothreonine; by PKB|||Polar residues|||Ral GTPase-activating protein subunit alpha-2|||Rap-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000286973|||http://purl.uniprot.org/annotation/VSP_025251|||http://purl.uniprot.org/annotation/VSP_025252 http://togogenome.org/gene/10090:Vps33b ^@ http://purl.uniprot.org/uniprot/P59016 ^@ Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict ^@ Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict ^@ N-acetylalanine|||Removed|||Vacuolar protein sorting-associated protein 33B ^@ http://purl.uniprot.org/annotation/PRO_0000206306 http://togogenome.org/gene/10090:Mroh8 ^@ http://purl.uniprot.org/uniprot/E9PYI4|||http://purl.uniprot.org/uniprot/Q3V109 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||RNA polymerase II assembly factor Rtp1 C-terminal ^@ http://togogenome.org/gene/10090:Tor1b ^@ http://purl.uniprot.org/uniprot/Q9ER41 ^@ Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Torsin-1B ^@ http://purl.uniprot.org/annotation/PRO_0000005510 http://togogenome.org/gene/10090:Mapk13 ^@ http://purl.uniprot.org/uniprot/Q3UIB2|||http://purl.uniprot.org/uniprot/Q9Z1B7 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict ^@ Mitogen-activated protein kinase 13|||Phosphoserine|||Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||TXY ^@ http://purl.uniprot.org/annotation/PRO_0000186287 http://togogenome.org/gene/10090:Lmbr1 ^@ http://purl.uniprot.org/uniprot/A0A0G2JFX9|||http://purl.uniprot.org/uniprot/Q9JIT0 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Limb region 1 protein ^@ http://purl.uniprot.org/annotation/PRO_0000053907|||http://purl.uniprot.org/annotation/VSP_016889|||http://purl.uniprot.org/annotation/VSP_016890|||http://purl.uniprot.org/annotation/VSP_016891 http://togogenome.org/gene/10090:Trmt10a ^@ http://purl.uniprot.org/uniprot/Q8C1Z8 ^@ 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|||Phosphoserine|||SAM-dependent MTase TRM10-type|||tRNA methyltransferase 10 homolog A ^@ http://purl.uniprot.org/annotation/PRO_0000311316 http://togogenome.org/gene/10090:Plk3 ^@ http://purl.uniprot.org/uniprot/Q6P571 ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site ^@ Binding Site|||Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||POLO box|||Pro residues|||Protein kinase ^@ http://togogenome.org/gene/10090:Scn3a ^@ http://purl.uniprot.org/uniprot/A2ASI5|||http://purl.uniprot.org/uniprot/Q3UF73 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane ^@ Basic and acidic residues|||Basic 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 isoform 2 and isoform 3.|||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)|||Ion transport|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pore-forming|||Sodium channel protein type 3 subunit alpha ^@ http://purl.uniprot.org/annotation/PRO_0000444899|||http://purl.uniprot.org/annotation/VSP_059662|||http://purl.uniprot.org/annotation/VSP_059663 http://togogenome.org/gene/10090:Piwil1 ^@ http://purl.uniprot.org/uniprot/Q9JMB7 ^@ Active 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|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn ^@ Abolishes piRNA-binding and ubiquitination by the APC/C.|||Abolishes ubiquitination by the APC/C.|||D-box|||Disordered|||Does not affect piRNA-binding but abolishes ubiquitination by the APC/C. Causes male sterility.|||Impairs binding to 2'-O-methylated 3'-end of piRNAs.|||In DAH mutant; causes male infertility due to derepression of LINE1 retrotransposons transcripts.|||In isoform 2.|||MID region|||Omega-N-methylarginine; alternate|||Omega-N-methylarginine; by PRMT5|||Omega-N-methylarginine; by PRMT5; alternate|||PAZ|||Piwi|||Piwi-like protein 1|||Required for binding 2'-O-methylated 3'-end of piRNAs|||Symmetric dimethylarginine; alternate|||Symmetric dimethylarginine; by PRMT5; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000234568|||http://purl.uniprot.org/annotation/VSP_036663 http://togogenome.org/gene/10090:Zfp41 ^@ http://purl.uniprot.org/uniprot/Q02526 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Region|||Zinc Finger ^@ Basic and acidic residues|||Basic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Zinc finger protein 41 ^@ http://purl.uniprot.org/annotation/PRO_0000047299 http://togogenome.org/gene/10090:Or4c117 ^@ http://purl.uniprot.org/uniprot/Q7TR02 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Cyp17a1 ^@ http://purl.uniprot.org/uniprot/P27786|||http://purl.uniprot.org/uniprot/Q3UYU1|||http://purl.uniprot.org/uniprot/Q53YJ1 ^@ Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Mutagenesis Site|||Signal Peptide ^@ 49% and 41% of wild-type 17alpha-hydroxylase activity with progesterone and pregnenolone respectively. 36% and 27% of wild type 17,20-lyase activity with 17alpha-hydroxyprogesterone and 17alpha-hydroxypregnenolone respectively.|||68% and 45% of wild-type 17alpha-hydroxylase activity with progesterone and pregnenolone respectively. 64% of wild type 17,20-lyase activity with 17alpha-hydroxyprogesterone.|||Steroid 17-alpha-hydroxylase/17,20 lyase|||axial binding residue ^@ http://purl.uniprot.org/annotation/PRO_0000051935|||http://purl.uniprot.org/annotation/PRO_5004230291|||http://purl.uniprot.org/annotation/PRO_5010139237 http://togogenome.org/gene/10090:H3c1 ^@ http://purl.uniprot.org/uniprot/P68433 ^@ Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand ^@ Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||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|||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; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoarginine|||Phosphoarginine; 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|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate ^@ http://purl.uniprot.org/annotation/PRO_0000221249 http://togogenome.org/gene/10090:Dock5 ^@ http://purl.uniprot.org/uniprot/B2RY04 ^@ 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|||C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 5|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000358858 http://togogenome.org/gene/10090:Bpgm ^@ http://purl.uniprot.org/uniprot/P15327 ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site ^@ Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Site ^@ Bisphosphoglycerate mutase|||N-acetylserine|||Phosphothreonine|||Proton donor/acceptor|||Removed|||Tele-phosphohistidine intermediate|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000179835 http://togogenome.org/gene/10090:Eif4b ^@ http://purl.uniprot.org/uniprot/Q8BGD9 ^@ 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|||Eukaryotic translation initiation factor 4B|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by RPS6KA1|||Phosphothreonine|||Polar residues|||Pro residues|||RRM ^@ http://purl.uniprot.org/annotation/PRO_0000081617 http://togogenome.org/gene/10090:Obp2a ^@ http://purl.uniprot.org/uniprot/Q8K1H9 ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide ^@ N-linked (GlcNAc...) asparagine|||Odorant-binding protein 2a ^@ http://purl.uniprot.org/annotation/PRO_0000017924 http://togogenome.org/gene/10090:Cyp3a57 ^@ http://purl.uniprot.org/uniprot/D3YYZ0 ^@ Binding Site|||Region|||Site|||Transmembrane ^@ Binding Site|||Transmembrane ^@ Helical|||axial binding residue ^@ http://togogenome.org/gene/10090:BC005537 ^@ http://purl.uniprot.org/uniprot/Q99LU8 ^@ Chain|||Molecule Processing ^@ Chain ^@ Uncharacterized protein C6orf62 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000089515 http://togogenome.org/gene/10090:Smim20 ^@ http://purl.uniprot.org/uniprot/D3Z7Q2 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Peptide|||Topological Domain|||Transmembrane ^@ Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Phenylalanine amide|||Phoenixin-14|||Phoenixin-20|||Small integral membrane protein 20 ^@ http://purl.uniprot.org/annotation/PRO_0000449030|||http://purl.uniprot.org/annotation/PRO_0000449031|||http://purl.uniprot.org/annotation/PRO_0000449032 http://togogenome.org/gene/10090:Amigo1 ^@ http://purl.uniprot.org/uniprot/Q80ZD8 ^@ 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|||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|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Amphoterin-induced protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Prevents from leaving the ER. ^@ http://purl.uniprot.org/annotation/PRO_0000014507|||http://purl.uniprot.org/annotation/VSP_014166|||http://purl.uniprot.org/annotation/VSP_014167 http://togogenome.org/gene/10090:Il21r ^@ http://purl.uniprot.org/uniprot/Q3TAI3|||http://purl.uniprot.org/uniprot/Q9JHX3 ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Box 1 motif|||C-linked (Man) tryptophan|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III domain-containing protein|||Helical|||In strain: BALB/c and SJL/J.|||Interleukin-21 receptor|||N-linked (GlcNAc...) asparagine|||WSXWS motif ^@ http://purl.uniprot.org/annotation/PRO_0000010882|||http://purl.uniprot.org/annotation/PRO_5010843241 http://togogenome.org/gene/10090:Opn1sw ^@ http://purl.uniprot.org/uniprot/P51491 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||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|||N6-(retinylidene)lysine|||Polar residues|||Short-wave-sensitive opsin 1 ^@ http://purl.uniprot.org/annotation/PRO_0000197766 http://togogenome.org/gene/10090:Naca ^@ http://purl.uniprot.org/uniprot/P70670|||http://purl.uniprot.org/uniprot/Q60817 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict ^@ Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Loss of interaction with SMYD1.|||N6-acetyllysine; alternate|||NAC-A/B|||Nascent polypeptide-associated complex subunit alpha|||Nascent polypeptide-associated complex subunit alpha, muscle-specific form|||PXLXP|||Phosphoserine|||Phosphoserine; by ILK1|||Phosphothreonine|||Phosphothreonine; by GSK3-beta|||Polar residues|||Pro residues|||RNA/DNA-binding|||Required for DNA-binding|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000135577|||http://purl.uniprot.org/annotation/PRO_0000135578 http://togogenome.org/gene/10090:Ehmt1 ^@ http://purl.uniprot.org/uniprot/A0A0H2UH19|||http://purl.uniprot.org/uniprot/Q5DW34|||http://purl.uniprot.org/uniprot/Q8BHB2|||http://purl.uniprot.org/uniprot/Q8C358 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant ^@ ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||Acidic residues|||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|||Histone H3K9me binding|||Histone-lysine N-methyltransferase EHMT1|||In LM3; does not form heterodimer with EHMT2 and is defective in mediating both H3K9me and DNA methylation.|||In LM4; does not prevent methyltransferase activity.|||In LM7; does not prevent methyltransferase activity; when associated with F-1240.|||In LM7; does not prevent methyltransferase activity; when associated with V-1153.|||In isoform 2.|||In isoform 3.|||Interaction with histone H3|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pre-SET|||Removed|||SET ^@ http://purl.uniprot.org/annotation/PRO_0000405844|||http://purl.uniprot.org/annotation/VSP_040724|||http://purl.uniprot.org/annotation/VSP_040725|||http://purl.uniprot.org/annotation/VSP_040726 http://togogenome.org/gene/10090:Pgap2 ^@ http://purl.uniprot.org/uniprot/Q3TQR0|||http://purl.uniprot.org/uniprot/Q3U6W8 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Post-GPI attachment to proteins factor 2 ^@ http://purl.uniprot.org/annotation/PRO_0000326095|||http://purl.uniprot.org/annotation/VSP_032552|||http://purl.uniprot.org/annotation/VSP_032553 http://togogenome.org/gene/10090:Eid1 ^@ http://purl.uniprot.org/uniprot/Q9DCR4 ^@ Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Helix|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Disordered|||EP300-interacting inhibitor of differentiation 1|||In isoform 2.|||Interaction with NR0B2|||LXCXE motif ^@ http://purl.uniprot.org/annotation/PRO_0000289157|||http://purl.uniprot.org/annotation/VSP_052455 http://togogenome.org/gene/10090:Tmem52 ^@ http://purl.uniprot.org/uniprot/B7ZN39|||http://purl.uniprot.org/uniprot/J3QNP8|||http://purl.uniprot.org/uniprot/Q9D702 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Region|||Signal Peptide|||Transmembrane ^@ Disordered|||Helical|||Transmembrane protein 52 ^@ http://purl.uniprot.org/annotation/PRO_0000284058|||http://purl.uniprot.org/annotation/PRO_5003777317|||http://purl.uniprot.org/annotation/PRO_5015087437 http://togogenome.org/gene/10090:Map1a ^@ http://purl.uniprot.org/uniprot/A2ARP8|||http://purl.uniprot.org/uniprot/Q9QYR6 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ 1|||10|||11|||11 X 3 AA approximate repeats of K-K-[DE]|||2|||3|||4|||5|||6|||7|||8|||9|||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_0000072753|||http://purl.uniprot.org/annotation/PRO_0000269727|||http://purl.uniprot.org/annotation/PRO_0000418377|||http://purl.uniprot.org/annotation/VSP_003201 http://togogenome.org/gene/10090:Or2at4 ^@ http://purl.uniprot.org/uniprot/E9Q518 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ubxn7 ^@ http://purl.uniprot.org/uniprot/G5E8R8 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||UBX ^@ http://togogenome.org/gene/10090:Sh3kbp1 ^@ http://purl.uniprot.org/uniprot/Q3TA88|||http://purl.uniprot.org/uniprot/Q3TT90|||http://purl.uniprot.org/uniprot/Q8R550 ^@ 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 ^@ Basic and acidic residues|||Disordered|||In isoform 2, isoform 3 and isoform 8.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 domain-containing kinase-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000097729|||http://purl.uniprot.org/annotation/VSP_007505|||http://purl.uniprot.org/annotation/VSP_007506|||http://purl.uniprot.org/annotation/VSP_007507|||http://purl.uniprot.org/annotation/VSP_007508|||http://purl.uniprot.org/annotation/VSP_007509|||http://purl.uniprot.org/annotation/VSP_007510|||http://purl.uniprot.org/annotation/VSP_007511 http://togogenome.org/gene/10090:Igfbp5 ^@ http://purl.uniprot.org/uniprot/Q07079|||http://purl.uniprot.org/uniprot/Q3UQV0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ Basic and acidic residues|||Disordered|||IGFBP N-terminal|||Insulin-like growth factor-binding protein 5|||Phosphoserine|||Thyroglobulin type-1 ^@ http://purl.uniprot.org/annotation/PRO_0000014386|||http://purl.uniprot.org/annotation/PRO_5014309217 http://togogenome.org/gene/10090:Bnc2 ^@ http://purl.uniprot.org/uniprot/Q2TBA4|||http://purl.uniprot.org/uniprot/Q8BMQ3 ^@ 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 ^@ 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 isoform 2.|||Phosphoserine|||Polar residues|||Zinc finger protein basonuclin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000046935|||http://purl.uniprot.org/annotation/VSP_051875 http://togogenome.org/gene/10090:Tcp10b ^@ http://purl.uniprot.org/uniprot/E9PYJ0|||http://purl.uniprot.org/uniprot/Q8C5S9 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Centromere protein J C-terminal|||Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Vamp5 ^@ http://purl.uniprot.org/uniprot/Q5M9K2|||http://purl.uniprot.org/uniprot/Q791P0|||http://purl.uniprot.org/uniprot/Q9Z2P8 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Modified Residue|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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_0000206734 http://togogenome.org/gene/10090:Ccl12 ^@ http://purl.uniprot.org/uniprot/Q545B5|||http://purl.uniprot.org/uniprot/Q62401 ^@ 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-C motif chemokine|||C-C motif chemokine 12|||Chemokine interleukin-8-like|||In strain: SJL/J. ^@ http://purl.uniprot.org/annotation/PRO_0000005199|||http://purl.uniprot.org/annotation/PRO_5014205865 http://togogenome.org/gene/10090:Abcb5 ^@ http://purl.uniprot.org/uniprot/B5X0E4|||http://purl.uniprot.org/uniprot/Q3UT27|||http://purl.uniprot.org/uniprot/Q9CTU3 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||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 B member 5|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000430433|||http://purl.uniprot.org/annotation/VSP_056757 http://togogenome.org/gene/10090:Tecr ^@ http://purl.uniprot.org/uniprot/G3UWE1|||http://purl.uniprot.org/uniprot/Q9CY27 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Transmembrane ^@ Helical|||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_0000213684 http://togogenome.org/gene/10090:Zbed5 ^@ http://purl.uniprot.org/uniprot/B2RPU8|||http://purl.uniprot.org/uniprot/Q8CEW7 ^@ Domain Extent|||Region ^@ Domain Extent|||Region ^@ DUF4371|||Disordered ^@ http://togogenome.org/gene/10090:Sppl2c ^@ http://purl.uniprot.org/uniprot/A2A6C4 ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Loss of aspartyl protease activity. Reduces interaction with FREY1 and FREY1 protein stability.|||Loss of glycosylation.|||Loss ofaspartyl protease activity. No effect on interaction with FREY.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on interaction with FREY1 and FREY1 protein stability.|||PA|||PAL|||Polar residues|||Signal peptide peptidase-like 2C ^@ http://purl.uniprot.org/annotation/PRO_0000314798|||http://purl.uniprot.org/annotation/VSP_030363|||http://purl.uniprot.org/annotation/VSP_030364 http://togogenome.org/gene/10090:Acap3 ^@ http://purl.uniprot.org/uniprot/Q6NXL5 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ ANK|||Acidic residues|||Arf-GAP|||Disordered|||PH|||Polar residues ^@ http://togogenome.org/gene/10090:Mrs2 ^@ http://purl.uniprot.org/uniprot/Q5NCE8 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Helical|||Magnesium transporter MRS2 homolog, mitochondrial|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000042839 http://togogenome.org/gene/10090:Cep126 ^@ http://purl.uniprot.org/uniprot/Q0VBV7 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Centrosomal protein of 126 kDa|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000295172 http://togogenome.org/gene/10090:Xlr4c ^@ http://purl.uniprot.org/uniprot/Q3TKR2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||Polar residues|||XLR/SYCP3/FAM9 ^@ http://togogenome.org/gene/10090:Abhd16b ^@ http://purl.uniprot.org/uniprot/Q80YU0 ^@ Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent ^@ AB hydrolase-1|||Charge relay system|||Protein ABHD16B ^@ http://purl.uniprot.org/annotation/PRO_0000079464 http://togogenome.org/gene/10090:Gpr17 ^@ http://purl.uniprot.org/uniprot/Q6NS65 ^@ 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|||Uracil nucleotide/cysteinyl leukotriene receptor ^@ http://purl.uniprot.org/annotation/PRO_0000278171 http://togogenome.org/gene/10090:Srgn ^@ http://purl.uniprot.org/uniprot/P13609 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Repeat|||Signal Peptide ^@ 1|||10|||10 X 2 AA tandem repeats of G-S|||2|||3|||4|||5|||6|||7|||8|||9|||Activation peptide|||Disordered|||O-linked (Xyl...) (glycosaminoglycan) serine|||Polar residues|||Serglycin ^@ http://purl.uniprot.org/annotation/PRO_0000026680|||http://purl.uniprot.org/annotation/PRO_0000290036 http://togogenome.org/gene/10090:Lsm3 ^@ http://purl.uniprot.org/uniprot/P62311 ^@ 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_0000125561 http://togogenome.org/gene/10090:Or6z1 ^@ http://purl.uniprot.org/uniprot/Q8VGH3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Gm4861 ^@ http://purl.uniprot.org/uniprot/Q8C5A4 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Signal Peptide|||Transmembrane ^@ Helical ^@ http://purl.uniprot.org/annotation/PRO_5015099090 http://togogenome.org/gene/10090:Exo5 ^@ http://purl.uniprot.org/uniprot/Q9CXP9 ^@ Binding Site|||Chain|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Region ^@ Disordered|||Exonuclease V ^@ http://purl.uniprot.org/annotation/PRO_0000307321 http://togogenome.org/gene/10090:Capn7 ^@ http://purl.uniprot.org/uniprot/Q9R1S8 ^@ Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Chain|||Domain Extent|||Modified Residue|||Region ^@ Calpain catalytic|||Calpain-7|||Domain III|||Domain N|||N-acetylmethionine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000207721 http://togogenome.org/gene/10090:Tln2 ^@ http://purl.uniprot.org/uniprot/E9PUM4|||http://purl.uniprot.org/uniprot/Q3TN69|||http://purl.uniprot.org/uniprot/Q68FD6|||http://purl.uniprot.org/uniprot/Q71LX4|||http://purl.uniprot.org/uniprot/Q8CDM9 ^@ Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn ^@ Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn ^@ FERM|||I/LWEQ|||Interaction with PIP5K1C|||Phosphoserine|||Phosphotyrosine|||Talin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000219432 http://togogenome.org/gene/10090:Rhot2 ^@ http://purl.uniprot.org/uniprot/Q8JZN7 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||EF-hand 1|||EF-hand 2|||Helical; Anchor for type IV membrane protein|||Miro 1|||Miro 2|||Mitochondrial Rho GTPase 2|||Mitochondrial intermembrane ^@ http://purl.uniprot.org/annotation/PRO_0000239319 http://togogenome.org/gene/10090:Pmfbp1 ^@ http://purl.uniprot.org/uniprot/B2RR67|||http://purl.uniprot.org/uniprot/Q9WVQ0 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polyamine-modulated factor 1-binding protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000304620 http://togogenome.org/gene/10090:Or52e8 ^@ http://purl.uniprot.org/uniprot/Q7TRP2 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Ipo4 ^@ http://purl.uniprot.org/uniprot/Q8VI75 ^@ Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat ^@ Chain|||Domain Extent|||Modified Residue|||Repeat ^@ HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||Importin N-terminal|||Importin-4|||N-acetylmethionine ^@ http://purl.uniprot.org/annotation/PRO_0000120749 http://togogenome.org/gene/10090:Fcgr4 ^@ http://purl.uniprot.org/uniprot/A0A0B4J1G0 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane ^@ Abolishes receptor ligation-induced phosphorylation.|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Important for receptor turnover|||Low affinity immunoglobulin gamma Fc region receptor III-A|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine ^@ http://purl.uniprot.org/annotation/PRO_5008204824 http://togogenome.org/gene/10090:Gjb3 ^@ http://purl.uniprot.org/uniprot/A0A654ICX2|||http://purl.uniprot.org/uniprot/P28231 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Region|||Topological Domain|||Transmembrane ^@ Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction beta-3 protein|||Gap junction protein cysteine-rich|||Helical ^@ http://purl.uniprot.org/annotation/PRO_0000057863 http://togogenome.org/gene/10090:Clec4a4 ^@ http://purl.uniprot.org/uniprot/Q5YIR8 ^@ Binding Site|||Disulfide Bond|||Domain Extent|||Modification|||Region|||Site|||Transmembrane ^@ Binding Site|||Disulfide Bond|||Domain Extent|||Transmembrane ^@ C-type lectin|||Helical ^@ http://togogenome.org/gene/10090:Nlgn1 ^@ http://purl.uniprot.org/uniprot/E9QK34|||http://purl.uniprot.org/uniprot/Q99K10 ^@ Chain|||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|||Turn ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Abolishes binding to heparan sulfate and reduces presynaptic differentiation.|||Carboxylesterase type B|||Cytoplasmic|||Decreased protein abundance. Not associated with changes in subcellular location.|||Decreased protein abundance. Not delivered to the plasma membrane.|||Decreased protein abundance. Not delivered to the plasma membrane. Heterozygotes mice with this mutation display abnormal social behavior.|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Neuroligin-1|||No effect on protein abundance. Not associated with changes in subcellular location.|||Not associated with changes in subcellular location.|||O-linked (GalNAc...) serine ^@ http://purl.uniprot.org/annotation/PRO_0000008641|||http://purl.uniprot.org/annotation/VSP_007528|||http://purl.uniprot.org/annotation/VSP_007529|||http://purl.uniprot.org/annotation/VSP_007530 http://togogenome.org/gene/10090:Rasa2 ^@ http://purl.uniprot.org/uniprot/P58069 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger ^@ Basic and acidic residues|||Btk-type|||C2 1|||C2 2|||Disordered|||Greatly reduced binding to IP4 and to phospholipids.|||N-acetylalanine|||No binding to IP4, reduced binding to phospholipids.|||PH|||Phosphoserine|||Ras GTPase-activating protein 2|||Ras-GAP|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000056639 http://togogenome.org/gene/10090:Blvra ^@ http://purl.uniprot.org/uniprot/Q9CY64 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Modified Residue|||Propeptide|||Sequence Conflict ^@ Biliverdin reductase A|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000010854|||http://purl.uniprot.org/annotation/PRO_0000010855 http://togogenome.org/gene/10090:Plekhm2 ^@ http://purl.uniprot.org/uniprot/A2ADE0|||http://purl.uniprot.org/uniprot/Q80TQ5|||http://purl.uniprot.org/uniprot/Z4YJW6 ^@ 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 3.|||Interaction with KIF5B|||N-acetylmethionine|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family M member 2|||Polar residues|||RUN ^@ http://purl.uniprot.org/annotation/PRO_0000309456|||http://purl.uniprot.org/annotation/VSP_029162|||http://purl.uniprot.org/annotation/VSP_029163|||http://purl.uniprot.org/annotation/VSP_029164 http://togogenome.org/gene/10090:Pik3ip1 ^@ http://purl.uniprot.org/uniprot/Q7TMJ8 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Kringle|||Phosphoinositide-3-kinase-interacting protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000280348|||http://purl.uniprot.org/annotation/VSP_023641|||http://purl.uniprot.org/annotation/VSP_023642 http://togogenome.org/gene/10090:Neurog2 ^@ http://purl.uniprot.org/uniprot/P70447|||http://purl.uniprot.org/uniprot/Q6GTH9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict ^@ BHLH|||Disordered|||Neurogenin-2|||Polar residues|||bHLH ^@ http://purl.uniprot.org/annotation/PRO_0000127401 http://togogenome.org/gene/10090:Gjc2 ^@ http://purl.uniprot.org/uniprot/Q8BQU6 ^@ 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 ^@ Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction gamma-2 protein|||Helical|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000057843 http://togogenome.org/gene/10090:Vmn1r159 ^@ http://purl.uniprot.org/uniprot/K7N701 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Clstn2 ^@ http://purl.uniprot.org/uniprot/Q9ER65 ^@ 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|||Cadherin 1|||Cadherin 2|||Calsyntenin-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000004024|||http://purl.uniprot.org/annotation/VSP_032037 http://togogenome.org/gene/10090:Or52a33 ^@ http://purl.uniprot.org/uniprot/Q8VGY7 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:AI182371 ^@ http://purl.uniprot.org/uniprot/A2AS37|||http://purl.uniprot.org/uniprot/Q8BWN9|||http://purl.uniprot.org/uniprot/Q8BWS8 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane ^@ Anaphylatoxin-like|||Basic and acidic residues|||Disordered|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5002642748|||http://purl.uniprot.org/annotation/PRO_5014312012 http://togogenome.org/gene/10090:Adam7 ^@ http://purl.uniprot.org/uniprot/O35227 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 7|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000029056|||http://purl.uniprot.org/annotation/PRO_0000419681 http://togogenome.org/gene/10090:Palb2 ^@ http://purl.uniprot.org/uniprot/D3YVU6|||http://purl.uniprot.org/uniprot/Q3U0P1 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Splice Variant ^@ ChAM (Chromatin-association motif); required for chromatin association, mediates nucleosome association|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with BRCA1|||Interaction with RAD51|||Interaction with RAD51 and BRCA2|||Interaction with RAD51, BRCA2 and POLH|||Partner and localiser of BRCA2 WD40|||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|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000252392|||http://purl.uniprot.org/annotation/VSP_020928|||http://purl.uniprot.org/annotation/VSP_020929|||http://purl.uniprot.org/annotation/VSP_020930|||http://purl.uniprot.org/annotation/VSP_020931 http://togogenome.org/gene/10090:Zfp982 ^@ http://purl.uniprot.org/uniprot/Q6PDN1 ^@ Domain Extent|||Region ^@ Domain Extent ^@ C2H2-type|||KRAB ^@ http://togogenome.org/gene/10090:Ergic1 ^@ http://purl.uniprot.org/uniprot/Q4FK22|||http://purl.uniprot.org/uniprot/Q9DC16 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Endoplasmic reticulum vesicle transporter C-terminal|||Endoplasmic reticulum vesicle transporter N-terminal|||Endoplasmic reticulum-Golgi intermediate compartment protein 1|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000087024 http://togogenome.org/gene/10090:Ncapg2 ^@ http://purl.uniprot.org/uniprot/Q3UT55|||http://purl.uniprot.org/uniprot/Q3UU24|||http://purl.uniprot.org/uniprot/Q6DFV1 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict ^@ Chain|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict ^@ Condensin-2 complex subunit G2|||HEAT|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000255943 http://togogenome.org/gene/10090:Vmn2r40 ^@ http://purl.uniprot.org/uniprot/F6W043 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5008414350 http://togogenome.org/gene/10090:Sox12 ^@ http://purl.uniprot.org/uniprot/Q04890 ^@ 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|||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_0000048755 http://togogenome.org/gene/10090:Dennd1b ^@ http://purl.uniprot.org/uniprot/Q3U1T9 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant ^@ Abolishes guanine nucleotide exchange factor (GEF) activity and impaired TCR down-modulation and recycling in TH2 cells.|||Basic and acidic residues|||Clathrin box|||DENN domain-containing protein 1B|||Disordered|||FXDXF motif|||Impaired interaction with the AP-2 complex and impaired TCR down-modulation and recycling in TH2 cells; when associated with 547-A--A-549.|||Impaired interaction with the AP-2 complex and impaired TCR down-modulation and recycling in TH2 cells; when associated with A-482.|||In isoform 1 and isoform 3.|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||cDENN|||dDENN|||uDENN ^@ http://purl.uniprot.org/annotation/PRO_0000304675|||http://purl.uniprot.org/annotation/VSP_058172|||http://purl.uniprot.org/annotation/VSP_058173|||http://purl.uniprot.org/annotation/VSP_058174|||http://purl.uniprot.org/annotation/VSP_058175|||http://purl.uniprot.org/annotation/VSP_058176 http://togogenome.org/gene/10090:Arhgap28 ^@ http://purl.uniprot.org/uniprot/E9Q642|||http://purl.uniprot.org/uniprot/Q8BN58 ^@ 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.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho GTPase-activating protein 28|||Rho-GAP ^@ http://purl.uniprot.org/annotation/PRO_0000280477|||http://purl.uniprot.org/annotation/VSP_023729|||http://purl.uniprot.org/annotation/VSP_023730|||http://purl.uniprot.org/annotation/VSP_023731 http://togogenome.org/gene/10090:Kctd15 ^@ http://purl.uniprot.org/uniprot/Q8K0E1 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ BTB|||BTB/POZ domain-containing protein KCTD15|||Disordered|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000247252 http://togogenome.org/gene/10090:Klk15 ^@ http://purl.uniprot.org/uniprot/Q8CGR4 ^@ Domain Extent|||Region ^@ Domain Extent ^@ Peptidase S1 ^@ http://togogenome.org/gene/10090:Naa50 ^@ http://purl.uniprot.org/uniprot/Q6PGB6 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant ^@ In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetyltransferase|||N-alpha-acetyltransferase 50|||N6-acetyllysine|||Phosphothreonine|||Phosphotyrosine|||Substrate ^@ http://purl.uniprot.org/annotation/PRO_0000284903|||http://purl.uniprot.org/annotation/VSP_024748|||http://purl.uniprot.org/annotation/VSP_024749|||http://purl.uniprot.org/annotation/VSP_024750|||http://purl.uniprot.org/annotation/VSP_024751 http://togogenome.org/gene/10090:Slc24a4 ^@ http://purl.uniprot.org/uniprot/A0A0R4J0Z4|||http://purl.uniprot.org/uniprot/Q8CGQ8 ^@ Chain|||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|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane ^@ Alpha-1|||Alpha-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Sodium/calcium exchanger membrane region|||Sodium/potassium/calcium exchanger 4 ^@ http://purl.uniprot.org/annotation/PRO_0000019374|||http://purl.uniprot.org/annotation/VSP_041610|||http://purl.uniprot.org/annotation/VSP_041611 http://togogenome.org/gene/10090:Fbn2 ^@ http://purl.uniprot.org/uniprot/Q61555 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide ^@ 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|||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_0000007585|||http://purl.uniprot.org/annotation/PRO_0000436889|||http://purl.uniprot.org/annotation/PRO_0000436890 http://togogenome.org/gene/10090:Suz12 ^@ http://purl.uniprot.org/uniprot/E9PW15|||http://purl.uniprot.org/uniprot/Q80U70 ^@ 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|||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|||Interaction with AEBP2 and PHF19|||Interaction with JARID2 and EPOP|||Phosphoserine|||Polar residues|||Polycomb protein Suz12|||Polycomb protein VEFS-Box|||VEFS-box ^@ http://purl.uniprot.org/annotation/PRO_0000047058 http://togogenome.org/gene/10090:Zfp326 ^@ http://purl.uniprot.org/uniprot/A0A0R4J098|||http://purl.uniprot.org/uniprot/O88291 ^@ 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 ^@ http://purl.uniprot.org/annotation/PRO_0000075387|||http://purl.uniprot.org/annotation/VSP_014957|||http://purl.uniprot.org/annotation/VSP_014958|||http://purl.uniprot.org/annotation/VSP_014959 http://togogenome.org/gene/10090:Serpina3b ^@ http://purl.uniprot.org/uniprot/Q05A44|||http://purl.uniprot.org/uniprot/Q8BYY9 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site ^@ Chain|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Site ^@ N-linked (GlcNAc...) asparagine|||RCL|||Reactive bond|||Serine protease inhibitor A3B|||Serpin ^@ http://purl.uniprot.org/annotation/PRO_0000032415|||http://purl.uniprot.org/annotation/PRO_5014306691 http://togogenome.org/gene/10090:Fbxo41 ^@ http://purl.uniprot.org/uniprot/Q3UGY7|||http://purl.uniprot.org/uniprot/Q6NS60 ^@ 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|||F-box|||F-box only protein 41|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000119941 http://togogenome.org/gene/10090:Prdm9 ^@ http://purl.uniprot.org/uniprot/E9Q4V2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||C2H2-type|||Disordered|||KRAB|||KRAB-related|||Polar residues|||SET ^@ http://togogenome.org/gene/10090:Or7g30 ^@ http://purl.uniprot.org/uniprot/Q8VFF6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Rbm12b1 ^@ http://purl.uniprot.org/uniprot/Q80YR9 ^@ 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|||Basic residues|||Disordered|||N6-acetyllysine|||Phosphoserine|||RNA-binding protein 12B-A|||RRM 1|||RRM 2|||RRM 3|||RRM 4 ^@ http://purl.uniprot.org/annotation/PRO_0000273368 http://togogenome.org/gene/10090:Rilp ^@ http://purl.uniprot.org/uniprot/Q14AQ2|||http://purl.uniprot.org/uniprot/Q5ND29 ^@ 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 ^@ Disordered|||Necessary for interaction with RAB7A and RAB34 and lysosomal distribution and morphology|||Phosphoserine|||Phosphothreonine|||Polar residues|||RH1|||RH2|||Rab-interacting lysosomal protein ^@ http://purl.uniprot.org/annotation/PRO_0000097340 http://togogenome.org/gene/10090:Relt ^@ http://purl.uniprot.org/uniprot/Q8BX43 ^@ Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Enamel of mutant mice has a rough surface and is hypomineralized.|||Extracellular|||Helical|||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_0000034601 http://togogenome.org/gene/10090:Pfn3 ^@ http://purl.uniprot.org/uniprot/Q9DAD6 ^@ Chain|||Molecule Processing ^@ Chain ^@ Profilin-3 ^@ http://purl.uniprot.org/annotation/PRO_0000199580 http://togogenome.org/gene/10090:Cct8l1 ^@ http://purl.uniprot.org/uniprot/Q80YT3 ^@ Compositionally Biased Region|||Region ^@ Compositionally Biased Region|||Region ^@ Disordered|||Polar residues ^@ http://togogenome.org/gene/10090:Arl6ip1 ^@ http://purl.uniprot.org/uniprot/Q80ZW9|||http://purl.uniprot.org/uniprot/Q9JKW0 ^@ Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Topological Domain|||Transmembrane ^@ ADP-ribosylation factor-like protein 6-interacting protein 1|||Cytoplasmic|||Helical|||Lumenal ^@ http://purl.uniprot.org/annotation/PRO_0000064656 http://togogenome.org/gene/10090:Pnliprp2 ^@ http://purl.uniprot.org/uniprot/P17892 ^@ 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 ^@ Charge relay system|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PLAT|||Pancreatic lipase-related protein 2|||Required for galactolipase activity ^@ http://purl.uniprot.org/annotation/PRO_0000017794 http://togogenome.org/gene/10090:Svs6 ^@ http://purl.uniprot.org/uniprot/Q9D268 ^@ Chain|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Region|||Signal Peptide ^@ Disordered ^@ http://purl.uniprot.org/annotation/PRO_5015099673 http://togogenome.org/gene/10090:Crppa ^@ http://purl.uniprot.org/uniprot/A0A1Y7VK76|||http://purl.uniprot.org/uniprot/A0A1Y7VM96|||http://purl.uniprot.org/uniprot/Q5RJG7 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Domain Extent|||Sequence Conflict|||Site|||Splice Variant ^@ D-ribitol-5-phosphate cytidylyltransferase|||D-ribitol-5-phosphate cytidylyltransferase C-terminal|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Positions substrate for the nucleophilic attack|||Transition state stabilizer ^@ http://purl.uniprot.org/annotation/PRO_0000343698|||http://purl.uniprot.org/annotation/VSP_034667|||http://purl.uniprot.org/annotation/VSP_034668|||http://purl.uniprot.org/annotation/VSP_034669|||http://purl.uniprot.org/annotation/VSP_034670|||http://purl.uniprot.org/annotation/VSP_034671|||http://purl.uniprot.org/annotation/VSP_034672|||http://purl.uniprot.org/annotation/VSP_034673 http://togogenome.org/gene/10090:Sln ^@ http://purl.uniprot.org/uniprot/Q9CQD6 ^@ Molecule Processing|||Peptide|||Region|||Topological Domain|||Transmembrane ^@ Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Helical|||Lumenal|||Sarcolipin ^@ http://purl.uniprot.org/annotation/PRO_0000045899 http://togogenome.org/gene/10090:Dnase1l2 ^@ http://purl.uniprot.org/uniprot/Q9D1G0 ^@ Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide ^@ Deoxyribonuclease-1-like 2|||Essential for enzymatic activity ^@ http://purl.uniprot.org/annotation/PRO_0000007287 http://togogenome.org/gene/10090:Ttc3 ^@ http://purl.uniprot.org/uniprot/G5E8T2 ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||Polar residues|||RING-type|||TPR ^@ http://togogenome.org/gene/10090:Aasdh ^@ http://purl.uniprot.org/uniprot/Q80WC9 ^@ 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 incorporation of beta-alanine.|||Basic and acidic residues|||Beta-alanine-activating enzyme|||Carrier|||Disordered|||In isoform 2.|||In isoform 3.|||O-(pantetheine 4'-phosphoryl)serine|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000315804|||http://purl.uniprot.org/annotation/VSP_030714|||http://purl.uniprot.org/annotation/VSP_030715 http://togogenome.org/gene/10090:Parp14 ^@ http://purl.uniprot.org/uniprot/Q2EMV9 ^@ 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 ^@ Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In strain: Czech II.|||Macro 1|||Macro 2|||Macro 3|||PARP catalytic|||Phosphoserine|||Protein mono-ADP-ribosyltransferase PARP14|||WWE ^@ http://purl.uniprot.org/annotation/PRO_0000247590|||http://purl.uniprot.org/annotation/VSP_020020 http://togogenome.org/gene/10090:Dync1h1 ^@ http://purl.uniprot.org/uniprot/Q9JHU4 ^@ 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|||Turn ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Turn ^@ AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Basic and acidic residues|||Cytoplasmic dynein 1 heavy chain 1|||Disordered|||In CRA1.|||In LOA.|||Interaction with DYNC1I2|||Interaction with DYNC1LI2|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Stalk|||Stem ^@ http://purl.uniprot.org/annotation/PRO_0000114628 http://togogenome.org/gene/10090:Ksr2 ^@ http://purl.uniprot.org/uniprot/A0A075EIS2|||http://purl.uniprot.org/uniprot/A0A8V5L0Q6|||http://purl.uniprot.org/uniprot/Q3UVC0 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger ^@ Disordered|||Kinase suppressor of Ras 2|||Phorbol-ester/DAG-type|||Phosphoserine; by MARK3|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000286965 http://togogenome.org/gene/10090:Obox3 ^@ http://purl.uniprot.org/uniprot/Q3UT54 ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region ^@ Disordered|||Homeobox|||Polar residues ^@ http://togogenome.org/gene/10090:Birc3 ^@ http://purl.uniprot.org/uniprot/A2CGA5|||http://purl.uniprot.org/uniprot/O08863|||http://purl.uniprot.org/uniprot/Q3TSE5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Zinc Finger ^@ BIR 1|||BIR 2|||BIR 3|||Baculoviral IAP repeat-containing protein 3|||CARD|||Disordered|||Phosphoserine|||RING-type ^@ http://purl.uniprot.org/annotation/PRO_0000122350 http://togogenome.org/gene/10090:Zfp27 ^@ http://purl.uniprot.org/uniprot/P10077 ^@ 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 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|||In isoform 2.|||KRAB|||Zinc finger protein 27 ^@ http://purl.uniprot.org/annotation/PRO_0000047288|||http://purl.uniprot.org/annotation/VSP_016025 http://togogenome.org/gene/10090:Arhgef28 ^@ http://purl.uniprot.org/uniprot/P97433 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Alters interaction with MAPK8IP1.|||Alters interaction with YWHAH.|||Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||Interaction with PTK2/FAK1; required for regulation of axonal branching and synapse formation|||Interaction with microtubules|||Loss of function.|||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_0000080967|||http://purl.uniprot.org/annotation/VSP_032145|||http://purl.uniprot.org/annotation/VSP_032146 http://togogenome.org/gene/10090:Apbb1 ^@ http://purl.uniprot.org/uniprot/A0A087WPI2|||http://purl.uniprot.org/uniprot/A0A087WPS7|||http://purl.uniprot.org/uniprot/A0A087WR62|||http://purl.uniprot.org/uniprot/A0A0R4J2C1|||http://purl.uniprot.org/uniprot/A0A0R4J2C6|||http://purl.uniprot.org/uniprot/Q9QXJ1 ^@ 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 ^@ Abolishes ligand binding; when associated with A-283.|||Abolishes ligand binding; when associated with F-280.|||Acidic residues|||Amyloid beta precursor protein binding family B member 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||N6-acetyllysine|||PID|||PID 1|||PID 2|||Phosphoserine|||Phosphoserine; by SGK1|||Phosphotyrosine; by ABL1|||Polar residues|||WW ^@ http://purl.uniprot.org/annotation/PRO_0000076050|||http://purl.uniprot.org/annotation/VSP_011659 http://togogenome.org/gene/10090:Gtpbp1 ^@ http://purl.uniprot.org/uniprot/O08582 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||G1|||G2|||G3|||G4|||G5|||GTP-binding protein 1|||Phosphoserine|||Polar residues|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000122470 http://togogenome.org/gene/10090:Terb1 ^@ http://purl.uniprot.org/uniprot/Q8C0V1 ^@ 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|||Splice Variant|||Strand ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand ^@ ARM 1|||ARM 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with TERF1|||Mimics phosphorylation state; impairs interaction with TERF1.|||Myb-like|||Phosphothreonine|||Telomere repeats-binding bouquet formation protein 1|||Telomere-attachment defects. ^@ http://purl.uniprot.org/annotation/PRO_0000320157|||http://purl.uniprot.org/annotation/VSP_031616|||http://purl.uniprot.org/annotation/VSP_031617|||http://purl.uniprot.org/annotation/VSP_031618|||http://purl.uniprot.org/annotation/VSP_031619|||http://purl.uniprot.org/annotation/VSP_031620|||http://purl.uniprot.org/annotation/VSP_031621|||http://purl.uniprot.org/annotation/VSP_031622|||http://purl.uniprot.org/annotation/VSP_031623 http://togogenome.org/gene/10090:Ino80e ^@ http://purl.uniprot.org/uniprot/Q8R359 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Signal Peptide ^@ Acidic residues|||Disordered|||Polar residues|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_5015099340 http://togogenome.org/gene/10090:Trir ^@ http://purl.uniprot.org/uniprot/Q9D735 ^@ 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|||N6-acetyllysine|||Polar residues|||Telomerase RNA component interacting RNase ^@ http://purl.uniprot.org/annotation/PRO_0000280763 http://togogenome.org/gene/10090:Rhof ^@ http://purl.uniprot.org/uniprot/Q8BYP3 ^@ 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|||N-acetylmethionine|||Removed in mature form|||Rho-related GTP-binding protein RhoF|||S-geranylgeranyl cysteine ^@ http://purl.uniprot.org/annotation/PRO_0000198866|||http://purl.uniprot.org/annotation/PRO_0000281217 http://togogenome.org/gene/10090:Mib2 ^@ http://purl.uniprot.org/uniprot/Q8R516 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger ^@ Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||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|||Abolishes ubiquitin ligase activity.|||E3 ubiquitin-protein ligase MIB2|||In isoform 2.|||In isoform 3.|||MIB/HERC2 1|||MIB/HERC2 2|||No effect.|||Phosphoserine|||RING-type 1|||RING-type 2|||ZZ-type ^@ http://purl.uniprot.org/annotation/PRO_0000055948|||http://purl.uniprot.org/annotation/VSP_014397|||http://purl.uniprot.org/annotation/VSP_014398|||http://purl.uniprot.org/annotation/VSP_014399|||http://purl.uniprot.org/annotation/VSP_014400|||http://purl.uniprot.org/annotation/VSP_014401 http://togogenome.org/gene/10090:Gabpb2 ^@ http://purl.uniprot.org/uniprot/P81069 ^@ Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant ^@ Chain|||Coiled-Coil|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant ^@ ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||GA-binding protein subunit beta-2|||In isoform 2.|||Phosphoserine ^@ http://purl.uniprot.org/annotation/PRO_0000066995|||http://purl.uniprot.org/annotation/VSP_032473 http://togogenome.org/gene/10090:Or4f57 ^@ http://purl.uniprot.org/uniprot/Q7TQX0 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Pten ^@ http://purl.uniprot.org/uniprot/A0A6G7SF19|||http://purl.uniprot.org/uniprot/O08586|||http://purl.uniprot.org/uniprot/Q3UUT8 ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||C2 tensin-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-acetylthreonine|||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 and PLK3|||Phosphoserine; by ROCK1|||Phosphothreonine|||Phosphothreonine; by GSK3-beta and PLK3|||Phosphothreonine; by ROCK1|||Phosphotyrosine; by FRK|||Polar residues|||Reduced excitatory synapse density in hippocampus. Decreased NMDAR-mediated synaptic transmission. Increased brain glycine levels.|||Removed|||Required for interaction with NOP53|||Tyrosine specific protein phosphatases ^@ http://purl.uniprot.org/annotation/PRO_0000215905 http://togogenome.org/gene/10090:Ccdc51 ^@ http://purl.uniprot.org/uniprot/Q3URS9 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane ^@ Helical|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrial potassium channel|||Mitochondrion ^@ http://purl.uniprot.org/annotation/PRO_0000288869|||http://purl.uniprot.org/annotation/VSP_025801 http://togogenome.org/gene/10090:Zfp945 ^@ http://purl.uniprot.org/uniprot/F6WAU7|||http://purl.uniprot.org/uniprot/Q3TGT7|||http://purl.uniprot.org/uniprot/Q66L36 ^@ Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region ^@ Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region ^@ C2H2-type|||Disordered|||KRAB|||Polar residues ^@ http://togogenome.org/gene/10090:Rfx6 ^@ http://purl.uniprot.org/uniprot/Q8C7R7 ^@ Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||DNA Binding|||Region|||Splice Variant ^@ DNA-binding protein RFX6|||Disordered|||In isoform 2.|||In isoform 3.|||RFX-type winged-helix ^@ http://purl.uniprot.org/annotation/PRO_0000313722|||http://purl.uniprot.org/annotation/VSP_030121|||http://purl.uniprot.org/annotation/VSP_030122|||http://purl.uniprot.org/annotation/VSP_030123 http://togogenome.org/gene/10090:Neu2 ^@ http://purl.uniprot.org/uniprot/A0A0R4J224|||http://purl.uniprot.org/uniprot/C0KJU9|||http://purl.uniprot.org/uniprot/E9Q0I0|||http://purl.uniprot.org/uniprot/Q0VGI4|||http://purl.uniprot.org/uniprot/Q3ULV6|||http://purl.uniprot.org/uniprot/Q9JMH3 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Motif|||Non-terminal Residue|||Repeat|||Sequence Conflict ^@ BNR 1|||BNR 2|||FRIP motif|||Nucleophile|||Proton acceptor|||Sialidase|||Sialidase-2 ^@ http://purl.uniprot.org/annotation/PRO_0000208900 http://togogenome.org/gene/10090:BC049715 ^@ http://purl.uniprot.org/uniprot/Q810N5 ^@ Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict ^@ Chain|||Region|||Sequence Conflict ^@ Disordered|||Uncharacterized protein C12orf60 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000274272 http://togogenome.org/gene/10090:Tas1r1 ^@ http://purl.uniprot.org/uniprot/Q3U5H1|||http://purl.uniprot.org/uniprot/Q99PG6 ^@ 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 ^@ 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 strain: 129/J.|||N-linked (GlcNAc...) asparagine|||Taste receptor type 1 member 1 ^@ http://purl.uniprot.org/annotation/PRO_0000012955|||http://purl.uniprot.org/annotation/PRO_5015097466 http://togogenome.org/gene/10090:Clcn4 ^@ http://purl.uniprot.org/uniprot/A0A1B0GT29|||http://purl.uniprot.org/uniprot/Q3LRV6|||http://purl.uniprot.org/uniprot/Q61418|||http://purl.uniprot.org/uniprot/Q8BQG0|||http://purl.uniprot.org/uniprot/Q8CBL5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane ^@ CBS|||CBS 1|||CBS 2|||Cytoplasmic|||H(+)/Cl(-) exchange transporter 4|||Helical|||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|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3 ^@ http://purl.uniprot.org/annotation/PRO_0000094444 http://togogenome.org/gene/10090:Osgepl1 ^@ http://purl.uniprot.org/uniprot/Q6PEB4 ^@ Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide ^@ Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide ^@ In isoform 2.|||Mitochondrion|||N6-acetyllysine|||tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000307779|||http://purl.uniprot.org/annotation/VSP_028831|||http://purl.uniprot.org/annotation/VSP_028832 http://togogenome.org/gene/10090:Hif1an ^@ http://purl.uniprot.org/uniprot/Q8BLR9 ^@ 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|||Site|||Splice Variant ^@ Disordered|||Hypoxia-inducible factor 1-alpha inhibitor|||Important for dimer formation|||In isoform 2.|||Interaction with VHL|||JmjC|||N-acetylalanine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000083975|||http://purl.uniprot.org/annotation/VSP_017537|||http://purl.uniprot.org/annotation/VSP_017538 http://togogenome.org/gene/10090:Fzd1 ^@ http://purl.uniprot.org/uniprot/O70421 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||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_0000012974 http://togogenome.org/gene/10090:Ccdc63 ^@ http://purl.uniprot.org/uniprot/D3YVN4|||http://purl.uniprot.org/uniprot/Q8CDV6 ^@ Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant ^@ Chain|||Coiled-Coil|||Splice Variant ^@ Coiled-coil domain-containing protein 63|||In isoform 2. ^@ http://purl.uniprot.org/annotation/PRO_0000288875|||http://purl.uniprot.org/annotation/VSP_025804 http://togogenome.org/gene/10090:Trim30a ^@ http://purl.uniprot.org/uniprot/P15533 ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Turn|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn|||Zinc Finger ^@ B box-type|||B30.2/SPRY|||Highly hydrophilic|||In isoform Beta.|||Nuclear localization signal|||RING-type|||Reduced interaction with NR2C2 and enhanced interaction with TAB2 and TAB3. Does not decrease TAB2 or TAB3 expression. No effect on inhibition of ROS or negative regulation of NLRP3 inflammasome activation.|||Tripartite motif-containing protein 30A ^@ http://purl.uniprot.org/annotation/PRO_0000056244|||http://purl.uniprot.org/annotation/VSP_005762|||http://purl.uniprot.org/annotation/VSP_005763 http://togogenome.org/gene/10090:Lancl2 ^@ http://purl.uniprot.org/uniprot/Q9JJK2 ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region ^@ Interaction with inositol phospholipids|||LanC-like protein 2|||N-myristoyl glycine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000191273 http://togogenome.org/gene/10090:Ptpn4 ^@ http://purl.uniprot.org/uniprot/Q8BQQ4|||http://purl.uniprot.org/uniprot/Q9WU22 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||FERM|||PDZ|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 4 ^@ http://purl.uniprot.org/annotation/PRO_0000320075 http://togogenome.org/gene/10090:P2rx5 ^@ http://purl.uniprot.org/uniprot/B9EHM6|||http://purl.uniprot.org/uniprot/Q3UYI1 ^@ Binding Site|||Disulfide Bond|||Modification|||Region|||Site|||Transmembrane ^@ Binding Site|||Disulfide Bond|||Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Ddo ^@ http://purl.uniprot.org/uniprot/A0A1L1SS55|||http://purl.uniprot.org/uniprot/A0A1L1SS65|||http://purl.uniprot.org/uniprot/Q2UVA9|||http://purl.uniprot.org/uniprot/Q922Z0|||http://purl.uniprot.org/uniprot/Q9CYP3|||http://purl.uniprot.org/uniprot/Q9D2B4 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict|||Signal Peptide ^@ D-aspartate oxidase|||FAD dependent oxidoreductase|||FAD dependent oxidoreductase domain-containing protein|||Microbody targeting signal ^@ http://purl.uniprot.org/annotation/PRO_0000162771|||http://purl.uniprot.org/annotation/PRO_5004324533|||http://purl.uniprot.org/annotation/PRO_5009681971|||http://purl.uniprot.org/annotation/PRO_5009681987|||http://purl.uniprot.org/annotation/PRO_5015097344|||http://purl.uniprot.org/annotation/PRO_5015099660 http://togogenome.org/gene/10090:Ccer1 ^@ http://purl.uniprot.org/uniprot/Q9CQL2 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region ^@ Acidic residues|||Basic residues|||Coiled-coil domain-containing glutamate-rich protein 1|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000288858 http://togogenome.org/gene/10090:Klra3 ^@ http://purl.uniprot.org/uniprot/Q64329 ^@ 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|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Greatly reduces MHC class I peptide tetramer binding; when associated with D-160.|||Greatly reduces MHC class I peptide tetramer binding; when associated with L-162.|||Greatly reduces MHC class I peptide tetramer binding; when associated with N-225.|||Greatly reduces MHC class I peptide tetramer binding; when associated with P-195.|||Greatly reduces MHC class I peptide tetramer binding; when associated with S-196.|||Greatly reduces MHC class I peptide tetramer binding; when associated with T-226.|||Helical; Signal-anchor for type II membrane protein|||Implicated in MHC class I binding|||In strain: A/Sn, BALB/c, C57BL/6, C57BL/6 XBALB/c, C57BL/6 XCBA, CB-17/SCID and NZB.|||In strain: C57BL/6 XBALB/c, NZB and C57BL/6.|||In strain: C57BL/6 and C57BL/6 XBALB/c.|||In strain: C57BL/6, C57BL/6 XBALB/c and NZB.|||In strain: C57BL/6, C57BL/6 XBALB/c and NZB; requires 2 nucleotide substitutions.|||In strain: NZB.|||Increases stability and improves binding to MHCI class ligand; when associated with G-121; G-175 and G-197.|||Increases stability and improves binding to MHCI class ligand; when associated with G-121; G-175 and K-227.|||Increases stability and improves binding to MHCI class ligand; when associated with G-175; G-197 and K-227.|||Increases stability. Increases stability and improves binding to MHCI class ligand; when associated with G-121; G-197 and K-227.|||Involved in dimerization|||Killer cell lectin-like receptor 3|||N-linked (GlcNAc...) asparagine|||No effect on MHC class I binding; when associated with S-173.|||No effect on MHC class I peptide tetramer binding.|||No effect on MHC class I peptide tetramer binding; when associated with D-250.|||No effect on MHC class I peptide tetramer binding; when associated with N-248.|||No effect on MHC class I peptide tetramer binding; when associated with Q-169.|||No effect on MHC class I peptide tetramer binding; when associated with S-174.|||No effect on MHC class I peptide tetramer binding; when associated with T-170. ^@ http://purl.uniprot.org/annotation/PRO_0000046681 http://togogenome.org/gene/10090:Mchr1 ^@ http://purl.uniprot.org/uniprot/Q8JZL2 ^@ 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; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||Melanin-concentrating hormone receptor 1|||N-linked (GlcNAc...) asparagine ^@ http://purl.uniprot.org/annotation/PRO_0000069736|||http://purl.uniprot.org/annotation/VSP_059222 http://togogenome.org/gene/10090:Map3k10 ^@ http://purl.uniprot.org/uniprot/Q66L42 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict ^@ Disordered|||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|||Pro residues|||Protein kinase|||Proton acceptor|||SH3 ^@ http://purl.uniprot.org/annotation/PRO_0000277826 http://togogenome.org/gene/10090:Mfap1a ^@ http://purl.uniprot.org/uniprot/C0HKD8|||http://purl.uniprot.org/uniprot/C0HKD9 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region ^@ Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Microfibrillar-associated protein 1A|||Microfibrillar-associated protein 1B|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000096459|||http://purl.uniprot.org/annotation/PRO_0000439458 http://togogenome.org/gene/10090:Stra6l ^@ http://purl.uniprot.org/uniprot/Q9DBN1 ^@ 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.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Stimulated by retinoic acid gene 6 protein-like ^@ http://purl.uniprot.org/annotation/PRO_0000438364|||http://purl.uniprot.org/annotation/VSP_058654 http://togogenome.org/gene/10090:Ppfibp2 ^@ http://purl.uniprot.org/uniprot/G3X957|||http://purl.uniprot.org/uniprot/O35711 ^@ 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 and isoform 4.|||In isoform 3.|||In isoform 4.|||Liprin-beta-2|||Phosphoserine|||Polar residues|||SAM|||SAM 1|||SAM 2|||SAM 3 ^@ http://purl.uniprot.org/annotation/PRO_0000191037|||http://purl.uniprot.org/annotation/VSP_009401|||http://purl.uniprot.org/annotation/VSP_009402|||http://purl.uniprot.org/annotation/VSP_009403|||http://purl.uniprot.org/annotation/VSP_026136 http://togogenome.org/gene/10090:Spinkl ^@ http://purl.uniprot.org/uniprot/Q8CEK3 ^@ Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide ^@ Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide ^@ Kazal-like|||N-linked (GlcNAc...) asparagine|||Serine protease inhibitor kazal-like protein, major form|||Serine protease inhibitor kazal-like protein, minor form ^@ http://purl.uniprot.org/annotation/PRO_0000271263|||http://purl.uniprot.org/annotation/PRO_0000368186 http://togogenome.org/gene/10090:Mdm2 ^@ http://purl.uniprot.org/uniprot/P23804 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger ^@ ARF-binding|||Acidic residues|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase Mdm2|||In isoform Mdm2-p76.|||Interaction with MTBP|||Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34|||Interaction with USP7|||Necessary for interaction with USP2|||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|||Reduced interaction with NDUFS1, ROS production and apoptosis.|||Region II|||SWIB/MDM2|||Sufficient to promote the mitochondrial pathway of apoptosis ^@ http://purl.uniprot.org/annotation/PRO_0000018650|||http://purl.uniprot.org/annotation/VSP_003215 http://togogenome.org/gene/10090:Or5p73 ^@ http://purl.uniprot.org/uniprot/Q8VEW2 ^@ 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 5P73 ^@ http://purl.uniprot.org/annotation/PRO_0000150852 http://togogenome.org/gene/10090:Slitrk4 ^@ http://purl.uniprot.org/uniprot/Q149A4|||http://purl.uniprot.org/uniprot/Q810B8 ^@ Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||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|||LRRCT 1|||LRRCT 2|||LRRNT|||N-linked (GlcNAc...) asparagine|||SLIT and NTRK-like protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000032680|||http://purl.uniprot.org/annotation/PRO_5014306920 http://togogenome.org/gene/10090:Tspyl4 ^@ http://purl.uniprot.org/uniprot/Q8VD63 ^@ Chain|||Compositionally Biased Region|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Region ^@ Basic and acidic residues|||Disordered|||Polar residues|||Testis-specific Y-encoded-like protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000185674 http://togogenome.org/gene/10090:Cab39 ^@ http://purl.uniprot.org/uniprot/Q06138 ^@ Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict ^@ Chain|||Sequence Conflict ^@ Calcium-binding protein 39 ^@ http://purl.uniprot.org/annotation/PRO_0000209825 http://togogenome.org/gene/10090:Tmem250-ps ^@ http://purl.uniprot.org/uniprot/A0A571BES4 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Htra1 ^@ http://purl.uniprot.org/uniprot/Q9R118 ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Charge relay system|||IGFBP N-terminal|||Involved in trimer stabilization|||Kazal-like|||Loss of efficient trimer formation.|||Loss of enzymatic activity. No effect on BMP4-binding.|||PDZ|||Serine protease|||Serine protease HTRA1 ^@ http://purl.uniprot.org/annotation/PRO_0000026944 http://togogenome.org/gene/10090:Hadhb ^@ http://purl.uniprot.org/uniprot/Q99JY0 ^@ Active Site|||Chain|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide ^@ Active Site|||Chain|||INTRAMEM|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide ^@ Acyl-thioester intermediate|||Increases nucleophilicity of active site Cys|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton donor/acceptor|||Trifunctional enzyme subunit beta, mitochondrial ^@ http://purl.uniprot.org/annotation/PRO_0000034082 http://togogenome.org/gene/10090:Wdr95 ^@ http://purl.uniprot.org/uniprot/E9PUB4|||http://purl.uniprot.org/uniprot/Q8BN84 ^@ Compositionally Biased Region|||Region|||Repeat ^@ Compositionally Biased Region|||Region|||Repeat ^@ Basic and acidic residues|||Disordered|||WD ^@ http://togogenome.org/gene/10090:Pdzd8 ^@ http://purl.uniprot.org/uniprot/B9EJ80 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger ^@ Disordered|||Helical|||PDZ|||PDZ domain-containing protein 8|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Pro residues|||SMP-LTD ^@ http://purl.uniprot.org/annotation/PRO_0000442772 http://togogenome.org/gene/10090:Eda ^@ http://purl.uniprot.org/uniprot/A0A0U5J8Q0|||http://purl.uniprot.org/uniprot/O54693|||http://purl.uniprot.org/uniprot/Q1L2D6|||http://purl.uniprot.org/uniprot/Q1L2D8|||http://purl.uniprot.org/uniprot/Q1L2D9|||http://purl.uniprot.org/uniprot/Q1L2E0|||http://purl.uniprot.org/uniprot/Q3UV69 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane ^@ 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 isoform TA-A2 and isoform TA-A3.|||In isoform TA-A3.|||In isoform TAB.|||In isoform TAC.|||In isoform TAD.|||N-linked (GlcNAc...) asparagine|||Pro residues|||TNF family profile ^@ http://purl.uniprot.org/annotation/PRO_0000034540|||http://purl.uniprot.org/annotation/PRO_0000034541|||http://purl.uniprot.org/annotation/VSP_006465|||http://purl.uniprot.org/annotation/VSP_006466|||http://purl.uniprot.org/annotation/VSP_006467|||http://purl.uniprot.org/annotation/VSP_006468|||http://purl.uniprot.org/annotation/VSP_006469|||http://purl.uniprot.org/annotation/VSP_006470|||http://purl.uniprot.org/annotation/VSP_006471 http://togogenome.org/gene/10090:Rpf2 ^@ http://purl.uniprot.org/uniprot/G3X926|||http://purl.uniprot.org/uniprot/Q9JJ80 ^@ 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|||Brix|||Disordered|||Ribosome production factor 2 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000120224 http://togogenome.org/gene/10090:Or7a42 ^@ http://purl.uniprot.org/uniprot/Q60892 ^@ 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 7A42 ^@ http://purl.uniprot.org/annotation/PRO_0000150807 http://togogenome.org/gene/10090:Wfdc15b ^@ http://purl.uniprot.org/uniprot/Q9JHY4 ^@ 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 15B ^@ http://purl.uniprot.org/annotation/PRO_0000041394 http://togogenome.org/gene/10090:Nrp2 ^@ http://purl.uniprot.org/uniprot/O35375|||http://purl.uniprot.org/uniprot/Q3U5I8|||http://purl.uniprot.org/uniprot/Q8QZY7 ^@ 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 ^@ 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.|||In isoform A5.|||In isoform B0.|||In isoform B5.|||MAM|||N-linked (GlcNAc...) asparagine|||Neuropilin|||Neuropilin-2|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000021864|||http://purl.uniprot.org/annotation/PRO_5004229827|||http://purl.uniprot.org/annotation/PRO_5015099334|||http://purl.uniprot.org/annotation/VSP_004343|||http://purl.uniprot.org/annotation/VSP_004344|||http://purl.uniprot.org/annotation/VSP_004345|||http://purl.uniprot.org/annotation/VSP_004346|||http://purl.uniprot.org/annotation/VSP_004347 http://togogenome.org/gene/10090:Ngrn ^@ http://purl.uniprot.org/uniprot/Q99KS2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant ^@ Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neugrin|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000294484|||http://purl.uniprot.org/annotation/VSP_039712|||http://purl.uniprot.org/annotation/VSP_039713 http://togogenome.org/gene/10090:Or1j15 ^@ http://purl.uniprot.org/uniprot/Q8VFP9 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Dclk3 ^@ http://purl.uniprot.org/uniprot/Q8BWQ5 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region ^@ Basic and acidic residues|||Disordered|||Doublecortin|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase DCLK3 ^@ http://purl.uniprot.org/annotation/PRO_0000252255 http://togogenome.org/gene/10090:Kash5 ^@ http://purl.uniprot.org/uniprot/Q80VJ8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Abolishes interaction with SUN1. Fails to localize at telomere.|||Acidic residues|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||Perinuclear space|||Protein KASH5 ^@ http://purl.uniprot.org/annotation/PRO_0000331528 http://togogenome.org/gene/10090:Stum ^@ http://purl.uniprot.org/uniprot/A0A1B0GS08|||http://purl.uniprot.org/uniprot/Q0VBF8|||http://purl.uniprot.org/uniprot/Q8CCZ7 ^@ Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Transmembrane ^@ Chain|||Modified Residue|||Non-terminal Residue|||Region|||Transmembrane ^@ Disordered|||Helical|||Phosphoserine|||Protein stum homolog ^@ http://purl.uniprot.org/annotation/PRO_0000278636 http://togogenome.org/gene/10090:Ssc5d ^@ http://purl.uniprot.org/uniprot/Q8BV57 ^@ 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 ^@ Disordered|||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_0000332986 http://togogenome.org/gene/10090:Cox16 ^@ http://purl.uniprot.org/uniprot/E9Q3U7|||http://purl.uniprot.org/uniprot/G3UWC6|||http://purl.uniprot.org/uniprot/Q497I8|||http://purl.uniprot.org/uniprot/Q9CR63 ^@ Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane ^@ Cytochrome c oxidase assembly protein COX16 homolog, mitochondrial|||Disordered|||Helical|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial matrix ^@ http://purl.uniprot.org/annotation/PRO_0000019557|||http://purl.uniprot.org/annotation/VSP_014603 http://togogenome.org/gene/10090:Nop56 ^@ http://purl.uniprot.org/uniprot/Q9D6Z1 ^@ 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|||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_0000219027 http://togogenome.org/gene/10090:4930522H14Rik ^@ http://purl.uniprot.org/uniprot/Q9CPZ3 ^@ 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|||Uncharacterized protein C1orf185 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000271102|||http://purl.uniprot.org/annotation/VSP_022279 http://togogenome.org/gene/10090:Slc17a1 ^@ http://purl.uniprot.org/uniprot/Q61983 ^@ Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Glycosylation Site|||Sequence Conflict|||Transmembrane ^@ Helical|||N-linked (GlcNAc...) asparagine|||Sodium-dependent phosphate transport protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000220937 http://togogenome.org/gene/10090:2700062C07Rik ^@ http://purl.uniprot.org/uniprot/Q5XFZ0 ^@ 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|||Phosphothreonine|||Polar residues|||UPF0711 protein C18orf21 homolog ^@ http://purl.uniprot.org/annotation/PRO_0000279449 http://togogenome.org/gene/10090:Loxl3 ^@ http://purl.uniprot.org/uniprot/Q9Z175 ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site ^@ Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide ^@ 2',4',5'-topaquinone|||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_0000018534 http://togogenome.org/gene/10090:Mettl14 ^@ http://purl.uniprot.org/uniprot/Q3UIK4 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with METTL3|||N6-adenosine-methyltransferase non-catalytic subunit|||Phosphoserine|||Positively charged region required for RNA-binding ^@ http://purl.uniprot.org/annotation/PRO_0000325791|||http://purl.uniprot.org/annotation/VSP_032406 http://togogenome.org/gene/10090:Cdpf1 ^@ http://purl.uniprot.org/uniprot/Q8CEZ9|||http://purl.uniprot.org/uniprot/Q8R3A2 ^@ Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Sequence Conflict ^@ Chain|||Non-terminal Residue|||Sequence Conflict ^@ Cysteine-rich DPF motif domain-containing protein 1 ^@ http://purl.uniprot.org/annotation/PRO_0000341361 http://togogenome.org/gene/10090:Mrgpra2a ^@ http://purl.uniprot.org/uniprot/A0A0R4J1Z0|||http://purl.uniprot.org/uniprot/Q91WW4 ^@ Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane ^@ Chain|||Domain Extent|||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|||Mas-related G-protein coupled receptor member A2 ^@ http://purl.uniprot.org/annotation/PRO_0000069748 http://togogenome.org/gene/10090:Rsc1a1 ^@ http://purl.uniprot.org/uniprot/Q9ER99 ^@ 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|||Regulatory solute carrier protein family 1 member 1|||UBA ^@ http://purl.uniprot.org/annotation/PRO_0000324151 http://togogenome.org/gene/10090:Dnaja3 ^@ http://purl.uniprot.org/uniprot/Q3TJA9|||http://purl.uniprot.org/uniprot/Q99M87 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide|||Zinc Finger ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transit Peptide|||Zinc Finger ^@ Basic and acidic residues|||CR-type|||CXXCXGXG motif|||Disordered|||DnaJ homolog subfamily A member 3, mitochondrial|||In isoform 2.|||In isoform 3.|||J|||Mitochondrion|||N6-acetyllysine|||Omega-N-methylarginine; by CARM1|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000007257|||http://purl.uniprot.org/annotation/VSP_007427|||http://purl.uniprot.org/annotation/VSP_007428|||http://purl.uniprot.org/annotation/VSP_007440 http://togogenome.org/gene/10090:Coro7 ^@ http://purl.uniprot.org/uniprot/Q9D2V7 ^@ 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 ^@ Coronin-7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||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_0000050935 http://togogenome.org/gene/10090:Or1e34 ^@ http://purl.uniprot.org/uniprot/Q8VGR5 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Trim72 ^@ http://purl.uniprot.org/uniprot/Q1XH17 ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Zinc Finger ^@ B box-type|||B30.2/SPRY|||Does not affect homooligomerization.|||Dominant-negative mutant that abolishes homooligomerization and function in membrane repair.|||Interchain|||Phosphoserine|||RING-type|||S-nitrosocysteine|||Tripartite motif-containing protein 72 ^@ http://purl.uniprot.org/annotation/PRO_0000278131 http://togogenome.org/gene/10090:Rpl18 ^@ http://purl.uniprot.org/uniprot/A0A1B0GSF7|||http://purl.uniprot.org/uniprot/P35980|||http://purl.uniprot.org/uniprot/Q58EW0|||http://purl.uniprot.org/uniprot/Q642K1 ^@ 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 residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL18|||Large ribosomal subunit protein uL15/eL18|||Phosphoserine|||Phosphothreonine ^@ http://purl.uniprot.org/annotation/PRO_0000132770 http://togogenome.org/gene/10090:Nsfl1c ^@ http://purl.uniprot.org/uniprot/Q3UVN5|||http://purl.uniprot.org/uniprot/Q9CZ44 ^@ 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 ^@ Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||NSFL1 cofactor p47|||Nuclear localization signal|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SEP|||UBX ^@ http://purl.uniprot.org/annotation/PRO_0000210989|||http://purl.uniprot.org/annotation/VSP_009264|||http://purl.uniprot.org/annotation/VSP_009265|||http://purl.uniprot.org/annotation/VSP_009266 http://togogenome.org/gene/10090:Gfra3 ^@ http://purl.uniprot.org/uniprot/O35118 ^@ Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide ^@ GDNF family receptor alpha-3|||GPI-anchor amidated asparagine|||N-linked (GlcNAc...) asparagine|||Removed in mature form ^@ http://purl.uniprot.org/annotation/PRO_0000010791|||http://purl.uniprot.org/annotation/PRO_0000010792 http://togogenome.org/gene/10090:Atg16l2 ^@ http://purl.uniprot.org/uniprot/Q6KAU8 ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant ^@ Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Splice Variant ^@ Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Protein Atg16l2|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@ http://purl.uniprot.org/annotation/PRO_0000337111|||http://purl.uniprot.org/annotation/VSP_033906|||http://purl.uniprot.org/annotation/VSP_033907|||http://purl.uniprot.org/annotation/VSP_060643 http://togogenome.org/gene/10090:Prr14 ^@ http://purl.uniprot.org/uniprot/Q7TPN9 ^@ Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Modified Residue|||Region ^@ Disordered|||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_0000307270 http://togogenome.org/gene/10090:Ttll1 ^@ http://purl.uniprot.org/uniprot/Q91V51 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Site ^@ Disordered|||Essential for specifying alpha-elongation versus initiation step of the polyglutamylase activity|||Polyglutamylase complex subunit TTLL1|||TTL ^@ http://purl.uniprot.org/annotation/PRO_0000212439 http://togogenome.org/gene/10090:Or8k40 ^@ http://purl.uniprot.org/uniprot/Q8VGA6 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Vmn2r51 ^@ http://purl.uniprot.org/uniprot/L7N215 ^@ Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane ^@ Chain|||Domain Extent|||Signal Peptide|||Transmembrane ^@ G-protein coupled receptors family 3 profile|||Helical ^@ http://purl.uniprot.org/annotation/PRO_5003982197 http://togogenome.org/gene/10090:Cpa2 ^@ http://purl.uniprot.org/uniprot/Q504N0 ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide|||Site ^@ Active Site|||Binding Site|||Chain|||Disulfide Bond|||Propeptide|||Signal Peptide ^@ Activation peptide|||Carboxypeptidase A2|||Proton donor/acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000280809|||http://purl.uniprot.org/annotation/PRO_0000280810 http://togogenome.org/gene/10090:Chgb ^@ http://purl.uniprot.org/uniprot/P16014|||http://purl.uniprot.org/uniprot/Q3TY66 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide ^@ Acidic residues|||Basic and acidic residues|||CCB peptide|||Disordered|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||PE-11|||Phosphoserine|||Secretogranin-1|||Sulfotyrosine ^@ http://purl.uniprot.org/annotation/PRO_0000005441|||http://purl.uniprot.org/annotation/PRO_0000411988|||http://purl.uniprot.org/annotation/PRO_0000432731|||http://purl.uniprot.org/annotation/PRO_5014309156 http://togogenome.org/gene/10090:Tmem238 ^@ http://purl.uniprot.org/uniprot/A9JSM3|||http://purl.uniprot.org/uniprot/Q9D7T0 ^@ Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane ^@ Chain|||Modified Residue|||Region|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Transmembrane protein 238 ^@ http://purl.uniprot.org/annotation/PRO_0000413541 http://togogenome.org/gene/10090:Naip1 ^@ http://purl.uniprot.org/uniprot/Q9QWK5 ^@ Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict ^@ BIR 1|||BIR 2|||BIR 3|||Baculoviral IAP repeat-containing protein 1a|||NACHT ^@ http://purl.uniprot.org/annotation/PRO_0000122342 http://togogenome.org/gene/10090:Mefv ^@ http://purl.uniprot.org/uniprot/Q32MT0|||http://purl.uniprot.org/uniprot/Q32MT1|||http://purl.uniprot.org/uniprot/Q9JJ26 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger ^@ B box-type|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Pyrin|||Required for homotrimerization and induction of pyroptosomes ^@ http://purl.uniprot.org/annotation/PRO_0000220365 http://togogenome.org/gene/10090:Ccdc34 ^@ http://purl.uniprot.org/uniprot/Q3UI66|||http://purl.uniprot.org/uniprot/Q8BIA8 ^@ 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 ^@ Coiled-coil|||Coiled-coil domain-containing protein 34|||Disordered|||Phosphoserine|||Pro residues ^@ http://purl.uniprot.org/annotation/PRO_0000339112 http://togogenome.org/gene/10090:Pcdhb14 ^@ http://purl.uniprot.org/uniprot/Q6PB90 ^@ Chain|||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|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-14 ^@ http://purl.uniprot.org/annotation/PRO_0000271745 http://togogenome.org/gene/10090:Smco4 ^@ http://purl.uniprot.org/uniprot/Q9JIS3 ^@ Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane ^@ Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Transmembrane ^@ Disordered|||Helical|||Single-pass membrane and coiled-coil domain-containing protein 4 ^@ http://purl.uniprot.org/annotation/PRO_0000087320 http://togogenome.org/gene/10090:Pla2g4d ^@ http://purl.uniprot.org/uniprot/Q50L43 ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict ^@ C2|||Cytosolic phospholipase A2 delta|||Nucleophile|||PLA2c|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000247024 http://togogenome.org/gene/10090:Otos ^@ http://purl.uniprot.org/uniprot/Q497Y7|||http://purl.uniprot.org/uniprot/Q8R448 ^@ Chain|||Molecule Processing|||Signal Peptide ^@ Chain|||Signal Peptide ^@ Otospiralin ^@ http://purl.uniprot.org/annotation/PRO_0000021977|||http://purl.uniprot.org/annotation/PRO_5014309329 http://togogenome.org/gene/10090:Or4x11 ^@ http://purl.uniprot.org/uniprot/Q8VEZ3 ^@ Domain Extent|||Region|||Transmembrane ^@ Domain Extent|||Transmembrane ^@ G-protein coupled receptors family 1 profile|||Helical ^@ http://togogenome.org/gene/10090:Spa17 ^@ http://purl.uniprot.org/uniprot/Q545M2|||http://purl.uniprot.org/uniprot/Q62252 ^@ Chain|||Domain Extent|||Molecule Processing|||Region ^@ Chain|||Domain Extent|||Region ^@ Disordered|||IQ|||RIIa|||Sperm surface protein Sp17 ^@ http://purl.uniprot.org/annotation/PRO_0000181344 http://togogenome.org/gene/10090:Eftud2 ^@ http://purl.uniprot.org/uniprot/A2AH85|||http://purl.uniprot.org/uniprot/O08810|||http://purl.uniprot.org/uniprot/Q543F1 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region ^@ 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|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Tr-type G|||tr-type G ^@ http://purl.uniprot.org/annotation/PRO_0000091564 http://togogenome.org/gene/10090:Atg9a ^@ http://purl.uniprot.org/uniprot/Q68FE2 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane ^@ Autophagy-related protein 9A|||Basic and acidic residues|||Cytoplasmic|||Decreased localization to the Golgi apparatus; when associated with 22-A--A-27.|||Decreased localization to the Golgi apparatus; when associated with 8-A--A-11.|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Removed|||Tyrosine-based sorting signal ^@ http://purl.uniprot.org/annotation/PRO_0000119821|||http://purl.uniprot.org/annotation/VSP_061206|||http://purl.uniprot.org/annotation/VSP_061207 http://togogenome.org/gene/10090:Tbc1d17 ^@ http://purl.uniprot.org/uniprot/I6L974|||http://purl.uniprot.org/uniprot/Q8BYH7 ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site ^@ Arginine finger|||Disordered|||Glutamine finger|||Phosphoserine|||Phosphothreonine|||Pro residues|||Rab-GAP TBC|||Required for interaction with OPTN|||TBC1 domain family member 17 ^@ http://purl.uniprot.org/annotation/PRO_0000208046 http://togogenome.org/gene/10090:Rab3il1 ^@ http://purl.uniprot.org/uniprot/D3Z585|||http://purl.uniprot.org/uniprot/Q8VDV3 ^@ 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 ^@ Disordered|||GDP/GTP exchange factor Sec2 N-terminal|||Guanine nucleotide exchange factor for Rab-3A|||In isoform 2.|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000305296|||http://purl.uniprot.org/annotation/VSP_028346 http://togogenome.org/gene/10090:Myh9 ^@ http://purl.uniprot.org/uniprot/Q8VDD5 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict ^@ Actin-binding|||Basic and acidic residues|||Disordered|||IQ|||Mediates interaction with LIMCH1|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-9|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed ^@ http://purl.uniprot.org/annotation/PRO_0000123417 http://togogenome.org/gene/10090:Ninl ^@ http://purl.uniprot.org/uniprot/Q6ZQ12 ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant ^@ Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant ^@ Basic and acidic residues|||D-box|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 1.|||In isoform 2.|||KEN box|||Ninein-like protein|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000259715|||http://purl.uniprot.org/annotation/VSP_021526|||http://purl.uniprot.org/annotation/VSP_037882 http://togogenome.org/gene/10090:Ubxn8 ^@ http://purl.uniprot.org/uniprot/Q3TTF2 ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane ^@ Basic and acidic residues|||Disordered|||Helical|||UBX ^@ http://togogenome.org/gene/10090:Acrv1 ^@ http://purl.uniprot.org/uniprot/P50289 ^@ Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide ^@ Acrosomal protein SP-10|||Basic and acidic residues|||Disordered|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000020761 http://togogenome.org/gene/10090:Hoxc11 ^@ http://purl.uniprot.org/uniprot/P31313 ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modification|||Molecule Processing|||Region ^@ Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Region ^@ Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox|||Homeobox protein Hox-C11|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000200195 http://togogenome.org/gene/10090:Azgp1 ^@ http://purl.uniprot.org/uniprot/Q64726 ^@ Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide ^@ Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide ^@ Ig-like C1-type|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid|||Zinc-alpha-2-glycoprotein ^@ http://purl.uniprot.org/annotation/PRO_0000019013 http://togogenome.org/gene/10090:Stab2 ^@ http://purl.uniprot.org/uniprot/E5RKF9|||http://purl.uniprot.org/uniprot/Q8R4U0 ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane ^@ Cytoplasmic|||Disordered|||EGF-like|||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|||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|||Short form stabilin-2|||Stabilin-2 ^@ http://purl.uniprot.org/annotation/PRO_0000007714|||http://purl.uniprot.org/annotation/PRO_0000007715|||http://purl.uniprot.org/annotation/PRO_5009953646 http://togogenome.org/gene/10090:Enthd1 ^@ http://purl.uniprot.org/uniprot/E9Q1Z2 ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Compositionally Biased Region|||Domain Extent|||Region ^@ Disordered|||ENTH|||Polar residues ^@ http://togogenome.org/gene/10090:Fmo6 ^@ http://purl.uniprot.org/uniprot/J3QMN6 ^@ Region|||Transmembrane ^@ Transmembrane ^@ Helical ^@ http://togogenome.org/gene/10090:Rad51d ^@ http://purl.uniprot.org/uniprot/B1ARD4|||http://purl.uniprot.org/uniprot/B5LBC4|||http://purl.uniprot.org/uniprot/O55230|||http://purl.uniprot.org/uniprot/Q3UGT8|||http://purl.uniprot.org/uniprot/Q9EP85 ^@ Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site ^@ Binding Site|||Chain|||Domain Extent|||Region ^@ DNA repair protein RAD51 homolog 4|||Interaction with RAD51C|||Interaction with XRCC2|||RecA family profile 1|||preferentially binds ssDNA ^@ http://purl.uniprot.org/annotation/PRO_0000122943 http://togogenome.org/gene/10090:Mylk2 ^@ http://purl.uniprot.org/uniprot/Q8VCR8 ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site ^@ Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region ^@ Calmodulin-binding|||Disordered|||Myosin light chain kinase 2, skeletal/cardiac muscle|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor ^@ http://purl.uniprot.org/annotation/PRO_0000086409 http://togogenome.org/gene/10090:Tmem214 ^@ http://purl.uniprot.org/uniprot/Q8BM55 ^@ Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane ^@ Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Removed|||Transmembrane protein 214 ^@ http://purl.uniprot.org/annotation/PRO_0000321898|||http://purl.uniprot.org/annotation/VSP_031816|||http://purl.uniprot.org/annotation/VSP_031817 http://togogenome.org/gene/10090:Klra9 ^@ http://purl.uniprot.org/uniprot/Q2TJJ8|||http://purl.uniprot.org/uniprot/Q64329 ^@ 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|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn ^@ C-type lectin|||Cytoplasmic|||Extracellular|||Greatly reduces MHC class I peptide tetramer binding; when associated with D-160.|||Greatly reduces MHC class I peptide tetramer binding; when associated with L-162.|||Greatly reduces MHC class I peptide tetramer binding; when associated with N-225.|||Greatly reduces MHC class I peptide tetramer binding; when associated with P-195.|||Greatly reduces MHC class I peptide tetramer binding; when associated with S-196.|||Greatly reduces MHC class I peptide tetramer binding; when associated with T-226.|||Helical|||Helical; Signal-anchor for type II membrane protein|||Implicated in MHC class I binding|||In strain: A/Sn, BALB/c, C57BL/6, C57BL/6 XBALB/c, C57BL/6 XCBA, CB-17/SCID and NZB.|||In strain: C57BL/6 XBALB/c, NZB and C57BL/6.|||In strain: C57BL/6 and C57BL/6 XBALB/c.|||In strain: C57BL/6, C57BL/6 XBALB/c and NZB.|||In strain: C57BL/6, C57BL/6 XBALB/c and NZB; requires 2 nucleotide substitutions.|||In strain: NZB.|||Increases stability and improves binding to MHCI class ligand; when associated with G-121; G-175 and G-197.|||Increases stability and improves binding to MHCI class ligand; when associated with G-121; G-175 and K-227.|||Increases stability and improves binding to MHCI class ligand; when associated with G-175; G-197 and K-227.|||Increases stability. Increases stability and improves binding to MHCI class ligand; when associated with G-121; G-197 and K-227.|||Involved in dimerization|||Killer cell lectin-like receptor 3|||N-linked (GlcNAc...) asparagine|||No effect on MHC class I binding; when associated with S-173.|||No effect on MHC class I peptide tetramer binding.|||No effect on MHC class I peptide tetramer binding; when associated with D-250.|||No effect on MHC class I peptide tetramer binding; when associated with N-248.|||No effect on MHC class I peptide tetramer binding; when associated with Q-169.|||No effect on MHC class I peptide tetramer binding; when associated with S-174.|||No effect on MHC class I peptide tetramer binding; when associated with T-170. ^@ http://purl.uniprot.org/annotation/PRO_0000046681 http://togogenome.org/gene/10090:Polr1a ^@ http://purl.uniprot.org/uniprot/O35134|||http://purl.uniprot.org/uniprot/Q3TU49|||http://purl.uniprot.org/uniprot/Q3UHI3 ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site ^@ Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Acidic residues|||Basic and acidic residues|||Bridging helix|||DNA-directed RNA polymerase I subunit RPA1|||Disordered|||Phosphoserine|||RNA polymerase N-terminal ^@ http://purl.uniprot.org/annotation/PRO_0000073924 http://togogenome.org/gene/10090:Cenpc1 ^@ http://purl.uniprot.org/uniprot/P49452|||http://purl.uniprot.org/uniprot/Q3UPF6 ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict ^@ Basic and acidic residues|||Basic residues|||CENP-C middle DNMT3B-binding|||Centromere protein C|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Kinetochore assembly subunit CENP-C N-terminal|||MIF2 homology domain II|||MIF2 homology domain III|||Nuclear localization signal|||Phosphoserine|||Polar residues ^@ http://purl.uniprot.org/annotation/PRO_0000089475 http://togogenome.org/gene/10090:Sccpdh ^@ http://purl.uniprot.org/uniprot/Q8R127 ^@ Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing ^@ Chain|||Initiator Methionine|||Modified Residue ^@ N-acetylalanine|||Phosphoserine|||Removed|||Saccharopine dehydrogenase-like oxidoreductase ^@ http://purl.uniprot.org/annotation/PRO_0000212841